data_8YB0
# 
_entry.id   8YB0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8YB0         pdb_00008yb0 10.2210/pdb8yb0/pdb 
WWPDB D_1300044633 ?            ?                   
# 
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 2025-02-12 ? 
2 'Structure model' 1 1 2025-03-26 ? 
3 'Structure model' 1 2 2025-04-02 ? 
# 
_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' 'Database references' 
2 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 3 'Structure model' citation        
# 
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.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.pdbx_database_id_DOI'    
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 3 'Structure model' '_citation.page_last'               
11 3 'Structure model' '_citation.pdbx_database_id_PubMed' 
12 3 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YB0 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              minoru.kubo@riken.jp 
_pdbx_contact_author.name_first         Minoru 
_pdbx_contact_author.name_last          Kubo 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1470-942X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nagao, S.'       1  ? 
'Kuwano, W.'      2  ? 
'Tosha, T.'       3  ? 
'Yamashita, K.'   4  ? 
'Stanfield, J.K.' 5  ? 
'Kasai, C.'       6  ? 
'Ariyasu, S.'     7  ? 
'Shoji, O.'       8  ? 
'Sugimoto, H.'    9  ? 
'Kubo, M.'        10 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3669 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                63 
_citation.page_last                 63 
_citation.title                     
'XFEL crystallography reveals catalytic cycle dynamics during non-native substrate oxidation by cytochrome P450BM3.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42004-025-01440-2 
_citation.pdbx_database_id_PubMed   40075209 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nagao, S.'       1  ? 
primary 'Kuwano, W.'      2  ? 
primary 'Tosha, T.'       3  ? 
primary 'Yamashita, K.'   4  ? 
primary 'Stanfield, J.K.' 5  ? 
primary 'Kasai, C.'       6  ? 
primary 'Ariyasu, S.'     7  ? 
primary 'Hirata, K.'      8  ? 
primary 'Ueno, G.'        9  ? 
primary 'Murakami, H.'    10 ? 
primary 'Ago, H.'         11 ? 
primary 'Yamamoto, M.'    12 ? 
primary 'Shoji, O.'       13 ? 
primary 'Sugimoto, H.'    14 ? 
primary 'Kubo, M.'        15 ? 
# 
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 'Bifunctional cytochrome P450/NADPH--P450 reductase'                           52160.434 2   1.14.14.1,1.6.2.4 ? 
? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                              616.487   2   ?                 ? 
? ? 
3 non-polymer syn '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' 360.490   2   ?                 ? 
? ? 
4 non-polymer syn ethenylbenzene                                                                 104.149   2   ?                 ? 
? ? 
5 non-polymer syn GLYCEROL                                                                       92.094    8   ?                 ? 
? ? 
6 water       nat water                                                                          18.015    875 ?                 ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytochrome P450(BM-3),Cytochrome P450BM-3,Fatty acid monooxygenase,Flavocytochrome P450 BM3' 
# 
_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       
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRD
FAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPHGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRD
FAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPHGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                              HEM 
3 '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' D0L 
4 ethenylbenzene                                                                 SYN 
5 GLYCEROL                                                                       GOL 
6 water                                                                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   ILE n 
1 3   LYS n 
1 4   GLU n 
1 5   MET n 
1 6   PRO n 
1 7   GLN n 
1 8   PRO n 
1 9   LYS n 
1 10  THR n 
1 11  PHE n 
1 12  GLY n 
1 13  GLU n 
1 14  LEU n 
1 15  LYS n 
1 16  ASN n 
1 17  LEU n 
1 18  PRO n 
1 19  LEU n 
1 20  LEU n 
1 21  ASN n 
1 22  THR n 
1 23  ASP n 
1 24  LYS n 
1 25  PRO n 
1 26  VAL n 
1 27  GLN n 
1 28  ALA n 
1 29  LEU n 
1 30  MET n 
1 31  LYS n 
1 32  ILE n 
1 33  ALA n 
1 34  ASP n 
1 35  GLU n 
1 36  LEU n 
1 37  GLY n 
1 38  GLU n 
1 39  ILE n 
1 40  PHE n 
1 41  LYS n 
1 42  PHE n 
1 43  GLU n 
1 44  ALA n 
1 45  PRO n 
1 46  GLY n 
1 47  ARG n 
1 48  VAL n 
1 49  THR n 
1 50  ARG n 
1 51  TYR n 
1 52  LEU n 
1 53  SER n 
1 54  SER n 
1 55  GLN n 
1 56  ARG n 
1 57  LEU n 
1 58  ILE n 
1 59  LYS n 
1 60  GLU n 
1 61  ALA n 
1 62  CYS n 
1 63  ASP n 
1 64  GLU n 
1 65  SER n 
1 66  ARG n 
1 67  PHE n 
1 68  ASP n 
1 69  LYS n 
1 70  ASN n 
1 71  LEU n 
1 72  SER n 
1 73  GLN n 
1 74  ALA n 
1 75  LEU n 
1 76  LYS n 
1 77  PHE n 
1 78  VAL n 
1 79  ARG n 
1 80  ASP n 
1 81  PHE n 
1 82  ALA n 
1 83  GLY n 
1 84  ASP n 
1 85  GLY n 
1 86  LEU n 
1 87  PHE n 
1 88  THR n 
1 89  SER n 
1 90  TRP n 
1 91  THR n 
1 92  HIS n 
1 93  GLU n 
1 94  LYS n 
1 95  ASN n 
1 96  TRP n 
1 97  LYS n 
1 98  LYS n 
1 99  ALA n 
1 100 HIS n 
1 101 ASN n 
1 102 ILE n 
1 103 LEU n 
1 104 LEU n 
1 105 PRO n 
1 106 SER n 
1 107 PHE n 
1 108 SER n 
1 109 GLN n 
1 110 GLN n 
1 111 ALA n 
1 112 MET n 
1 113 LYS n 
1 114 GLY n 
1 115 TYR n 
1 116 HIS n 
1 117 ALA n 
1 118 MET n 
1 119 MET n 
1 120 VAL n 
1 121 ASP n 
1 122 ILE n 
1 123 ALA n 
1 124 VAL n 
1 125 GLN n 
1 126 LEU n 
1 127 VAL n 
1 128 GLN n 
1 129 LYS n 
1 130 TRP n 
1 131 GLU n 
1 132 ARG n 
1 133 LEU n 
1 134 ASN n 
1 135 ALA n 
1 136 ASP n 
1 137 GLU n 
1 138 HIS n 
1 139 ILE n 
1 140 GLU n 
1 141 VAL n 
1 142 PRO n 
1 143 GLU n 
1 144 ASP n 
1 145 MET n 
1 146 THR n 
1 147 ARG n 
1 148 LEU n 
1 149 THR n 
1 150 LEU n 
1 151 ASP n 
1 152 THR n 
1 153 ILE n 
1 154 GLY n 
1 155 LEU n 
1 156 CYS n 
1 157 GLY n 
1 158 PHE n 
1 159 ASN n 
1 160 TYR n 
1 161 ARG n 
1 162 PHE n 
1 163 ASN n 
1 164 SER n 
1 165 PHE n 
1 166 TYR n 
1 167 ARG n 
1 168 ASP n 
1 169 GLN n 
1 170 PRO n 
1 171 HIS n 
1 172 PRO n 
1 173 PHE n 
1 174 ILE n 
1 175 THR n 
1 176 SER n 
1 177 MET n 
1 178 VAL n 
1 179 ARG n 
1 180 ALA n 
1 181 LEU n 
1 182 ASP n 
1 183 GLU n 
1 184 ALA n 
1 185 MET n 
1 186 ASN n 
1 187 LYS n 
1 188 LEU n 
1 189 GLN n 
1 190 ARG n 
1 191 ALA n 
1 192 ASN n 
1 193 PRO n 
1 194 ASP n 
1 195 ASP n 
1 196 PRO n 
1 197 ALA n 
1 198 TYR n 
1 199 ASP n 
1 200 GLU n 
1 201 ASN n 
1 202 LYS n 
1 203 ARG n 
1 204 GLN n 
1 205 PHE n 
1 206 GLN n 
1 207 GLU n 
1 208 ASP n 
1 209 ILE n 
1 210 LYS n 
1 211 VAL n 
1 212 MET n 
1 213 ASN n 
1 214 ASP n 
1 215 LEU n 
1 216 VAL n 
1 217 ASP n 
1 218 LYS n 
1 219 ILE n 
1 220 ILE n 
1 221 ALA n 
1 222 ASP n 
1 223 ARG n 
1 224 LYS n 
1 225 ALA n 
1 226 SER n 
1 227 GLY n 
1 228 GLU n 
1 229 GLN n 
1 230 SER n 
1 231 ASP n 
1 232 ASP n 
1 233 LEU n 
1 234 LEU n 
1 235 THR n 
1 236 HIS n 
1 237 MET n 
1 238 LEU n 
1 239 ASN n 
1 240 GLY n 
1 241 LYS n 
1 242 ASP n 
1 243 PRO n 
1 244 GLU n 
1 245 THR n 
1 246 GLY n 
1 247 GLU n 
1 248 PRO n 
1 249 LEU n 
1 250 ASP n 
1 251 ASP n 
1 252 GLU n 
1 253 ASN n 
1 254 ILE n 
1 255 ARG n 
1 256 TYR n 
1 257 GLN n 
1 258 ILE n 
1 259 ILE n 
1 260 THR n 
1 261 PHE n 
1 262 LEU n 
1 263 ILE n 
1 264 ALA n 
1 265 GLY n 
1 266 HIS n 
1 267 GLU n 
1 268 THR n 
1 269 THR n 
1 270 SER n 
1 271 GLY n 
1 272 LEU n 
1 273 LEU n 
1 274 SER n 
1 275 PHE n 
1 276 ALA n 
1 277 LEU n 
1 278 TYR n 
1 279 PHE n 
1 280 LEU n 
1 281 VAL n 
1 282 LYS n 
1 283 ASN n 
1 284 PRO n 
1 285 HIS n 
1 286 VAL n 
1 287 LEU n 
1 288 GLN n 
1 289 LYS n 
1 290 ALA n 
1 291 ALA n 
1 292 GLU n 
1 293 GLU n 
1 294 ALA n 
1 295 ALA n 
1 296 ARG n 
1 297 VAL n 
1 298 LEU n 
1 299 VAL n 
1 300 ASP n 
1 301 PRO n 
1 302 VAL n 
1 303 PRO n 
1 304 SER n 
1 305 TYR n 
1 306 LYS n 
1 307 GLN n 
1 308 VAL n 
1 309 LYS n 
1 310 GLN n 
1 311 LEU n 
1 312 LYS n 
1 313 TYR n 
1 314 VAL n 
1 315 GLY n 
1 316 MET n 
1 317 VAL n 
1 318 LEU n 
1 319 ASN n 
1 320 GLU n 
1 321 ALA n 
1 322 LEU n 
1 323 ARG n 
1 324 LEU n 
1 325 TRP n 
1 326 PRO n 
1 327 THR n 
1 328 ALA n 
1 329 PRO n 
1 330 ALA n 
1 331 PHE n 
1 332 SER n 
1 333 LEU n 
1 334 TYR n 
1 335 ALA n 
1 336 LYS n 
1 337 GLU n 
1 338 ASP n 
1 339 THR n 
1 340 VAL n 
1 341 LEU n 
1 342 GLY n 
1 343 GLY n 
1 344 GLU n 
1 345 TYR n 
1 346 PRO n 
1 347 LEU n 
1 348 GLU n 
1 349 LYS n 
1 350 GLY n 
1 351 ASP n 
1 352 GLU n 
1 353 LEU n 
1 354 MET n 
1 355 VAL n 
1 356 LEU n 
1 357 ILE n 
1 358 PRO n 
1 359 GLN n 
1 360 LEU n 
1 361 HIS n 
1 362 ARG n 
1 363 ASP n 
1 364 LYS n 
1 365 THR n 
1 366 ILE n 
1 367 TRP n 
1 368 GLY n 
1 369 ASP n 
1 370 ASP n 
1 371 VAL n 
1 372 GLU n 
1 373 GLU n 
1 374 PHE n 
1 375 ARG n 
1 376 PRO n 
1 377 GLU n 
1 378 ARG n 
1 379 PHE n 
1 380 GLU n 
1 381 ASN n 
1 382 PRO n 
1 383 SER n 
1 384 ALA n 
1 385 ILE n 
1 386 PRO n 
1 387 GLN n 
1 388 HIS n 
1 389 ALA n 
1 390 PHE n 
1 391 LYS n 
1 392 PRO n 
1 393 HIS n 
1 394 GLY n 
1 395 ASN n 
1 396 GLY n 
1 397 GLN n 
1 398 ARG n 
1 399 ALA n 
1 400 CYS n 
1 401 ILE n 
1 402 GLY n 
1 403 GLN n 
1 404 GLN n 
1 405 PHE n 
1 406 ALA n 
1 407 LEU n 
1 408 HIS n 
1 409 GLU n 
1 410 ALA n 
1 411 THR n 
1 412 LEU n 
1 413 VAL n 
1 414 LEU n 
1 415 GLY n 
1 416 MET n 
1 417 MET n 
1 418 LEU n 
1 419 LYS n 
1 420 HIS n 
1 421 PHE n 
1 422 ASP n 
1 423 PHE n 
1 424 GLU n 
1 425 ASP n 
1 426 HIS n 
1 427 THR n 
1 428 ASN n 
1 429 TYR n 
1 430 GLU n 
1 431 LEU n 
1 432 ASP n 
1 433 ILE n 
1 434 LYS n 
1 435 GLU n 
1 436 THR n 
1 437 LEU n 
1 438 THR n 
1 439 LEU n 
1 440 LYS n 
1 441 PRO n 
1 442 GLU n 
1 443 GLY n 
1 444 PHE n 
1 445 VAL n 
1 446 VAL n 
1 447 LYS n 
1 448 ALA n 
1 449 LYS n 
1 450 SER n 
1 451 LYS n 
1 452 LYS n 
1 453 ILE n 
1 454 PRO n 
1 455 LEU 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                   455 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'NBRC 15308 = ATCC 14581' 
_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      'Priestia megaterium NBRC 15308 = ATCC 14581' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1348623 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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               'BL21(DE3)' 
_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 
CYS 'L-peptide linking' y CYSTEINE                                                                       ? 'C3 H7 N O2 S'     
121.158 
D0L non-polymer         . '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' ? 'C21 H32 N2 O3'    
360.490 
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  
GOL non-polymer         . GLYCEROL                                                                       
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                              HEME 'C34 H32 Fe N4 O4' 
616.487 
HIS 'L-peptide linking' y HISTIDINE                                                                      ? 'C6 H10 N3 O2 1'   
156.162 
HOH non-polymer         . WATER                                                                          ? 'H2 O'             
18.015  
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 
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 
SYN non-polymer         . ethenylbenzene                                                                 styrene 'C8 H8' 104.149 
THR 'L-peptide linking' y THREONINE                                                                      ? 'C4 H9 N O3'       
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                     ? 'C11 H12 N2 O2'    
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                       ? 'C9 H11 N O3'      
181.189 
VAL 'L-peptide linking' y VALINE                                                                         ? 'C5 H11 N O2'      
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   THR 1   1   1   THR THR A . n 
A 1 2   ILE 2   2   2   ILE ILE A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   MET 5   5   5   MET MET A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   GLN 7   7   7   GLN GLN A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  PRO 18  18  18  PRO PRO A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  MET 30  30  30  MET MET A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  CYS 62  62  62  CYS CYS A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  PHE 77  77  77  PHE PHE A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  TRP 90  90  90  TRP TRP A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  TRP 96  96  96  TRP TRP A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 MET 112 112 112 MET MET A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 HIS 116 116 116 HIS HIS A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLN 125 125 125 GLN GLN A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 TRP 130 130 130 TRP TRP A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 MET 145 145 145 MET MET A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 ASN 163 163 163 ASN ASN A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 HIS 171 171 171 HIS HIS A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 MET 177 177 177 MET MET A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ASN 192 192 192 ASN ASN A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 ASP 194 194 194 ASP ASP A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 LYS 202 202 202 LYS LYS A . n 
A 1 203 ARG 203 203 203 ARG ARG A . n 
A 1 204 GLN 204 204 204 GLN GLN A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 GLN 206 206 206 GLN GLN A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 LYS 210 210 210 LYS LYS A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 MET 212 212 212 MET MET A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 ASP 217 217 217 ASP ASP A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 HIS 236 236 236 HIS HIS A . n 
A 1 237 MET 237 237 237 MET MET A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 GLU 252 252 252 GLU GLU A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 ILE 254 254 254 ILE ILE A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 THR 260 260 260 THR THR A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 HIS 266 266 266 HIS HIS A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 TYR 278 278 278 TYR TYR A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 VAL 281 281 281 VAL VAL A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 ASN 283 283 283 ASN ASN A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 HIS 285 285 285 HIS HIS A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 ASP 300 300 300 ASP ASP A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 TYR 305 305 305 TYR TYR A . n 
A 1 306 LYS 306 306 306 LYS LYS A . n 
A 1 307 GLN 307 307 307 GLN GLN A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 TYR 313 313 313 TYR TYR A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 MET 316 316 316 MET MET A . n 
A 1 317 VAL 317 317 317 VAL VAL A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 ASN 319 319 319 ASN ASN A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 ARG 323 323 323 ARG ARG A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 TRP 325 325 325 TRP TRP A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 PRO 329 329 329 PRO PRO A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 PHE 331 331 331 PHE PHE A . n 
A 1 332 SER 332 332 332 SER SER A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 TYR 334 334 334 TYR TYR A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 ASP 338 338 338 ASP ASP A . n 
A 1 339 THR 339 339 339 THR THR A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 TYR 345 345 345 TYR TYR A . n 
A 1 346 PRO 346 346 346 PRO PRO A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 GLU 348 348 348 GLU GLU A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 ASP 351 351 351 ASP ASP A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 MET 354 354 354 MET MET A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 PRO 358 358 358 PRO PRO A . n 
A 1 359 GLN 359 359 359 GLN GLN A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 HIS 361 361 361 HIS HIS A . n 
A 1 362 ARG 362 362 362 ARG ARG A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 LYS 364 364 364 LYS LYS A . n 
A 1 365 THR 365 365 365 THR THR A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 TRP 367 367 367 TRP TRP A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 ASP 370 370 370 ASP ASP A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 PHE 374 374 374 PHE PHE A . n 
A 1 375 ARG 375 375 375 ARG ARG A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 GLU 377 377 377 GLU GLU A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 PHE 379 379 379 PHE PHE A . n 
A 1 380 GLU 380 380 380 GLU GLU A . n 
A 1 381 ASN 381 381 381 ASN ASN A . n 
A 1 382 PRO 382 382 382 PRO PRO A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 ALA 384 384 384 ALA ALA A . n 
A 1 385 ILE 385 385 385 ILE ILE A . n 
A 1 386 PRO 386 386 386 PRO PRO A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 HIS 388 388 388 HIS HIS A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 PHE 390 390 390 PHE PHE A . n 
A 1 391 LYS 391 391 391 LYS LYS A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 HIS 393 393 393 HIS HIS A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 GLY 396 396 396 GLY GLY A . n 
A 1 397 GLN 397 397 397 GLN GLN A . n 
A 1 398 ARG 398 398 398 ARG ARG A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 CYS 400 400 400 CYS CYS A . n 
A 1 401 ILE 401 401 401 ILE ILE A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 GLN 403 403 403 GLN GLN A . n 
A 1 404 GLN 404 404 404 GLN GLN A . n 
A 1 405 PHE 405 405 405 PHE PHE A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 LEU 407 407 407 LEU LEU A . n 
A 1 408 HIS 408 408 408 HIS HIS A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 THR 411 411 411 THR THR A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 VAL 413 413 413 VAL VAL A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 GLY 415 415 415 GLY GLY A . n 
A 1 416 MET 416 416 416 MET MET A . n 
A 1 417 MET 417 417 417 MET MET A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 LYS 419 419 419 LYS LYS A . n 
A 1 420 HIS 420 420 420 HIS HIS A . n 
A 1 421 PHE 421 421 421 PHE PHE A . n 
A 1 422 ASP 422 422 422 ASP ASP A . n 
A 1 423 PHE 423 423 423 PHE PHE A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 HIS 426 426 426 HIS HIS A . n 
A 1 427 THR 427 427 427 THR THR A . n 
A 1 428 ASN 428 428 428 ASN ASN A . n 
A 1 429 TYR 429 429 429 TYR TYR A . n 
A 1 430 GLU 430 430 430 GLU GLU A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 ILE 433 433 433 ILE ILE A . n 
A 1 434 LYS 434 434 434 LYS LYS A . n 
A 1 435 GLU 435 435 435 GLU GLU A . n 
A 1 436 THR 436 436 436 THR THR A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 PRO 441 441 441 PRO PRO A . n 
A 1 442 GLU 442 442 442 GLU GLU A . n 
A 1 443 GLY 443 443 443 GLY GLY A . n 
A 1 444 PHE 444 444 444 PHE PHE A . n 
A 1 445 VAL 445 445 445 VAL VAL A . n 
A 1 446 VAL 446 446 446 VAL VAL A . n 
A 1 447 LYS 447 447 447 LYS LYS A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 LYS 449 449 449 LYS LYS A . n 
A 1 450 SER 450 450 450 SER SER A . n 
A 1 451 LYS 451 451 451 LYS LYS A . n 
A 1 452 LYS 452 452 452 LYS LYS A . n 
A 1 453 ILE 453 453 453 ILE ILE A . n 
A 1 454 PRO 454 454 454 PRO PRO A . n 
A 1 455 LEU 455 455 455 LEU LEU A . n 
B 1 1   THR 1   1   1   THR THR B . n 
B 1 2   ILE 2   2   2   ILE ILE B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   GLU 4   4   4   GLU GLU B . n 
B 1 5   MET 5   5   5   MET MET B . n 
B 1 6   PRO 6   6   6   PRO PRO B . n 
B 1 7   GLN 7   7   7   GLN GLN B . n 
B 1 8   PRO 8   8   8   PRO PRO B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  THR 10  10  10  THR THR B . n 
B 1 11  PHE 11  11  11  PHE PHE B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  GLU 13  13  13  GLU GLU B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  PRO 18  18  18  PRO PRO B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  ASN 21  21  21  ASN ASN B . n 
B 1 22  THR 22  22  22  THR THR B . n 
B 1 23  ASP 23  23  23  ASP ASP B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  VAL 26  26  26  VAL VAL B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  MET 30  30  30  MET MET B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  ALA 33  33  33  ALA ALA B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  GLU 38  38  38  GLU GLU B . n 
B 1 39  ILE 39  39  39  ILE ILE B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  PHE 42  42  42  PHE PHE B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  GLN 55  55  55  GLN GLN B . n 
B 1 56  ARG 56  56  56  ARG ARG B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  CYS 62  62  62  CYS CYS B . n 
B 1 63  ASP 63  63  63  ASP ASP B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  PHE 67  67  67  PHE PHE B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  GLN 73  73  73  GLN GLN B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  PHE 77  77  77  PHE PHE B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  PHE 81  81  81  PHE PHE B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  TRP 90  90  90  TRP TRP B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  HIS 92  92  92  HIS HIS B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  TRP 96  96  96  TRP TRP B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  LYS 98  98  98  LYS LYS B . n 
B 1 99  ALA 99  99  99  ALA ALA B . n 
B 1 100 HIS 100 100 100 HIS HIS B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 PRO 105 105 105 PRO PRO B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 PHE 107 107 107 PHE PHE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLN 109 109 109 GLN GLN B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 MET 112 112 112 MET MET B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 TYR 115 115 115 TYR TYR B . n 
B 1 116 HIS 116 116 116 HIS HIS B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 MET 118 118 118 MET MET B . n 
B 1 119 MET 119 119 119 MET MET B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 GLN 125 125 125 GLN GLN B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 GLN 128 128 128 GLN GLN B . n 
B 1 129 LYS 129 129 129 LYS LYS B . n 
B 1 130 TRP 130 130 130 TRP TRP B . n 
B 1 131 GLU 131 131 131 GLU GLU B . n 
B 1 132 ARG 132 132 132 ARG ARG B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 GLU 143 143 143 GLU GLU B . n 
B 1 144 ASP 144 144 144 ASP ASP B . n 
B 1 145 MET 145 145 145 MET MET B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 ARG 147 147 147 ARG ARG B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 ASP 151 151 151 ASP ASP B . n 
B 1 152 THR 152 152 152 THR THR B . n 
B 1 153 ILE 153 153 153 ILE ILE B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 GLY 157 157 157 GLY GLY B . n 
B 1 158 PHE 158 158 158 PHE PHE B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 TYR 160 160 160 TYR TYR B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 PHE 162 162 162 PHE PHE B . n 
B 1 163 ASN 163 163 163 ASN ASN B . n 
B 1 164 SER 164 164 164 SER SER B . n 
B 1 165 PHE 165 165 165 PHE PHE B . n 
B 1 166 TYR 166 166 166 TYR TYR B . n 
B 1 167 ARG 167 167 167 ARG ARG B . n 
B 1 168 ASP 168 168 168 ASP ASP B . n 
B 1 169 GLN 169 169 169 GLN GLN B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 HIS 171 171 171 HIS HIS B . n 
B 1 172 PRO 172 172 172 PRO PRO B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 ILE 174 174 174 ILE ILE B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 SER 176 176 176 SER SER B . n 
B 1 177 MET 177 177 177 MET MET B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 ARG 179 179 179 ARG ARG B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 ASP 182 182 182 ASP ASP B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 ALA 184 184 184 ALA ALA B . n 
B 1 185 MET 185 185 185 MET MET B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 LYS 187 187 187 LYS LYS B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 ARG 190 190 190 ARG ARG B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 ASN 192 192 192 ASN ASN B . n 
B 1 193 PRO 193 193 193 PRO PRO B . n 
B 1 194 ASP 194 194 194 ASP ASP B . n 
B 1 195 ASP 195 195 195 ASP ASP B . n 
B 1 196 PRO 196 196 196 PRO PRO B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 TYR 198 198 198 TYR TYR B . n 
B 1 199 ASP 199 199 199 ASP ASP B . n 
B 1 200 GLU 200 200 200 GLU GLU B . n 
B 1 201 ASN 201 201 201 ASN ASN B . n 
B 1 202 LYS 202 202 202 LYS LYS B . n 
B 1 203 ARG 203 203 203 ARG ARG B . n 
B 1 204 GLN 204 204 204 GLN GLN B . n 
B 1 205 PHE 205 205 205 PHE PHE B . n 
B 1 206 GLN 206 206 206 GLN GLN B . n 
B 1 207 GLU 207 207 207 GLU GLU B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 ILE 209 209 209 ILE ILE B . n 
B 1 210 LYS 210 210 210 LYS LYS B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 MET 212 212 212 MET MET B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 ASP 214 214 214 ASP ASP B . n 
B 1 215 LEU 215 215 215 LEU LEU B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 ASP 217 217 217 ASP ASP B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 ALA 221 221 221 ALA ALA B . n 
B 1 222 ASP 222 222 222 ASP ASP B . n 
B 1 223 ARG 223 223 223 ARG ARG B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 SER 226 226 226 SER SER B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 SER 230 230 230 SER SER B . n 
B 1 231 ASP 231 231 231 ASP ASP B . n 
B 1 232 ASP 232 232 232 ASP ASP B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 THR 235 235 235 THR THR B . n 
B 1 236 HIS 236 236 236 HIS HIS B . n 
B 1 237 MET 237 237 237 MET MET B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 ASN 239 239 239 ASN ASN B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 LYS 241 241 241 LYS LYS B . n 
B 1 242 ASP 242 242 242 ASP ASP B . n 
B 1 243 PRO 243 243 243 PRO PRO B . n 
B 1 244 GLU 244 244 244 GLU GLU B . n 
B 1 245 THR 245 245 245 THR THR B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 PRO 248 248 248 PRO PRO B . n 
B 1 249 LEU 249 249 249 LEU LEU B . n 
B 1 250 ASP 250 250 250 ASP ASP B . n 
B 1 251 ASP 251 251 251 ASP ASP B . n 
B 1 252 GLU 252 252 252 GLU GLU B . n 
B 1 253 ASN 253 253 253 ASN ASN B . n 
B 1 254 ILE 254 254 254 ILE ILE B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 TYR 256 256 256 TYR TYR B . n 
B 1 257 GLN 257 257 257 GLN GLN B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 THR 260 260 260 THR THR B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ILE 263 263 263 ILE ILE B . n 
B 1 264 ALA 264 264 264 ALA ALA B . n 
B 1 265 GLY 265 265 265 GLY GLY B . n 
B 1 266 HIS 266 266 266 HIS HIS B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 THR 268 268 268 THR THR B . n 
B 1 269 THR 269 269 269 THR THR B . n 
B 1 270 SER 270 270 270 SER SER B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 SER 274 274 274 SER SER B . n 
B 1 275 PHE 275 275 275 PHE PHE B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 TYR 278 278 278 TYR TYR B . n 
B 1 279 PHE 279 279 279 PHE PHE B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 VAL 281 281 281 VAL VAL B . n 
B 1 282 LYS 282 282 282 LYS LYS B . n 
B 1 283 ASN 283 283 283 ASN ASN B . n 
B 1 284 PRO 284 284 284 PRO PRO B . n 
B 1 285 HIS 285 285 285 HIS HIS B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLN 288 288 288 GLN GLN B . n 
B 1 289 LYS 289 289 289 LYS LYS B . n 
B 1 290 ALA 290 290 290 ALA ALA B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 GLU 292 292 292 GLU GLU B . n 
B 1 293 GLU 293 293 293 GLU GLU B . n 
B 1 294 ALA 294 294 294 ALA ALA B . n 
B 1 295 ALA 295 295 295 ALA ALA B . n 
B 1 296 ARG 296 296 296 ARG ARG B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 LEU 298 298 298 LEU LEU B . n 
B 1 299 VAL 299 299 299 VAL VAL B . n 
B 1 300 ASP 300 300 300 ASP ASP B . n 
B 1 301 PRO 301 301 301 PRO PRO B . n 
B 1 302 VAL 302 302 302 VAL VAL B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 SER 304 304 304 SER SER B . n 
B 1 305 TYR 305 305 305 TYR TYR B . n 
B 1 306 LYS 306 306 306 LYS LYS B . n 
B 1 307 GLN 307 307 307 GLN GLN B . n 
B 1 308 VAL 308 308 308 VAL VAL B . n 
B 1 309 LYS 309 309 309 LYS LYS B . n 
B 1 310 GLN 310 310 310 GLN GLN B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 LYS 312 312 312 LYS LYS B . n 
B 1 313 TYR 313 313 313 TYR TYR B . n 
B 1 314 VAL 314 314 314 VAL VAL B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 MET 316 316 316 MET MET B . n 
B 1 317 VAL 317 317 317 VAL VAL B . n 
B 1 318 LEU 318 318 318 LEU LEU B . n 
B 1 319 ASN 319 319 319 ASN ASN B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 ALA 321 321 321 ALA ALA B . n 
B 1 322 LEU 322 322 322 LEU LEU B . n 
B 1 323 ARG 323 323 323 ARG ARG B . n 
B 1 324 LEU 324 324 324 LEU LEU B . n 
B 1 325 TRP 325 325 325 TRP TRP B . n 
B 1 326 PRO 326 326 326 PRO PRO B . n 
B 1 327 THR 327 327 327 THR THR B . n 
B 1 328 ALA 328 328 328 ALA ALA B . n 
B 1 329 PRO 329 329 329 PRO PRO B . n 
B 1 330 ALA 330 330 330 ALA ALA B . n 
B 1 331 PHE 331 331 331 PHE PHE B . n 
B 1 332 SER 332 332 332 SER SER B . n 
B 1 333 LEU 333 333 333 LEU LEU B . n 
B 1 334 TYR 334 334 334 TYR TYR B . n 
B 1 335 ALA 335 335 335 ALA ALA B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 GLU 337 337 337 GLU GLU B . n 
B 1 338 ASP 338 338 338 ASP ASP B . n 
B 1 339 THR 339 339 339 THR THR B . n 
B 1 340 VAL 340 340 340 VAL VAL B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 GLY 342 342 342 GLY GLY B . n 
B 1 343 GLY 343 343 343 GLY GLY B . n 
B 1 344 GLU 344 344 344 GLU GLU B . n 
B 1 345 TYR 345 345 345 TYR TYR B . n 
B 1 346 PRO 346 346 346 PRO PRO B . n 
B 1 347 LEU 347 347 347 LEU LEU B . n 
B 1 348 GLU 348 348 348 GLU GLU B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 GLY 350 350 350 GLY GLY B . n 
B 1 351 ASP 351 351 351 ASP ASP B . n 
B 1 352 GLU 352 352 352 GLU GLU B . n 
B 1 353 LEU 353 353 353 LEU LEU B . n 
B 1 354 MET 354 354 354 MET MET B . n 
B 1 355 VAL 355 355 355 VAL VAL B . n 
B 1 356 LEU 356 356 356 LEU LEU B . n 
B 1 357 ILE 357 357 357 ILE ILE B . n 
B 1 358 PRO 358 358 358 PRO PRO B . n 
B 1 359 GLN 359 359 359 GLN GLN B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 HIS 361 361 361 HIS HIS B . n 
B 1 362 ARG 362 362 362 ARG ARG B . n 
B 1 363 ASP 363 363 363 ASP ASP B . n 
B 1 364 LYS 364 364 364 LYS LYS B . n 
B 1 365 THR 365 365 365 THR THR B . n 
B 1 366 ILE 366 366 366 ILE ILE B . n 
B 1 367 TRP 367 367 367 TRP TRP B . n 
B 1 368 GLY 368 368 368 GLY GLY B . n 
B 1 369 ASP 369 369 369 ASP ASP B . n 
B 1 370 ASP 370 370 370 ASP ASP B . n 
B 1 371 VAL 371 371 371 VAL VAL B . n 
B 1 372 GLU 372 372 372 GLU GLU B . n 
B 1 373 GLU 373 373 373 GLU GLU B . n 
B 1 374 PHE 374 374 374 PHE PHE B . n 
B 1 375 ARG 375 375 375 ARG ARG B . n 
B 1 376 PRO 376 376 376 PRO PRO B . n 
B 1 377 GLU 377 377 377 GLU GLU B . n 
B 1 378 ARG 378 378 378 ARG ARG B . n 
B 1 379 PHE 379 379 379 PHE PHE B . n 
B 1 380 GLU 380 380 380 GLU GLU B . n 
B 1 381 ASN 381 381 381 ASN ASN B . n 
B 1 382 PRO 382 382 382 PRO PRO B . n 
B 1 383 SER 383 383 383 SER SER B . n 
B 1 384 ALA 384 384 384 ALA ALA B . n 
B 1 385 ILE 385 385 385 ILE ILE B . n 
B 1 386 PRO 386 386 386 PRO PRO B . n 
B 1 387 GLN 387 387 387 GLN GLN B . n 
B 1 388 HIS 388 388 388 HIS HIS B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 PHE 390 390 390 PHE PHE B . n 
B 1 391 LYS 391 391 391 LYS LYS B . n 
B 1 392 PRO 392 392 392 PRO PRO B . n 
B 1 393 HIS 393 393 393 HIS HIS B . n 
B 1 394 GLY 394 394 394 GLY GLY B . n 
B 1 395 ASN 395 395 395 ASN ASN B . n 
B 1 396 GLY 396 396 396 GLY GLY B . n 
B 1 397 GLN 397 397 397 GLN GLN B . n 
B 1 398 ARG 398 398 398 ARG ARG B . n 
B 1 399 ALA 399 399 399 ALA ALA B . n 
B 1 400 CYS 400 400 400 CYS CYS B . n 
B 1 401 ILE 401 401 401 ILE ILE B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 GLN 403 403 403 GLN GLN B . n 
B 1 404 GLN 404 404 404 GLN GLN B . n 
B 1 405 PHE 405 405 405 PHE PHE B . n 
B 1 406 ALA 406 406 406 ALA ALA B . n 
B 1 407 LEU 407 407 407 LEU LEU B . n 
B 1 408 HIS 408 408 408 HIS HIS B . n 
B 1 409 GLU 409 409 409 GLU GLU B . n 
B 1 410 ALA 410 410 410 ALA ALA B . n 
B 1 411 THR 411 411 411 THR THR B . n 
B 1 412 LEU 412 412 412 LEU LEU B . n 
B 1 413 VAL 413 413 413 VAL VAL B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 GLY 415 415 415 GLY GLY B . n 
B 1 416 MET 416 416 416 MET MET B . n 
B 1 417 MET 417 417 417 MET MET B . n 
B 1 418 LEU 418 418 418 LEU LEU B . n 
B 1 419 LYS 419 419 419 LYS LYS B . n 
B 1 420 HIS 420 420 420 HIS HIS B . n 
B 1 421 PHE 421 421 421 PHE PHE B . n 
B 1 422 ASP 422 422 422 ASP ASP B . n 
B 1 423 PHE 423 423 423 PHE PHE B . n 
B 1 424 GLU 424 424 424 GLU GLU B . n 
B 1 425 ASP 425 425 425 ASP ASP B . n 
B 1 426 HIS 426 426 426 HIS HIS B . n 
B 1 427 THR 427 427 427 THR THR B . n 
B 1 428 ASN 428 428 428 ASN ASN B . n 
B 1 429 TYR 429 429 429 TYR TYR B . n 
B 1 430 GLU 430 430 430 GLU GLU B . n 
B 1 431 LEU 431 431 431 LEU LEU B . n 
B 1 432 ASP 432 432 432 ASP ASP B . n 
B 1 433 ILE 433 433 433 ILE ILE B . n 
B 1 434 LYS 434 434 434 LYS LYS B . n 
B 1 435 GLU 435 435 435 GLU GLU B . n 
B 1 436 THR 436 436 436 THR THR B . n 
B 1 437 LEU 437 437 437 LEU LEU B . n 
B 1 438 THR 438 438 438 THR THR B . n 
B 1 439 LEU 439 439 439 LEU LEU B . n 
B 1 440 LYS 440 440 440 LYS LYS B . n 
B 1 441 PRO 441 441 441 PRO PRO B . n 
B 1 442 GLU 442 442 442 GLU GLU B . n 
B 1 443 GLY 443 443 443 GLY GLY B . n 
B 1 444 PHE 444 444 444 PHE PHE B . n 
B 1 445 VAL 445 445 445 VAL VAL B . n 
B 1 446 VAL 446 446 446 VAL VAL B . n 
B 1 447 LYS 447 447 447 LYS LYS B . n 
B 1 448 ALA 448 448 448 ALA ALA B . n 
B 1 449 LYS 449 449 449 LYS LYS B . n 
B 1 450 SER 450 450 450 SER SER B . n 
B 1 451 LYS 451 451 451 LYS LYS B . n 
B 1 452 LYS 452 452 452 LYS LYS B . n 
B 1 453 ILE 453 453 453 ILE ILE B . n 
B 1 454 PRO 454 454 454 PRO PRO B . n 
B 1 455 LEU 455 455 455 LEU LEU B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 HEM ? ? HEM ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SYN ? ? SYN ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEM 1   501  501 HEM HEM A . 
D 3 D0L 1   502  503 D0L 7PF A . 
E 4 SYN 1   503  601 SYN SYN A . 
F 5 GOL 1   504  602 GOL GOL A . 
G 5 GOL 1   505  603 GOL GOL A . 
H 5 GOL 1   506  604 GOL GOL A . 
I 2 HEM 1   501  501 HEM HEM B . 
J 3 D0L 1   502  503 D0L 7PF B . 
K 4 SYN 1   503  601 SYN SYN B . 
L 5 GOL 1   504  602 GOL GOL B . 
M 5 GOL 1   505  603 GOL GOL B . 
N 5 GOL 1   506  604 GOL GOL B . 
O 5 GOL 1   507  605 GOL GOL B . 
P 5 GOL 1   508  606 GOL GOL B . 
Q 6 HOH 1   601  861 HOH HOH A . 
Q 6 HOH 2   602  859 HOH HOH A . 
Q 6 HOH 3   603  215 HOH HOH A . 
Q 6 HOH 4   604  425 HOH HOH A . 
Q 6 HOH 5   605  738 HOH HOH A . 
Q 6 HOH 6   606  657 HOH HOH A . 
Q 6 HOH 7   607  721 HOH HOH A . 
Q 6 HOH 8   608  580 HOH HOH A . 
Q 6 HOH 9   609  621 HOH HOH A . 
Q 6 HOH 10  610  202 HOH HOH A . 
Q 6 HOH 11  611  556 HOH HOH A . 
Q 6 HOH 12  612  521 HOH HOH A . 
Q 6 HOH 13  613  122 HOH HOH A . 
Q 6 HOH 14  614  544 HOH HOH A . 
Q 6 HOH 15  615  493 HOH HOH A . 
Q 6 HOH 16  616  481 HOH HOH A . 
Q 6 HOH 17  617  652 HOH HOH A . 
Q 6 HOH 18  618  564 HOH HOH A . 
Q 6 HOH 19  619  309 HOH HOH A . 
Q 6 HOH 20  620  701 HOH HOH A . 
Q 6 HOH 21  621  866 HOH HOH A . 
Q 6 HOH 22  622  524 HOH HOH A . 
Q 6 HOH 23  623  601 HOH HOH A . 
Q 6 HOH 24  624  747 HOH HOH A . 
Q 6 HOH 25  625  641 HOH HOH A . 
Q 6 HOH 26  626  248 HOH HOH A . 
Q 6 HOH 27  627  873 HOH HOH A . 
Q 6 HOH 28  628  643 HOH HOH A . 
Q 6 HOH 29  629  8   HOH HOH A . 
Q 6 HOH 30  630  788 HOH HOH A . 
Q 6 HOH 31  631  154 HOH HOH A . 
Q 6 HOH 32  632  320 HOH HOH A . 
Q 6 HOH 33  633  61  HOH HOH A . 
Q 6 HOH 34  634  438 HOH HOH A . 
Q 6 HOH 35  635  282 HOH HOH A . 
Q 6 HOH 36  636  269 HOH HOH A . 
Q 6 HOH 37  637  487 HOH HOH A . 
Q 6 HOH 38  638  614 HOH HOH A . 
Q 6 HOH 39  639  551 HOH HOH A . 
Q 6 HOH 40  640  18  HOH HOH A . 
Q 6 HOH 41  641  646 HOH HOH A . 
Q 6 HOH 42  642  168 HOH HOH A . 
Q 6 HOH 43  643  622 HOH HOH A . 
Q 6 HOH 44  644  205 HOH HOH A . 
Q 6 HOH 45  645  760 HOH HOH A . 
Q 6 HOH 46  646  62  HOH HOH A . 
Q 6 HOH 47  647  520 HOH HOH A . 
Q 6 HOH 48  648  227 HOH HOH A . 
Q 6 HOH 49  649  851 HOH HOH A . 
Q 6 HOH 50  650  34  HOH HOH A . 
Q 6 HOH 51  651  95  HOH HOH A . 
Q 6 HOH 52  652  404 HOH HOH A . 
Q 6 HOH 53  653  333 HOH HOH A . 
Q 6 HOH 54  654  381 HOH HOH A . 
Q 6 HOH 55  655  579 HOH HOH A . 
Q 6 HOH 56  656  714 HOH HOH A . 
Q 6 HOH 57  657  402 HOH HOH A . 
Q 6 HOH 58  658  75  HOH HOH A . 
Q 6 HOH 59  659  52  HOH HOH A . 
Q 6 HOH 60  660  51  HOH HOH A . 
Q 6 HOH 61  661  383 HOH HOH A . 
Q 6 HOH 62  662  70  HOH HOH A . 
Q 6 HOH 63  663  79  HOH HOH A . 
Q 6 HOH 64  664  505 HOH HOH A . 
Q 6 HOH 65  665  64  HOH HOH A . 
Q 6 HOH 66  666  153 HOH HOH A . 
Q 6 HOH 67  667  193 HOH HOH A . 
Q 6 HOH 68  668  163 HOH HOH A . 
Q 6 HOH 69  669  19  HOH HOH A . 
Q 6 HOH 70  670  354 HOH HOH A . 
Q 6 HOH 71  671  538 HOH HOH A . 
Q 6 HOH 72  672  625 HOH HOH A . 
Q 6 HOH 73  673  663 HOH HOH A . 
Q 6 HOH 74  674  597 HOH HOH A . 
Q 6 HOH 75  675  385 HOH HOH A . 
Q 6 HOH 76  676  200 HOH HOH A . 
Q 6 HOH 77  677  245 HOH HOH A . 
Q 6 HOH 78  678  369 HOH HOH A . 
Q 6 HOH 79  679  281 HOH HOH A . 
Q 6 HOH 80  680  81  HOH HOH A . 
Q 6 HOH 81  681  547 HOH HOH A . 
Q 6 HOH 82  682  588 HOH HOH A . 
Q 6 HOH 83  683  305 HOH HOH A . 
Q 6 HOH 84  684  716 HOH HOH A . 
Q 6 HOH 85  685  313 HOH HOH A . 
Q 6 HOH 86  686  415 HOH HOH A . 
Q 6 HOH 87  687  162 HOH HOH A . 
Q 6 HOH 88  688  102 HOH HOH A . 
Q 6 HOH 89  689  768 HOH HOH A . 
Q 6 HOH 90  690  50  HOH HOH A . 
Q 6 HOH 91  691  749 HOH HOH A . 
Q 6 HOH 92  692  1   HOH HOH A . 
Q 6 HOH 93  693  325 HOH HOH A . 
Q 6 HOH 94  694  783 HOH HOH A . 
Q 6 HOH 95  695  761 HOH HOH A . 
Q 6 HOH 96  696  775 HOH HOH A . 
Q 6 HOH 97  697  66  HOH HOH A . 
Q 6 HOH 98  698  442 HOH HOH A . 
Q 6 HOH 99  699  195 HOH HOH A . 
Q 6 HOH 100 700  177 HOH HOH A . 
Q 6 HOH 101 701  723 HOH HOH A . 
Q 6 HOH 102 702  15  HOH HOH A . 
Q 6 HOH 103 703  82  HOH HOH A . 
Q 6 HOH 104 704  429 HOH HOH A . 
Q 6 HOH 105 705  300 HOH HOH A . 
Q 6 HOH 106 706  179 HOH HOH A . 
Q 6 HOH 107 707  96  HOH HOH A . 
Q 6 HOH 108 708  38  HOH HOH A . 
Q 6 HOH 109 709  242 HOH HOH A . 
Q 6 HOH 110 710  94  HOH HOH A . 
Q 6 HOH 111 711  545 HOH HOH A . 
Q 6 HOH 112 712  664 HOH HOH A . 
Q 6 HOH 113 713  92  HOH HOH A . 
Q 6 HOH 114 714  22  HOH HOH A . 
Q 6 HOH 115 715  181 HOH HOH A . 
Q 6 HOH 116 716  659 HOH HOH A . 
Q 6 HOH 117 717  262 HOH HOH A . 
Q 6 HOH 118 718  357 HOH HOH A . 
Q 6 HOH 119 719  537 HOH HOH A . 
Q 6 HOH 120 720  347 HOH HOH A . 
Q 6 HOH 121 721  201 HOH HOH A . 
Q 6 HOH 122 722  213 HOH HOH A . 
Q 6 HOH 123 723  387 HOH HOH A . 
Q 6 HOH 124 724  190 HOH HOH A . 
Q 6 HOH 125 725  240 HOH HOH A . 
Q 6 HOH 126 726  12  HOH HOH A . 
Q 6 HOH 127 727  165 HOH HOH A . 
Q 6 HOH 128 728  683 HOH HOH A . 
Q 6 HOH 129 729  595 HOH HOH A . 
Q 6 HOH 130 730  204 HOH HOH A . 
Q 6 HOH 131 731  572 HOH HOH A . 
Q 6 HOH 132 732  67  HOH HOH A . 
Q 6 HOH 133 733  99  HOH HOH A . 
Q 6 HOH 134 734  159 HOH HOH A . 
Q 6 HOH 135 735  230 HOH HOH A . 
Q 6 HOH 136 736  48  HOH HOH A . 
Q 6 HOH 137 737  782 HOH HOH A . 
Q 6 HOH 138 738  161 HOH HOH A . 
Q 6 HOH 139 739  408 HOH HOH A . 
Q 6 HOH 140 740  630 HOH HOH A . 
Q 6 HOH 141 741  617 HOH HOH A . 
Q 6 HOH 142 742  329 HOH HOH A . 
Q 6 HOH 143 743  37  HOH HOH A . 
Q 6 HOH 144 744  377 HOH HOH A . 
Q 6 HOH 145 745  84  HOH HOH A . 
Q 6 HOH 146 746  188 HOH HOH A . 
Q 6 HOH 147 747  334 HOH HOH A . 
Q 6 HOH 148 748  375 HOH HOH A . 
Q 6 HOH 149 749  655 HOH HOH A . 
Q 6 HOH 150 750  257 HOH HOH A . 
Q 6 HOH 151 751  512 HOH HOH A . 
Q 6 HOH 152 752  596 HOH HOH A . 
Q 6 HOH 153 753  137 HOH HOH A . 
Q 6 HOH 154 754  16  HOH HOH A . 
Q 6 HOH 155 755  103 HOH HOH A . 
Q 6 HOH 156 756  779 HOH HOH A . 
Q 6 HOH 157 757  138 HOH HOH A . 
Q 6 HOH 158 758  132 HOH HOH A . 
Q 6 HOH 159 759  209 HOH HOH A . 
Q 6 HOH 160 760  288 HOH HOH A . 
Q 6 HOH 161 761  508 HOH HOH A . 
Q 6 HOH 162 762  203 HOH HOH A . 
Q 6 HOH 163 763  9   HOH HOH A . 
Q 6 HOH 164 764  417 HOH HOH A . 
Q 6 HOH 165 765  361 HOH HOH A . 
Q 6 HOH 166 766  238 HOH HOH A . 
Q 6 HOH 167 767  296 HOH HOH A . 
Q 6 HOH 168 768  534 HOH HOH A . 
Q 6 HOH 169 769  726 HOH HOH A . 
Q 6 HOH 170 770  808 HOH HOH A . 
Q 6 HOH 171 771  125 HOH HOH A . 
Q 6 HOH 172 772  6   HOH HOH A . 
Q 6 HOH 173 773  518 HOH HOH A . 
Q 6 HOH 174 774  26  HOH HOH A . 
Q 6 HOH 175 775  393 HOH HOH A . 
Q 6 HOH 176 776  27  HOH HOH A . 
Q 6 HOH 177 777  114 HOH HOH A . 
Q 6 HOH 178 778  139 HOH HOH A . 
Q 6 HOH 179 779  55  HOH HOH A . 
Q 6 HOH 180 780  765 HOH HOH A . 
Q 6 HOH 181 781  233 HOH HOH A . 
Q 6 HOH 182 782  800 HOH HOH A . 
Q 6 HOH 183 783  810 HOH HOH A . 
Q 6 HOH 184 784  832 HOH HOH A . 
Q 6 HOH 185 785  390 HOH HOH A . 
Q 6 HOH 186 786  500 HOH HOH A . 
Q 6 HOH 187 787  117 HOH HOH A . 
Q 6 HOH 188 788  119 HOH HOH A . 
Q 6 HOH 189 789  306 HOH HOH A . 
Q 6 HOH 190 790  475 HOH HOH A . 
Q 6 HOH 191 791  53  HOH HOH A . 
Q 6 HOH 192 792  342 HOH HOH A . 
Q 6 HOH 193 793  448 HOH HOH A . 
Q 6 HOH 194 794  685 HOH HOH A . 
Q 6 HOH 195 795  74  HOH HOH A . 
Q 6 HOH 196 796  263 HOH HOH A . 
Q 6 HOH 197 797  365 HOH HOH A . 
Q 6 HOH 198 798  259 HOH HOH A . 
Q 6 HOH 199 799  741 HOH HOH A . 
Q 6 HOH 200 800  529 HOH HOH A . 
Q 6 HOH 201 801  546 HOH HOH A . 
Q 6 HOH 202 802  793 HOH HOH A . 
Q 6 HOH 203 803  292 HOH HOH A . 
Q 6 HOH 204 804  684 HOH HOH A . 
Q 6 HOH 205 805  17  HOH HOH A . 
Q 6 HOH 206 806  468 HOH HOH A . 
Q 6 HOH 207 807  312 HOH HOH A . 
Q 6 HOH 208 808  73  HOH HOH A . 
Q 6 HOH 209 809  228 HOH HOH A . 
Q 6 HOH 210 810  208 HOH HOH A . 
Q 6 HOH 211 811  486 HOH HOH A . 
Q 6 HOH 212 812  519 HOH HOH A . 
Q 6 HOH 213 813  317 HOH HOH A . 
Q 6 HOH 214 814  331 HOH HOH A . 
Q 6 HOH 215 815  777 HOH HOH A . 
Q 6 HOH 216 816  207 HOH HOH A . 
Q 6 HOH 217 817  792 HOH HOH A . 
Q 6 HOH 218 818  336 HOH HOH A . 
Q 6 HOH 219 819  758 HOH HOH A . 
Q 6 HOH 220 820  374 HOH HOH A . 
Q 6 HOH 221 821  366 HOH HOH A . 
Q 6 HOH 222 822  219 HOH HOH A . 
Q 6 HOH 223 823  278 HOH HOH A . 
Q 6 HOH 224 824  183 HOH HOH A . 
Q 6 HOH 225 825  145 HOH HOH A . 
Q 6 HOH 226 826  93  HOH HOH A . 
Q 6 HOH 227 827  58  HOH HOH A . 
Q 6 HOH 228 828  674 HOH HOH A . 
Q 6 HOH 229 829  98  HOH HOH A . 
Q 6 HOH 230 830  694 HOH HOH A . 
Q 6 HOH 231 831  45  HOH HOH A . 
Q 6 HOH 232 832  284 HOH HOH A . 
Q 6 HOH 233 833  297 HOH HOH A . 
Q 6 HOH 234 834  598 HOH HOH A . 
Q 6 HOH 235 835  135 HOH HOH A . 
Q 6 HOH 236 836  252 HOH HOH A . 
Q 6 HOH 237 837  231 HOH HOH A . 
Q 6 HOH 238 838  254 HOH HOH A . 
Q 6 HOH 239 839  744 HOH HOH A . 
Q 6 HOH 240 840  152 HOH HOH A . 
Q 6 HOH 241 841  20  HOH HOH A . 
Q 6 HOH 242 842  211 HOH HOH A . 
Q 6 HOH 243 843  266 HOH HOH A . 
Q 6 HOH 244 844  651 HOH HOH A . 
Q 6 HOH 245 845  573 HOH HOH A . 
Q 6 HOH 246 846  167 HOH HOH A . 
Q 6 HOH 247 847  821 HOH HOH A . 
Q 6 HOH 248 848  797 HOH HOH A . 
Q 6 HOH 249 849  416 HOH HOH A . 
Q 6 HOH 250 850  160 HOH HOH A . 
Q 6 HOH 251 851  796 HOH HOH A . 
Q 6 HOH 252 852  358 HOH HOH A . 
Q 6 HOH 253 853  389 HOH HOH A . 
Q 6 HOH 254 854  618 HOH HOH A . 
Q 6 HOH 255 855  780 HOH HOH A . 
Q 6 HOH 256 856  326 HOH HOH A . 
Q 6 HOH 257 857  826 HOH HOH A . 
Q 6 HOH 258 858  324 HOH HOH A . 
Q 6 HOH 259 859  815 HOH HOH A . 
Q 6 HOH 260 860  419 HOH HOH A . 
Q 6 HOH 261 861  682 HOH HOH A . 
Q 6 HOH 262 862  790 HOH HOH A . 
Q 6 HOH 263 863  443 HOH HOH A . 
Q 6 HOH 264 864  454 HOH HOH A . 
Q 6 HOH 265 865  403 HOH HOH A . 
Q 6 HOH 266 866  199 HOH HOH A . 
Q 6 HOH 267 867  105 HOH HOH A . 
Q 6 HOH 268 868  286 HOH HOH A . 
Q 6 HOH 269 869  461 HOH HOH A . 
Q 6 HOH 270 870  314 HOH HOH A . 
Q 6 HOH 271 871  766 HOH HOH A . 
Q 6 HOH 272 872  294 HOH HOH A . 
Q 6 HOH 273 873  735 HOH HOH A . 
Q 6 HOH 274 874  699 HOH HOH A . 
Q 6 HOH 275 875  107 HOH HOH A . 
Q 6 HOH 276 876  589 HOH HOH A . 
Q 6 HOH 277 877  89  HOH HOH A . 
Q 6 HOH 278 878  499 HOH HOH A . 
Q 6 HOH 279 879  47  HOH HOH A . 
Q 6 HOH 280 880  304 HOH HOH A . 
Q 6 HOH 281 881  108 HOH HOH A . 
Q 6 HOH 282 882  740 HOH HOH A . 
Q 6 HOH 283 883  599 HOH HOH A . 
Q 6 HOH 284 884  405 HOH HOH A . 
Q 6 HOH 285 885  474 HOH HOH A . 
Q 6 HOH 286 886  290 HOH HOH A . 
Q 6 HOH 287 887  206 HOH HOH A . 
Q 6 HOH 288 888  585 HOH HOH A . 
Q 6 HOH 289 889  852 HOH HOH A . 
Q 6 HOH 290 890  730 HOH HOH A . 
Q 6 HOH 291 891  874 HOH HOH A . 
Q 6 HOH 292 892  490 HOH HOH A . 
Q 6 HOH 293 893  633 HOH HOH A . 
Q 6 HOH 294 894  590 HOH HOH A . 
Q 6 HOH 295 895  776 HOH HOH A . 
Q 6 HOH 296 896  100 HOH HOH A . 
Q 6 HOH 297 897  870 HOH HOH A . 
Q 6 HOH 298 898  220 HOH HOH A . 
Q 6 HOH 299 899  604 HOH HOH A . 
Q 6 HOH 300 900  711 HOH HOH A . 
Q 6 HOH 301 901  249 HOH HOH A . 
Q 6 HOH 302 902  750 HOH HOH A . 
Q 6 HOH 303 903  608 HOH HOH A . 
Q 6 HOH 304 904  728 HOH HOH A . 
Q 6 HOH 305 905  216 HOH HOH A . 
Q 6 HOH 306 906  720 HOH HOH A . 
Q 6 HOH 307 907  224 HOH HOH A . 
Q 6 HOH 308 908  504 HOH HOH A . 
Q 6 HOH 309 909  813 HOH HOH A . 
Q 6 HOH 310 910  856 HOH HOH A . 
Q 6 HOH 311 911  764 HOH HOH A . 
Q 6 HOH 312 912  523 HOH HOH A . 
Q 6 HOH 313 913  755 HOH HOH A . 
Q 6 HOH 314 914  283 HOH HOH A . 
Q 6 HOH 315 915  613 HOH HOH A . 
Q 6 HOH 316 916  428 HOH HOH A . 
Q 6 HOH 317 917  769 HOH HOH A . 
Q 6 HOH 318 918  833 HOH HOH A . 
Q 6 HOH 319 919  773 HOH HOH A . 
Q 6 HOH 320 920  752 HOH HOH A . 
Q 6 HOH 321 921  446 HOH HOH A . 
Q 6 HOH 322 922  642 HOH HOH A . 
Q 6 HOH 323 923  756 HOH HOH A . 
Q 6 HOH 324 924  447 HOH HOH A . 
Q 6 HOH 325 925  515 HOH HOH A . 
Q 6 HOH 326 926  842 HOH HOH A . 
Q 6 HOH 327 927  413 HOH HOH A . 
Q 6 HOH 328 928  834 HOH HOH A . 
Q 6 HOH 329 929  506 HOH HOH A . 
Q 6 HOH 330 930  785 HOH HOH A . 
Q 6 HOH 331 931  310 HOH HOH A . 
Q 6 HOH 332 932  803 HOH HOH A . 
Q 6 HOH 333 933  677 HOH HOH A . 
Q 6 HOH 334 934  805 HOH HOH A . 
Q 6 HOH 335 935  806 HOH HOH A . 
Q 6 HOH 336 936  536 HOH HOH A . 
Q 6 HOH 337 937  570 HOH HOH A . 
Q 6 HOH 338 938  492 HOH HOH A . 
Q 6 HOH 339 939  804 HOH HOH A . 
Q 6 HOH 340 940  827 HOH HOH A . 
Q 6 HOH 341 941  13  HOH HOH A . 
Q 6 HOH 342 942  600 HOH HOH A . 
Q 6 HOH 343 943  562 HOH HOH A . 
Q 6 HOH 344 944  584 HOH HOH A . 
Q 6 HOH 345 945  830 HOH HOH A . 
Q 6 HOH 346 946  574 HOH HOH A . 
Q 6 HOH 347 947  418 HOH HOH A . 
Q 6 HOH 348 948  169 HOH HOH A . 
Q 6 HOH 349 949  639 HOH HOH A . 
Q 6 HOH 350 950  837 HOH HOH A . 
Q 6 HOH 351 951  857 HOH HOH A . 
Q 6 HOH 352 952  541 HOH HOH A . 
Q 6 HOH 353 953  321 HOH HOH A . 
Q 6 HOH 354 954  798 HOH HOH A . 
Q 6 HOH 355 955  218 HOH HOH A . 
Q 6 HOH 356 956  587 HOH HOH A . 
Q 6 HOH 357 957  502 HOH HOH A . 
Q 6 HOH 358 958  802 HOH HOH A . 
Q 6 HOH 359 959  736 HOH HOH A . 
Q 6 HOH 360 960  526 HOH HOH A . 
Q 6 HOH 361 961  527 HOH HOH A . 
Q 6 HOH 362 962  713 HOH HOH A . 
Q 6 HOH 363 963  561 HOH HOH A . 
Q 6 HOH 364 964  476 HOH HOH A . 
Q 6 HOH 365 965  739 HOH HOH A . 
Q 6 HOH 366 966  318 HOH HOH A . 
Q 6 HOH 367 967  539 HOH HOH A . 
Q 6 HOH 368 968  323 HOH HOH A . 
Q 6 HOH 369 969  661 HOH HOH A . 
Q 6 HOH 370 970  555 HOH HOH A . 
Q 6 HOH 371 971  532 HOH HOH A . 
Q 6 HOH 372 972  434 HOH HOH A . 
Q 6 HOH 373 973  695 HOH HOH A . 
Q 6 HOH 374 974  771 HOH HOH A . 
Q 6 HOH 375 975  287 HOH HOH A . 
Q 6 HOH 376 976  609 HOH HOH A . 
Q 6 HOH 377 977  703 HOH HOH A . 
Q 6 HOH 378 978  423 HOH HOH A . 
Q 6 HOH 379 979  624 HOH HOH A . 
Q 6 HOH 380 980  467 HOH HOH A . 
Q 6 HOH 381 981  316 HOH HOH A . 
Q 6 HOH 382 982  340 HOH HOH A . 
Q 6 HOH 383 983  814 HOH HOH A . 
Q 6 HOH 384 984  846 HOH HOH A . 
Q 6 HOH 385 985  686 HOH HOH A . 
Q 6 HOH 386 986  654 HOH HOH A . 
Q 6 HOH 387 987  724 HOH HOH A . 
Q 6 HOH 388 988  560 HOH HOH A . 
Q 6 HOH 389 989  460 HOH HOH A . 
Q 6 HOH 390 990  449 HOH HOH A . 
Q 6 HOH 391 991  734 HOH HOH A . 
Q 6 HOH 392 992  729 HOH HOH A . 
Q 6 HOH 393 993  243 HOH HOH A . 
Q 6 HOH 394 994  676 HOH HOH A . 
Q 6 HOH 395 995  710 HOH HOH A . 
Q 6 HOH 396 996  843 HOH HOH A . 
Q 6 HOH 397 997  696 HOH HOH A . 
Q 6 HOH 398 998  234 HOH HOH A . 
Q 6 HOH 399 999  847 HOH HOH A . 
Q 6 HOH 400 1000 364 HOH HOH A . 
Q 6 HOH 401 1001 825 HOH HOH A . 
Q 6 HOH 402 1002 801 HOH HOH A . 
Q 6 HOH 403 1003 820 HOH HOH A . 
Q 6 HOH 404 1004 850 HOH HOH A . 
R 6 HOH 1   601  862 HOH HOH B . 
R 6 HOH 2   602  791 HOH HOH B . 
R 6 HOH 3   603  611 HOH HOH B . 
R 6 HOH 4   604  863 HOH HOH B . 
R 6 HOH 5   605  605 HOH HOH B . 
R 6 HOH 6   606  276 HOH HOH B . 
R 6 HOH 7   607  732 HOH HOH B . 
R 6 HOH 8   608  637 HOH HOH B . 
R 6 HOH 9   609  510 HOH HOH B . 
R 6 HOH 10  610  509 HOH HOH B . 
R 6 HOH 11  611  557 HOH HOH B . 
R 6 HOH 12  612  558 HOH HOH B . 
R 6 HOH 13  613  542 HOH HOH B . 
R 6 HOH 14  614  485 HOH HOH B . 
R 6 HOH 15  615  422 HOH HOH B . 
R 6 HOH 16  616  671 HOH HOH B . 
R 6 HOH 17  617  535 HOH HOH B . 
R 6 HOH 18  618  348 HOH HOH B . 
R 6 HOH 19  619  872 HOH HOH B . 
R 6 HOH 20  620  258 HOH HOH B . 
R 6 HOH 21  621  398 HOH HOH B . 
R 6 HOH 22  622  647 HOH HOH B . 
R 6 HOH 23  623  391 HOH HOH B . 
R 6 HOH 24  624  868 HOH HOH B . 
R 6 HOH 25  625  380 HOH HOH B . 
R 6 HOH 26  626  496 HOH HOH B . 
R 6 HOH 27  627  591 HOH HOH B . 
R 6 HOH 28  628  483 HOH HOH B . 
R 6 HOH 29  629  444 HOH HOH B . 
R 6 HOH 30  630  349 HOH HOH B . 
R 6 HOH 31  631  575 HOH HOH B . 
R 6 HOH 32  632  268 HOH HOH B . 
R 6 HOH 33  633  632 HOH HOH B . 
R 6 HOH 34  634  848 HOH HOH B . 
R 6 HOH 35  635  261 HOH HOH B . 
R 6 HOH 36  636  236 HOH HOH B . 
R 6 HOH 37  637  795 HOH HOH B . 
R 6 HOH 38  638  631 HOH HOH B . 
R 6 HOH 39  639  488 HOH HOH B . 
R 6 HOH 40  640  384 HOH HOH B . 
R 6 HOH 41  641  221 HOH HOH B . 
R 6 HOH 42  642  463 HOH HOH B . 
R 6 HOH 43  643  244 HOH HOH B . 
R 6 HOH 44  644  871 HOH HOH B . 
R 6 HOH 45  645  7   HOH HOH B . 
R 6 HOH 46  646  174 HOH HOH B . 
R 6 HOH 47  647  424 HOH HOH B . 
R 6 HOH 48  648  277 HOH HOH B . 
R 6 HOH 49  649  175 HOH HOH B . 
R 6 HOH 50  650  727 HOH HOH B . 
R 6 HOH 51  651  56  HOH HOH B . 
R 6 HOH 52  652  101 HOH HOH B . 
R 6 HOH 53  653  274 HOH HOH B . 
R 6 HOH 54  654  307 HOH HOH B . 
R 6 HOH 55  655  24  HOH HOH B . 
R 6 HOH 56  656  498 HOH HOH B . 
R 6 HOH 57  657  757 HOH HOH B . 
R 6 HOH 58  658  586 HOH HOH B . 
R 6 HOH 59  659  533 HOH HOH B . 
R 6 HOH 60  660  412 HOH HOH B . 
R 6 HOH 61  661  123 HOH HOH B . 
R 6 HOH 62  662  623 HOH HOH B . 
R 6 HOH 63  663  731 HOH HOH B . 
R 6 HOH 64  664  222 HOH HOH B . 
R 6 HOH 65  665  83  HOH HOH B . 
R 6 HOH 66  666  49  HOH HOH B . 
R 6 HOH 67  667  786 HOH HOH B . 
R 6 HOH 68  668  133 HOH HOH B . 
R 6 HOH 69  669  315 HOH HOH B . 
R 6 HOH 70  670  432 HOH HOH B . 
R 6 HOH 71  671  189 HOH HOH B . 
R 6 HOH 72  672  718 HOH HOH B . 
R 6 HOH 73  673  359 HOH HOH B . 
R 6 HOH 74  674  65  HOH HOH B . 
R 6 HOH 75  675  302 HOH HOH B . 
R 6 HOH 76  676  260 HOH HOH B . 
R 6 HOH 77  677  667 HOH HOH B . 
R 6 HOH 78  678  295 HOH HOH B . 
R 6 HOH 79  679  869 HOH HOH B . 
R 6 HOH 80  680  552 HOH HOH B . 
R 6 HOH 81  681  112 HOH HOH B . 
R 6 HOH 82  682  68  HOH HOH B . 
R 6 HOH 83  683  129 HOH HOH B . 
R 6 HOH 84  684  182 HOH HOH B . 
R 6 HOH 85  685  531 HOH HOH B . 
R 6 HOH 86  686  279 HOH HOH B . 
R 6 HOH 87  687  540 HOH HOH B . 
R 6 HOH 88  688  568 HOH HOH B . 
R 6 HOH 89  689  80  HOH HOH B . 
R 6 HOH 90  690  592 HOH HOH B . 
R 6 HOH 91  691  164 HOH HOH B . 
R 6 HOH 92  692  115 HOH HOH B . 
R 6 HOH 93  693  149 HOH HOH B . 
R 6 HOH 94  694  606 HOH HOH B . 
R 6 HOH 95  695  265 HOH HOH B . 
R 6 HOH 96  696  57  HOH HOH B . 
R 6 HOH 97  697  453 HOH HOH B . 
R 6 HOH 98  698  603 HOH HOH B . 
R 6 HOH 99  699  337 HOH HOH B . 
R 6 HOH 100 700  28  HOH HOH B . 
R 6 HOH 101 701  275 HOH HOH B . 
R 6 HOH 102 702  675 HOH HOH B . 
R 6 HOH 103 703  426 HOH HOH B . 
R 6 HOH 104 704  131 HOH HOH B . 
R 6 HOH 105 705  482 HOH HOH B . 
R 6 HOH 106 706  246 HOH HOH B . 
R 6 HOH 107 707  71  HOH HOH B . 
R 6 HOH 108 708  113 HOH HOH B . 
R 6 HOH 109 709  799 HOH HOH B . 
R 6 HOH 110 710  155 HOH HOH B . 
R 6 HOH 111 711  3   HOH HOH B . 
R 6 HOH 112 712  241 HOH HOH B . 
R 6 HOH 113 713  822 HOH HOH B . 
R 6 HOH 114 714  158 HOH HOH B . 
R 6 HOH 115 715  186 HOH HOH B . 
R 6 HOH 116 716  673 HOH HOH B . 
R 6 HOH 117 717  528 HOH HOH B . 
R 6 HOH 118 718  303 HOH HOH B . 
R 6 HOH 119 719  33  HOH HOH B . 
R 6 HOH 120 720  459 HOH HOH B . 
R 6 HOH 121 721  409 HOH HOH B . 
R 6 HOH 122 722  156 HOH HOH B . 
R 6 HOH 123 723  433 HOH HOH B . 
R 6 HOH 124 724  401 HOH HOH B . 
R 6 HOH 125 725  90  HOH HOH B . 
R 6 HOH 126 726  494 HOH HOH B . 
R 6 HOH 127 727  25  HOH HOH B . 
R 6 HOH 128 728  121 HOH HOH B . 
R 6 HOH 129 729  679 HOH HOH B . 
R 6 HOH 130 730  31  HOH HOH B . 
R 6 HOH 131 731  116 HOH HOH B . 
R 6 HOH 132 732  110 HOH HOH B . 
R 6 HOH 133 733  626 HOH HOH B . 
R 6 HOH 134 734  5   HOH HOH B . 
R 6 HOH 135 735  484 HOH HOH B . 
R 6 HOH 136 736  610 HOH HOH B . 
R 6 HOH 137 737  612 HOH HOH B . 
R 6 HOH 138 738  192 HOH HOH B . 
R 6 HOH 139 739  85  HOH HOH B . 
R 6 HOH 140 740  411 HOH HOH B . 
R 6 HOH 141 741  666 HOH HOH B . 
R 6 HOH 142 742  346 HOH HOH B . 
R 6 HOH 143 743  176 HOH HOH B . 
R 6 HOH 144 744  330 HOH HOH B . 
R 6 HOH 145 745  392 HOH HOH B . 
R 6 HOH 146 746  650 HOH HOH B . 
R 6 HOH 147 747  840 HOH HOH B . 
R 6 HOH 148 748  745 HOH HOH B . 
R 6 HOH 149 749  620 HOH HOH B . 
R 6 HOH 150 750  854 HOH HOH B . 
R 6 HOH 151 751  109 HOH HOH B . 
R 6 HOH 152 752  437 HOH HOH B . 
R 6 HOH 153 753  130 HOH HOH B . 
R 6 HOH 154 754  270 HOH HOH B . 
R 6 HOH 155 755  180 HOH HOH B . 
R 6 HOH 156 756  414 HOH HOH B . 
R 6 HOH 157 757  147 HOH HOH B . 
R 6 HOH 158 758  338 HOH HOH B . 
R 6 HOH 159 759  72  HOH HOH B . 
R 6 HOH 160 760  742 HOH HOH B . 
R 6 HOH 161 761  76  HOH HOH B . 
R 6 HOH 162 762  253 HOH HOH B . 
R 6 HOH 163 763  54  HOH HOH B . 
R 6 HOH 164 764  649 HOH HOH B . 
R 6 HOH 165 765  184 HOH HOH B . 
R 6 HOH 166 766  21  HOH HOH B . 
R 6 HOH 167 767  362 HOH HOH B . 
R 6 HOH 168 768  267 HOH HOH B . 
R 6 HOH 169 769  693 HOH HOH B . 
R 6 HOH 170 770  602 HOH HOH B . 
R 6 HOH 171 771  42  HOH HOH B . 
R 6 HOH 172 772  583 HOH HOH B . 
R 6 HOH 173 773  754 HOH HOH B . 
R 6 HOH 174 774  91  HOH HOH B . 
R 6 HOH 175 775  10  HOH HOH B . 
R 6 HOH 176 776  39  HOH HOH B . 
R 6 HOH 177 777  343 HOH HOH B . 
R 6 HOH 178 778  514 HOH HOH B . 
R 6 HOH 179 779  40  HOH HOH B . 
R 6 HOH 180 780  126 HOH HOH B . 
R 6 HOH 181 781  60  HOH HOH B . 
R 6 HOH 182 782  634 HOH HOH B . 
R 6 HOH 183 783  4   HOH HOH B . 
R 6 HOH 184 784  378 HOH HOH B . 
R 6 HOH 185 785  350 HOH HOH B . 
R 6 HOH 186 786  372 HOH HOH B . 
R 6 HOH 187 787  2   HOH HOH B . 
R 6 HOH 188 788  353 HOH HOH B . 
R 6 HOH 189 789  78  HOH HOH B . 
R 6 HOH 190 790  273 HOH HOH B . 
R 6 HOH 191 791  462 HOH HOH B . 
R 6 HOH 192 792  662 HOH HOH B . 
R 6 HOH 193 793  146 HOH HOH B . 
R 6 HOH 194 794  250 HOH HOH B . 
R 6 HOH 195 795  86  HOH HOH B . 
R 6 HOH 196 796  124 HOH HOH B . 
R 6 HOH 197 797  516 HOH HOH B . 
R 6 HOH 198 798  503 HOH HOH B . 
R 6 HOH 199 799  507 HOH HOH B . 
R 6 HOH 200 800  166 HOH HOH B . 
R 6 HOH 201 801  477 HOH HOH B . 
R 6 HOH 202 802  69  HOH HOH B . 
R 6 HOH 203 803  30  HOH HOH B . 
R 6 HOH 204 804  351 HOH HOH B . 
R 6 HOH 205 805  360 HOH HOH B . 
R 6 HOH 206 806  700 HOH HOH B . 
R 6 HOH 207 807  751 HOH HOH B . 
R 6 HOH 208 808  322 HOH HOH B . 
R 6 HOH 209 809  187 HOH HOH B . 
R 6 HOH 210 810  128 HOH HOH B . 
R 6 HOH 211 811  855 HOH HOH B . 
R 6 HOH 212 812  41  HOH HOH B . 
R 6 HOH 213 813  36  HOH HOH B . 
R 6 HOH 214 814  681 HOH HOH B . 
R 6 HOH 215 815  127 HOH HOH B . 
R 6 HOH 216 816  271 HOH HOH B . 
R 6 HOH 217 817  593 HOH HOH B . 
R 6 HOH 218 818  339 HOH HOH B . 
R 6 HOH 219 819  554 HOH HOH B . 
R 6 HOH 220 820  299 HOH HOH B . 
R 6 HOH 221 821  212 HOH HOH B . 
R 6 HOH 222 822  171 HOH HOH B . 
R 6 HOH 223 823  466 HOH HOH B . 
R 6 HOH 224 824  77  HOH HOH B . 
R 6 HOH 225 825  455 HOH HOH B . 
R 6 HOH 226 826  344 HOH HOH B . 
R 6 HOH 227 827  456 HOH HOH B . 
R 6 HOH 228 828  382 HOH HOH B . 
R 6 HOH 229 829  691 HOH HOH B . 
R 6 HOH 230 830  225 HOH HOH B . 
R 6 HOH 231 831  229 HOH HOH B . 
R 6 HOH 232 832  311 HOH HOH B . 
R 6 HOH 233 833  867 HOH HOH B . 
R 6 HOH 234 834  14  HOH HOH B . 
R 6 HOH 235 835  619 HOH HOH B . 
R 6 HOH 236 836  291 HOH HOH B . 
R 6 HOH 237 837  327 HOH HOH B . 
R 6 HOH 238 838  11  HOH HOH B . 
R 6 HOH 239 839  264 HOH HOH B . 
R 6 HOH 240 840  289 HOH HOH B . 
R 6 HOH 241 841  214 HOH HOH B . 
R 6 HOH 242 842  638 HOH HOH B . 
R 6 HOH 243 843  397 HOH HOH B . 
R 6 HOH 244 844  669 HOH HOH B . 
R 6 HOH 245 845  470 HOH HOH B . 
R 6 HOH 246 846  59  HOH HOH B . 
R 6 HOH 247 847  141 HOH HOH B . 
R 6 HOH 248 848  32  HOH HOH B . 
R 6 HOH 249 849  368 HOH HOH B . 
R 6 HOH 250 850  860 HOH HOH B . 
R 6 HOH 251 851  473 HOH HOH B . 
R 6 HOH 252 852  97  HOH HOH B . 
R 6 HOH 253 853  824 HOH HOH B . 
R 6 HOH 254 854  23  HOH HOH B . 
R 6 HOH 255 855  178 HOH HOH B . 
R 6 HOH 256 856  43  HOH HOH B . 
R 6 HOH 257 857  226 HOH HOH B . 
R 6 HOH 258 858  157 HOH HOH B . 
R 6 HOH 259 859  111 HOH HOH B . 
R 6 HOH 260 860  44  HOH HOH B . 
R 6 HOH 261 861  376 HOH HOH B . 
R 6 HOH 262 862  29  HOH HOH B . 
R 6 HOH 263 863  172 HOH HOH B . 
R 6 HOH 264 864  725 HOH HOH B . 
R 6 HOH 265 865  841 HOH HOH B . 
R 6 HOH 266 866  469 HOH HOH B . 
R 6 HOH 267 867  332 HOH HOH B . 
R 6 HOH 268 868  272 HOH HOH B . 
R 6 HOH 269 869  471 HOH HOH B . 
R 6 HOH 270 870  668 HOH HOH B . 
R 6 HOH 271 871  355 HOH HOH B . 
R 6 HOH 272 872  87  HOH HOH B . 
R 6 HOH 273 873  335 HOH HOH B . 
R 6 HOH 274 874  479 HOH HOH B . 
R 6 HOH 275 875  396 HOH HOH B . 
R 6 HOH 276 876  563 HOH HOH B . 
R 6 HOH 277 877  198 HOH HOH B . 
R 6 HOH 278 878  356 HOH HOH B . 
R 6 HOH 279 879  235 HOH HOH B . 
R 6 HOH 280 880  46  HOH HOH B . 
R 6 HOH 281 881  864 HOH HOH B . 
R 6 HOH 282 882  237 HOH HOH B . 
R 6 HOH 283 883  430 HOH HOH B . 
R 6 HOH 284 884  328 HOH HOH B . 
R 6 HOH 285 885  759 HOH HOH B . 
R 6 HOH 286 886  875 HOH HOH B . 
R 6 HOH 287 887  341 HOH HOH B . 
R 6 HOH 288 888  298 HOH HOH B . 
R 6 HOH 289 889  120 HOH HOH B . 
R 6 HOH 290 890  836 HOH HOH B . 
R 6 HOH 291 891  136 HOH HOH B . 
R 6 HOH 292 892  407 HOH HOH B . 
R 6 HOH 293 893  191 HOH HOH B . 
R 6 HOH 294 894  823 HOH HOH B . 
R 6 HOH 295 895  399 HOH HOH B . 
R 6 HOH 296 896  185 HOH HOH B . 
R 6 HOH 297 897  517 HOH HOH B . 
R 6 HOH 298 898  689 HOH HOH B . 
R 6 HOH 299 899  194 HOH HOH B . 
R 6 HOH 300 900  256 HOH HOH B . 
R 6 HOH 301 901  106 HOH HOH B . 
R 6 HOH 302 902  706 HOH HOH B . 
R 6 HOH 303 903  285 HOH HOH B . 
R 6 HOH 304 904  148 HOH HOH B . 
R 6 HOH 305 905  705 HOH HOH B . 
R 6 HOH 306 906  88  HOH HOH B . 
R 6 HOH 307 907  232 HOH HOH B . 
R 6 HOH 308 908  640 HOH HOH B . 
R 6 HOH 309 909  778 HOH HOH B . 
R 6 HOH 310 910  142 HOH HOH B . 
R 6 HOH 311 911  150 HOH HOH B . 
R 6 HOH 312 912  431 HOH HOH B . 
R 6 HOH 313 913  457 HOH HOH B . 
R 6 HOH 314 914  543 HOH HOH B . 
R 6 HOH 315 915  151 HOH HOH B . 
R 6 HOH 316 916  566 HOH HOH B . 
R 6 HOH 317 917  367 HOH HOH B . 
R 6 HOH 318 918  717 HOH HOH B . 
R 6 HOH 319 919  255 HOH HOH B . 
R 6 HOH 320 920  774 HOH HOH B . 
R 6 HOH 321 921  480 HOH HOH B . 
R 6 HOH 322 922  173 HOH HOH B . 
R 6 HOH 323 923  143 HOH HOH B . 
R 6 HOH 324 924  386 HOH HOH B . 
R 6 HOH 325 925  301 HOH HOH B . 
R 6 HOH 326 926  709 HOH HOH B . 
R 6 HOH 327 927  410 HOH HOH B . 
R 6 HOH 328 928  435 HOH HOH B . 
R 6 HOH 329 929  690 HOH HOH B . 
R 6 HOH 330 930  550 HOH HOH B . 
R 6 HOH 331 931  489 HOH HOH B . 
R 6 HOH 332 932  223 HOH HOH B . 
R 6 HOH 333 933  118 HOH HOH B . 
R 6 HOH 334 934  522 HOH HOH B . 
R 6 HOH 335 935  363 HOH HOH B . 
R 6 HOH 336 936  458 HOH HOH B . 
R 6 HOH 337 937  144 HOH HOH B . 
R 6 HOH 338 938  853 HOH HOH B . 
R 6 HOH 339 939  772 HOH HOH B . 
R 6 HOH 340 940  491 HOH HOH B . 
R 6 HOH 341 941  217 HOH HOH B . 
R 6 HOH 342 942  548 HOH HOH B . 
R 6 HOH 343 943  63  HOH HOH B . 
R 6 HOH 344 944  565 HOH HOH B . 
R 6 HOH 345 945  692 HOH HOH B . 
R 6 HOH 346 946  308 HOH HOH B . 
R 6 HOH 347 947  722 HOH HOH B . 
R 6 HOH 348 948  839 HOH HOH B . 
R 6 HOH 349 949  636 HOH HOH B . 
R 6 HOH 350 950  436 HOH HOH B . 
R 6 HOH 351 951  577 HOH HOH B . 
R 6 HOH 352 952  865 HOH HOH B . 
R 6 HOH 353 953  746 HOH HOH B . 
R 6 HOH 354 954  559 HOH HOH B . 
R 6 HOH 355 955  319 HOH HOH B . 
R 6 HOH 356 956  571 HOH HOH B . 
R 6 HOH 357 957  697 HOH HOH B . 
R 6 HOH 358 958  567 HOH HOH B . 
R 6 HOH 359 959  762 HOH HOH B . 
R 6 HOH 360 960  170 HOH HOH B . 
R 6 HOH 361 961  607 HOH HOH B . 
R 6 HOH 362 962  345 HOH HOH B . 
R 6 HOH 363 963  581 HOH HOH B . 
R 6 HOH 364 964  763 HOH HOH B . 
R 6 HOH 365 965  427 HOH HOH B . 
R 6 HOH 366 966  451 HOH HOH B . 
R 6 HOH 367 967  464 HOH HOH B . 
R 6 HOH 368 968  280 HOH HOH B . 
R 6 HOH 369 969  644 HOH HOH B . 
R 6 HOH 370 970  672 HOH HOH B . 
R 6 HOH 371 971  472 HOH HOH B . 
R 6 HOH 372 972  665 HOH HOH B . 
R 6 HOH 373 973  400 HOH HOH B . 
R 6 HOH 374 974  753 HOH HOH B . 
R 6 HOH 375 975  478 HOH HOH B . 
R 6 HOH 376 976  627 HOH HOH B . 
R 6 HOH 377 977  817 HOH HOH B . 
R 6 HOH 378 978  578 HOH HOH B . 
R 6 HOH 379 979  576 HOH HOH B . 
R 6 HOH 380 980  406 HOH HOH B . 
R 6 HOH 381 981  712 HOH HOH B . 
R 6 HOH 382 982  770 HOH HOH B . 
R 6 HOH 383 983  787 HOH HOH B . 
R 6 HOH 384 984  828 HOH HOH B . 
R 6 HOH 385 985  794 HOH HOH B . 
R 6 HOH 386 986  838 HOH HOH B . 
R 6 HOH 387 987  452 HOH HOH B . 
R 6 HOH 388 988  645 HOH HOH B . 
R 6 HOH 389 989  818 HOH HOH B . 
R 6 HOH 390 990  35  HOH HOH B . 
R 6 HOH 391 991  835 HOH HOH B . 
R 6 HOH 392 992  379 HOH HOH B . 
R 6 HOH 393 993  553 HOH HOH B . 
R 6 HOH 394 994  807 HOH HOH B . 
R 6 HOH 395 995  615 HOH HOH B . 
R 6 HOH 396 996  420 HOH HOH B . 
R 6 HOH 397 997  680 HOH HOH B . 
R 6 HOH 398 998  440 HOH HOH B . 
R 6 HOH 399 999  371 HOH HOH B . 
R 6 HOH 400 1000 395 HOH HOH B . 
R 6 HOH 401 1001 687 HOH HOH B . 
R 6 HOH 402 1002 702 HOH HOH B . 
R 6 HOH 403 1003 858 HOH HOH B . 
R 6 HOH 404 1004 497 HOH HOH B . 
R 6 HOH 405 1005 704 HOH HOH B . 
R 6 HOH 406 1006 445 HOH HOH B . 
R 6 HOH 407 1007 748 HOH HOH B . 
R 6 HOH 408 1008 210 HOH HOH B . 
R 6 HOH 409 1009 549 HOH HOH B . 
R 6 HOH 410 1010 439 HOH HOH B . 
R 6 HOH 411 1011 373 HOH HOH B . 
R 6 HOH 412 1012 465 HOH HOH B . 
R 6 HOH 413 1013 809 HOH HOH B . 
R 6 HOH 414 1014 707 HOH HOH B . 
R 6 HOH 415 1015 816 HOH HOH B . 
R 6 HOH 416 1016 501 HOH HOH B . 
R 6 HOH 417 1017 594 HOH HOH B . 
R 6 HOH 418 1018 845 HOH HOH B . 
R 6 HOH 419 1019 251 HOH HOH B . 
R 6 HOH 420 1020 196 HOH HOH B . 
R 6 HOH 421 1021 670 HOH HOH B . 
R 6 HOH 422 1022 394 HOH HOH B . 
R 6 HOH 423 1023 678 HOH HOH B . 
R 6 HOH 424 1024 495 HOH HOH B . 
R 6 HOH 425 1025 781 HOH HOH B . 
R 6 HOH 426 1026 239 HOH HOH B . 
R 6 HOH 427 1027 737 HOH HOH B . 
R 6 HOH 428 1028 525 HOH HOH B . 
R 6 HOH 429 1029 715 HOH HOH B . 
R 6 HOH 430 1030 134 HOH HOH B . 
R 6 HOH 431 1031 658 HOH HOH B . 
R 6 HOH 432 1032 388 HOH HOH B . 
R 6 HOH 433 1033 530 HOH HOH B . 
R 6 HOH 434 1034 140 HOH HOH B . 
R 6 HOH 435 1035 513 HOH HOH B . 
R 6 HOH 436 1036 829 HOH HOH B . 
R 6 HOH 437 1037 698 HOH HOH B . 
R 6 HOH 438 1038 811 HOH HOH B . 
R 6 HOH 439 1039 293 HOH HOH B . 
R 6 HOH 440 1040 849 HOH HOH B . 
R 6 HOH 441 1041 582 HOH HOH B . 
R 6 HOH 442 1042 733 HOH HOH B . 
R 6 HOH 443 1043 708 HOH HOH B . 
R 6 HOH 444 1044 688 HOH HOH B . 
R 6 HOH 445 1045 352 HOH HOH B . 
R 6 HOH 446 1046 789 HOH HOH B . 
R 6 HOH 447 1047 370 HOH HOH B . 
R 6 HOH 448 1048 247 HOH HOH B . 
R 6 HOH 449 1049 569 HOH HOH B . 
R 6 HOH 450 1050 767 HOH HOH B . 
R 6 HOH 451 1051 831 HOH HOH B . 
R 6 HOH 452 1052 629 HOH HOH B . 
R 6 HOH 453 1053 616 HOH HOH B . 
R 6 HOH 454 1054 819 HOH HOH B . 
R 6 HOH 455 1055 719 HOH HOH B . 
R 6 HOH 456 1056 450 HOH HOH B . 
R 6 HOH 457 1057 635 HOH HOH B . 
R 6 HOH 458 1058 197 HOH HOH B . 
R 6 HOH 459 1059 784 HOH HOH B . 
R 6 HOH 460 1060 656 HOH HOH B . 
R 6 HOH 461 1061 441 HOH HOH B . 
R 6 HOH 462 1062 844 HOH HOH B . 
R 6 HOH 463 1063 743 HOH HOH B . 
R 6 HOH 464 1064 421 HOH HOH B . 
R 6 HOH 465 1065 104 HOH HOH B . 
R 6 HOH 466 1066 511 HOH HOH B . 
R 6 HOH 467 1067 628 HOH HOH B . 
R 6 HOH 468 1068 653 HOH HOH B . 
R 6 HOH 469 1069 648 HOH HOH B . 
R 6 HOH 470 1070 812 HOH HOH B . 
R 6 HOH 471 1071 660 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.19.2_4158: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_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                     8YB0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.830 
_cell.length_a_esd                 ? 
_cell.length_b                     128.430 
_cell.length_b_esd                 ? 
_cell.length_c                     149.530 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8YB0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8YB0 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.57 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.4 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'50 mM Tris-HCl buffer, 120 mM MgCl2, 16-18% PEG 8000, 200 uM N-Enanthyl-L-Prolyl-L-Phenylalanine, 1%(v/v) styrene' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX300-HS' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9539 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SACLA BEAMLINE BL2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9539 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL2 
_diffrn_source.pdbx_synchrotron_site       SACLA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YB0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.6 
_reflns.d_resolution_low                               10 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     149224 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                158.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.55 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.973 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.6 
_reflns_shell.d_res_low                                     1.61 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.63 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3692 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.567 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8YB0 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.60 
_refine.ls_d_res_low                             9.99 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     149070 
_refine.ls_number_reflns_R_free                  7467 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1764 
_refine.ls_R_factor_R_free                       0.2050 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1749 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.02 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        9.99 
_refine_hist.number_atoms_solvent             875 
_refine_hist.number_atoms_total               8417 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        7340 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         202 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 7755  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.990 ? 10492 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.753 ? 1077  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054 ? 1108  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 1369  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.60 1.62 . . 236 4679 100.00 . . . . 0.3845 . . . . . . . . . . . 0.3851 
'X-RAY DIFFRACTION' 1.62 1.64 . . 242 4707 100.00 . . . . 0.3729 . . . . . . . . . . . 0.3802 
'X-RAY DIFFRACTION' 1.64 1.66 . . 243 4646 100.00 . . . . 0.3661 . . . . . . . . . . . 0.3848 
'X-RAY DIFFRACTION' 1.66 1.68 . . 270 4670 100.00 . . . . 0.3568 . . . . . . . . . . . 0.3826 
'X-RAY DIFFRACTION' 1.68 1.70 . . 239 4657 100.00 . . . . 0.3440 . . . . . . . . . . . 0.3824 
'X-RAY DIFFRACTION' 1.70 1.72 . . 262 4660 100.00 . . . . 0.3305 . . . . . . . . . . . 0.3589 
'X-RAY DIFFRACTION' 1.72 1.75 . . 267 4655 100.00 . . . . 0.3206 . . . . . . . . . . . 0.3564 
'X-RAY DIFFRACTION' 1.75 1.77 . . 229 4689 100.00 . . . . 0.3048 . . . . . . . . . . . 0.3096 
'X-RAY DIFFRACTION' 1.77 1.80 . . 256 4658 100.00 . . . . 0.2846 . . . . . . . . . . . 0.3427 
'X-RAY DIFFRACTION' 1.80 1.83 . . 239 4691 100.00 . . . . 0.2751 . . . . . . . . . . . 0.3091 
'X-RAY DIFFRACTION' 1.83 1.86 . . 258 4682 100.00 . . . . 0.2495 . . . . . . . . . . . 0.2922 
'X-RAY DIFFRACTION' 1.86 1.90 . . 271 4684 100.00 . . . . 0.2309 . . . . . . . . . . . 0.2508 
'X-RAY DIFFRACTION' 1.90 1.93 . . 256 4640 100.00 . . . . 0.2284 . . . . . . . . . . . 0.2985 
'X-RAY DIFFRACTION' 1.93 1.97 . . 231 4714 100.00 . . . . 0.2003 . . . . . . . . . . . 0.2252 
'X-RAY DIFFRACTION' 1.97 2.01 . . 240 4714 100.00 . . . . 0.1850 . . . . . . . . . . . 0.1975 
'X-RAY DIFFRACTION' 2.01 2.06 . . 260 4670 100.00 . . . . 0.1790 . . . . . . . . . . . 0.2193 
'X-RAY DIFFRACTION' 2.06 2.11 . . 266 4691 100.00 . . . . 0.1711 . . . . . . . . . . . 0.1981 
'X-RAY DIFFRACTION' 2.11 2.17 . . 247 4724 100.00 . . . . 0.1703 . . . . . . . . . . . 0.2104 
'X-RAY DIFFRACTION' 2.17 2.23 . . 260 4674 100.00 . . . . 0.1714 . . . . . . . . . . . 0.1966 
'X-RAY DIFFRACTION' 2.23 2.30 . . 226 4726 100.00 . . . . 0.1713 . . . . . . . . . . . 0.2193 
'X-RAY DIFFRACTION' 2.30 2.38 . . 219 4761 100.00 . . . . 0.1693 . . . . . . . . . . . 0.2106 
'X-RAY DIFFRACTION' 2.38 2.48 . . 271 4734 100.00 . . . . 0.1655 . . . . . . . . . . . 0.1949 
'X-RAY DIFFRACTION' 2.48 2.59 . . 246 4716 100.00 . . . . 0.1690 . . . . . . . . . . . 0.1946 
'X-RAY DIFFRACTION' 2.59 2.72 . . 220 4781 100.00 . . . . 0.1725 . . . . . . . . . . . 0.2153 
'X-RAY DIFFRACTION' 2.72 2.89 . . 275 4718 100.00 . . . . 0.1693 . . . . . . . . . . . 0.1828 
'X-RAY DIFFRACTION' 2.89 3.10 . . 236 4787 100.00 . . . . 0.1707 . . . . . . . . . . . 0.2011 
'X-RAY DIFFRACTION' 3.10 3.41 . . 249 4788 100.00 . . . . 0.1616 . . . . . . . . . . . 0.1993 
'X-RAY DIFFRACTION' 3.41 3.87 . . 241 4834 100.00 . . . . 0.1520 . . . . . . . . . . . 0.1849 
'X-RAY DIFFRACTION' 3.87 4.79 . . 230 4870 100.00 . . . . 0.1406 . . . . . . . . . . . 0.1675 
'X-RAY DIFFRACTION' 4.79 9.99 . . 282 4983 100.00 . . . . 0.1667 . . . . . . . . . . . 0.1818 
# 
_struct.entry_id                     8YB0 
_struct.title                        
'XFEL crystal structure of the reduced form of F393H P450BM3 with N-enanthyl-L-prolyl-L-phenylalanine in complex with styrene' 
_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        8YB0 
_struct_keywords.text            'Cytochrome P450, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 5 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 6 ? 
R N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CPXB_PRIM2 
_struct_ref.pdbx_db_accession          P14779 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRD
FAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_struct_ref.pdbx_align_begin           0 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8YB0 A 1 ? 455 ? P14779 2 ? 456 ? 1 455 
2 1 8YB0 B 1 ? 455 ? P14779 2 ? 456 ? 1 455 
# 
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 8YB0 HIS A 393 ? UNP P14779 PHE 394 'engineered mutation' 393 1 
2 8YB0 HIS B 393 ? UNP P14779 PHE 394 'engineered mutation' 393 2 
# 
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 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1320  ? 
1 MORE         -21   ? 
1 'SSA (A^2)'  19080 ? 
2 'ABSA (A^2)' 1330  ? 
2 MORE         -21   ? 
2 'SSA (A^2)'  18970 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,Q     
2 1 B,I,J,K,L,M,N,O,P,R 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PHE A 11  ? LYS A 15  ? PHE A 11  LYS A 15  5 ? 5  
HELX_P HELX_P2  AA2 ASN A 16  ? ASN A 21  ? ASN A 16  ASN A 21  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 24  ? GLY A 37  ? LYS A 24  GLY A 37  1 ? 14 
HELX_P HELX_P4  AA4 SER A 54  ? CYS A 62  ? SER A 54  CYS A 62  1 ? 9  
HELX_P HELX_P5  AA5 SER A 72  ? GLY A 83  ? SER A 72  GLY A 83  1 ? 12 
HELX_P HELX_P6  AA6 GLU A 93  ? LEU A 104 ? GLU A 93  LEU A 104 1 ? 12 
HELX_P HELX_P7  AA7 PRO A 105 ? PHE A 107 ? PRO A 105 PHE A 107 5 ? 3  
HELX_P HELX_P8  AA8 SER A 108 ? ARG A 132 ? SER A 108 ARG A 132 1 ? 25 
HELX_P HELX_P9  AA9 VAL A 141 ? ASN A 159 ? VAL A 141 ASN A 159 1 ? 19 
HELX_P HELX_P10 AB1 ASN A 163 ? ARG A 167 ? ASN A 163 ARG A 167 5 ? 5  
HELX_P HELX_P11 AB2 HIS A 171 ? LEU A 188 ? HIS A 171 LEU A 188 1 ? 18 
HELX_P HELX_P12 AB3 ASP A 195 ? ALA A 197 ? ASP A 195 ALA A 197 5 ? 3  
HELX_P HELX_P13 AB4 TYR A 198 ? SER A 226 ? TYR A 198 SER A 226 1 ? 29 
HELX_P HELX_P14 AB5 ASP A 232 ? GLY A 240 ? ASP A 232 GLY A 240 1 ? 9  
HELX_P HELX_P15 AB6 ASP A 250 ? GLY A 265 ? ASP A 250 GLY A 265 1 ? 16 
HELX_P HELX_P16 AB7 HIS A 266 ? ASN A 283 ? HIS A 266 ASN A 283 1 ? 18 
HELX_P HELX_P17 AB8 ASN A 283 ? LEU A 298 ? ASN A 283 LEU A 298 1 ? 16 
HELX_P HELX_P18 AB9 SER A 304 ? GLN A 310 ? SER A 304 GLN A 310 1 ? 7  
HELX_P HELX_P19 AC1 LEU A 311 ? TRP A 325 ? LEU A 311 TRP A 325 1 ? 15 
HELX_P HELX_P20 AC2 ILE A 357 ? HIS A 361 ? ILE A 357 HIS A 361 1 ? 5  
HELX_P HELX_P21 AC3 ASP A 363 ? GLY A 368 ? ASP A 363 GLY A 368 1 ? 6  
HELX_P HELX_P22 AC4 ARG A 375 ? GLU A 380 ? ARG A 375 GLU A 380 5 ? 6  
HELX_P HELX_P23 AC5 ASN A 381 ? ILE A 385 ? ASN A 381 ILE A 385 5 ? 5  
HELX_P HELX_P24 AC6 ASN A 395 ? ALA A 399 ? ASN A 395 ALA A 399 5 ? 5  
HELX_P HELX_P25 AC7 GLY A 402 ? HIS A 420 ? GLY A 402 HIS A 420 1 ? 19 
HELX_P HELX_P26 AC8 PHE B 11  ? LYS B 15  ? PHE B 11  LYS B 15  5 ? 5  
HELX_P HELX_P27 AC9 ASN B 16  ? ASN B 21  ? ASN B 16  ASN B 21  5 ? 6  
HELX_P HELX_P28 AD1 LYS B 24  ? GLY B 37  ? LYS B 24  GLY B 37  1 ? 14 
HELX_P HELX_P29 AD2 SER B 54  ? CYS B 62  ? SER B 54  CYS B 62  1 ? 9  
HELX_P HELX_P30 AD3 SER B 72  ? GLY B 83  ? SER B 72  GLY B 83  1 ? 12 
HELX_P HELX_P31 AD4 GLU B 93  ? LEU B 104 ? GLU B 93  LEU B 104 1 ? 12 
HELX_P HELX_P32 AD5 PRO B 105 ? PHE B 107 ? PRO B 105 PHE B 107 5 ? 3  
HELX_P HELX_P33 AD6 SER B 108 ? ARG B 132 ? SER B 108 ARG B 132 1 ? 25 
HELX_P HELX_P34 AD7 VAL B 141 ? ASN B 159 ? VAL B 141 ASN B 159 1 ? 19 
HELX_P HELX_P35 AD8 ASN B 163 ? ARG B 167 ? ASN B 163 ARG B 167 5 ? 5  
HELX_P HELX_P36 AD9 HIS B 171 ? LEU B 188 ? HIS B 171 LEU B 188 1 ? 18 
HELX_P HELX_P37 AE1 ASP B 195 ? ALA B 197 ? ASP B 195 ALA B 197 5 ? 3  
HELX_P HELX_P38 AE2 TYR B 198 ? ALA B 225 ? TYR B 198 ALA B 225 1 ? 28 
HELX_P HELX_P39 AE3 ASP B 232 ? GLY B 240 ? ASP B 232 GLY B 240 1 ? 9  
HELX_P HELX_P40 AE4 ASP B 250 ? GLY B 265 ? ASP B 250 GLY B 265 1 ? 16 
HELX_P HELX_P41 AE5 HIS B 266 ? ASN B 283 ? HIS B 266 ASN B 283 1 ? 18 
HELX_P HELX_P42 AE6 ASN B 283 ? LEU B 298 ? ASN B 283 LEU B 298 1 ? 16 
HELX_P HELX_P43 AE7 SER B 304 ? GLN B 310 ? SER B 304 GLN B 310 1 ? 7  
HELX_P HELX_P44 AE8 LEU B 311 ? TRP B 325 ? LEU B 311 TRP B 325 1 ? 15 
HELX_P HELX_P45 AE9 GLY B 342 ? GLU B 344 ? GLY B 342 GLU B 344 5 ? 3  
HELX_P HELX_P46 AF1 ILE B 357 ? HIS B 361 ? ILE B 357 HIS B 361 1 ? 5  
HELX_P HELX_P47 AF2 ASP B 363 ? GLY B 368 ? ASP B 363 GLY B 368 1 ? 6  
HELX_P HELX_P48 AF3 ARG B 375 ? GLU B 380 ? ARG B 375 GLU B 380 5 ? 6  
HELX_P HELX_P49 AF4 ASN B 381 ? ILE B 385 ? ASN B 381 ILE B 385 5 ? 5  
HELX_P HELX_P50 AF5 ASN B 395 ? ALA B 399 ? ASN B 395 ALA B 399 5 ? 5  
HELX_P HELX_P51 AF6 GLY B 402 ? HIS B 420 ? GLY B 402 HIS B 420 1 ? 19 
# 
_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 CYS 400 SG ? ? ? 1_555 C HEM . FE ? ? A CYS 400 A HEM 501 1_555 ? ? ? ? ? ? ? 2.448 ? ? 
metalc2 metalc ? ? B CYS 400 SG ? ? ? 1_555 I HEM . FE ? ? B CYS 400 B HEM 501 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
# 
_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  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NA ? C HEM . ? A HEM 501 ? 1_555 102.7 ? 
2  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 90.6  ? 
3  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 88.4  ? 
4  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 87.8  ? 
5  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 168.7 ? 
6  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 87.2  ? 
7  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 100.3 ? 
8  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 91.5  ? 
9  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 168.8 ? 
10 NC ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 90.8  ? 
11 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? I HEM . ? B HEM 501 ? 1_555 NA ? I HEM . ? B HEM 501 ? 1_555 102.7 ? 
12 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? I HEM . ? B HEM 501 ? 1_555 NB ? I HEM . ? B HEM 501 ? 1_555 90.3  ? 
13 NA ? I HEM .   ? B HEM 501 ? 1_555 FE ? I HEM . ? B HEM 501 ? 1_555 NB ? I HEM . ? B HEM 501 ? 1_555 89.4  ? 
14 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? I HEM . ? B HEM 501 ? 1_555 NC ? I HEM . ? B HEM 501 ? 1_555 87.8  ? 
15 NA ? I HEM .   ? B HEM 501 ? 1_555 FE ? I HEM . ? B HEM 501 ? 1_555 NC ? I HEM . ? B HEM 501 ? 1_555 169.1 ? 
16 NB ? I HEM .   ? B HEM 501 ? 1_555 FE ? I HEM . ? B HEM 501 ? 1_555 NC ? I HEM . ? B HEM 501 ? 1_555 87.5  ? 
17 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? I HEM . ? B HEM 501 ? 1_555 ND ? I HEM . ? B HEM 501 ? 1_555 100.6 ? 
18 NA ? I HEM .   ? B HEM 501 ? 1_555 FE ? I HEM . ? B HEM 501 ? 1_555 ND ? I HEM . ? B HEM 501 ? 1_555 91.0  ? 
19 NB ? I HEM .   ? B HEM 501 ? 1_555 FE ? I HEM . ? B HEM 501 ? 1_555 ND ? I HEM . ? B HEM 501 ? 1_555 168.7 ? 
20 NC ? I HEM .   ? B HEM 501 ? 1_555 FE ? I HEM . ? B HEM 501 ? 1_555 ND ? I HEM . ? B HEM 501 ? 1_555 90.1  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 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 ILE A 39  ? ALA A 44  ? ILE A 39  ALA A 44  
AA1 2 ARG A 47  ? LEU A 52  ? ARG A 47  LEU A 52  
AA1 3 GLU A 352 ? LEU A 356 ? GLU A 352 LEU A 356 
AA1 4 ALA A 330 ? ALA A 335 ? ALA A 330 ALA A 335 
AA1 5 PHE A 67  ? ASN A 70  ? PHE A 67  ASN A 70  
AA2 1 ILE A 139 ? GLU A 140 ? ILE A 139 GLU A 140 
AA2 2 VAL A 445 ? SER A 450 ? VAL A 445 SER A 450 
AA2 3 PHE A 421 ? GLU A 424 ? PHE A 421 GLU A 424 
AA3 1 THR A 339 ? LEU A 341 ? THR A 339 LEU A 341 
AA3 2 TYR A 345 ? LEU A 347 ? TYR A 345 LEU A 347 
AA4 1 ILE A 433 ? GLU A 435 ? ILE A 433 GLU A 435 
AA4 2 LEU A 439 ? PRO A 441 ? LEU A 439 PRO A 441 
AA5 1 ILE B 39  ? ALA B 44  ? ILE B 39  ALA B 44  
AA5 2 ARG B 47  ? LEU B 52  ? ARG B 47  LEU B 52  
AA5 3 GLU B 352 ? LEU B 356 ? GLU B 352 LEU B 356 
AA5 4 ALA B 330 ? ALA B 335 ? ALA B 330 ALA B 335 
AA5 5 PHE B 67  ? ASN B 70  ? PHE B 67  ASN B 70  
AA6 1 ILE B 139 ? GLU B 140 ? ILE B 139 GLU B 140 
AA6 2 VAL B 445 ? SER B 450 ? VAL B 445 SER B 450 
AA6 3 PHE B 421 ? GLU B 424 ? PHE B 421 GLU B 424 
AA7 1 THR B 339 ? LEU B 341 ? THR B 339 LEU B 341 
AA7 2 TYR B 345 ? LEU B 347 ? TYR B 345 LEU B 347 
AA8 1 ILE B 433 ? GLU B 435 ? ILE B 433 GLU B 435 
AA8 2 LEU B 439 ? PRO B 441 ? LEU B 439 PRO B 441 
# 
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 ALA A 44  ? N ALA A 44  O ARG A 47  ? O ARG A 47  
AA1 2 3 N ARG A 50  ? N ARG A 50  O MET A 354 ? O MET A 354 
AA1 3 4 O VAL A 355 ? O VAL A 355 N PHE A 331 ? N PHE A 331 
AA1 4 5 O SER A 332 ? O SER A 332 N ASN A 70  ? N ASN A 70  
AA2 1 2 N ILE A 139 ? N ILE A 139 O VAL A 446 ? O VAL A 446 
AA2 2 3 O LYS A 449 ? O LYS A 449 N ASP A 422 ? N ASP A 422 
AA3 1 2 N THR A 339 ? N THR A 339 O LEU A 347 ? O LEU A 347 
AA4 1 2 N LYS A 434 ? N LYS A 434 O LYS A 440 ? O LYS A 440 
AA5 1 2 N PHE B 42  ? N PHE B 42  O THR B 49  ? O THR B 49  
AA5 2 3 N LEU B 52  ? N LEU B 52  O MET B 354 ? O MET B 354 
AA5 3 4 O VAL B 355 ? O VAL B 355 N PHE B 331 ? N PHE B 331 
AA5 4 5 O SER B 332 ? O SER B 332 N ASN B 70  ? N ASN B 70  
AA6 1 2 N ILE B 139 ? N ILE B 139 O VAL B 446 ? O VAL B 446 
AA6 2 3 O LYS B 449 ? O LYS B 449 N ASP B 422 ? N ASP B 422 
AA7 1 2 N THR B 339 ? N THR B 339 O LEU B 347 ? O LEU B 347 
AA8 1 2 N LYS B 434 ? N LYS B 434 O LYS B 440 ? O LYS B 440 
# 
_pdbx_entry_details.entry_id                   8YB0 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND1 B HIS 393  ? ? O B HOH 601  ? ? 2.08 
2 1 O   A HOH 793  ? ? O A HOH 949  ? ? 2.11 
3 1 O   A HOH 779  ? ? O A HOH 853  ? ? 2.12 
4 1 O   A HOH 1001 ? ? O A HOH 1004 ? ? 2.17 
# 
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 LYS A 15  ? ? 51.85   -123.48 
2  1 ASP A 84  ? ? -97.47  34.37   
3  1 ASP A 232 ? ? -127.11 -164.17 
4  1 GLU A 244 ? ? -74.64  -81.64  
5  1 HIS A 266 ? ? -143.54 -33.96  
6  1 ASP A 370 ? ? -78.36  33.11   
7  1 LEU A 437 ? ? 69.00   -59.93  
8  1 LYS B 15  ? ? 56.09   -125.69 
9  1 ASP B 84  ? ? -98.55  36.92   
10 1 ASP B 232 ? ? -127.44 -164.61 
11 1 HIS B 266 ? ? -139.02 -35.10  
12 1 ASP B 370 ? ? -91.73  38.25   
13 1 LEU B 437 ? ? 72.31   -57.68  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1004 ? 5.89 . 
2 1 O ? B HOH 1071 ? 5.85 . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
D0L C1   C  Y N 88  
D0L C2   C  Y N 89  
D0L C15  C  N N 90  
D0L C14  C  N N 91  
D0L C7   C  N N 92  
D0L C12  C  N N 93  
D0L C10  C  N N 94  
D0L C3   C  Y N 95  
D0L C13  C  N N 96  
D0L C11  C  N S 97  
D0L C6   C  Y N 98  
D0L C8   C  N S 99  
D0L C5   C  Y N 100 
D0L C9   C  N N 101 
D0L C4   C  Y N 102 
D0L O2   O  N N 103 
D0L O3   O  N N 104 
D0L O1   O  N N 105 
D0L N2   N  N N 106 
D0L C16  C  N N 107 
D0L C17  C  N N 108 
D0L C18  C  N N 109 
D0L C19  C  N N 110 
D0L C20  C  N N 111 
D0L C21  C  N N 112 
D0L N1   N  N N 113 
D0L H1   H  N N 114 
D0L H2   H  N N 115 
D0L H3   H  N N 116 
D0L H4   H  N N 117 
D0L H5   H  N N 118 
D0L H6   H  N N 119 
D0L H7   H  N N 120 
D0L H8   H  N N 121 
D0L H9   H  N N 122 
D0L H10  H  N N 123 
D0L H11  H  N N 124 
D0L H12  H  N N 125 
D0L H13  H  N N 126 
D0L H14  H  N N 127 
D0L H15  H  N N 128 
D0L H16  H  N N 129 
D0L H17  H  N N 130 
D0L H18  H  N N 131 
D0L H20  H  N N 132 
D0L H21  H  N N 133 
D0L H22  H  N N 134 
D0L H23  H  N N 135 
D0L H24  H  N N 136 
D0L H25  H  N N 137 
D0L H26  H  N N 138 
D0L H27  H  N N 139 
D0L H28  H  N N 140 
D0L H29  H  N N 141 
D0L H30  H  N N 142 
D0L H31  H  N N 143 
D0L H32  H  N N 144 
D0L H33  H  N N 145 
GLN N    N  N N 146 
GLN CA   C  N S 147 
GLN C    C  N N 148 
GLN O    O  N N 149 
GLN CB   C  N N 150 
GLN CG   C  N N 151 
GLN CD   C  N N 152 
GLN OE1  O  N N 153 
GLN NE2  N  N N 154 
GLN OXT  O  N N 155 
GLN H    H  N N 156 
GLN H2   H  N N 157 
GLN HA   H  N N 158 
GLN HB2  H  N N 159 
GLN HB3  H  N N 160 
GLN HG2  H  N N 161 
GLN HG3  H  N N 162 
GLN HE21 H  N N 163 
GLN HE22 H  N N 164 
GLN HXT  H  N N 165 
GLU N    N  N N 166 
GLU CA   C  N S 167 
GLU C    C  N N 168 
GLU O    O  N N 169 
GLU CB   C  N N 170 
GLU CG   C  N N 171 
GLU CD   C  N N 172 
GLU OE1  O  N N 173 
GLU OE2  O  N N 174 
GLU OXT  O  N N 175 
GLU H    H  N N 176 
GLU H2   H  N N 177 
GLU HA   H  N N 178 
GLU HB2  H  N N 179 
GLU HB3  H  N N 180 
GLU HG2  H  N N 181 
GLU HG3  H  N N 182 
GLU HE2  H  N N 183 
GLU HXT  H  N N 184 
GLY N    N  N N 185 
GLY CA   C  N N 186 
GLY C    C  N N 187 
GLY O    O  N N 188 
GLY OXT  O  N N 189 
GLY H    H  N N 190 
GLY H2   H  N N 191 
GLY HA2  H  N N 192 
GLY HA3  H  N N 193 
GLY HXT  H  N N 194 
GOL C1   C  N N 195 
GOL O1   O  N N 196 
GOL C2   C  N N 197 
GOL O2   O  N N 198 
GOL C3   C  N N 199 
GOL O3   O  N N 200 
GOL H11  H  N N 201 
GOL H12  H  N N 202 
GOL HO1  H  N N 203 
GOL H2   H  N N 204 
GOL HO2  H  N N 205 
GOL H31  H  N N 206 
GOL H32  H  N N 207 
GOL HO3  H  N N 208 
HEM CHA  C  N N 209 
HEM CHB  C  N N 210 
HEM CHC  C  N N 211 
HEM CHD  C  N N 212 
HEM C1A  C  Y N 213 
HEM C2A  C  Y N 214 
HEM C3A  C  Y N 215 
HEM C4A  C  Y N 216 
HEM CMA  C  N N 217 
HEM CAA  C  N N 218 
HEM CBA  C  N N 219 
HEM CGA  C  N N 220 
HEM O1A  O  N N 221 
HEM O2A  O  N N 222 
HEM C1B  C  N N 223 
HEM C2B  C  N N 224 
HEM C3B  C  N N 225 
HEM C4B  C  N N 226 
HEM CMB  C  N N 227 
HEM CAB  C  N N 228 
HEM CBB  C  N N 229 
HEM C1C  C  Y N 230 
HEM C2C  C  Y N 231 
HEM C3C  C  Y N 232 
HEM C4C  C  Y N 233 
HEM CMC  C  N N 234 
HEM CAC  C  N N 235 
HEM CBC  C  N N 236 
HEM C1D  C  N N 237 
HEM C2D  C  N N 238 
HEM C3D  C  N N 239 
HEM C4D  C  N N 240 
HEM CMD  C  N N 241 
HEM CAD  C  N N 242 
HEM CBD  C  N N 243 
HEM CGD  C  N N 244 
HEM O1D  O  N N 245 
HEM O2D  O  N N 246 
HEM NA   N  Y N 247 
HEM NB   N  N N 248 
HEM NC   N  Y N 249 
HEM ND   N  N N 250 
HEM FE   FE N N 251 
HEM HHB  H  N N 252 
HEM HHC  H  N N 253 
HEM HHD  H  N N 254 
HEM HMA  H  N N 255 
HEM HMAA H  N N 256 
HEM HMAB H  N N 257 
HEM HAA  H  N N 258 
HEM HAAA H  N N 259 
HEM HBA  H  N N 260 
HEM HBAA H  N N 261 
HEM HMB  H  N N 262 
HEM HMBA H  N N 263 
HEM HMBB H  N N 264 
HEM HAB  H  N N 265 
HEM HBB  H  N N 266 
HEM HBBA H  N N 267 
HEM HMC  H  N N 268 
HEM HMCA H  N N 269 
HEM HMCB H  N N 270 
HEM HAC  H  N N 271 
HEM HBC  H  N N 272 
HEM HBCA H  N N 273 
HEM HMD  H  N N 274 
HEM HMDA H  N N 275 
HEM HMDB H  N N 276 
HEM HAD  H  N N 277 
HEM HADA H  N N 278 
HEM HBD  H  N N 279 
HEM HBDA H  N N 280 
HEM H2A  H  N N 281 
HEM H2D  H  N N 282 
HEM HHA  H  N N 283 
HIS N    N  N N 284 
HIS CA   C  N S 285 
HIS C    C  N N 286 
HIS O    O  N N 287 
HIS CB   C  N N 288 
HIS CG   C  Y N 289 
HIS ND1  N  Y N 290 
HIS CD2  C  Y N 291 
HIS CE1  C  Y N 292 
HIS NE2  N  Y N 293 
HIS OXT  O  N N 294 
HIS H    H  N N 295 
HIS H2   H  N N 296 
HIS HA   H  N N 297 
HIS HB2  H  N N 298 
HIS HB3  H  N N 299 
HIS HD1  H  N N 300 
HIS HD2  H  N N 301 
HIS HE1  H  N N 302 
HIS HE2  H  N N 303 
HIS HXT  H  N N 304 
HOH O    O  N N 305 
HOH H1   H  N N 306 
HOH H2   H  N N 307 
ILE N    N  N N 308 
ILE CA   C  N S 309 
ILE C    C  N N 310 
ILE O    O  N N 311 
ILE CB   C  N S 312 
ILE CG1  C  N N 313 
ILE CG2  C  N N 314 
ILE CD1  C  N N 315 
ILE OXT  O  N N 316 
ILE H    H  N N 317 
ILE H2   H  N N 318 
ILE HA   H  N N 319 
ILE HB   H  N N 320 
ILE HG12 H  N N 321 
ILE HG13 H  N N 322 
ILE HG21 H  N N 323 
ILE HG22 H  N N 324 
ILE HG23 H  N N 325 
ILE HD11 H  N N 326 
ILE HD12 H  N N 327 
ILE HD13 H  N N 328 
ILE HXT  H  N N 329 
LEU N    N  N N 330 
LEU CA   C  N S 331 
LEU C    C  N N 332 
LEU O    O  N N 333 
LEU CB   C  N N 334 
LEU CG   C  N N 335 
LEU CD1  C  N N 336 
LEU CD2  C  N N 337 
LEU OXT  O  N N 338 
LEU H    H  N N 339 
LEU H2   H  N N 340 
LEU HA   H  N N 341 
LEU HB2  H  N N 342 
LEU HB3  H  N N 343 
LEU HG   H  N N 344 
LEU HD11 H  N N 345 
LEU HD12 H  N N 346 
LEU HD13 H  N N 347 
LEU HD21 H  N N 348 
LEU HD22 H  N N 349 
LEU HD23 H  N N 350 
LEU HXT  H  N N 351 
LYS N    N  N N 352 
LYS CA   C  N S 353 
LYS C    C  N N 354 
LYS O    O  N N 355 
LYS CB   C  N N 356 
LYS CG   C  N N 357 
LYS CD   C  N N 358 
LYS CE   C  N N 359 
LYS NZ   N  N N 360 
LYS OXT  O  N N 361 
LYS H    H  N N 362 
LYS H2   H  N N 363 
LYS HA   H  N N 364 
LYS HB2  H  N N 365 
LYS HB3  H  N N 366 
LYS HG2  H  N N 367 
LYS HG3  H  N N 368 
LYS HD2  H  N N 369 
LYS HD3  H  N N 370 
LYS HE2  H  N N 371 
LYS HE3  H  N N 372 
LYS HZ1  H  N N 373 
LYS HZ2  H  N N 374 
LYS HZ3  H  N N 375 
LYS HXT  H  N N 376 
MET N    N  N N 377 
MET CA   C  N S 378 
MET C    C  N N 379 
MET O    O  N N 380 
MET CB   C  N N 381 
MET CG   C  N N 382 
MET SD   S  N N 383 
MET CE   C  N N 384 
MET OXT  O  N N 385 
MET H    H  N N 386 
MET H2   H  N N 387 
MET HA   H  N N 388 
MET HB2  H  N N 389 
MET HB3  H  N N 390 
MET HG2  H  N N 391 
MET HG3  H  N N 392 
MET HE1  H  N N 393 
MET HE2  H  N N 394 
MET HE3  H  N N 395 
MET HXT  H  N N 396 
PHE N    N  N N 397 
PHE CA   C  N S 398 
PHE C    C  N N 399 
PHE O    O  N N 400 
PHE CB   C  N N 401 
PHE CG   C  Y N 402 
PHE CD1  C  Y N 403 
PHE CD2  C  Y N 404 
PHE CE1  C  Y N 405 
PHE CE2  C  Y N 406 
PHE CZ   C  Y N 407 
PHE OXT  O  N N 408 
PHE H    H  N N 409 
PHE H2   H  N N 410 
PHE HA   H  N N 411 
PHE HB2  H  N N 412 
PHE HB3  H  N N 413 
PHE HD1  H  N N 414 
PHE HD2  H  N N 415 
PHE HE1  H  N N 416 
PHE HE2  H  N N 417 
PHE HZ   H  N N 418 
PHE HXT  H  N N 419 
PRO N    N  N N 420 
PRO CA   C  N S 421 
PRO C    C  N N 422 
PRO O    O  N N 423 
PRO CB   C  N N 424 
PRO CG   C  N N 425 
PRO CD   C  N N 426 
PRO OXT  O  N N 427 
PRO H    H  N N 428 
PRO HA   H  N N 429 
PRO HB2  H  N N 430 
PRO HB3  H  N N 431 
PRO HG2  H  N N 432 
PRO HG3  H  N N 433 
PRO HD2  H  N N 434 
PRO HD3  H  N N 435 
PRO HXT  H  N N 436 
SER N    N  N N 437 
SER CA   C  N S 438 
SER C    C  N N 439 
SER O    O  N N 440 
SER CB   C  N N 441 
SER OG   O  N N 442 
SER OXT  O  N N 443 
SER H    H  N N 444 
SER H2   H  N N 445 
SER HA   H  N N 446 
SER HB2  H  N N 447 
SER HB3  H  N N 448 
SER HG   H  N N 449 
SER HXT  H  N N 450 
SYN CAF  C  Y N 451 
SYN CAD  C  Y N 452 
SYN CAC  C  Y N 453 
SYN CAE  C  Y N 454 
SYN CAG  C  Y N 455 
SYN CAH  C  Y N 456 
SYN CAB  C  N N 457 
SYN CAA  C  N N 458 
SYN H1   H  N N 459 
SYN H2   H  N N 460 
SYN H3   H  N N 461 
SYN H4   H  N N 462 
SYN H5   H  N N 463 
SYN H6   H  N N 464 
SYN H8   H  N N 465 
SYN H9   H  N N 466 
THR N    N  N N 467 
THR CA   C  N S 468 
THR C    C  N N 469 
THR O    O  N N 470 
THR CB   C  N R 471 
THR OG1  O  N N 472 
THR CG2  C  N N 473 
THR OXT  O  N N 474 
THR H    H  N N 475 
THR H2   H  N N 476 
THR HA   H  N N 477 
THR HB   H  N N 478 
THR HG1  H  N N 479 
THR HG21 H  N N 480 
THR HG22 H  N N 481 
THR HG23 H  N N 482 
THR HXT  H  N N 483 
TRP N    N  N N 484 
TRP CA   C  N S 485 
TRP C    C  N N 486 
TRP O    O  N N 487 
TRP CB   C  N N 488 
TRP CG   C  Y N 489 
TRP CD1  C  Y N 490 
TRP CD2  C  Y N 491 
TRP NE1  N  Y N 492 
TRP CE2  C  Y N 493 
TRP CE3  C  Y N 494 
TRP CZ2  C  Y N 495 
TRP CZ3  C  Y N 496 
TRP CH2  C  Y N 497 
TRP OXT  O  N N 498 
TRP H    H  N N 499 
TRP H2   H  N N 500 
TRP HA   H  N N 501 
TRP HB2  H  N N 502 
TRP HB3  H  N N 503 
TRP HD1  H  N N 504 
TRP HE1  H  N N 505 
TRP HE3  H  N N 506 
TRP HZ2  H  N N 507 
TRP HZ3  H  N N 508 
TRP HH2  H  N N 509 
TRP HXT  H  N N 510 
TYR N    N  N N 511 
TYR CA   C  N S 512 
TYR C    C  N N 513 
TYR O    O  N N 514 
TYR CB   C  N N 515 
TYR CG   C  Y N 516 
TYR CD1  C  Y N 517 
TYR CD2  C  Y N 518 
TYR CE1  C  Y N 519 
TYR CE2  C  Y N 520 
TYR CZ   C  Y N 521 
TYR OH   O  N N 522 
TYR OXT  O  N N 523 
TYR H    H  N N 524 
TYR H2   H  N N 525 
TYR HA   H  N N 526 
TYR HB2  H  N N 527 
TYR HB3  H  N N 528 
TYR HD1  H  N N 529 
TYR HD2  H  N N 530 
TYR HE1  H  N N 531 
TYR HE2  H  N N 532 
TYR HH   H  N N 533 
TYR HXT  H  N N 534 
VAL N    N  N N 535 
VAL CA   C  N S 536 
VAL C    C  N N 537 
VAL O    O  N N 538 
VAL CB   C  N N 539 
VAL CG1  C  N N 540 
VAL CG2  C  N N 541 
VAL OXT  O  N N 542 
VAL H    H  N N 543 
VAL H2   H  N N 544 
VAL HA   H  N N 545 
VAL HB   H  N N 546 
VAL HG11 H  N N 547 
VAL HG12 H  N N 548 
VAL HG13 H  N N 549 
VAL HG21 H  N N 550 
VAL HG22 H  N N 551 
VAL HG23 H  N N 552 
VAL HXT  H  N N 553 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
D0L C21 C20  sing N N 83  
D0L C20 C19  sing N N 84  
D0L C19 C18  sing N N 85  
D0L C18 C17  sing N N 86  
D0L C14 N2   sing N N 87  
D0L C14 C13  sing N N 88  
D0L C17 C16  sing N N 89  
D0L C15 N2   sing N N 90  
D0L C15 C16  sing N N 91  
D0L N2  C11  sing N N 92  
D0L C13 C12  sing N N 93  
D0L O2  C9   doub N N 94  
D0L C11 C12  sing N N 95  
D0L C11 C10  sing N N 96  
D0L C5  C4   doub Y N 97  
D0L C5  C6   sing Y N 98  
D0L C4  C3   sing Y N 99  
D0L C6  C1   doub Y N 100 
D0L N1  C10  sing N N 101 
D0L N1  C8   sing N N 102 
D0L C9  O1   sing N N 103 
D0L C9  C8   sing N N 104 
D0L C10 O3   doub N N 105 
D0L C3  C2   doub Y N 106 
D0L C1  C2   sing Y N 107 
D0L C8  C7   sing N N 108 
D0L C2  C7   sing N N 109 
D0L C1  H1   sing N N 110 
D0L C15 H2   sing N N 111 
D0L C15 H3   sing N N 112 
D0L C14 H4   sing N N 113 
D0L C14 H5   sing N N 114 
D0L C7  H6   sing N N 115 
D0L C7  H7   sing N N 116 
D0L C12 H8   sing N N 117 
D0L C12 H9   sing N N 118 
D0L C3  H10  sing N N 119 
D0L C13 H11  sing N N 120 
D0L C13 H12  sing N N 121 
D0L C11 H13  sing N N 122 
D0L C6  H14  sing N N 123 
D0L C8  H15  sing N N 124 
D0L C5  H16  sing N N 125 
D0L C4  H17  sing N N 126 
D0L O1  H18  sing N N 127 
D0L C16 H20  sing N N 128 
D0L C16 H21  sing N N 129 
D0L C17 H22  sing N N 130 
D0L C17 H23  sing N N 131 
D0L C18 H24  sing N N 132 
D0L C18 H25  sing N N 133 
D0L C19 H26  sing N N 134 
D0L C19 H27  sing N N 135 
D0L C20 H28  sing N N 136 
D0L C20 H29  sing N N 137 
D0L C21 H30  sing N N 138 
D0L C21 H31  sing N N 139 
D0L C21 H32  sing N N 140 
D0L N1  H33  sing N N 141 
GLN N   CA   sing N N 142 
GLN N   H    sing N N 143 
GLN N   H2   sing N N 144 
GLN CA  C    sing N N 145 
GLN CA  CB   sing N N 146 
GLN CA  HA   sing N N 147 
GLN C   O    doub N N 148 
GLN C   OXT  sing N N 149 
GLN CB  CG   sing N N 150 
GLN CB  HB2  sing N N 151 
GLN CB  HB3  sing N N 152 
GLN CG  CD   sing N N 153 
GLN CG  HG2  sing N N 154 
GLN CG  HG3  sing N N 155 
GLN CD  OE1  doub N N 156 
GLN CD  NE2  sing N N 157 
GLN NE2 HE21 sing N N 158 
GLN NE2 HE22 sing N N 159 
GLN OXT HXT  sing N N 160 
GLU N   CA   sing N N 161 
GLU N   H    sing N N 162 
GLU N   H2   sing N N 163 
GLU CA  C    sing N N 164 
GLU CA  CB   sing N N 165 
GLU CA  HA   sing N N 166 
GLU C   O    doub N N 167 
GLU C   OXT  sing N N 168 
GLU CB  CG   sing N N 169 
GLU CB  HB2  sing N N 170 
GLU CB  HB3  sing N N 171 
GLU CG  CD   sing N N 172 
GLU CG  HG2  sing N N 173 
GLU CG  HG3  sing N N 174 
GLU CD  OE1  doub N N 175 
GLU CD  OE2  sing N N 176 
GLU OE2 HE2  sing N N 177 
GLU OXT HXT  sing N N 178 
GLY N   CA   sing N N 179 
GLY N   H    sing N N 180 
GLY N   H2   sing N N 181 
GLY CA  C    sing N N 182 
GLY CA  HA2  sing N N 183 
GLY CA  HA3  sing N N 184 
GLY C   O    doub N N 185 
GLY C   OXT  sing N N 186 
GLY OXT HXT  sing N N 187 
GOL C1  O1   sing N N 188 
GOL C1  C2   sing N N 189 
GOL C1  H11  sing N N 190 
GOL C1  H12  sing N N 191 
GOL O1  HO1  sing N N 192 
GOL C2  O2   sing N N 193 
GOL C2  C3   sing N N 194 
GOL C2  H2   sing N N 195 
GOL O2  HO2  sing N N 196 
GOL C3  O3   sing N N 197 
GOL C3  H31  sing N N 198 
GOL C3  H32  sing N N 199 
GOL O3  HO3  sing N N 200 
HEM CHA C1A  sing N N 201 
HEM CHA C4D  doub N N 202 
HEM CHA HHA  sing N N 203 
HEM CHB C4A  sing N N 204 
HEM CHB C1B  doub N N 205 
HEM CHB HHB  sing N N 206 
HEM CHC C4B  sing N N 207 
HEM CHC C1C  doub N N 208 
HEM CHC HHC  sing N N 209 
HEM CHD C4C  doub N N 210 
HEM CHD C1D  sing N N 211 
HEM CHD HHD  sing N N 212 
HEM C1A C2A  doub Y N 213 
HEM C1A NA   sing Y N 214 
HEM C2A C3A  sing Y N 215 
HEM C2A CAA  sing N N 216 
HEM C3A C4A  doub Y N 217 
HEM C3A CMA  sing N N 218 
HEM C4A NA   sing Y N 219 
HEM CMA HMA  sing N N 220 
HEM CMA HMAA sing N N 221 
HEM CMA HMAB sing N N 222 
HEM CAA CBA  sing N N 223 
HEM CAA HAA  sing N N 224 
HEM CAA HAAA sing N N 225 
HEM CBA CGA  sing N N 226 
HEM CBA HBA  sing N N 227 
HEM CBA HBAA sing N N 228 
HEM CGA O1A  doub N N 229 
HEM CGA O2A  sing N N 230 
HEM C1B C2B  sing N N 231 
HEM C1B NB   sing N N 232 
HEM C2B C3B  doub N N 233 
HEM C2B CMB  sing N N 234 
HEM C3B C4B  sing N N 235 
HEM C3B CAB  sing N N 236 
HEM C4B NB   doub N N 237 
HEM CMB HMB  sing N N 238 
HEM CMB HMBA sing N N 239 
HEM CMB HMBB sing N N 240 
HEM CAB CBB  doub N N 241 
HEM CAB HAB  sing N N 242 
HEM CBB HBB  sing N N 243 
HEM CBB HBBA sing N N 244 
HEM C1C C2C  sing Y N 245 
HEM C1C NC   sing Y N 246 
HEM C2C C3C  doub Y N 247 
HEM C2C CMC  sing N N 248 
HEM C3C C4C  sing Y N 249 
HEM C3C CAC  sing N N 250 
HEM C4C NC   sing Y N 251 
HEM CMC HMC  sing N N 252 
HEM CMC HMCA sing N N 253 
HEM CMC HMCB sing N N 254 
HEM CAC CBC  doub N N 255 
HEM CAC HAC  sing N N 256 
HEM CBC HBC  sing N N 257 
HEM CBC HBCA sing N N 258 
HEM C1D C2D  sing N N 259 
HEM C1D ND   doub N N 260 
HEM C2D C3D  doub N N 261 
HEM C2D CMD  sing N N 262 
HEM C3D C4D  sing N N 263 
HEM C3D CAD  sing N N 264 
HEM C4D ND   sing N N 265 
HEM CMD HMD  sing N N 266 
HEM CMD HMDA sing N N 267 
HEM CMD HMDB sing N N 268 
HEM CAD CBD  sing N N 269 
HEM CAD HAD  sing N N 270 
HEM CAD HADA sing N N 271 
HEM CBD CGD  sing N N 272 
HEM CBD HBD  sing N N 273 
HEM CBD HBDA sing N N 274 
HEM CGD O1D  doub N N 275 
HEM CGD O2D  sing N N 276 
HEM O2A H2A  sing N N 277 
HEM O2D H2D  sing N N 278 
HEM FE  NA   sing N N 279 
HEM FE  NB   sing N N 280 
HEM FE  NC   sing N N 281 
HEM FE  ND   sing N N 282 
HIS N   CA   sing N N 283 
HIS N   H    sing N N 284 
HIS N   H2   sing N N 285 
HIS CA  C    sing N N 286 
HIS CA  CB   sing N N 287 
HIS CA  HA   sing N N 288 
HIS C   O    doub N N 289 
HIS C   OXT  sing N N 290 
HIS CB  CG   sing N N 291 
HIS CB  HB2  sing N N 292 
HIS CB  HB3  sing N N 293 
HIS CG  ND1  sing Y N 294 
HIS CG  CD2  doub Y N 295 
HIS ND1 CE1  doub Y N 296 
HIS ND1 HD1  sing N N 297 
HIS CD2 NE2  sing Y N 298 
HIS CD2 HD2  sing N N 299 
HIS CE1 NE2  sing Y N 300 
HIS CE1 HE1  sing N N 301 
HIS NE2 HE2  sing N N 302 
HIS OXT HXT  sing N N 303 
HOH O   H1   sing N N 304 
HOH O   H2   sing N N 305 
ILE N   CA   sing N N 306 
ILE N   H    sing N N 307 
ILE N   H2   sing N N 308 
ILE CA  C    sing N N 309 
ILE CA  CB   sing N N 310 
ILE CA  HA   sing N N 311 
ILE C   O    doub N N 312 
ILE C   OXT  sing N N 313 
ILE CB  CG1  sing N N 314 
ILE CB  CG2  sing N N 315 
ILE CB  HB   sing N N 316 
ILE CG1 CD1  sing N N 317 
ILE CG1 HG12 sing N N 318 
ILE CG1 HG13 sing N N 319 
ILE CG2 HG21 sing N N 320 
ILE CG2 HG22 sing N N 321 
ILE CG2 HG23 sing N N 322 
ILE CD1 HD11 sing N N 323 
ILE CD1 HD12 sing N N 324 
ILE CD1 HD13 sing N N 325 
ILE OXT HXT  sing N N 326 
LEU N   CA   sing N N 327 
LEU N   H    sing N N 328 
LEU N   H2   sing N N 329 
LEU CA  C    sing N N 330 
LEU CA  CB   sing N N 331 
LEU CA  HA   sing N N 332 
LEU C   O    doub N N 333 
LEU C   OXT  sing N N 334 
LEU CB  CG   sing N N 335 
LEU CB  HB2  sing N N 336 
LEU CB  HB3  sing N N 337 
LEU CG  CD1  sing N N 338 
LEU CG  CD2  sing N N 339 
LEU CG  HG   sing N N 340 
LEU CD1 HD11 sing N N 341 
LEU CD1 HD12 sing N N 342 
LEU CD1 HD13 sing N N 343 
LEU CD2 HD21 sing N N 344 
LEU CD2 HD22 sing N N 345 
LEU CD2 HD23 sing N N 346 
LEU OXT HXT  sing N N 347 
LYS N   CA   sing N N 348 
LYS N   H    sing N N 349 
LYS N   H2   sing N N 350 
LYS CA  C    sing N N 351 
LYS CA  CB   sing N N 352 
LYS CA  HA   sing N N 353 
LYS C   O    doub N N 354 
LYS C   OXT  sing N N 355 
LYS CB  CG   sing N N 356 
LYS CB  HB2  sing N N 357 
LYS CB  HB3  sing N N 358 
LYS CG  CD   sing N N 359 
LYS CG  HG2  sing N N 360 
LYS CG  HG3  sing N N 361 
LYS CD  CE   sing N N 362 
LYS CD  HD2  sing N N 363 
LYS CD  HD3  sing N N 364 
LYS CE  NZ   sing N N 365 
LYS CE  HE2  sing N N 366 
LYS CE  HE3  sing N N 367 
LYS NZ  HZ1  sing N N 368 
LYS NZ  HZ2  sing N N 369 
LYS NZ  HZ3  sing N N 370 
LYS OXT HXT  sing N N 371 
MET N   CA   sing N N 372 
MET N   H    sing N N 373 
MET N   H2   sing N N 374 
MET CA  C    sing N N 375 
MET CA  CB   sing N N 376 
MET CA  HA   sing N N 377 
MET C   O    doub N N 378 
MET C   OXT  sing N N 379 
MET CB  CG   sing N N 380 
MET CB  HB2  sing N N 381 
MET CB  HB3  sing N N 382 
MET CG  SD   sing N N 383 
MET CG  HG2  sing N N 384 
MET CG  HG3  sing N N 385 
MET SD  CE   sing N N 386 
MET CE  HE1  sing N N 387 
MET CE  HE2  sing N N 388 
MET CE  HE3  sing N N 389 
MET OXT HXT  sing N N 390 
PHE N   CA   sing N N 391 
PHE N   H    sing N N 392 
PHE N   H2   sing N N 393 
PHE CA  C    sing N N 394 
PHE CA  CB   sing N N 395 
PHE CA  HA   sing N N 396 
PHE C   O    doub N N 397 
PHE C   OXT  sing N N 398 
PHE CB  CG   sing N N 399 
PHE CB  HB2  sing N N 400 
PHE CB  HB3  sing N N 401 
PHE CG  CD1  doub Y N 402 
PHE CG  CD2  sing Y N 403 
PHE CD1 CE1  sing Y N 404 
PHE CD1 HD1  sing N N 405 
PHE CD2 CE2  doub Y N 406 
PHE CD2 HD2  sing N N 407 
PHE CE1 CZ   doub Y N 408 
PHE CE1 HE1  sing N N 409 
PHE CE2 CZ   sing Y N 410 
PHE CE2 HE2  sing N N 411 
PHE CZ  HZ   sing N N 412 
PHE OXT HXT  sing N N 413 
PRO N   CA   sing N N 414 
PRO N   CD   sing N N 415 
PRO N   H    sing N N 416 
PRO CA  C    sing N N 417 
PRO CA  CB   sing N N 418 
PRO CA  HA   sing N N 419 
PRO C   O    doub N N 420 
PRO C   OXT  sing N N 421 
PRO CB  CG   sing N N 422 
PRO CB  HB2  sing N N 423 
PRO CB  HB3  sing N N 424 
PRO CG  CD   sing N N 425 
PRO CG  HG2  sing N N 426 
PRO CG  HG3  sing N N 427 
PRO CD  HD2  sing N N 428 
PRO CD  HD3  sing N N 429 
PRO OXT HXT  sing N N 430 
SER N   CA   sing N N 431 
SER N   H    sing N N 432 
SER N   H2   sing N N 433 
SER CA  C    sing N N 434 
SER CA  CB   sing N N 435 
SER CA  HA   sing N N 436 
SER C   O    doub N N 437 
SER C   OXT  sing N N 438 
SER CB  OG   sing N N 439 
SER CB  HB2  sing N N 440 
SER CB  HB3  sing N N 441 
SER OG  HG   sing N N 442 
SER OXT HXT  sing N N 443 
SYN CAC CAE  doub Y N 444 
SYN CAC CAD  sing Y N 445 
SYN CAE CAG  sing Y N 446 
SYN CAD CAF  doub Y N 447 
SYN CAG CAH  doub Y N 448 
SYN CAF CAH  sing Y N 449 
SYN CAH CAB  sing N N 450 
SYN CAB CAA  doub N N 451 
SYN CAF H1   sing N N 452 
SYN CAD H2   sing N N 453 
SYN CAC H3   sing N N 454 
SYN CAE H4   sing N N 455 
SYN CAG H5   sing N N 456 
SYN CAB H6   sing N N 457 
SYN CAA H8   sing N N 458 
SYN CAA H9   sing N N 459 
THR N   CA   sing N N 460 
THR N   H    sing N N 461 
THR N   H2   sing N N 462 
THR CA  C    sing N N 463 
THR CA  CB   sing N N 464 
THR CA  HA   sing N N 465 
THR C   O    doub N N 466 
THR C   OXT  sing N N 467 
THR CB  OG1  sing N N 468 
THR CB  CG2  sing N N 469 
THR CB  HB   sing N N 470 
THR OG1 HG1  sing N N 471 
THR CG2 HG21 sing N N 472 
THR CG2 HG22 sing N N 473 
THR CG2 HG23 sing N N 474 
THR OXT HXT  sing N N 475 
TRP N   CA   sing N N 476 
TRP N   H    sing N N 477 
TRP N   H2   sing N N 478 
TRP CA  C    sing N N 479 
TRP CA  CB   sing N N 480 
TRP CA  HA   sing N N 481 
TRP C   O    doub N N 482 
TRP C   OXT  sing N N 483 
TRP CB  CG   sing N N 484 
TRP CB  HB2  sing N N 485 
TRP CB  HB3  sing N N 486 
TRP CG  CD1  doub Y N 487 
TRP CG  CD2  sing Y N 488 
TRP CD1 NE1  sing Y N 489 
TRP CD1 HD1  sing N N 490 
TRP CD2 CE2  doub Y N 491 
TRP CD2 CE3  sing Y N 492 
TRP NE1 CE2  sing Y N 493 
TRP NE1 HE1  sing N N 494 
TRP CE2 CZ2  sing Y N 495 
TRP CE3 CZ3  doub Y N 496 
TRP CE3 HE3  sing N N 497 
TRP CZ2 CH2  doub Y N 498 
TRP CZ2 HZ2  sing N N 499 
TRP CZ3 CH2  sing Y N 500 
TRP CZ3 HZ3  sing N N 501 
TRP CH2 HH2  sing N N 502 
TRP OXT HXT  sing N N 503 
TYR N   CA   sing N N 504 
TYR N   H    sing N N 505 
TYR N   H2   sing N N 506 
TYR CA  C    sing N N 507 
TYR CA  CB   sing N N 508 
TYR CA  HA   sing N N 509 
TYR C   O    doub N N 510 
TYR C   OXT  sing N N 511 
TYR CB  CG   sing N N 512 
TYR CB  HB2  sing N N 513 
TYR CB  HB3  sing N N 514 
TYR CG  CD1  doub Y N 515 
TYR CG  CD2  sing Y N 516 
TYR CD1 CE1  sing Y N 517 
TYR CD1 HD1  sing N N 518 
TYR CD2 CE2  doub Y N 519 
TYR CD2 HD2  sing N N 520 
TYR CE1 CZ   doub Y N 521 
TYR CE1 HE1  sing N N 522 
TYR CE2 CZ   sing Y N 523 
TYR CE2 HE2  sing N N 524 
TYR CZ  OH   sing N N 525 
TYR OH  HH   sing N N 526 
TYR OXT HXT  sing N N 527 
VAL N   CA   sing N N 528 
VAL N   H    sing N N 529 
VAL N   H2   sing N N 530 
VAL CA  C    sing N N 531 
VAL CA  CB   sing N N 532 
VAL CA  HA   sing N N 533 
VAL C   O    doub N N 534 
VAL C   OXT  sing N N 535 
VAL CB  CG1  sing N N 536 
VAL CB  CG2  sing N N 537 
VAL CB  HB   sing N N 538 
VAL CG1 HG11 sing N N 539 
VAL CG1 HG12 sing N N 540 
VAL CG1 HG13 sing N N 541 
VAL CG2 HG21 sing N N 542 
VAL CG2 HG22 sing N N 543 
VAL CG2 HG23 sing N N 544 
VAL OXT HXT  sing N N 545 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Science and Technology'                      Japan JPMJCR15P3 1 
'Japan Society for the Promotion of Science (JSPS)' Japan JP19H05784 2 
'Japan Society for the Promotion of Science (JSPS)' Japan JP18KK0397 3 
'Japan Society for the Promotion of Science (JSPS)' Japan JP19K22403 4 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6K58 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_data_reduction.diffrn_id             1 
_pdbx_serial_crystallography_data_reduction.frames_total          ? 
_pdbx_serial_crystallography_data_reduction.xfel_pulse_events     ? 
_pdbx_serial_crystallography_data_reduction.frame_hits            ? 
_pdbx_serial_crystallography_data_reduction.crystal_hits          30786 
_pdbx_serial_crystallography_data_reduction.droplet_hits          ? 
_pdbx_serial_crystallography_data_reduction.frames_failed_index   ? 
_pdbx_serial_crystallography_data_reduction.frames_indexed        22930 
_pdbx_serial_crystallography_data_reduction.lattices_indexed      ? 
_pdbx_serial_crystallography_data_reduction.xfel_run_numbers      ? 
_pdbx_serial_crystallography_data_reduction.lattices_merged       ? 
# 
_pdbx_serial_crystallography_measurement.diffrn_id                    1 
_pdbx_serial_crystallography_measurement.pulse_energy                 ? 
_pdbx_serial_crystallography_measurement.pulse_duration               10 
_pdbx_serial_crystallography_measurement.xfel_pulse_repetition_rate   30 
_pdbx_serial_crystallography_measurement.pulse_photon_energy          13 
_pdbx_serial_crystallography_measurement.photons_per_pulse            ? 
_pdbx_serial_crystallography_measurement.source_size                  ? 
_pdbx_serial_crystallography_measurement.source_distance              ? 
_pdbx_serial_crystallography_measurement.focal_spot_size              19.313 
_pdbx_serial_crystallography_measurement.collimation                  ? 
_pdbx_serial_crystallography_measurement.collection_time_total        6.4 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   Fixed-target 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_pdbx_serial_crystallography_sample_delivery_fixed_target.diffrn_id                       1 
_pdbx_serial_crystallography_sample_delivery_fixed_target.description                     
'microcrystals were mounted on mesh loop and flash-frozen by liquid nitrogen' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_holding                  'polyimide film' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.support_base                    'SPINE magnet base' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_unit_size                36 
_pdbx_serial_crystallography_sample_delivery_fixed_target.crystals_per_unit               50 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_solvent                  
'125 mM Tris-HCl (pH 8.3), 14% w/v PEG 8000, 60 mM MgCl2, saturated styrene, and 30% glycerol' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_dehydration_prevention   none 
_pdbx_serial_crystallography_sample_delivery_fixed_target.motion_control                  'stepper motors' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_horizontal             ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_vertical               ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.details                         ? 
# 
_atom_sites.entry_id                    8YB0 
_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]   0.016998 
_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]   0.007786 
_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]   0.006688 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . THR A 1 1   ? -11.102 -23.445 -24.689 1.00 80.76  ? 1    THR A N   1 
ATOM   2    C  CA  . THR A 1 1   ? -9.871  -23.740 -23.963 1.00 79.03  ? 1    THR A CA  1 
ATOM   3    C  C   . THR A 1 1   ? -10.165 -24.410 -22.621 1.00 73.67  ? 1    THR A C   1 
ATOM   4    O  O   . THR A 1 1   ? -9.705  -23.952 -21.574 1.00 73.16  ? 1    THR A O   1 
ATOM   5    C  CB  . THR A 1 1   ? -9.039  -22.464 -23.716 1.00 81.14  ? 1    THR A CB  1 
ATOM   6    O  OG1 . THR A 1 1   ? -7.991  -22.746 -22.776 1.00 83.22  ? 1    THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 1   ? -9.923  -21.347 -23.172 1.00 74.69  ? 1    THR A CG2 1 
ATOM   8    N  N   . ILE A 1 2   ? -10.925 -25.501 -22.666 1.00 72.57  ? 2    ILE A N   1 
ATOM   9    C  CA  . ILE A 1 2   ? -11.311 -26.235 -21.464 1.00 69.48  ? 2    ILE A CA  1 
ATOM   10   C  C   . ILE A 1 2   ? -10.103 -27.034 -20.977 1.00 70.63  ? 2    ILE A C   1 
ATOM   11   O  O   . ILE A 1 2   ? -9.653  -27.967 -21.647 1.00 70.41  ? 2    ILE A O   1 
ATOM   12   C  CB  . ILE A 1 2   ? -12.509 -27.151 -21.732 1.00 69.06  ? 2    ILE A CB  1 
ATOM   13   C  CG1 . ILE A 1 2   ? -13.746 -26.311 -22.067 1.00 70.30  ? 2    ILE A CG1 1 
ATOM   14   C  CG2 . ILE A 1 2   ? -12.765 -28.055 -20.532 1.00 66.88  ? 2    ILE A CG2 1 
ATOM   15   C  CD1 . ILE A 1 2   ? -14.953 -27.124 -22.488 1.00 72.95  ? 2    ILE A CD1 1 
ATOM   16   N  N   . LYS A 1 3   ? -9.578  -26.665 -19.808 1.00 68.08  ? 3    LYS A N   1 
ATOM   17   C  CA  . LYS A 1 3   ? -8.457  -27.350 -19.180 1.00 63.98  ? 3    LYS A CA  1 
ATOM   18   C  C   . LYS A 1 3   ? -8.942  -28.451 -18.244 1.00 64.52  ? 3    LYS A C   1 
ATOM   19   O  O   . LYS A 1 3   ? -10.092 -28.463 -17.792 1.00 62.06  ? 3    LYS A O   1 
ATOM   20   C  CB  . LYS A 1 3   ? -7.593  -26.372 -18.385 1.00 59.25  ? 3    LYS A CB  1 
ATOM   21   C  CG  . LYS A 1 3   ? -6.545  -25.650 -19.182 1.00 65.87  ? 3    LYS A CG  1 
ATOM   22   C  CD  . LYS A 1 3   ? -5.473  -25.111 -18.258 1.00 61.61  ? 3    LYS A CD  1 
ATOM   23   C  CE  . LYS A 1 3   ? -4.402  -24.385 -19.040 1.00 69.29  ? 3    LYS A CE  1 
ATOM   24   N  NZ  . LYS A 1 3   ? -4.906  -23.108 -19.613 1.00 72.49  ? 3    LYS A NZ  1 
ATOM   25   N  N   . GLU A 1 4   ? -8.031  -29.372 -17.939 1.00 64.15  ? 4    GLU A N   1 
ATOM   26   C  CA  . GLU A 1 4   ? -8.243  -30.400 -16.930 1.00 62.45  ? 4    GLU A CA  1 
ATOM   27   C  C   . GLU A 1 4   ? -7.433  -30.024 -15.696 1.00 55.30  ? 4    GLU A C   1 
ATOM   28   O  O   . GLU A 1 4   ? -6.211  -29.865 -15.768 1.00 59.21  ? 4    GLU A O   1 
ATOM   29   C  CB  . GLU A 1 4   ? -7.847  -31.784 -17.447 1.00 65.01  ? 4    GLU A CB  1 
ATOM   30   C  CG  . GLU A 1 4   ? -8.081  -32.889 -16.436 1.00 67.92  ? 4    GLU A CG  1 
ATOM   31   C  CD  . GLU A 1 4   ? -9.503  -33.413 -16.478 1.00 78.14  ? 4    GLU A CD  1 
ATOM   32   O  OE1 . GLU A 1 4   ? -9.686  -34.651 -16.481 1.00 82.65  ? 4    GLU A OE1 1 
ATOM   33   O  OE2 . GLU A 1 4   ? -10.439 -32.585 -16.507 1.00 79.15  ? 4    GLU A OE2 1 
ATOM   34   N  N   . MET A 1 5   ? -8.109  -29.880 -14.582 1.00 58.26  ? 5    MET A N   1 
ATOM   35   C  CA  . MET A 1 5   ? -7.446  -29.338 -13.406 1.00 47.24  ? 5    MET A CA  1 
ATOM   36   C  C   . MET A 1 5   ? -6.756  -30.458 -12.627 1.00 43.37  ? 5    MET A C   1 
ATOM   37   O  O   . MET A 1 5   ? -7.239  -31.590 -12.612 1.00 43.24  ? 5    MET A O   1 
ATOM   38   C  CB  . MET A 1 5   ? -8.479  -28.584 -12.569 1.00 52.35  ? 5    MET A CB  1 
ATOM   39   C  CG  . MET A 1 5   ? -9.460  -29.427 -11.799 1.00 46.84  ? 5    MET A CG  1 
ATOM   40   S  SD  . MET A 1 5   ? -10.293 -28.496 -10.501 1.00 44.58  ? 5    MET A SD  1 
ATOM   41   C  CE  . MET A 1 5   ? -11.582 -27.761 -11.503 1.00 50.01  ? 5    MET A CE  1 
ATOM   42   N  N   . PRO A 1 6   ? -5.589  -30.191 -12.047 1.00 41.30  ? 6    PRO A N   1 
ATOM   43   C  CA  . PRO A 1 6   ? -4.876  -31.236 -11.306 1.00 43.45  ? 6    PRO A CA  1 
ATOM   44   C  C   . PRO A 1 6   ? -5.627  -31.632 -10.043 1.00 45.48  ? 6    PRO A C   1 
ATOM   45   O  O   . PRO A 1 6   ? -6.595  -30.992 -9.622  1.00 41.38  ? 6    PRO A O   1 
ATOM   46   C  CB  . PRO A 1 6   ? -3.532  -30.588 -10.973 1.00 43.80  ? 6    PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 6   ? -3.805  -29.122 -11.002 1.00 45.13  ? 6    PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 6   ? -4.836  -28.925 -12.079 1.00 42.35  ? 6    PRO A CD  1 
ATOM   49   N  N   . GLN A 1 7   ? -5.156  -32.723 -9.439  1.00 43.51  ? 7    GLN A N   1 
ATOM   50   C  CA  . GLN A 1 7   ? -5.758  -33.294 -8.249  1.00 41.03  ? 7    GLN A CA  1 
ATOM   51   C  C   . GLN A 1 7   ? -4.628  -33.923 -7.451  1.00 45.67  ? 7    GLN A C   1 
ATOM   52   O  O   . GLN A 1 7   ? -3.784  -34.618 -8.046  1.00 40.71  ? 7    GLN A O   1 
ATOM   53   C  CB  . GLN A 1 7   ? -6.811  -34.349 -8.576  1.00 41.66  ? 7    GLN A CB  1 
ATOM   54   C  CG  . GLN A 1 7   ? -7.453  -34.990 -7.349  1.00 41.77  ? 7    GLN A CG  1 
ATOM   55   C  CD  . GLN A 1 7   ? -8.560  -35.938 -7.733  1.00 44.63  ? 7    GLN A CD  1 
ATOM   56   O  OE1 . GLN A 1 7   ? -8.745  -36.231 -8.911  1.00 46.99  ? 7    GLN A OE1 1 
ATOM   57   N  NE2 . GLN A 1 7   ? -9.319  -36.413 -6.748  1.00 42.02  ? 7    GLN A NE2 1 
ATOM   58   N  N   . PRO A 1 8   ? -4.572  -33.705 -6.134  1.00 41.27  ? 8    PRO A N   1 
ATOM   59   C  CA  . PRO A 1 8   ? -3.523  -34.351 -5.335  1.00 38.31  ? 8    PRO A CA  1 
ATOM   60   C  C   . PRO A 1 8   ? -3.743  -35.849 -5.198  1.00 36.95  ? 8    PRO A C   1 
ATOM   61   O  O   . PRO A 1 8   ? -4.735  -36.400 -5.684  1.00 39.42  ? 8    PRO A O   1 
ATOM   62   C  CB  . PRO A 1 8   ? -3.615  -33.633 -3.975  1.00 39.51  ? 8    PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 8   ? -5.048  -33.147 -3.902  1.00 37.72  ? 8    PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 8   ? -5.377  -32.756 -5.334  1.00 40.88  ? 8    PRO A CD  1 
ATOM   65   N  N   . LYS A 1 9   ? -2.807  -36.509 -4.521  1.00 39.42  ? 9    LYS A N   1 
ATOM   66   C  CA  . LYS A 1 9   ? -2.784  -37.967 -4.470  1.00 42.44  ? 9    LYS A CA  1 
ATOM   67   C  C   . LYS A 1 9   ? -4.021  -38.529 -3.781  1.00 39.74  ? 9    LYS A C   1 
ATOM   68   O  O   . LYS A 1 9   ? -4.519  -37.964 -2.803  1.00 38.98  ? 9    LYS A O   1 
ATOM   69   C  CB  . LYS A 1 9   ? -1.523  -38.442 -3.748  1.00 37.49  ? 9    LYS A CB  1 
ATOM   70   C  CG  . LYS A 1 9   ? -1.345  -37.950 -2.312  1.00 41.09  ? 9    LYS A CG  1 
ATOM   71   C  CD  . LYS A 1 9   ? 0.045   -38.317 -1.803  1.00 41.36  ? 9    LYS A CD  1 
ATOM   72   C  CE  . LYS A 1 9   ? 0.298   -37.802 -0.408  1.00 43.55  ? 9    LYS A CE  1 
ATOM   73   N  NZ  . LYS A 1 9   ? 1.733   -37.760 -0.012  1.00 42.94  ? 9    LYS A NZ  1 
ATOM   74   N  N   . THR A 1 10  ? -4.481  -39.675 -4.270  1.00 40.30  ? 10   THR A N   1 
ATOM   75   C  CA  . THR A 1 10  ? -5.692  -40.328 -3.805  1.00 38.16  ? 10   THR A CA  1 
ATOM   76   C  C   . THR A 1 10  ? -5.373  -41.606 -3.040  1.00 42.55  ? 10   THR A C   1 
ATOM   77   O  O   . THR A 1 10  ? -4.270  -42.165 -3.121  1.00 38.39  ? 10   THR A O   1 
ATOM   78   C  CB  . THR A 1 10  ? -6.635  -40.640 -4.977  1.00 43.08  ? 10   THR A CB  1 
ATOM   79   O  OG1 . THR A 1 10  ? -5.967  -41.475 -5.939  1.00 43.20  ? 10   THR A OG1 1 
ATOM   80   C  CG2 . THR A 1 10  ? -7.104  -39.342 -5.661  1.00 42.37  ? 10   THR A CG2 1 
ATOM   81   N  N   . PHE A 1 11  ? -6.386  -42.072 -2.311  1.00 40.75  ? 11   PHE A N   1 
ATOM   82   C  CA  . PHE A 1 11  ? -6.275  -43.194 -1.390  1.00 41.14  ? 11   PHE A CA  1 
ATOM   83   C  C   . PHE A 1 11  ? -7.424  -44.161 -1.653  1.00 41.00  ? 11   PHE A C   1 
ATOM   84   O  O   . PHE A 1 11  ? -8.218  -44.481 -0.769  1.00 43.12  ? 11   PHE A O   1 
ATOM   85   C  CB  . PHE A 1 11  ? -6.287  -42.703 0.066   1.00 38.24  ? 11   PHE A CB  1 
ATOM   86   C  CG  . PHE A 1 11  ? -5.116  -41.835 0.432   1.00 39.22  ? 11   PHE A CG  1 
ATOM   87   C  CD1 . PHE A 1 11  ? -5.028  -40.516 -0.005  1.00 35.19  ? 11   PHE A CD1 1 
ATOM   88   C  CD2 . PHE A 1 11  ? -4.097  -42.331 1.222   1.00 39.30  ? 11   PHE A CD2 1 
ATOM   89   C  CE1 . PHE A 1 11  ? -3.949  -39.725 0.343   1.00 36.48  ? 11   PHE A CE1 1 
ATOM   90   C  CE2 . PHE A 1 11  ? -3.023  -41.539 1.576   1.00 39.76  ? 11   PHE A CE2 1 
ATOM   91   C  CZ  . PHE A 1 11  ? -2.945  -40.233 1.134   1.00 38.33  ? 11   PHE A CZ  1 
ATOM   92   N  N   . GLY A 1 12  ? -7.524  -44.625 -2.896  1.00 39.78  ? 12   GLY A N   1 
ATOM   93   C  CA  . GLY A 1 12  ? -8.583  -45.556 -3.249  1.00 40.42  ? 12   GLY A CA  1 
ATOM   94   C  C   . GLY A 1 12  ? -9.958  -44.973 -2.981  1.00 48.17  ? 12   GLY A C   1 
ATOM   95   O  O   . GLY A 1 12  ? -10.256 -43.827 -3.338  1.00 44.46  ? 12   GLY A O   1 
ATOM   96   N  N   . GLU A 1 13  ? -10.815 -45.768 -2.339  1.00 42.77  ? 13   GLU A N   1 
ATOM   97   C  CA  . GLU A 1 13  ? -12.185 -45.325 -2.100  1.00 50.98  ? 13   GLU A CA  1 
ATOM   98   C  C   . GLU A 1 13  ? -12.264 -44.099 -1.198  1.00 50.74  ? 13   GLU A C   1 
ATOM   99   O  O   . GLU A 1 13  ? -13.280 -43.393 -1.228  1.00 50.74  ? 13   GLU A O   1 
ATOM   100  C  CB  . GLU A 1 13  ? -13.024 -46.458 -1.499  1.00 55.16  ? 13   GLU A CB  1 
ATOM   101  C  CG  . GLU A 1 13  ? -13.273 -47.615 -2.458  1.00 62.48  ? 13   GLU A CG  1 
ATOM   102  C  CD  . GLU A 1 13  ? -14.168 -47.224 -3.628  1.00 74.51  ? 13   GLU A CD  1 
ATOM   103  O  OE1 . GLU A 1 13  ? -14.922 -48.096 -4.120  1.00 77.43  ? 13   GLU A OE1 1 
ATOM   104  O  OE2 . GLU A 1 13  ? -14.116 -46.049 -4.062  1.00 79.50  ? 13   GLU A OE2 1 
ATOM   105  N  N   . LEU A 1 14  ? -11.236 -43.832 -0.396  1.00 42.42  ? 14   LEU A N   1 
ATOM   106  C  CA  . LEU A 1 14  ? -11.238 -42.640 0.445   1.00 44.86  ? 14   LEU A CA  1 
ATOM   107  C  C   . LEU A 1 14  ? -10.887 -41.380 -0.329  1.00 47.83  ? 14   LEU A C   1 
ATOM   108  O  O   . LEU A 1 14  ? -10.914 -40.288 0.252   1.00 43.86  ? 14   LEU A O   1 
ATOM   109  C  CB  . LEU A 1 14  ? -10.269 -42.813 1.615   1.00 44.70  ? 14   LEU A CB  1 
ATOM   110  C  CG  . LEU A 1 14  ? -10.516 -44.030 2.513   1.00 45.05  ? 14   LEU A CG  1 
ATOM   111  C  CD1 . LEU A 1 14  ? -9.456  -44.109 3.586   1.00 46.42  ? 14   LEU A CD1 1 
ATOM   112  C  CD2 . LEU A 1 14  ? -11.894 -43.951 3.140   1.00 54.35  ? 14   LEU A CD2 1 
ATOM   113  N  N   . LYS A 1 15  ? -10.540 -41.515 -1.610  1.00 43.19  ? 15   LYS A N   1 
ATOM   114  C  CA  . LYS A 1 15  ? -10.191 -40.389 -2.471  1.00 43.48  ? 15   LYS A CA  1 
ATOM   115  C  C   . LYS A 1 15  ? -9.121  -39.511 -1.826  1.00 44.35  ? 15   LYS A C   1 
ATOM   116  O  O   . LYS A 1 15  ? -8.042  -40.012 -1.497  1.00 40.25  ? 15   LYS A O   1 
ATOM   117  C  CB  . LYS A 1 15  ? -11.474 -39.636 -2.826  1.00 47.29  ? 15   LYS A CB  1 
ATOM   118  C  CG  . LYS A 1 15  ? -12.496 -40.642 -3.370  1.00 49.49  ? 15   LYS A CG  1 
ATOM   119  C  CD  . LYS A 1 15  ? -13.466 -40.091 -4.386  1.00 55.45  ? 15   LYS A CD  1 
ATOM   120  C  CE  . LYS A 1 15  ? -14.662 -41.034 -4.522  1.00 57.82  ? 15   LYS A CE  1 
ATOM   121  N  NZ  . LYS A 1 15  ? -15.713 -40.492 -5.423  1.00 64.22  ? 15   LYS A NZ  1 
ATOM   122  N  N   . ASN A 1 16  ? -9.373  -38.212 -1.645  1.00 40.94  ? 16   ASN A N   1 
ATOM   123  C  CA  . ASN A 1 16  ? -8.371  -37.344 -1.035  1.00 39.91  ? 16   ASN A CA  1 
ATOM   124  C  C   . ASN A 1 16  ? -8.542  -37.174 0.468   1.00 35.52  ? 16   ASN A C   1 
ATOM   125  O  O   . ASN A 1 16  ? -7.734  -36.484 1.088   1.00 39.85  ? 16   ASN A O   1 
ATOM   126  C  CB  . ASN A 1 16  ? -8.383  -35.956 -1.683  1.00 40.49  ? 16   ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 16  ? -7.961  -35.988 -3.131  1.00 40.44  ? 16   ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 16  ? -8.715  -35.588 -4.013  1.00 40.27  ? 16   ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 16  ? -6.756  -36.490 -3.386  1.00 41.63  ? 16   ASN A ND2 1 
ATOM   130  N  N   . LEU A 1 17  ? -9.564  -37.782 1.070   1.00 43.60  ? 17   LEU A N   1 
ATOM   131  C  CA  . LEU A 1 17  ? -9.834  -37.539 2.484   1.00 41.46  ? 17   LEU A CA  1 
ATOM   132  C  C   . LEU A 1 17  ? -8.608  -37.677 3.370   1.00 43.91  ? 17   LEU A C   1 
ATOM   133  O  O   . LEU A 1 17  ? -8.409  -36.807 4.233   1.00 40.95  ? 17   LEU A O   1 
ATOM   134  C  CB  . LEU A 1 17  ? -10.952 -38.467 2.970   1.00 45.12  ? 17   LEU A CB  1 
ATOM   135  C  CG  . LEU A 1 17  ? -11.874 -37.854 4.021   1.00 48.34  ? 17   LEU A CG  1 
ATOM   136  C  CD1 . LEU A 1 17  ? -12.237 -36.412 3.659   1.00 48.16  ? 17   LEU A CD1 1 
ATOM   137  C  CD2 . LEU A 1 17  ? -13.130 -38.706 4.150   1.00 47.95  ? 17   LEU A CD2 1 
ATOM   138  N  N   . PRO A 1 18  ? -7.740  -38.683 3.204   1.00 39.66  ? 18   PRO A N   1 
ATOM   139  C  CA  . PRO A 1 18  ? -6.630  -38.846 4.152   1.00 39.10  ? 18   PRO A CA  1 
ATOM   140  C  C   . PRO A 1 18  ? -5.615  -37.719 4.131   1.00 37.94  ? 18   PRO A C   1 
ATOM   141  O  O   . PRO A 1 18  ? -4.820  -37.614 5.074   1.00 39.06  ? 18   PRO A O   1 
ATOM   142  C  CB  . PRO A 1 18  ? -5.996  -40.179 3.726   1.00 41.42  ? 18   PRO A CB  1 
ATOM   143  C  CG  . PRO A 1 18  ? -7.126  -40.925 3.146   1.00 38.09  ? 18   PRO A CG  1 
ATOM   144  C  CD  . PRO A 1 18  ? -7.904  -39.878 2.360   1.00 42.54  ? 18   PRO A CD  1 
ATOM   145  N  N   . LEU A 1 19  ? -5.615  -36.865 3.111   1.00 37.42  ? 19   LEU A N   1 
ATOM   146  C  CA  . LEU A 1 19  ? -4.744  -35.697 3.133   1.00 38.60  ? 19   LEU A CA  1 
ATOM   147  C  C   . LEU A 1 19  ? -5.102  -34.733 4.264   1.00 39.61  ? 19   LEU A C   1 
ATOM   148  O  O   . LEU A 1 19  ? -4.254  -33.940 4.685   1.00 41.00  ? 19   LEU A O   1 
ATOM   149  C  CB  . LEU A 1 19  ? -4.814  -34.992 1.781   1.00 41.23  ? 19   LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 19  ? -4.350  -35.872 0.610   1.00 41.94  ? 19   LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 19  ? -4.626  -35.196 -0.733  1.00 43.23  ? 19   LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 19  ? -2.874  -36.194 0.769   1.00 40.37  ? 19   LEU A CD2 1 
ATOM   153  N  N   . LEU A 1 20  ? -6.334  -34.786 4.759   1.00 39.50  ? 20   LEU A N   1 
ATOM   154  C  CA  . LEU A 1 20  ? -6.751  -34.002 5.913   1.00 38.28  ? 20   LEU A CA  1 
ATOM   155  C  C   . LEU A 1 20  ? -6.404  -34.672 7.237   1.00 42.60  ? 20   LEU A C   1 
ATOM   156  O  O   . LEU A 1 20  ? -6.667  -34.093 8.301   1.00 41.32  ? 20   LEU A O   1 
ATOM   157  C  CB  . LEU A 1 20  ? -8.258  -33.750 5.847   1.00 39.72  ? 20   LEU A CB  1 
ATOM   158  C  CG  . LEU A 1 20  ? -8.701  -33.057 4.558   1.00 41.88  ? 20   LEU A CG  1 
ATOM   159  C  CD1 . LEU A 1 20  ? -10.208 -32.858 4.486   1.00 41.74  ? 20   LEU A CD1 1 
ATOM   160  C  CD2 . LEU A 1 20  ? -7.951  -31.731 4.412   1.00 41.99  ? 20   LEU A CD2 1 
ATOM   161  N  N   . ASN A 1 21  ? -5.806  -35.866 7.212   1.00 41.71  ? 21   ASN A N   1 
ATOM   162  C  CA  . ASN A 1 21  ? -5.466  -36.541 8.466   1.00 43.80  ? 21   ASN A CA  1 
ATOM   163  C  C   . ASN A 1 21  ? -4.124  -35.993 8.947   1.00 44.12  ? 21   ASN A C   1 
ATOM   164  O  O   . ASN A 1 21  ? -3.076  -36.634 8.850   1.00 46.74  ? 21   ASN A O   1 
ATOM   165  C  CB  . ASN A 1 21  ? -5.413  -38.052 8.293   1.00 43.48  ? 21   ASN A CB  1 
ATOM   166  C  CG  . ASN A 1 21  ? -5.066  -38.764 9.591   1.00 54.30  ? 21   ASN A CG  1 
ATOM   167  O  OD1 . ASN A 1 21  ? -4.738  -38.125 10.593  1.00 52.88  ? 21   ASN A OD1 1 
ATOM   168  N  ND2 . ASN A 1 21  ? -5.111  -40.087 9.572   1.00 56.41  ? 21   ASN A ND2 1 
ATOM   169  N  N   . THR A 1 22  ? -4.180  -34.771 9.471   1.00 39.00  ? 22   THR A N   1 
ATOM   170  C  CA  . THR A 1 22  ? -3.029  -34.024 9.949   1.00 40.58  ? 22   THR A CA  1 
ATOM   171  C  C   . THR A 1 22  ? -3.540  -32.974 10.926  1.00 43.21  ? 22   THR A C   1 
ATOM   172  O  O   . THR A 1 22  ? -4.707  -32.583 10.868  1.00 41.72  ? 22   THR A O   1 
ATOM   173  C  CB  . THR A 1 22  ? -2.274  -33.357 8.794   1.00 43.32  ? 22   THR A CB  1 
ATOM   174  O  OG1 . THR A 1 22  ? -1.270  -32.474 9.312   1.00 46.93  ? 22   THR A OG1 1 
ATOM   175  C  CG2 . THR A 1 22  ? -3.250  -32.568 7.919   1.00 39.22  ? 22   THR A CG2 1 
ATOM   176  N  N   . ASP A 1 23  ? -2.671  -32.533 11.837  1.00 40.43  ? 23   ASP A N   1 
ATOM   177  C  CA  . ASP A 1 23  ? -3.083  -31.481 12.756  1.00 44.42  ? 23   ASP A CA  1 
ATOM   178  C  C   . ASP A 1 23  ? -3.002  -30.110 12.113  1.00 38.73  ? 23   ASP A C   1 
ATOM   179  O  O   . ASP A 1 23  ? -3.449  -29.130 12.714  1.00 37.79  ? 23   ASP A O   1 
ATOM   180  C  CB  . ASP A 1 23  ? -2.218  -31.489 14.012  1.00 46.70  ? 23   ASP A CB  1 
ATOM   181  C  CG  . ASP A 1 23  ? -0.741  -31.481 13.688  1.00 51.63  ? 23   ASP A CG  1 
ATOM   182  O  OD1 . ASP A 1 23  ? -0.358  -32.088 12.657  1.00 56.12  ? 23   ASP A OD1 1 
ATOM   183  O  OD2 . ASP A 1 23  ? 0.041   -30.892 14.467  1.00 63.74  ? 23   ASP A OD2 1 
ATOM   184  N  N   . LYS A 1 24  ? -2.426  -30.016 10.916  1.00 38.88  ? 24   LYS A N   1 
ATOM   185  C  CA  . LYS A 1 24  ? -2.285  -28.749 10.202  1.00 39.19  ? 24   LYS A CA  1 
ATOM   186  C  C   . LYS A 1 24  ? -2.819  -28.902 8.783   1.00 36.76  ? 24   LYS A C   1 
ATOM   187  O  O   . LYS A 1 24  ? -2.063  -28.849 7.804   1.00 37.03  ? 24   LYS A O   1 
ATOM   188  C  CB  . LYS A 1 24  ? -0.827  -28.300 10.219  1.00 35.17  ? 24   LYS A CB  1 
ATOM   189  C  CG  . LYS A 1 24  ? -0.311  -28.046 11.632  1.00 38.97  ? 24   LYS A CG  1 
ATOM   190  C  CD  . LYS A 1 24  ? 1.175   -27.679 11.653  1.00 41.20  ? 24   LYS A CD  1 
ATOM   191  C  CE  . LYS A 1 24  ? 1.620   -27.355 13.077  1.00 41.74  ? 24   LYS A CE  1 
ATOM   192  N  NZ  . LYS A 1 24  ? 2.986   -26.769 13.146  1.00 43.22  ? 24   LYS A NZ  1 
ATOM   193  N  N   . PRO A 1 25  ? -4.136  -29.082 8.640   1.00 36.55  ? 25   PRO A N   1 
ATOM   194  C  CA  . PRO A 1 25  ? -4.696  -29.337 7.303   1.00 38.63  ? 25   PRO A CA  1 
ATOM   195  C  C   . PRO A 1 25  ? -4.643  -28.139 6.362   1.00 39.20  ? 25   PRO A C   1 
ATOM   196  O  O   . PRO A 1 25  ? -4.436  -28.333 5.156   1.00 35.34  ? 25   PRO A O   1 
ATOM   197  C  CB  . PRO A 1 25  ? -6.139  -29.763 7.611   1.00 35.92  ? 25   PRO A CB  1 
ATOM   198  C  CG  . PRO A 1 25  ? -6.436  -29.110 8.938   1.00 35.08  ? 25   PRO A CG  1 
ATOM   199  C  CD  . PRO A 1 25  ? -5.151  -29.193 9.704   1.00 38.44  ? 25   PRO A CD  1 
ATOM   200  N  N   . VAL A 1 26  ? -4.861  -26.916 6.859   1.00 34.99  ? 26   VAL A N   1 
ATOM   201  C  CA  . VAL A 1 26  ? -4.771  -25.749 5.984   1.00 39.00  ? 26   VAL A CA  1 
ATOM   202  C  C   . VAL A 1 26  ? -3.359  -25.602 5.444   1.00 39.59  ? 26   VAL A C   1 
ATOM   203  O  O   . VAL A 1 26  ? -3.155  -25.305 4.259   1.00 38.63  ? 26   VAL A O   1 
ATOM   204  C  CB  . VAL A 1 26  ? -5.204  -24.472 6.721   1.00 36.03  ? 26   VAL A CB  1 
ATOM   205  C  CG1 . VAL A 1 26  ? -4.906  -23.256 5.834   1.00 34.07  ? 26   VAL A CG1 1 
ATOM   206  C  CG2 . VAL A 1 26  ? -6.675  -24.545 7.072   1.00 35.23  ? 26   VAL A CG2 1 
ATOM   207  N  N   . GLN A 1 27  ? -2.361  -25.788 6.309   1.00 35.95  ? 27   GLN A N   1 
ATOM   208  C  CA  . GLN A 1 27  ? -0.983  -25.653 5.863   1.00 38.33  ? 27   GLN A CA  1 
ATOM   209  C  C   . GLN A 1 27  ? -0.593  -26.767 4.896   1.00 38.22  ? 27   GLN A C   1 
ATOM   210  O  O   . GLN A 1 27  ? 0.176   -26.530 3.957   1.00 40.94  ? 27   GLN A O   1 
ATOM   211  C  CB  . GLN A 1 27  ? -0.062  -25.610 7.081   1.00 34.48  ? 27   GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 27  ? -0.219  -24.313 7.886   1.00 33.99  ? 27   GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 27  ? 0.364   -24.401 9.277   1.00 36.48  ? 27   GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 27  ? 1.543   -24.104 9.490   1.00 37.34  ? 27   GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 27  ? -0.464  -24.798 10.243  1.00 36.83  ? 27   GLN A NE2 1 
ATOM   216  N  N   . ALA A 1 28  ? -1.132  -27.972 5.087   1.00 37.10  ? 28   ALA A N   1 
ATOM   217  C  CA  . ALA A 1 28  ? -0.934  -29.032 4.103   1.00 38.34  ? 28   ALA A CA  1 
ATOM   218  C  C   . ALA A 1 28  ? -1.550  -28.659 2.762   1.00 39.51  ? 28   ALA A C   1 
ATOM   219  O  O   . ALA A 1 28  ? -0.963  -28.927 1.702   1.00 39.32  ? 28   ALA A O   1 
ATOM   220  C  CB  . ALA A 1 28  ? -1.535  -30.340 4.614   1.00 40.32  ? 28   ALA A CB  1 
ATOM   221  N  N   . LEU A 1 29  ? -2.749  -28.060 2.789   1.00 36.35  ? 29   LEU A N   1 
ATOM   222  C  CA  . LEU A 1 29  ? -3.418  -27.655 1.556   1.00 36.40  ? 29   LEU A CA  1 
ATOM   223  C  C   . LEU A 1 29  ? -2.658  -26.548 0.859   1.00 35.36  ? 29   LEU A C   1 
ATOM   224  O  O   . LEU A 1 29  ? -2.655  -26.480 -0.379  1.00 37.97  ? 29   LEU A O   1 
ATOM   225  C  CB  . LEU A 1 29  ? -4.856  -27.200 1.853   1.00 36.77  ? 29   LEU A CB  1 
ATOM   226  C  CG  . LEU A 1 29  ? -5.829  -28.351 2.143   1.00 37.42  ? 29   LEU A CG  1 
ATOM   227  C  CD1 . LEU A 1 29  ? -7.061  -27.901 2.953   1.00 36.34  ? 29   LEU A CD1 1 
ATOM   228  C  CD2 . LEU A 1 29  ? -6.245  -28.998 0.858   1.00 37.24  ? 29   LEU A CD2 1 
ATOM   229  N  N   . MET A 1 30  ? -2.025  -25.672 1.635   1.00 36.93  ? 30   MET A N   1 
ATOM   230  C  CA  . MET A 1 30  ? -1.173  -24.636 1.069   1.00 37.98  ? 30   MET A CA  1 
ATOM   231  C  C   . MET A 1 30  ? 0.001   -25.259 0.318   1.00 41.66  ? 30   MET A C   1 
ATOM   232  O  O   . MET A 1 30  ? 0.400   -24.778 -0.751  1.00 41.46  ? 30   MET A O   1 
ATOM   233  C  CB  . MET A 1 30  ? -0.664  -23.736 2.188   1.00 37.51  ? 30   MET A CB  1 
ATOM   234  C  CG  . MET A 1 30  ? -1.601  -22.585 2.524   1.00 39.85  ? 30   MET A CG  1 
ATOM   235  S  SD  . MET A 1 30  ? -1.175  -21.834 4.089   1.00 38.00  ? 30   MET A SD  1 
ATOM   236  C  CE  . MET A 1 30  ? -0.010  -20.613 3.477   1.00 41.27  ? 30   MET A CE  1 
ATOM   237  N  N   . LYS A 1 31  ? 0.561   -26.340 0.867   1.00 40.84  ? 31   LYS A N   1 
ATOM   238  C  CA  . LYS A 1 31  ? 1.696   -27.011 0.229   1.00 39.79  ? 31   LYS A CA  1 
ATOM   239  C  C   . LYS A 1 31  ? 1.261   -27.718 -1.048  1.00 41.38  ? 31   LYS A C   1 
ATOM   240  O  O   . LYS A 1 31  ? 2.002   -27.741 -2.042  1.00 42.17  ? 31   LYS A O   1 
ATOM   241  C  CB  . LYS A 1 31  ? 2.323   -27.998 1.220   1.00 45.86  ? 31   LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 31  ? 3.657   -28.593 0.795   1.00 48.71  ? 31   LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 31  ? 4.503   -28.924 2.022   1.00 57.07  ? 31   LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 31  ? 5.012   -27.661 2.714   1.00 64.54  ? 31   LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 31  ? 5.027   -27.797 4.210   1.00 68.83  ? 31   LYS A NZ  1 
ATOM   246  N  N   . ILE A 1 32  ? 0.052   -28.280 -1.050  1.00 37.07  ? 32   ILE A N   1 
ATOM   247  C  CA  . ILE A 1 32  ? -0.515  -28.835 -2.272  1.00 40.11  ? 32   ILE A CA  1 
ATOM   248  C  C   . ILE A 1 32  ? -0.688  -27.739 -3.324  1.00 42.73  ? 32   ILE A C   1 
ATOM   249  O  O   . ILE A 1 32  ? -0.323  -27.911 -4.493  1.00 40.25  ? 32   ILE A O   1 
ATOM   250  C  CB  . ILE A 1 32  ? -1.842  -29.551 -1.962  1.00 38.75  ? 32   ILE A CB  1 
ATOM   251  C  CG1 . ILE A 1 32  ? -1.594  -30.773 -1.070  1.00 40.65  ? 32   ILE A CG1 1 
ATOM   252  C  CG2 . ILE A 1 32  ? -2.539  -29.976 -3.253  1.00 39.03  ? 32   ILE A CG2 1 
ATOM   253  C  CD1 . ILE A 1 32  ? -2.875  -31.431 -0.554  1.00 38.32  ? 32   ILE A CD1 1 
ATOM   254  N  N   . ALA A 1 33  ? -1.247  -26.590 -2.926  1.00 39.74  ? 33   ALA A N   1 
ATOM   255  C  CA  . ALA A 1 33  ? -1.368  -25.475 -3.865  1.00 40.02  ? 33   ALA A CA  1 
ATOM   256  C  C   . ALA A 1 33  ? -0.009  -25.067 -4.422  1.00 41.66  ? 33   ALA A C   1 
ATOM   257  O  O   . ALA A 1 33  ? 0.111   -24.745 -5.609  1.00 44.31  ? 33   ALA A O   1 
ATOM   258  C  CB  . ALA A 1 33  ? -2.046  -24.281 -3.187  1.00 41.18  ? 33   ALA A CB  1 
ATOM   259  N  N   . ASP A 1 34  ? 1.021   -25.055 -3.573  1.00 40.95  ? 34   ASP A N   1 
ATOM   260  C  CA  . ASP A 1 34  ? 2.370   -24.752 -4.043  1.00 41.57  ? 34   ASP A CA  1 
ATOM   261  C  C   . ASP A 1 34  ? 2.751   -25.683 -5.187  1.00 46.35  ? 34   ASP A C   1 
ATOM   262  O  O   . ASP A 1 34  ? 3.385   -25.269 -6.166  1.00 45.36  ? 34   ASP A O   1 
ATOM   263  C  CB  . ASP A 1 34  ? 3.373   -24.927 -2.904  1.00 44.48  ? 34   ASP A CB  1 
ATOM   264  C  CG  . ASP A 1 34  ? 3.483   -23.711 -2.003  1.00 49.89  ? 34   ASP A CG  1 
ATOM   265  O  OD1 . ASP A 1 34  ? 3.926   -23.904 -0.852  1.00 52.82  ? 34   ASP A OD1 1 
ATOM   266  O  OD2 . ASP A 1 34  ? 3.138   -22.586 -2.418  1.00 53.99  ? 34   ASP A OD2 1 
ATOM   267  N  N   . GLU A 1 35  ? 2.389   -26.957 -5.064  1.00 45.30  ? 35   GLU A N   1 
ATOM   268  C  CA  . GLU A 1 35  ? 2.796   -27.964 -6.036  1.00 46.19  ? 35   GLU A CA  1 
ATOM   269  C  C   . GLU A 1 35  ? 1.891   -27.977 -7.266  1.00 46.79  ? 35   GLU A C   1 
ATOM   270  O  O   . GLU A 1 35  ? 2.375   -28.169 -8.390  1.00 47.35  ? 35   GLU A O   1 
ATOM   271  C  CB  . GLU A 1 35  ? 2.819   -29.341 -5.363  1.00 50.18  ? 35   GLU A CB  1 
ATOM   272  C  CG  . GLU A 1 35  ? 3.151   -30.502 -6.285  1.00 58.21  ? 35   GLU A CG  1 
ATOM   273  C  CD  . GLU A 1 35  ? 3.001   -31.850 -5.593  1.00 61.43  ? 35   GLU A CD  1 
ATOM   274  O  OE1 . GLU A 1 35  ? 3.521   -32.003 -4.465  1.00 63.98  ? 35   GLU A OE1 1 
ATOM   275  O  OE2 . GLU A 1 35  ? 2.374   -32.759 -6.184  1.00 65.85  ? 35   GLU A OE2 1 
ATOM   276  N  N   . LEU A 1 36  ? 0.582   -27.775 -7.093  1.00 40.14  ? 36   LEU A N   1 
ATOM   277  C  CA  . LEU A 1 36  ? -0.362  -27.980 -8.189  1.00 42.08  ? 36   LEU A CA  1 
ATOM   278  C  C   . LEU A 1 36  ? -0.847  -26.694 -8.853  1.00 45.09  ? 36   LEU A C   1 
ATOM   279  O  O   . LEU A 1 36  ? -1.316  -26.749 -10.001 1.00 43.38  ? 36   LEU A O   1 
ATOM   280  C  CB  . LEU A 1 36  ? -1.576  -28.778 -7.702  1.00 41.11  ? 36   LEU A CB  1 
ATOM   281  C  CG  . LEU A 1 36  ? -1.239  -30.135 -7.078  1.00 45.25  ? 36   LEU A CG  1 
ATOM   282  C  CD1 . LEU A 1 36  ? -2.508  -30.928 -6.812  1.00 42.81  ? 36   LEU A CD1 1 
ATOM   283  C  CD2 . LEU A 1 36  ? -0.297  -30.902 -8.007  1.00 45.12  ? 36   LEU A CD2 1 
ATOM   284  N  N   . GLY A 1 37  ? -0.765  -25.561 -8.172  1.00 41.43  ? 37   GLY A N   1 
ATOM   285  C  CA  . GLY A 1 37  ? -1.078  -24.270 -8.754  1.00 38.52  ? 37   GLY A CA  1 
ATOM   286  C  C   . GLY A 1 37  ? -2.393  -23.681 -8.273  1.00 44.20  ? 37   GLY A C   1 
ATOM   287  O  O   . GLY A 1 37  ? -2.915  -24.005 -7.193  1.00 40.77  ? 37   GLY A O   1 
ATOM   288  N  N   . GLU A 1 38  ? -2.946  -22.801 -9.117  1.00 40.99  ? 38   GLU A N   1 
ATOM   289  C  CA  . GLU A 1 38  ? -4.047  -21.921 -8.723  1.00 38.94  ? 38   GLU A CA  1 
ATOM   290  C  C   . GLU A 1 38  ? -5.371  -22.649 -8.531  1.00 39.40  ? 38   GLU A C   1 
ATOM   291  O  O   . GLU A 1 38  ? -6.279  -22.084 -7.906  1.00 36.16  ? 38   GLU A O   1 
ATOM   292  C  CB  . GLU A 1 38  ? -4.221  -20.820 -9.774  1.00 37.44  ? 38   GLU A CB  1 
ATOM   293  C  CG  . GLU A 1 38  ? -4.690  -21.366 -11.111 1.00 38.54  ? 38   GLU A CG  1 
ATOM   294  C  CD  . GLU A 1 38  ? -4.833  -20.286 -12.174 1.00 44.42  ? 38   GLU A CD  1 
ATOM   295  O  OE1 . GLU A 1 38  ? -4.927  -19.089 -11.808 1.00 39.92  ? 38   GLU A OE1 1 
ATOM   296  O  OE2 . GLU A 1 38  ? -4.849  -20.640 -13.373 1.00 44.93  ? 38   GLU A OE2 1 
ATOM   297  N  N   . ILE A 1 39  ? -5.525  -23.864 -9.057  1.00 37.73  ? 39   ILE A N   1 
ATOM   298  C  CA  . ILE A 1 39  ? -6.771  -24.600 -8.886  1.00 37.21  ? 39   ILE A CA  1 
ATOM   299  C  C   . ILE A 1 39  ? -6.470  -26.093 -8.819  1.00 43.31  ? 39   ILE A C   1 
ATOM   300  O  O   . ILE A 1 39  ? -5.730  -26.623 -9.653  1.00 40.36  ? 39   ILE A O   1 
ATOM   301  C  CB  . ILE A 1 39  ? -7.782  -24.293 -10.009 1.00 38.23  ? 39   ILE A CB  1 
ATOM   302  C  CG1 . ILE A 1 39  ? -9.114  -24.981 -9.720  1.00 37.87  ? 39   ILE A CG1 1 
ATOM   303  C  CG2 . ILE A 1 39  ? -7.250  -24.725 -11.382 1.00 43.42  ? 39   ILE A CG2 1 
ATOM   304  C  CD1 . ILE A 1 39  ? -10.224 -24.527 -10.646 1.00 43.40  ? 39   ILE A CD1 1 
ATOM   305  N  N   . PHE A 1 40  ? -7.050  -26.785 -7.832  1.00 36.61  ? 40   PHE A N   1 
ATOM   306  C  CA  . PHE A 1 40  ? -6.993  -28.243 -7.850  1.00 36.60  ? 40   PHE A CA  1 
ATOM   307  C  C   . PHE A 1 40  ? -8.283  -28.854 -7.321  1.00 41.37  ? 40   PHE A C   1 
ATOM   308  O  O   . PHE A 1 40  ? -8.958  -28.293 -6.448  1.00 38.57  ? 40   PHE A O   1 
ATOM   309  C  CB  . PHE A 1 40  ? -5.755  -28.786 -7.085  1.00 36.77  ? 40   PHE A CB  1 
ATOM   310  C  CG  . PHE A 1 40  ? -5.704  -28.444 -5.607  1.00 37.62  ? 40   PHE A CG  1 
ATOM   311  C  CD1 . PHE A 1 40  ? -6.292  -29.270 -4.665  1.00 38.98  ? 40   PHE A CD1 1 
ATOM   312  C  CD2 . PHE A 1 40  ? -4.991  -27.339 -5.168  1.00 36.36  ? 40   PHE A CD2 1 
ATOM   313  C  CE1 . PHE A 1 40  ? -6.211  -28.965 -3.306  1.00 37.86  ? 40   PHE A CE1 1 
ATOM   314  C  CE2 . PHE A 1 40  ? -4.893  -27.032 -3.820  1.00 38.48  ? 40   PHE A CE2 1 
ATOM   315  C  CZ  . PHE A 1 40  ? -5.507  -27.849 -2.888  1.00 38.53  ? 40   PHE A CZ  1 
ATOM   316  N  N   . LYS A 1 41  ? -8.633  -30.002 -7.899  1.00 37.38  ? 41   LYS A N   1 
ATOM   317  C  CA  . LYS A 1 41  ? -9.790  -30.776 -7.473  1.00 39.86  ? 41   LYS A CA  1 
ATOM   318  C  C   . LYS A 1 41  ? -9.462  -31.547 -6.194  1.00 37.07  ? 41   LYS A C   1 
ATOM   319  O  O   . LYS A 1 41  ? -8.341  -32.022 -6.019  1.00 39.58  ? 41   LYS A O   1 
ATOM   320  C  CB  . LYS A 1 41  ? -10.188 -31.740 -8.592  1.00 42.27  ? 41   LYS A CB  1 
ATOM   321  C  CG  . LYS A 1 41  ? -11.342 -32.666 -8.276  1.00 42.54  ? 41   LYS A CG  1 
ATOM   322  C  CD  . LYS A 1 41  ? -11.927 -33.226 -9.571  1.00 50.36  ? 41   LYS A CD  1 
ATOM   323  C  CE  . LYS A 1 41  ? -12.943 -34.321 -9.298  1.00 52.93  ? 41   LYS A CE  1 
ATOM   324  N  NZ  . LYS A 1 41  ? -13.641 -34.768 -10.544 1.00 61.19  ? 41   LYS A NZ  1 
ATOM   325  N  N   . PHE A 1 42  ? -10.434 -31.635 -5.281  1.00 39.72  ? 42   PHE A N   1 
ATOM   326  C  CA  . PHE A 1 42  ? -10.265 -32.375 -4.033  1.00 38.29  ? 42   PHE A CA  1 
ATOM   327  C  C   . PHE A 1 42  ? -11.548 -33.155 -3.802  1.00 42.61  ? 42   PHE A C   1 
ATOM   328  O  O   . PHE A 1 42  ? -12.631 -32.560 -3.717  1.00 40.80  ? 42   PHE A O   1 
ATOM   329  C  CB  . PHE A 1 42  ? -9.979  -31.424 -2.860  1.00 39.58  ? 42   PHE A CB  1 
ATOM   330  C  CG  . PHE A 1 42  ? -9.565  -32.118 -1.569  1.00 38.04  ? 42   PHE A CG  1 
ATOM   331  C  CD1 . PHE A 1 42  ? -10.502 -32.765 -0.772  1.00 40.99  ? 42   PHE A CD1 1 
ATOM   332  C  CD2 . PHE A 1 42  ? -8.243  -32.083 -1.144  1.00 40.74  ? 42   PHE A CD2 1 
ATOM   333  C  CE1 . PHE A 1 42  ? -10.119 -33.380 0.431   1.00 38.66  ? 42   PHE A CE1 1 
ATOM   334  C  CE2 . PHE A 1 42  ? -7.857  -32.701 0.051   1.00 43.50  ? 42   PHE A CE2 1 
ATOM   335  C  CZ  . PHE A 1 42  ? -8.807  -33.339 0.837   1.00 37.42  ? 42   PHE A CZ  1 
ATOM   336  N  N   . GLU A 1 43  ? -11.441 -34.482 -3.738  1.00 39.18  ? 43   GLU A N   1 
ATOM   337  C  CA  . GLU A 1 43  ? -12.605 -35.341 -3.598  1.00 40.97  ? 43   GLU A CA  1 
ATOM   338  C  C   . GLU A 1 43  ? -12.578 -36.075 -2.263  1.00 41.20  ? 43   GLU A C   1 
ATOM   339  O  O   . GLU A 1 43  ? -11.516 -36.421 -1.741  1.00 39.85  ? 43   GLU A O   1 
ATOM   340  C  CB  . GLU A 1 43  ? -12.699 -36.370 -4.731  1.00 44.26  ? 43   GLU A CB  1 
ATOM   341  C  CG  . GLU A 1 43  ? -12.981 -35.789 -6.102  1.00 50.23  ? 43   GLU A CG  1 
ATOM   342  C  CD  . GLU A 1 43  ? -12.895 -36.845 -7.181  1.00 53.45  ? 43   GLU A CD  1 
ATOM   343  O  OE1 . GLU A 1 43  ? -11.886 -37.583 -7.203  1.00 56.14  ? 43   GLU A OE1 1 
ATOM   344  O  OE2 . GLU A 1 43  ? -13.845 -36.953 -7.982  1.00 58.41  ? 43   GLU A OE2 1 
ATOM   345  N  N   . ALA A 1 44  ? -13.762 -36.290 -1.716  1.00 42.26  ? 44   ALA A N   1 
ATOM   346  C  CA  . ALA A 1 44  ? -14.003 -37.218 -0.622  1.00 43.20  ? 44   ALA A CA  1 
ATOM   347  C  C   . ALA A 1 44  ? -15.161 -38.099 -1.037  1.00 42.71  ? 44   ALA A C   1 
ATOM   348  O  O   . ALA A 1 44  ? -15.857 -37.809 -2.015  1.00 43.29  ? 44   ALA A O   1 
ATOM   349  C  CB  . ALA A 1 44  ? -14.331 -36.483 0.689   1.00 44.52  ? 44   ALA A CB  1 
ATOM   350  N  N   . PRO A 1 45  ? -15.399 -39.192 -0.326  1.00 45.92  ? 45   PRO A N   1 
ATOM   351  C  CA  . PRO A 1 45  ? -16.583 -39.997 -0.637  1.00 48.58  ? 45   PRO A CA  1 
ATOM   352  C  C   . PRO A 1 45  ? -17.819 -39.115 -0.654  1.00 47.89  ? 45   PRO A C   1 
ATOM   353  O  O   . PRO A 1 45  ? -18.105 -38.420 0.328   1.00 48.39  ? 45   PRO A O   1 
ATOM   354  C  CB  . PRO A 1 45  ? -16.619 -41.029 0.495   1.00 48.82  ? 45   PRO A CB  1 
ATOM   355  C  CG  . PRO A 1 45  ? -15.189 -41.152 0.922   1.00 49.83  ? 45   PRO A CG  1 
ATOM   356  C  CD  . PRO A 1 45  ? -14.594 -39.777 0.763   1.00 42.88  ? 45   PRO A CD  1 
ATOM   357  N  N   . GLY A 1 46  ? -18.518 -39.092 -1.787  1.00 48.92  ? 46   GLY A N   1 
ATOM   358  C  CA  . GLY A 1 46  ? -19.743 -38.322 -1.917  1.00 52.97  ? 46   GLY A CA  1 
ATOM   359  C  C   . GLY A 1 46  ? -19.590 -36.814 -1.897  1.00 53.35  ? 46   GLY A C   1 
ATOM   360  O  O   . GLY A 1 46  ? -20.539 -36.115 -1.530  1.00 58.37  ? 46   GLY A O   1 
ATOM   361  N  N   . ARG A 1 47  ? -18.425 -36.286 -2.274  1.00 50.14  ? 47   ARG A N   1 
ATOM   362  C  CA  . ARG A 1 47  ? -18.256 -34.838 -2.318  1.00 50.69  ? 47   ARG A CA  1 
ATOM   363  C  C   . ARG A 1 47  ? -17.059 -34.462 -3.180  1.00 46.74  ? 47   ARG A C   1 
ATOM   364  O  O   . ARG A 1 47  ? -16.020 -35.129 -3.145  1.00 47.40  ? 47   ARG A O   1 
ATOM   365  C  CB  . ARG A 1 47  ? -18.082 -34.229 -0.920  1.00 44.98  ? 47   ARG A CB  1 
ATOM   366  C  CG  . ARG A 1 47  ? -17.598 -32.782 -1.004  1.00 51.38  ? 47   ARG A CG  1 
ATOM   367  C  CD  . ARG A 1 47  ? -17.876 -31.963 0.238   1.00 52.79  ? 47   ARG A CD  1 
ATOM   368  N  NE  . ARG A 1 47  ? -17.287 -30.629 0.141   1.00 53.67  ? 47   ARG A NE  1 
ATOM   369  C  CZ  . ARG A 1 47  ? -16.763 -29.977 1.173   1.00 50.40  ? 47   ARG A CZ  1 
ATOM   370  N  NH1 . ARG A 1 47  ? -16.743 -30.512 2.385   1.00 53.56  ? 47   ARG A NH1 1 
ATOM   371  N  NH2 . ARG A 1 47  ? -16.227 -28.772 0.982   1.00 38.21  ? 47   ARG A NH2 1 
ATOM   372  N  N   . VAL A 1 48  ? -17.210 -33.370 -3.929  1.00 43.36  ? 48   VAL A N   1 
ATOM   373  C  CA  . VAL A 1 48  ? -16.138 -32.771 -4.713  1.00 42.32  ? 48   VAL A CA  1 
ATOM   374  C  C   . VAL A 1 48  ? -16.099 -31.281 -4.395  1.00 40.16  ? 48   VAL A C   1 
ATOM   375  O  O   . VAL A 1 48  ? -17.148 -30.636 -4.297  1.00 39.49  ? 48   VAL A O   1 
ATOM   376  C  CB  . VAL A 1 48  ? -16.341 -32.974 -6.231  1.00 43.70  ? 48   VAL A CB  1 
ATOM   377  C  CG1 . VAL A 1 48  ? -15.301 -32.182 -7.010  1.00 44.55  ? 48   VAL A CG1 1 
ATOM   378  C  CG2 . VAL A 1 48  ? -16.288 -34.451 -6.608  1.00 50.42  ? 48   VAL A CG2 1 
ATOM   379  N  N   . THR A 1 49  ? -14.900 -30.731 -4.249  1.00 39.29  ? 49   THR A N   1 
ATOM   380  C  CA  . THR A 1 49  ? -14.733 -29.286 -4.245  1.00 38.77  ? 49   THR A CA  1 
ATOM   381  C  C   . THR A 1 49  ? -13.467 -28.945 -5.016  1.00 39.83  ? 49   THR A C   1 
ATOM   382  O  O   . THR A 1 49  ? -12.705 -29.830 -5.422  1.00 41.90  ? 49   THR A O   1 
ATOM   383  C  CB  . THR A 1 49  ? -14.705 -28.714 -2.817  1.00 38.63  ? 49   THR A CB  1 
ATOM   384  O  OG1 . THR A 1 49  ? -14.798 -27.285 -2.878  1.00 39.37  ? 49   THR A OG1 1 
ATOM   385  C  CG2 . THR A 1 49  ? -13.439 -29.111 -2.103  1.00 35.05  ? 49   THR A CG2 1 
ATOM   386  N  N   . ARG A 1 50  ? -13.256 -27.650 -5.237  1.00 36.55  ? 50   ARG A N   1 
ATOM   387  C  CA  . ARG A 1 50  ? -12.096 -27.161 -5.974  1.00 37.43  ? 50   ARG A CA  1 
ATOM   388  C  C   . ARG A 1 50  ? -11.444 -26.045 -5.170  1.00 37.49  ? 50   ARG A C   1 
ATOM   389  O  O   . ARG A 1 50  ? -12.102 -25.054 -4.833  1.00 38.37  ? 50   ARG A O   1 
ATOM   390  C  CB  . ARG A 1 50  ? -12.510 -26.669 -7.368  1.00 43.22  ? 50   ARG A CB  1 
ATOM   391  C  CG  . ARG A 1 50  ? -13.248 -27.742 -8.159  1.00 39.36  ? 50   ARG A CG  1 
ATOM   392  C  CD  . ARG A 1 50  ? -14.497 -27.195 -8.812  1.00 42.28  ? 50   ARG A CD  1 
ATOM   393  N  NE  . ARG A 1 50  ? -15.319 -28.239 -9.406  1.00 42.09  ? 50   ARG A NE  1 
ATOM   394  C  CZ  . ARG A 1 50  ? -16.323 -28.841 -8.779  1.00 44.12  ? 50   ARG A CZ  1 
ATOM   395  N  NH1 . ARG A 1 50  ? -16.678 -28.502 -7.549  1.00 40.54  ? 50   ARG A NH1 1 
ATOM   396  N  NH2 . ARG A 1 50  ? -16.991 -29.808 -9.397  1.00 43.22  ? 50   ARG A NH2 1 
ATOM   397  N  N   . TYR A 1 51  ? -10.154 -26.186 -4.884  1.00 35.17  ? 51   TYR A N   1 
ATOM   398  C  CA  . TYR A 1 51  ? -9.422  -25.197 -4.102  1.00 36.57  ? 51   TYR A CA  1 
ATOM   399  C  C   . TYR A 1 51  ? -8.806  -24.142 -5.020  1.00 40.90  ? 51   TYR A C   1 
ATOM   400  O  O   . TYR A 1 51  ? -7.978  -24.468 -5.884  1.00 37.85  ? 51   TYR A O   1 
ATOM   401  C  CB  . TYR A 1 51  ? -8.346  -25.884 -3.268  1.00 35.31  ? 51   TYR A CB  1 
ATOM   402  C  CG  . TYR A 1 51  ? -8.902  -26.571 -2.032  1.00 36.88  ? 51   TYR A CG  1 
ATOM   403  C  CD1 . TYR A 1 51  ? -9.443  -27.846 -2.110  1.00 36.33  ? 51   TYR A CD1 1 
ATOM   404  C  CD2 . TYR A 1 51  ? -8.891  -25.934 -0.792  1.00 35.74  ? 51   TYR A CD2 1 
ATOM   405  C  CE1 . TYR A 1 51  ? -9.957  -28.473 -0.985  1.00 36.00  ? 51   TYR A CE1 1 
ATOM   406  C  CE2 . TYR A 1 51  ? -9.388  -26.550 0.329   1.00 35.58  ? 51   TYR A CE2 1 
ATOM   407  C  CZ  . TYR A 1 51  ? -9.925  -27.815 0.226   1.00 36.98  ? 51   TYR A CZ  1 
ATOM   408  O  OH  . TYR A 1 51  ? -10.430 -28.428 1.337   1.00 36.29  ? 51   TYR A OH  1 
ATOM   409  N  N   . LEU A 1 52  ? -9.203  -22.880 -4.828  1.00 37.18  ? 52   LEU A N   1 
ATOM   410  C  CA  . LEU A 1 52  ? -8.692  -21.747 -5.598  1.00 38.91  ? 52   LEU A CA  1 
ATOM   411  C  C   . LEU A 1 52  ? -7.655  -20.978 -4.788  1.00 38.18  ? 52   LEU A C   1 
ATOM   412  O  O   . LEU A 1 52  ? -7.844  -20.719 -3.595  1.00 33.77  ? 52   LEU A O   1 
ATOM   413  C  CB  . LEU A 1 52  ? -9.824  -20.794 -6.001  1.00 35.87  ? 52   LEU A CB  1 
ATOM   414  C  CG  . LEU A 1 52  ? -11.025 -21.335 -6.763  1.00 39.06  ? 52   LEU A CG  1 
ATOM   415  C  CD1 . LEU A 1 52  ? -11.950 -20.172 -7.161  1.00 39.38  ? 52   LEU A CD1 1 
ATOM   416  C  CD2 . LEU A 1 52  ? -10.590 -22.116 -7.996  1.00 39.86  ? 52   LEU A CD2 1 
ATOM   417  N  N   . SER A 1 53  ? -6.556  -20.612 -5.446  1.00 32.51  ? 53   SER A N   1 
ATOM   418  C  CA  . SER A 1 53  ? -5.441  -19.938 -4.806  1.00 35.45  ? 53   SER A CA  1 
ATOM   419  C  C   . SER A 1 53  ? -4.987  -18.672 -5.522  1.00 35.33  ? 53   SER A C   1 
ATOM   420  O  O   . SER A 1 53  ? -4.109  -17.984 -4.999  1.00 35.91  ? 53   SER A O   1 
ATOM   421  C  CB  . SER A 1 53  ? -4.227  -20.884 -4.718  1.00 38.86  ? 53   SER A CB  1 
ATOM   422  O  OG  . SER A 1 53  ? -4.497  -21.945 -3.832  1.00 45.33  ? 53   SER A OG  1 
ATOM   423  N  N   . SER A 1 54  ? -5.496  -18.373 -6.715  1.00 37.05  ? 54   SER A N   1 
ATOM   424  C  CA  . SER A 1 54  ? -4.997  -17.222 -7.454  1.00 38.05  ? 54   SER A CA  1 
ATOM   425  C  C   . SER A 1 54  ? -6.031  -16.105 -7.468  1.00 35.43  ? 54   SER A C   1 
ATOM   426  O  O   . SER A 1 54  ? -7.238  -16.352 -7.531  1.00 35.99  ? 54   SER A O   1 
ATOM   427  C  CB  . SER A 1 54  ? -4.618  -17.591 -8.898  1.00 36.57  ? 54   SER A CB  1 
ATOM   428  O  OG  . SER A 1 54  ? -5.753  -17.944 -9.661  1.00 34.88  ? 54   SER A OG  1 
ATOM   429  N  N   . GLN A 1 55  ? -5.541  -14.866 -7.449  1.00 34.64  ? 55   GLN A N   1 
ATOM   430  C  CA  . GLN A 1 55  ? -6.454  -13.742 -7.619  1.00 35.08  ? 55   GLN A CA  1 
ATOM   431  C  C   . GLN A 1 55  ? -7.162  -13.814 -8.966  1.00 36.27  ? 55   GLN A C   1 
ATOM   432  O  O   . GLN A 1 55  ? -8.335  -13.438 -9.069  1.00 35.70  ? 55   GLN A O   1 
ATOM   433  C  CB  . GLN A 1 55  ? -5.689  -12.425 -7.455  1.00 38.65  ? 55   GLN A CB  1 
ATOM   434  C  CG  . GLN A 1 55  ? -6.557  -11.167 -7.526  1.00 32.64  ? 55   GLN A CG  1 
ATOM   435  C  CD  . GLN A 1 55  ? -6.649  -10.599 -8.946  1.00 39.98  ? 55   GLN A CD  1 
ATOM   436  O  OE1 . GLN A 1 55  ? -6.028  -11.117 -9.881  1.00 39.29  ? 55   GLN A OE1 1 
ATOM   437  N  NE2 . GLN A 1 55  ? -7.422  -9.535  -9.111  1.00 35.71  ? 55   GLN A NE2 1 
ATOM   438  N  N   . ARG A 1 56  ? -6.484  -14.326 -10.000 1.00 36.47  ? 56   ARG A N   1 
ATOM   439  C  CA  . ARG A 1 56  ? -7.110  -14.446 -11.315 1.00 38.78  ? 56   ARG A CA  1 
ATOM   440  C  C   . ARG A 1 56  ? -8.454  -15.160 -11.231 1.00 38.27  ? 56   ARG A C   1 
ATOM   441  O  O   . ARG A 1 56  ? -9.450  -14.710 -11.814 1.00 38.49  ? 56   ARG A O   1 
ATOM   442  C  CB  . ARG A 1 56  ? -6.166  -15.180 -12.278 1.00 38.94  ? 56   ARG A CB  1 
ATOM   443  C  CG  . ARG A 1 56  ? -6.735  -15.410 -13.677 1.00 45.11  ? 56   ARG A CG  1 
ATOM   444  C  CD  . ARG A 1 56  ? -5.754  -16.194 -14.558 1.00 44.44  ? 56   ARG A CD  1 
ATOM   445  N  NE  . ARG A 1 56  ? -5.950  -17.638 -14.487 1.00 46.44  ? 56   ARG A NE  1 
ATOM   446  C  CZ  . ARG A 1 56  ? -6.779  -18.337 -15.257 1.00 49.29  ? 56   ARG A CZ  1 
ATOM   447  N  NH1 . ARG A 1 56  ? -7.567  -17.750 -16.149 1.00 46.55  ? 56   ARG A NH1 1 
ATOM   448  N  NH2 . ARG A 1 56  ? -6.815  -19.664 -15.136 1.00 46.13  ? 56   ARG A NH2 1 
ATOM   449  N  N   . LEU A 1 57  ? -8.503  -16.283 -10.508 1.00 36.18  ? 57   LEU A N   1 
ATOM   450  C  CA  . LEU A 1 57  ? -9.732  -17.055 -10.418 1.00 35.47  ? 57   LEU A CA  1 
ATOM   451  C  C   . LEU A 1 57  ? -10.626 -16.604 -9.266  1.00 34.06  ? 57   LEU A C   1 
ATOM   452  O  O   . LEU A 1 57  ? -11.860 -16.663 -9.377  1.00 35.54  ? 57   LEU A O   1 
ATOM   453  C  CB  . LEU A 1 57  ? -9.405  -18.546 -10.267 1.00 37.52  ? 57   LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 57  ? -8.787  -19.211 -11.511 1.00 37.47  ? 57   LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 57  ? -8.447  -20.658 -11.229 1.00 39.68  ? 57   LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 57  ? -9.745  -19.119 -12.700 1.00 36.25  ? 57   LEU A CD2 1 
ATOM   457  N  N   . ILE A 1 58  ? -10.037 -16.155 -8.164  1.00 33.64  ? 58   ILE A N   1 
ATOM   458  C  CA  . ILE A 1 58  ? -10.858 -15.812 -7.007  1.00 33.93  ? 58   ILE A CA  1 
ATOM   459  C  C   . ILE A 1 58  ? -11.669 -14.541 -7.271  1.00 34.36  ? 58   ILE A C   1 
ATOM   460  O  O   . ILE A 1 58  ? -12.793 -14.393 -6.772  1.00 35.40  ? 58   ILE A O   1 
ATOM   461  C  CB  . ILE A 1 58  ? -9.946  -15.721 -5.768  1.00 32.29  ? 58   ILE A CB  1 
ATOM   462  C  CG1 . ILE A 1 58  ? -9.573  -17.144 -5.314  1.00 34.29  ? 58   ILE A CG1 1 
ATOM   463  C  CG2 . ILE A 1 58  ? -10.637 -14.953 -4.635  1.00 33.19  ? 58   ILE A CG2 1 
ATOM   464  C  CD1 . ILE A 1 58  ? -8.385  -17.197 -4.355  1.00 33.18  ? 58   ILE A CD1 1 
ATOM   465  N  N   . LYS A 1 59  ? -11.160 -13.632 -8.113  1.00 35.00  ? 59   LYS A N   1 
ATOM   466  C  CA  . LYS A 1 59  ? -11.938 -12.439 -8.439  1.00 32.33  ? 59   LYS A CA  1 
ATOM   467  C  C   . LYS A 1 59  ? -13.233 -12.803 -9.155  1.00 36.72  ? 59   LYS A C   1 
ATOM   468  O  O   . LYS A 1 59  ? -14.238 -12.098 -9.012  1.00 39.42  ? 59   LYS A O   1 
ATOM   469  C  CB  . LYS A 1 59  ? -11.097 -11.453 -9.267  1.00 34.40  ? 59   LYS A CB  1 
ATOM   470  C  CG  . LYS A 1 59  ? -10.933 -11.804 -10.739 1.00 35.90  ? 59   LYS A CG  1 
ATOM   471  C  CD  . LYS A 1 59  ? -9.812  -10.967 -11.381 1.00 39.25  ? 59   LYS A CD  1 
ATOM   472  C  CE  . LYS A 1 59  ? -9.523  -11.431 -12.800 1.00 41.87  ? 59   LYS A CE  1 
ATOM   473  N  NZ  . LYS A 1 59  ? -8.411  -10.651 -13.417 1.00 44.46  ? 59   LYS A NZ  1 
ATOM   474  N  N   . GLU A 1 60  ? -13.245 -13.907 -9.912  1.00 35.23  ? 60   GLU A N   1 
ATOM   475  C  CA  . GLU A 1 60  ? -14.496 -14.366 -10.513 1.00 35.68  ? 60   GLU A CA  1 
ATOM   476  C  C   . GLU A 1 60  ? -15.379 -15.066 -9.490  1.00 37.32  ? 60   GLU A C   1 
ATOM   477  O  O   . GLU A 1 60  ? -16.601 -14.903 -9.508  1.00 36.53  ? 60   GLU A O   1 
ATOM   478  C  CB  . GLU A 1 60  ? -14.221 -15.303 -11.692 1.00 36.72  ? 60   GLU A CB  1 
ATOM   479  C  CG  . GLU A 1 60  ? -13.472 -14.644 -12.841 1.00 42.48  ? 60   GLU A CG  1 
ATOM   480  C  CD  . GLU A 1 60  ? -13.435 -15.513 -14.083 1.00 43.74  ? 60   GLU A CD  1 
ATOM   481  O  OE1 . GLU A 1 60  ? -14.320 -16.382 -14.225 1.00 42.38  ? 60   GLU A OE1 1 
ATOM   482  O  OE2 . GLU A 1 60  ? -12.529 -15.309 -14.923 1.00 46.75  ? 60   GLU A OE2 1 
ATOM   483  N  N   . ALA A 1 61  ? -14.775 -15.860 -8.606  1.00 34.27  ? 61   ALA A N   1 
ATOM   484  C  CA  . ALA A 1 61  ? -15.528 -16.523 -7.550  1.00 36.22  ? 61   ALA A CA  1 
ATOM   485  C  C   . ALA A 1 61  ? -16.264 -15.519 -6.664  1.00 36.95  ? 61   ALA A C   1 
ATOM   486  O  O   . ALA A 1 61  ? -17.327 -15.841 -6.113  1.00 34.65  ? 61   ALA A O   1 
ATOM   487  C  CB  . ALA A 1 61  ? -14.577 -17.385 -6.714  1.00 32.02  ? 61   ALA A CB  1 
ATOM   488  N  N   . CYS A 1 62  ? -15.724 -14.300 -6.517  1.00 33.39  ? 62   CYS A N   1 
ATOM   489  C  CA  . CYS A 1 62  ? -16.338 -13.281 -5.670  1.00 34.65  ? 62   CYS A CA  1 
ATOM   490  C  C   . CYS A 1 62  ? -17.471 -12.527 -6.349  1.00 36.98  ? 62   CYS A C   1 
ATOM   491  O  O   . CYS A 1 62  ? -17.987 -11.570 -5.761  1.00 33.00  ? 62   CYS A O   1 
ATOM   492  C  CB  . CYS A 1 62  ? -15.276 -12.299 -5.185  1.00 35.43  ? 62   CYS A CB  1 
ATOM   493  S  SG  . CYS A 1 62  ? -14.170 -13.058 -3.979  1.00 35.06  ? 62   CYS A SG  1 
ATOM   494  N  N   . ASP A 1 63  ? -17.864 -12.937 -7.554  1.00 36.15  ? 63   ASP A N   1 
ATOM   495  C  CA  . ASP A 1 63  ? -19.024 -12.379 -8.247  1.00 34.70  ? 63   ASP A CA  1 
ATOM   496  C  C   . ASP A 1 63  ? -20.286 -12.983 -7.639  1.00 32.12  ? 63   ASP A C   1 
ATOM   497  O  O   . ASP A 1 63  ? -20.598 -14.153 -7.882  1.00 35.65  ? 63   ASP A O   1 
ATOM   498  C  CB  . ASP A 1 63  ? -18.919 -12.699 -9.738  1.00 38.09  ? 63   ASP A CB  1 
ATOM   499  C  CG  . ASP A 1 63  ? -20.073 -12.147 -10.556 1.00 40.43  ? 63   ASP A CG  1 
ATOM   500  O  OD1 . ASP A 1 63  ? -21.107 -11.753 -9.994  1.00 36.90  ? 63   ASP A OD1 1 
ATOM   501  O  OD2 . ASP A 1 63  ? -19.956 -12.162 -11.800 1.00 43.20  ? 63   ASP A OD2 1 
ATOM   502  N  N   . GLU A 1 64  ? -21.021 -12.186 -6.851  1.00 35.04  ? 64   GLU A N   1 
ATOM   503  C  CA  . GLU A 1 64  ? -22.193 -12.694 -6.139  1.00 35.59  ? 64   GLU A CA  1 
ATOM   504  C  C   . GLU A 1 64  ? -23.356 -13.032 -7.060  1.00 36.69  ? 64   GLU A C   1 
ATOM   505  O  O   . GLU A 1 64  ? -24.290 -13.723 -6.633  1.00 34.80  ? 64   GLU A O   1 
ATOM   506  C  CB  . GLU A 1 64  ? -22.680 -11.678 -5.100  1.00 34.92  ? 64   GLU A CB  1 
ATOM   507  C  CG  . GLU A 1 64  ? -21.646 -11.222 -4.105  1.00 35.39  ? 64   GLU A CG  1 
ATOM   508  C  CD  . GLU A 1 64  ? -22.212 -10.257 -3.081  1.00 39.36  ? 64   GLU A CD  1 
ATOM   509  O  OE1 . GLU A 1 64  ? -22.749 -10.729 -2.065  1.00 35.58  ? 64   GLU A OE1 1 
ATOM   510  O  OE2 . GLU A 1 64  ? -22.125 -9.022  -3.282  1.00 40.50  ? 64   GLU A OE2 1 
ATOM   511  N  N   . SER A 1 65  ? -23.353 -12.539 -8.297  1.00 35.26  ? 65   SER A N   1 
ATOM   512  C  CA  . SER A 1 65  ? -24.374 -12.986 -9.233  1.00 36.47  ? 65   SER A CA  1 
ATOM   513  C  C   . SER A 1 65  ? -24.134 -14.418 -9.676  1.00 38.87  ? 65   SER A C   1 
ATOM   514  O  O   . SER A 1 65  ? -25.072 -15.074 -10.129 1.00 39.85  ? 65   SER A O   1 
ATOM   515  C  CB  . SER A 1 65  ? -24.429 -12.057 -10.460 1.00 36.79  ? 65   SER A CB  1 
ATOM   516  O  OG  . SER A 1 65  ? -23.319 -12.264 -11.321 1.00 37.16  ? 65   SER A OG  1 
ATOM   517  N  N   . ARG A 1 66  ? -22.906 -14.921 -9.544  1.00 33.23  ? 66   ARG A N   1 
ATOM   518  C  CA  . ARG A 1 66  ? -22.543 -16.260 -9.999  1.00 35.65  ? 66   ARG A CA  1 
ATOM   519  C  C   . ARG A 1 66  ? -22.342 -17.267 -8.873  1.00 37.34  ? 66   ARG A C   1 
ATOM   520  O  O   . ARG A 1 66  ? -22.575 -18.462 -9.089  1.00 35.78  ? 66   ARG A O   1 
ATOM   521  C  CB  . ARG A 1 66  ? -21.250 -16.205 -10.838 1.00 36.09  ? 66   ARG A CB  1 
ATOM   522  C  CG  . ARG A 1 66  ? -21.358 -15.407 -12.151 1.00 45.32  ? 66   ARG A CG  1 
ATOM   523  C  CD  . ARG A 1 66  ? -19.975 -15.022 -12.721 1.00 41.29  ? 66   ARG A CD  1 
ATOM   524  N  NE  . ARG A 1 66  ? -19.265 -16.172 -13.262 1.00 44.04  ? 66   ARG A NE  1 
ATOM   525  C  CZ  . ARG A 1 66  ? -17.980 -16.184 -13.589 1.00 46.47  ? 66   ARG A CZ  1 
ATOM   526  N  NH1 . ARG A 1 66  ? -17.213 -15.114 -13.435 1.00 45.85  ? 66   ARG A NH1 1 
ATOM   527  N  NH2 . ARG A 1 66  ? -17.446 -17.299 -14.081 1.00 49.10  ? 66   ARG A NH2 1 
ATOM   528  N  N   . PHE A 1 67  ? -21.899 -16.821 -7.693  1.00 36.98  ? 67   PHE A N   1 
ATOM   529  C  CA  . PHE A 1 67  ? -21.554 -17.703 -6.586  1.00 32.84  ? 67   PHE A CA  1 
ATOM   530  C  C   . PHE A 1 67  ? -22.104 -17.144 -5.284  1.00 32.18  ? 67   PHE A C   1 
ATOM   531  O  O   . PHE A 1 67  ? -22.057 -15.935 -5.052  1.00 31.43  ? 67   PHE A O   1 
ATOM   532  C  CB  . PHE A 1 67  ? -20.033 -17.883 -6.463  1.00 33.36  ? 67   PHE A CB  1 
ATOM   533  C  CG  . PHE A 1 67  ? -19.394 -18.437 -7.708  1.00 38.76  ? 67   PHE A CG  1 
ATOM   534  C  CD1 . PHE A 1 67  ? -19.284 -19.807 -7.896  1.00 37.03  ? 67   PHE A CD1 1 
ATOM   535  C  CD2 . PHE A 1 67  ? -18.908 -17.588 -8.693  1.00 36.54  ? 67   PHE A CD2 1 
ATOM   536  C  CE1 . PHE A 1 67  ? -18.707 -20.320 -9.052  1.00 38.35  ? 67   PHE A CE1 1 
ATOM   537  C  CE2 . PHE A 1 67  ? -18.333 -18.097 -9.851  1.00 39.91  ? 67   PHE A CE2 1 
ATOM   538  C  CZ  . PHE A 1 67  ? -18.226 -19.461 -10.027 1.00 41.09  ? 67   PHE A CZ  1 
ATOM   539  N  N   . ASP A 1 68  ? -22.611 -18.036 -4.441  1.00 32.50  ? 68   ASP A N   1 
ATOM   540  C  CA  . ASP A 1 68  ? -23.166 -17.711 -3.134  1.00 33.98  ? 68   ASP A CA  1 
ATOM   541  C  C   . ASP A 1 68  ? -22.335 -18.431 -2.078  1.00 36.86  ? 68   ASP A C   1 
ATOM   542  O  O   . ASP A 1 68  ? -21.604 -19.375 -2.387  1.00 31.59  ? 68   ASP A O   1 
ATOM   543  C  CB  . ASP A 1 68  ? -24.642 -18.144 -3.064  1.00 34.48  ? 68   ASP A CB  1 
ATOM   544  C  CG  . ASP A 1 68  ? -25.319 -17.787 -1.745  1.00 35.95  ? 68   ASP A CG  1 
ATOM   545  O  OD1 . ASP A 1 68  ? -24.894 -16.821 -1.070  1.00 35.10  ? 68   ASP A OD1 1 
ATOM   546  O  OD2 . ASP A 1 68  ? -26.307 -18.473 -1.408  1.00 32.86  ? 68   ASP A OD2 1 
ATOM   547  N  N   . LYS A 1 69  ? -22.454 -17.988 -0.824  1.00 34.16  ? 69   LYS A N   1 
ATOM   548  C  CA  . LYS A 1 69  ? -21.747 -18.664 0.259   1.00 34.49  ? 69   LYS A CA  1 
ATOM   549  C  C   . LYS A 1 69  ? -22.226 -20.105 0.396   1.00 32.79  ? 69   LYS A C   1 
ATOM   550  O  O   . LYS A 1 69  ? -23.430 -20.386 0.414   1.00 34.21  ? 69   LYS A O   1 
ATOM   551  C  CB  . LYS A 1 69  ? -21.947 -17.940 1.596   1.00 30.64  ? 69   LYS A CB  1 
ATOM   552  C  CG  . LYS A 1 69  ? -21.542 -18.806 2.813   1.00 31.64  ? 69   LYS A CG  1 
ATOM   553  C  CD  . LYS A 1 69  ? -21.280 -17.949 4.079   1.00 31.28  ? 69   LYS A CD  1 
ATOM   554  C  CE  . LYS A 1 69  ? -21.077 -18.813 5.330   1.00 30.42  ? 69   LYS A CE  1 
ATOM   555  N  NZ  . LYS A 1 69  ? -20.338 -18.129 6.430   1.00 30.85  ? 69   LYS A NZ  1 
ATOM   556  N  N   . ASN A 1 70  ? -21.275 -21.008 0.533   1.00 29.68  ? 70   ASN A N   1 
ATOM   557  C  CA  . ASN A 1 70  ? -21.532 -22.413 0.799   1.00 31.83  ? 70   ASN A CA  1 
ATOM   558  C  C   . ASN A 1 70  ? -21.094 -22.757 2.215   1.00 32.90  ? 70   ASN A C   1 
ATOM   559  O  O   . ASN A 1 70  ? -20.160 -22.154 2.746   1.00 33.02  ? 70   ASN A O   1 
ATOM   560  C  CB  . ASN A 1 70  ? -20.765 -23.285 -0.205  1.00 33.08  ? 70   ASN A CB  1 
ATOM   561  C  CG  . ASN A 1 70  ? -21.016 -24.759 0.001   1.00 36.47  ? 70   ASN A CG  1 
ATOM   562  O  OD1 . ASN A 1 70  ? -22.158 -25.200 -0.034  1.00 37.26  ? 70   ASN A OD1 1 
ATOM   563  N  ND2 . ASN A 1 70  ? -19.951 -25.526 0.223   1.00 38.07  ? 70   ASN A ND2 1 
ATOM   564  N  N   . LEU A 1 71  ? -21.774 -23.723 2.841   1.00 31.50  ? 71   LEU A N   1 
ATOM   565  C  CA  . LEU A 1 71  ? -21.282 -24.274 4.104   1.00 32.97  ? 71   LEU A CA  1 
ATOM   566  C  C   . LEU A 1 71  ? -20.268 -25.363 3.784   1.00 34.61  ? 71   LEU A C   1 
ATOM   567  O  O   . LEU A 1 71  ? -20.620 -26.415 3.241   1.00 35.41  ? 71   LEU A O   1 
ATOM   568  C  CB  . LEU A 1 71  ? -22.413 -24.802 4.980   1.00 33.52  ? 71   LEU A CB  1 
ATOM   569  C  CG  . LEU A 1 71  ? -23.463 -23.765 5.362   1.00 32.32  ? 71   LEU A CG  1 
ATOM   570  C  CD1 . LEU A 1 71  ? -24.389 -24.323 6.423   1.00 35.94  ? 71   LEU A CD1 1 
ATOM   571  C  CD2 . LEU A 1 71  ? -22.809 -22.434 5.853   1.00 33.24  ? 71   LEU A CD2 1 
ATOM   572  N  N   . SER A 1 72  ? -19.003 -25.096 4.089   1.00 32.73  ? 72   SER A N   1 
ATOM   573  C  CA  . SER A 1 72  ? -17.998 -26.147 4.048   1.00 36.44  ? 72   SER A CA  1 
ATOM   574  C  C   . SER A 1 72  ? -18.365 -27.241 5.051   1.00 35.73  ? 72   SER A C   1 
ATOM   575  O  O   . SER A 1 72  ? -19.223 -27.065 5.924   1.00 34.45  ? 72   SER A O   1 
ATOM   576  C  CB  . SER A 1 72  ? -16.620 -25.576 4.369   1.00 31.20  ? 72   SER A CB  1 
ATOM   577  O  OG  . SER A 1 72  ? -16.614 -24.993 5.673   1.00 33.93  ? 72   SER A OG  1 
ATOM   578  N  N   . GLN A 1 73  ? -17.706 -28.390 4.927   1.00 36.29  ? 73   GLN A N   1 
ATOM   579  C  CA  . GLN A 1 73  ? -17.900 -29.426 5.935   1.00 37.06  ? 73   GLN A CA  1 
ATOM   580  C  C   . GLN A 1 73  ? -17.604 -28.881 7.327   1.00 33.55  ? 73   GLN A C   1 
ATOM   581  O  O   . GLN A 1 73  ? -18.346 -29.146 8.282   1.00 35.53  ? 73   GLN A O   1 
ATOM   582  C  CB  . GLN A 1 73  ? -17.021 -30.644 5.633   1.00 37.95  ? 73   GLN A CB  1 
ATOM   583  C  CG  . GLN A 1 73  ? -17.534 -31.887 6.337   1.00 44.54  ? 73   GLN A CG  1 
ATOM   584  C  CD  . GLN A 1 73  ? -18.972 -32.172 5.967   1.00 49.53  ? 73   GLN A CD  1 
ATOM   585  O  OE1 . GLN A 1 73  ? -19.328 -32.177 4.792   1.00 46.19  ? 73   GLN A OE1 1 
ATOM   586  N  NE2 . GLN A 1 73  ? -19.825 -32.330 6.980   1.00 49.86  ? 73   GLN A NE2 1 
ATOM   587  N  N   . ALA A 1 74  ? -16.519 -28.123 7.459   1.00 32.96  ? 74   ALA A N   1 
ATOM   588  C  CA  . ALA A 1 74  ? -16.192 -27.513 8.743   1.00 33.56  ? 74   ALA A CA  1 
ATOM   589  C  C   . ALA A 1 74  ? -17.374 -26.730 9.304   1.00 33.73  ? 74   ALA A C   1 
ATOM   590  O  O   . ALA A 1 74  ? -17.711 -26.857 10.485  1.00 36.66  ? 74   ALA A O   1 
ATOM   591  C  CB  . ALA A 1 74  ? -14.972 -26.605 8.594   1.00 33.84  ? 74   ALA A CB  1 
ATOM   592  N  N   . LEU A 1 75  ? -18.001 -25.892 8.481   1.00 34.87  ? 75   LEU A N   1 
ATOM   593  C  CA  . LEU A 1 75  ? -19.126 -25.099 8.976   1.00 32.02  ? 75   LEU A CA  1 
ATOM   594  C  C   . LEU A 1 75  ? -20.359 -25.956 9.227   1.00 34.10  ? 75   LEU A C   1 
ATOM   595  O  O   . LEU A 1 75  ? -21.143 -25.650 10.128  1.00 33.75  ? 75   LEU A O   1 
ATOM   596  C  CB  . LEU A 1 75  ? -19.456 -23.967 8.001   1.00 32.00  ? 75   LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 75  ? -18.423 -22.834 7.858   1.00 32.84  ? 75   LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 75  ? -19.022 -21.652 7.097   1.00 33.23  ? 75   LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 75  ? -17.928 -22.386 9.229   1.00 32.85  ? 75   LEU A CD2 1 
ATOM   600  N  N   . LYS A 1 76  ? -20.570 -27.019 8.445   1.00 33.95  ? 76   LYS A N   1 
ATOM   601  C  CA  . LYS A 1 76  ? -21.667 -27.930 8.777   1.00 34.70  ? 76   LYS A CA  1 
ATOM   602  C  C   . LYS A 1 76  ? -21.475 -28.556 10.158  1.00 34.50  ? 76   LYS A C   1 
ATOM   603  O  O   . LYS A 1 76  ? -22.446 -28.743 10.904  1.00 35.90  ? 76   LYS A O   1 
ATOM   604  C  CB  . LYS A 1 76  ? -21.800 -29.007 7.704   1.00 35.35  ? 76   LYS A CB  1 
ATOM   605  C  CG  . LYS A 1 76  ? -22.266 -28.410 6.378   1.00 37.53  ? 76   LYS A CG  1 
ATOM   606  C  CD  . LYS A 1 76  ? -22.511 -29.447 5.317   1.00 42.82  ? 76   LYS A CD  1 
ATOM   607  C  CE  . LYS A 1 76  ? -22.855 -28.750 3.998   1.00 45.72  ? 76   LYS A CE  1 
ATOM   608  N  NZ  . LYS A 1 76  ? -23.057 -29.722 2.900   1.00 55.83  ? 76   LYS A NZ  1 
ATOM   609  N  N   . PHE A 1 77  ? -20.231 -28.883 10.518  1.00 34.92  ? 77   PHE A N   1 
ATOM   610  C  CA  . PHE A 1 77  ? -19.984 -29.452 11.839  1.00 35.76  ? 77   PHE A CA  1 
ATOM   611  C  C   . PHE A 1 77  ? -20.164 -28.401 12.930  1.00 36.00  ? 77   PHE A C   1 
ATOM   612  O  O   . PHE A 1 77  ? -20.755 -28.682 13.979  1.00 39.31  ? 77   PHE A O   1 
ATOM   613  C  CB  . PHE A 1 77  ? -18.577 -30.055 11.909  1.00 38.79  ? 77   PHE A CB  1 
ATOM   614  C  CG  . PHE A 1 77  ? -18.364 -31.249 11.017  1.00 42.45  ? 77   PHE A CG  1 
ATOM   615  C  CD1 . PHE A 1 77  ? -19.423 -32.031 10.609  1.00 43.06  ? 77   PHE A CD1 1 
ATOM   616  C  CD2 . PHE A 1 77  ? -17.082 -31.604 10.608  1.00 39.69  ? 77   PHE A CD2 1 
ATOM   617  C  CE1 . PHE A 1 77  ? -19.215 -33.135 9.784   1.00 47.47  ? 77   PHE A CE1 1 
ATOM   618  C  CE2 . PHE A 1 77  ? -16.868 -32.701 9.789   1.00 43.84  ? 77   PHE A CE2 1 
ATOM   619  C  CZ  . PHE A 1 77  ? -17.938 -33.468 9.376   1.00 44.01  ? 77   PHE A CZ  1 
ATOM   620  N  N   . VAL A 1 78  ? -19.663 -27.186 12.699  1.00 35.86  ? 78   VAL A N   1 
ATOM   621  C  CA  . VAL A 1 78  ? -19.801 -26.125 13.693  1.00 34.41  ? 78   VAL A CA  1 
ATOM   622  C  C   . VAL A 1 78  ? -21.265 -25.751 13.864  1.00 33.93  ? 78   VAL A C   1 
ATOM   623  O  O   . VAL A 1 78  ? -21.680 -25.302 14.940  1.00 35.94  ? 78   VAL A O   1 
ATOM   624  C  CB  . VAL A 1 78  ? -18.933 -24.926 13.275  1.00 37.98  ? 78   VAL A CB  1 
ATOM   625  C  CG1 . VAL A 1 78  ? -19.440 -23.648 13.912  1.00 46.30  ? 78   VAL A CG1 1 
ATOM   626  C  CG2 . VAL A 1 78  ? -17.476 -25.208 13.646  1.00 41.56  ? 78   VAL A CG2 1 
ATOM   627  N  N   . ARG A 1 79  ? -22.062 -25.913 12.805  1.00 32.66  ? 79   ARG A N   1 
ATOM   628  C  CA  . ARG A 1 79  ? -23.491 -25.656 12.900  1.00 34.06  ? 79   ARG A CA  1 
ATOM   629  C  C   . ARG A 1 79  ? -24.161 -26.540 13.943  1.00 35.41  ? 79   ARG A C   1 
ATOM   630  O  O   . ARG A 1 79  ? -25.251 -26.199 14.415  1.00 34.51  ? 79   ARG A O   1 
ATOM   631  C  CB  . ARG A 1 79  ? -24.154 -25.857 11.533  1.00 35.45  ? 79   ARG A CB  1 
ATOM   632  C  CG  . ARG A 1 79  ? -25.660 -25.612 11.524  1.00 37.99  ? 79   ARG A CG  1 
ATOM   633  C  CD  . ARG A 1 79  ? -26.177 -25.292 10.132  1.00 34.70  ? 79   ARG A CD  1 
ATOM   634  N  NE  . ARG A 1 79  ? -27.639 -25.237 10.104  1.00 39.00  ? 79   ARG A NE  1 
ATOM   635  C  CZ  . ARG A 1 79  ? -28.362 -24.353 9.423   1.00 42.83  ? 79   ARG A CZ  1 
ATOM   636  N  NH1 . ARG A 1 79  ? -27.792 -23.427 8.665   1.00 35.73  ? 79   ARG A NH1 1 
ATOM   637  N  NH2 . ARG A 1 79  ? -29.692 -24.385 9.524   1.00 39.71  ? 79   ARG A NH2 1 
ATOM   638  N  N   . ASP A 1 80  ? -23.550 -27.670 14.306  1.00 35.29  ? 80   ASP A N   1 
ATOM   639  C  CA  . ASP A 1 80  ? -24.119 -28.482 15.383  1.00 38.48  ? 80   ASP A CA  1 
ATOM   640  C  C   . ASP A 1 80  ? -24.289 -27.682 16.671  1.00 38.77  ? 80   ASP A C   1 
ATOM   641  O  O   . ASP A 1 80  ? -25.198 -27.973 17.458  1.00 40.47  ? 80   ASP A O   1 
ATOM   642  C  CB  . ASP A 1 80  ? -23.264 -29.725 15.642  1.00 37.09  ? 80   ASP A CB  1 
ATOM   643  C  CG  . ASP A 1 80  ? -23.459 -30.794 14.583  1.00 43.81  ? 80   ASP A CG  1 
ATOM   644  O  OD1 . ASP A 1 80  ? -24.453 -30.722 13.839  1.00 39.96  ? 80   ASP A OD1 1 
ATOM   645  O  OD2 . ASP A 1 80  ? -22.624 -31.714 14.507  1.00 49.73  ? 80   ASP A OD2 1 
ATOM   646  N  N   . PHE A 1 81  ? -23.452 -26.667 16.912  1.00 35.13  ? 81   PHE A N   1 
ATOM   647  C  CA  . PHE A 1 81  ? -23.694 -25.796 18.053  1.00 37.93  ? 81   PHE A CA  1 
ATOM   648  C  C   . PHE A 1 81  ? -24.012 -24.349 17.693  1.00 35.27  ? 81   PHE A C   1 
ATOM   649  O  O   . PHE A 1 81  ? -24.626 -23.662 18.512  1.00 36.20  ? 81   PHE A O   1 
ATOM   650  C  CB  . PHE A 1 81  ? -22.520 -25.828 19.062  1.00 35.19  ? 81   PHE A CB  1 
ATOM   651  C  CG  . PHE A 1 81  ? -21.149 -25.575 18.469  1.00 36.22  ? 81   PHE A CG  1 
ATOM   652  C  CD1 . PHE A 1 81  ? -20.645 -24.281 18.379  1.00 36.85  ? 81   PHE A CD1 1 
ATOM   653  C  CD2 . PHE A 1 81  ? -20.341 -26.633 18.065  1.00 39.70  ? 81   PHE A CD2 1 
ATOM   654  C  CE1 . PHE A 1 81  ? -19.370 -24.039 17.860  1.00 34.45  ? 81   PHE A CE1 1 
ATOM   655  C  CE2 . PHE A 1 81  ? -19.071 -26.404 17.545  1.00 39.34  ? 81   PHE A CE2 1 
ATOM   656  C  CZ  . PHE A 1 81  ? -18.581 -25.110 17.442  1.00 36.56  ? 81   PHE A CZ  1 
ATOM   657  N  N   . ALA A 1 82  ? -23.659 -23.875 16.497  1.00 34.86  ? 82   ALA A N   1 
ATOM   658  C  CA  . ALA A 1 82  ? -23.962 -22.498 16.113  1.00 33.16  ? 82   ALA A CA  1 
ATOM   659  C  C   . ALA A 1 82  ? -25.237 -22.364 15.285  1.00 32.95  ? 82   ALA A C   1 
ATOM   660  O  O   . ALA A 1 82  ? -25.628 -21.242 14.969  1.00 32.68  ? 82   ALA A O   1 
ATOM   661  C  CB  . ALA A 1 82  ? -22.778 -21.891 15.348  1.00 35.13  ? 82   ALA A CB  1 
ATOM   662  N  N   . GLY A 1 83  ? -25.883 -23.475 14.921  1.00 35.12  ? 83   GLY A N   1 
ATOM   663  C  CA  . GLY A 1 83  ? -27.208 -23.433 14.323  1.00 35.90  ? 83   GLY A CA  1 
ATOM   664  C  C   . GLY A 1 83  ? -27.304 -22.556 13.091  1.00 36.57  ? 83   GLY A C   1 
ATOM   665  O  O   . GLY A 1 83  ? -26.419 -22.549 12.225  1.00 35.20  ? 83   GLY A O   1 
ATOM   666  N  N   . ASP A 1 84  ? -28.420 -21.829 12.979  1.00 32.69  ? 84   ASP A N   1 
ATOM   667  C  CA  . ASP A 1 84  ? -28.583 -20.840 11.919  1.00 34.46  ? 84   ASP A CA  1 
ATOM   668  C  C   . ASP A 1 84  ? -28.256 -19.432 12.406  1.00 32.05  ? 84   ASP A C   1 
ATOM   669  O  O   . ASP A 1 84  ? -28.872 -18.466 11.969  1.00 32.84  ? 84   ASP A O   1 
ATOM   670  C  CB  . ASP A 1 84  ? -29.988 -20.904 11.292  1.00 36.04  ? 84   ASP A CB  1 
ATOM   671  C  CG  . ASP A 1 84  ? -31.114 -20.696 12.300  1.00 37.90  ? 84   ASP A CG  1 
ATOM   672  O  OD1 . ASP A 1 84  ? -30.847 -20.693 13.510  1.00 35.97  ? 84   ASP A OD1 1 
ATOM   673  O  OD2 . ASP A 1 84  ? -32.282 -20.544 11.873  1.00 37.53  ? 84   ASP A OD2 1 
ATOM   674  N  N   . GLY A 1 85  ? -27.285 -19.298 13.313  1.00 31.44  ? 85   GLY A N   1 
ATOM   675  C  CA  . GLY A 1 85  ? -26.635 -18.015 13.513  1.00 32.56  ? 85   GLY A CA  1 
ATOM   676  C  C   . GLY A 1 85  ? -26.014 -17.500 12.217  1.00 33.88  ? 85   GLY A C   1 
ATOM   677  O  O   . GLY A 1 85  ? -25.989 -18.173 11.180  1.00 32.62  ? 85   GLY A O   1 
ATOM   678  N  N   . LEU A 1 86  ? -25.504 -16.261 12.272  1.00 30.08  ? 86   LEU A N   1 
ATOM   679  C  CA  . LEU A 1 86  ? -25.111 -15.590 11.030  1.00 30.01  ? 86   LEU A CA  1 
ATOM   680  C  C   . LEU A 1 86  ? -23.982 -16.324 10.309  1.00 29.39  ? 86   LEU A C   1 
ATOM   681  O  O   . LEU A 1 86  ? -23.930 -16.316 9.073   1.00 31.82  ? 86   LEU A O   1 
ATOM   682  C  CB  . LEU A 1 86  ? -24.703 -14.132 11.297  1.00 32.32  ? 86   LEU A CB  1 
ATOM   683  C  CG  . LEU A 1 86  ? -25.860 -13.135 11.476  1.00 31.40  ? 86   LEU A CG  1 
ATOM   684  C  CD1 . LEU A 1 86  ? -25.330 -11.796 11.955  1.00 36.45  ? 86   LEU A CD1 1 
ATOM   685  C  CD2 . LEU A 1 86  ? -26.618 -12.951 10.178  1.00 29.83  ? 86   LEU A CD2 1 
ATOM   686  N  N   . PHE A 1 87  ? -23.038 -16.918 11.058  1.00 31.24  ? 87   PHE A N   1 
ATOM   687  C  CA  . PHE A 1 87  ? -21.842 -17.500 10.434  1.00 30.32  ? 87   PHE A CA  1 
ATOM   688  C  C   . PHE A 1 87  ? -22.168 -18.803 9.709   1.00 33.21  ? 87   PHE A C   1 
ATOM   689  O  O   . PHE A 1 87  ? -21.520 -19.145 8.714   1.00 31.89  ? 87   PHE A O   1 
ATOM   690  C  CB  . PHE A 1 87  ? -20.752 -17.746 11.495  1.00 29.38  ? 87   PHE A CB  1 
ATOM   691  C  CG  . PHE A 1 87  ? -19.328 -17.635 10.977  1.00 32.00  ? 87   PHE A CG  1 
ATOM   692  C  CD1 . PHE A 1 87  ? -18.762 -18.645 10.196  1.00 29.53  ? 87   PHE A CD1 1 
ATOM   693  C  CD2 . PHE A 1 87  ? -18.550 -16.534 11.311  1.00 30.33  ? 87   PHE A CD2 1 
ATOM   694  C  CE1 . PHE A 1 87  ? -17.447 -18.532 9.728   1.00 33.02  ? 87   PHE A CE1 1 
ATOM   695  C  CE2 . PHE A 1 87  ? -17.229 -16.417 10.851  1.00 33.76  ? 87   PHE A CE2 1 
ATOM   696  C  CZ  . PHE A 1 87  ? -16.691 -17.422 10.054  1.00 32.80  ? 87   PHE A CZ  1 
ATOM   697  N  N   . THR A 1 88  ? -23.163 -19.542 10.182  1.00 31.35  ? 88   THR A N   1 
ATOM   698  C  CA  . THR A 1 88  ? -23.407 -20.884 9.669   1.00 31.33  ? 88   THR A CA  1 
ATOM   699  C  C   . THR A 1 88  ? -24.780 -21.022 9.014   1.00 34.59  ? 88   THR A C   1 
ATOM   700  O  O   . THR A 1 88  ? -25.241 -22.141 8.783   1.00 34.71  ? 88   THR A O   1 
ATOM   701  C  CB  . THR A 1 88  ? -23.236 -21.916 10.787  1.00 34.53  ? 88   THR A CB  1 
ATOM   702  O  OG1 . THR A 1 88  ? -23.996 -21.517 11.938  1.00 33.79  ? 88   THR A OG1 1 
ATOM   703  C  CG2 . THR A 1 88  ? -21.775 -22.022 11.169  1.00 33.50  ? 88   THR A CG2 1 
ATOM   704  N  N   . SER A 1 89  ? -25.432 -19.917 8.688   1.00 32.52  ? 89   SER A N   1 
ATOM   705  C  CA  . SER A 1 89  ? -26.696 -19.989 7.979   1.00 33.30  ? 89   SER A CA  1 
ATOM   706  C  C   . SER A 1 89  ? -26.468 -19.857 6.472   1.00 35.38  ? 89   SER A C   1 
ATOM   707  O  O   . SER A 1 89  ? -25.481 -19.267 6.017   1.00 30.75  ? 89   SER A O   1 
ATOM   708  C  CB  . SER A 1 89  ? -27.649 -18.916 8.500   1.00 37.24  ? 89   SER A CB  1 
ATOM   709  O  OG  . SER A 1 89  ? -27.065 -17.628 8.432   1.00 39.40  ? 89   SER A OG  1 
ATOM   710  N  N   . TRP A 1 90  ? -27.358 -20.473 5.696   1.00 33.42  ? 90   TRP A N   1 
ATOM   711  C  CA  . TRP A 1 90  ? -27.353 -20.244 4.260   1.00 37.12  ? 90   TRP A CA  1 
ATOM   712  C  C   . TRP A 1 90  ? -27.979 -18.890 3.962   1.00 33.97  ? 90   TRP A C   1 
ATOM   713  O  O   . TRP A 1 90  ? -28.876 -18.430 4.670   1.00 33.88  ? 90   TRP A O   1 
ATOM   714  C  CB  . TRP A 1 90  ? -28.141 -21.328 3.513   1.00 36.42  ? 90   TRP A CB  1 
ATOM   715  C  CG  . TRP A 1 90  ? -27.645 -22.712 3.752   1.00 35.82  ? 90   TRP A CG  1 
ATOM   716  C  CD1 . TRP A 1 90  ? -28.060 -23.569 4.728   1.00 33.17  ? 90   TRP A CD1 1 
ATOM   717  C  CD2 . TRP A 1 90  ? -26.662 -23.413 2.988   1.00 33.87  ? 90   TRP A CD2 1 
ATOM   718  N  NE1 . TRP A 1 90  ? -27.389 -24.770 4.624   1.00 34.19  ? 90   TRP A NE1 1 
ATOM   719  C  CE2 . TRP A 1 90  ? -26.527 -24.700 3.561   1.00 33.04  ? 90   TRP A CE2 1 
ATOM   720  C  CE3 . TRP A 1 90  ? -25.893 -23.088 1.864   1.00 32.05  ? 90   TRP A CE3 1 
ATOM   721  C  CZ2 . TRP A 1 90  ? -25.642 -25.654 3.057   1.00 40.12  ? 90   TRP A CZ2 1 
ATOM   722  C  CZ3 . TRP A 1 90  ? -25.000 -24.036 1.371   1.00 37.08  ? 90   TRP A CZ3 1 
ATOM   723  C  CH2 . TRP A 1 90  ? -24.883 -25.306 1.973   1.00 35.53  ? 90   TRP A CH2 1 
ATOM   724  N  N   . THR A 1 91  ? -27.532 -18.277 2.868   1.00 33.61  ? 91   THR A N   1 
ATOM   725  C  CA  . THR A 1 91  ? -28.037 -16.957 2.523   1.00 33.94  ? 91   THR A CA  1 
ATOM   726  C  C   . THR A 1 91  ? -29.546 -16.981 2.340   1.00 33.09  ? 91   THR A C   1 
ATOM   727  O  O   . THR A 1 91  ? -30.213 -15.979 2.599   1.00 33.22  ? 91   THR A O   1 
ATOM   728  C  CB  . THR A 1 91  ? -27.325 -16.445 1.267   1.00 31.48  ? 91   THR A CB  1 
ATOM   729  O  OG1 . THR A 1 91  ? -25.897 -16.549 1.446   1.00 31.57  ? 91   THR A OG1 1 
ATOM   730  C  CG2 . THR A 1 91  ? -27.703 -15.006 0.949   1.00 35.31  ? 91   THR A CG2 1 
ATOM   731  N  N   . HIS A 1 92  ? -30.101 -18.117 1.907   1.00 34.82  ? 92   HIS A N   1 
ATOM   732  C  CA  . HIS A 1 92  ? -31.522 -18.213 1.593   1.00 34.83  ? 92   HIS A CA  1 
ATOM   733  C  C   . HIS A 1 92  ? -32.380 -18.617 2.787   1.00 37.70  ? 92   HIS A C   1 
ATOM   734  O  O   . HIS A 1 92  ? -33.612 -18.647 2.662   1.00 36.52  ? 92   HIS A O   1 
ATOM   735  C  CB  . HIS A 1 92  ? -31.740 -19.199 0.434   1.00 36.27  ? 92   HIS A CB  1 
ATOM   736  C  CG  . HIS A 1 92  ? -31.064 -20.521 0.634   1.00 36.75  ? 92   HIS A CG  1 
ATOM   737  N  ND1 . HIS A 1 92  ? -31.540 -21.479 1.507   1.00 37.67  ? 92   HIS A ND1 1 
ATOM   738  C  CD2 . HIS A 1 92  ? -29.936 -21.035 0.087   1.00 36.75  ? 92   HIS A CD2 1 
ATOM   739  C  CE1 . HIS A 1 92  ? -30.740 -22.532 1.474   1.00 36.61  ? 92   HIS A CE1 1 
ATOM   740  N  NE2 . HIS A 1 92  ? -29.758 -22.285 0.628   1.00 36.50  ? 92   HIS A NE2 1 
ATOM   741  N  N   . GLU A 1 93  ? -31.777 -18.919 3.937   1.00 33.33  ? 93   GLU A N   1 
ATOM   742  C  CA  . GLU A 1 93  ? -32.570 -19.155 5.138   1.00 33.80  ? 93   GLU A CA  1 
ATOM   743  C  C   . GLU A 1 93  ? -33.108 -17.834 5.661   1.00 35.86  ? 93   GLU A C   1 
ATOM   744  O  O   . GLU A 1 93  ? -32.376 -16.840 5.734   1.00 36.00  ? 93   GLU A O   1 
ATOM   745  C  CB  . GLU A 1 93  ? -31.738 -19.840 6.222   1.00 34.10  ? 93   GLU A CB  1 
ATOM   746  C  CG  . GLU A 1 93  ? -31.443 -21.323 5.952   1.00 34.44  ? 93   GLU A CG  1 
ATOM   747  C  CD  . GLU A 1 93  ? -30.585 -21.948 7.048   1.00 37.67  ? 93   GLU A CD  1 
ATOM   748  O  OE1 . GLU A 1 93  ? -29.348 -21.735 7.052   1.00 35.81  ? 93   GLU A OE1 1 
ATOM   749  O  OE2 . GLU A 1 93  ? -31.154 -22.654 7.909   1.00 40.12  ? 93   GLU A OE2 1 
ATOM   750  N  N   . LYS A 1 94  ? -34.400 -17.819 6.000   1.00 37.00  ? 94   LYS A N   1 
ATOM   751  C  CA  . LYS A 1 94  ? -35.028 -16.600 6.499   1.00 34.67  ? 94   LYS A CA  1 
ATOM   752  C  C   . LYS A 1 94  ? -34.167 -15.930 7.567   1.00 35.45  ? 94   LYS A C   1 
ATOM   753  O  O   . LYS A 1 94  ? -33.985 -14.708 7.555   1.00 35.84  ? 94   LYS A O   1 
ATOM   754  C  CB  . LYS A 1 94  ? -36.415 -16.918 7.064   1.00 40.24  ? 94   LYS A CB  1 
ATOM   755  C  CG  . LYS A 1 94  ? -37.090 -15.740 7.753   1.00 38.97  ? 94   LYS A CG  1 
ATOM   756  C  CD  . LYS A 1 94  ? -38.443 -16.134 8.364   1.00 41.07  ? 94   LYS A CD  1 
ATOM   757  C  CE  . LYS A 1 94  ? -39.031 -14.998 9.166   1.00 48.66  ? 94   LYS A CE  1 
ATOM   758  N  NZ  . LYS A 1 94  ? -40.294 -15.395 9.848   1.00 56.27  ? 94   LYS A NZ  1 
ATOM   759  N  N   . ASN A 1 95  ? -33.606 -16.720 8.479   1.00 33.12  ? 95   ASN A N   1 
ATOM   760  C  CA  . ASN A 1 95  ? -32.908 -16.135 9.614   1.00 35.49  ? 95   ASN A CA  1 
ATOM   761  C  C   . ASN A 1 95  ? -31.581 -15.479 9.239   1.00 34.62  ? 95   ASN A C   1 
ATOM   762  O  O   . ASN A 1 95  ? -31.056 -14.708 10.052  1.00 33.77  ? 95   ASN A O   1 
ATOM   763  C  CB  . ASN A 1 95  ? -32.691 -17.192 10.695  1.00 35.00  ? 95   ASN A CB  1 
ATOM   764  C  CG  . ASN A 1 95  ? -33.895 -17.319 11.616  1.00 37.84  ? 95   ASN A CG  1 
ATOM   765  O  OD1 . ASN A 1 95  ? -34.675 -16.378 11.739  1.00 41.24  ? 95   ASN A OD1 1 
ATOM   766  N  ND2 . ASN A 1 95  ? -34.047 -18.470 12.262  1.00 39.65  ? 95   ASN A ND2 1 
ATOM   767  N  N   . TRP A 1 96  ? -31.041 -15.713 8.040   1.00 32.16  ? 96   TRP A N   1 
ATOM   768  C  CA  . TRP A 1 96  ? -29.821 -14.988 7.700   1.00 33.70  ? 96   TRP A CA  1 
ATOM   769  C  C   . TRP A 1 96  ? -30.110 -13.502 7.509   1.00 32.74  ? 96   TRP A C   1 
ATOM   770  O  O   . TRP A 1 96  ? -29.598 -12.660 8.254   1.00 32.65  ? 96   TRP A O   1 
ATOM   771  C  CB  . TRP A 1 96  ? -29.104 -15.552 6.462   1.00 33.05  ? 96   TRP A CB  1 
ATOM   772  C  CG  . TRP A 1 96  ? -27.935 -14.629 6.244   1.00 31.07  ? 96   TRP A CG  1 
ATOM   773  C  CD1 . TRP A 1 96  ? -26.825 -14.530 7.039   1.00 32.48  ? 96   TRP A CD1 1 
ATOM   774  C  CD2 . TRP A 1 96  ? -27.850 -13.554 5.300   1.00 34.69  ? 96   TRP A CD2 1 
ATOM   775  N  NE1 . TRP A 1 96  ? -26.024 -13.492 6.605   1.00 32.48  ? 96   TRP A NE1 1 
ATOM   776  C  CE2 . TRP A 1 96  ? -26.632 -12.873 5.545   1.00 32.08  ? 96   TRP A CE2 1 
ATOM   777  C  CE3 . TRP A 1 96  ? -28.672 -13.109 4.260   1.00 34.05  ? 96   TRP A CE3 1 
ATOM   778  C  CZ2 . TRP A 1 96  ? -26.210 -11.783 4.771   1.00 36.29  ? 96   TRP A CZ2 1 
ATOM   779  C  CZ3 . TRP A 1 96  ? -28.253 -12.014 3.488   1.00 36.11  ? 96   TRP A CZ3 1 
ATOM   780  C  CH2 . TRP A 1 96  ? -27.030 -11.369 3.749   1.00 37.41  ? 96   TRP A CH2 1 
ATOM   781  N  N   . LYS A 1 97  ? -30.937 -13.149 6.521   1.00 31.88  ? 97   LYS A N   1 
ATOM   782  C  CA  . LYS A 1 97  ? -31.154 -11.728 6.276   1.00 31.96  ? 97   LYS A CA  1 
ATOM   783  C  C   . LYS A 1 97  ? -31.840 -11.061 7.458   1.00 35.62  ? 97   LYS A C   1 
ATOM   784  O  O   . LYS A 1 97  ? -31.584 -9.892  7.743   1.00 32.70  ? 97   LYS A O   1 
ATOM   785  C  CB  . LYS A 1 97  ? -31.974 -11.521 5.002   1.00 38.20  ? 97   LYS A CB  1 
ATOM   786  C  CG  . LYS A 1 97  ? -32.181 -10.052 4.648   1.00 40.38  ? 97   LYS A CG  1 
ATOM   787  C  CD  . LYS A 1 97  ? -30.853 -9.366  4.330   1.00 43.61  ? 97   LYS A CD  1 
ATOM   788  C  CE  . LYS A 1 97  ? -31.077 -8.023  3.652   1.00 47.41  ? 97   LYS A CE  1 
ATOM   789  N  NZ  . LYS A 1 97  ? -29.786 -7.324  3.405   1.00 50.79  ? 97   LYS A NZ  1 
ATOM   790  N  N   . LYS A 1 98  ? -32.700 -11.787 8.170   1.00 32.79  ? 98   LYS A N   1 
ATOM   791  C  CA  . LYS A 1 98  ? -33.412 -11.175 9.286   1.00 33.35  ? 98   LYS A CA  1 
ATOM   792  C  C   . LYS A 1 98  ? -32.432 -10.773 10.388  1.00 35.27  ? 98   LYS A C   1 
ATOM   793  O  O   . LYS A 1 98  ? -32.453 -9.639  10.879  1.00 33.71  ? 98   LYS A O   1 
ATOM   794  C  CB  . LYS A 1 98  ? -34.475 -12.149 9.804   1.00 38.12  ? 98   LYS A CB  1 
ATOM   795  C  CG  . LYS A 1 98  ? -35.269 -11.674 11.016  1.00 38.40  ? 98   LYS A CG  1 
ATOM   796  C  CD  . LYS A 1 98  ? -36.205 -12.802 11.478  1.00 40.12  ? 98   LYS A CD  1 
ATOM   797  C  CE  . LYS A 1 98  ? -36.899 -12.478 12.795  1.00 42.88  ? 98   LYS A CE  1 
ATOM   798  N  NZ  . LYS A 1 98  ? -37.842 -13.593 13.135  1.00 44.54  ? 98   LYS A NZ  1 
ATOM   799  N  N   . ALA A 1 99  ? -31.526 -11.680 10.755  1.00 33.09  ? 99   ALA A N   1 
ATOM   800  C  CA  . ALA A 1 99  ? -30.554 -11.347 11.797  1.00 32.75  ? 99   ALA A CA  1 
ATOM   801  C  C   . ALA A 1 99  ? -29.523 -10.341 11.299  1.00 32.63  ? 99   ALA A C   1 
ATOM   802  O  O   . ALA A 1 99  ? -29.034 -9.515  12.078  1.00 33.10  ? 99   ALA A O   1 
ATOM   803  C  CB  . ALA A 1 99  ? -29.855 -12.614 12.293  1.00 32.96  ? 99   ALA A CB  1 
ATOM   804  N  N   . HIS A 1 100 ? -29.166 -10.405 10.014  1.00 32.03  ? 100  HIS A N   1 
ATOM   805  C  CA  . HIS A 1 100 ? -28.261 -9.408  9.456   1.00 33.68  ? 100  HIS A CA  1 
ATOM   806  C  C   . HIS A 1 100 ? -28.851 -8.010  9.594   1.00 34.97  ? 100  HIS A C   1 
ATOM   807  O  O   . HIS A 1 100 ? -28.185 -7.083  10.071  1.00 35.09  ? 100  HIS A O   1 
ATOM   808  C  CB  . HIS A 1 100 ? -27.973 -9.737  7.987   1.00 34.51  ? 100  HIS A CB  1 
ATOM   809  C  CG  . HIS A 1 100 ? -27.274 -8.640  7.247   1.00 38.67  ? 100  HIS A CG  1 
ATOM   810  N  ND1 . HIS A 1 100 ? -25.903 -8.505  7.241   1.00 43.82  ? 100  HIS A ND1 1 
ATOM   811  C  CD2 . HIS A 1 100 ? -27.756 -7.636  6.475   1.00 45.91  ? 100  HIS A CD2 1 
ATOM   812  C  CE1 . HIS A 1 100 ? -25.567 -7.467  6.495   1.00 42.94  ? 100  HIS A CE1 1 
ATOM   813  N  NE2 . HIS A 1 100 ? -26.674 -6.918  6.023   1.00 47.00  ? 100  HIS A NE2 1 
ATOM   814  N  N   . ASN A 1 101 ? -30.122 -7.843  9.200   1.00 34.06  ? 101  ASN A N   1 
ATOM   815  C  CA  . ASN A 1 101 ? -30.760 -6.532  9.323   1.00 34.55  ? 101  ASN A CA  1 
ATOM   816  C  C   . ASN A 1 101 ? -30.805 -6.075  10.774  1.00 33.64  ? 101  ASN A C   1 
ATOM   817  O  O   . ASN A 1 101 ? -30.604 -4.891  11.069  1.00 35.04  ? 101  ASN A O   1 
ATOM   818  C  CB  . ASN A 1 101 ? -32.181 -6.583  8.745   1.00 33.23  ? 101  ASN A CB  1 
ATOM   819  C  CG  . ASN A 1 101 ? -32.190 -6.629  7.226   1.00 37.15  ? 101  ASN A CG  1 
ATOM   820  O  OD1 . ASN A 1 101 ? -31.204 -6.276  6.580   1.00 36.79  ? 101  ASN A OD1 1 
ATOM   821  N  ND2 . ASN A 1 101 ? -33.311 -7.072  6.647   1.00 35.19  ? 101  ASN A ND2 1 
ATOM   822  N  N   . ILE A 1 102 ? -31.093 -7.000  11.691  1.00 33.39  ? 102  ILE A N   1 
ATOM   823  C  CA  . ILE A 1 102 ? -31.265 -6.645  13.098  1.00 35.25  ? 102  ILE A CA  1 
ATOM   824  C  C   . ILE A 1 102 ? -29.930 -6.328  13.748  1.00 35.47  ? 102  ILE A C   1 
ATOM   825  O  O   . ILE A 1 102 ? -29.852 -5.459  14.621  1.00 34.16  ? 102  ILE A O   1 
ATOM   826  C  CB  . ILE A 1 102 ? -31.992 -7.781  13.847  1.00 32.74  ? 102  ILE A CB  1 
ATOM   827  C  CG1 . ILE A 1 102 ? -33.464 -7.859  13.389  1.00 36.63  ? 102  ILE A CG1 1 
ATOM   828  C  CG2 . ILE A 1 102 ? -31.838 -7.634  15.366  1.00 38.53  ? 102  ILE A CG2 1 
ATOM   829  C  CD1 . ILE A 1 102 ? -34.204 -9.124  13.831  1.00 35.35  ? 102  ILE A CD1 1 
ATOM   830  N  N   . LEU A 1 103 ? -28.862 -7.000  13.339  1.00 33.76  ? 103  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 103 ? -27.594 -6.836  14.046  1.00 33.48  ? 103  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 103 ? -26.612 -5.897  13.355  1.00 33.11  ? 103  LEU A C   1 
ATOM   833  O  O   . LEU A 1 103 ? -25.662 -5.445  14.002  1.00 33.85  ? 103  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 103 ? -26.953 -8.211  14.271  1.00 33.83  ? 103  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 103 ? -27.808 -9.143  15.148  1.00 33.04  ? 103  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 103 ? -27.125 -10.495 15.287  1.00 32.72  ? 103  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 103 ? -28.085 -8.538  16.542  1.00 34.58  ? 103  LEU A CD2 1 
ATOM   838  N  N   . LEU A 1 104 ? -26.805 -5.579  12.076  1.00 34.40  ? 104  LEU A N   1 
ATOM   839  C  CA  . LEU A 1 104 ? -25.915 -4.623  11.425  1.00 37.64  ? 104  LEU A CA  1 
ATOM   840  C  C   . LEU A 1 104 ? -25.778 -3.328  12.222  1.00 37.95  ? 104  LEU A C   1 
ATOM   841  O  O   . LEU A 1 104 ? -24.645 -2.835  12.357  1.00 36.23  ? 104  LEU A O   1 
ATOM   842  C  CB  . LEU A 1 104 ? -26.400 -4.352  9.991   1.00 34.44  ? 104  LEU A CB  1 
ATOM   843  C  CG  . LEU A 1 104 ? -25.438 -3.553  9.105   1.00 40.18  ? 104  LEU A CG  1 
ATOM   844  C  CD1 . LEU A 1 104 ? -24.113 -4.301  8.974   1.00 44.07  ? 104  LEU A CD1 1 
ATOM   845  C  CD2 . LEU A 1 104 ? -26.059 -3.291  7.731   1.00 40.50  ? 104  LEU A CD2 1 
ATOM   846  N  N   . PRO A 1 105 ? -26.841 -2.761  12.802  1.00 35.85  ? 105  PRO A N   1 
ATOM   847  C  CA  . PRO A 1 105 ? -26.681 -1.521  13.585  1.00 38.97  ? 105  PRO A CA  1 
ATOM   848  C  C   . PRO A 1 105 ? -25.767 -1.664  14.793  1.00 37.49  ? 105  PRO A C   1 
ATOM   849  O  O   . PRO A 1 105 ? -25.239 -0.653  15.270  1.00 36.88  ? 105  PRO A O   1 
ATOM   850  C  CB  . PRO A 1 105 ? -28.118 -1.191  14.016  1.00 38.34  ? 105  PRO A CB  1 
ATOM   851  C  CG  . PRO A 1 105 ? -28.971 -1.832  12.960  1.00 38.90  ? 105  PRO A CG  1 
ATOM   852  C  CD  . PRO A 1 105 ? -28.260 -3.126  12.636  1.00 35.44  ? 105  PRO A CD  1 
ATOM   853  N  N   . SER A 1 106 ? -25.564 -2.875  15.303  1.00 34.02  ? 106  SER A N   1 
ATOM   854  C  CA  . SER A 1 106 ? -24.630 -3.091  16.405  1.00 35.02  ? 106  SER A CA  1 
ATOM   855  C  C   . SER A 1 106 ? -23.169 -2.898  16.004  1.00 34.93  ? 106  SER A C   1 
ATOM   856  O  O   . SER A 1 106 ? -22.288 -2.991  16.872  1.00 35.35  ? 106  SER A O   1 
ATOM   857  C  CB  . SER A 1 106 ? -24.822 -4.496  16.971  1.00 37.43  ? 106  SER A CB  1 
ATOM   858  O  OG  . SER A 1 106 ? -26.067 -4.565  17.633  1.00 43.58  ? 106  SER A OG  1 
ATOM   859  N  N   . PHE A 1 107 ? -22.884 -2.631  14.731  1.00 36.05  ? 107  PHE A N   1 
ATOM   860  C  CA  . PHE A 1 107 ? -21.515 -2.385  14.289  1.00 34.72  ? 107  PHE A CA  1 
ATOM   861  C  C   . PHE A 1 107 ? -21.398 -1.062  13.539  1.00 37.96  ? 107  PHE A C   1 
ATOM   862  O  O   . PHE A 1 107 ? -20.405 -0.830  12.847  1.00 37.43  ? 107  PHE A O   1 
ATOM   863  C  CB  . PHE A 1 107 ? -21.019 -3.573  13.462  1.00 35.79  ? 107  PHE A CB  1 
ATOM   864  C  CG  . PHE A 1 107 ? -21.047 -4.844  14.244  1.00 37.19  ? 107  PHE A CG  1 
ATOM   865  C  CD1 . PHE A 1 107 ? -20.023 -5.130  15.131  1.00 35.70  ? 107  PHE A CD1 1 
ATOM   866  C  CD2 . PHE A 1 107 ? -22.156 -5.681  14.213  1.00 35.50  ? 107  PHE A CD2 1 
ATOM   867  C  CE1 . PHE A 1 107 ? -20.062 -6.266  15.921  1.00 36.59  ? 107  PHE A CE1 1 
ATOM   868  C  CE2 . PHE A 1 107 ? -22.208 -6.834  14.996  1.00 35.85  ? 107  PHE A CE2 1 
ATOM   869  C  CZ  . PHE A 1 107 ? -21.165 -7.127  15.864  1.00 34.30  ? 107  PHE A CZ  1 
ATOM   870  N  N   . SER A 1 108 ? -22.371 -0.174  13.718  1.00 37.66  ? 108  SER A N   1 
ATOM   871  C  CA  . SER A 1 108 ? -22.304 1.175   13.185  1.00 40.75  ? 108  SER A CA  1 
ATOM   872  C  C   . SER A 1 108 ? -21.220 1.979   13.899  1.00 44.19  ? 108  SER A C   1 
ATOM   873  O  O   . SER A 1 108 ? -20.708 1.589   14.954  1.00 37.77  ? 108  SER A O   1 
ATOM   874  C  CB  . SER A 1 108 ? -23.644 1.870   13.356  1.00 45.48  ? 108  SER A CB  1 
ATOM   875  O  OG  . SER A 1 108 ? -23.904 2.076   14.738  1.00 42.69  ? 108  SER A OG  1 
ATOM   876  N  N   . GLN A 1 109 ? -20.881 3.132   13.309  1.00 43.52  ? 109  GLN A N   1 
ATOM   877  C  CA  . GLN A 1 109 ? -19.951 4.061   13.953  1.00 41.07  ? 109  GLN A CA  1 
ATOM   878  C  C   . GLN A 1 109 ? -20.422 4.422   15.358  1.00 39.66  ? 109  GLN A C   1 
ATOM   879  O  O   . GLN A 1 109 ? -19.642 4.385   16.320  1.00 42.75  ? 109  GLN A O   1 
ATOM   880  C  CB  . GLN A 1 109 ? -19.786 5.322   13.089  1.00 44.59  ? 109  GLN A CB  1 
ATOM   881  C  CG  . GLN A 1 109 ? -18.912 5.128   11.840  1.00 52.68  ? 109  GLN A CG  1 
ATOM   882  C  CD  . GLN A 1 109 ? -18.990 6.297   10.839  1.00 51.05  ? 109  GLN A CD  1 
ATOM   883  O  OE1 . GLN A 1 109 ? -19.671 7.298   11.075  1.00 52.61  ? 109  GLN A OE1 1 
ATOM   884  N  NE2 . GLN A 1 109 ? -18.304 6.153   9.707   1.00 55.76  ? 109  GLN A NE2 1 
ATOM   885  N  N   . GLN A 1 110 ? -21.706 4.773   15.501  1.00 39.70  ? 110  GLN A N   1 
ATOM   886  C  CA  . GLN A 1 110 ? -22.241 5.086   16.824  1.00 43.70  ? 110  GLN A CA  1 
ATOM   887  C  C   . GLN A 1 110 ? -22.056 3.925   17.796  1.00 41.83  ? 110  GLN A C   1 
ATOM   888  O  O   . GLN A 1 110 ? -21.703 4.134   18.968  1.00 39.91  ? 110  GLN A O   1 
ATOM   889  C  CB  . GLN A 1 110 ? -23.723 5.463   16.720  1.00 50.33  ? 110  GLN A CB  1 
ATOM   890  C  CG  . GLN A 1 110 ? -24.164 6.547   17.694  1.00 58.16  ? 110  GLN A CG  1 
ATOM   891  C  CD  . GLN A 1 110 ? -23.815 7.952   17.223  1.00 70.35  ? 110  GLN A CD  1 
ATOM   892  O  OE1 . GLN A 1 110 ? -22.737 8.469   17.531  1.00 66.78  ? 110  GLN A OE1 1 
ATOM   893  N  NE2 . GLN A 1 110 ? -24.721 8.574   16.466  1.00 73.48  ? 110  GLN A NE2 1 
ATOM   894  N  N   . ALA A 1 111 ? -22.326 2.697   17.342  1.00 42.36  ? 111  ALA A N   1 
ATOM   895  C  CA  . ALA A 1 111 ? -22.155 1.537   18.211  1.00 39.90  ? 111  ALA A CA  1 
ATOM   896  C  C   . ALA A 1 111 ? -20.700 1.368   18.617  1.00 37.89  ? 111  ALA A C   1 
ATOM   897  O  O   . ALA A 1 111 ? -20.415 1.091   19.784  1.00 39.14  ? 111  ALA A O   1 
ATOM   898  C  CB  . ALA A 1 111 ? -22.668 0.265   17.525  1.00 39.04  ? 111  ALA A CB  1 
ATOM   899  N  N   . MET A 1 112 ? -19.765 1.517   17.668  1.00 35.86  ? 112  MET A N   1 
ATOM   900  C  CA  . MET A 1 112 ? -18.347 1.389   18.014  1.00 37.94  ? 112  MET A CA  1 
ATOM   901  C  C   . MET A 1 112 ? -17.898 2.451   19.005  1.00 38.28  ? 112  MET A C   1 
ATOM   902  O  O   . MET A 1 112 ? -17.102 2.165   19.907  1.00 35.75  ? 112  MET A O   1 
ATOM   903  C  CB  . MET A 1 112 ? -17.460 1.400   16.771  1.00 37.44  ? 112  MET A CB  1 
ATOM   904  C  CG  . MET A 1 112 ? -17.820 0.342   15.746  1.00 43.65  ? 112  MET A CG  1 
ATOM   905  S  SD  . MET A 1 112 ? -17.196 -1.218  16.480  1.00 41.90  ? 112  MET A SD  1 
ATOM   906  C  CE  . MET A 1 112 ? -15.662 -0.697  17.197  1.00 40.77  ? 112  MET A CE  1 
ATOM   907  N  N   . LYS A 1 113 ? -18.374 3.682   18.849  1.00 39.85  ? 113  LYS A N   1 
ATOM   908  C  CA  . LYS A 1 113 ? -18.075 4.681   19.866  1.00 39.39  ? 113  LYS A CA  1 
ATOM   909  C  C   . LYS A 1 113 ? -18.584 4.233   21.231  1.00 40.22  ? 113  LYS A C   1 
ATOM   910  O  O   . LYS A 1 113 ? -17.917 4.445   22.249  1.00 40.50  ? 113  LYS A O   1 
ATOM   911  C  CB  . LYS A 1 113 ? -18.666 6.028   19.461  1.00 39.14  ? 113  LYS A CB  1 
ATOM   912  C  CG  . LYS A 1 113 ? -18.019 6.592   18.199  1.00 41.18  ? 113  LYS A CG  1 
ATOM   913  C  CD  . LYS A 1 113 ? -18.671 7.882   17.730  1.00 46.58  ? 113  LYS A CD  1 
ATOM   914  C  CE  . LYS A 1 113 ? -18.029 8.381   16.433  1.00 50.34  ? 113  LYS A CE  1 
ATOM   915  N  NZ  . LYS A 1 113 ? -18.882 9.386   15.728  1.00 49.55  ? 113  LYS A NZ  1 
ATOM   916  N  N   . GLY A 1 114 ? -19.749 3.576   21.267  1.00 34.21  ? 114  GLY A N   1 
ATOM   917  C  CA  . GLY A 1 114 ? -20.294 3.116   22.536  1.00 40.99  ? 114  GLY A CA  1 
ATOM   918  C  C   . GLY A 1 114 ? -19.549 1.937   23.139  1.00 38.85  ? 114  GLY A C   1 
ATOM   919  O  O   . GLY A 1 114 ? -19.597 1.729   24.356  1.00 39.64  ? 114  GLY A O   1 
ATOM   920  N  N   . TYR A 1 115 ? -18.880 1.135   22.307  1.00 38.03  ? 115  TYR A N   1 
ATOM   921  C  CA  . TYR A 1 115 ? -18.095 0.011   22.804  1.00 35.41  ? 115  TYR A CA  1 
ATOM   922  C  C   . TYR A 1 115 ? -16.739 0.434   23.339  1.00 36.04  ? 115  TYR A C   1 
ATOM   923  O  O   . TYR A 1 115 ? -16.125 -0.314  24.109  1.00 34.80  ? 115  TYR A O   1 
ATOM   924  C  CB  . TYR A 1 115 ? -17.830 -1.014  21.697  1.00 34.81  ? 115  TYR A CB  1 
ATOM   925  C  CG  . TYR A 1 115 ? -19.047 -1.678  21.110  1.00 32.82  ? 115  TYR A CG  1 
ATOM   926  C  CD1 . TYR A 1 115 ? -20.113 -2.064  21.911  1.00 36.14  ? 115  TYR A CD1 1 
ATOM   927  C  CD2 . TYR A 1 115 ? -19.110 -1.945  19.742  1.00 36.66  ? 115  TYR A CD2 1 
ATOM   928  C  CE1 . TYR A 1 115 ? -21.215 -2.688  21.361  1.00 39.23  ? 115  TYR A CE1 1 
ATOM   929  C  CE2 . TYR A 1 115 ? -20.196 -2.566  19.189  1.00 32.95  ? 115  TYR A CE2 1 
ATOM   930  C  CZ  . TYR A 1 115 ? -21.246 -2.937  19.999  1.00 34.24  ? 115  TYR A CZ  1 
ATOM   931  O  OH  . TYR A 1 115 ? -22.341 -3.560  19.445  1.00 37.92  ? 115  TYR A OH  1 
ATOM   932  N  N   . HIS A 1 116 ? -16.263 1.606   22.929  1.00 34.58  ? 116  HIS A N   1 
ATOM   933  C  CA  . HIS A 1 116 ? -14.858 1.950   23.112  1.00 34.24  ? 116  HIS A CA  1 
ATOM   934  C  C   . HIS A 1 116 ? -14.427 1.904   24.583  1.00 35.02  ? 116  HIS A C   1 
ATOM   935  O  O   . HIS A 1 116 ? -13.345 1.399   24.895  1.00 35.37  ? 116  HIS A O   1 
ATOM   936  C  CB  . HIS A 1 116 ? -14.584 3.329   22.514  1.00 34.03  ? 116  HIS A CB  1 
ATOM   937  C  CG  . HIS A 1 116 ? -13.156 3.750   22.646  1.00 34.37  ? 116  HIS A CG  1 
ATOM   938  N  ND1 . HIS A 1 116 ? -12.193 3.417   21.717  1.00 35.35  ? 116  HIS A ND1 1 
ATOM   939  C  CD2 . HIS A 1 116 ? -12.514 4.424   23.632  1.00 36.88  ? 116  HIS A CD2 1 
ATOM   940  C  CE1 . HIS A 1 116 ? -11.022 3.886   22.112  1.00 39.11  ? 116  HIS A CE1 1 
ATOM   941  N  NE2 . HIS A 1 116 ? -11.190 4.502   23.270  1.00 36.04  ? 116  HIS A NE2 1 
ATOM   942  N  N   . ALA A 1 117 ? -15.233 2.452   25.494  1.00 36.52  ? 117  ALA A N   1 
ATOM   943  C  CA  . ALA A 1 117 ? -14.823 2.486   26.903  1.00 39.21  ? 117  ALA A CA  1 
ATOM   944  C  C   . ALA A 1 117 ? -14.613 1.080   27.465  1.00 35.94  ? 117  ALA A C   1 
ATOM   945  O  O   . ALA A 1 117 ? -13.664 0.841   28.221  1.00 33.56  ? 117  ALA A O   1 
ATOM   946  C  CB  . ALA A 1 117 ? -15.854 3.249   27.744  1.00 38.01  ? 117  ALA A CB  1 
ATOM   947  N  N   . MET A 1 118 ? -15.489 0.133   27.116  1.00 33.21  ? 118  MET A N   1 
ATOM   948  C  CA  . MET A 1 118 ? -15.321 -1.220  27.639  1.00 33.45  ? 118  MET A CA  1 
ATOM   949  C  C   . MET A 1 118 ? -14.142 -1.937  26.980  1.00 32.73  ? 118  MET A C   1 
ATOM   950  O  O   . MET A 1 118 ? -13.516 -2.792  27.608  1.00 32.69  ? 118  MET A O   1 
ATOM   951  C  CB  . MET A 1 118 ? -16.614 -2.010  27.469  1.00 35.89  ? 118  MET A CB  1 
ATOM   952  C  CG  . MET A 1 118 ? -17.705 -1.565  28.438  1.00 39.67  ? 118  MET A CG  1 
ATOM   953  S  SD  . MET A 1 118 ? -19.290 -2.359  28.063  1.00 50.00  ? 118  MET A SD  1 
ATOM   954  C  CE  . MET A 1 118 ? -20.063 -2.353  29.697  1.00 48.34  ? 118  MET A CE  1 
ATOM   955  N  N   . MET A 1 119 ? -13.824 -1.608  25.724  1.00 32.47  ? 119  MET A N   1 
ATOM   956  C  CA  . MET A 1 119 ? -12.608 -2.136  25.132  1.00 29.79  ? 119  MET A CA  1 
ATOM   957  C  C   . MET A 1 119 ? -11.393 -1.680  25.939  1.00 33.62  ? 119  MET A C   1 
ATOM   958  O  O   . MET A 1 119 ? -10.457 -2.454  26.172  1.00 33.34  ? 119  MET A O   1 
ATOM   959  C  CB  . MET A 1 119 ? -12.495 -1.667  23.684  1.00 33.38  ? 119  MET A CB  1 
ATOM   960  C  CG  . MET A 1 119 ? -13.331 -2.505  22.723  1.00 33.85  ? 119  MET A CG  1 
ATOM   961  S  SD  . MET A 1 119 ? -12.924 -2.069  21.031  1.00 33.92  ? 119  MET A SD  1 
ATOM   962  C  CE  . MET A 1 119 ? -14.273 -2.796  20.107  1.00 34.09  ? 119  MET A CE  1 
ATOM   963  N  N   . VAL A 1 120 ? -11.385 -0.406  26.342  1.00 32.28  ? 120  VAL A N   1 
ATOM   964  C  CA  . VAL A 1 120 ? -10.259 0.135   27.098  1.00 32.18  ? 120  VAL A CA  1 
ATOM   965  C  C   . VAL A 1 120 ? -10.159 -0.555  28.449  1.00 32.85  ? 120  VAL A C   1 
ATOM   966  O  O   . VAL A 1 120 ? -9.060  -0.887  28.919  1.00 36.47  ? 120  VAL A O   1 
ATOM   967  C  CB  . VAL A 1 120 ? -10.404 1.664   27.246  1.00 33.29  ? 120  VAL A CB  1 
ATOM   968  C  CG1 . VAL A 1 120 ? -9.371  2.200   28.233  1.00 36.40  ? 120  VAL A CG1 1 
ATOM   969  C  CG2 . VAL A 1 120 ? -10.223 2.358   25.895  1.00 33.74  ? 120  VAL A CG2 1 
ATOM   970  N  N   . ASP A 1 121 ? -11.310 -0.808  29.081  1.00 33.37  ? 121  ASP A N   1 
ATOM   971  C  CA  . ASP A 1 121 ? -11.335 -1.551  30.336  1.00 33.66  ? 121  ASP A CA  1 
ATOM   972  C  C   . ASP A 1 121 ? -10.488 -2.817  30.229  1.00 35.71  ? 121  ASP A C   1 
ATOM   973  O  O   . ASP A 1 121 ? -9.583  -3.043  31.040  1.00 32.18  ? 121  ASP A O   1 
ATOM   974  C  CB  . ASP A 1 121 ? -12.789 -1.878  30.710  1.00 31.86  ? 121  ASP A CB  1 
ATOM   975  C  CG  . ASP A 1 121 ? -12.933 -2.554  32.076  1.00 34.05  ? 121  ASP A CG  1 
ATOM   976  O  OD1 . ASP A 1 121 ? -12.400 -3.667  32.286  1.00 35.40  ? 121  ASP A OD1 1 
ATOM   977  O  OD2 . ASP A 1 121 ? -13.662 -2.000  32.922  1.00 35.43  ? 121  ASP A OD2 1 
ATOM   978  N  N   . ILE A 1 122 ? -10.734 -3.634  29.198  1.00 33.07  ? 122  ILE A N   1 
ATOM   979  C  CA  . ILE A 1 122 ? -10.004 -4.894  29.074  1.00 33.29  ? 122  ILE A CA  1 
ATOM   980  C  C   . ILE A 1 122 ? -8.555  -4.633  28.674  1.00 34.59  ? 122  ILE A C   1 
ATOM   981  O  O   . ILE A 1 122 ? -7.628  -5.296  29.165  1.00 32.87  ? 122  ILE A O   1 
ATOM   982  C  CB  . ILE A 1 122 ? -10.705 -5.835  28.076  1.00 32.52  ? 122  ILE A CB  1 
ATOM   983  C  CG1 . ILE A 1 122 ? -12.173 -6.000  28.450  1.00 28.64  ? 122  ILE A CG1 1 
ATOM   984  C  CG2 . ILE A 1 122 ? -9.992  -7.202  28.030  1.00 31.58  ? 122  ILE A CG2 1 
ATOM   985  C  CD1 . ILE A 1 122 ? -12.390 -6.400  29.922  1.00 30.77  ? 122  ILE A CD1 1 
ATOM   986  N  N   . ALA A 1 123 ? -8.337  -3.668  27.782  1.00 32.48  ? 123  ALA A N   1 
ATOM   987  C  CA  . ALA A 1 123 ? -6.981  -3.355  27.339  1.00 32.08  ? 123  ALA A CA  1 
ATOM   988  C  C   . ALA A 1 123 ? -6.112  -2.931  28.511  1.00 33.60  ? 123  ALA A C   1 
ATOM   989  O  O   . ALA A 1 123 ? -4.940  -3.322  28.611  1.00 33.53  ? 123  ALA A O   1 
ATOM   990  C  CB  . ALA A 1 123 ? -7.016  -2.241  26.289  1.00 33.40  ? 123  ALA A CB  1 
ATOM   991  N  N   . VAL A 1 124 ? -6.665  -2.108  29.393  1.00 34.25  ? 124  VAL A N   1 
ATOM   992  C  CA  . VAL A 1 124 ? -5.913  -1.685  30.571  1.00 32.53  ? 124  VAL A CA  1 
ATOM   993  C  C   . VAL A 1 124 ? -5.580  -2.886  31.457  1.00 34.97  ? 124  VAL A C   1 
ATOM   994  O  O   . VAL A 1 124 ? -4.479  -2.980  32.005  1.00 35.75  ? 124  VAL A O   1 
ATOM   995  C  CB  . VAL A 1 124 ? -6.697  -0.599  31.325  1.00 35.61  ? 124  VAL A CB  1 
ATOM   996  C  CG1 . VAL A 1 124 ? -6.147  -0.421  32.733  1.00 33.42  ? 124  VAL A CG1 1 
ATOM   997  C  CG2 . VAL A 1 124 ? -6.618  0.727   30.565  1.00 33.25  ? 124  VAL A CG2 1 
ATOM   998  N  N   . GLN A 1 125 ? -6.506  -3.843  31.587  1.00 34.11  ? 125  GLN A N   1 
ATOM   999  C  CA  . GLN A 1 125 ? -6.189  -5.043  32.356  1.00 31.96  ? 125  GLN A CA  1 
ATOM   1000 C  C   . GLN A 1 125 ? -5.008  -5.794  31.747  1.00 34.12  ? 125  GLN A C   1 
ATOM   1001 O  O   . GLN A 1 125 ? -4.171  -6.336  32.474  1.00 35.52  ? 125  GLN A O   1 
ATOM   1002 C  CB  . GLN A 1 125 ? -7.404  -5.965  32.456  1.00 31.89  ? 125  GLN A CB  1 
ATOM   1003 C  CG  . GLN A 1 125 ? -8.528  -5.408  33.314  1.00 32.75  ? 125  GLN A CG  1 
ATOM   1004 C  CD  . GLN A 1 125 ? -9.602  -6.445  33.602  1.00 31.79  ? 125  GLN A CD  1 
ATOM   1005 O  OE1 . GLN A 1 125 ? -9.309  -7.581  34.009  1.00 33.96  ? 125  GLN A OE1 1 
ATOM   1006 N  NE2 . GLN A 1 125 ? -10.857 -6.068  33.364  1.00 31.93  ? 125  GLN A NE2 1 
ATOM   1007 N  N   . LEU A 1 126 ? -4.941  -5.870  30.412  1.00 32.00  ? 126  LEU A N   1 
ATOM   1008 C  CA  . LEU A 1 126 ? -3.798  -6.509  29.775  1.00 29.75  ? 126  LEU A CA  1 
ATOM   1009 C  C   . LEU A 1 126 ? -2.515  -5.747  30.084  1.00 33.09  ? 126  LEU A C   1 
ATOM   1010 O  O   . LEU A 1 126 ? -1.509  -6.341  30.494  1.00 35.99  ? 126  LEU A O   1 
ATOM   1011 C  CB  . LEU A 1 126 ? -4.013  -6.609  28.257  1.00 32.36  ? 126  LEU A CB  1 
ATOM   1012 C  CG  . LEU A 1 126 ? -2.759  -7.096  27.527  1.00 34.46  ? 126  LEU A CG  1 
ATOM   1013 C  CD1 . LEU A 1 126 ? -2.553  -8.598  27.749  1.00 35.60  ? 126  LEU A CD1 1 
ATOM   1014 C  CD2 . LEU A 1 126 ? -2.823  -6.781  26.033  1.00 38.19  ? 126  LEU A CD2 1 
ATOM   1015 N  N   . VAL A 1 127 ? -2.533  -4.423  29.902  1.00 32.39  ? 127  VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 127 ? -1.323  -3.640  30.157  1.00 35.51  ? 127  VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 127 ? -0.879  -3.801  31.610  1.00 37.25  ? 127  VAL A C   1 
ATOM   1018 O  O   . VAL A 1 127 ? 0.310   -3.986  31.892  1.00 36.14  ? 127  VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 127 ? -1.546  -2.166  29.778  1.00 38.06  ? 127  VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 127 ? -0.373  -1.313  30.268  1.00 38.16  ? 127  VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 127 ? -1.704  -2.043  28.248  1.00 35.74  ? 127  VAL A CG2 1 
ATOM   1022 N  N   . GLN A 1 128 ? -1.827  -3.774  32.546  1.00 35.93  ? 128  GLN A N   1 
ATOM   1023 C  CA  . GLN A 1 128 ? -1.483  -3.929  33.962  1.00 37.28  ? 128  GLN A CA  1 
ATOM   1024 C  C   . GLN A 1 128 ? -0.895  -5.307  34.257  1.00 37.61  ? 128  GLN A C   1 
ATOM   1025 O  O   . GLN A 1 128 ? 0.074   -5.416  35.021  1.00 37.37  ? 128  GLN A O   1 
ATOM   1026 C  CB  . GLN A 1 128 ? -2.729  -3.650  34.806  1.00 34.77  ? 128  GLN A CB  1 
ATOM   1027 C  CG  . GLN A 1 128 ? -3.126  -2.183  34.757  1.00 36.24  ? 128  GLN A CG  1 
ATOM   1028 C  CD  . GLN A 1 128 ? -4.117  -1.804  35.819  1.00 49.40  ? 128  GLN A CD  1 
ATOM   1029 O  OE1 . GLN A 1 128 ? -3.948  -0.804  36.526  1.00 56.69  ? 128  GLN A OE1 1 
ATOM   1030 N  NE2 . GLN A 1 128 ? -5.218  -2.560  35.886  1.00 48.24  ? 128  GLN A NE2 1 
ATOM   1031 N  N   . LYS A 1 129 ? -1.441  -6.372  33.656  1.00 33.19  ? 129  LYS A N   1 
ATOM   1032 C  CA  . LYS A 1 129 ? -0.848  -7.693  33.847  1.00 33.15  ? 129  LYS A CA  1 
ATOM   1033 C  C   . LYS A 1 129 ? 0.632   -7.675  33.471  1.00 37.20  ? 129  LYS A C   1 
ATOM   1034 O  O   . LYS A 1 129 ? 1.493   -8.175  34.208  1.00 34.90  ? 129  LYS A O   1 
ATOM   1035 C  CB  . LYS A 1 129 ? -1.571  -8.752  33.009  1.00 34.49  ? 129  LYS A CB  1 
ATOM   1036 C  CG  . LYS A 1 129 ? -0.883  -10.104 33.114  1.00 37.53  ? 129  LYS A CG  1 
ATOM   1037 C  CD  . LYS A 1 129 ? -1.683  -11.242 32.509  1.00 34.22  ? 129  LYS A CD  1 
ATOM   1038 C  CE  . LYS A 1 129 ? -0.918  -12.563 32.646  1.00 37.85  ? 129  LYS A CE  1 
ATOM   1039 N  NZ  . LYS A 1 129 ? -1.626  -13.739 32.069  1.00 37.17  ? 129  LYS A NZ  1 
ATOM   1040 N  N   . TRP A 1 130 ? 0.943   -7.084  32.320  1.00 32.99  ? 130  TRP A N   1 
ATOM   1041 C  CA  . TRP A 1 130 ? 2.317   -7.115  31.833  1.00 35.03  ? 130  TRP A CA  1 
ATOM   1042 C  C   . TRP A 1 130 ? 3.213   -6.183  32.641  1.00 35.91  ? 130  TRP A C   1 
ATOM   1043 O  O   . TRP A 1 130 ? 4.389   -6.506  32.869  1.00 37.70  ? 130  TRP A O   1 
ATOM   1044 C  CB  . TRP A 1 130 ? 2.328   -6.756  30.339  1.00 31.86  ? 130  TRP A CB  1 
ATOM   1045 C  CG  . TRP A 1 130 ? 1.745   -7.841  29.470  1.00 33.53  ? 130  TRP A CG  1 
ATOM   1046 C  CD1 . TRP A 1 130 ? 1.167   -9.021  29.883  1.00 33.76  ? 130  TRP A CD1 1 
ATOM   1047 C  CD2 . TRP A 1 130 ? 1.603   -7.803  28.049  1.00 33.00  ? 130  TRP A CD2 1 
ATOM   1048 N  NE1 . TRP A 1 130 ? 0.716   -9.734  28.791  1.00 31.87  ? 130  TRP A NE1 1 
ATOM   1049 C  CE2 . TRP A 1 130 ? 0.974   -9.005  27.655  1.00 33.06  ? 130  TRP A CE2 1 
ATOM   1050 C  CE3 . TRP A 1 130 ? 1.972   -6.876  27.066  1.00 35.57  ? 130  TRP A CE3 1 
ATOM   1051 C  CZ2 . TRP A 1 130 ? 0.707   -9.305  26.318  1.00 33.85  ? 130  TRP A CZ2 1 
ATOM   1052 C  CZ3 . TRP A 1 130 ? 1.707   -7.178  25.730  1.00 32.94  ? 130  TRP A CZ3 1 
ATOM   1053 C  CH2 . TRP A 1 130 ? 1.085   -8.385  25.372  1.00 34.90  ? 130  TRP A CH2 1 
ATOM   1054 N  N   . GLU A 1 131 ? 2.688   -5.041  33.089  1.00 35.00  ? 131  GLU A N   1 
ATOM   1055 C  CA  . GLU A 1 131 ? 3.454   -4.171  33.984  1.00 37.11  ? 131  GLU A CA  1 
ATOM   1056 C  C   . GLU A 1 131 ? 3.826   -4.883  35.278  1.00 39.70  ? 131  GLU A C   1 
ATOM   1057 O  O   . GLU A 1 131 ? 4.853   -4.564  35.894  1.00 36.36  ? 131  GLU A O   1 
ATOM   1058 C  CB  . GLU A 1 131 ? 2.665   -2.901  34.315  1.00 39.24  ? 131  GLU A CB  1 
ATOM   1059 C  CG  . GLU A 1 131 ? 2.356   -1.975  33.124  1.00 40.52  ? 131  GLU A CG  1 
ATOM   1060 C  CD  . GLU A 1 131 ? 3.518   -1.058  32.743  1.00 46.13  ? 131  GLU A CD  1 
ATOM   1061 O  OE1 . GLU A 1 131 ? 4.693   -1.409  33.011  1.00 42.45  ? 131  GLU A OE1 1 
ATOM   1062 O  OE2 . GLU A 1 131 ? 3.252   0.030   32.188  1.00 46.31  ? 131  GLU A OE2 1 
ATOM   1063 N  N   . ARG A 1 132 ? 3.021   -5.855  35.699  1.00 35.49  ? 132  ARG A N   1 
ATOM   1064 C  CA  . ARG A 1 132 ? 3.197   -6.504  36.993  1.00 35.10  ? 132  ARG A CA  1 
ATOM   1065 C  C   . ARG A 1 132 ? 4.022   -7.781  36.935  1.00 37.59  ? 132  ARG A C   1 
ATOM   1066 O  O   . ARG A 1 132 ? 4.205   -8.430  37.976  1.00 37.07  ? 132  ARG A O   1 
ATOM   1067 C  CB  . ARG A 1 132 ? 1.820   -6.798  37.617  1.00 33.80  ? 132  ARG A CB  1 
ATOM   1068 C  CG  . ARG A 1 132 ? 1.126   -5.528  38.076  1.00 34.81  ? 132  ARG A CG  1 
ATOM   1069 C  CD  . ARG A 1 132 ? -0.331  -5.738  38.454  1.00 33.80  ? 132  ARG A CD  1 
ATOM   1070 N  NE  . ARG A 1 132 ? -0.940  -4.476  38.869  1.00 34.39  ? 132  ARG A NE  1 
ATOM   1071 C  CZ  . ARG A 1 132 ? -2.247  -4.256  38.942  1.00 38.26  ? 132  ARG A CZ  1 
ATOM   1072 N  NH1 . ARG A 1 132 ? -3.127  -5.179  38.586  1.00 37.03  ? 132  ARG A NH1 1 
ATOM   1073 N  NH2 . ARG A 1 132 ? -2.683  -3.096  39.419  1.00 38.90  ? 132  ARG A NH2 1 
ATOM   1074 N  N   . LEU A 1 133 ? 4.544   -8.146  35.766  1.00 36.17  ? 133  LEU A N   1 
ATOM   1075 C  CA  . LEU A 1 133 ? 5.404   -9.309  35.669  1.00 30.74  ? 133  LEU A CA  1 
ATOM   1076 C  C   . LEU A 1 133 ? 6.733   -9.034  36.359  1.00 39.52  ? 133  LEU A C   1 
ATOM   1077 O  O   . LEU A 1 133 ? 7.200   -7.892  36.410  1.00 40.12  ? 133  LEU A O   1 
ATOM   1078 C  CB  . LEU A 1 133 ? 5.647   -9.666  34.204  1.00 38.02  ? 133  LEU A CB  1 
ATOM   1079 C  CG  . LEU A 1 133 ? 4.402   -10.242 33.531  1.00 35.31  ? 133  LEU A CG  1 
ATOM   1080 C  CD1 . LEU A 1 133 ? 4.731   -10.635 32.083  1.00 38.41  ? 133  LEU A CD1 1 
ATOM   1081 C  CD2 . LEU A 1 133 ? 3.870   -11.435 34.302  1.00 37.14  ? 133  LEU A CD2 1 
ATOM   1082 N  N   . ASN A 1 134 ? 7.340   -10.091 36.894  1.00 36.59  ? 134  ASN A N   1 
ATOM   1083 C  CA  . ASN A 1 134 ? 8.661   -9.925  37.472  1.00 41.01  ? 134  ASN A CA  1 
ATOM   1084 C  C   . ASN A 1 134 ? 9.715   -10.007 36.380  1.00 42.66  ? 134  ASN A C   1 
ATOM   1085 O  O   . ASN A 1 134 ? 9.441   -10.412 35.252  1.00 42.54  ? 134  ASN A O   1 
ATOM   1086 C  CB  . ASN A 1 134 ? 8.936   -10.980 38.537  1.00 37.43  ? 134  ASN A CB  1 
ATOM   1087 C  CG  . ASN A 1 134 ? 7.956   -10.898 39.678  1.00 36.28  ? 134  ASN A CG  1 
ATOM   1088 O  OD1 . ASN A 1 134 ? 7.907   -9.898  40.392  1.00 36.77  ? 134  ASN A OD1 1 
ATOM   1089 N  ND2 . ASN A 1 134 ? 7.157   -11.940 39.841  1.00 38.93  ? 134  ASN A ND2 1 
ATOM   1090 N  N   . ALA A 1 135 ? 10.942  -9.639  36.745  1.00 47.25  ? 135  ALA A N   1 
ATOM   1091 C  CA  . ALA A 1 135 ? 12.043  -9.634  35.790  1.00 53.41  ? 135  ALA A CA  1 
ATOM   1092 C  C   . ALA A 1 135 ? 12.260  -11.023 35.206  1.00 49.06  ? 135  ALA A C   1 
ATOM   1093 O  O   . ALA A 1 135 ? 12.289  -12.025 35.925  1.00 47.16  ? 135  ALA A O   1 
ATOM   1094 C  CB  . ALA A 1 135 ? 13.323  -9.140  36.463  1.00 55.39  ? 135  ALA A CB  1 
ATOM   1095 N  N   . ASP A 1 136 ? 12.417  -11.087 33.890  1.00 54.15  ? 136  ASP A N   1 
ATOM   1096 C  CA  . ASP A 1 136 ? 12.708  -12.329 33.189  1.00 56.23  ? 136  ASP A CA  1 
ATOM   1097 C  C   . ASP A 1 136 ? 11.552  -13.324 33.236  1.00 56.36  ? 136  ASP A C   1 
ATOM   1098 O  O   . ASP A 1 136 ? 11.710  -14.453 32.741  1.00 57.52  ? 136  ASP A O   1 
ATOM   1099 C  CB  . ASP A 1 136 ? 13.985  -13.000 33.718  1.00 63.14  ? 136  ASP A CB  1 
ATOM   1100 C  CG  . ASP A 1 136 ? 15.241  -12.192 33.398  1.00 65.56  ? 136  ASP A CG  1 
ATOM   1101 O  OD1 . ASP A 1 136 ? 15.155  -11.240 32.585  1.00 67.36  ? 136  ASP A OD1 1 
ATOM   1102 O  OD2 . ASP A 1 136 ? 16.310  -12.502 33.965  1.00 73.57  ? 136  ASP A OD2 1 
ATOM   1103 N  N   . GLU A 1 137 ? 10.403  -12.962 33.816  1.00 48.60  ? 137  GLU A N   1 
ATOM   1104 C  CA  . GLU A 1 137 ? 9.176   -13.644 33.438  1.00 41.97  ? 137  GLU A CA  1 
ATOM   1105 C  C   . GLU A 1 137 ? 8.844   -13.274 32.001  1.00 41.03  ? 137  GLU A C   1 
ATOM   1106 O  O   . GLU A 1 137 ? 9.329   -12.280 31.462  1.00 44.43  ? 137  GLU A O   1 
ATOM   1107 C  CB  . GLU A 1 137 ? 8.017   -13.269 34.367  1.00 38.93  ? 137  GLU A CB  1 
ATOM   1108 C  CG  . GLU A 1 137 ? 8.238   -13.842 35.763  1.00 43.89  ? 137  GLU A CG  1 
ATOM   1109 C  CD  . GLU A 1 137 ? 7.126   -13.562 36.748  1.00 46.30  ? 137  GLU A CD  1 
ATOM   1110 O  OE1 . GLU A 1 137 ? 6.229   -12.732 36.468  1.00 40.23  ? 137  GLU A OE1 1 
ATOM   1111 O  OE2 . GLU A 1 137 ? 7.163   -14.187 37.830  1.00 50.90  ? 137  GLU A OE2 1 
ATOM   1112 N  N   . HIS A 1 138 ? 8.002   -14.072 31.380  1.00 38.03  ? 138  HIS A N   1 
ATOM   1113 C  CA  . HIS A 1 138 ? 7.667   -13.783 29.998  1.00 41.88  ? 138  HIS A CA  1 
ATOM   1114 C  C   . HIS A 1 138 ? 6.159   -13.789 29.826  1.00 40.19  ? 138  HIS A C   1 
ATOM   1115 O  O   . HIS A 1 138 ? 5.398   -14.104 30.745  1.00 37.96  ? 138  HIS A O   1 
ATOM   1116 C  CB  . HIS A 1 138 ? 8.327   -14.785 29.054  1.00 38.63  ? 138  HIS A CB  1 
ATOM   1117 C  CG  . HIS A 1 138 ? 7.877   -16.189 29.269  1.00 40.79  ? 138  HIS A CG  1 
ATOM   1118 N  ND1 . HIS A 1 138 ? 8.628   -17.107 29.967  1.00 49.09  ? 138  HIS A ND1 1 
ATOM   1119 C  CD2 . HIS A 1 138 ? 6.750   -16.832 28.891  1.00 39.16  ? 138  HIS A CD2 1 
ATOM   1120 C  CE1 . HIS A 1 138 ? 7.986   -18.261 30.000  1.00 49.00  ? 138  HIS A CE1 1 
ATOM   1121 N  NE2 . HIS A 1 138 ? 6.843   -18.121 29.352  1.00 44.27  ? 138  HIS A NE2 1 
ATOM   1122 N  N   . ILE A 1 139 ? 5.749   -13.456 28.611  1.00 37.92  ? 139  ILE A N   1 
ATOM   1123 C  CA  . ILE A 1 139 ? 4.349   -13.356 28.223  1.00 36.06  ? 139  ILE A CA  1 
ATOM   1124 C  C   . ILE A 1 139 ? 4.025   -14.537 27.329  1.00 38.67  ? 139  ILE A C   1 
ATOM   1125 O  O   . ILE A 1 139 ? 4.766   -14.821 26.378  1.00 38.45  ? 139  ILE A O   1 
ATOM   1126 C  CB  . ILE A 1 139 ? 4.090   -12.033 27.487  1.00 33.74  ? 139  ILE A CB  1 
ATOM   1127 C  CG1 . ILE A 1 139 ? 4.210   -10.863 28.458  1.00 34.81  ? 139  ILE A CG1 1 
ATOM   1128 C  CG2 . ILE A 1 139 ? 2.754   -12.067 26.723  1.00 36.04  ? 139  ILE A CG2 1 
ATOM   1129 C  CD1 . ILE A 1 139 ? 4.559   -9.571  27.767  1.00 36.73  ? 139  ILE A CD1 1 
ATOM   1130 N  N   . GLU A 1 140 ? 2.921   -15.226 27.630  1.00 36.23  ? 140  GLU A N   1 
ATOM   1131 C  CA  . GLU A 1 140 ? 2.371   -16.252 26.753  1.00 34.76  ? 140  GLU A CA  1 
ATOM   1132 C  C   . GLU A 1 140 ? 1.393   -15.539 25.823  1.00 38.11  ? 140  GLU A C   1 
ATOM   1133 O  O   . GLU A 1 140 ? 0.287   -15.176 26.234  1.00 34.21  ? 140  GLU A O   1 
ATOM   1134 C  CB  . GLU A 1 140 ? 1.701   -17.351 27.567  1.00 36.06  ? 140  GLU A CB  1 
ATOM   1135 C  CG  . GLU A 1 140 ? 2.670   -18.124 28.461  1.00 39.17  ? 140  GLU A CG  1 
ATOM   1136 C  CD  . GLU A 1 140 ? 1.977   -19.185 29.298  1.00 50.37  ? 140  GLU A CD  1 
ATOM   1137 O  OE1 . GLU A 1 140 ? 0.792   -18.993 29.656  1.00 44.57  ? 140  GLU A OE1 1 
ATOM   1138 O  OE2 . GLU A 1 140 ? 2.621   -20.211 29.597  1.00 52.74  ? 140  GLU A OE2 1 
ATOM   1139 N  N   . VAL A 1 141 ? 1.809   -15.301 24.580  1.00 37.82  ? 141  VAL A N   1 
ATOM   1140 C  CA  . VAL A 1 141 ? 1.136   -14.307 23.739  1.00 33.57  ? 141  VAL A CA  1 
ATOM   1141 C  C   . VAL A 1 141 ? -0.262  -14.757 23.320  1.00 32.95  ? 141  VAL A C   1 
ATOM   1142 O  O   . VAL A 1 141 ? -1.238  -14.054 23.632  1.00 36.39  ? 141  VAL A O   1 
ATOM   1143 C  CB  . VAL A 1 141 ? 1.986   -13.948 22.511  1.00 36.57  ? 141  VAL A CB  1 
ATOM   1144 C  CG1 . VAL A 1 141 ? 1.195   -13.049 21.572  1.00 35.17  ? 141  VAL A CG1 1 
ATOM   1145 C  CG2 . VAL A 1 141 ? 3.257   -13.252 22.958  1.00 36.99  ? 141  VAL A CG2 1 
ATOM   1146 N  N   . PRO A 1 142 ? -0.430  -15.877 22.607  1.00 35.96  ? 142  PRO A N   1 
ATOM   1147 C  CA  . PRO A 1 142 ? -1.796  -16.261 22.214  1.00 35.09  ? 142  PRO A CA  1 
ATOM   1148 C  C   . PRO A 1 142 ? -2.708  -16.447 23.409  1.00 35.72  ? 142  PRO A C   1 
ATOM   1149 O  O   . PRO A 1 142 ? -3.905  -16.126 23.338  1.00 31.70  ? 142  PRO A O   1 
ATOM   1150 C  CB  . PRO A 1 142 ? -1.591  -17.561 21.420  1.00 36.44  ? 142  PRO A CB  1 
ATOM   1151 C  CG  . PRO A 1 142 ? -0.189  -18.021 21.772  1.00 37.29  ? 142  PRO A CG  1 
ATOM   1152 C  CD  . PRO A 1 142 ? 0.575   -16.766 22.008  1.00 36.16  ? 142  PRO A CD  1 
ATOM   1153 N  N   . GLU A 1 143 ? -2.161  -16.913 24.524  1.00 33.61  ? 143  GLU A N   1 
ATOM   1154 C  CA  . GLU A 1 143 ? -2.964  -17.093 25.724  1.00 32.25  ? 143  GLU A CA  1 
ATOM   1155 C  C   . GLU A 1 143 ? -3.518  -15.761 26.218  1.00 34.22  ? 143  GLU A C   1 
ATOM   1156 O  O   . GLU A 1 143 ? -4.722  -15.634 26.490  1.00 33.20  ? 143  GLU A O   1 
ATOM   1157 C  CB  . GLU A 1 143 ? -2.114  -17.780 26.797  1.00 32.39  ? 143  GLU A CB  1 
ATOM   1158 C  CG  . GLU A 1 143 ? -1.794  -19.253 26.492  1.00 35.28  ? 143  GLU A CG  1 
ATOM   1159 C  CD  . GLU A 1 143 ? -0.689  -19.479 25.447  1.00 38.59  ? 143  GLU A CD  1 
ATOM   1160 O  OE1 . GLU A 1 143 ? 0.021   -18.528 25.031  1.00 35.84  ? 143  GLU A OE1 1 
ATOM   1161 O  OE2 . GLU A 1 143 ? -0.550  -20.640 25.019  1.00 42.78  ? 143  GLU A OE2 1 
ATOM   1162 N  N   . ASP A 1 144 ? -2.651  -14.749 26.345  1.00 30.35  ? 144  ASP A N   1 
ATOM   1163 C  CA  . ASP A 1 144 ? -3.107  -13.441 26.787  1.00 30.78  ? 144  ASP A CA  1 
ATOM   1164 C  C   . ASP A 1 144 ? -3.966  -12.736 25.737  1.00 32.46  ? 144  ASP A C   1 
ATOM   1165 O  O   . ASP A 1 144 ? -4.873  -11.978 26.096  1.00 31.18  ? 144  ASP A O   1 
ATOM   1166 C  CB  . ASP A 1 144 ? -1.905  -12.568 27.163  1.00 31.60  ? 144  ASP A CB  1 
ATOM   1167 C  CG  . ASP A 1 144 ? -1.472  -12.773 28.607  1.00 38.32  ? 144  ASP A CG  1 
ATOM   1168 O  OD1 . ASP A 1 144 ? -2.251  -13.377 29.370  1.00 33.94  ? 144  ASP A OD1 1 
ATOM   1169 O  OD2 . ASP A 1 144 ? -0.368  -12.323 28.981  1.00 36.63  ? 144  ASP A OD2 1 
ATOM   1170 N  N   . MET A 1 145 ? -3.701  -12.955 24.445  1.00 33.69  ? 145  MET A N   1 
ATOM   1171 C  CA  . MET A 1 145 ? -4.543  -12.327 23.430  1.00 31.10  ? 145  MET A CA  1 
ATOM   1172 C  C   . MET A 1 145 ? -5.954  -12.904 23.486  1.00 30.92  ? 145  MET A C   1 
ATOM   1173 O  O   . MET A 1 145 ? -6.938  -12.192 23.255  1.00 32.51  ? 145  MET A O   1 
ATOM   1174 C  CB  . MET A 1 145 ? -3.923  -12.552 22.050  1.00 29.91  ? 145  MET A CB  1 
ATOM   1175 C  CG  . MET A 1 145 ? -2.690  -11.672 21.757  1.00 32.83  ? 145  MET A CG  1 
ATOM   1176 S  SD  . MET A 1 145 ? -2.716  -9.975  22.325  1.00 35.87  ? 145  MET A SD  1 
ATOM   1177 C  CE  . MET A 1 145 ? -1.939  -10.027 23.945  1.00 38.96  ? 145  MET A CE  1 
ATOM   1178 N  N   . THR A 1 146 ? -6.066  -14.196 23.799  1.00 29.85  ? 146  THR A N   1 
ATOM   1179 C  CA  . THR A 1 146 ? -7.376  -14.821 23.956  1.00 32.29  ? 146  THR A CA  1 
ATOM   1180 C  C   . THR A 1 146 ? -8.082  -14.313 25.201  1.00 30.48  ? 146  THR A C   1 
ATOM   1181 O  O   . THR A 1 146 ? -9.289  -14.046 25.166  1.00 31.45  ? 146  THR A O   1 
ATOM   1182 C  CB  . THR A 1 146 ? -7.220  -16.344 23.981  1.00 32.44  ? 146  THR A CB  1 
ATOM   1183 O  OG1 . THR A 1 146 ? -6.827  -16.784 22.679  1.00 39.20  ? 146  THR A OG1 1 
ATOM   1184 C  CG2 . THR A 1 146 ? -8.518  -17.057 24.353  1.00 33.11  ? 146  THR A CG2 1 
ATOM   1185 N  N   . ARG A 1 147 ? -7.360  -14.188 26.324  1.00 30.41  ? 147  ARG A N   1 
ATOM   1186 C  CA  . ARG A 1 147 ? -7.938  -13.513 27.488  1.00 30.72  ? 147  ARG A CA  1 
ATOM   1187 C  C   . ARG A 1 147 ? -8.524  -12.168 27.096  1.00 32.53  ? 147  ARG A C   1 
ATOM   1188 O  O   . ARG A 1 147 ? -9.675  -11.857 27.418  1.00 33.58  ? 147  ARG A O   1 
ATOM   1189 C  CB  . ARG A 1 147 ? -6.879  -13.306 28.571  1.00 32.02  ? 147  ARG A CB  1 
ATOM   1190 C  CG  . ARG A 1 147 ? -6.378  -14.568 29.233  1.00 33.97  ? 147  ARG A CG  1 
ATOM   1191 C  CD  . ARG A 1 147 ? -5.451  -14.191 30.378  1.00 34.23  ? 147  ARG A CD  1 
ATOM   1192 N  NE  . ARG A 1 147 ? -5.172  -15.344 31.224  1.00 33.84  ? 147  ARG A NE  1 
ATOM   1193 C  CZ  . ARG A 1 147 ? -4.176  -16.199 31.033  1.00 40.25  ? 147  ARG A CZ  1 
ATOM   1194 N  NH1 . ARG A 1 147 ? -3.296  -16.040 30.049  1.00 36.23  ? 147  ARG A NH1 1 
ATOM   1195 N  NH2 . ARG A 1 147 ? -4.067  -17.251 31.841  1.00 39.54  ? 147  ARG A NH2 1 
ATOM   1196 N  N   . LEU A 1 148 ? -7.736  -11.355 26.386  1.00 30.94  ? 148  LEU A N   1 
ATOM   1197 C  CA  . LEU A 1 148 ? -8.194  -10.019 26.030  1.00 32.24  ? 148  LEU A CA  1 
ATOM   1198 C  C   . LEU A 1 148 ? -9.401  -10.076 25.107  1.00 31.50  ? 148  LEU A C   1 
ATOM   1199 O  O   . LEU A 1 148 ? -10.406 -9.389  25.337  1.00 32.77  ? 148  LEU A O   1 
ATOM   1200 C  CB  . LEU A 1 148 ? -7.069  -9.225  25.361  1.00 34.52  ? 148  LEU A CB  1 
ATOM   1201 C  CG  . LEU A 1 148 ? -7.658  -7.896  24.869  1.00 32.36  ? 148  LEU A CG  1 
ATOM   1202 C  CD1 . LEU A 1 148 ? -6.996  -6.752  25.586  1.00 34.84  ? 148  LEU A CD1 1 
ATOM   1203 C  CD2 . LEU A 1 148 ? -7.535  -7.755  23.359  1.00 38.06  ? 148  LEU A CD2 1 
ATOM   1204 N  N   . THR A 1 149 ? -9.314  -10.854 24.030  1.00 30.24  ? 149  THR A N   1 
ATOM   1205 C  CA  . THR A 1 149 ? -10.378 -10.752 23.032  1.00 27.64  ? 149  THR A CA  1 
ATOM   1206 C  C   . THR A 1 149 ? -11.675 -11.386 23.523  1.00 31.29  ? 149  THR A C   1 
ATOM   1207 O  O   . THR A 1 149 ? -12.765 -10.859 23.260  1.00 29.92  ? 149  THR A O   1 
ATOM   1208 C  CB  . THR A 1 149 ? -9.939  -11.351 21.697  1.00 30.53  ? 149  THR A CB  1 
ATOM   1209 O  OG1 . THR A 1 149 ? -9.644  -12.740 21.857  1.00 31.18  ? 149  THR A OG1 1 
ATOM   1210 C  CG2 . THR A 1 149 ? -8.709  -10.595 21.150  1.00 29.21  ? 149  THR A CG2 1 
ATOM   1211 N  N   . LEU A 1 150 ? -11.595 -12.521 24.218  1.00 31.02  ? 150  LEU A N   1 
ATOM   1212 C  CA  . LEU A 1 150 ? -12.811 -13.075 24.806  1.00 31.89  ? 150  LEU A CA  1 
ATOM   1213 C  C   . LEU A 1 150 ? -13.447 -12.085 25.777  1.00 33.08  ? 150  LEU A C   1 
ATOM   1214 O  O   . LEU A 1 150 ? -14.670 -11.894 25.777  1.00 31.52  ? 150  LEU A O   1 
ATOM   1215 C  CB  . LEU A 1 150 ? -12.511 -14.390 25.525  1.00 33.22  ? 150  LEU A CB  1 
ATOM   1216 C  CG  . LEU A 1 150 ? -13.732 -14.943 26.264  1.00 34.17  ? 150  LEU A CG  1 
ATOM   1217 C  CD1 . LEU A 1 150 ? -14.710 -15.508 25.233  1.00 35.11  ? 150  LEU A CD1 1 
ATOM   1218 C  CD2 . LEU A 1 150 ? -13.321 -16.001 27.295  1.00 36.35  ? 150  LEU A CD2 1 
ATOM   1219 N  N   . ASP A 1 151 ? -12.641 -11.443 26.624  1.00 30.15  ? 151  ASP A N   1 
ATOM   1220 C  CA  . ASP A 1 151 ? -13.242 -10.547 27.604  1.00 30.28  ? 151  ASP A CA  1 
ATOM   1221 C  C   . ASP A 1 151 ? -13.845 -9.330  26.928  1.00 29.11  ? 151  ASP A C   1 
ATOM   1222 O  O   . ASP A 1 151 ? -14.886 -8.820  27.365  1.00 32.33  ? 151  ASP A O   1 
ATOM   1223 C  CB  . ASP A 1 151 ? -12.207 -10.133 28.650  1.00 30.34  ? 151  ASP A CB  1 
ATOM   1224 C  CG  . ASP A 1 151 ? -12.049 -11.187 29.753  1.00 29.68  ? 151  ASP A CG  1 
ATOM   1225 O  OD1 . ASP A 1 151 ? -12.279 -12.385 29.484  1.00 35.90  ? 151  ASP A OD1 1 
ATOM   1226 O  OD2 . ASP A 1 151 ? -11.734 -10.801 30.882  1.00 34.89  ? 151  ASP A OD2 1 
ATOM   1227 N  N   . THR A 1 152 ? -13.236 -8.890  25.838  1.00 31.11  ? 152  THR A N   1 
ATOM   1228 C  CA  . THR A 1 152 ? -13.738 -7.720  25.146  1.00 30.07  ? 152  THR A CA  1 
ATOM   1229 C  C   . THR A 1 152 ? -15.092 -8.002  24.498  1.00 32.02  ? 152  THR A C   1 
ATOM   1230 O  O   . THR A 1 152 ? -16.019 -7.199  24.630  1.00 32.13  ? 152  THR A O   1 
ATOM   1231 C  CB  . THR A 1 152 ? -12.700 -7.244  24.133  1.00 30.43  ? 152  THR A CB  1 
ATOM   1232 O  OG1 . THR A 1 152 ? -11.533 -6.822  24.860  1.00 31.70  ? 152  THR A OG1 1 
ATOM   1233 C  CG2 . THR A 1 152 ? -13.227 -6.055  23.365  1.00 30.86  ? 152  THR A CG2 1 
ATOM   1234 N  N   . ILE A 1 153 ? -15.246 -9.143  23.816  1.00 30.91  ? 153  ILE A N   1 
ATOM   1235 C  CA  . ILE A 1 153 ? -16.568 -9.397  23.227  1.00 30.70  ? 153  ILE A CA  1 
ATOM   1236 C  C   . ILE A 1 153 ? -17.593 -9.668  24.327  1.00 32.06  ? 153  ILE A C   1 
ATOM   1237 O  O   . ILE A 1 153 ? -18.761 -9.265  24.214  1.00 29.77  ? 153  ILE A O   1 
ATOM   1238 C  CB  . ILE A 1 153 ? -16.531 -10.526 22.170  1.00 29.77  ? 153  ILE A CB  1 
ATOM   1239 C  CG1 . ILE A 1 153 ? -17.888 -10.633 21.436  1.00 31.10  ? 153  ILE A CG1 1 
ATOM   1240 C  CG2 . ILE A 1 153 ? -16.203 -11.884 22.795  1.00 31.22  ? 153  ILE A CG2 1 
ATOM   1241 C  CD1 . ILE A 1 153 ? -18.255 -9.393  20.593  1.00 32.15  ? 153  ILE A CD1 1 
ATOM   1242 N  N   . GLY A 1 154 ? -17.188 -10.305 25.426  1.00 29.71  ? 154  GLY A N   1 
ATOM   1243 C  CA  . GLY A 1 154 ? -18.150 -10.554 26.501  1.00 34.09  ? 154  GLY A CA  1 
ATOM   1244 C  C   . GLY A 1 154 ? -18.668 -9.262  27.112  1.00 35.01  ? 154  GLY A C   1 
ATOM   1245 O  O   . GLY A 1 154 ? -19.877 -9.093  27.336  1.00 33.04  ? 154  GLY A O   1 
ATOM   1246 N  N   . LEU A 1 155 ? -17.756 -8.335  27.403  1.00 32.38  ? 155  LEU A N   1 
ATOM   1247 C  CA  . LEU A 1 155 ? -18.131 -7.092  28.076  1.00 29.56  ? 155  LEU A CA  1 
ATOM   1248 C  C   . LEU A 1 155 ? -18.855 -6.149  27.118  1.00 31.86  ? 155  LEU A C   1 
ATOM   1249 O  O   . LEU A 1 155 ? -19.973 -5.702  27.402  1.00 32.57  ? 155  LEU A O   1 
ATOM   1250 C  CB  . LEU A 1 155 ? -16.878 -6.430  28.671  1.00 32.00  ? 155  LEU A CB  1 
ATOM   1251 C  CG  . LEU A 1 155 ? -17.140 -5.134  29.454  1.00 34.17  ? 155  LEU A CG  1 
ATOM   1252 C  CD1 . LEU A 1 155 ? -18.112 -5.414  30.604  1.00 34.02  ? 155  LEU A CD1 1 
ATOM   1253 C  CD2 . LEU A 1 155 ? -15.843 -4.534  30.005  1.00 33.02  ? 155  LEU A CD2 1 
ATOM   1254 N  N   . CYS A 1 156 ? -18.241 -5.848  25.965  1.00 33.00  ? 156  CYS A N   1 
ATOM   1255 C  CA  . CYS A 1 156 ? -18.856 -4.928  25.005  1.00 33.36  ? 156  CYS A CA  1 
ATOM   1256 C  C   . CYS A 1 156 ? -20.154 -5.491  24.450  1.00 34.76  ? 156  CYS A C   1 
ATOM   1257 O  O   . CYS A 1 156 ? -21.139 -4.760  24.290  1.00 32.98  ? 156  CYS A O   1 
ATOM   1258 C  CB  . CYS A 1 156 ? -17.897 -4.641  23.849  1.00 34.01  ? 156  CYS A CB  1 
ATOM   1259 S  SG  . CYS A 1 156 ? -16.337 -3.878  24.321  1.00 36.51  ? 156  CYS A SG  1 
ATOM   1260 N  N   . GLY A 1 157 ? -20.167 -6.782  24.119  1.00 32.38  ? 157  GLY A N   1 
ATOM   1261 C  CA  . GLY A 1 157 ? -21.325 -7.365  23.462  1.00 29.99  ? 157  GLY A CA  1 
ATOM   1262 C  C   . GLY A 1 157 ? -22.459 -7.710  24.403  1.00 34.11  ? 157  GLY A C   1 
ATOM   1263 O  O   . GLY A 1 157 ? -23.630 -7.546  24.041  1.00 32.85  ? 157  GLY A O   1 
ATOM   1264 N  N   . PHE A 1 158 ? -22.135 -8.169  25.619  1.00 31.07  ? 158  PHE A N   1 
ATOM   1265 C  CA  . PHE A 1 158 ? -23.124 -8.797  26.487  1.00 33.47  ? 158  PHE A CA  1 
ATOM   1266 C  C   . PHE A 1 158 ? -23.094 -8.306  27.922  1.00 36.65  ? 158  PHE A C   1 
ATOM   1267 O  O   . PHE A 1 158 ? -23.858 -8.824  28.747  1.00 37.11  ? 158  PHE A O   1 
ATOM   1268 C  CB  . PHE A 1 158 ? -22.935 -10.320 26.453  1.00 33.06  ? 158  PHE A CB  1 
ATOM   1269 C  CG  . PHE A 1 158 ? -22.967 -10.858 25.060  1.00 34.12  ? 158  PHE A CG  1 
ATOM   1270 C  CD1 . PHE A 1 158 ? -24.172 -11.165 24.457  1.00 29.46  ? 158  PHE A CD1 1 
ATOM   1271 C  CD2 . PHE A 1 158 ? -21.803 -10.961 24.321  1.00 31.87  ? 158  PHE A CD2 1 
ATOM   1272 C  CE1 . PHE A 1 158 ? -24.205 -11.610 23.135  1.00 28.57  ? 158  PHE A CE1 1 
ATOM   1273 C  CE2 . PHE A 1 158 ? -21.827 -11.400 23.010  1.00 30.92  ? 158  PHE A CE2 1 
ATOM   1274 C  CZ  . PHE A 1 158 ? -23.033 -11.725 22.413  1.00 33.82  ? 158  PHE A CZ  1 
ATOM   1275 N  N   . ASN A 1 159 ? -22.254 -7.320  28.234  1.00 33.11  ? 159  ASN A N   1 
ATOM   1276 C  CA  . ASN A 1 159 ? -22.099 -6.824  29.600  1.00 35.26  ? 159  ASN A CA  1 
ATOM   1277 C  C   . ASN A 1 159 ? -21.845 -7.969  30.575  1.00 38.25  ? 159  ASN A C   1 
ATOM   1278 O  O   . ASN A 1 159 ? -22.389 -8.006  31.686  1.00 33.27  ? 159  ASN A O   1 
ATOM   1279 C  CB  . ASN A 1 159 ? -23.317 -5.998  30.032  1.00 41.36  ? 159  ASN A CB  1 
ATOM   1280 C  CG  . ASN A 1 159 ? -22.983 -5.050  31.154  1.00 46.34  ? 159  ASN A CG  1 
ATOM   1281 O  OD1 . ASN A 1 159 ? -21.812 -4.734  31.368  1.00 37.71  ? 159  ASN A OD1 1 
ATOM   1282 N  ND2 . ASN A 1 159 ? -23.996 -4.608  31.895  1.00 48.78  ? 159  ASN A ND2 1 
ATOM   1283 N  N   . TYR A 1 160 ? -21.002 -8.919  30.162  1.00 34.96  ? 160  TYR A N   1 
ATOM   1284 C  CA  . TYR A 1 160 ? -20.649 -10.071 30.983  1.00 34.25  ? 160  TYR A CA  1 
ATOM   1285 C  C   . TYR A 1 160 ? -19.134 -10.105 31.118  1.00 34.09  ? 160  TYR A C   1 
ATOM   1286 O  O   . TYR A 1 160 ? -18.417 -9.916  30.127  1.00 32.79  ? 160  TYR A O   1 
ATOM   1287 C  CB  . TYR A 1 160 ? -21.159 -11.376 30.364  1.00 33.61  ? 160  TYR A CB  1 
ATOM   1288 C  CG  . TYR A 1 160 ? -20.922 -12.590 31.221  1.00 36.63  ? 160  TYR A CG  1 
ATOM   1289 C  CD1 . TYR A 1 160 ? -21.756 -12.870 32.297  1.00 36.94  ? 160  TYR A CD1 1 
ATOM   1290 C  CD2 . TYR A 1 160 ? -19.852 -13.448 30.970  1.00 35.77  ? 160  TYR A CD2 1 
ATOM   1291 C  CE1 . TYR A 1 160 ? -21.547 -13.977 33.096  1.00 38.93  ? 160  TYR A CE1 1 
ATOM   1292 C  CE2 . TYR A 1 160 ? -19.622 -14.569 31.775  1.00 38.95  ? 160  TYR A CE2 1 
ATOM   1293 C  CZ  . TYR A 1 160 ? -20.481 -14.822 32.838  1.00 40.72  ? 160  TYR A CZ  1 
ATOM   1294 O  OH  . TYR A 1 160 ? -20.281 -15.917 33.642  1.00 44.05  ? 160  TYR A OH  1 
ATOM   1295 N  N   . ARG A 1 161 ? -18.643 -10.330 32.334  1.00 32.51  ? 161  ARG A N   1 
ATOM   1296 C  CA  . ARG A 1 161 ? -17.198 -10.338 32.575  1.00 35.29  ? 161  ARG A CA  1 
ATOM   1297 C  C   . ARG A 1 161 ? -16.728 -11.782 32.696  1.00 31.94  ? 161  ARG A C   1 
ATOM   1298 O  O   . ARG A 1 161 ? -17.017 -12.460 33.681  1.00 33.70  ? 161  ARG A O   1 
ATOM   1299 C  CB  . ARG A 1 161 ? -16.847 -9.520  33.812  1.00 33.89  ? 161  ARG A CB  1 
ATOM   1300 C  CG  . ARG A 1 161 ? -17.000 -8.023  33.540  1.00 34.95  ? 161  ARG A CG  1 
ATOM   1301 C  CD  . ARG A 1 161 ? -16.468 -7.150  34.646  1.00 35.41  ? 161  ARG A CD  1 
ATOM   1302 N  NE  . ARG A 1 161 ? -16.666 -5.738  34.337  1.00 35.30  ? 161  ARG A NE  1 
ATOM   1303 C  CZ  . ARG A 1 161 ? -15.737 -4.931  33.842  1.00 35.23  ? 161  ARG A CZ  1 
ATOM   1304 N  NH1 . ARG A 1 161 ? -14.507 -5.357  33.582  1.00 32.77  ? 161  ARG A NH1 1 
ATOM   1305 N  NH2 . ARG A 1 161 ? -16.045 -3.663  33.609  1.00 33.16  ? 161  ARG A NH2 1 
ATOM   1306 N  N   . PHE A 1 162 ? -16.022 -12.262 31.671  1.00 30.64  ? 162  PHE A N   1 
ATOM   1307 C  CA  . PHE A 1 162 ? -15.364 -13.557 31.788  1.00 30.84  ? 162  PHE A CA  1 
ATOM   1308 C  C   . PHE A 1 162 ? -14.207 -13.518 32.785  1.00 32.09  ? 162  PHE A C   1 
ATOM   1309 O  O   . PHE A 1 162 ? -13.802 -14.572 33.291  1.00 34.24  ? 162  PHE A O   1 
ATOM   1310 C  CB  . PHE A 1 162 ? -14.847 -14.006 30.417  1.00 33.62  ? 162  PHE A CB  1 
ATOM   1311 C  CG  . PHE A 1 162 ? -15.930 -14.453 29.469  1.00 31.79  ? 162  PHE A CG  1 
ATOM   1312 C  CD1 . PHE A 1 162 ? -16.419 -15.745 29.515  1.00 37.43  ? 162  PHE A CD1 1 
ATOM   1313 C  CD2 . PHE A 1 162 ? -16.414 -13.587 28.491  1.00 35.21  ? 162  PHE A CD2 1 
ATOM   1314 C  CE1 . PHE A 1 162 ? -17.411 -16.166 28.621  1.00 39.25  ? 162  PHE A CE1 1 
ATOM   1315 C  CE2 . PHE A 1 162 ? -17.403 -14.003 27.598  1.00 37.04  ? 162  PHE A CE2 1 
ATOM   1316 C  CZ  . PHE A 1 162 ? -17.904 -15.296 27.676  1.00 36.50  ? 162  PHE A CZ  1 
ATOM   1317 N  N   . ASN A 1 163 ? -13.671 -12.330 33.066  1.00 33.38  ? 163  ASN A N   1 
ATOM   1318 C  CA  . ASN A 1 163 ? -12.605 -12.159 34.064  1.00 33.27  ? 163  ASN A CA  1 
ATOM   1319 C  C   . ASN A 1 163 ? -11.420 -13.074 33.766  1.00 31.91  ? 163  ASN A C   1 
ATOM   1320 O  O   . ASN A 1 163 ? -10.819 -13.686 34.656  1.00 34.88  ? 163  ASN A O   1 
ATOM   1321 C  CB  . ASN A 1 163 ? -13.151 -12.358 35.475  1.00 34.50  ? 163  ASN A CB  1 
ATOM   1322 C  CG  . ASN A 1 163 ? -13.960 -11.165 35.927  1.00 32.68  ? 163  ASN A CG  1 
ATOM   1323 O  OD1 . ASN A 1 163 ? -13.536 -10.031 35.736  1.00 35.10  ? 163  ASN A OD1 1 
ATOM   1324 N  ND2 . ASN A 1 163 ? -15.161 -11.407 36.494  1.00 31.18  ? 163  ASN A ND2 1 
ATOM   1325 N  N   . SER A 1 164 ? -11.057 -13.131 32.486  1.00 32.07  ? 164  SER A N   1 
ATOM   1326 C  CA  . SER A 1 164 ? -10.014 -14.041 32.045  1.00 33.29  ? 164  SER A CA  1 
ATOM   1327 C  C   . SER A 1 164 ? -8.659  -13.703 32.655  1.00 35.04  ? 164  SER A C   1 
ATOM   1328 O  O   . SER A 1 164 ? -7.824  -14.602 32.817  1.00 32.92  ? 164  SER A O   1 
ATOM   1329 C  CB  . SER A 1 164 ? -9.920  -14.036 30.514  1.00 32.71  ? 164  SER A CB  1 
ATOM   1330 O  OG  . SER A 1 164 ? -11.111 -14.560 29.938  1.00 33.01  ? 164  SER A OG  1 
ATOM   1331 N  N   . PHE A 1 165 ? -8.418  -12.434 32.995  1.00 32.07  ? 165  PHE A N   1 
ATOM   1332 C  CA  . PHE A 1 165 ? -7.137  -12.071 33.597  1.00 33.89  ? 165  PHE A CA  1 
ATOM   1333 C  C   . PHE A 1 165 ? -7.073  -12.395 35.081  1.00 35.95  ? 165  PHE A C   1 
ATOM   1334 O  O   . PHE A 1 165 ? -6.016  -12.200 35.699  1.00 35.76  ? 165  PHE A O   1 
ATOM   1335 C  CB  . PHE A 1 165 ? -6.831  -10.591 33.368  1.00 32.84  ? 165  PHE A CB  1 
ATOM   1336 C  CG  . PHE A 1 165 ? -6.478  -10.281 31.945  1.00 33.95  ? 165  PHE A CG  1 
ATOM   1337 C  CD1 . PHE A 1 165 ? -5.289  -10.751 31.400  1.00 33.90  ? 165  PHE A CD1 1 
ATOM   1338 C  CD2 . PHE A 1 165 ? -7.353  -9.582  31.135  1.00 33.92  ? 165  PHE A CD2 1 
ATOM   1339 C  CE1 . PHE A 1 165 ? -4.962  -10.490 30.071  1.00 34.08  ? 165  PHE A CE1 1 
ATOM   1340 C  CE2 . PHE A 1 165 ? -7.027  -9.315  29.798  1.00 32.67  ? 165  PHE A CE2 1 
ATOM   1341 C  CZ  . PHE A 1 165 ? -5.834  -9.772  29.274  1.00 35.07  ? 165  PHE A CZ  1 
ATOM   1342 N  N   . TYR A 1 166 ? -8.166  -12.886 35.655  1.00 33.67  ? 166  TYR A N   1 
ATOM   1343 C  CA  . TYR A 1 166 ? -8.172  -13.444 37.004  1.00 34.97  ? 166  TYR A CA  1 
ATOM   1344 C  C   . TYR A 1 166 ? -7.973  -14.951 37.000  1.00 36.85  ? 166  TYR A C   1 
ATOM   1345 O  O   . TYR A 1 166 ? -8.097  -15.583 38.050  1.00 37.95  ? 166  TYR A O   1 
ATOM   1346 C  CB  . TYR A 1 166 ? -9.478  -13.061 37.711  1.00 32.87  ? 166  TYR A CB  1 
ATOM   1347 C  CG  . TYR A 1 166 ? -9.539  -11.572 37.931  1.00 33.76  ? 166  TYR A CG  1 
ATOM   1348 C  CD1 . TYR A 1 166 ? -10.010 -10.719 36.932  1.00 31.26  ? 166  TYR A CD1 1 
ATOM   1349 C  CD2 . TYR A 1 166 ? -9.063  -11.007 39.120  1.00 32.94  ? 166  TYR A CD2 1 
ATOM   1350 C  CE1 . TYR A 1 166 ? -10.046 -9.344  37.120  1.00 31.46  ? 166  TYR A CE1 1 
ATOM   1351 C  CE2 . TYR A 1 166 ? -9.077  -9.645  39.314  1.00 32.11  ? 166  TYR A CE2 1 
ATOM   1352 C  CZ  . TYR A 1 166 ? -9.577  -8.816  38.314  1.00 30.25  ? 166  TYR A CZ  1 
ATOM   1353 O  OH  . TYR A 1 166 ? -9.581  -7.469  38.497  1.00 33.17  ? 166  TYR A OH  1 
ATOM   1354 N  N   . ARG A 1 167 ? -7.616  -15.538 35.850  1.00 34.70  ? 167  ARG A N   1 
ATOM   1355 C  CA  . ARG A 1 167 ? -7.469  -16.981 35.721  1.00 37.04  ? 167  ARG A CA  1 
ATOM   1356 C  C   . ARG A 1 167 ? -6.091  -17.316 35.176  1.00 41.41  ? 167  ARG A C   1 
ATOM   1357 O  O   . ARG A 1 167 ? -5.620  -16.677 34.232  1.00 41.61  ? 167  ARG A O   1 
ATOM   1358 C  CB  . ARG A 1 167 ? -8.518  -17.574 34.789  1.00 38.94  ? 167  ARG A CB  1 
ATOM   1359 C  CG  . ARG A 1 167 ? -9.936  -17.399 35.273  1.00 41.75  ? 167  ARG A CG  1 
ATOM   1360 C  CD  . ARG A 1 167 ? -10.900 -17.747 34.172  1.00 40.79  ? 167  ARG A CD  1 
ATOM   1361 N  NE  . ARG A 1 167 ? -12.212 -17.177 34.435  1.00 45.69  ? 167  ARG A NE  1 
ATOM   1362 C  CZ  . ARG A 1 167 ? -13.165 -17.806 35.104  1.00 49.52  ? 167  ARG A CZ  1 
ATOM   1363 N  NH1 . ARG A 1 167 ? -13.023 -19.071 35.477  1.00 47.72  ? 167  ARG A NH1 1 
ATOM   1364 N  NH2 . ARG A 1 167 ? -14.289 -17.153 35.397  1.00 50.75  ? 167  ARG A NH2 1 
ATOM   1365 N  N   . ASP A 1 168 ? -5.457  -18.333 35.761  1.00 42.72  ? 168  ASP A N   1 
ATOM   1366 C  CA  . ASP A 1 168 ? -4.211  -18.839 35.201  1.00 42.87  ? 168  ASP A CA  1 
ATOM   1367 C  C   . ASP A 1 168 ? -4.456  -19.936 34.176  1.00 46.98  ? 168  ASP A C   1 
ATOM   1368 O  O   . ASP A 1 168 ? -3.569  -20.218 33.366  1.00 50.53  ? 168  ASP A O   1 
ATOM   1369 C  CB  . ASP A 1 168 ? -3.277  -19.349 36.316  1.00 47.39  ? 168  ASP A CB  1 
ATOM   1370 C  CG  . ASP A 1 168 ? -3.958  -20.320 37.263  1.00 52.75  ? 168  ASP A CG  1 
ATOM   1371 O  OD1 . ASP A 1 168 ? -4.741  -19.899 38.148  1.00 50.91  ? 168  ASP A OD1 1 
ATOM   1372 O  OD2 . ASP A 1 168 ? -3.698  -21.533 37.125  1.00 63.23  ? 168  ASP A OD2 1 
ATOM   1373 N  N   . GLN A 1 169 ? -5.639  -20.541 34.186  1.00 46.69  ? 169  GLN A N   1 
ATOM   1374 C  CA  . GLN A 1 169 ? -6.087  -21.496 33.192  1.00 50.04  ? 169  GLN A CA  1 
ATOM   1375 C  C   . GLN A 1 169 ? -7.201  -20.890 32.350  1.00 49.84  ? 169  GLN A C   1 
ATOM   1376 O  O   . GLN A 1 169 ? -7.878  -19.951 32.779  1.00 49.34  ? 169  GLN A O   1 
ATOM   1377 C  CB  . GLN A 1 169 ? -6.601  -22.777 33.860  1.00 54.70  ? 169  GLN A CB  1 
ATOM   1378 C  CG  . GLN A 1 169 ? -5.592  -23.461 34.767  1.00 59.17  ? 169  GLN A CG  1 
ATOM   1379 C  CD  . GLN A 1 169 ? -6.185  -24.672 35.456  1.00 68.24  ? 169  GLN A CD  1 
ATOM   1380 O  OE1 . GLN A 1 169 ? -6.224  -25.767 34.891  1.00 72.26  ? 169  GLN A OE1 1 
ATOM   1381 N  NE2 . GLN A 1 169 ? -6.677  -24.474 36.675  1.00 68.71  ? 169  GLN A NE2 1 
ATOM   1382 N  N   . PRO A 1 170 ? -7.440  -21.417 31.150  1.00 52.62  ? 170  PRO A N   1 
ATOM   1383 C  CA  . PRO A 1 170 ? -8.476  -20.834 30.291  1.00 47.89  ? 170  PRO A CA  1 
ATOM   1384 C  C   . PRO A 1 170 ? -9.848  -20.914 30.944  1.00 50.00  ? 170  PRO A C   1 
ATOM   1385 O  O   . PRO A 1 170 ? -10.143 -21.831 31.717  1.00 46.78  ? 170  PRO A O   1 
ATOM   1386 C  CB  . PRO A 1 170 ? -8.411  -21.697 29.021  1.00 50.36  ? 170  PRO A CB  1 
ATOM   1387 C  CG  . PRO A 1 170 ? -7.075  -22.347 29.056  1.00 47.62  ? 170  PRO A CG  1 
ATOM   1388 C  CD  . PRO A 1 170 ? -6.760  -22.555 30.505  1.00 48.68  ? 170  PRO A CD  1 
ATOM   1389 N  N   . HIS A 1 171 ? -10.692 -19.935 30.630  1.00 46.37  ? 171  HIS A N   1 
ATOM   1390 C  CA  . HIS A 1 171 ? -12.081 -20.012 31.052  1.00 47.91  ? 171  HIS A CA  1 
ATOM   1391 C  C   . HIS A 1 171 ? -12.682 -21.331 30.563  1.00 46.56  ? 171  HIS A C   1 
ATOM   1392 O  O   . HIS A 1 171 ? -12.329 -21.801 29.470  1.00 45.16  ? 171  HIS A O   1 
ATOM   1393 C  CB  . HIS A 1 171 ? -12.870 -18.824 30.492  1.00 43.32  ? 171  HIS A CB  1 
ATOM   1394 C  CG  . HIS A 1 171 ? -14.231 -18.663 31.090  1.00 45.62  ? 171  HIS A CG  1 
ATOM   1395 N  ND1 . HIS A 1 171 ? -15.296 -19.463 30.741  1.00 45.94  ? 171  HIS A ND1 1 
ATOM   1396 C  CD2 . HIS A 1 171 ? -14.705 -17.781 32.004  1.00 40.83  ? 171  HIS A CD2 1 
ATOM   1397 C  CE1 . HIS A 1 171 ? -16.366 -19.095 31.425  1.00 49.90  ? 171  HIS A CE1 1 
ATOM   1398 N  NE2 . HIS A 1 171 ? -16.033 -18.080 32.204  1.00 46.06  ? 171  HIS A NE2 1 
ATOM   1399 N  N   . PRO A 1 172 ? -13.564 -21.963 31.340  1.00 46.62  ? 172  PRO A N   1 
ATOM   1400 C  CA  . PRO A 1 172 ? -14.214 -23.197 30.863  1.00 43.56  ? 172  PRO A CA  1 
ATOM   1401 C  C   . PRO A 1 172 ? -14.812 -23.064 29.472  1.00 45.06  ? 172  PRO A C   1 
ATOM   1402 O  O   . PRO A 1 172 ? -14.826 -24.037 28.701  1.00 40.82  ? 172  PRO A O   1 
ATOM   1403 C  CB  . PRO A 1 172 ? -15.303 -23.440 31.912  1.00 48.45  ? 172  PRO A CB  1 
ATOM   1404 C  CG  . PRO A 1 172 ? -14.757 -22.803 33.159  1.00 51.28  ? 172  PRO A CG  1 
ATOM   1405 C  CD  . PRO A 1 172 ? -13.985 -21.599 32.707  1.00 45.88  ? 172  PRO A CD  1 
ATOM   1406 N  N   . PHE A 1 173 ? -15.325 -21.882 29.132  1.00 44.82  ? 173  PHE A N   1 
ATOM   1407 C  CA  . PHE A 1 173 ? -15.869 -21.676 27.794  1.00 40.45  ? 173  PHE A CA  1 
ATOM   1408 C  C   . PHE A 1 173 ? -14.796 -21.897 26.740  1.00 40.49  ? 173  PHE A C   1 
ATOM   1409 O  O   . PHE A 1 173 ? -15.028 -22.566 25.728  1.00 42.13  ? 173  PHE A O   1 
ATOM   1410 C  CB  . PHE A 1 173 ? -16.459 -20.268 27.675  1.00 43.70  ? 173  PHE A CB  1 
ATOM   1411 C  CG  . PHE A 1 173 ? -17.192 -20.029 26.384  1.00 40.72  ? 173  PHE A CG  1 
ATOM   1412 C  CD1 . PHE A 1 173 ? -18.535 -20.344 26.265  1.00 40.74  ? 173  PHE A CD1 1 
ATOM   1413 C  CD2 . PHE A 1 173 ? -16.523 -19.515 25.285  1.00 42.43  ? 173  PHE A CD2 1 
ATOM   1414 C  CE1 . PHE A 1 173 ? -19.208 -20.137 25.067  1.00 41.87  ? 173  PHE A CE1 1 
ATOM   1415 C  CE2 . PHE A 1 173 ? -17.182 -19.308 24.081  1.00 39.72  ? 173  PHE A CE2 1 
ATOM   1416 C  CZ  . PHE A 1 173 ? -18.529 -19.615 23.972  1.00 38.98  ? 173  PHE A CZ  1 
ATOM   1417 N  N   . ILE A 1 174 ? -13.615 -21.325 26.955  1.00 40.11  ? 174  ILE A N   1 
ATOM   1418 C  CA  . ILE A 1 174 ? -12.528 -21.504 26.001  1.00 39.75  ? 174  ILE A CA  1 
ATOM   1419 C  C   . ILE A 1 174 ? -12.150 -22.975 25.893  1.00 43.46  ? 174  ILE A C   1 
ATOM   1420 O  O   . ILE A 1 174 ? -11.926 -23.492 24.792  1.00 39.94  ? 174  ILE A O   1 
ATOM   1421 C  CB  . ILE A 1 174 ? -11.317 -20.643 26.397  1.00 39.48  ? 174  ILE A CB  1 
ATOM   1422 C  CG1 . ILE A 1 174 ? -11.619 -19.147 26.221  1.00 39.14  ? 174  ILE A CG1 1 
ATOM   1423 C  CG2 . ILE A 1 174 ? -10.094 -21.081 25.585  1.00 43.35  ? 174  ILE A CG2 1 
ATOM   1424 C  CD1 . ILE A 1 174 ? -12.004 -18.737 24.772  1.00 34.75  ? 174  ILE A CD1 1 
ATOM   1425 N  N   . THR A 1 175 ? -12.049 -23.669 27.031  1.00 40.93  ? 175  THR A N   1 
ATOM   1426 C  CA  . THR A 1 175 ? -11.631 -25.069 26.997  1.00 39.96  ? 175  THR A CA  1 
ATOM   1427 C  C   . THR A 1 175 ? -12.576 -25.897 26.142  1.00 40.61  ? 175  THR A C   1 
ATOM   1428 O  O   . THR A 1 175 ? -12.141 -26.693 25.301  1.00 38.90  ? 175  THR A O   1 
ATOM   1429 C  CB  . THR A 1 175 ? -11.574 -25.636 28.409  1.00 42.42  ? 175  THR A CB  1 
ATOM   1430 O  OG1 . THR A 1 175 ? -10.529 -24.977 29.132  1.00 45.62  ? 175  THR A OG1 1 
ATOM   1431 C  CG2 . THR A 1 175 ? -11.319 -27.145 28.361  1.00 42.90  ? 175  THR A CG2 1 
ATOM   1432 N  N   . SER A 1 176 ? -13.879 -25.732 26.364  1.00 37.88  ? 176  SER A N   1 
ATOM   1433 C  CA  . SER A 1 176 ? -14.869 -26.482 25.608  1.00 40.42  ? 176  SER A CA  1 
ATOM   1434 C  C   . SER A 1 176 ? -14.940 -26.001 24.157  1.00 40.58  ? 176  SER A C   1 
ATOM   1435 O  O   . SER A 1 176 ? -15.136 -26.814 23.251  1.00 37.63  ? 176  SER A O   1 
ATOM   1436 C  CB  . SER A 1 176 ? -16.234 -26.376 26.295  1.00 41.21  ? 176  SER A CB  1 
ATOM   1437 O  OG  . SER A 1 176 ? -16.251 -27.096 27.523  1.00 44.03  ? 176  SER A OG  1 
ATOM   1438 N  N   . MET A 1 177 ? -14.791 -24.689 23.919  1.00 38.57  ? 177  MET A N   1 
ATOM   1439 C  CA  . MET A 1 177 ? -14.770 -24.177 22.549  1.00 37.92  ? 177  MET A CA  1 
ATOM   1440 C  C   . MET A 1 177 ? -13.634 -24.793 21.752  1.00 38.18  ? 177  MET A C   1 
ATOM   1441 O  O   . MET A 1 177 ? -13.832 -25.272 20.629  1.00 36.16  ? 177  MET A O   1 
ATOM   1442 C  CB  . MET A 1 177 ? -14.585 -22.664 22.526  1.00 40.70  ? 177  MET A CB  1 
ATOM   1443 C  CG  . MET A 1 177 ? -14.425 -22.177 21.077  1.00 35.26  ? 177  MET A CG  1 
ATOM   1444 S  SD  . MET A 1 177 ? -13.958 -20.461 20.994  1.00 37.57  ? 177  MET A SD  1 
ATOM   1445 C  CE  . MET A 1 177 ? -12.180 -20.732 21.152  1.00 34.54  ? 177  MET A CE  1 
ATOM   1446 N  N   . VAL A 1 178 ? -12.420 -24.752 22.307  1.00 38.58  ? 178  VAL A N   1 
ATOM   1447 C  CA  . VAL A 1 178 ? -11.268 -25.306 21.602  1.00 40.28  ? 178  VAL A CA  1 
ATOM   1448 C  C   . VAL A 1 178 ? -11.465 -26.790 21.333  1.00 43.03  ? 178  VAL A C   1 
ATOM   1449 O  O   . VAL A 1 178 ? -11.191 -27.280 20.229  1.00 41.02  ? 178  VAL A O   1 
ATOM   1450 C  CB  . VAL A 1 178 ? -9.978  -25.045 22.395  1.00 39.47  ? 178  VAL A CB  1 
ATOM   1451 C  CG1 . VAL A 1 178 ? -8.808  -25.777 21.738  1.00 44.35  ? 178  VAL A CG1 1 
ATOM   1452 C  CG2 . VAL A 1 178 ? -9.707  -23.546 22.499  1.00 41.14  ? 178  VAL A CG2 1 
ATOM   1453 N  N   . ARG A 1 179 ? -11.944 -27.529 22.335  1.00 40.99  ? 179  ARG A N   1 
ATOM   1454 C  CA  . ARG A 1 179 ? -12.189 -28.956 22.147  1.00 40.88  ? 179  ARG A CA  1 
ATOM   1455 C  C   . ARG A 1 179 ? -13.261 -29.206 21.090  1.00 42.70  ? 179  ARG A C   1 
ATOM   1456 O  O   . ARG A 1 179 ? -13.201 -30.202 20.358  1.00 40.53  ? 179  ARG A O   1 
ATOM   1457 C  CB  . ARG A 1 179 ? -12.587 -29.589 23.481  1.00 44.03  ? 179  ARG A CB  1 
ATOM   1458 C  CG  . ARG A 1 179 ? -12.152 -31.028 23.657  1.00 50.96  ? 179  ARG A CG  1 
ATOM   1459 C  CD  . ARG A 1 179 ? -11.778 -31.272 25.125  1.00 53.00  ? 179  ARG A CD  1 
ATOM   1460 N  NE  . ARG A 1 179 ? -12.875 -30.923 26.025  1.00 53.00  ? 179  ARG A NE  1 
ATOM   1461 C  CZ  . ARG A 1 179 ? -12.732 -30.586 27.302  1.00 55.03  ? 179  ARG A CZ  1 
ATOM   1462 N  NH1 . ARG A 1 179 ? -11.540 -30.534 27.878  1.00 53.53  ? 179  ARG A NH1 1 
ATOM   1463 N  NH2 . ARG A 1 179 ? -13.813 -30.284 28.019  1.00 53.60  ? 179  ARG A NH2 1 
ATOM   1464 N  N   . ALA A 1 180 ? -14.267 -28.329 21.010  1.00 37.16  ? 180  ALA A N   1 
ATOM   1465 C  CA  . ALA A 1 180 ? -15.297 -28.500 19.994  1.00 36.38  ? 180  ALA A CA  1 
ATOM   1466 C  C   . ALA A 1 180 ? -14.737 -28.228 18.603  1.00 38.27  ? 180  ALA A C   1 
ATOM   1467 O  O   . ALA A 1 180 ? -15.022 -28.972 17.654  1.00 36.56  ? 180  ALA A O   1 
ATOM   1468 C  CB  . ALA A 1 180 ? -16.493 -27.593 20.288  1.00 38.79  ? 180  ALA A CB  1 
ATOM   1469 N  N   . LEU A 1 181 ? -13.922 -27.176 18.470  1.00 37.47  ? 181  LEU A N   1 
ATOM   1470 C  CA  . LEU A 1 181 ? -13.302 -26.860 17.185  1.00 37.57  ? 181  LEU A CA  1 
ATOM   1471 C  C   . LEU A 1 181 ? -12.296 -27.935 16.783  1.00 40.01  ? 181  LEU A C   1 
ATOM   1472 O  O   . LEU A 1 181 ? -12.206 -28.300 15.604  1.00 37.81  ? 181  LEU A O   1 
ATOM   1473 C  CB  . LEU A 1 181 ? -12.618 -25.489 17.261  1.00 37.29  ? 181  LEU A CB  1 
ATOM   1474 C  CG  . LEU A 1 181 ? -13.555 -24.291 17.445  1.00 34.12  ? 181  LEU A CG  1 
ATOM   1475 C  CD1 . LEU A 1 181 ? -12.741 -23.032 17.653  1.00 35.48  ? 181  LEU A CD1 1 
ATOM   1476 C  CD2 . LEU A 1 181 ? -14.457 -24.161 16.210  1.00 34.64  ? 181  LEU A CD2 1 
ATOM   1477 N  N   . ASP A 1 182 ? -11.511 -28.424 17.750  1.00 37.96  ? 182  ASP A N   1 
ATOM   1478 C  CA  . ASP A 1 182 ? -10.599 -29.541 17.510  1.00 42.40  ? 182  ASP A CA  1 
ATOM   1479 C  C   . ASP A 1 182 ? -11.349 -30.731 16.935  1.00 41.12  ? 182  ASP A C   1 
ATOM   1480 O  O   . ASP A 1 182 ? -10.913 -31.356 15.960  1.00 42.74  ? 182  ASP A O   1 
ATOM   1481 C  CB  . ASP A 1 182 ? -9.933  -29.967 18.818  1.00 42.68  ? 182  ASP A CB  1 
ATOM   1482 C  CG  . ASP A 1 182 ? -8.751  -29.111 19.189  1.00 50.37  ? 182  ASP A CG  1 
ATOM   1483 O  OD1 . ASP A 1 182 ? -8.285  -28.323 18.342  1.00 53.01  ? 182  ASP A OD1 1 
ATOM   1484 O  OD2 . ASP A 1 182 ? -8.300  -29.216 20.356  1.00 56.09  ? 182  ASP A OD2 1 
ATOM   1485 N  N   . GLU A 1 183 ? -12.475 -31.076 17.559  1.00 40.85  ? 183  GLU A N   1 
ATOM   1486 C  CA  . GLU A 1 183 ? -13.261 -32.218 17.106  1.00 41.64  ? 183  GLU A CA  1 
ATOM   1487 C  C   . GLU A 1 183 ? -13.802 -31.986 15.702  1.00 40.89  ? 183  GLU A C   1 
ATOM   1488 O  O   . GLU A 1 183 ? -13.762 -32.890 14.856  1.00 40.45  ? 183  GLU A O   1 
ATOM   1489 C  CB  . GLU A 1 183 ? -14.399 -32.492 18.090  1.00 42.26  ? 183  GLU A CB  1 
ATOM   1490 C  CG  . GLU A 1 183 ? -15.517 -33.394 17.560  1.00 44.38  ? 183  GLU A CG  1 
ATOM   1491 C  CD  . GLU A 1 183 ? -15.116 -34.868 17.391  1.00 46.05  ? 183  GLU A CD  1 
ATOM   1492 O  OE1 . GLU A 1 183 ? -13.955 -35.223 17.675  1.00 43.15  ? 183  GLU A OE1 1 
ATOM   1493 O  OE2 . GLU A 1 183 ? -15.976 -35.668 16.958  1.00 44.71  ? 183  GLU A OE2 1 
ATOM   1494 N  N   . ALA A 1 184 ? -14.321 -30.783 15.438  1.00 40.34  ? 184  ALA A N   1 
ATOM   1495 C  CA  . ALA A 1 184 ? -14.827 -30.490 14.102  1.00 41.11  ? 184  ALA A CA  1 
ATOM   1496 C  C   . ALA A 1 184 ? -13.719 -30.614 13.065  1.00 38.73  ? 184  ALA A C   1 
ATOM   1497 O  O   . ALA A 1 184 ? -13.948 -31.139 11.970  1.00 39.12  ? 184  ALA A O   1 
ATOM   1498 C  CB  . ALA A 1 184 ? -15.452 -29.090 14.057  1.00 35.58  ? 184  ALA A CB  1 
ATOM   1499 N  N   . MET A 1 185 ? -12.510 -30.138 13.391  1.00 37.49  ? 185  MET A N   1 
ATOM   1500 C  CA  . MET A 1 185 ? -11.389 -30.257 12.458  1.00 37.42  ? 185  MET A CA  1 
ATOM   1501 C  C   . MET A 1 185 ? -11.022 -31.716 12.224  1.00 41.19  ? 185  MET A C   1 
ATOM   1502 O  O   . MET A 1 185 ? -10.828 -32.151 11.084  1.00 37.65  ? 185  MET A O   1 
ATOM   1503 C  CB  . MET A 1 185 ? -10.149 -29.534 12.980  1.00 35.53  ? 185  MET A CB  1 
ATOM   1504 C  CG  . MET A 1 185 ? -9.113  -29.336 11.872  1.00 32.64  ? 185  MET A CG  1 
ATOM   1505 S  SD  . MET A 1 185 ? -7.710  -28.336 12.370  1.00 40.16  ? 185  MET A SD  1 
ATOM   1506 C  CE  . MET A 1 185 ? -6.896  -29.437 13.525  1.00 43.62  ? 185  MET A CE  1 
ATOM   1507 N  N   . ASN A 1 186 ? -10.872 -32.475 13.310  1.00 41.06  ? 186  ASN A N   1 
ATOM   1508 C  CA  . ASN A 1 186 ? -10.505 -33.879 13.189  1.00 41.41  ? 186  ASN A CA  1 
ATOM   1509 C  C   . ASN A 1 186 ? -11.583 -34.675 12.478  1.00 40.23  ? 186  ASN A C   1 
ATOM   1510 O  O   . ASN A 1 186 ? -11.276 -35.649 11.787  1.00 42.55  ? 186  ASN A O   1 
ATOM   1511 C  CB  . ASN A 1 186 ? -10.234 -34.464 14.580  1.00 39.62  ? 186  ASN A CB  1 
ATOM   1512 C  CG  . ASN A 1 186 ? -9.657  -35.873 14.521  1.00 48.61  ? 186  ASN A CG  1 
ATOM   1513 O  OD1 . ASN A 1 186 ? -10.389 -36.862 14.627  1.00 49.20  ? 186  ASN A OD1 1 
ATOM   1514 N  ND2 . ASN A 1 186 ? -8.340  -35.968 14.347  1.00 44.96  ? 186  ASN A ND2 1 
ATOM   1515 N  N   . LYS A 1 187 ? -12.851 -34.287 12.633  1.00 40.73  ? 187  LYS A N   1 
ATOM   1516 C  CA  . LYS A 1 187 ? -13.923 -35.029 11.982  1.00 44.70  ? 187  LYS A CA  1 
ATOM   1517 C  C   . LYS A 1 187 ? -13.900 -34.865 10.461  1.00 43.06  ? 187  LYS A C   1 
ATOM   1518 O  O   . LYS A 1 187 ? -14.514 -35.670 9.753   1.00 44.53  ? 187  LYS A O   1 
ATOM   1519 C  CB  . LYS A 1 187 ? -15.275 -34.585 12.545  1.00 43.64  ? 187  LYS A CB  1 
ATOM   1520 C  CG  . LYS A 1 187 ? -16.417 -35.559 12.302  1.00 49.48  ? 187  LYS A CG  1 
ATOM   1521 C  CD  . LYS A 1 187 ? -17.729 -35.003 12.848  1.00 51.83  ? 187  LYS A CD  1 
ATOM   1522 C  CE  . LYS A 1 187 ? -17.559 -34.575 14.290  1.00 51.70  ? 187  LYS A CE  1 
ATOM   1523 N  NZ  . LYS A 1 187 ? -18.788 -34.752 15.134  1.00 59.61  ? 187  LYS A NZ  1 
ATOM   1524 N  N   . LEU A 1 188 ? -13.200 -33.850 9.951   1.00 39.42  ? 188  LEU A N   1 
ATOM   1525 C  CA  . LEU A 1 188 ? -13.160 -33.621 8.510   1.00 42.52  ? 188  LEU A CA  1 
ATOM   1526 C  C   . LEU A 1 188 ? -12.674 -34.858 7.756   1.00 42.98  ? 188  LEU A C   1 
ATOM   1527 O  O   . LEU A 1 188 ? -13.174 -35.166 6.671   1.00 43.89  ? 188  LEU A O   1 
ATOM   1528 C  CB  . LEU A 1 188 ? -12.270 -32.416 8.199   1.00 38.03  ? 188  LEU A CB  1 
ATOM   1529 C  CG  . LEU A 1 188 ? -12.859 -31.079 8.671   1.00 40.02  ? 188  LEU A CG  1 
ATOM   1530 C  CD1 . LEU A 1 188 ? -11.881 -29.933 8.470   1.00 40.96  ? 188  LEU A CD1 1 
ATOM   1531 C  CD2 . LEU A 1 188 ? -14.207 -30.810 7.987   1.00 37.68  ? 188  LEU A CD2 1 
ATOM   1532 N  N   . GLN A 1 189 ? -11.717 -35.587 8.318   1.00 45.94  ? 189  GLN A N   1 
ATOM   1533 C  CA  . GLN A 1 189 ? -11.107 -36.719 7.629   1.00 47.69  ? 189  GLN A CA  1 
ATOM   1534 C  C   . GLN A 1 189 ? -11.736 -38.068 7.978   1.00 51.54  ? 189  GLN A C   1 
ATOM   1535 O  O   . GLN A 1 189 ? -11.292 -39.097 7.454   1.00 50.02  ? 189  GLN A O   1 
ATOM   1536 C  CB  . GLN A 1 189 ? -9.593  -36.727 7.909   1.00 48.07  ? 189  GLN A CB  1 
ATOM   1537 C  CG  . GLN A 1 189 ? -9.224  -36.689 9.384   1.00 48.04  ? 189  GLN A CG  1 
ATOM   1538 C  CD  . GLN A 1 189 ? -9.231  -38.042 10.051  1.00 54.19  ? 189  GLN A CD  1 
ATOM   1539 O  OE1 . GLN A 1 189 ? -8.623  -38.998 9.567   1.00 57.21  ? 189  GLN A OE1 1 
ATOM   1540 N  NE2 . GLN A 1 189 ? -9.943  -38.137 11.167  1.00 55.31  ? 189  GLN A NE2 1 
ATOM   1541 N  N   . ARG A 1 190 ? -12.778 -38.094 8.810   1.00 47.44  ? 190  ARG A N   1 
ATOM   1542 C  CA  . ARG A 1 190 ? -13.391 -39.349 9.244   1.00 50.11  ? 190  ARG A CA  1 
ATOM   1543 C  C   . ARG A 1 190 ? -14.285 -39.908 8.148   1.00 56.09  ? 190  ARG A C   1 
ATOM   1544 O  O   . ARG A 1 190 ? -15.351 -39.352 7.862   1.00 55.87  ? 190  ARG A O   1 
ATOM   1545 C  CB  . ARG A 1 190 ? -14.195 -39.137 10.518  1.00 53.12  ? 190  ARG A CB  1 
ATOM   1546 C  CG  . ARG A 1 190 ? -13.451 -39.495 11.754  1.00 52.23  ? 190  ARG A CG  1 
ATOM   1547 C  CD  . ARG A 1 190 ? -14.248 -39.098 12.970  1.00 50.85  ? 190  ARG A CD  1 
ATOM   1548 N  NE  . ARG A 1 190 ? -13.405 -38.329 13.868  1.00 50.41  ? 190  ARG A NE  1 
ATOM   1549 C  CZ  . ARG A 1 190 ? -13.849 -37.666 14.921  1.00 48.99  ? 190  ARG A CZ  1 
ATOM   1550 N  NH1 . ARG A 1 190 ? -15.136 -37.650 15.235  1.00 46.37  ? 190  ARG A NH1 1 
ATOM   1551 N  NH2 . ARG A 1 190 ? -12.981 -37.014 15.681  1.00 45.58  ? 190  ARG A NH2 1 
ATOM   1552 N  N   . ALA A 1 191 ? -13.871 -41.029 7.550   1.00 58.31  ? 191  ALA A N   1 
ATOM   1553 C  CA  . ALA A 1 191 ? -14.689 -41.650 6.512   1.00 57.43  ? 191  ALA A CA  1 
ATOM   1554 C  C   . ALA A 1 191 ? -15.955 -42.267 7.098   1.00 60.96  ? 191  ALA A C   1 
ATOM   1555 O  O   . ALA A 1 191 ? -17.030 -42.189 6.490   1.00 58.67  ? 191  ALA A O   1 
ATOM   1556 C  CB  . ALA A 1 191 ? -13.872 -42.701 5.760   1.00 59.30  ? 191  ALA A CB  1 
ATOM   1557 N  N   . ASN A 1 192 ? -15.853 -42.882 8.278   1.00 58.03  ? 192  ASN A N   1 
ATOM   1558 C  CA  . ASN A 1 192 ? -16.988 -43.511 8.953   1.00 64.42  ? 192  ASN A CA  1 
ATOM   1559 C  C   . ASN A 1 192 ? -17.165 -42.850 10.315  1.00 58.47  ? 192  ASN A C   1 
ATOM   1560 O  O   . ASN A 1 192 ? -16.798 -43.419 11.355  1.00 57.90  ? 192  ASN A O   1 
ATOM   1561 C  CB  . ASN A 1 192 ? -16.803 -45.023 9.072   1.00 64.65  ? 192  ASN A CB  1 
ATOM   1562 C  CG  . ASN A 1 192 ? -16.093 -45.619 7.867   1.00 66.66  ? 192  ASN A CG  1 
ATOM   1563 O  OD1 . ASN A 1 192 ? -14.925 -46.007 7.941   1.00 71.61  ? 192  ASN A OD1 1 
ATOM   1564 N  ND2 . ASN A 1 192 ? -16.794 -45.668 6.739   1.00 65.81  ? 192  ASN A ND2 1 
ATOM   1565 N  N   . PRO A 1 193 ? -17.749 -41.650 10.348  1.00 60.28  ? 193  PRO A N   1 
ATOM   1566 C  CA  . PRO A 1 193 ? -17.892 -40.937 11.625  1.00 59.05  ? 193  PRO A CA  1 
ATOM   1567 C  C   . PRO A 1 193 ? -18.902 -41.570 12.562  1.00 61.70  ? 193  PRO A C   1 
ATOM   1568 O  O   . PRO A 1 193 ? -18.917 -41.222 13.750  1.00 58.30  ? 193  PRO A O   1 
ATOM   1569 C  CB  . PRO A 1 193 ? -18.338 -39.539 11.192  1.00 58.75  ? 193  PRO A CB  1 
ATOM   1570 C  CG  . PRO A 1 193 ? -19.038 -39.757 9.857   1.00 60.88  ? 193  PRO A CG  1 
ATOM   1571 C  CD  . PRO A 1 193 ? -18.650 -41.114 9.316   1.00 60.37  ? 193  PRO A CD  1 
ATOM   1572 N  N   . ASP A 1 194 ? -19.744 -42.478 12.074  1.00 59.48  ? 194  ASP A N   1 
ATOM   1573 C  CA  . ASP A 1 194 ? -20.678 -43.191 12.932  1.00 61.34  ? 194  ASP A CA  1 
ATOM   1574 C  C   . ASP A 1 194 ? -20.114 -44.506 13.453  1.00 64.72  ? 194  ASP A C   1 
ATOM   1575 O  O   . ASP A 1 194 ? -20.840 -45.251 14.121  1.00 65.81  ? 194  ASP A O   1 
ATOM   1576 C  CB  . ASP A 1 194 ? -21.996 -43.433 12.197  1.00 64.11  ? 194  ASP A CB  1 
ATOM   1577 C  CG  . ASP A 1 194 ? -22.812 -42.166 12.042  1.00 67.40  ? 194  ASP A CG  1 
ATOM   1578 O  OD1 . ASP A 1 194 ? -22.671 -41.255 12.892  1.00 65.78  ? 194  ASP A OD1 1 
ATOM   1579 O  OD2 . ASP A 1 194 ? -23.583 -42.074 11.068  1.00 73.79  ? 194  ASP A OD2 1 
ATOM   1580 N  N   . ASP A 1 195 ? -18.844 -44.806 13.175  1.00 60.92  ? 195  ASP A N   1 
ATOM   1581 C  CA  . ASP A 1 195 ? -18.217 -45.975 13.779  1.00 65.91  ? 195  ASP A CA  1 
ATOM   1582 C  C   . ASP A 1 195 ? -18.193 -45.829 15.298  1.00 66.97  ? 195  ASP A C   1 
ATOM   1583 O  O   . ASP A 1 195 ? -17.795 -44.771 15.807  1.00 65.80  ? 195  ASP A O   1 
ATOM   1584 C  CB  . ASP A 1 195 ? -16.794 -46.169 13.260  1.00 67.41  ? 195  ASP A CB  1 
ATOM   1585 C  CG  . ASP A 1 195 ? -16.135 -47.421 13.826  1.00 71.25  ? 195  ASP A CG  1 
ATOM   1586 O  OD1 . ASP A 1 195 ? -16.650 -48.529 13.568  1.00 78.58  ? 195  ASP A OD1 1 
ATOM   1587 O  OD2 . ASP A 1 195 ? -15.110 -47.304 14.530  1.00 68.63  ? 195  ASP A OD2 1 
ATOM   1588 N  N   . PRO A 1 196 ? -18.570 -46.866 16.053  1.00 69.21  ? 196  PRO A N   1 
ATOM   1589 C  CA  . PRO A 1 196 ? -18.615 -46.741 17.518  1.00 64.82  ? 196  PRO A CA  1 
ATOM   1590 C  C   . PRO A 1 196 ? -17.292 -46.290 18.123  1.00 65.07  ? 196  PRO A C   1 
ATOM   1591 O  O   . PRO A 1 196 ? -17.253 -45.852 19.277  1.00 65.38  ? 196  PRO A O   1 
ATOM   1592 C  CB  . PRO A 1 196 ? -18.987 -48.157 17.978  1.00 67.90  ? 196  PRO A CB  1 
ATOM   1593 C  CG  . PRO A 1 196 ? -19.689 -48.762 16.811  1.00 68.78  ? 196  PRO A CG  1 
ATOM   1594 C  CD  . PRO A 1 196 ? -19.008 -48.196 15.596  1.00 69.66  ? 196  PRO A CD  1 
ATOM   1595 N  N   . ALA A 1 197 ? -16.202 -46.389 17.358  1.00 63.00  ? 197  ALA A N   1 
ATOM   1596 C  CA  . ALA A 1 197 ? -14.917 -45.890 17.832  1.00 64.26  ? 197  ALA A CA  1 
ATOM   1597 C  C   . ALA A 1 197 ? -14.968 -44.412 18.199  1.00 63.54  ? 197  ALA A C   1 
ATOM   1598 O  O   . ALA A 1 197 ? -14.137 -43.950 18.988  1.00 62.44  ? 197  ALA A O   1 
ATOM   1599 C  CB  . ALA A 1 197 ? -13.839 -46.120 16.774  1.00 61.88  ? 197  ALA A CB  1 
ATOM   1600 N  N   . TYR A 1 198 ? -15.916 -43.657 17.644  1.00 62.12  ? 198  TYR A N   1 
ATOM   1601 C  CA  . TYR A 1 198 ? -16.039 -42.235 17.930  1.00 61.61  ? 198  TYR A CA  1 
ATOM   1602 C  C   . TYR A 1 198 ? -17.189 -41.935 18.883  1.00 58.73  ? 198  TYR A C   1 
ATOM   1603 O  O   . TYR A 1 198 ? -17.692 -40.805 18.906  1.00 52.04  ? 198  TYR A O   1 
ATOM   1604 C  CB  . TYR A 1 198 ? -16.222 -41.448 16.635  1.00 58.47  ? 198  TYR A CB  1 
ATOM   1605 C  CG  . TYR A 1 198 ? -15.180 -41.737 15.585  1.00 54.49  ? 198  TYR A CG  1 
ATOM   1606 C  CD1 . TYR A 1 198 ? -15.523 -42.406 14.419  1.00 59.01  ? 198  TYR A CD1 1 
ATOM   1607 C  CD2 . TYR A 1 198 ? -13.855 -41.367 15.766  1.00 56.09  ? 198  TYR A CD2 1 
ATOM   1608 C  CE1 . TYR A 1 198 ? -14.586 -42.680 13.449  1.00 58.37  ? 198  TYR A CE1 1 
ATOM   1609 C  CE2 . TYR A 1 198 ? -12.901 -41.645 14.798  1.00 57.22  ? 198  TYR A CE2 1 
ATOM   1610 C  CZ  . TYR A 1 198 ? -13.276 -42.303 13.642  1.00 58.88  ? 198  TYR A CZ  1 
ATOM   1611 O  OH  . TYR A 1 198 ? -12.346 -42.583 12.664  1.00 67.60  ? 198  TYR A OH  1 
ATOM   1612 N  N   . ASP A 1 199 ? -17.642 -42.934 19.643  1.00 58.40  ? 199  ASP A N   1 
ATOM   1613 C  CA  . ASP A 1 199 ? -18.678 -42.688 20.638  1.00 58.52  ? 199  ASP A CA  1 
ATOM   1614 C  C   . ASP A 1 199 ? -18.201 -41.686 21.676  1.00 55.72  ? 199  ASP A C   1 
ATOM   1615 O  O   . ASP A 1 199 ? -18.928 -40.754 22.038  1.00 54.41  ? 199  ASP A O   1 
ATOM   1616 C  CB  . ASP A 1 199 ? -19.087 -43.998 21.311  1.00 60.71  ? 199  ASP A CB  1 
ATOM   1617 C  CG  . ASP A 1 199 ? -19.934 -44.866 20.420  1.00 63.20  ? 199  ASP A CG  1 
ATOM   1618 O  OD1 . ASP A 1 199 ? -20.546 -44.326 19.475  1.00 63.17  ? 199  ASP A OD1 1 
ATOM   1619 O  OD2 . ASP A 1 199 ? -19.998 -46.086 20.676  1.00 66.98  ? 199  ASP A OD2 1 
ATOM   1620 N  N   . GLU A 1 200 ? -16.974 -41.866 22.169  1.00 54.78  ? 200  GLU A N   1 
ATOM   1621 C  CA  . GLU A 1 200 ? -16.433 -40.943 23.161  1.00 58.64  ? 200  GLU A CA  1 
ATOM   1622 C  C   . GLU A 1 200 ? -16.311 -39.534 22.595  1.00 55.01  ? 200  GLU A C   1 
ATOM   1623 O  O   . GLU A 1 200 ? -16.647 -38.558 23.274  1.00 51.31  ? 200  GLU A O   1 
ATOM   1624 C  CB  . GLU A 1 200 ? -15.080 -41.448 23.668  1.00 57.41  ? 200  GLU A CB  1 
ATOM   1625 C  CG  . GLU A 1 200 ? -14.332 -40.463 24.555  1.00 60.63  ? 200  GLU A CG  1 
ATOM   1626 C  CD  . GLU A 1 200 ? -15.079 -40.096 25.837  1.00 65.79  ? 200  GLU A CD  1 
ATOM   1627 O  OE1 . GLU A 1 200 ? -16.060 -40.788 26.196  1.00 65.29  ? 200  GLU A OE1 1 
ATOM   1628 O  OE2 . GLU A 1 200 ? -14.685 -39.096 26.481  1.00 67.59  ? 200  GLU A OE2 1 
ATOM   1629 N  N   . ASN A 1 201 ? -15.830 -39.405 21.353  1.00 54.04  ? 201  ASN A N   1 
ATOM   1630 C  CA  . ASN A 1 201 ? -15.807 -38.098 20.697  1.00 52.32  ? 201  ASN A CA  1 
ATOM   1631 C  C   . ASN A 1 201 ? -17.185 -37.455 20.733  1.00 52.33  ? 201  ASN A C   1 
ATOM   1632 O  O   . ASN A 1 201 ? -17.327 -36.261 21.029  1.00 49.91  ? 201  ASN A O   1 
ATOM   1633 C  CB  . ASN A 1 201 ? -15.335 -38.234 19.245  1.00 51.19  ? 201  ASN A CB  1 
ATOM   1634 C  CG  . ASN A 1 201 ? -13.959 -38.850 19.129  1.00 54.84  ? 201  ASN A CG  1 
ATOM   1635 O  OD1 . ASN A 1 201 ? -13.816 -40.072 19.102  1.00 61.51  ? 201  ASN A OD1 1 
ATOM   1636 N  ND2 . ASN A 1 201 ? -12.938 -38.007 19.042  1.00 56.29  ? 201  ASN A ND2 1 
ATOM   1637 N  N   . LYS A 1 202 ? -18.219 -38.240 20.425  1.00 49.44  ? 202  LYS A N   1 
ATOM   1638 C  CA  . LYS A 1 202 ? -19.569 -37.696 20.401  1.00 50.49  ? 202  LYS A CA  1 
ATOM   1639 C  C   . LYS A 1 202 ? -19.993 -37.245 21.793  1.00 50.30  ? 202  LYS A C   1 
ATOM   1640 O  O   . LYS A 1 202 ? -20.600 -36.179 21.952  1.00 48.52  ? 202  LYS A O   1 
ATOM   1641 C  CB  . LYS A 1 202 ? -20.545 -38.737 19.857  1.00 53.98  ? 202  LYS A CB  1 
ATOM   1642 C  CG  . LYS A 1 202 ? -20.905 -38.568 18.390  1.00 56.34  ? 202  LYS A CG  1 
ATOM   1643 C  CD  . LYS A 1 202 ? -21.241 -39.917 17.768  1.00 53.04  ? 202  LYS A CD  1 
ATOM   1644 C  CE  . LYS A 1 202 ? -21.154 -39.877 16.250  1.00 59.14  ? 202  LYS A CE  1 
ATOM   1645 N  NZ  . LYS A 1 202 ? -20.839 -41.218 15.701  1.00 61.69  ? 202  LYS A NZ  1 
ATOM   1646 N  N   . ARG A 1 203 ? -19.676 -38.044 22.816  1.00 49.88  ? 203  ARG A N   1 
ATOM   1647 C  CA  . ARG A 1 203 ? -20.043 -37.678 24.181  1.00 50.07  ? 203  ARG A CA  1 
ATOM   1648 C  C   . ARG A 1 203 ? -19.340 -36.393 24.600  1.00 48.11  ? 203  ARG A C   1 
ATOM   1649 O  O   . ARG A 1 203 ? -19.958 -35.486 25.176  1.00 49.18  ? 203  ARG A O   1 
ATOM   1650 C  CB  . ARG A 1 203 ? -19.688 -38.813 25.146  1.00 55.06  ? 203  ARG A CB  1 
ATOM   1651 C  CG  . ARG A 1 203 ? -20.042 -38.504 26.598  1.00 59.47  ? 203  ARG A CG  1 
ATOM   1652 C  CD  . ARG A 1 203 ? -19.230 -39.332 27.589  1.00 57.34  ? 203  ARG A CD  1 
ATOM   1653 N  NE  . ARG A 1 203 ? -17.854 -38.849 27.671  1.00 62.50  ? 203  ARG A NE  1 
ATOM   1654 C  CZ  . ARG A 1 203 ? -17.495 -37.696 28.224  1.00 63.43  ? 203  ARG A CZ  1 
ATOM   1655 N  NH1 . ARG A 1 203 ? -18.384 -36.889 28.784  1.00 63.04  ? 203  ARG A NH1 1 
ATOM   1656 N  NH2 . ARG A 1 203 ? -16.211 -37.343 28.214  1.00 63.48  ? 203  ARG A NH2 1 
ATOM   1657 N  N   . GLN A 1 204 ? -18.036 -36.311 24.327  1.00 48.63  ? 204  GLN A N   1 
ATOM   1658 C  CA  . GLN A 1 204 ? -17.258 -35.133 24.689  1.00 49.02  ? 204  GLN A CA  1 
ATOM   1659 C  C   . GLN A 1 204 ? -17.749 -33.904 23.934  1.00 48.69  ? 204  GLN A C   1 
ATOM   1660 O  O   . GLN A 1 204 ? -17.886 -32.821 24.517  1.00 48.15  ? 204  GLN A O   1 
ATOM   1661 C  CB  . GLN A 1 204 ? -15.778 -35.384 24.398  1.00 50.65  ? 204  GLN A CB  1 
ATOM   1662 C  CG  . GLN A 1 204 ? -14.855 -34.239 24.775  1.00 52.85  ? 204  GLN A CG  1 
ATOM   1663 C  CD  . GLN A 1 204 ? -14.909 -33.926 26.255  1.00 55.08  ? 204  GLN A CD  1 
ATOM   1664 O  OE1 . GLN A 1 204 ? -15.521 -32.940 26.680  1.00 54.53  ? 204  GLN A OE1 1 
ATOM   1665 N  NE2 . GLN A 1 204 ? -14.289 -34.784 27.054  1.00 59.67  ? 204  GLN A NE2 1 
ATOM   1666 N  N   . PHE A 1 205 ? -18.005 -34.054 22.631  1.00 42.74  ? 205  PHE A N   1 
ATOM   1667 C  CA  . PHE A 1 205 ? -18.591 -32.972 21.844  1.00 47.64  ? 205  PHE A CA  1 
ATOM   1668 C  C   . PHE A 1 205 ? -19.865 -32.452 22.499  1.00 45.98  ? 205  PHE A C   1 
ATOM   1669 O  O   . PHE A 1 205 ? -20.024 -31.243 22.708  1.00 43.72  ? 205  PHE A O   1 
ATOM   1670 C  CB  . PHE A 1 205 ? -18.870 -33.473 20.425  1.00 44.44  ? 205  PHE A CB  1 
ATOM   1671 C  CG  . PHE A 1 205 ? -19.074 -32.380 19.399  1.00 42.93  ? 205  PHE A CG  1 
ATOM   1672 C  CD1 . PHE A 1 205 ? -18.070 -31.459 19.125  1.00 40.97  ? 205  PHE A CD1 1 
ATOM   1673 C  CD2 . PHE A 1 205 ? -20.243 -32.325 18.659  1.00 44.10  ? 205  PHE A CD2 1 
ATOM   1674 C  CE1 . PHE A 1 205 ? -18.256 -30.472 18.151  1.00 41.50  ? 205  PHE A CE1 1 
ATOM   1675 C  CE2 . PHE A 1 205 ? -20.435 -31.344 17.680  1.00 42.70  ? 205  PHE A CE2 1 
ATOM   1676 C  CZ  . PHE A 1 205 ? -19.446 -30.422 17.431  1.00 47.27  ? 205  PHE A CZ  1 
ATOM   1677 N  N   . GLN A 1 206 ? -20.778 -33.360 22.847  1.00 44.87  ? 206  GLN A N   1 
ATOM   1678 C  CA  . GLN A 1 206 ? -22.039 -32.949 23.457  1.00 48.43  ? 206  GLN A CA  1 
ATOM   1679 C  C   . GLN A 1 206 ? -21.794 -32.225 24.776  1.00 49.72  ? 206  GLN A C   1 
ATOM   1680 O  O   . GLN A 1 206 ? -22.449 -31.217 25.083  1.00 46.12  ? 206  GLN A O   1 
ATOM   1681 C  CB  . GLN A 1 206 ? -22.923 -34.174 23.670  1.00 48.06  ? 206  GLN A CB  1 
ATOM   1682 C  CG  . GLN A 1 206 ? -23.648 -34.590 22.408  1.00 56.05  ? 206  GLN A CG  1 
ATOM   1683 C  CD  . GLN A 1 206 ? -24.195 -33.399 21.648  1.00 59.04  ? 206  GLN A CD  1 
ATOM   1684 O  OE1 . GLN A 1 206 ? -24.841 -32.519 22.227  1.00 60.27  ? 206  GLN A OE1 1 
ATOM   1685 N  NE2 . GLN A 1 206 ? -23.893 -33.335 20.353  1.00 55.01  ? 206  GLN A NE2 1 
ATOM   1686 N  N   . GLU A 1 207 ? -20.841 -32.724 25.560  1.00 47.97  ? 207  GLU A N   1 
ATOM   1687 C  CA  . GLU A 1 207 ? -20.512 -32.106 26.836  1.00 48.68  ? 207  GLU A CA  1 
ATOM   1688 C  C   . GLU A 1 207 ? -19.975 -30.694 26.638  1.00 47.51  ? 207  GLU A C   1 
ATOM   1689 O  O   . GLU A 1 207 ? -20.297 -29.781 27.408  1.00 44.10  ? 207  GLU A O   1 
ATOM   1690 C  CB  . GLU A 1 207 ? -19.498 -32.981 27.570  1.00 50.43  ? 207  GLU A CB  1 
ATOM   1691 C  CG  . GLU A 1 207 ? -18.969 -32.422 28.869  1.00 55.17  ? 207  GLU A CG  1 
ATOM   1692 C  CD  . GLU A 1 207 ? -17.997 -33.383 29.534  1.00 61.39  ? 207  GLU A CD  1 
ATOM   1693 O  OE1 . GLU A 1 207 ? -18.434 -34.492 29.921  1.00 63.06  ? 207  GLU A OE1 1 
ATOM   1694 O  OE2 . GLU A 1 207 ? -16.799 -33.031 29.658  1.00 64.45  ? 207  GLU A OE2 1 
ATOM   1695 N  N   . ASP A 1 208 ? -19.145 -30.496 25.615  1.00 43.45  ? 208  ASP A N   1 
ATOM   1696 C  CA  . ASP A 1 208 ? -18.623 -29.160 25.361  1.00 43.01  ? 208  ASP A CA  1 
ATOM   1697 C  C   . ASP A 1 208 ? -19.711 -28.225 24.852  1.00 42.04  ? 208  ASP A C   1 
ATOM   1698 O  O   . ASP A 1 208 ? -19.691 -27.027 25.159  1.00 44.94  ? 208  ASP A O   1 
ATOM   1699 C  CB  . ASP A 1 208 ? -17.459 -29.237 24.380  1.00 43.99  ? 208  ASP A CB  1 
ATOM   1700 C  CG  . ASP A 1 208 ? -16.245 -29.890 24.987  1.00 45.21  ? 208  ASP A CG  1 
ATOM   1701 O  OD1 . ASP A 1 208 ? -15.981 -29.635 26.180  1.00 48.58  ? 208  ASP A OD1 1 
ATOM   1702 O  OD2 . ASP A 1 208 ? -15.564 -30.669 24.283  1.00 46.96  ? 208  ASP A OD2 1 
ATOM   1703 N  N   . ILE A 1 209 ? -20.676 -28.748 24.096  1.00 42.23  ? 209  ILE A N   1 
ATOM   1704 C  CA  . ILE A 1 209 ? -21.789 -27.920 23.644  1.00 41.97  ? 209  ILE A CA  1 
ATOM   1705 C  C   . ILE A 1 209 ? -22.647 -27.485 24.830  1.00 45.76  ? 209  ILE A C   1 
ATOM   1706 O  O   . ILE A 1 209 ? -23.143 -26.349 24.879  1.00 44.20  ? 209  ILE A O   1 
ATOM   1707 C  CB  . ILE A 1 209 ? -22.601 -28.671 22.572  1.00 44.74  ? 209  ILE A CB  1 
ATOM   1708 C  CG1 . ILE A 1 209 ? -21.738 -28.858 21.309  1.00 43.90  ? 209  ILE A CG1 1 
ATOM   1709 C  CG2 . ILE A 1 209 ? -23.878 -27.933 22.256  1.00 44.50  ? 209  ILE A CG2 1 
ATOM   1710 C  CD1 . ILE A 1 209 ? -22.345 -29.768 20.256  1.00 43.16  ? 209  ILE A CD1 1 
ATOM   1711 N  N   . LYS A 1 210 ? -22.816 -28.368 25.818  1.00 45.17  ? 210  LYS A N   1 
ATOM   1712 C  CA  . LYS A 1 210 ? -23.568 -28.005 27.017  1.00 42.59  ? 210  LYS A CA  1 
ATOM   1713 C  C   . LYS A 1 210 ? -22.855 -26.923 27.822  1.00 44.46  ? 210  LYS A C   1 
ATOM   1714 O  O   . LYS A 1 210 ? -23.497 -25.988 28.314  1.00 43.50  ? 210  LYS A O   1 
ATOM   1715 C  CB  . LYS A 1 210 ? -23.805 -29.248 27.877  1.00 43.79  ? 210  LYS A CB  1 
ATOM   1716 C  CG  . LYS A 1 210 ? -24.463 -28.975 29.237  1.00 50.53  ? 210  LYS A CG  1 
ATOM   1717 C  CD  . LYS A 1 210 ? -25.991 -28.944 29.155  1.00 52.77  ? 210  LYS A CD  1 
ATOM   1718 C  CE  . LYS A 1 210 ? -26.624 -28.498 30.476  1.00 56.17  ? 210  LYS A CE  1 
ATOM   1719 N  NZ  . LYS A 1 210 ? -25.793 -28.882 31.655  1.00 54.74  ? 210  LYS A NZ  1 
ATOM   1720 N  N   . VAL A 1 211 ? -21.532 -27.042 27.989  1.00 41.03  ? 211  VAL A N   1 
ATOM   1721 C  CA  . VAL A 1 211 ? -20.776 -26.017 28.709  1.00 46.00  ? 211  VAL A CA  1 
ATOM   1722 C  C   . VAL A 1 211 ? -20.987 -24.656 28.059  1.00 45.17  ? 211  VAL A C   1 
ATOM   1723 O  O   . VAL A 1 211 ? -21.213 -23.644 28.735  1.00 40.53  ? 211  VAL A O   1 
ATOM   1724 C  CB  . VAL A 1 211 ? -19.281 -26.392 28.764  1.00 45.11  ? 211  VAL A CB  1 
ATOM   1725 C  CG1 . VAL A 1 211 ? -18.428 -25.208 29.226  1.00 47.12  ? 211  VAL A CG1 1 
ATOM   1726 C  CG2 . VAL A 1 211 ? -19.064 -27.592 29.679  1.00 43.01  ? 211  VAL A CG2 1 
ATOM   1727 N  N   . MET A 1 212 ? -20.935 -24.615 26.725  1.00 41.41  ? 212  MET A N   1 
ATOM   1728 C  CA  . MET A 1 212 ? -21.066 -23.347 26.024  1.00 43.37  ? 212  MET A CA  1 
ATOM   1729 C  C   . MET A 1 212 ? -22.476 -22.791 26.181  1.00 42.34  ? 212  MET A C   1 
ATOM   1730 O  O   . MET A 1 212 ? -22.655 -21.590 26.417  1.00 41.96  ? 212  MET A O   1 
ATOM   1731 C  CB  . MET A 1 212 ? -20.684 -23.544 24.552  1.00 42.02  ? 212  MET A CB  1 
ATOM   1732 C  CG  . MET A 1 212 ? -19.167 -23.670 24.356  1.00 40.24  ? 212  MET A CG  1 
ATOM   1733 S  SD  . MET A 1 212 ? -18.575 -23.587 22.633  1.00 45.34  ? 212  MET A SD  1 
ATOM   1734 C  CE  . MET A 1 212 ? -19.250 -25.098 21.942  1.00 42.54  ? 212  MET A CE  1 
ATOM   1735 N  N   . ASN A 1 213 ? -23.484 -23.664 26.107  1.00 39.62  ? 213  ASN A N   1 
ATOM   1736 C  CA  . ASN A 1 213 ? -24.875 -23.233 26.224  1.00 44.25  ? 213  ASN A CA  1 
ATOM   1737 C  C   . ASN A 1 213 ? -25.218 -22.812 27.649  1.00 45.85  ? 213  ASN A C   1 
ATOM   1738 O  O   . ASN A 1 213 ? -26.027 -21.899 27.852  1.00 46.43  ? 213  ASN A O   1 
ATOM   1739 C  CB  . ASN A 1 213 ? -25.805 -24.354 25.769  1.00 43.44  ? 213  ASN A CB  1 
ATOM   1740 C  CG  . ASN A 1 213 ? -26.185 -24.228 24.320  1.00 50.57  ? 213  ASN A CG  1 
ATOM   1741 O  OD1 . ASN A 1 213 ? -27.171 -23.572 23.986  1.00 59.10  ? 213  ASN A OD1 1 
ATOM   1742 N  ND2 . ASN A 1 213 ? -25.408 -24.856 23.443  1.00 46.24  ? 213  ASN A ND2 1 
ATOM   1743 N  N   . ASP A 1 214 ? -24.648 -23.495 28.645  1.00 43.23  ? 214  ASP A N   1 
ATOM   1744 C  CA  . ASP A 1 214 ? -24.836 -23.083 30.034  1.00 43.41  ? 214  ASP A CA  1 
ATOM   1745 C  C   . ASP A 1 214 ? -24.411 -21.634 30.241  1.00 43.65  ? 214  ASP A C   1 
ATOM   1746 O  O   . ASP A 1 214 ? -25.065 -20.886 30.976  1.00 42.27  ? 214  ASP A O   1 
ATOM   1747 C  CB  . ASP A 1 214 ? -24.030 -23.986 30.968  1.00 41.77  ? 214  ASP A CB  1 
ATOM   1748 C  CG  . ASP A 1 214 ? -24.678 -25.339 31.190  1.00 48.64  ? 214  ASP A CG  1 
ATOM   1749 O  OD1 . ASP A 1 214 ? -25.848 -25.515 30.808  1.00 46.33  ? 214  ASP A OD1 1 
ATOM   1750 O  OD2 . ASP A 1 214 ? -24.003 -26.227 31.748  1.00 51.16  ? 214  ASP A OD2 1 
ATOM   1751 N  N   . LEU A 1 215 ? -23.299 -21.228 29.622  1.00 44.33  ? 215  LEU A N   1 
ATOM   1752 C  CA  . LEU A 1 215 ? -22.860 -19.843 29.743  1.00 39.05  ? 215  LEU A CA  1 
ATOM   1753 C  C   . LEU A 1 215 ? -23.817 -18.908 29.023  1.00 43.08  ? 215  LEU A C   1 
ATOM   1754 O  O   . LEU A 1 215 ? -24.123 -17.814 29.521  1.00 42.08  ? 215  LEU A O   1 
ATOM   1755 C  CB  . LEU A 1 215 ? -21.449 -19.674 29.182  1.00 42.06  ? 215  LEU A CB  1 
ATOM   1756 C  CG  . LEU A 1 215 ? -21.054 -18.207 29.360  1.00 48.14  ? 215  LEU A CG  1 
ATOM   1757 C  CD1 . LEU A 1 215 ? -20.252 -18.059 30.649  1.00 46.59  ? 215  LEU A CD1 1 
ATOM   1758 C  CD2 . LEU A 1 215 ? -20.333 -17.628 28.165  1.00 45.76  ? 215  LEU A CD2 1 
ATOM   1759 N  N   . VAL A 1 216 ? -24.291 -19.314 27.837  1.00 41.10  ? 216  VAL A N   1 
ATOM   1760 C  CA  . VAL A 1 216 ? -25.296 -18.521 27.133  1.00 42.53  ? 216  VAL A CA  1 
ATOM   1761 C  C   . VAL A 1 216 ? -26.512 -18.289 28.023  1.00 46.01  ? 216  VAL A C   1 
ATOM   1762 O  O   . VAL A 1 216 ? -27.024 -17.167 28.122  1.00 44.92  ? 216  VAL A O   1 
ATOM   1763 C  CB  . VAL A 1 216 ? -25.680 -19.191 25.803  1.00 43.41  ? 216  VAL A CB  1 
ATOM   1764 C  CG1 . VAL A 1 216 ? -26.791 -18.408 25.124  1.00 46.85  ? 216  VAL A CG1 1 
ATOM   1765 C  CG2 . VAL A 1 216 ? -24.467 -19.249 24.894  1.00 41.97  ? 216  VAL A CG2 1 
ATOM   1766 N  N   . ASP A 1 217 ? -26.995 -19.347 28.683  1.00 45.72  ? 217  ASP A N   1 
ATOM   1767 C  CA  . ASP A 1 217 ? -28.184 -19.205 29.517  1.00 45.21  ? 217  ASP A CA  1 
ATOM   1768 C  C   . ASP A 1 217 ? -27.960 -18.175 30.619  1.00 46.73  ? 217  ASP A C   1 
ATOM   1769 O  O   . ASP A 1 217 ? -28.855 -17.382 30.933  1.00 42.86  ? 217  ASP A O   1 
ATOM   1770 C  CB  . ASP A 1 217 ? -28.569 -20.559 30.116  1.00 51.44  ? 217  ASP A CB  1 
ATOM   1771 C  CG  . ASP A 1 217 ? -29.043 -21.550 29.067  1.00 50.84  ? 217  ASP A CG  1 
ATOM   1772 O  OD1 . ASP A 1 217 ? -29.398 -21.134 27.935  1.00 55.72  ? 217  ASP A OD1 1 
ATOM   1773 O  OD2 . ASP A 1 217 ? -29.045 -22.756 29.384  1.00 60.51  ? 217  ASP A OD2 1 
ATOM   1774 N  N   . LYS A 1 218 ? -26.764 -18.172 31.213  1.00 42.81  ? 218  LYS A N   1 
ATOM   1775 C  CA  . LYS A 1 218 ? -26.448 -17.202 32.260  1.00 45.45  ? 218  LYS A CA  1 
ATOM   1776 C  C   . LYS A 1 218 ? -26.420 -15.784 31.711  1.00 44.80  ? 218  LYS A C   1 
ATOM   1777 O  O   . LYS A 1 218 ? -26.949 -14.856 32.334  1.00 44.20  ? 218  LYS A O   1 
ATOM   1778 C  CB  . LYS A 1 218 ? -25.109 -17.554 32.902  1.00 43.04  ? 218  LYS A CB  1 
ATOM   1779 C  CG  . LYS A 1 218 ? -24.606 -16.552 33.955  1.00 49.85  ? 218  LYS A CG  1 
ATOM   1780 C  CD  . LYS A 1 218 ? -25.164 -16.851 35.345  1.00 56.23  ? 218  LYS A CD  1 
ATOM   1781 C  CE  . LYS A 1 218 ? -25.269 -15.596 36.226  1.00 57.29  ? 218  LYS A CE  1 
ATOM   1782 N  NZ  . LYS A 1 218 ? -24.032 -14.724 36.237  1.00 47.60  ? 218  LYS A NZ  1 
ATOM   1783 N  N   . ILE A 1 219 ? -25.799 -15.592 30.546  1.00 36.43  ? 219  ILE A N   1 
ATOM   1784 C  CA  . ILE A 1 219 ? -25.785 -14.270 29.937  1.00 36.91  ? 219  ILE A CA  1 
ATOM   1785 C  C   . ILE A 1 219 ? -27.207 -13.782 29.702  1.00 40.06  ? 219  ILE A C   1 
ATOM   1786 O  O   . ILE A 1 219 ? -27.522 -12.607 29.931  1.00 39.97  ? 219  ILE A O   1 
ATOM   1787 C  CB  . ILE A 1 219 ? -24.975 -14.303 28.627  1.00 39.47  ? 219  ILE A CB  1 
ATOM   1788 C  CG1 . ILE A 1 219 ? -23.487 -14.474 28.934  1.00 36.76  ? 219  ILE A CG1 1 
ATOM   1789 C  CG2 . ILE A 1 219 ? -25.270 -13.066 27.809  1.00 36.82  ? 219  ILE A CG2 1 
ATOM   1790 C  CD1 . ILE A 1 219 ? -22.635 -14.774 27.691  1.00 39.80  ? 219  ILE A CD1 1 
ATOM   1791 N  N   . ILE A 1 220 ? -28.086 -14.668 29.225  1.00 39.35  ? 220  ILE A N   1 
ATOM   1792 C  CA  . ILE A 1 220 ? -29.461 -14.261 28.956  1.00 43.12  ? 220  ILE A CA  1 
ATOM   1793 C  C   . ILE A 1 220 ? -30.197 -13.983 30.259  1.00 44.91  ? 220  ILE A C   1 
ATOM   1794 O  O   . ILE A 1 220 ? -30.891 -12.971 30.388  1.00 45.03  ? 220  ILE A O   1 
ATOM   1795 C  CB  . ILE A 1 220 ? -30.193 -15.316 28.110  1.00 43.85  ? 220  ILE A CB  1 
ATOM   1796 C  CG1 . ILE A 1 220 ? -29.659 -15.315 26.673  1.00 39.78  ? 220  ILE A CG1 1 
ATOM   1797 C  CG2 . ILE A 1 220 ? -31.687 -15.037 28.112  1.00 49.72  ? 220  ILE A CG2 1 
ATOM   1798 C  CD1 . ILE A 1 220 ? -30.030 -16.553 25.880  1.00 44.82  ? 220  ILE A CD1 1 
ATOM   1799 N  N   . ALA A 1 221 ? -30.054 -14.873 31.242  1.00 46.32  ? 221  ALA A N   1 
ATOM   1800 C  CA  . ALA A 1 221 ? -30.751 -14.683 32.515  1.00 47.69  ? 221  ALA A CA  1 
ATOM   1801 C  C   . ALA A 1 221 ? -30.313 -13.390 33.192  1.00 50.64  ? 221  ALA A C   1 
ATOM   1802 O  O   . ALA A 1 221 ? -31.147 -12.605 33.662  1.00 49.44  ? 221  ALA A O   1 
ATOM   1803 C  CB  . ALA A 1 221 ? -30.504 -15.878 33.436  1.00 46.87  ? 221  ALA A CB  1 
ATOM   1804 N  N   . ASP A 1 222 ? -28.999 -13.150 33.251  1.00 47.03  ? 222  ASP A N   1 
ATOM   1805 C  CA  . ASP A 1 222 ? -28.496 -11.933 33.880  1.00 49.47  ? 222  ASP A CA  1 
ATOM   1806 C  C   . ASP A 1 222 ? -29.072 -10.687 33.221  1.00 49.01  ? 222  ASP A C   1 
ATOM   1807 O  O   . ASP A 1 222 ? -29.430 -9.722  33.908  1.00 48.36  ? 222  ASP A O   1 
ATOM   1808 C  CB  . ASP A 1 222 ? -26.972 -11.904 33.818  1.00 43.92  ? 222  ASP A CB  1 
ATOM   1809 C  CG  . ASP A 1 222 ? -26.335 -12.895 34.765  1.00 50.91  ? 222  ASP A CG  1 
ATOM   1810 O  OD1 . ASP A 1 222 ? -27.083 -13.621 35.453  1.00 49.25  ? 222  ASP A OD1 1 
ATOM   1811 O  OD2 . ASP A 1 222 ? -25.089 -12.960 34.808  1.00 50.48  ? 222  ASP A OD2 1 
ATOM   1812 N  N   . ARG A 1 223 ? -29.147 -10.673 31.887  1.00 41.76  ? 223  ARG A N   1 
ATOM   1813 C  CA  . ARG A 1 223 ? -29.648 -9.484  31.213  1.00 40.80  ? 223  ARG A CA  1 
ATOM   1814 C  C   . ARG A 1 223 ? -31.113 -9.254  31.551  1.00 47.57  ? 223  ARG A C   1 
ATOM   1815 O  O   . ARG A 1 223 ? -31.515 -8.137  31.891  1.00 47.88  ? 223  ARG A O   1 
ATOM   1816 C  CB  . ARG A 1 223 ? -29.480 -9.610  29.696  1.00 40.04  ? 223  ARG A CB  1 
ATOM   1817 C  CG  . ARG A 1 223 ? -30.116 -8.452  28.924  1.00 39.20  ? 223  ARG A CG  1 
ATOM   1818 C  CD  . ARG A 1 223 ? -29.548 -7.096  29.343  1.00 42.98  ? 223  ARG A CD  1 
ATOM   1819 N  NE  . ARG A 1 223 ? -28.094 -7.068  29.206  1.00 40.20  ? 223  ARG A NE  1 
ATOM   1820 C  CZ  . ARG A 1 223 ? -27.449 -6.608  28.140  1.00 43.52  ? 223  ARG A CZ  1 
ATOM   1821 N  NH1 . ARG A 1 223 ? -28.094 -6.053  27.121  1.00 35.97  ? 223  ARG A NH1 1 
ATOM   1822 N  NH2 . ARG A 1 223 ? -26.123 -6.723  28.087  1.00 38.81  ? 223  ARG A NH2 1 
ATOM   1823 N  N   . LYS A 1 224 ? -31.932 -10.302 31.452  1.00 42.97  ? 224  LYS A N   1 
ATOM   1824 C  CA  . LYS A 1 224 ? -33.369 -10.091 31.621  1.00 55.46  ? 224  LYS A CA  1 
ATOM   1825 C  C   . LYS A 1 224 ? -33.745 -9.813  33.070  1.00 55.93  ? 224  LYS A C   1 
ATOM   1826 O  O   . LYS A 1 224 ? -34.832 -9.281  33.322  1.00 61.23  ? 224  LYS A O   1 
ATOM   1827 C  CB  . LYS A 1 224 ? -34.163 -11.279 31.065  1.00 57.42  ? 224  LYS A CB  1 
ATOM   1828 C  CG  . LYS A 1 224 ? -33.826 -12.646 31.640  1.00 60.88  ? 224  LYS A CG  1 
ATOM   1829 C  CD  . LYS A 1 224 ? -34.636 -13.729 30.911  1.00 64.12  ? 224  LYS A CD  1 
ATOM   1830 C  CE  . LYS A 1 224 ? -33.912 -15.081 30.866  1.00 59.30  ? 224  LYS A CE  1 
ATOM   1831 N  NZ  . LYS A 1 224 ? -34.372 -15.921 29.720  1.00 61.65  ? 224  LYS A NZ  1 
ATOM   1832 N  N   . ALA A 1 225 ? -32.872 -10.136 34.017  1.00 54.00  ? 225  ALA A N   1 
ATOM   1833 C  CA  . ALA A 1 225 ? -33.100 -9.807  35.418  1.00 58.07  ? 225  ALA A CA  1 
ATOM   1834 C  C   . ALA A 1 225 ? -32.459 -8.488  35.821  1.00 63.85  ? 225  ALA A C   1 
ATOM   1835 O  O   . ALA A 1 225 ? -32.721 -8.002  36.926  1.00 71.56  ? 225  ALA A O   1 
ATOM   1836 C  CB  . ALA A 1 225 ? -32.570 -10.929 36.317  1.00 55.47  ? 225  ALA A CB  1 
ATOM   1837 N  N   . SER A 1 226 ? -31.640 -7.898  34.955  1.00 60.06  ? 226  SER A N   1 
ATOM   1838 C  CA  . SER A 1 226 ? -30.891 -6.699  35.302  1.00 68.31  ? 226  SER A CA  1 
ATOM   1839 C  C   . SER A 1 226 ? -31.808 -5.492  35.441  1.00 77.29  ? 226  SER A C   1 
ATOM   1840 O  O   . SER A 1 226 ? -32.866 -5.407  34.811  1.00 73.26  ? 226  SER A O   1 
ATOM   1841 C  CB  . SER A 1 226 ? -29.829 -6.403  34.242  1.00 67.74  ? 226  SER A CB  1 
ATOM   1842 O  OG  . SER A 1 226 ? -29.259 -5.120  34.440  1.00 75.59  ? 226  SER A OG  1 
ATOM   1843 N  N   . GLY A 1 227 ? -31.379 -4.547  36.277  1.00 81.24  ? 227  GLY A N   1 
ATOM   1844 C  CA  . GLY A 1 227 ? -32.058 -3.275  36.417  1.00 83.44  ? 227  GLY A CA  1 
ATOM   1845 C  C   . GLY A 1 227 ? -31.352 -2.182  35.642  1.00 89.69  ? 227  GLY A C   1 
ATOM   1846 O  O   . GLY A 1 227 ? -31.941 -1.137  35.345  1.00 94.34  ? 227  GLY A O   1 
ATOM   1847 N  N   . GLU A 1 228 ? -30.084 -2.415  35.310  1.00 88.76  ? 228  GLU A N   1 
ATOM   1848 C  CA  . GLU A 1 228 ? -29.333 -1.461  34.511  1.00 87.68  ? 228  GLU A CA  1 
ATOM   1849 C  C   . GLU A 1 228 ? -29.863 -1.433  33.081  1.00 87.41  ? 228  GLU A C   1 
ATOM   1850 O  O   . GLU A 1 228 ? -30.503 -2.375  32.602  1.00 87.44  ? 228  GLU A O   1 
ATOM   1851 C  CB  . GLU A 1 228 ? -27.842 -1.806  34.511  1.00 88.72  ? 228  GLU A CB  1 
ATOM   1852 C  CG  . GLU A 1 228 ? -27.265 -2.153  35.882  1.00 90.77  ? 228  GLU A CG  1 
ATOM   1853 C  CD  . GLU A 1 228 ? -27.365 -1.008  36.875  1.00 94.28  ? 228  GLU A CD  1 
ATOM   1854 O  OE1 . GLU A 1 228 ? -27.229 0.162   36.455  1.00 92.53  ? 228  GLU A OE1 1 
ATOM   1855 O  OE2 . GLU A 1 228 ? -27.574 -1.279  38.078  1.00 96.60  ? 228  GLU A OE2 1 
ATOM   1856 N  N   . GLN A 1 229 ? -29.590 -0.329  32.396  1.00 87.61  ? 229  GLN A N   1 
ATOM   1857 C  CA  . GLN A 1 229 ? -30.016 -0.138  31.016  1.00 84.43  ? 229  GLN A CA  1 
ATOM   1858 C  C   . GLN A 1 229 ? -28.814 -0.288  30.098  1.00 79.37  ? 229  GLN A C   1 
ATOM   1859 O  O   . GLN A 1 229 ? -27.880 0.520   30.151  1.00 79.22  ? 229  GLN A O   1 
ATOM   1860 C  CB  . GLN A 1 229 ? -30.670 1.229   30.825  1.00 88.57  ? 229  GLN A CB  1 
ATOM   1861 C  CG  . GLN A 1 229 ? -31.964 1.375   31.589  1.00 93.29  ? 229  GLN A CG  1 
ATOM   1862 C  CD  . GLN A 1 229 ? -33.127 0.770   30.840  1.00 97.30  ? 229  GLN A CD  1 
ATOM   1863 O  OE1 . GLN A 1 229 ? -33.633 -0.289  31.211  1.00 97.64  ? 229  GLN A OE1 1 
ATOM   1864 N  NE2 . GLN A 1 229 ? -33.552 1.432   29.768  1.00 100.39 ? 229  GLN A NE2 1 
ATOM   1865 N  N   . SER A 1 230 ? -28.839 -1.319  29.263  1.00 72.95  ? 230  SER A N   1 
ATOM   1866 C  CA  . SER A 1 230 ? -27.798 -1.544  28.278  1.00 62.23  ? 230  SER A CA  1 
ATOM   1867 C  C   . SER A 1 230 ? -28.309 -1.184  26.888  1.00 59.65  ? 230  SER A C   1 
ATOM   1868 O  O   . SER A 1 230 ? -29.515 -1.178  26.616  1.00 55.32  ? 230  SER A O   1 
ATOM   1869 C  CB  . SER A 1 230 ? -27.314 -3.000  28.303  1.00 59.53  ? 230  SER A CB  1 
ATOM   1870 O  OG  . SER A 1 230 ? -26.424 -3.234  29.390  1.00 59.10  ? 230  SER A OG  1 
ATOM   1871 N  N   . ASP A 1 231 ? -27.360 -0.853  26.015  1.00 52.17  ? 231  ASP A N   1 
ATOM   1872 C  CA  . ASP A 1 231 ? -27.608 -0.654  24.607  1.00 51.96  ? 231  ASP A CA  1 
ATOM   1873 C  C   . ASP A 1 231 ? -26.428 -1.302  23.880  1.00 51.72  ? 231  ASP A C   1 
ATOM   1874 O  O   . ASP A 1 231 ? -25.555 -0.630  23.338  1.00 55.42  ? 231  ASP A O   1 
ATOM   1875 C  CB  . ASP A 1 231 ? -27.747 0.828   24.255  1.00 55.54  ? 231  ASP A CB  1 
ATOM   1876 C  CG  . ASP A 1 231 ? -28.102 1.054   22.794  1.00 61.42  ? 231  ASP A CG  1 
ATOM   1877 O  OD1 . ASP A 1 231 ? -28.654 0.132   22.156  1.00 62.98  ? 231  ASP A OD1 1 
ATOM   1878 O  OD2 . ASP A 1 231 ? -27.828 2.160   22.278  1.00 70.49  ? 231  ASP A OD2 1 
ATOM   1879 N  N   . ASP A 1 232 ? -26.387 -2.633  23.894  1.00 41.75  ? 232  ASP A N   1 
ATOM   1880 C  CA  . ASP A 1 232 ? -25.260 -3.326  23.279  1.00 41.37  ? 232  ASP A CA  1 
ATOM   1881 C  C   . ASP A 1 232 ? -25.725 -4.369  22.276  1.00 40.18  ? 232  ASP A C   1 
ATOM   1882 O  O   . ASP A 1 232 ? -26.882 -4.356  21.843  1.00 37.09  ? 232  ASP A O   1 
ATOM   1883 C  CB  . ASP A 1 232 ? -24.377 -3.949  24.369  1.00 37.20  ? 232  ASP A CB  1 
ATOM   1884 C  CG  . ASP A 1 232 ? -25.134 -4.918  25.286  1.00 40.94  ? 232  ASP A CG  1 
ATOM   1885 O  OD1 . ASP A 1 232 ? -26.245 -5.390  24.933  1.00 37.43  ? 232  ASP A OD1 1 
ATOM   1886 O  OD2 . ASP A 1 232 ? -24.592 -5.225  26.379  1.00 39.48  ? 232  ASP A OD2 1 
ATOM   1887 N  N   . LEU A 1 233 ? -24.831 -5.278  21.894  1.00 37.86  ? 233  LEU A N   1 
ATOM   1888 C  CA  . LEU A 1 233 ? -25.197 -6.295  20.916  1.00 34.94  ? 233  LEU A CA  1 
ATOM   1889 C  C   . LEU A 1 233 ? -26.349 -7.152  21.425  1.00 35.22  ? 233  LEU A C   1 
ATOM   1890 O  O   . LEU A 1 233 ? -27.290 -7.461  20.678  1.00 35.22  ? 233  LEU A O   1 
ATOM   1891 C  CB  . LEU A 1 233 ? -23.974 -7.158  20.598  1.00 36.16  ? 233  LEU A CB  1 
ATOM   1892 C  CG  . LEU A 1 233 ? -24.073 -8.310  19.610  1.00 37.19  ? 233  LEU A CG  1 
ATOM   1893 C  CD1 . LEU A 1 233 ? -24.475 -7.859  18.181  1.00 32.63  ? 233  LEU A CD1 1 
ATOM   1894 C  CD2 . LEU A 1 233 ? -22.716 -9.031  19.575  1.00 35.73  ? 233  LEU A CD2 1 
ATOM   1895 N  N   . LEU A 1 234 ? -26.295 -7.546  22.699  1.00 35.18  ? 234  LEU A N   1 
ATOM   1896 C  CA  . LEU A 1 234 ? -27.373 -8.341  23.272  1.00 33.54  ? 234  LEU A CA  1 
ATOM   1897 C  C   . LEU A 1 234 ? -28.694 -7.574  23.257  1.00 35.21  ? 234  LEU A C   1 
ATOM   1898 O  O   . LEU A 1 234 ? -29.759 -8.161  23.035  1.00 36.42  ? 234  LEU A O   1 
ATOM   1899 C  CB  . LEU A 1 234 ? -27.014 -8.750  24.700  1.00 34.50  ? 234  LEU A CB  1 
ATOM   1900 C  CG  . LEU A 1 234 ? -28.017 -9.692  25.370  1.00 34.01  ? 234  LEU A CG  1 
ATOM   1901 C  CD1 . LEU A 1 234 ? -28.255 -10.892 24.492  1.00 37.93  ? 234  LEU A CD1 1 
ATOM   1902 C  CD2 . LEU A 1 234 ? -27.497 -10.132 26.738  1.00 38.33  ? 234  LEU A CD2 1 
ATOM   1903 N  N   . THR A 1 235 ? -28.647 -6.266  23.516  1.00 35.90  ? 235  THR A N   1 
ATOM   1904 C  CA  . THR A 1 235 ? -29.860 -5.453  23.435  1.00 39.26  ? 235  THR A CA  1 
ATOM   1905 C  C   . THR A 1 235 ? -30.516 -5.585  22.068  1.00 40.62  ? 235  THR A C   1 
ATOM   1906 O  O   . THR A 1 235 ? -31.738 -5.750  21.963  1.00 37.29  ? 235  THR A O   1 
ATOM   1907 C  CB  . THR A 1 235 ? -29.548 -3.983  23.717  1.00 40.22  ? 235  THR A CB  1 
ATOM   1908 O  OG1 . THR A 1 235 ? -28.852 -3.863  24.961  1.00 39.26  ? 235  THR A OG1 1 
ATOM   1909 C  CG2 . THR A 1 235 ? -30.848 -3.180  23.780  1.00 39.99  ? 235  THR A CG2 1 
ATOM   1910 N  N   . HIS A 1 236 ? -29.718 -5.495  21.003  1.00 37.02  ? 236  HIS A N   1 
ATOM   1911 C  CA  . HIS A 1 236 ? -30.280 -5.630  19.663  1.00 38.97  ? 236  HIS A CA  1 
ATOM   1912 C  C   . HIS A 1 236 ? -30.818 -7.034  19.423  1.00 40.30  ? 236  HIS A C   1 
ATOM   1913 O  O   . HIS A 1 236 ? -31.873 -7.201  18.795  1.00 37.60  ? 236  HIS A O   1 
ATOM   1914 C  CB  . HIS A 1 236 ? -29.244 -5.270  18.601  1.00 37.47  ? 236  HIS A CB  1 
ATOM   1915 C  CG  . HIS A 1 236 ? -28.924 -3.809  18.533  1.00 45.40  ? 236  HIS A CG  1 
ATOM   1916 N  ND1 . HIS A 1 236 ? -28.090 -3.185  19.436  1.00 44.08  ? 236  HIS A ND1 1 
ATOM   1917 C  CD2 . HIS A 1 236 ? -29.350 -2.841  17.685  1.00 46.19  ? 236  HIS A CD2 1 
ATOM   1918 C  CE1 . HIS A 1 236 ? -27.994 -1.903  19.133  1.00 46.29  ? 236  HIS A CE1 1 
ATOM   1919 N  NE2 . HIS A 1 236 ? -28.750 -1.666  18.076  1.00 45.49  ? 236  HIS A NE2 1 
ATOM   1920 N  N   . MET A 1 237 ? -30.107 -8.060  19.901  1.00 35.83  ? 237  MET A N   1 
ATOM   1921 C  CA  . MET A 1 237 ? -30.594 -9.428  19.752  1.00 36.96  ? 237  MET A CA  1 
ATOM   1922 C  C   . MET A 1 237 ? -31.964 -9.602  20.387  1.00 40.12  ? 237  MET A C   1 
ATOM   1923 O  O   . MET A 1 237 ? -32.846 -10.250 19.812  1.00 40.33  ? 237  MET A O   1 
ATOM   1924 C  CB  . MET A 1 237 ? -29.610 -10.424 20.373  1.00 34.18  ? 237  MET A CB  1 
ATOM   1925 C  CG  . MET A 1 237 ? -28.390 -10.678 19.552  1.00 37.22  ? 237  MET A CG  1 
ATOM   1926 S  SD  . MET A 1 237 ? -27.327 -11.871 20.402  1.00 35.26  ? 237  MET A SD  1 
ATOM   1927 C  CE  . MET A 1 237 ? -25.764 -11.600 19.553  1.00 34.10  ? 237  MET A CE  1 
ATOM   1928 N  N   . LEU A 1 238 ? -32.156 -9.030  21.577  1.00 37.67  ? 238  LEU A N   1 
ATOM   1929 C  CA  . LEU A 1 238 ? -33.385 -9.255  22.329  1.00 39.63  ? 238  LEU A CA  1 
ATOM   1930 C  C   . LEU A 1 238 ? -34.509 -8.337  21.884  1.00 42.20  ? 238  LEU A C   1 
ATOM   1931 O  O   . LEU A 1 238 ? -35.680 -8.677  22.058  1.00 43.21  ? 238  LEU A O   1 
ATOM   1932 C  CB  . LEU A 1 238 ? -33.129 -9.077  23.830  1.00 39.83  ? 238  LEU A CB  1 
ATOM   1933 C  CG  . LEU A 1 238 ? -32.128 -10.046 24.479  1.00 41.27  ? 238  LEU A CG  1 
ATOM   1934 C  CD1 . LEU A 1 238 ? -31.841 -9.680  25.942  1.00 37.32  ? 238  LEU A CD1 1 
ATOM   1935 C  CD2 . LEU A 1 238 ? -32.643 -11.469 24.386  1.00 43.99  ? 238  LEU A CD2 1 
ATOM   1936 N  N   . ASN A 1 239 ? -34.191 -7.174  21.328  1.00 41.15  ? 239  ASN A N   1 
ATOM   1937 C  CA  . ASN A 1 239 ? -35.210 -6.164  21.084  1.00 43.61  ? 239  ASN A CA  1 
ATOM   1938 C  C   . ASN A 1 239 ? -35.321 -5.707  19.641  1.00 47.71  ? 239  ASN A C   1 
ATOM   1939 O  O   . ASN A 1 239 ? -36.387 -5.206  19.252  1.00 43.15  ? 239  ASN A O   1 
ATOM   1940 C  CB  . ASN A 1 239 ? -34.957 -4.942  21.976  1.00 43.91  ? 239  ASN A CB  1 
ATOM   1941 C  CG  . ASN A 1 239 ? -34.938 -5.306  23.441  1.00 49.79  ? 239  ASN A CG  1 
ATOM   1942 O  OD1 . ASN A 1 239 ? -33.888 -5.299  24.087  1.00 52.49  ? 239  ASN A OD1 1 
ATOM   1943 N  ND2 . ASN A 1 239 ? -36.107 -5.648  23.974  1.00 52.54  ? 239  ASN A ND2 1 
ATOM   1944 N  N   . GLY A 1 240 ? -34.280 -5.878  18.834  1.00 39.29  ? 240  GLY A N   1 
ATOM   1945 C  CA  . GLY A 1 240 ? -34.291 -5.308  17.511  1.00 40.21  ? 240  GLY A CA  1 
ATOM   1946 C  C   . GLY A 1 240 ? -35.312 -5.979  16.616  1.00 40.66  ? 240  GLY A C   1 
ATOM   1947 O  O   . GLY A 1 240 ? -35.589 -7.175  16.727  1.00 41.03  ? 240  GLY A O   1 
ATOM   1948 N  N   . LYS A 1 241 ? -35.868 -5.186  15.702  1.00 40.02  ? 241  LYS A N   1 
ATOM   1949 C  CA  . LYS A 1 241 ? -36.902 -5.643  14.785  1.00 42.97  ? 241  LYS A CA  1 
ATOM   1950 C  C   . LYS A 1 241 ? -36.382 -5.532  13.361  1.00 41.33  ? 241  LYS A C   1 
ATOM   1951 O  O   . LYS A 1 241 ? -35.879 -4.474  12.962  1.00 42.26  ? 241  LYS A O   1 
ATOM   1952 C  CB  . LYS A 1 241 ? -38.168 -4.806  14.937  1.00 46.69  ? 241  LYS A CB  1 
ATOM   1953 C  CG  . LYS A 1 241 ? -38.740 -4.802  16.343  1.00 50.75  ? 241  LYS A CG  1 
ATOM   1954 C  CD  . LYS A 1 241 ? -38.881 -6.197  16.914  1.00 49.02  ? 241  LYS A CD  1 
ATOM   1955 C  CE  . LYS A 1 241 ? -40.150 -6.299  17.755  1.00 59.24  ? 241  LYS A CE  1 
ATOM   1956 N  NZ  . LYS A 1 241 ? -39.864 -6.356  19.224  1.00 63.26  ? 241  LYS A NZ  1 
ATOM   1957 N  N   . ASP A 1 242 ? -36.500 -6.613  12.608  1.00 41.73  ? 242  ASP A N   1 
ATOM   1958 C  CA  . ASP A 1 242 ? -36.135 -6.619  11.200  1.00 43.10  ? 242  ASP A CA  1 
ATOM   1959 C  C   . ASP A 1 242 ? -37.062 -5.680  10.434  1.00 51.45  ? 242  ASP A C   1 
ATOM   1960 O  O   . ASP A 1 242 ? -38.287 -5.884  10.451  1.00 53.55  ? 242  ASP A O   1 
ATOM   1961 C  CB  . ASP A 1 242 ? -36.225 -8.048  10.659  1.00 41.89  ? 242  ASP A CB  1 
ATOM   1962 C  CG  . ASP A 1 242 ? -36.011 -8.140  9.147   1.00 42.75  ? 242  ASP A CG  1 
ATOM   1963 O  OD1 . ASP A 1 242 ? -35.533 -7.169  8.525   1.00 44.14  ? 242  ASP A OD1 1 
ATOM   1964 O  OD2 . ASP A 1 242 ? -36.299 -9.220  8.587   1.00 40.00  ? 242  ASP A OD2 1 
ATOM   1965 N  N   . PRO A 1 243 ? -36.543 -4.633  9.791   1.00 49.25  ? 243  PRO A N   1 
ATOM   1966 C  CA  . PRO A 1 243 ? -37.430 -3.742  9.023   1.00 55.17  ? 243  PRO A CA  1 
ATOM   1967 C  C   . PRO A 1 243 ? -38.262 -4.474  7.987   1.00 50.65  ? 243  PRO A C   1 
ATOM   1968 O  O   . PRO A 1 243 ? -39.402 -4.071  7.725   1.00 66.84  ? 243  PRO A O   1 
ATOM   1969 C  CB  . PRO A 1 243 ? -36.449 -2.754  8.373   1.00 54.43  ? 243  PRO A CB  1 
ATOM   1970 C  CG  . PRO A 1 243 ? -35.237 -2.787  9.274   1.00 53.15  ? 243  PRO A CG  1 
ATOM   1971 C  CD  . PRO A 1 243 ? -35.129 -4.228  9.683   1.00 46.80  ? 243  PRO A CD  1 
ATOM   1972 N  N   . GLU A 1 244 ? -37.731 -5.548  7.400   1.00 57.03  ? 244  GLU A N   1 
ATOM   1973 C  CA  . GLU A 1 244 ? -38.418 -6.307  6.358   1.00 54.86  ? 244  GLU A CA  1 
ATOM   1974 C  C   . GLU A 1 244 ? -39.541 -7.167  6.936   1.00 64.83  ? 244  GLU A C   1 
ATOM   1975 O  O   . GLU A 1 244 ? -40.712 -6.768  6.901   1.00 70.04  ? 244  GLU A O   1 
ATOM   1976 C  CB  . GLU A 1 244 ? -37.413 -7.170  5.582   1.00 54.46  ? 244  GLU A CB  1 
ATOM   1977 C  CG  . GLU A 1 244 ? -38.046 -8.085  4.543   1.00 61.73  ? 244  GLU A CG  1 
ATOM   1978 C  CD  . GLU A 1 244 ? -37.090 -9.139  3.998   1.00 67.29  ? 244  GLU A CD  1 
ATOM   1979 O  OE1 . GLU A 1 244 ? -35.856 -8.974  4.138   1.00 63.34  ? 244  GLU A OE1 1 
ATOM   1980 O  OE2 . GLU A 1 244 ? -37.580 -10.141 3.427   1.00 70.09  ? 244  GLU A OE2 1 
ATOM   1981 N  N   . THR A 1 245 ? -39.194 -8.344  7.475   1.00 59.88  ? 245  THR A N   1 
ATOM   1982 C  CA  . THR A 1 245 ? -40.185 -9.274  8.015   1.00 55.63  ? 245  THR A CA  1 
ATOM   1983 C  C   . THR A 1 245 ? -40.950 -8.709  9.207   1.00 55.10  ? 245  THR A C   1 
ATOM   1984 O  O   . THR A 1 245 ? -41.942 -9.318  9.619   1.00 62.58  ? 245  THR A O   1 
ATOM   1985 C  CB  . THR A 1 245 ? -39.513 -10.599 8.416   1.00 56.18  ? 245  THR A CB  1 
ATOM   1986 O  OG1 . THR A 1 245 ? -38.578 -10.383 9.488   1.00 45.32  ? 245  THR A OG1 1 
ATOM   1987 C  CG2 . THR A 1 245 ? -38.785 -11.241 7.215   1.00 56.09  ? 245  THR A CG2 1 
ATOM   1988 N  N   . GLY A 1 246 ? -40.518 -7.578  9.770   1.00 56.61  ? 246  GLY A N   1 
ATOM   1989 C  CA  . GLY A 1 246 ? -41.171 -6.960  10.911  1.00 56.08  ? 246  GLY A CA  1 
ATOM   1990 C  C   . GLY A 1 246 ? -40.896 -7.605  12.256  1.00 56.17  ? 246  GLY A C   1 
ATOM   1991 O  O   . GLY A 1 246 ? -41.096 -6.955  13.293  1.00 53.62  ? 246  GLY A O   1 
ATOM   1992 N  N   . GLU A 1 247 ? -40.399 -8.902  12.279  1.00 56.86  ? 247  GLU A N   1 
ATOM   1993 C  CA  . GLU A 1 247 ? -40.253 -9.728  13.468  1.00 48.96  ? 247  GLU A CA  1 
ATOM   1994 C  C   . GLU A 1 247 ? -38.906 -9.511  14.169  1.00 48.27  ? 247  GLU A C   1 
ATOM   1995 O  O   . GLU A 1 247 ? -37.922 -9.112  13.542  1.00 43.67  ? 247  GLU A O   1 
ATOM   1996 C  CB  . GLU A 1 247 ? -40.403 -11.211 13.105  1.00 52.82  ? 247  GLU A CB  1 
ATOM   1997 C  CG  . GLU A 1 247 ? -41.385 -11.507 11.950  1.00 51.68  ? 247  GLU A CG  1 
ATOM   1998 C  CD  . GLU A 1 247 ? -41.208 -12.901 11.354  1.00 56.81  ? 247  GLU A CD  1 
ATOM   1999 O  OE1 . GLU A 1 247 ? -40.110 -13.486 11.473  1.00 53.77  ? 247  GLU A OE1 1 
ATOM   2000 O  OE2 . GLU A 1 247 ? -42.183 -13.427 10.774  1.00 58.82  ? 247  GLU A OE2 1 
ATOM   2001 N  N   . PRO A 1 248 ? -38.837 -9.768  15.469  1.00 46.73  ? 248  PRO A N   1 
ATOM   2002 C  CA  . PRO A 1 248 ? -37.540 -9.898  16.135  1.00 42.56  ? 248  PRO A CA  1 
ATOM   2003 C  C   . PRO A 1 248 ? -37.052 -11.336 16.009  1.00 41.33  ? 248  PRO A C   1 
ATOM   2004 O  O   . PRO A 1 248 ? -37.776 -12.229 15.558  1.00 40.43  ? 248  PRO A O   1 
ATOM   2005 C  CB  . PRO A 1 248 ? -37.867 -9.539  17.589  1.00 46.19  ? 248  PRO A CB  1 
ATOM   2006 C  CG  . PRO A 1 248 ? -39.252 -10.083 17.771  1.00 50.46  ? 248  PRO A CG  1 
ATOM   2007 C  CD  . PRO A 1 248 ? -39.956 -9.914  16.419  1.00 49.96  ? 248  PRO A CD  1 
ATOM   2008 N  N   . LEU A 1 249 ? -35.789 -11.544 16.379  1.00 36.96  ? 249  LEU A N   1 
ATOM   2009 C  CA  . LEU A 1 249 ? -35.280 -12.905 16.450  1.00 38.30  ? 249  LEU A CA  1 
ATOM   2010 C  C   . LEU A 1 249 ? -36.069 -13.690 17.486  1.00 38.91  ? 249  LEU A C   1 
ATOM   2011 O  O   . LEU A 1 249 ? -36.481 -13.144 18.511  1.00 39.27  ? 249  LEU A O   1 
ATOM   2012 C  CB  . LEU A 1 249 ? -33.799 -12.911 16.825  1.00 32.39  ? 249  LEU A CB  1 
ATOM   2013 C  CG  . LEU A 1 249 ? -32.903 -12.124 15.875  1.00 35.69  ? 249  LEU A CG  1 
ATOM   2014 C  CD1 . LEU A 1 249 ? -31.457 -12.270 16.337  1.00 35.99  ? 249  LEU A CD1 1 
ATOM   2015 C  CD2 . LEU A 1 249 ? -33.068 -12.611 14.442  1.00 37.69  ? 249  LEU A CD2 1 
ATOM   2016 N  N   . ASP A 1 250 ? -36.284 -14.976 17.225  1.00 38.72  ? 250  ASP A N   1 
ATOM   2017 C  CA  . ASP A 1 250 ? -36.917 -15.783 18.258  1.00 42.72  ? 250  ASP A CA  1 
ATOM   2018 C  C   . ASP A 1 250 ? -35.846 -16.331 19.199  1.00 42.64  ? 250  ASP A C   1 
ATOM   2019 O  O   . ASP A 1 250 ? -34.642 -16.175 18.970  1.00 40.77  ? 250  ASP A O   1 
ATOM   2020 C  CB  . ASP A 1 250 ? -37.804 -16.871 17.625  1.00 46.78  ? 250  ASP A CB  1 
ATOM   2021 C  CG  . ASP A 1 250 ? -37.031 -17.955 16.889  1.00 49.98  ? 250  ASP A CG  1 
ATOM   2022 O  OD1 . ASP A 1 250 ? -35.800 -18.086 17.021  1.00 47.26  ? 250  ASP A OD1 1 
ATOM   2023 O  OD2 . ASP A 1 250 ? -37.682 -18.653 16.094  1.00 60.13  ? 250  ASP A OD2 1 
ATOM   2024 N  N   . ASP A 1 251 ? -36.297 -16.945 20.296  1.00 39.84  ? 251  ASP A N   1 
ATOM   2025 C  CA  . ASP A 1 251 ? -35.373 -17.330 21.358  1.00 45.62  ? 251  ASP A CA  1 
ATOM   2026 C  C   . ASP A 1 251 ? -34.347 -18.344 20.879  1.00 43.57  ? 251  ASP A C   1 
ATOM   2027 O  O   . ASP A 1 251 ? -33.172 -18.265 21.255  1.00 40.26  ? 251  ASP A O   1 
ATOM   2028 C  CB  . ASP A 1 251 ? -36.141 -17.889 22.554  1.00 46.97  ? 251  ASP A CB  1 
ATOM   2029 C  CG  . ASP A 1 251 ? -36.761 -16.804 23.396  1.00 53.10  ? 251  ASP A CG  1 
ATOM   2030 O  OD1 . ASP A 1 251 ? -36.511 -15.616 23.110  1.00 55.36  ? 251  ASP A OD1 1 
ATOM   2031 O  OD2 . ASP A 1 251 ? -37.489 -17.142 24.350  1.00 56.13  ? 251  ASP A OD2 1 
ATOM   2032 N  N   . GLU A 1 252 ? -34.771 -19.325 20.078  1.00 41.05  ? 252  GLU A N   1 
ATOM   2033 C  CA  . GLU A 1 252 ? -33.818 -20.322 19.597  1.00 41.97  ? 252  GLU A CA  1 
ATOM   2034 C  C   . GLU A 1 252 ? -32.714 -19.665 18.777  1.00 38.30  ? 252  GLU A C   1 
ATOM   2035 O  O   . GLU A 1 252 ? -31.528 -19.973 18.947  1.00 38.02  ? 252  GLU A O   1 
ATOM   2036 C  CB  . GLU A 1 252 ? -34.514 -21.399 18.761  1.00 43.01  ? 252  GLU A CB  1 
ATOM   2037 C  CG  . GLU A 1 252 ? -33.517 -22.469 18.314  1.00 43.26  ? 252  GLU A CG  1 
ATOM   2038 C  CD  . GLU A 1 252 ? -34.109 -23.542 17.408  1.00 53.12  ? 252  GLU A CD  1 
ATOM   2039 O  OE1 . GLU A 1 252 ? -34.106 -23.353 16.167  1.00 54.72  ? 252  GLU A OE1 1 
ATOM   2040 O  OE2 . GLU A 1 252 ? -34.566 -24.577 17.930  1.00 61.72  ? 252  GLU A OE2 1 
ATOM   2041 N  N   . ASN A 1 253 ? -33.083 -18.757 17.873  1.00 33.48  ? 253  ASN A N   1 
ATOM   2042 C  CA  . ASN A 1 253 ? -32.048 -18.127 17.061  1.00 33.57  ? 253  ASN A CA  1 
ATOM   2043 C  C   . ASN A 1 253 ? -31.150 -17.223 17.902  1.00 36.92  ? 253  ASN A C   1 
ATOM   2044 O  O   . ASN A 1 253 ? -29.934 -17.166 17.666  1.00 35.03  ? 253  ASN A O   1 
ATOM   2045 C  CB  . ASN A 1 253 ? -32.654 -17.339 15.909  1.00 33.77  ? 253  ASN A CB  1 
ATOM   2046 C  CG  . ASN A 1 253 ? -31.589 -16.847 14.953  1.00 34.89  ? 253  ASN A CG  1 
ATOM   2047 O  OD1 . ASN A 1 253 ? -31.250 -15.674 14.954  1.00 35.98  ? 253  ASN A OD1 1 
ATOM   2048 N  ND2 . ASN A 1 253 ? -31.015 -17.760 14.180  1.00 31.59  ? 253  ASN A ND2 1 
ATOM   2049 N  N   . ILE A 1 254 ? -31.720 -16.501 18.876  1.00 36.41  ? 254  ILE A N   1 
ATOM   2050 C  CA  . ILE A 1 254 ? -30.900 -15.664 19.757  1.00 32.73  ? 254  ILE A CA  1 
ATOM   2051 C  C   . ILE A 1 254 ? -29.781 -16.483 20.398  1.00 32.75  ? 254  ILE A C   1 
ATOM   2052 O  O   . ILE A 1 254 ? -28.617 -16.056 20.436  1.00 34.71  ? 254  ILE A O   1 
ATOM   2053 C  CB  . ILE A 1 254 ? -31.772 -14.978 20.829  1.00 35.42  ? 254  ILE A CB  1 
ATOM   2054 C  CG1 . ILE A 1 254 ? -32.648 -13.898 20.192  1.00 38.40  ? 254  ILE A CG1 1 
ATOM   2055 C  CG2 . ILE A 1 254 ? -30.870 -14.384 21.935  1.00 34.20  ? 254  ILE A CG2 1 
ATOM   2056 C  CD1 . ILE A 1 254 ? -33.728 -13.343 21.116  1.00 40.80  ? 254  ILE A CD1 1 
ATOM   2057 N  N   A ARG A 1 255 ? -30.116 -17.669 20.927  0.65 34.00  ? 255  ARG A N   1 
ATOM   2058 N  N   B ARG A 1 255 ? -30.121 -17.660 20.935  0.35 34.07  ? 255  ARG A N   1 
ATOM   2059 C  CA  A ARG A 1 255 ? -29.095 -18.509 21.551  0.65 36.23  ? 255  ARG A CA  1 
ATOM   2060 C  CA  B ARG A 1 255 ? -29.101 -18.509 21.544  0.35 36.26  ? 255  ARG A CA  1 
ATOM   2061 C  C   A ARG A 1 255 ? -27.989 -18.852 20.561  0.65 34.33  ? 255  ARG A C   1 
ATOM   2062 C  C   B ARG A 1 255 ? -27.992 -18.827 20.554  0.35 34.37  ? 255  ARG A C   1 
ATOM   2063 O  O   A ARG A 1 255 ? -26.802 -18.849 20.913  0.65 33.77  ? 255  ARG A O   1 
ATOM   2064 O  O   B ARG A 1 255 ? -26.804 -18.782 20.900  0.35 33.82  ? 255  ARG A O   1 
ATOM   2065 C  CB  A ARG A 1 255 ? -29.711 -19.796 22.109  0.65 39.92  ? 255  ARG A CB  1 
ATOM   2066 C  CB  B ARG A 1 255 ? -29.718 -19.806 22.064  0.35 39.92  ? 255  ARG A CB  1 
ATOM   2067 C  CG  A ARG A 1 255 ? -30.621 -19.612 23.323  0.65 42.03  ? 255  ARG A CG  1 
ATOM   2068 C  CG  B ARG A 1 255 ? -30.936 -19.627 22.940  0.35 42.36  ? 255  ARG A CG  1 
ATOM   2069 C  CD  A ARG A 1 255 ? -30.964 -20.957 23.962  0.65 43.45  ? 255  ARG A CD  1 
ATOM   2070 C  CD  B ARG A 1 255 ? -31.620 -20.960 23.170  0.35 45.32  ? 255  ARG A CD  1 
ATOM   2071 N  NE  A ARG A 1 255 ? -31.524 -21.907 23.004  0.65 49.48  ? 255  ARG A NE  1 
ATOM   2072 N  NE  B ARG A 1 255 ? -31.933 -21.167 24.577  0.35 49.10  ? 255  ARG A NE  1 
ATOM   2073 C  CZ  A ARG A 1 255 ? -32.818 -22.059 22.748  0.65 45.35  ? 255  ARG A CZ  1 
ATOM   2074 C  CZ  B ARG A 1 255 ? -31.033 -21.443 25.512  0.35 49.92  ? 255  ARG A CZ  1 
ATOM   2075 N  NH1 A ARG A 1 255 ? -33.736 -21.316 23.346  0.65 49.16  ? 255  ARG A NH1 1 
ATOM   2076 N  NH1 B ARG A 1 255 ? -29.753 -21.596 25.217  0.35 47.98  ? 255  ARG A NH1 1 
ATOM   2077 N  NH2 A ARG A 1 255 ? -33.200 -22.986 21.875  0.65 47.30  ? 255  ARG A NH2 1 
ATOM   2078 N  NH2 B ARG A 1 255 ? -31.430 -21.573 26.774  0.35 51.42  ? 255  ARG A NH2 1 
ATOM   2079 N  N   . TYR A 1 256 ? -28.362 -19.175 19.321  1.00 35.19  ? 256  TYR A N   1 
ATOM   2080 C  CA  . TYR A 1 256 ? -27.348 -19.445 18.305  1.00 30.95  ? 256  TYR A CA  1 
ATOM   2081 C  C   . TYR A 1 256 ? -26.483 -18.216 18.059  1.00 33.72  ? 256  TYR A C   1 
ATOM   2082 O  O   . TYR A 1 256 ? -25.262 -18.335 17.874  1.00 33.17  ? 256  TYR A O   1 
ATOM   2083 C  CB  . TYR A 1 256 ? -28.010 -19.892 17.005  1.00 32.49  ? 256  TYR A CB  1 
ATOM   2084 C  CG  . TYR A 1 256 ? -28.512 -21.312 17.051  1.00 34.01  ? 256  TYR A CG  1 
ATOM   2085 C  CD1 . TYR A 1 256 ? -27.760 -22.317 17.651  1.00 37.08  ? 256  TYR A CD1 1 
ATOM   2086 C  CD2 . TYR A 1 256 ? -29.752 -21.642 16.521  1.00 36.41  ? 256  TYR A CD2 1 
ATOM   2087 C  CE1 . TYR A 1 256 ? -28.219 -23.616 17.703  1.00 41.07  ? 256  TYR A CE1 1 
ATOM   2088 C  CE2 . TYR A 1 256 ? -30.217 -22.947 16.565  1.00 40.06  ? 256  TYR A CE2 1 
ATOM   2089 C  CZ  . TYR A 1 256 ? -29.454 -23.923 17.164  1.00 39.90  ? 256  TYR A CZ  1 
ATOM   2090 O  OH  . TYR A 1 256 ? -29.910 -25.223 17.207  1.00 42.80  ? 256  TYR A OH  1 
ATOM   2091 N  N   . GLN A 1 257 ? -27.097 -17.028 18.009  1.00 31.98  ? 257  GLN A N   1 
ATOM   2092 C  CA  . GLN A 1 257 ? -26.305 -15.827 17.731  1.00 30.94  ? 257  GLN A CA  1 
ATOM   2093 C  C   . GLN A 1 257 ? -25.341 -15.527 18.870  1.00 32.57  ? 257  GLN A C   1 
ATOM   2094 O  O   . GLN A 1 257 ? -24.216 -15.089 18.631  1.00 31.18  ? 257  GLN A O   1 
ATOM   2095 C  CB  . GLN A 1 257 ? -27.186 -14.604 17.481  1.00 32.12  ? 257  GLN A CB  1 
ATOM   2096 C  CG  . GLN A 1 257 ? -28.244 -14.775 16.394  1.00 31.33  ? 257  GLN A CG  1 
ATOM   2097 C  CD  . GLN A 1 257 ? -27.689 -14.865 14.972  1.00 34.75  ? 257  GLN A CD  1 
ATOM   2098 O  OE1 . GLN A 1 257 ? -26.475 -14.783 14.741  1.00 30.33  ? 257  GLN A OE1 1 
ATOM   2099 N  NE2 . GLN A 1 257 ? -28.589 -15.020 14.006  1.00 31.10  ? 257  GLN A NE2 1 
ATOM   2100 N  N   . ILE A 1 258 ? -25.760 -15.731 20.120  1.00 31.29  ? 258  ILE A N   1 
ATOM   2101 C  CA  . ILE A 1 258 ? -24.842 -15.483 21.232  1.00 32.80  ? 258  ILE A CA  1 
ATOM   2102 C  C   . ILE A 1 258 ? -23.626 -16.401 21.131  1.00 33.25  ? 258  ILE A C   1 
ATOM   2103 O  O   . ILE A 1 258 ? -22.474 -15.953 21.240  1.00 32.63  ? 258  ILE A O   1 
ATOM   2104 C  CB  . ILE A 1 258 ? -25.560 -15.645 22.585  1.00 33.43  ? 258  ILE A CB  1 
ATOM   2105 C  CG1 . ILE A 1 258 ? -26.658 -14.595 22.740  1.00 35.31  ? 258  ILE A CG1 1 
ATOM   2106 C  CG2 . ILE A 1 258 ? -24.549 -15.498 23.737  1.00 36.16  ? 258  ILE A CG2 1 
ATOM   2107 C  CD1 . ILE A 1 258 ? -27.471 -14.769 24.040  1.00 34.10  ? 258  ILE A CD1 1 
ATOM   2108 N  N   . ILE A 1 259 ? -23.864 -17.702 20.929  1.00 32.57  ? 259  ILE A N   1 
ATOM   2109 C  CA  . ILE A 1 259 ? -22.763 -18.653 20.738  1.00 31.90  ? 259  ILE A CA  1 
ATOM   2110 C  C   . ILE A 1 259 ? -21.860 -18.195 19.602  1.00 31.34  ? 259  ILE A C   1 
ATOM   2111 O  O   . ILE A 1 259 ? -20.628 -18.154 19.730  1.00 32.44  ? 259  ILE A O   1 
ATOM   2112 C  CB  . ILE A 1 259 ? -23.322 -20.060 20.449  1.00 36.72  ? 259  ILE A CB  1 
ATOM   2113 C  CG1 . ILE A 1 259 ? -23.924 -20.679 21.711  1.00 42.79  ? 259  ILE A CG1 1 
ATOM   2114 C  CG2 . ILE A 1 259 ? -22.252 -20.957 19.783  1.00 40.45  ? 259  ILE A CG2 1 
ATOM   2115 C  CD1 . ILE A 1 259 ? -24.301 -22.127 21.544  1.00 47.49  ? 259  ILE A CD1 1 
ATOM   2116 N  N   . THR A 1 260 ? -22.474 -17.858 18.466  1.00 30.81  ? 260  THR A N   1 
ATOM   2117 C  CA  . THR A 1 260 ? -21.737 -17.426 17.283  1.00 30.13  ? 260  THR A CA  1 
ATOM   2118 C  C   . THR A 1 260 ? -20.875 -16.207 17.588  1.00 32.08  ? 260  THR A C   1 
ATOM   2119 O  O   . THR A 1 260 ? -19.683 -16.160 17.241  1.00 32.85  ? 260  THR A O   1 
ATOM   2120 C  CB  . THR A 1 260 ? -22.734 -17.107 16.157  1.00 30.12  ? 260  THR A CB  1 
ATOM   2121 O  OG1 . THR A 1 260 ? -23.443 -18.296 15.782  1.00 33.93  ? 260  THR A OG1 1 
ATOM   2122 C  CG2 . THR A 1 260 ? -22.042 -16.510 14.952  1.00 30.66  ? 260  THR A CG2 1 
ATOM   2123 N  N   . PHE A 1 261 ? -21.469 -15.190 18.205  1.00 29.56  ? 261  PHE A N   1 
ATOM   2124 C  CA  . PHE A 1 261 ? -20.713 -13.963 18.413  1.00 30.69  ? 261  PHE A CA  1 
ATOM   2125 C  C   . PHE A 1 261 ? -19.665 -14.126 19.507  1.00 31.65  ? 261  PHE A C   1 
ATOM   2126 O  O   . PHE A 1 261 ? -18.602 -13.510 19.418  1.00 30.79  ? 261  PHE A O   1 
ATOM   2127 C  CB  . PHE A 1 261 ? -21.667 -12.796 18.689  1.00 32.95  ? 261  PHE A CB  1 
ATOM   2128 C  CG  . PHE A 1 261 ? -22.188 -12.165 17.420  1.00 31.38  ? 261  PHE A CG  1 
ATOM   2129 C  CD1 . PHE A 1 261 ? -23.305 -12.686 16.781  1.00 30.54  ? 261  PHE A CD1 1 
ATOM   2130 C  CD2 . PHE A 1 261 ? -21.532 -11.090 16.837  1.00 31.29  ? 261  PHE A CD2 1 
ATOM   2131 C  CE1 . PHE A 1 261 ? -23.775 -12.128 15.607  1.00 31.14  ? 261  PHE A CE1 1 
ATOM   2132 C  CE2 . PHE A 1 261 ? -21.996 -10.516 15.674  1.00 30.28  ? 261  PHE A CE2 1 
ATOM   2133 C  CZ  . PHE A 1 261 ? -23.117 -11.044 15.037  1.00 29.85  ? 261  PHE A CZ  1 
ATOM   2134 N  N   . LEU A 1 262 ? -19.902 -14.976 20.512  1.00 30.34  ? 262  LEU A N   1 
ATOM   2135 C  CA  . LEU A 1 262 ? -18.843 -15.206 21.502  1.00 31.13  ? 262  LEU A CA  1 
ATOM   2136 C  C   . LEU A 1 262 ? -17.606 -15.837 20.858  1.00 33.22  ? 262  LEU A C   1 
ATOM   2137 O  O   . LEU A 1 262 ? -16.468 -15.535 21.251  1.00 33.43  ? 262  LEU A O   1 
ATOM   2138 C  CB  . LEU A 1 262 ? -19.339 -16.086 22.647  1.00 31.22  ? 262  LEU A CB  1 
ATOM   2139 C  CG  . LEU A 1 262 ? -20.294 -15.379 23.609  1.00 35.56  ? 262  LEU A CG  1 
ATOM   2140 C  CD1 . LEU A 1 262 ? -20.851 -16.371 24.626  1.00 34.93  ? 262  LEU A CD1 1 
ATOM   2141 C  CD2 . LEU A 1 262 ? -19.595 -14.197 24.288  1.00 32.86  ? 262  LEU A CD2 1 
ATOM   2142 N  N   . ILE A 1 263 ? -17.810 -16.724 19.883  1.00 30.68  ? 263  ILE A N   1 
ATOM   2143 C  CA  . ILE A 1 263 ? -16.709 -17.464 19.271  1.00 31.61  ? 263  ILE A CA  1 
ATOM   2144 C  C   . ILE A 1 263 ? -16.116 -16.649 18.128  1.00 32.66  ? 263  ILE A C   1 
ATOM   2145 O  O   . ILE A 1 263 ? -14.914 -16.346 18.122  1.00 31.27  ? 263  ILE A O   1 
ATOM   2146 C  CB  . ILE A 1 263 ? -17.170 -18.850 18.781  1.00 32.28  ? 263  ILE A CB  1 
ATOM   2147 C  CG1 . ILE A 1 263 ? -17.633 -19.706 19.969  1.00 33.59  ? 263  ILE A CG1 1 
ATOM   2148 C  CG2 . ILE A 1 263 ? -16.061 -19.541 18.002  1.00 34.42  ? 263  ILE A CG2 1 
ATOM   2149 C  CD1 . ILE A 1 263 ? -18.197 -21.085 19.544  1.00 34.97  ? 263  ILE A CD1 1 
ATOM   2150 N  N   . ALA A 1 264 ? -16.949 -16.308 17.140  1.00 31.22  ? 264  ALA A N   1 
ATOM   2151 C  CA  . ALA A 1 264 ? -16.463 -15.518 16.013  1.00 32.27  ? 264  ALA A CA  1 
ATOM   2152 C  C   . ALA A 1 264 ? -15.980 -14.144 16.460  1.00 30.24  ? 264  ALA A C   1 
ATOM   2153 O  O   . ALA A 1 264 ? -15.083 -13.565 15.832  1.00 30.74  ? 264  ALA A O   1 
ATOM   2154 C  CB  . ALA A 1 264 ? -17.569 -15.378 14.959  1.00 29.45  ? 264  ALA A CB  1 
ATOM   2155 N  N   . GLY A 1 265 ? -16.545 -13.609 17.545  1.00 29.52  ? 265  GLY A N   1 
ATOM   2156 C  CA  . GLY A 1 265 ? -16.209 -12.282 18.019  1.00 29.60  ? 265  GLY A CA  1 
ATOM   2157 C  C   . GLY A 1 265 ? -14.926 -12.180 18.810  1.00 31.68  ? 265  GLY A C   1 
ATOM   2158 O  O   . GLY A 1 265 ? -14.595 -11.086 19.281  1.00 31.36  ? 265  GLY A O   1 
ATOM   2159 N  N   . HIS A 1 266 ? -14.193 -13.281 18.979  1.00 31.43  ? 266  HIS A N   1 
ATOM   2160 C  CA  . HIS A 1 266 ? -12.891 -13.186 19.652  1.00 30.43  ? 266  HIS A CA  1 
ATOM   2161 C  C   . HIS A 1 266 ? -11.812 -14.106 19.098  1.00 33.27  ? 266  HIS A C   1 
ATOM   2162 O  O   . HIS A 1 266 ? -10.640 -13.717 19.128  1.00 31.94  ? 266  HIS A O   1 
ATOM   2163 C  CB  . HIS A 1 266 ? -13.030 -13.469 21.172  1.00 30.41  ? 266  HIS A CB  1 
ATOM   2164 C  CG  . HIS A 1 266 ? -12.752 -14.893 21.546  1.00 29.17  ? 266  HIS A CG  1 
ATOM   2165 N  ND1 . HIS A 1 266 ? -13.723 -15.871 21.520  1.00 31.55  ? 266  HIS A ND1 1 
ATOM   2166 C  CD2 . HIS A 1 266 ? -11.609 -15.506 21.949  1.00 30.34  ? 266  HIS A CD2 1 
ATOM   2167 C  CE1 . HIS A 1 266 ? -13.192 -17.026 21.884  1.00 32.87  ? 266  HIS A CE1 1 
ATOM   2168 N  NE2 . HIS A 1 266 ? -11.910 -16.834 22.139  1.00 33.30  ? 266  HIS A NE2 1 
ATOM   2169 N  N   . GLU A 1 267 ? -12.133 -15.309 18.621  1.00 31.21  ? 267  GLU A N   1 
ATOM   2170 C  CA  . GLU A 1 267 ? -11.072 -16.284 18.372  1.00 29.81  ? 267  GLU A CA  1 
ATOM   2171 C  C   . GLU A 1 267 ? -10.121 -15.781 17.289  1.00 32.06  ? 267  GLU A C   1 
ATOM   2172 O  O   . GLU A 1 267 ? -8.895  -15.812 17.453  1.00 32.16  ? 267  GLU A O   1 
ATOM   2173 C  CB  . GLU A 1 267 ? -11.690 -17.634 17.997  1.00 30.97  ? 267  GLU A CB  1 
ATOM   2174 C  CG  . GLU A 1 267 ? -10.814 -18.548 17.170  1.00 34.42  ? 267  GLU A CG  1 
ATOM   2175 C  CD  . GLU A 1 267 ? -9.582  -19.016 17.904  1.00 38.73  ? 267  GLU A CD  1 
ATOM   2176 O  OE1 . GLU A 1 267 ? -9.616  -19.111 19.147  1.00 36.89  ? 267  GLU A OE1 1 
ATOM   2177 O  OE2 . GLU A 1 267 ? -8.571  -19.287 17.214  1.00 41.88  ? 267  GLU A OE2 1 
ATOM   2178 N  N   . THR A 1 268 ? -10.669 -15.260 16.204  1.00 29.39  ? 268  THR A N   1 
ATOM   2179 C  CA  . THR A 1 268 ? -9.824  -14.834 15.091  1.00 31.56  ? 268  THR A CA  1 
ATOM   2180 C  C   . THR A 1 268 ? -9.100  -13.533 15.381  1.00 32.20  ? 268  THR A C   1 
ATOM   2181 O  O   . THR A 1 268 ? -8.042  -13.275 14.779  1.00 32.71  ? 268  THR A O   1 
ATOM   2182 C  CB  . THR A 1 268 ? -10.677 -14.705 13.831  1.00 33.91  ? 268  THR A CB  1 
ATOM   2183 O  OG1 . THR A 1 268 ? -11.918 -14.054 14.161  1.00 29.81  ? 268  THR A OG1 1 
ATOM   2184 C  CG2 . THR A 1 268 ? -10.966 -16.108 13.259  1.00 30.12  ? 268  THR A CG2 1 
ATOM   2185 N  N   . THR A 1 269 ? -9.651  -12.707 16.276  1.00 29.30  ? 269  THR A N   1 
ATOM   2186 C  CA  . THR A 1 269 ? -8.969  -11.482 16.684  1.00 29.91  ? 269  THR A CA  1 
ATOM   2187 C  C   . THR A 1 269 ? -7.789  -11.803 17.600  1.00 32.29  ? 269  THR A C   1 
ATOM   2188 O  O   . THR A 1 269 ? -6.761  -11.112 17.551  1.00 31.20  ? 269  THR A O   1 
ATOM   2189 C  CB  . THR A 1 269 ? -9.964  -10.524 17.366  1.00 29.77  ? 269  THR A CB  1 
ATOM   2190 O  OG1 . THR A 1 269 ? -11.057 -10.263 16.453  1.00 28.99  ? 269  THR A OG1 1 
ATOM   2191 C  CG2 . THR A 1 269 ? -9.293  -9.190  17.713  1.00 29.09  ? 269  THR A CG2 1 
ATOM   2192 N  N   A SER A 1 270 ? -7.904  -12.849 18.422  0.45 30.97  ? 270  SER A N   1 
ATOM   2193 N  N   B SER A 1 270 ? -7.918  -12.830 18.444  0.55 30.95  ? 270  SER A N   1 
ATOM   2194 C  CA  A SER A 1 270 ? -6.748  -13.271 19.212  0.45 30.21  ? 270  SER A CA  1 
ATOM   2195 C  CA  B SER A 1 270 ? -6.757  -13.286 19.209  0.55 30.19  ? 270  SER A CA  1 
ATOM   2196 C  C   A SER A 1 270 ? -5.640  -13.809 18.311  0.45 31.65  ? 270  SER A C   1 
ATOM   2197 C  C   B SER A 1 270 ? -5.650  -13.757 18.275  0.55 31.64  ? 270  SER A C   1 
ATOM   2198 O  O   A SER A 1 270 ? -4.453  -13.554 18.555  0.45 32.31  ? 270  SER A O   1 
ATOM   2199 O  O   B SER A 1 270 ? -4.474  -13.415 18.465  0.55 32.32  ? 270  SER A O   1 
ATOM   2200 C  CB  A SER A 1 270 ? -7.163  -14.316 20.254  0.45 32.57  ? 270  SER A CB  1 
ATOM   2201 C  CB  B SER A 1 270 ? -7.152  -14.409 20.171  0.55 32.57  ? 270  SER A CB  1 
ATOM   2202 O  OG  A SER A 1 270 ? -7.448  -15.574 19.670  0.45 31.25  ? 270  SER A OG  1 
ATOM   2203 O  OG  B SER A 1 270 ? -6.003  -15.118 20.628  0.55 32.07  ? 270  SER A OG  1 
ATOM   2204 N  N   . GLY A 1 271 ? -6.007  -14.547 17.263  1.00 32.64  ? 271  GLY A N   1 
ATOM   2205 C  CA  . GLY A 1 271 ? -5.017  -14.955 16.274  1.00 31.36  ? 271  GLY A CA  1 
ATOM   2206 C  C   . GLY A 1 271 ? -4.355  -13.769 15.598  1.00 36.82  ? 271  GLY A C   1 
ATOM   2207 O  O   . GLY A 1 271 ? -3.130  -13.721 15.451  1.00 32.91  ? 271  GLY A O   1 
ATOM   2208 N  N   . LEU A 1 272 ? -5.156  -12.790 15.176  1.00 31.70  ? 272  LEU A N   1 
ATOM   2209 C  CA  . LEU A 1 272 ? -4.595  -11.617 14.506  1.00 35.32  ? 272  LEU A CA  1 
ATOM   2210 C  C   . LEU A 1 272 ? -3.567  -10.903 15.383  1.00 34.33  ? 272  LEU A C   1 
ATOM   2211 O  O   . LEU A 1 272 ? -2.461  -10.572 14.931  1.00 33.83  ? 272  LEU A O   1 
ATOM   2212 C  CB  . LEU A 1 272 ? -5.716  -10.654 14.129  1.00 33.74  ? 272  LEU A CB  1 
ATOM   2213 C  CG  . LEU A 1 272 ? -5.272  -9.279  13.640  1.00 33.18  ? 272  LEU A CG  1 
ATOM   2214 C  CD1 . LEU A 1 272 ? -4.307  -9.410  12.451  1.00 31.50  ? 272  LEU A CD1 1 
ATOM   2215 C  CD2 . LEU A 1 272 ? -6.511  -8.447  13.242  1.00 33.48  ? 272  LEU A CD2 1 
ATOM   2216 N  N   . LEU A 1 273 ? -3.925  -10.627 16.636  1.00 31.11  ? 273  LEU A N   1 
ATOM   2217 C  CA  . LEU A 1 273 ? -3.005  -9.913  17.507  1.00 32.11  ? 273  LEU A CA  1 
ATOM   2218 C  C   . LEU A 1 273 ? -1.751  -10.739 17.753  1.00 32.43  ? 273  LEU A C   1 
ATOM   2219 O  O   . LEU A 1 273 ? -0.644  -10.189 17.806  1.00 34.84  ? 273  LEU A O   1 
ATOM   2220 C  CB  . LEU A 1 273 ? -3.692  -9.543  18.826  1.00 32.98  ? 273  LEU A CB  1 
ATOM   2221 C  CG  . LEU A 1 273 ? -4.634  -8.343  18.767  1.00 30.85  ? 273  LEU A CG  1 
ATOM   2222 C  CD1 . LEU A 1 273 ? -5.578  -8.308  19.994  1.00 32.17  ? 273  LEU A CD1 1 
ATOM   2223 C  CD2 . LEU A 1 273 ? -3.856  -7.036  18.680  1.00 33.78  ? 273  LEU A CD2 1 
ATOM   2224 N  N   . SER A 1 274 ? -1.902  -12.061 17.892  1.00 32.88  ? 274  SER A N   1 
ATOM   2225 C  CA  . SER A 1 274 ? -0.733  -12.917 18.096  1.00 32.48  ? 274  SER A CA  1 
ATOM   2226 C  C   . SER A 1 274 ? 0.191   -12.865 16.881  1.00 37.46  ? 274  SER A C   1 
ATOM   2227 O  O   . SER A 1 274 ? 1.403   -12.631 17.018  1.00 34.92  ? 274  SER A O   1 
ATOM   2228 C  CB  . SER A 1 274 ? -1.173  -14.353 18.400  1.00 33.36  ? 274  SER A CB  1 
ATOM   2229 O  OG  . SER A 1 274 ? -2.064  -14.378 19.527  1.00 31.16  ? 274  SER A OG  1 
ATOM   2230 N  N   . PHE A 1 275 ? -0.371  -13.050 15.677  1.00 33.88  ? 275  PHE A N   1 
ATOM   2231 C  CA  . PHE A 1 275 ? 0.439   -12.931 14.462  1.00 34.34  ? 275  PHE A CA  1 
ATOM   2232 C  C   . PHE A 1 275 ? 1.039   -11.533 14.317  1.00 34.95  ? 275  PHE A C   1 
ATOM   2233 O  O   . PHE A 1 275 ? 2.190   -11.387 13.874  1.00 36.50  ? 275  PHE A O   1 
ATOM   2234 C  CB  . PHE A 1 275 ? -0.385  -13.283 13.218  1.00 32.81  ? 275  PHE A CB  1 
ATOM   2235 C  CG  . PHE A 1 275 ? -0.542  -14.755 12.979  1.00 34.63  ? 275  PHE A CG  1 
ATOM   2236 C  CD1 . PHE A 1 275 ? 0.566   -15.564 12.748  1.00 35.48  ? 275  PHE A CD1 1 
ATOM   2237 C  CD2 . PHE A 1 275 ? -1.798  -15.336 12.991  1.00 29.53  ? 275  PHE A CD2 1 
ATOM   2238 C  CE1 . PHE A 1 275 ? 0.415   -16.919 12.504  1.00 35.82  ? 275  PHE A CE1 1 
ATOM   2239 C  CE2 . PHE A 1 275 ? -1.966  -16.674 12.760  1.00 34.21  ? 275  PHE A CE2 1 
ATOM   2240 C  CZ  . PHE A 1 275 ? -0.854  -17.487 12.516  1.00 38.03  ? 275  PHE A CZ  1 
ATOM   2241 N  N   . ALA A 1 276 ? 0.279   -10.489 14.652  1.00 33.00  ? 276  ALA A N   1 
ATOM   2242 C  CA  . ALA A 1 276 ? 0.801   -9.135  14.481  1.00 34.60  ? 276  ALA A CA  1 
ATOM   2243 C  C   . ALA A 1 276 ? 2.005   -8.903  15.388  1.00 38.46  ? 276  ALA A C   1 
ATOM   2244 O  O   . ALA A 1 276 ? 3.023   -8.351  14.957  1.00 35.73  ? 276  ALA A O   1 
ATOM   2245 C  CB  . ALA A 1 276 ? -0.290  -8.092  14.745  1.00 35.15  ? 276  ALA A CB  1 
ATOM   2246 N  N   . LEU A 1 277 ? 1.924   -9.341  16.646  1.00 36.85  ? 277  LEU A N   1 
ATOM   2247 C  CA  . LEU A 1 277 ? 3.067   -9.139  17.535  1.00 34.90  ? 277  LEU A CA  1 
ATOM   2248 C  C   . LEU A 1 277 ? 4.256   -9.968  17.078  1.00 38.23  ? 277  LEU A C   1 
ATOM   2249 O  O   . LEU A 1 277 ? 5.408   -9.522  17.173  1.00 36.88  ? 277  LEU A O   1 
ATOM   2250 C  CB  . LEU A 1 277 ? 2.697   -9.492  18.977  1.00 35.53  ? 277  LEU A CB  1 
ATOM   2251 C  CG  . LEU A 1 277 ? 3.809   -9.232  19.999  1.00 38.31  ? 277  LEU A CG  1 
ATOM   2252 C  CD1 . LEU A 1 277 ? 4.205   -7.754  19.989  1.00 34.99  ? 277  LEU A CD1 1 
ATOM   2253 C  CD2 . LEU A 1 277 ? 3.331   -9.649  21.391  1.00 36.98  ? 277  LEU A CD2 1 
ATOM   2254 N  N   . TYR A 1 278 ? 3.992   -11.174 16.576  1.00 31.76  ? 278  TYR A N   1 
ATOM   2255 C  CA  . TYR A 1 278 ? 5.057   -12.007 16.032  1.00 35.97  ? 278  TYR A CA  1 
ATOM   2256 C  C   . TYR A 1 278 ? 5.791   -11.277 14.915  1.00 40.62  ? 278  TYR A C   1 
ATOM   2257 O  O   . TYR A 1 278 ? 7.025   -11.174 14.929  1.00 36.69  ? 278  TYR A O   1 
ATOM   2258 C  CB  . TYR A 1 278 ? 4.486   -13.339 15.527  1.00 33.47  ? 278  TYR A CB  1 
ATOM   2259 C  CG  . TYR A 1 278 ? 5.436   -14.112 14.633  1.00 37.46  ? 278  TYR A CG  1 
ATOM   2260 C  CD1 . TYR A 1 278 ? 6.364   -14.993 15.175  1.00 38.15  ? 278  TYR A CD1 1 
ATOM   2261 C  CD2 . TYR A 1 278 ? 5.425   -13.937 13.249  1.00 36.77  ? 278  TYR A CD2 1 
ATOM   2262 C  CE1 . TYR A 1 278 ? 7.248   -15.697 14.367  1.00 40.94  ? 278  TYR A CE1 1 
ATOM   2263 C  CE2 . TYR A 1 278 ? 6.302   -14.635 12.437  1.00 39.60  ? 278  TYR A CE2 1 
ATOM   2264 C  CZ  . TYR A 1 278 ? 7.218   -15.508 13.002  1.00 42.26  ? 278  TYR A CZ  1 
ATOM   2265 O  OH  . TYR A 1 278 ? 8.099   -16.203 12.189  1.00 42.33  ? 278  TYR A OH  1 
ATOM   2266 N  N   . PHE A 1 279 ? 5.047   -10.745 13.940  1.00 36.20  ? 279  PHE A N   1 
ATOM   2267 C  CA  . PHE A 1 279 ? 5.721   -10.069 12.835  1.00 35.68  ? 279  PHE A CA  1 
ATOM   2268 C  C   . PHE A 1 279 ? 6.429   -8.805  13.309  1.00 40.00  ? 279  PHE A C   1 
ATOM   2269 O  O   . PHE A 1 279 ? 7.489   -8.463  12.776  1.00 42.68  ? 279  PHE A O   1 
ATOM   2270 C  CB  . PHE A 1 279 ? 4.730   -9.759  11.703  1.00 35.48  ? 279  PHE A CB  1 
ATOM   2271 C  CG  . PHE A 1 279 ? 4.370   -10.961 10.869  1.00 36.59  ? 279  PHE A CG  1 
ATOM   2272 C  CD1 . PHE A 1 279 ? 5.335   -11.634 10.140  1.00 38.19  ? 279  PHE A CD1 1 
ATOM   2273 C  CD2 . PHE A 1 279 ? 3.063   -11.428 10.825  1.00 36.55  ? 279  PHE A CD2 1 
ATOM   2274 C  CE1 . PHE A 1 279 ? 5.014   -12.752 9.397   1.00 36.71  ? 279  PHE A CE1 1 
ATOM   2275 C  CE2 . PHE A 1 279 ? 2.732   -12.547 10.073  1.00 37.37  ? 279  PHE A CE2 1 
ATOM   2276 C  CZ  . PHE A 1 279 ? 3.708   -13.203 9.348   1.00 41.35  ? 279  PHE A CZ  1 
ATOM   2277 N  N   . LEU A 1 280 ? 5.897   -8.129  14.330  1.00 36.63  ? 280  LEU A N   1 
ATOM   2278 C  CA  . LEU A 1 280 ? 6.525   -6.900  14.809  1.00 35.78  ? 280  LEU A CA  1 
ATOM   2279 C  C   . LEU A 1 280 ? 7.875   -7.188  15.468  1.00 42.75  ? 280  LEU A C   1 
ATOM   2280 O  O   . LEU A 1 280 ? 8.862   -6.485  15.201  1.00 39.44  ? 280  LEU A O   1 
ATOM   2281 C  CB  . LEU A 1 280 ? 5.598   -6.157  15.771  1.00 37.29  ? 280  LEU A CB  1 
ATOM   2282 C  CG  . LEU A 1 280 ? 4.472   -5.328  15.140  1.00 37.59  ? 280  LEU A CG  1 
ATOM   2283 C  CD1 . LEU A 1 280 ? 3.675   -4.557  16.204  1.00 40.60  ? 280  LEU A CD1 1 
ATOM   2284 C  CD2 . LEU A 1 280 ? 4.997   -4.379  14.060  1.00 41.23  ? 280  LEU A CD2 1 
ATOM   2285 N  N   . VAL A 1 281 ? 7.950   -8.219  16.323  1.00 40.24  ? 281  VAL A N   1 
ATOM   2286 C  CA  . VAL A 1 281 ? 9.250   -8.529  16.940  1.00 38.68  ? 281  VAL A CA  1 
ATOM   2287 C  C   . VAL A 1 281 ? 10.209  -9.136  15.923  1.00 44.43  ? 281  VAL A C   1 
ATOM   2288 O  O   . VAL A 1 281 ? 11.435  -9.024  16.075  1.00 42.33  ? 281  VAL A O   1 
ATOM   2289 C  CB  . VAL A 1 281 ? 9.098   -9.445  18.174  1.00 41.90  ? 281  VAL A CB  1 
ATOM   2290 C  CG1 . VAL A 1 281 ? 8.197   -8.792  19.206  1.00 44.99  ? 281  VAL A CG1 1 
ATOM   2291 C  CG2 . VAL A 1 281 ? 8.609   -10.842 17.775  1.00 36.60  ? 281  VAL A CG2 1 
ATOM   2292 N  N   . LYS A 1 282 ? 9.692   -9.781  14.878  1.00 40.31  ? 282  LYS A N   1 
ATOM   2293 C  CA  . LYS A 1 282 ? 10.571  -10.278 13.827  1.00 41.74  ? 282  LYS A CA  1 
ATOM   2294 C  C   . LYS A 1 282 ? 11.004  -9.188  12.850  1.00 44.49  ? 282  LYS A C   1 
ATOM   2295 O  O   . LYS A 1 282 ? 11.873  -9.445  12.010  1.00 46.85  ? 282  LYS A O   1 
ATOM   2296 C  CB  . LYS A 1 282 ? 9.902   -11.414 13.053  1.00 41.86  ? 282  LYS A CB  1 
ATOM   2297 C  CG  . LYS A 1 282 ? 9.647   -12.713 13.842  1.00 42.52  ? 282  LYS A CG  1 
ATOM   2298 C  CD  . LYS A 1 282 ? 10.924  -13.292 14.508  1.00 40.40  ? 282  LYS A CD  1 
ATOM   2299 C  CE  . LYS A 1 282 ? 10.715  -14.734 14.957  1.00 39.23  ? 282  LYS A CE  1 
ATOM   2300 N  NZ  . LYS A 1 282 ? 11.918  -15.350 15.661  1.00 42.16  ? 282  LYS A NZ  1 
ATOM   2301 N  N   . ASN A 1 283 ? 10.441  -7.983  12.941  1.00 41.51  ? 283  ASN A N   1 
ATOM   2302 C  CA  . ASN A 1 283 ? 10.747  -6.894  12.009  1.00 40.87  ? 283  ASN A CA  1 
ATOM   2303 C  C   . ASN A 1 283 ? 10.892  -5.606  12.799  1.00 44.61  ? 283  ASN A C   1 
ATOM   2304 O  O   . ASN A 1 283 ? 10.025  -4.724  12.753  1.00 43.21  ? 283  ASN A O   1 
ATOM   2305 C  CB  . ASN A 1 283 ? 9.660   -6.769  10.936  1.00 40.56  ? 283  ASN A CB  1 
ATOM   2306 C  CG  . ASN A 1 283 ? 9.611   -7.971  10.025  1.00 39.32  ? 283  ASN A CG  1 
ATOM   2307 O  OD1 . ASN A 1 283 ? 10.316  -8.030  9.013   1.00 44.02  ? 283  ASN A OD1 1 
ATOM   2308 N  ND2 . ASN A 1 283 ? 8.784   -8.947  10.375  1.00 38.73  ? 283  ASN A ND2 1 
ATOM   2309 N  N   . PRO A 1 284 ? 12.006  -5.453  13.524  1.00 45.10  ? 284  PRO A N   1 
ATOM   2310 C  CA  . PRO A 1 284 ? 12.108  -4.341  14.484  1.00 48.77  ? 284  PRO A CA  1 
ATOM   2311 C  C   . PRO A 1 284 ? 11.948  -2.979  13.849  1.00 42.95  ? 284  PRO A C   1 
ATOM   2312 O  O   . PRO A 1 284 ? 11.532  -2.034  14.538  1.00 48.11  ? 284  PRO A O   1 
ATOM   2313 C  CB  . PRO A 1 284 ? 13.514  -4.514  15.079  1.00 50.48  ? 284  PRO A CB  1 
ATOM   2314 C  CG  . PRO A 1 284 ? 13.893  -5.934  14.785  1.00 46.66  ? 284  PRO A CG  1 
ATOM   2315 C  CD  . PRO A 1 284 ? 13.205  -6.304  13.514  1.00 46.86  ? 284  PRO A CD  1 
ATOM   2316 N  N   . HIS A 1 285 ? 12.300  -2.839  12.568  1.00 46.06  ? 285  HIS A N   1 
ATOM   2317 C  CA  . HIS A 1 285 ? 12.117  -1.561  11.886  1.00 47.76  ? 285  HIS A CA  1 
ATOM   2318 C  C   . HIS A 1 285 ? 10.639  -1.213  11.801  1.00 44.76  ? 285  HIS A C   1 
ATOM   2319 O  O   . HIS A 1 285 ? 10.241  -0.066  12.046  1.00 44.21  ? 285  HIS A O   1 
ATOM   2320 C  CB  . HIS A 1 285 ? 12.737  -1.605  10.483  1.00 48.68  ? 285  HIS A CB  1 
ATOM   2321 C  CG  . HIS A 1 285 ? 14.216  -1.875  10.469  1.00 59.61  ? 285  HIS A CG  1 
ATOM   2322 N  ND1 . HIS A 1 285 ? 14.810  -2.735  9.567   1.00 63.64  ? 285  HIS A ND1 1 
ATOM   2323 C  CD2 . HIS A 1 285 ? 15.218  -1.403  11.250  1.00 58.72  ? 285  HIS A CD2 1 
ATOM   2324 C  CE1 . HIS A 1 285 ? 16.113  -2.773  9.785   1.00 61.19  ? 285  HIS A CE1 1 
ATOM   2325 N  NE2 . HIS A 1 285 ? 16.386  -1.977  10.803  1.00 62.69  ? 285  HIS A NE2 1 
ATOM   2326 N  N   . VAL A 1 286 ? 9.809   -2.212  11.493  1.00 45.91  ? 286  VAL A N   1 
ATOM   2327 C  CA  . VAL A 1 286 ? 8.358   -2.019  11.477  1.00 44.57  ? 286  VAL A CA  1 
ATOM   2328 C  C   . VAL A 1 286 ? 7.839   -1.735  12.881  1.00 39.90  ? 286  VAL A C   1 
ATOM   2329 O  O   . VAL A 1 286 ? 7.012   -0.833  13.090  1.00 42.46  ? 286  VAL A O   1 
ATOM   2330 C  CB  . VAL A 1 286 ? 7.679   -3.252  10.858  1.00 41.39  ? 286  VAL A CB  1 
ATOM   2331 C  CG1 . VAL A 1 286 ? 6.144   -3.063  10.812  1.00 41.72  ? 286  VAL A CG1 1 
ATOM   2332 C  CG2 . VAL A 1 286 ? 8.257   -3.547  9.463   1.00 42.13  ? 286  VAL A CG2 1 
ATOM   2333 N  N   . LEU A 1 287 ? 8.318   -2.490  13.873  1.00 44.52  ? 287  LEU A N   1 
ATOM   2334 C  CA  . LEU A 1 287 ? 7.929   -2.213  15.250  1.00 41.39  ? 287  LEU A CA  1 
ATOM   2335 C  C   . LEU A 1 287 ? 8.185   -0.754  15.610  1.00 41.68  ? 287  LEU A C   1 
ATOM   2336 O  O   . LEU A 1 287 ? 7.309   -0.064  16.144  1.00 42.09  ? 287  LEU A O   1 
ATOM   2337 C  CB  . LEU A 1 287 ? 8.679   -3.154  16.197  1.00 43.15  ? 287  LEU A CB  1 
ATOM   2338 C  CG  . LEU A 1 287 ? 8.012   -3.377  17.556  1.00 44.23  ? 287  LEU A CG  1 
ATOM   2339 C  CD1 . LEU A 1 287 ? 8.572   -4.640  18.215  1.00 48.78  ? 287  LEU A CD1 1 
ATOM   2340 C  CD2 . LEU A 1 287 ? 8.193   -2.154  18.446  1.00 45.60  ? 287  LEU A CD2 1 
ATOM   2341 N  N   . GLN A 1 288 ? 9.389   -0.256  15.305  1.00 45.13  ? 288  GLN A N   1 
ATOM   2342 C  CA  . GLN A 1 288 ? 9.714   1.129   15.636  1.00 42.43  ? 288  GLN A CA  1 
ATOM   2343 C  C   . GLN A 1 288 ? 8.738   2.114   15.003  1.00 41.48  ? 288  GLN A C   1 
ATOM   2344 O  O   . GLN A 1 288 ? 8.249   3.036   15.667  1.00 45.04  ? 288  GLN A O   1 
ATOM   2345 C  CB  . GLN A 1 288 ? 11.140  1.471   15.203  1.00 50.76  ? 288  GLN A CB  1 
ATOM   2346 C  CG  . GLN A 1 288 ? 11.606  2.759   15.838  1.00 50.63  ? 288  GLN A CG  1 
ATOM   2347 C  CD  . GLN A 1 288 ? 12.875  3.289   15.225  1.00 61.23  ? 288  GLN A CD  1 
ATOM   2348 O  OE1 . GLN A 1 288 ? 13.743  2.524   14.796  1.00 64.55  ? 288  GLN A OE1 1 
ATOM   2349 N  NE2 . GLN A 1 288 ? 12.984  4.610   15.155  1.00 61.81  ? 288  GLN A NE2 1 
ATOM   2350 N  N   . LYS A 1 289 ? 8.469   1.965   13.705  1.00 45.42  ? 289  LYS A N   1 
ATOM   2351 C  CA  . LYS A 1 289 ? 7.565   2.906   13.052  1.00 41.53  ? 289  LYS A CA  1 
ATOM   2352 C  C   . LYS A 1 289 ? 6.199   2.906   13.725  1.00 39.76  ? 289  LYS A C   1 
ATOM   2353 O  O   . LYS A 1 289 ? 5.622   3.971   13.991  1.00 39.63  ? 289  LYS A O   1 
ATOM   2354 C  CB  . LYS A 1 289 ? 7.443   2.565   11.568  1.00 42.73  ? 289  LYS A CB  1 
ATOM   2355 C  CG  . LYS A 1 289 ? 6.762   3.638   10.728  1.00 41.88  ? 289  LYS A CG  1 
ATOM   2356 C  CD  . LYS A 1 289 ? 7.036   3.385   9.242   1.00 46.29  ? 289  LYS A CD  1 
ATOM   2357 C  CE  . LYS A 1 289 ? 6.083   4.165   8.354   1.00 46.10  ? 289  LYS A CE  1 
ATOM   2358 N  NZ  . LYS A 1 289 ? 6.257   3.748   6.936   1.00 49.75  ? 289  LYS A NZ  1 
ATOM   2359 N  N   . ALA A 1 290 ? 5.681   1.717   14.038  1.00 44.07  ? 290  ALA A N   1 
ATOM   2360 C  CA  . ALA A 1 290 ? 4.378   1.621   14.691  1.00 43.33  ? 290  ALA A CA  1 
ATOM   2361 C  C   . ALA A 1 290 ? 4.428   2.170   16.115  1.00 38.30  ? 290  ALA A C   1 
ATOM   2362 O  O   . ALA A 1 290 ? 3.482   2.830   16.568  1.00 41.66  ? 290  ALA A O   1 
ATOM   2363 C  CB  . ALA A 1 290 ? 3.903   0.168   14.669  1.00 41.07  ? 290  ALA A CB  1 
ATOM   2364 N  N   . ALA A 1 291 ? 5.527   1.921   16.833  1.00 40.91  ? 291  ALA A N   1 
ATOM   2365 C  CA  . ALA A 1 291 ? 5.665   2.483   18.177  1.00 43.55  ? 291  ALA A CA  1 
ATOM   2366 C  C   . ALA A 1 291 ? 5.761   4.001   18.127  1.00 41.93  ? 291  ALA A C   1 
ATOM   2367 O  O   . ALA A 1 291 ? 5.212   4.702   18.986  1.00 41.17  ? 291  ALA A O   1 
ATOM   2368 C  CB  . ALA A 1 291 ? 6.887   1.883   18.877  1.00 41.39  ? 291  ALA A CB  1 
ATOM   2369 N  N   . GLU A 1 292 ? 6.443   4.528   17.112  1.00 44.14  ? 292  GLU A N   1 
ATOM   2370 C  CA  . GLU A 1 292 ? 6.512   5.972   16.939  1.00 40.69  ? 292  GLU A CA  1 
ATOM   2371 C  C   . GLU A 1 292 ? 5.127   6.570   16.739  1.00 45.06  ? 292  GLU A C   1 
ATOM   2372 O  O   . GLU A 1 292 ? 4.799   7.606   17.332  1.00 45.51  ? 292  GLU A O   1 
ATOM   2373 C  CB  . GLU A 1 292 ? 7.427   6.278   15.758  1.00 46.67  ? 292  GLU A CB  1 
ATOM   2374 C  CG  . GLU A 1 292 ? 8.880   5.975   16.082  1.00 50.95  ? 292  GLU A CG  1 
ATOM   2375 C  CD  . GLU A 1 292 ? 9.813   6.365   14.965  1.00 57.23  ? 292  GLU A CD  1 
ATOM   2376 O  OE1 . GLU A 1 292 ? 9.308   6.761   13.894  1.00 59.88  ? 292  GLU A OE1 1 
ATOM   2377 O  OE2 . GLU A 1 292 ? 11.042  6.245   15.150  1.00 56.72  ? 292  GLU A OE2 1 
ATOM   2378 N  N   . GLU A 1 293 ? 4.288   5.923   15.921  1.00 44.44  ? 293  GLU A N   1 
ATOM   2379 C  CA  . GLU A 1 293 ? 2.918   6.403   15.766  1.00 42.36  ? 293  GLU A CA  1 
ATOM   2380 C  C   . GLU A 1 293 ? 2.180   6.355   17.093  1.00 40.46  ? 293  GLU A C   1 
ATOM   2381 O  O   . GLU A 1 293 ? 1.519   7.321   17.490  1.00 41.56  ? 293  GLU A O   1 
ATOM   2382 C  CB  . GLU A 1 293 ? 2.166   5.582   14.708  1.00 37.42  ? 293  GLU A CB  1 
ATOM   2383 C  CG  . GLU A 1 293 ? 0.744   6.078   14.466  1.00 40.02  ? 293  GLU A CG  1 
ATOM   2384 C  CD  . GLU A 1 293 ? 0.035   5.275   13.400  1.00 41.52  ? 293  GLU A CD  1 
ATOM   2385 O  OE1 . GLU A 1 293 ? -0.362  4.135   13.703  1.00 38.39  ? 293  GLU A OE1 1 
ATOM   2386 O  OE2 . GLU A 1 293 ? -0.108  5.769   12.261  1.00 40.99  ? 293  GLU A OE2 1 
ATOM   2387 N  N   . ALA A 1 294 ? 2.275   5.225   17.793  1.00 44.01  ? 294  ALA A N   1 
ATOM   2388 C  CA  . ALA A 1 294 ? 1.548   5.081   19.050  1.00 41.03  ? 294  ALA A CA  1 
ATOM   2389 C  C   . ALA A 1 294 ? 1.912   6.194   20.028  1.00 39.21  ? 294  ALA A C   1 
ATOM   2390 O  O   . ALA A 1 294 ? 1.030   6.802   20.643  1.00 40.79  ? 294  ALA A O   1 
ATOM   2391 C  CB  . ALA A 1 294 ? 1.821   3.700   19.646  1.00 40.49  ? 294  ALA A CB  1 
ATOM   2392 N  N   . ALA A 1 295 ? 3.205   6.514   20.138  1.00 46.00  ? 295  ALA A N   1 
ATOM   2393 C  CA  . ALA A 1 295 ? 3.636   7.584   21.034  1.00 46.86  ? 295  ALA A CA  1 
ATOM   2394 C  C   . ALA A 1 295 ? 3.098   8.942   20.594  1.00 44.57  ? 295  ALA A C   1 
ATOM   2395 O  O   . ALA A 1 295 ? 2.676   9.753   21.428  1.00 46.03  ? 295  ALA A O   1 
ATOM   2396 C  CB  . ALA A 1 295 ? 5.162   7.616   21.107  1.00 48.06  ? 295  ALA A CB  1 
ATOM   2397 N  N   . ARG A 1 296 ? 3.095   9.210   19.286  1.00 47.73  ? 296  ARG A N   1 
ATOM   2398 C  CA  . ARG A 1 296 ? 2.622   10.507  18.814  1.00 43.37  ? 296  ARG A CA  1 
ATOM   2399 C  C   . ARG A 1 296 ? 1.114   10.658  18.971  1.00 47.74  ? 296  ARG A C   1 
ATOM   2400 O  O   . ARG A 1 296 ? 0.627   11.760  19.243  1.00 48.03  ? 296  ARG A O   1 
ATOM   2401 C  CB  . ARG A 1 296 ? 3.023   10.712  17.349  1.00 51.07  ? 296  ARG A CB  1 
ATOM   2402 C  CG  . ARG A 1 296 ? 2.224   11.805  16.654  1.00 48.19  ? 296  ARG A CG  1 
ATOM   2403 C  CD  . ARG A 1 296 ? 2.816   12.174  15.301  1.00 54.39  ? 296  ARG A CD  1 
ATOM   2404 N  NE  . ARG A 1 296 ? 3.530   11.055  14.701  1.00 55.71  ? 296  ARG A NE  1 
ATOM   2405 C  CZ  . ARG A 1 296 ? 2.963   10.141  13.926  1.00 53.65  ? 296  ARG A CZ  1 
ATOM   2406 N  NH1 . ARG A 1 296 ? 1.662   10.170  13.663  1.00 58.16  ? 296  ARG A NH1 1 
ATOM   2407 N  NH2 . ARG A 1 296 ? 3.718   9.176   13.399  1.00 54.17  ? 296  ARG A NH2 1 
ATOM   2408 N  N   . VAL A 1 297 ? 0.357   9.576   18.815  1.00 45.26  ? 297  VAL A N   1 
ATOM   2409 C  CA  . VAL A 1 297 ? -1.098  9.691   18.812  1.00 42.75  ? 297  VAL A CA  1 
ATOM   2410 C  C   . VAL A 1 297 ? -1.692  9.515   20.201  1.00 39.65  ? 297  VAL A C   1 
ATOM   2411 O  O   . VAL A 1 297 ? -2.626  10.229  20.575  1.00 41.85  ? 297  VAL A O   1 
ATOM   2412 C  CB  . VAL A 1 297 ? -1.702  8.679   17.819  1.00 39.30  ? 297  VAL A CB  1 
ATOM   2413 C  CG1 . VAL A 1 297 ? -3.211  8.579   18.030  1.00 40.61  ? 297  VAL A CG1 1 
ATOM   2414 C  CG2 . VAL A 1 297 ? -1.363  9.079   16.388  1.00 43.06  ? 297  VAL A CG2 1 
ATOM   2415 N  N   . LEU A 1 298 ? -1.196  8.547   20.974  1.00 44.56  ? 298  LEU A N   1 
ATOM   2416 C  CA  . LEU A 1 298 ? -1.823  8.185   22.246  1.00 41.30  ? 298  LEU A CA  1 
ATOM   2417 C  C   . LEU A 1 298 ? -1.209  9.050   23.344  1.00 47.02  ? 298  LEU A C   1 
ATOM   2418 O  O   . LEU A 1 298 ? -0.393  8.609   24.159  1.00 49.43  ? 298  LEU A O   1 
ATOM   2419 C  CB  . LEU A 1 298 ? -1.662  6.693   22.512  1.00 39.58  ? 298  LEU A CB  1 
ATOM   2420 C  CG  . LEU A 1 298 ? -2.279  5.794   21.429  1.00 42.25  ? 298  LEU A CG  1 
ATOM   2421 C  CD1 . LEU A 1 298 ? -2.027  4.306   21.720  1.00 38.67  ? 298  LEU A CD1 1 
ATOM   2422 C  CD2 . LEU A 1 298 ? -3.765  6.082   21.319  1.00 40.68  ? 298  LEU A CD2 1 
ATOM   2423 N  N   . VAL A 1 299 ? -1.631  10.321  23.353  1.00 47.86  ? 299  VAL A N   1 
ATOM   2424 C  CA  . VAL A 1 299 ? -1.075  11.329  24.255  1.00 47.66  ? 299  VAL A CA  1 
ATOM   2425 C  C   . VAL A 1 299 ? -1.794  11.397  25.597  1.00 50.38  ? 299  VAL A C   1 
ATOM   2426 O  O   . VAL A 1 299 ? -1.361  12.151  26.483  1.00 49.74  ? 299  VAL A O   1 
ATOM   2427 C  CB  . VAL A 1 299 ? -1.114  12.720  23.588  1.00 47.87  ? 299  VAL A CB  1 
ATOM   2428 C  CG1 . VAL A 1 299 ? -0.287  12.724  22.302  1.00 49.33  ? 299  VAL A CG1 1 
ATOM   2429 C  CG2 . VAL A 1 299 ? -2.562  13.140  23.313  1.00 48.20  ? 299  VAL A CG2 1 
ATOM   2430 N  N   . ASP A 1 300 ? -2.879  10.655  25.778  1.00 46.15  ? 300  ASP A N   1 
ATOM   2431 C  CA  . ASP A 1 300 ? -3.586  10.624  27.046  1.00 47.93  ? 300  ASP A CA  1 
ATOM   2432 C  C   . ASP A 1 300 ? -3.391  9.285   27.753  1.00 48.05  ? 300  ASP A C   1 
ATOM   2433 O  O   . ASP A 1 300 ? -3.001  8.288   27.135  1.00 45.81  ? 300  ASP A O   1 
ATOM   2434 C  CB  . ASP A 1 300 ? -5.078  10.889  26.822  1.00 48.65  ? 300  ASP A CB  1 
ATOM   2435 C  CG  . ASP A 1 300 ? -5.333  12.241  26.191  1.00 53.74  ? 300  ASP A CG  1 
ATOM   2436 O  OD1 . ASP A 1 300 ? -4.620  13.202  26.550  1.00 50.38  ? 300  ASP A OD1 1 
ATOM   2437 O  OD2 . ASP A 1 300 ? -6.228  12.336  25.321  1.00 55.80  ? 300  ASP A OD2 1 
ATOM   2438 N  N   . PRO A 1 301 ? -3.636  9.229   29.064  1.00 49.52  ? 301  PRO A N   1 
ATOM   2439 C  CA  . PRO A 1 301 ? -3.508  7.935   29.761  1.00 47.67  ? 301  PRO A CA  1 
ATOM   2440 C  C   . PRO A 1 301 ? -4.428  6.868   29.194  1.00 45.99  ? 301  PRO A C   1 
ATOM   2441 O  O   . PRO A 1 301 ? -4.028  5.705   29.093  1.00 50.07  ? 301  PRO A O   1 
ATOM   2442 C  CB  . PRO A 1 301 ? -3.862  8.281   31.217  1.00 51.33  ? 301  PRO A CB  1 
ATOM   2443 C  CG  . PRO A 1 301 ? -3.686  9.765   31.325  1.00 53.28  ? 301  PRO A CG  1 
ATOM   2444 C  CD  . PRO A 1 301 ? -4.007  10.326  29.972  1.00 50.58  ? 301  PRO A CD  1 
ATOM   2445 N  N   . VAL A 1 302 ? -5.643  7.245   28.819  1.00 44.14  ? 302  VAL A N   1 
ATOM   2446 C  CA  . VAL A 1 302 ? -6.645  6.354   28.235  1.00 48.68  ? 302  VAL A CA  1 
ATOM   2447 C  C   . VAL A 1 302 ? -6.801  6.737   26.766  1.00 48.63  ? 302  VAL A C   1 
ATOM   2448 O  O   . VAL A 1 302 ? -7.094  7.902   26.476  1.00 48.14  ? 302  VAL A O   1 
ATOM   2449 C  CB  . VAL A 1 302 ? -8.000  6.488   28.960  1.00 47.50  ? 302  VAL A CB  1 
ATOM   2450 C  CG1 . VAL A 1 302 ? -9.022  5.525   28.383  1.00 53.22  ? 302  VAL A CG1 1 
ATOM   2451 C  CG2 . VAL A 1 302 ? -7.844  6.340   30.479  1.00 55.44  ? 302  VAL A CG2 1 
ATOM   2452 N  N   . PRO A 1 303 ? -6.632  5.814   25.820  1.00 47.48  ? 303  PRO A N   1 
ATOM   2453 C  CA  . PRO A 1 303 ? -6.891  6.165   24.413  1.00 42.25  ? 303  PRO A CA  1 
ATOM   2454 C  C   . PRO A 1 303 ? -8.364  6.477   24.182  1.00 42.51  ? 303  PRO A C   1 
ATOM   2455 O  O   . PRO A 1 303 ? -9.249  5.876   24.793  1.00 39.08  ? 303  PRO A O   1 
ATOM   2456 C  CB  . PRO A 1 303 ? -6.451  4.915   23.641  1.00 47.46  ? 303  PRO A CB  1 
ATOM   2457 C  CG  . PRO A 1 303 ? -5.558  4.161   24.598  1.00 46.43  ? 303  PRO A CG  1 
ATOM   2458 C  CD  . PRO A 1 303 ? -6.096  4.449   25.962  1.00 46.41  ? 303  PRO A CD  1 
ATOM   2459 N  N   . SER A 1 304 ? -8.626  7.436   23.293  1.00 39.69  ? 304  SER A N   1 
ATOM   2460 C  CA  . SER A 1 304 ? -9.992  7.762   22.916  1.00 37.83  ? 304  SER A CA  1 
ATOM   2461 C  C   . SER A 1 304 ? -10.344 7.131   21.571  1.00 37.11  ? 304  SER A C   1 
ATOM   2462 O  O   . SER A 1 304 ? -9.474  6.730   20.798  1.00 37.25  ? 304  SER A O   1 
ATOM   2463 C  CB  . SER A 1 304 ? -10.193 9.277   22.834  1.00 42.58  ? 304  SER A CB  1 
ATOM   2464 O  OG  . SER A 1 304 ? -9.555  9.786   21.684  1.00 41.79  ? 304  SER A OG  1 
ATOM   2465 N  N   . TYR A 1 305 ? -11.649 7.059   21.299  1.00 37.37  ? 305  TYR A N   1 
ATOM   2466 C  CA  . TYR A 1 305 ? -12.102 6.557   20.003  1.00 40.90  ? 305  TYR A CA  1 
ATOM   2467 C  C   . TYR A 1 305 ? -11.410 7.290   18.860  1.00 40.26  ? 305  TYR A C   1 
ATOM   2468 O  O   . TYR A 1 305 ? -10.907 6.667   17.918  1.00 39.89  ? 305  TYR A O   1 
ATOM   2469 C  CB  . TYR A 1 305 ? -13.617 6.697   19.891  1.00 39.59  ? 305  TYR A CB  1 
ATOM   2470 C  CG  . TYR A 1 305 ? -14.164 6.187   18.576  1.00 42.31  ? 305  TYR A CG  1 
ATOM   2471 C  CD1 . TYR A 1 305 ? -14.474 4.843   18.412  1.00 41.15  ? 305  TYR A CD1 1 
ATOM   2472 C  CD2 . TYR A 1 305 ? -14.370 7.048   17.501  1.00 45.15  ? 305  TYR A CD2 1 
ATOM   2473 C  CE1 . TYR A 1 305 ? -14.969 4.361   17.212  1.00 44.02  ? 305  TYR A CE1 1 
ATOM   2474 C  CE2 . TYR A 1 305 ? -14.864 6.568   16.291  1.00 44.04  ? 305  TYR A CE2 1 
ATOM   2475 C  CZ  . TYR A 1 305 ? -15.157 5.220   16.162  1.00 43.00  ? 305  TYR A CZ  1 
ATOM   2476 O  OH  . TYR A 1 305 ? -15.654 4.720   14.979  1.00 52.03  ? 305  TYR A OH  1 
ATOM   2477 N  N   . LYS A 1 306 ? -11.362 8.626   18.939  1.00 41.37  ? 306  LYS A N   1 
ATOM   2478 C  CA  . LYS A 1 306 ? -10.786 9.423   17.858  1.00 41.93  ? 306  LYS A CA  1 
ATOM   2479 C  C   . LYS A 1 306 ? -9.310  9.116   17.668  1.00 40.91  ? 306  LYS A C   1 
ATOM   2480 O  O   . LYS A 1 306 ? -8.820  9.068   16.532  1.00 40.71  ? 306  LYS A O   1 
ATOM   2481 C  CB  . LYS A 1 306 ? -10.989 10.916  18.139  1.00 46.94  ? 306  LYS A CB  1 
ATOM   2482 C  CG  . LYS A 1 306 ? -12.416 11.398  17.965  1.00 52.46  ? 306  LYS A CG  1 
ATOM   2483 C  CD  . LYS A 1 306 ? -12.489 12.916  18.022  1.00 54.76  ? 306  LYS A CD  1 
ATOM   2484 C  CE  . LYS A 1 306 ? -13.883 13.366  18.422  1.00 64.06  ? 306  LYS A CE  1 
ATOM   2485 N  NZ  . LYS A 1 306 ? -13.832 14.485  19.411  1.00 71.39  ? 306  LYS A NZ  1 
ATOM   2486 N  N   . GLN A 1 307 ? -8.581  8.903   18.768  1.00 40.94  ? 307  GLN A N   1 
ATOM   2487 C  CA  . GLN A 1 307 ? -7.154  8.625   18.663  1.00 38.29  ? 307  GLN A CA  1 
ATOM   2488 C  C   . GLN A 1 307 ? -6.899  7.274   18.005  1.00 36.44  ? 307  GLN A C   1 
ATOM   2489 O  O   . GLN A 1 307 ? -5.974  7.139   17.194  1.00 40.29  ? 307  GLN A O   1 
ATOM   2490 C  CB  . GLN A 1 307 ? -6.510  8.694   20.052  1.00 38.72  ? 307  GLN A CB  1 
ATOM   2491 C  CG  . GLN A 1 307 ? -6.541  10.103  20.618  1.00 41.70  ? 307  GLN A CG  1 
ATOM   2492 C  CD  . GLN A 1 307 ? -6.232  10.158  22.104  1.00 46.49  ? 307  GLN A CD  1 
ATOM   2493 O  OE1 . GLN A 1 307 ? -6.352  9.160   22.814  1.00 42.72  ? 307  GLN A OE1 1 
ATOM   2494 N  NE2 . GLN A 1 307 ? -5.838  11.336  22.582  1.00 46.02  ? 307  GLN A NE2 1 
ATOM   2495 N  N   . VAL A 1 308 ? -7.702  6.256   18.341  1.00 38.28  ? 308  VAL A N   1 
ATOM   2496 C  CA  . VAL A 1 308 ? -7.505  4.951   17.709  1.00 38.29  ? 308  VAL A CA  1 
ATOM   2497 C  C   . VAL A 1 308 ? -7.713  5.059   16.202  1.00 37.13  ? 308  VAL A C   1 
ATOM   2498 O  O   . VAL A 1 308 ? -7.029  4.397   15.415  1.00 37.67  ? 308  VAL A O   1 
ATOM   2499 C  CB  . VAL A 1 308 ? -8.434  3.895   18.340  1.00 39.73  ? 308  VAL A CB  1 
ATOM   2500 C  CG1 . VAL A 1 308 ? -8.402  2.590   17.521  1.00 35.83  ? 308  VAL A CG1 1 
ATOM   2501 C  CG2 . VAL A 1 308 ? -8.040  3.642   19.799  1.00 38.25  ? 308  VAL A CG2 1 
ATOM   2502 N  N   . LYS A 1 309 ? -8.652  5.904   15.775  1.00 39.56  ? 309  LYS A N   1 
ATOM   2503 C  CA  . LYS A 1 309 ? -8.873  6.091   14.344  1.00 42.45  ? 309  LYS A CA  1 
ATOM   2504 C  C   . LYS A 1 309 ? -7.671  6.727   13.656  1.00 41.52  ? 309  LYS A C   1 
ATOM   2505 O  O   . LYS A 1 309 ? -7.540  6.620   12.433  1.00 41.37  ? 309  LYS A O   1 
ATOM   2506 C  CB  . LYS A 1 309 ? -10.123 6.935   14.110  1.00 42.35  ? 309  LYS A CB  1 
ATOM   2507 C  CG  . LYS A 1 309 ? -11.416 6.220   14.486  1.00 43.96  ? 309  LYS A CG  1 
ATOM   2508 C  CD  . LYS A 1 309 ? -11.532 4.910   13.706  1.00 46.16  ? 309  LYS A CD  1 
ATOM   2509 C  CE  . LYS A 1 309 ? -12.895 4.263   13.857  1.00 49.26  ? 309  LYS A CE  1 
ATOM   2510 N  NZ  . LYS A 1 309 ? -12.912 2.903   13.230  1.00 53.68  ? 309  LYS A NZ  1 
ATOM   2511 N  N   . GLN A 1 310 ? -6.788  7.372   14.406  1.00 40.23  ? 310  GLN A N   1 
ATOM   2512 C  CA  . GLN A 1 310 ? -5.593  7.965   13.825  1.00 41.95  ? 310  GLN A CA  1 
ATOM   2513 C  C   . GLN A 1 310 ? -4.385  7.041   13.870  1.00 41.70  ? 310  GLN A C   1 
ATOM   2514 O  O   . GLN A 1 310 ? -3.304  7.437   13.418  1.00 41.35  ? 310  GLN A O   1 
ATOM   2515 C  CB  . GLN A 1 310 ? -5.278  9.295   14.520  1.00 42.64  ? 310  GLN A CB  1 
ATOM   2516 C  CG  . GLN A 1 310 ? -6.313  10.376  14.217  1.00 46.29  ? 310  GLN A CG  1 
ATOM   2517 C  CD  . GLN A 1 310 ? -6.604  10.497  12.722  1.00 51.34  ? 310  GLN A CD  1 
ATOM   2518 O  OE1 . GLN A 1 310 ? -5.683  10.509  11.904  1.00 52.59  ? 310  GLN A OE1 1 
ATOM   2519 N  NE2 . GLN A 1 310 ? -7.884  10.588  12.360  1.00 48.29  ? 310  GLN A NE2 1 
ATOM   2520 N  N   . LEU A 1 311 ? -4.537  5.813   14.364  1.00 36.30  ? 311  LEU A N   1 
ATOM   2521 C  CA  . LEU A 1 311 ? -3.428  4.853   14.388  1.00 36.69  ? 311  LEU A CA  1 
ATOM   2522 C  C   . LEU A 1 311 ? -3.372  4.127   13.041  1.00 42.24  ? 311  LEU A C   1 
ATOM   2523 O  O   . LEU A 1 311 ? -3.615  2.922   12.906  1.00 38.56  ? 311  LEU A O   1 
ATOM   2524 C  CB  . LEU A 1 311 ? -3.572  3.890   15.560  1.00 37.06  ? 311  LEU A CB  1 
ATOM   2525 C  CG  . LEU A 1 311 ? -3.412  4.508   16.958  1.00 36.53  ? 311  LEU A CG  1 
ATOM   2526 C  CD1 . LEU A 1 311 ? -3.717  3.463   18.028  1.00 35.38  ? 311  LEU A CD1 1 
ATOM   2527 C  CD2 . LEU A 1 311 ? -1.999  5.076   17.153  1.00 39.41  ? 311  LEU A CD2 1 
ATOM   2528 N  N   . LYS A 1 312 ? -3.023  4.905   12.024  1.00 38.94  ? 312  LYS A N   1 
ATOM   2529 C  CA  . LYS A 1 312 ? -3.230  4.452   10.660  1.00 40.97  ? 312  LYS A CA  1 
ATOM   2530 C  C   . LYS A 1 312 ? -2.162  3.440   10.256  1.00 38.36  ? 312  LYS A C   1 
ATOM   2531 O  O   . LYS A 1 312 ? -2.467  2.441   9.597   1.00 37.21  ? 312  LYS A O   1 
ATOM   2532 C  CB  . LYS A 1 312 ? -3.285  5.687   9.760   1.00 41.95  ? 312  LYS A CB  1 
ATOM   2533 C  CG  . LYS A 1 312 ? -4.731  6.100   9.586   1.00 45.69  ? 312  LYS A CG  1 
ATOM   2534 C  CD  . LYS A 1 312 ? -4.923  7.546   9.186   1.00 52.77  ? 312  LYS A CD  1 
ATOM   2535 C  CE  . LYS A 1 312 ? -6.383  7.769   8.812   1.00 54.65  ? 312  LYS A CE  1 
ATOM   2536 N  NZ  . LYS A 1 312 ? -6.657  9.171   8.410   1.00 64.30  ? 312  LYS A NZ  1 
ATOM   2537 N  N   . TYR A 1 313 ? -0.916  3.639   10.699  1.00 37.54  ? 313  TYR A N   1 
ATOM   2538 C  CA  . TYR A 1 313 ? 0.118   2.653   10.423  1.00 36.15  ? 313  TYR A CA  1 
ATOM   2539 C  C   . TYR A 1 313 ? -0.124  1.353   11.184  1.00 35.75  ? 313  TYR A C   1 
ATOM   2540 O  O   . TYR A 1 313 ? 0.130   0.263   10.653  1.00 36.05  ? 313  TYR A O   1 
ATOM   2541 C  CB  . TYR A 1 313 ? 1.498   3.207   10.767  1.00 40.48  ? 313  TYR A CB  1 
ATOM   2542 C  CG  . TYR A 1 313 ? 2.601   2.322   10.245  1.00 38.33  ? 313  TYR A CG  1 
ATOM   2543 C  CD1 . TYR A 1 313 ? 2.898   2.288   8.885   1.00 42.85  ? 313  TYR A CD1 1 
ATOM   2544 C  CD2 . TYR A 1 313 ? 3.336   1.506   11.094  1.00 39.30  ? 313  TYR A CD2 1 
ATOM   2545 C  CE1 . TYR A 1 313 ? 3.893   1.479   8.398   1.00 43.10  ? 313  TYR A CE1 1 
ATOM   2546 C  CE2 . TYR A 1 313 ? 4.332   0.684   10.610  1.00 40.32  ? 313  TYR A CE2 1 
ATOM   2547 C  CZ  . TYR A 1 313 ? 4.606   0.682   9.257   1.00 42.68  ? 313  TYR A CZ  1 
ATOM   2548 O  OH  . TYR A 1 313 ? 5.585   -0.125  8.756   1.00 42.39  ? 313  TYR A OH  1 
ATOM   2549 N  N   . VAL A 1 314 ? -0.568  1.442   12.441  1.00 36.70  ? 314  VAL A N   1 
ATOM   2550 C  CA  . VAL A 1 314 ? -0.947  0.230   13.165  1.00 36.24  ? 314  VAL A CA  1 
ATOM   2551 C  C   . VAL A 1 314 ? -2.007  -0.530  12.373  1.00 34.06  ? 314  VAL A C   1 
ATOM   2552 O  O   . VAL A 1 314 ? -1.985  -1.766  12.291  1.00 34.59  ? 314  VAL A O   1 
ATOM   2553 C  CB  . VAL A 1 314 ? -1.439  0.590   14.578  1.00 35.35  ? 314  VAL A CB  1 
ATOM   2554 C  CG1 . VAL A 1 314 ? -1.926  -0.660  15.329  1.00 36.45  ? 314  VAL A CG1 1 
ATOM   2555 C  CG2 . VAL A 1 314 ? -0.323  1.324   15.384  1.00 35.62  ? 314  VAL A CG2 1 
ATOM   2556 N  N   . GLY A 1 315 ? -2.936  0.204   11.764  1.00 35.64  ? 315  GLY A N   1 
ATOM   2557 C  CA  . GLY A 1 315 ? -3.935  -0.434  10.914  1.00 37.04  ? 315  GLY A CA  1 
ATOM   2558 C  C   . GLY A 1 315 ? -3.329  -1.204  9.750   1.00 39.46  ? 315  GLY A C   1 
ATOM   2559 O  O   . GLY A 1 315 ? -3.788  -2.303  9.415   1.00 35.64  ? 315  GLY A O   1 
ATOM   2560 N  N   . MET A 1 316 ? -2.312  -0.628  9.092   1.00 36.20  ? 316  MET A N   1 
ATOM   2561 C  CA  . MET A 1 316 ? -1.649  -1.347  8.006   1.00 33.40  ? 316  MET A CA  1 
ATOM   2562 C  C   . MET A 1 316 ? -0.853  -2.544  8.513   1.00 34.77  ? 316  MET A C   1 
ATOM   2563 O  O   . MET A 1 316 ? -0.756  -3.560  7.813   1.00 33.02  ? 316  MET A O   1 
ATOM   2564 C  CB  . MET A 1 316 ? -0.736  -0.404  7.199   1.00 37.26  ? 316  MET A CB  1 
ATOM   2565 C  CG  . MET A 1 316 ? -1.461  0.833   6.663   1.00 42.17  ? 316  MET A CG  1 
ATOM   2566 S  SD  . MET A 1 316 ? -0.367  2.121   5.980   1.00 51.08  ? 316  MET A SD  1 
ATOM   2567 C  CE  . MET A 1 316 ? 1.083   1.200   5.537   1.00 47.31  ? 316  MET A CE  1 
ATOM   2568 N  N   . VAL A 1 317 ? -0.262  -2.443  9.708   1.00 35.71  ? 317  VAL A N   1 
ATOM   2569 C  CA  . VAL A 1 317 ? 0.387   -3.601  10.322  1.00 34.53  ? 317  VAL A CA  1 
ATOM   2570 C  C   . VAL A 1 317 ? -0.595  -4.763  10.437  1.00 34.46  ? 317  VAL A C   1 
ATOM   2571 O  O   . VAL A 1 317 ? -0.290  -5.905  10.075  1.00 35.04  ? 317  VAL A O   1 
ATOM   2572 C  CB  . VAL A 1 317 ? 0.960   -3.216  11.700  1.00 38.05  ? 317  VAL A CB  1 
ATOM   2573 C  CG1 . VAL A 1 317 ? 1.301   -4.472  12.499  1.00 35.28  ? 317  VAL A CG1 1 
ATOM   2574 C  CG2 . VAL A 1 317 ? 2.185   -2.299  11.549  1.00 36.52  ? 317  VAL A CG2 1 
ATOM   2575 N  N   . LEU A 1 318 ? -1.795  -4.480  10.940  1.00 35.97  ? 318  LEU A N   1 
ATOM   2576 C  CA  . LEU A 1 318 ? -2.785  -5.528  11.123  1.00 35.16  ? 318  LEU A CA  1 
ATOM   2577 C  C   . LEU A 1 318 ? -3.235  -6.097  9.787   1.00 33.42  ? 318  LEU A C   1 
ATOM   2578 O  O   . LEU A 1 318 ? -3.399  -7.310  9.651   1.00 31.88  ? 318  LEU A O   1 
ATOM   2579 C  CB  . LEU A 1 318 ? -3.972  -4.975  11.912  1.00 33.17  ? 318  LEU A CB  1 
ATOM   2580 C  CG  . LEU A 1 318 ? -3.630  -4.651  13.366  1.00 33.68  ? 318  LEU A CG  1 
ATOM   2581 C  CD1 . LEU A 1 318 ? -4.728  -3.766  13.947  1.00 36.01  ? 318  LEU A CD1 1 
ATOM   2582 C  CD2 . LEU A 1 318 ? -3.491  -5.967  14.130  1.00 33.29  ? 318  LEU A CD2 1 
ATOM   2583 N  N   . ASN A 1 319 ? -3.416  -5.244  8.775   1.00 33.41  ? 319  ASN A N   1 
ATOM   2584 C  CA  . ASN A 1 319 ? -3.781  -5.767  7.468   1.00 32.78  ? 319  ASN A CA  1 
ATOM   2585 C  C   . ASN A 1 319 ? -2.677  -6.650  6.902   1.00 32.82  ? 319  ASN A C   1 
ATOM   2586 O  O   . ASN A 1 319 ? -2.956  -7.666  6.266   1.00 32.66  ? 319  ASN A O   1 
ATOM   2587 C  CB  . ASN A 1 319 ? -4.124  -4.619  6.521   1.00 35.36  ? 319  ASN A CB  1 
ATOM   2588 C  CG  . ASN A 1 319 ? -5.548  -4.147  6.704   1.00 41.38  ? 319  ASN A CG  1 
ATOM   2589 O  OD1 . ASN A 1 319 ? -6.444  -4.952  6.969   1.00 38.63  ? 319  ASN A OD1 1 
ATOM   2590 N  ND2 . ASN A 1 319 ? -5.764  -2.842  6.601   1.00 45.05  ? 319  ASN A ND2 1 
ATOM   2591 N  N   . GLU A 1 320 ? -1.411  -6.278  7.119   1.00 33.09  ? 320  GLU A N   1 
ATOM   2592 C  CA  . GLU A 1 320 ? -0.320  -7.087  6.581   1.00 33.27  ? 320  GLU A CA  1 
ATOM   2593 C  C   . GLU A 1 320 ? -0.234  -8.435  7.304   1.00 34.21  ? 320  GLU A C   1 
ATOM   2594 O  O   . GLU A 1 320 ? 0.058   -9.464  6.681   1.00 33.17  ? 320  GLU A O   1 
ATOM   2595 C  CB  . GLU A 1 320 ? 0.987   -6.284  6.677   1.00 33.69  ? 320  GLU A CB  1 
ATOM   2596 C  CG  . GLU A 1 320 ? 2.249   -6.978  6.171   1.00 37.71  ? 320  GLU A CG  1 
ATOM   2597 C  CD  . GLU A 1 320 ? 2.273   -7.189  4.665   1.00 39.28  ? 320  GLU A CD  1 
ATOM   2598 O  OE1 . GLU A 1 320 ? 1.207   -7.105  4.005   1.00 36.87  ? 320  GLU A OE1 1 
ATOM   2599 O  OE2 . GLU A 1 320 ? 3.371   -7.463  4.132   1.00 37.28  ? 320  GLU A OE2 1 
ATOM   2600 N  N   . ALA A 1 321 ? -0.544  -8.455  8.609   1.00 33.55  ? 321  ALA A N   1 
ATOM   2601 C  CA  . ALA A 1 321 ? -0.635  -9.713  9.350   1.00 32.76  ? 321  ALA A CA  1 
ATOM   2602 C  C   . ALA A 1 321 ? -1.806  -10.566 8.862   1.00 31.08  ? 321  ALA A C   1 
ATOM   2603 O  O   . ALA A 1 321 ? -1.696  -11.794 8.791   1.00 32.38  ? 321  ALA A O   1 
ATOM   2604 C  CB  . ALA A 1 321 ? -0.754  -9.426  10.856  1.00 32.33  ? 321  ALA A CB  1 
ATOM   2605 N  N   . LEU A 1 322 ? -2.941  -9.936  8.522   1.00 32.78  ? 322  LEU A N   1 
ATOM   2606 C  CA  . LEU A 1 322 ? -4.035  -10.687 7.908   1.00 33.22  ? 322  LEU A CA  1 
ATOM   2607 C  C   . LEU A 1 322 ? -3.682  -11.172 6.504   1.00 35.18  ? 322  LEU A C   1 
ATOM   2608 O  O   . LEU A 1 322 ? -4.228  -12.180 6.041   1.00 32.76  ? 322  LEU A O   1 
ATOM   2609 C  CB  . LEU A 1 322 ? -5.310  -9.838  7.842   1.00 31.19  ? 322  LEU A CB  1 
ATOM   2610 C  CG  . LEU A 1 322 ? -6.015  -9.608  9.182   1.00 33.08  ? 322  LEU A CG  1 
ATOM   2611 C  CD1 . LEU A 1 322 ? -7.178  -8.633  8.978   1.00 37.32  ? 322  LEU A CD1 1 
ATOM   2612 C  CD2 . LEU A 1 322 ? -6.493  -10.925 9.786   1.00 36.67  ? 322  LEU A CD2 1 
ATOM   2613 N  N   . ARG A 1 323 ? -2.809  -10.459 5.786   1.00 32.94  ? 323  ARG A N   1 
ATOM   2614 C  CA  . ARG A 1 323 ? -2.409  -10.961 4.476   1.00 31.83  ? 323  ARG A CA  1 
ATOM   2615 C  C   . ARG A 1 323 ? -1.657  -12.280 4.618   1.00 30.35  ? 323  ARG A C   1 
ATOM   2616 O  O   . ARG A 1 323 ? -2.015  -13.287 4.006   1.00 32.32  ? 323  ARG A O   1 
ATOM   2617 C  CB  . ARG A 1 323 ? -1.557  -9.925  3.739   1.00 31.16  ? 323  ARG A CB  1 
ATOM   2618 C  CG  . ARG A 1 323 ? -1.250  -10.354 2.299   1.00 34.92  ? 323  ARG A CG  1 
ATOM   2619 C  CD  . ARG A 1 323 ? -0.304  -9.375  1.568   1.00 34.02  ? 323  ARG A CD  1 
ATOM   2620 N  NE  . ARG A 1 323 ? 1.012   -9.273  2.199   1.00 34.74  ? 323  ARG A NE  1 
ATOM   2621 C  CZ  . ARG A 1 323 ? 2.019   -10.116 1.998   1.00 35.58  ? 323  ARG A CZ  1 
ATOM   2622 N  NH1 . ARG A 1 323 ? 1.900   -11.152 1.200   1.00 35.66  ? 323  ARG A NH1 1 
ATOM   2623 N  NH2 . ARG A 1 323 ? 3.171   -9.923  2.641   1.00 34.70  ? 323  ARG A NH2 1 
ATOM   2624 N  N   . LEU A 1 324 ? -0.633  -12.308 5.478   1.00 34.75  ? 324  LEU A N   1 
ATOM   2625 C  CA  . LEU A 1 324 ? 0.211   -13.499 5.555   1.00 33.45  ? 324  LEU A CA  1 
ATOM   2626 C  C   . LEU A 1 324 ? -0.486  -14.657 6.265   1.00 35.88  ? 324  LEU A C   1 
ATOM   2627 O  O   . LEU A 1 324 ? -0.322  -15.821 5.881   1.00 35.39  ? 324  LEU A O   1 
ATOM   2628 C  CB  . LEU A 1 324 ? 1.522   -13.136 6.248   1.00 39.39  ? 324  LEU A CB  1 
ATOM   2629 C  CG  . LEU A 1 324 ? 2.423   -12.375 5.269   1.00 36.76  ? 324  LEU A CG  1 
ATOM   2630 C  CD1 . LEU A 1 324 ? 3.635   -11.765 5.984   1.00 42.15  ? 324  LEU A CD1 1 
ATOM   2631 C  CD2 . LEU A 1 324 ? 2.850   -13.308 4.130   1.00 41.21  ? 324  LEU A CD2 1 
ATOM   2632 N  N   . TRP A 1 325 ? -1.267  -14.376 7.300   1.00 33.33  ? 325  TRP A N   1 
ATOM   2633 C  CA  . TRP A 1 325 ? -1.923  -15.436 8.066   1.00 31.87  ? 325  TRP A CA  1 
ATOM   2634 C  C   . TRP A 1 325 ? -3.344  -15.028 8.413   1.00 32.48  ? 325  TRP A C   1 
ATOM   2635 O  O   . TRP A 1 325 ? -3.650  -14.670 9.555   1.00 33.34  ? 325  TRP A O   1 
ATOM   2636 C  CB  . TRP A 1 325 ? -1.105  -15.782 9.311   1.00 33.73  ? 325  TRP A CB  1 
ATOM   2637 C  CG  . TRP A 1 325 ? 0.082   -16.558 8.885   1.00 33.56  ? 325  TRP A CG  1 
ATOM   2638 C  CD1 . TRP A 1 325 ? 1.385   -16.171 8.970   1.00 37.01  ? 325  TRP A CD1 1 
ATOM   2639 C  CD2 . TRP A 1 325 ? 0.075   -17.827 8.227   1.00 35.80  ? 325  TRP A CD2 1 
ATOM   2640 N  NE1 . TRP A 1 325 ? 2.196   -17.136 8.422   1.00 36.40  ? 325  TRP A NE1 1 
ATOM   2641 C  CE2 . TRP A 1 325 ? 1.416   -18.166 7.963   1.00 37.97  ? 325  TRP A CE2 1 
ATOM   2642 C  CE3 . TRP A 1 325 ? -0.936  -18.714 7.835   1.00 36.18  ? 325  TRP A CE3 1 
ATOM   2643 C  CZ2 . TRP A 1 325 ? 1.777   -19.359 7.327   1.00 38.44  ? 325  TRP A CZ2 1 
ATOM   2644 C  CZ3 . TRP A 1 325 ? -0.575  -19.906 7.195   1.00 36.75  ? 325  TRP A CZ3 1 
ATOM   2645 C  CH2 . TRP A 1 325 ? 0.778   -20.213 6.959   1.00 40.07  ? 325  TRP A CH2 1 
ATOM   2646 N  N   . PRO A 1 326 ? -4.251  -15.081 7.441   1.00 32.09  ? 326  PRO A N   1 
ATOM   2647 C  CA  . PRO A 1 326 ? -5.667  -14.787 7.731   1.00 30.92  ? 326  PRO A CA  1 
ATOM   2648 C  C   . PRO A 1 326 ? -6.224  -15.866 8.647   1.00 32.47  ? 326  PRO A C   1 
ATOM   2649 O  O   . PRO A 1 326 ? -6.159  -17.058 8.332   1.00 33.11  ? 326  PRO A O   1 
ATOM   2650 C  CB  . PRO A 1 326 ? -6.320  -14.808 6.343   1.00 32.35  ? 326  PRO A CB  1 
ATOM   2651 C  CG  . PRO A 1 326 ? -5.418  -15.697 5.516   1.00 32.77  ? 326  PRO A CG  1 
ATOM   2652 C  CD  . PRO A 1 326 ? -4.027  -15.421 6.023   1.00 30.66  ? 326  PRO A CD  1 
ATOM   2653 N  N   . THR A 1 327 ? -6.767  -15.443 9.794   1.00 34.23  ? 327  THR A N   1 
ATOM   2654 C  CA  . THR A 1 327 ? -7.009  -16.374 10.891  1.00 32.56  ? 327  THR A CA  1 
ATOM   2655 C  C   . THR A 1 327 ? -8.296  -17.180 10.721  1.00 33.25  ? 327  THR A C   1 
ATOM   2656 O  O   . THR A 1 327 ? -8.448  -18.222 11.371  1.00 31.39  ? 327  THR A O   1 
ATOM   2657 C  CB  . THR A 1 327 ? -6.994  -15.607 12.219  1.00 31.98  ? 327  THR A CB  1 
ATOM   2658 O  OG1 . THR A 1 327 ? -7.826  -14.448 12.109  1.00 31.11  ? 327  THR A OG1 1 
ATOM   2659 C  CG2 . THR A 1 327 ? -5.561  -15.137 12.536  1.00 32.66  ? 327  THR A CG2 1 
ATOM   2660 N  N   . ALA A 1 328 ? -9.203  -16.754 9.834   1.00 31.61  ? 328  ALA A N   1 
ATOM   2661 C  CA  . ALA A 1 328 ? -10.261 -17.626 9.332   1.00 30.51  ? 328  ALA A CA  1 
ATOM   2662 C  C   . ALA A 1 328 ? -9.875  -17.979 7.899   1.00 32.58  ? 328  ALA A C   1 
ATOM   2663 O  O   . ALA A 1 328 ? -10.225 -17.249 6.958   1.00 33.73  ? 328  ALA A O   1 
ATOM   2664 C  CB  . ALA A 1 328 ? -11.627 -16.939 9.387   1.00 32.30  ? 328  ALA A CB  1 
ATOM   2665 N  N   . PRO A 1 329 ? -9.142  -19.076 7.680   1.00 32.79  ? 329  PRO A N   1 
ATOM   2666 C  CA  . PRO A 1 329 ? -8.275  -19.165 6.496   1.00 32.01  ? 329  PRO A CA  1 
ATOM   2667 C  C   . PRO A 1 329 ? -8.951  -19.649 5.226   1.00 33.75  ? 329  PRO A C   1 
ATOM   2668 O  O   . PRO A 1 329 ? -8.267  -19.814 4.209   1.00 33.43  ? 329  PRO A O   1 
ATOM   2669 C  CB  . PRO A 1 329 ? -7.183  -20.154 6.946   1.00 31.21  ? 329  PRO A CB  1 
ATOM   2670 C  CG  . PRO A 1 329 ? -7.872  -21.060 7.932   1.00 34.77  ? 329  PRO A CG  1 
ATOM   2671 C  CD  . PRO A 1 329 ? -8.902  -20.175 8.647   1.00 33.59  ? 329  PRO A CD  1 
ATOM   2672 N  N   . ALA A 1 330 ? -10.255 -19.887 5.228   1.00 31.73  ? 330  ALA A N   1 
ATOM   2673 C  CA  . ALA A 1 330 ? -10.912 -20.270 3.988   1.00 32.92  ? 330  ALA A CA  1 
ATOM   2674 C  C   . ALA A 1 330 ? -12.381 -19.922 4.115   1.00 30.95  ? 330  ALA A C   1 
ATOM   2675 O  O   . ALA A 1 330 ? -12.909 -19.780 5.222   1.00 33.36  ? 330  ALA A O   1 
ATOM   2676 C  CB  . ALA A 1 330 ? -10.748 -21.766 3.681   1.00 34.94  ? 330  ALA A CB  1 
ATOM   2677 N  N   . PHE A 1 331 ? -13.019 -19.763 2.963   1.00 30.70  ? 331  PHE A N   1 
ATOM   2678 C  CA  . PHE A 1 331 ? -14.463 -19.758 2.879   1.00 32.75  ? 331  PHE A CA  1 
ATOM   2679 C  C   . PHE A 1 331 ? -14.841 -20.508 1.617   1.00 32.90  ? 331  PHE A C   1 
ATOM   2680 O  O   . PHE A 1 331 ? -14.005 -20.742 0.738   1.00 33.90  ? 331  PHE A O   1 
ATOM   2681 C  CB  . PHE A 1 331 ? -15.061 -18.342 2.919   1.00 33.10  ? 331  PHE A CB  1 
ATOM   2682 C  CG  . PHE A 1 331 ? -14.537 -17.400 1.866   1.00 31.31  ? 331  PHE A CG  1 
ATOM   2683 C  CD1 . PHE A 1 331 ? -13.399 -16.645 2.091   1.00 34.31  ? 331  PHE A CD1 1 
ATOM   2684 C  CD2 . PHE A 1 331 ? -15.222 -17.227 0.672   1.00 30.11  ? 331  PHE A CD2 1 
ATOM   2685 C  CE1 . PHE A 1 331 ? -12.940 -15.743 1.147   1.00 34.88  ? 331  PHE A CE1 1 
ATOM   2686 C  CE2 . PHE A 1 331 ? -14.763 -16.316 -0.288  1.00 34.39  ? 331  PHE A CE2 1 
ATOM   2687 C  CZ  . PHE A 1 331 ? -13.623 -15.581 -0.048  1.00 33.36  ? 331  PHE A CZ  1 
ATOM   2688 N  N   . SER A 1 332 ? -16.103 -20.908 1.554   1.00 34.39  ? 332  SER A N   1 
ATOM   2689 C  CA  . SER A 1 332 ? -16.583 -21.836 0.545   1.00 35.55  ? 332  SER A CA  1 
ATOM   2690 C  C   . SER A 1 332 ? -17.709 -21.175 -0.234  1.00 34.56  ? 332  SER A C   1 
ATOM   2691 O  O   . SER A 1 332 ? -18.446 -20.345 0.305   1.00 34.45  ? 332  SER A O   1 
ATOM   2692 C  CB  . SER A 1 332 ? -17.056 -23.137 1.211   1.00 33.13  ? 332  SER A CB  1 
ATOM   2693 O  OG  . SER A 1 332 ? -17.484 -24.097 0.265   1.00 35.95  ? 332  SER A OG  1 
ATOM   2694 N  N   . LEU A 1 333 ? -17.824 -21.540 -1.510  1.00 32.87  ? 333  LEU A N   1 
ATOM   2695 C  CA  . LEU A 1 333 ? -18.819 -20.977 -2.414  1.00 32.87  ? 333  LEU A CA  1 
ATOM   2696 C  C   . LEU A 1 333 ? -19.421 -22.106 -3.240  1.00 33.68  ? 333  LEU A C   1 
ATOM   2697 O  O   . LEU A 1 333 ? -18.802 -23.158 -3.426  1.00 36.02  ? 333  LEU A O   1 
ATOM   2698 C  CB  . LEU A 1 333 ? -18.196 -19.909 -3.344  1.00 33.07  ? 333  LEU A CB  1 
ATOM   2699 C  CG  . LEU A 1 333 ? -17.449 -18.749 -2.665  1.00 35.97  ? 333  LEU A CG  1 
ATOM   2700 C  CD1 . LEU A 1 333 ? -16.422 -18.097 -3.597  1.00 36.04  ? 333  LEU A CD1 1 
ATOM   2701 C  CD2 . LEU A 1 333 ? -18.442 -17.701 -2.123  1.00 35.43  ? 333  LEU A CD2 1 
ATOM   2702 N  N   . TYR A 1 334 ? -20.640 -21.887 -3.735  1.00 33.70  ? 334  TYR A N   1 
ATOM   2703 C  CA  . TYR A 1 334 ? -21.237 -22.772 -4.734  1.00 34.17  ? 334  TYR A CA  1 
ATOM   2704 C  C   . TYR A 1 334 ? -21.740 -21.960 -5.920  1.00 36.37  ? 334  TYR A C   1 
ATOM   2705 O  O   . TYR A 1 334 ? -22.154 -20.806 -5.784  1.00 35.11  ? 334  TYR A O   1 
ATOM   2706 C  CB  . TYR A 1 334 ? -22.385 -23.623 -4.151  1.00 35.46  ? 334  TYR A CB  1 
ATOM   2707 C  CG  . TYR A 1 334 ? -23.629 -22.821 -3.787  1.00 33.98  ? 334  TYR A CG  1 
ATOM   2708 C  CD1 . TYR A 1 334 ? -23.754 -22.200 -2.538  1.00 34.60  ? 334  TYR A CD1 1 
ATOM   2709 C  CD2 . TYR A 1 334 ? -24.681 -22.686 -4.694  1.00 34.57  ? 334  TYR A CD2 1 
ATOM   2710 C  CE1 . TYR A 1 334 ? -24.892 -21.454 -2.215  1.00 35.73  ? 334  TYR A CE1 1 
ATOM   2711 C  CE2 . TYR A 1 334 ? -25.805 -21.951 -4.385  1.00 38.36  ? 334  TYR A CE2 1 
ATOM   2712 C  CZ  . TYR A 1 334 ? -25.915 -21.339 -3.145  1.00 38.69  ? 334  TYR A CZ  1 
ATOM   2713 O  OH  . TYR A 1 334 ? -27.051 -20.613 -2.853  1.00 38.96  ? 334  TYR A OH  1 
ATOM   2714 N  N   . ALA A 1 335 ? -21.691 -22.577 -7.100  1.00 35.97  ? 335  ALA A N   1 
ATOM   2715 C  CA  . ALA A 1 335 ? -22.151 -21.894 -8.305  1.00 37.13  ? 335  ALA A CA  1 
ATOM   2716 C  C   . ALA A 1 335 ? -23.672 -21.798 -8.317  1.00 37.53  ? 335  ALA A C   1 
ATOM   2717 O  O   . ALA A 1 335 ? -24.376 -22.805 -8.193  1.00 36.78  ? 335  ALA A O   1 
ATOM   2718 C  CB  . ALA A 1 335 ? -21.652 -22.630 -9.555  1.00 37.87  ? 335  ALA A CB  1 
ATOM   2719 N  N   . LYS A 1 336 ? -24.181 -20.580 -8.486  1.00 37.36  ? 336  LYS A N   1 
ATOM   2720 C  CA  . LYS A 1 336 ? -25.624 -20.382 -8.548  1.00 36.95  ? 336  LYS A CA  1 
ATOM   2721 C  C   . LYS A 1 336 ? -26.222 -20.935 -9.838  1.00 41.38  ? 336  LYS A C   1 
ATOM   2722 O  O   . LYS A 1 336 ? -27.394 -21.327 -9.854  1.00 48.20  ? 336  LYS A O   1 
ATOM   2723 C  CB  . LYS A 1 336 ? -25.945 -18.895 -8.414  1.00 38.84  ? 336  LYS A CB  1 
ATOM   2724 C  CG  . LYS A 1 336 ? -25.678 -18.348 -7.001  1.00 38.66  ? 336  LYS A CG  1 
ATOM   2725 C  CD  . LYS A 1 336 ? -25.607 -16.829 -6.994  1.00 42.65  ? 336  LYS A CD  1 
ATOM   2726 C  CE  . LYS A 1 336 ? -26.937 -16.198 -7.365  1.00 41.19  ? 336  LYS A CE  1 
ATOM   2727 N  NZ  . LYS A 1 336 ? -28.047 -16.629 -6.478  1.00 45.41  ? 336  LYS A NZ  1 
ATOM   2728 N  N   . GLU A 1 337 ? -25.434 -20.980 -10.910 1.00 37.96  ? 337  GLU A N   1 
ATOM   2729 C  CA  . GLU A 1 337 ? -25.866 -21.484 -12.209 1.00 42.47  ? 337  GLU A CA  1 
ATOM   2730 C  C   . GLU A 1 337 ? -24.650 -22.056 -12.924 1.00 43.15  ? 337  GLU A C   1 
ATOM   2731 O  O   . GLU A 1 337 ? -23.511 -21.829 -12.521 1.00 39.33  ? 337  GLU A O   1 
ATOM   2732 C  CB  . GLU A 1 337 ? -26.495 -20.376 -13.060 1.00 43.57  ? 337  GLU A CB  1 
ATOM   2733 C  CG  . GLU A 1 337 ? -27.766 -19.768 -12.497 1.00 47.84  ? 337  GLU A CG  1 
ATOM   2734 C  CD  . GLU A 1 337 ? -28.910 -20.762 -12.424 1.00 54.70  ? 337  GLU A CD  1 
ATOM   2735 O  OE1 . GLU A 1 337 ? -28.892 -21.746 -13.192 1.00 58.94  ? 337  GLU A OE1 1 
ATOM   2736 O  OE2 . GLU A 1 337 ? -29.825 -20.567 -11.590 1.00 59.49  ? 337  GLU A OE2 1 
ATOM   2737 N  N   . ASP A 1 338 ? -24.888 -22.770 -14.026 1.00 45.98  ? 338  ASP A N   1 
ATOM   2738 C  CA  . ASP A 1 338 ? -23.767 -23.185 -14.856 1.00 43.12  ? 338  ASP A CA  1 
ATOM   2739 C  C   . ASP A 1 338 ? -22.918 -21.969 -15.197 1.00 45.13  ? 338  ASP A C   1 
ATOM   2740 O  O   . ASP A 1 338 ? -23.437 -20.901 -15.526 1.00 46.33  ? 338  ASP A O   1 
ATOM   2741 C  CB  . ASP A 1 338 ? -24.255 -23.861 -16.147 1.00 47.88  ? 338  ASP A CB  1 
ATOM   2742 C  CG  . ASP A 1 338 ? -25.046 -25.139 -15.894 1.00 48.82  ? 338  ASP A CG  1 
ATOM   2743 O  OD1 . ASP A 1 338 ? -25.063 -25.639 -14.748 1.00 48.15  ? 338  ASP A OD1 1 
ATOM   2744 O  OD2 . ASP A 1 338 ? -25.667 -25.649 -16.859 1.00 48.69  ? 338  ASP A OD2 1 
ATOM   2745 N  N   . THR A 1 339 ? -21.604 -22.125 -15.118 1.00 42.01  ? 339  THR A N   1 
ATOM   2746 C  CA  . THR A 1 339 ? -20.733 -21.003 -15.427 1.00 46.45  ? 339  THR A CA  1 
ATOM   2747 C  C   . THR A 1 339 ? -19.334 -21.537 -15.676 1.00 43.98  ? 339  THR A C   1 
ATOM   2748 O  O   . THR A 1 339 ? -19.015 -22.671 -15.313 1.00 48.25  ? 339  THR A O   1 
ATOM   2749 C  CB  . THR A 1 339 ? -20.749 -19.963 -14.294 1.00 45.51  ? 339  THR A CB  1 
ATOM   2750 O  OG1 . THR A 1 339 ? -20.283 -18.704 -14.791 1.00 46.23  ? 339  THR A OG1 1 
ATOM   2751 C  CG2 . THR A 1 339 ? -19.879 -20.427 -13.122 1.00 42.40  ? 339  THR A CG2 1 
ATOM   2752 N  N   . VAL A 1 340 ? -18.501 -20.706 -16.301 1.00 43.16  ? 340  VAL A N   1 
ATOM   2753 C  CA  . VAL A 1 340 ? -17.133 -21.068 -16.653 1.00 43.72  ? 340  VAL A CA  1 
ATOM   2754 C  C   . VAL A 1 340 ? -16.173 -20.154 -15.907 1.00 43.65  ? 340  VAL A C   1 
ATOM   2755 O  O   . VAL A 1 340 ? -16.263 -18.925 -16.010 1.00 45.74  ? 340  VAL A O   1 
ATOM   2756 C  CB  . VAL A 1 340 ? -16.890 -20.982 -18.173 1.00 45.28  ? 340  VAL A CB  1 
ATOM   2757 C  CG1 . VAL A 1 340 ? -15.412 -21.165 -18.474 1.00 46.79  ? 340  VAL A CG1 1 
ATOM   2758 C  CG2 . VAL A 1 340 ? -17.704 -22.041 -18.893 1.00 41.34  ? 340  VAL A CG2 1 
ATOM   2759 N  N   . LEU A 1 341 ? -15.243 -20.754 -15.177 1.00 45.17  ? 341  LEU A N   1 
ATOM   2760 C  CA  . LEU A 1 341 ? -14.280 -20.008 -14.386 1.00 46.49  ? 341  LEU A CA  1 
ATOM   2761 C  C   . LEU A 1 341 ? -13.024 -19.757 -15.211 1.00 46.39  ? 341  LEU A C   1 
ATOM   2762 O  O   . LEU A 1 341 ? -12.442 -20.696 -15.759 1.00 47.35  ? 341  LEU A O   1 
ATOM   2763 C  CB  . LEU A 1 341 ? -13.935 -20.794 -13.119 1.00 45.67  ? 341  LEU A CB  1 
ATOM   2764 C  CG  . LEU A 1 341 ? -13.594 -20.022 -11.859 1.00 50.43  ? 341  LEU A CG  1 
ATOM   2765 C  CD1 . LEU A 1 341 ? -14.756 -19.106 -11.490 1.00 43.01  ? 341  LEU A CD1 1 
ATOM   2766 C  CD2 . LEU A 1 341 ? -13.293 -21.018 -10.743 1.00 46.85  ? 341  LEU A CD2 1 
ATOM   2767 N  N   . GLY A 1 342 ? -12.604 -18.495 -15.292 1.00 43.54  ? 342  GLY A N   1 
ATOM   2768 C  CA  . GLY A 1 342 ? -11.333 -18.176 -15.922 1.00 46.05  ? 342  GLY A CA  1 
ATOM   2769 C  C   . GLY A 1 342 ? -11.220 -18.582 -17.376 1.00 50.95  ? 342  GLY A C   1 
ATOM   2770 O  O   . GLY A 1 342 ? -10.104 -18.738 -17.888 1.00 51.46  ? 342  GLY A O   1 
ATOM   2771 N  N   . GLY A 1 343 ? -12.346 -18.767 -18.060 1.00 48.88  ? 343  GLY A N   1 
ATOM   2772 C  CA  . GLY A 1 343 ? -12.319 -19.188 -19.451 1.00 50.74  ? 343  GLY A CA  1 
ATOM   2773 C  C   . GLY A 1 343 ? -11.868 -20.611 -19.683 1.00 53.35  ? 343  GLY A C   1 
ATOM   2774 O  O   . GLY A 1 343 ? -11.743 -21.019 -20.839 1.00 49.91  ? 343  GLY A O   1 
ATOM   2775 N  N   . GLU A 1 344 ? -11.634 -21.386 -18.621 1.00 47.08  ? 344  GLU A N   1 
ATOM   2776 C  CA  . GLU A 1 344 ? -11.009 -22.696 -18.760 1.00 51.74  ? 344  GLU A CA  1 
ATOM   2777 C  C   . GLU A 1 344 ? -11.730 -23.792 -17.986 1.00 53.30  ? 344  GLU A C   1 
ATOM   2778 O  O   . GLU A 1 344 ? -11.661 -24.964 -18.366 1.00 53.73  ? 344  GLU A O   1 
ATOM   2779 C  CB  . GLU A 1 344 ? -9.549  -22.639 -18.299 1.00 54.70  ? 344  GLU A CB  1 
ATOM   2780 C  CG  . GLU A 1 344 ? -8.835  -21.331 -18.596 1.00 57.64  ? 344  GLU A CG  1 
ATOM   2781 C  CD  . GLU A 1 344 ? -7.324  -21.468 -18.567 1.00 64.04  ? 344  GLU A CD  1 
ATOM   2782 O  OE1 . GLU A 1 344 ? -6.722  -21.732 -19.629 1.00 69.19  ? 344  GLU A OE1 1 
ATOM   2783 O  OE2 . GLU A 1 344 ? -6.734  -21.310 -17.477 1.00 66.57  ? 344  GLU A OE2 1 
ATOM   2784 N  N   . TYR A 1 345 ? -12.410 -23.450 -16.894 1.00 45.79  ? 345  TYR A N   1 
ATOM   2785 C  CA  . TYR A 1 345 ? -12.928 -24.480 -15.992 1.00 48.27  ? 345  TYR A CA  1 
ATOM   2786 C  C   . TYR A 1 345 ? -14.442 -24.414 -15.885 1.00 47.96  ? 345  TYR A C   1 
ATOM   2787 O  O   . TYR A 1 345 ? -14.982 -23.630 -15.082 1.00 46.91  ? 345  TYR A O   1 
ATOM   2788 C  CB  . TYR A 1 345 ? -12.280 -24.365 -14.614 1.00 43.37  ? 345  TYR A CB  1 
ATOM   2789 C  CG  . TYR A 1 345 ? -10.782 -24.471 -14.682 1.00 42.37  ? 345  TYR A CG  1 
ATOM   2790 C  CD1 . TYR A 1 345 ? -10.159 -25.700 -14.877 1.00 47.68  ? 345  TYR A CD1 1 
ATOM   2791 C  CD2 . TYR A 1 345 ? -9.985  -23.348 -14.560 1.00 46.01  ? 345  TYR A CD2 1 
ATOM   2792 C  CE1 . TYR A 1 345 ? -8.780  -25.800 -14.954 1.00 46.15  ? 345  TYR A CE1 1 
ATOM   2793 C  CE2 . TYR A 1 345 ? -8.602  -23.435 -14.626 1.00 47.69  ? 345  TYR A CE2 1 
ATOM   2794 C  CZ  . TYR A 1 345 ? -8.005  -24.665 -14.824 1.00 50.82  ? 345  TYR A CZ  1 
ATOM   2795 O  OH  . TYR A 1 345 ? -6.628  -24.747 -14.894 1.00 48.78  ? 345  TYR A OH  1 
ATOM   2796 N  N   . PRO A 1 346 ? -15.162 -25.223 -16.660 1.00 44.50  ? 346  PRO A N   1 
ATOM   2797 C  CA  . PRO A 1 346 ? -16.625 -25.204 -16.598 1.00 47.10  ? 346  PRO A CA  1 
ATOM   2798 C  C   . PRO A 1 346 ? -17.142 -25.784 -15.290 1.00 47.71  ? 346  PRO A C   1 
ATOM   2799 O  O   . PRO A 1 346 ? -16.641 -26.796 -14.791 1.00 45.36  ? 346  PRO A O   1 
ATOM   2800 C  CB  . PRO A 1 346 ? -17.038 -26.072 -17.793 1.00 48.81  ? 346  PRO A CB  1 
ATOM   2801 C  CG  . PRO A 1 346 ? -15.881 -26.990 -17.988 1.00 53.03  ? 346  PRO A CG  1 
ATOM   2802 C  CD  . PRO A 1 346 ? -14.668 -26.153 -17.690 1.00 47.93  ? 346  PRO A CD  1 
ATOM   2803 N  N   . LEU A 1 347 ? -18.167 -25.127 -14.748 1.00 43.03  ? 347  LEU A N   1 
ATOM   2804 C  CA  . LEU A 1 347 ? -18.839 -25.554 -13.532 1.00 43.69  ? 347  LEU A CA  1 
ATOM   2805 C  C   . LEU A 1 347 ? -20.331 -25.680 -13.793 1.00 42.22  ? 347  LEU A C   1 
ATOM   2806 O  O   . LEU A 1 347 ? -20.923 -24.883 -14.527 1.00 46.20  ? 347  LEU A O   1 
ATOM   2807 C  CB  . LEU A 1 347 ? -18.606 -24.559 -12.381 1.00 40.72  ? 347  LEU A CB  1 
ATOM   2808 C  CG  . LEU A 1 347 ? -17.147 -24.241 -12.060 1.00 42.65  ? 347  LEU A CG  1 
ATOM   2809 C  CD1 . LEU A 1 347 ? -17.043 -23.108 -11.027 1.00 44.32  ? 347  LEU A CD1 1 
ATOM   2810 C  CD2 . LEU A 1 347 ? -16.427 -25.490 -11.567 1.00 41.67  ? 347  LEU A CD2 1 
ATOM   2811 N  N   . GLU A 1 348 ? -20.937 -26.672 -13.152 1.00 42.59  ? 348  GLU A N   1 
ATOM   2812 C  CA  . GLU A 1 348 ? -22.376 -26.869 -13.148 1.00 43.31  ? 348  GLU A CA  1 
ATOM   2813 C  C   . GLU A 1 348 ? -22.991 -26.229 -11.907 1.00 45.56  ? 348  GLU A C   1 
ATOM   2814 O  O   . GLU A 1 348 ? -22.361 -26.153 -10.848 1.00 42.72  ? 348  GLU A O   1 
ATOM   2815 C  CB  . GLU A 1 348 ? -22.711 -28.359 -13.172 1.00 46.45  ? 348  GLU A CB  1 
ATOM   2816 C  CG  . GLU A 1 348 ? -21.956 -29.115 -14.262 1.00 46.33  ? 348  GLU A CG  1 
ATOM   2817 C  CD  . GLU A 1 348 ? -22.515 -30.503 -14.513 1.00 59.08  ? 348  GLU A CD  1 
ATOM   2818 O  OE1 . GLU A 1 348 ? -22.697 -30.851 -15.697 1.00 65.93  ? 348  GLU A OE1 1 
ATOM   2819 O  OE2 . GLU A 1 348 ? -22.775 -31.242 -13.543 1.00 68.70  ? 348  GLU A OE2 1 
ATOM   2820 N  N   . LYS A 1 349 ? -24.235 -25.780 -12.045 1.00 44.22  ? 349  LYS A N   1 
ATOM   2821 C  CA  . LYS A 1 349 ? -24.996 -25.290 -10.904 1.00 45.79  ? 349  LYS A CA  1 
ATOM   2822 C  C   . LYS A 1 349 ? -24.805 -26.198 -9.696  1.00 46.06  ? 349  LYS A C   1 
ATOM   2823 O  O   . LYS A 1 349 ? -24.920 -27.424 -9.795  1.00 44.76  ? 349  LYS A O   1 
ATOM   2824 C  CB  . LYS A 1 349 ? -26.479 -25.208 -11.274 1.00 46.40  ? 349  LYS A CB  1 
ATOM   2825 C  CG  . LYS A 1 349 ? -27.384 -24.632 -10.191 1.00 51.38  ? 349  LYS A CG  1 
ATOM   2826 C  CD  . LYS A 1 349 ? -28.801 -25.163 -10.346 1.00 53.44  ? 349  LYS A CD  1 
ATOM   2827 C  CE  . LYS A 1 349 ? -29.786 -24.433 -9.450  1.00 56.13  ? 349  LYS A CE  1 
ATOM   2828 N  NZ  . LYS A 1 349 ? -30.052 -23.061 -9.961  1.00 62.47  ? 349  LYS A NZ  1 
ATOM   2829 N  N   . GLY A 1 350 ? -24.489 -25.591 -8.555  1.00 39.50  ? 350  GLY A N   1 
ATOM   2830 C  CA  . GLY A 1 350 ? -24.287 -26.335 -7.335  1.00 40.26  ? 350  GLY A CA  1 
ATOM   2831 C  C   . GLY A 1 350 ? -22.854 -26.732 -7.065  1.00 41.43  ? 350  GLY A C   1 
ATOM   2832 O  O   . GLY A 1 350 ? -22.530 -27.102 -5.922  1.00 41.45  ? 350  GLY A O   1 
ATOM   2833 N  N   . ASP A 1 351 ? -21.986 -26.655 -8.073  1.00 38.85  ? 351  ASP A N   1 
ATOM   2834 C  CA  . ASP A 1 351 ? -20.581 -27.003 -7.879  1.00 38.45  ? 351  ASP A CA  1 
ATOM   2835 C  C   . ASP A 1 351 ? -19.932 -26.103 -6.831  1.00 38.36  ? 351  ASP A C   1 
ATOM   2836 O  O   . ASP A 1 351 ? -20.175 -24.895 -6.793  1.00 37.28  ? 351  ASP A O   1 
ATOM   2837 C  CB  . ASP A 1 351 ? -19.816 -26.884 -9.193  1.00 38.86  ? 351  ASP A CB  1 
ATOM   2838 C  CG  . ASP A 1 351 ? -19.978 -28.111 -10.082 1.00 44.28  ? 351  ASP A CG  1 
ATOM   2839 O  OD1 . ASP A 1 351 ? -20.725 -29.041 -9.693  1.00 41.21  ? 351  ASP A OD1 1 
ATOM   2840 O  OD2 . ASP A 1 351 ? -19.354 -28.128 -11.169 1.00 40.12  ? 351  ASP A OD2 1 
ATOM   2841 N  N   . GLU A 1 352 ? -19.053 -26.700 -6.021  1.00 38.01  ? 352  GLU A N   1 
ATOM   2842 C  CA  . GLU A 1 352 ? -18.446 -26.082 -4.847  1.00 40.52  ? 352  GLU A CA  1 
ATOM   2843 C  C   . GLU A 1 352 ? -17.026 -25.601 -5.130  1.00 41.63  ? 352  GLU A C   1 
ATOM   2844 O  O   . GLU A 1 352 ? -16.275 -26.229 -5.884  1.00 40.75  ? 352  GLU A O   1 
ATOM   2845 C  CB  . GLU A 1 352 ? -18.422 -27.100 -3.702  1.00 37.12  ? 352  GLU A CB  1 
ATOM   2846 C  CG  . GLU A 1 352 ? -19.791 -27.374 -3.161  1.00 45.63  ? 352  GLU A CG  1 
ATOM   2847 C  CD  . GLU A 1 352 ? -19.769 -28.192 -1.879  1.00 48.37  ? 352  GLU A CD  1 
ATOM   2848 O  OE1 . GLU A 1 352 ? -18.754 -28.161 -1.137  1.00 45.96  ? 352  GLU A OE1 1 
ATOM   2849 O  OE2 . GLU A 1 352 ? -20.785 -28.860 -1.631  1.00 55.32  ? 352  GLU A OE2 1 
ATOM   2850 N  N   . LEU A 1 353 ? -16.655 -24.493 -4.482  1.00 37.27  ? 353  LEU A N   1 
ATOM   2851 C  CA  . LEU A 1 353 ? -15.303 -23.958 -4.499  1.00 36.15  ? 353  LEU A CA  1 
ATOM   2852 C  C   . LEU A 1 353 ? -14.819 -23.751 -3.074  1.00 38.89  ? 353  LEU A C   1 
ATOM   2853 O  O   . LEU A 1 353 ? -15.625 -23.476 -2.178  1.00 35.96  ? 353  LEU A O   1 
ATOM   2854 C  CB  . LEU A 1 353 ? -15.228 -22.615 -5.221  1.00 35.06  ? 353  LEU A CB  1 
ATOM   2855 C  CG  . LEU A 1 353 ? -15.714 -22.578 -6.650  1.00 40.12  ? 353  LEU A CG  1 
ATOM   2856 C  CD1 . LEU A 1 353 ? -15.792 -21.125 -7.106  1.00 37.58  ? 353  LEU A CD1 1 
ATOM   2857 C  CD2 . LEU A 1 353 ? -14.760 -23.398 -7.495  1.00 39.85  ? 353  LEU A CD2 1 
ATOM   2858 N  N   . MET A 1 354 ? -13.499 -23.843 -2.862  1.00 37.11  ? 354  MET A N   1 
ATOM   2859 C  CA  . MET A 1 354 ? -12.930 -23.460 -1.579  1.00 38.93  ? 354  MET A CA  1 
ATOM   2860 C  C   . MET A 1 354 ? -11.939 -22.352 -1.889  1.00 36.76  ? 354  MET A C   1 
ATOM   2861 O  O   . MET A 1 354 ? -11.089 -22.514 -2.766  1.00 37.34  ? 354  MET A O   1 
ATOM   2862 C  CB  . MET A 1 354 ? -12.201 -24.631 -0.896  1.00 33.68  ? 354  MET A CB  1 
ATOM   2863 C  CG  . MET A 1 354 ? -13.232 -25.608 -0.433  1.00 35.92  ? 354  MET A CG  1 
ATOM   2864 S  SD  . MET A 1 354 ? -14.235 -25.206 1.015   1.00 38.59  ? 354  MET A SD  1 
ATOM   2865 C  CE  . MET A 1 354 ? -13.043 -24.846 2.292   1.00 39.55  ? 354  MET A CE  1 
ATOM   2866 N  N   . VAL A 1 355 ? -12.055 -21.220 -1.209  1.00 34.29  ? 355  VAL A N   1 
ATOM   2867 C  CA  . VAL A 1 355 ? -11.114 -20.121 -1.388  1.00 32.94  ? 355  VAL A CA  1 
ATOM   2868 C  C   . VAL A 1 355 ? -10.005 -20.259 -0.342  1.00 33.43  ? 355  VAL A C   1 
ATOM   2869 O  O   . VAL A 1 355 ? -10.249 -20.102 0.854   1.00 33.38  ? 355  VAL A O   1 
ATOM   2870 C  CB  . VAL A 1 355 ? -11.816 -18.763 -1.273  1.00 33.81  ? 355  VAL A CB  1 
ATOM   2871 C  CG1 . VAL A 1 355 ? -10.794 -17.630 -1.348  1.00 34.45  ? 355  VAL A CG1 1 
ATOM   2872 C  CG2 . VAL A 1 355 ? -12.866 -18.619 -2.378  1.00 29.17  ? 355  VAL A CG2 1 
ATOM   2873 N  N   . LEU A 1 356 ? -8.769  -20.528 -0.785  1.00 31.10  ? 356  LEU A N   1 
ATOM   2874 C  CA  . LEU A 1 356 ? -7.672  -20.807 0.159   1.00 31.19  ? 356  LEU A CA  1 
ATOM   2875 C  C   . LEU A 1 356 ? -6.934  -19.502 0.438   1.00 34.48  ? 356  LEU A C   1 
ATOM   2876 O  O   . LEU A 1 356 ? -5.997  -19.135 -0.269  1.00 34.19  ? 356  LEU A O   1 
ATOM   2877 C  CB  . LEU A 1 356 ? -6.741  -21.878 -0.399  1.00 32.24  ? 356  LEU A CB  1 
ATOM   2878 C  CG  . LEU A 1 356 ? -5.631  -22.375 0.548   1.00 37.50  ? 356  LEU A CG  1 
ATOM   2879 C  CD1 . LEU A 1 356 ? -6.218  -23.010 1.791   1.00 37.67  ? 356  LEU A CD1 1 
ATOM   2880 C  CD2 . LEU A 1 356 ? -4.701  -23.371 -0.160  1.00 40.50  ? 356  LEU A CD2 1 
ATOM   2881 N  N   . ILE A 1 357 ? -7.367  -18.777 1.482   1.00 32.44  ? 357  ILE A N   1 
ATOM   2882 C  CA  . ILE A 1 357 ? -6.989  -17.366 1.608   1.00 31.60  ? 357  ILE A CA  1 
ATOM   2883 C  C   . ILE A 1 357 ? -5.488  -17.171 1.786   1.00 33.90  ? 357  ILE A C   1 
ATOM   2884 O  O   . ILE A 1 357 ? -4.928  -16.257 1.157   1.00 33.91  ? 357  ILE A O   1 
ATOM   2885 C  CB  . ILE A 1 357 ? -7.787  -16.689 2.732   1.00 33.95  ? 357  ILE A CB  1 
ATOM   2886 C  CG1 . ILE A 1 357 ? -9.293  -16.896 2.562   1.00 30.74  ? 357  ILE A CG1 1 
ATOM   2887 C  CG2 . ILE A 1 357 ? -7.519  -15.197 2.691   1.00 31.74  ? 357  ILE A CG2 1 
ATOM   2888 C  CD1 . ILE A 1 357 ? -10.111 -16.376 3.793   1.00 31.73  ? 357  ILE A CD1 1 
ATOM   2889 N  N   . PRO A 1 358 ? -4.792  -17.928 2.640   1.00 33.32  ? 358  PRO A N   1 
ATOM   2890 C  CA  . PRO A 1 358 ? -3.356  -17.657 2.798   1.00 34.38  ? 358  PRO A CA  1 
ATOM   2891 C  C   . PRO A 1 358 ? -2.595  -17.823 1.491   1.00 33.55  ? 358  PRO A C   1 
ATOM   2892 O  O   . PRO A 1 358 ? -1.593  -17.131 1.273   1.00 36.09  ? 358  PRO A O   1 
ATOM   2893 C  CB  . PRO A 1 358 ? -2.911  -18.666 3.869   1.00 36.24  ? 358  PRO A CB  1 
ATOM   2894 C  CG  . PRO A 1 358 ? -4.225  -19.046 4.611   1.00 33.44  ? 358  PRO A CG  1 
ATOM   2895 C  CD  . PRO A 1 358 ? -5.263  -19.021 3.517   1.00 32.20  ? 358  PRO A CD  1 
ATOM   2896 N  N   . GLN A 1 359 ? -3.073  -18.688 0.599   1.00 33.36  ? 359  GLN A N   1 
ATOM   2897 C  CA  . GLN A 1 359 ? -2.400  -18.880 -0.682  1.00 36.76  ? 359  GLN A CA  1 
ATOM   2898 C  C   . GLN A 1 359 ? -2.744  -17.755 -1.662  1.00 35.89  ? 359  GLN A C   1 
ATOM   2899 O  O   . GLN A 1 359 ? -1.858  -17.241 -2.353  1.00 36.11  ? 359  GLN A O   1 
ATOM   2900 C  CB  . GLN A 1 359 ? -2.777  -20.250 -1.241  1.00 37.75  ? 359  GLN A CB  1 
ATOM   2901 C  CG  . GLN A 1 359 ? -1.802  -20.800 -2.250  1.00 41.60  ? 359  GLN A CG  1 
ATOM   2902 C  CD  . GLN A 1 359 ? -0.445  -21.140 -1.660  1.00 42.46  ? 359  GLN A CD  1 
ATOM   2903 O  OE1 . GLN A 1 359 ? -0.239  -21.146 -0.430  1.00 39.73  ? 359  GLN A OE1 1 
ATOM   2904 N  NE2 . GLN A 1 359 ? 0.506   -21.428 -2.551  1.00 43.84  ? 359  GLN A NE2 1 
ATOM   2905 N  N   . LEU A 1 360 ? -4.019  -17.350 -1.726  1.00 35.39  ? 360  LEU A N   1 
ATOM   2906 C  CA  . LEU A 1 360 ? -4.386  -16.132 -2.448  1.00 34.76  ? 360  LEU A CA  1 
ATOM   2907 C  C   . LEU A 1 360 ? -3.473  -14.970 -2.073  1.00 34.20  ? 360  LEU A C   1 
ATOM   2908 O  O   . LEU A 1 360 ? -2.977  -14.241 -2.941  1.00 36.31  ? 360  LEU A O   1 
ATOM   2909 C  CB  . LEU A 1 360 ? -5.853  -15.766 -2.161  1.00 31.92  ? 360  LEU A CB  1 
ATOM   2910 C  CG  . LEU A 1 360 ? -6.259  -14.339 -2.580  1.00 34.37  ? 360  LEU A CG  1 
ATOM   2911 C  CD1 . LEU A 1 360 ? -6.345  -14.209 -4.099  1.00 32.21  ? 360  LEU A CD1 1 
ATOM   2912 C  CD2 . LEU A 1 360 ? -7.585  -13.918 -1.936  1.00 35.86  ? 360  LEU A CD2 1 
ATOM   2913 N  N   . HIS A 1 361 ? -3.248  -14.771 -0.778  1.00 32.56  ? 361  HIS A N   1 
ATOM   2914 C  CA  . HIS A 1 361 ? -2.460  -13.643 -0.304  1.00 32.10  ? 361  HIS A CA  1 
ATOM   2915 C  C   . HIS A 1 361 ? -0.966  -13.796 -0.590  1.00 32.07  ? 361  HIS A C   1 
ATOM   2916 O  O   . HIS A 1 361 ? -0.184  -12.931 -0.190  1.00 34.63  ? 361  HIS A O   1 
ATOM   2917 C  CB  . HIS A 1 361 ? -2.690  -13.455 1.197   1.00 34.19  ? 361  HIS A CB  1 
ATOM   2918 C  CG  . HIS A 1 361 ? -4.075  -12.983 1.546   1.00 30.90  ? 361  HIS A CG  1 
ATOM   2919 N  ND1 . HIS A 1 361 ? -4.522  -12.891 2.849   1.00 32.60  ? 361  HIS A ND1 1 
ATOM   2920 C  CD2 . HIS A 1 361 ? -5.096  -12.552 0.767   1.00 33.17  ? 361  HIS A CD2 1 
ATOM   2921 C  CE1 . HIS A 1 361 ? -5.766  -12.431 2.856   1.00 33.23  ? 361  HIS A CE1 1 
ATOM   2922 N  NE2 . HIS A 1 361 ? -6.136  -12.215 1.605   1.00 31.72  ? 361  HIS A NE2 1 
ATOM   2923 N  N   . ARG A 1 362 ? -0.560  -14.895 -1.217  1.00 37.55  ? 362  ARG A N   1 
ATOM   2924 C  CA  . ARG A 1 362 ? 0.825   -15.102 -1.625  1.00 37.70  ? 362  ARG A CA  1 
ATOM   2925 C  C   . ARG A 1 362 ? 0.954   -15.119 -3.147  1.00 40.16  ? 362  ARG A C   1 
ATOM   2926 O  O   . ARG A 1 362 ? 1.967   -15.579 -3.684  1.00 40.72  ? 362  ARG A O   1 
ATOM   2927 C  CB  . ARG A 1 362 ? 1.369   -16.394 -1.018  1.00 34.47  ? 362  ARG A CB  1 
ATOM   2928 C  CG  . ARG A 1 362 ? 1.738   -16.275 0.471   1.00 38.57  ? 362  ARG A CG  1 
ATOM   2929 C  CD  . ARG A 1 362 ? 1.863   -17.640 1.146   1.00 39.07  ? 362  ARG A CD  1 
ATOM   2930 N  NE  . ARG A 1 362 ? 2.365   -17.498 2.511   1.00 39.33  ? 362  ARG A NE  1 
ATOM   2931 C  CZ  . ARG A 1 362 ? 1.630   -17.070 3.530   1.00 39.93  ? 362  ARG A CZ  1 
ATOM   2932 N  NH1 . ARG A 1 362 ? 0.345   -16.778 3.381   1.00 33.99  ? 362  ARG A NH1 1 
ATOM   2933 N  NH2 . ARG A 1 362 ? 2.198   -16.915 4.722   1.00 39.12  ? 362  ARG A NH2 1 
ATOM   2934 N  N   . ASP A 1 363 ? -0.059  -14.621 -3.853  1.00 36.11  ? 363  ASP A N   1 
ATOM   2935 C  CA  . ASP A 1 363 ? -0.032  -14.558 -5.311  1.00 37.56  ? 363  ASP A CA  1 
ATOM   2936 C  C   . ASP A 1 363 ? 1.037   -13.556 -5.746  1.00 36.03  ? 363  ASP A C   1 
ATOM   2937 O  O   . ASP A 1 363 ? 0.871   -12.341 -5.585  1.00 36.59  ? 363  ASP A O   1 
ATOM   2938 C  CB  . ASP A 1 363 ? -1.423  -14.167 -5.816  1.00 38.20  ? 363  ASP A CB  1 
ATOM   2939 C  CG  . ASP A 1 363 ? -1.575  -14.291 -7.324  1.00 41.61  ? 363  ASP A CG  1 
ATOM   2940 O  OD1 . ASP A 1 363 ? -0.549  -14.181 -8.035  1.00 38.07  ? 363  ASP A OD1 1 
ATOM   2941 O  OD2 . ASP A 1 363 ? -2.726  -14.490 -7.791  1.00 38.27  ? 363  ASP A OD2 1 
ATOM   2942 N  N   . LYS A 1 364 ? 2.155   -14.049 -6.285  1.00 40.81  ? 364  LYS A N   1 
ATOM   2943 C  CA  . LYS A 1 364 ? 3.229   -13.127 -6.656  1.00 41.57  ? 364  LYS A CA  1 
ATOM   2944 C  C   . LYS A 1 364 ? 2.815   -12.185 -7.777  1.00 40.71  ? 364  LYS A C   1 
ATOM   2945 O  O   . LYS A 1 364 ? 3.375   -11.086 -7.894  1.00 40.87  ? 364  LYS A O   1 
ATOM   2946 C  CB  . LYS A 1 364 ? 4.476   -13.905 -7.064  1.00 42.74  ? 364  LYS A CB  1 
ATOM   2947 C  CG  . LYS A 1 364 ? 4.978   -14.817 -5.963  1.00 50.07  ? 364  LYS A CG  1 
ATOM   2948 C  CD  . LYS A 1 364 ? 5.461   -16.105 -6.575  1.00 54.19  ? 364  LYS A CD  1 
ATOM   2949 C  CE  . LYS A 1 364 ? 4.340   -16.674 -7.474  1.00 58.65  ? 364  LYS A CE  1 
ATOM   2950 N  NZ  . LYS A 1 364 ? 2.955   -16.682 -6.844  1.00 44.31  ? 364  LYS A NZ  1 
ATOM   2951 N  N   . THR A 1 365 ? 1.857   -12.586 -8.614  1.00 37.28  ? 365  THR A N   1 
ATOM   2952 C  CA  . THR A 1 365 ? 1.454   -11.671 -9.676  1.00 40.53  ? 365  THR A CA  1 
ATOM   2953 C  C   . THR A 1 365 ? 0.792   -10.423 -9.111  1.00 43.97  ? 365  THR A C   1 
ATOM   2954 O  O   . THR A 1 365 ? 0.740   -9.399  -9.796  1.00 39.33  ? 365  THR A O   1 
ATOM   2955 C  CB  . THR A 1 365 ? 0.528   -12.358 -10.685 1.00 40.22  ? 365  THR A CB  1 
ATOM   2956 O  OG1 . THR A 1 365 ? -0.768  -12.571 -10.111 1.00 40.92  ? 365  THR A OG1 1 
ATOM   2957 C  CG2 . THR A 1 365 ? 1.106   -13.699 -11.123 1.00 40.14  ? 365  THR A CG2 1 
ATOM   2958 N  N   . ILE A 1 366 ? 0.323   -10.477 -7.868  1.00 38.58  ? 366  ILE A N   1 
ATOM   2959 C  CA  . ILE A 1 366 ? -0.314  -9.339  -7.209  1.00 37.09  ? 366  ILE A CA  1 
ATOM   2960 C  C   . ILE A 1 366 ? 0.680   -8.562  -6.357  1.00 41.27  ? 366  ILE A C   1 
ATOM   2961 O  O   . ILE A 1 366 ? 0.822   -7.347  -6.496  1.00 40.99  ? 366  ILE A O   1 
ATOM   2962 C  CB  . ILE A 1 366 ? -1.497  -9.831  -6.344  1.00 35.58  ? 366  ILE A CB  1 
ATOM   2963 C  CG1 . ILE A 1 366 ? -2.572  -10.501 -7.202  1.00 36.04  ? 366  ILE A CG1 1 
ATOM   2964 C  CG2 . ILE A 1 366 ? -2.045  -8.693  -5.526  1.00 37.08  ? 366  ILE A CG2 1 
ATOM   2965 C  CD1 . ILE A 1 366 ? -3.254  -9.585  -8.189  1.00 37.78  ? 366  ILE A CD1 1 
ATOM   2966 N  N   . TRP A 1 367 ? 1.400   -9.261  -5.479  1.00 38.66  ? 367  TRP A N   1 
ATOM   2967 C  CA  . TRP A 1 367 ? 2.171   -8.615  -4.430  1.00 38.75  ? 367  TRP A CA  1 
ATOM   2968 C  C   . TRP A 1 367 ? 3.645   -8.466  -4.769  1.00 43.03  ? 367  TRP A C   1 
ATOM   2969 O  O   . TRP A 1 367 ? 4.360   -7.747  -4.061  1.00 50.95  ? 367  TRP A O   1 
ATOM   2970 C  CB  . TRP A 1 367 ? 2.004   -9.397  -3.119  1.00 40.90  ? 367  TRP A CB  1 
ATOM   2971 C  CG  . TRP A 1 367 ? 0.545   -9.572  -2.746  1.00 36.62  ? 367  TRP A CG  1 
ATOM   2972 C  CD1 . TRP A 1 367 ? -0.219  -10.676 -2.946  1.00 36.23  ? 367  TRP A CD1 1 
ATOM   2973 C  CD2 . TRP A 1 367 ? -0.309  -8.596  -2.138  1.00 38.10  ? 367  TRP A CD2 1 
ATOM   2974 N  NE1 . TRP A 1 367 ? -1.498  -10.456 -2.498  1.00 37.38  ? 367  TRP A NE1 1 
ATOM   2975 C  CE2 . TRP A 1 367 ? -1.579  -9.186  -1.997  1.00 34.35  ? 367  TRP A CE2 1 
ATOM   2976 C  CE3 . TRP A 1 367 ? -0.120  -7.281  -1.695  1.00 38.17  ? 367  TRP A CE3 1 
ATOM   2977 C  CZ2 . TRP A 1 367 ? -2.659  -8.513  -1.410  1.00 33.06  ? 367  TRP A CZ2 1 
ATOM   2978 C  CZ3 . TRP A 1 367 ? -1.189  -6.609  -1.130  1.00 37.87  ? 367  TRP A CZ3 1 
ATOM   2979 C  CH2 . TRP A 1 367 ? -2.442  -7.226  -0.993  1.00 35.11  ? 367  TRP A CH2 1 
ATOM   2980 N  N   . GLY A 1 368 ? 4.110   -9.110  -5.819  1.00 41.16  ? 368  GLY A N   1 
ATOM   2981 C  CA  . GLY A 1 368 ? 5.499   -8.994  -6.196  1.00 46.67  ? 368  GLY A CA  1 
ATOM   2982 C  C   . GLY A 1 368 ? 6.335   -10.118 -5.631  1.00 55.55  ? 368  GLY A C   1 
ATOM   2983 O  O   . GLY A 1 368 ? 5.851   -11.050 -4.976  1.00 49.32  ? 368  GLY A O   1 
ATOM   2984 N  N   . ASP A 1 369 ? 7.640   -10.010 -5.897  1.00 52.45  ? 369  ASP A N   1 
ATOM   2985 C  CA  . ASP A 1 369 ? 8.566   -11.069 -5.510  1.00 57.68  ? 369  ASP A CA  1 
ATOM   2986 C  C   . ASP A 1 369 ? 8.701   -11.166 -3.992  1.00 53.72  ? 369  ASP A C   1 
ATOM   2987 O  O   . ASP A 1 369 ? 8.844   -12.266 -3.451  1.00 58.62  ? 369  ASP A O   1 
ATOM   2988 C  CB  . ASP A 1 369 ? 9.928   -10.821 -6.166  1.00 60.00  ? 369  ASP A CB  1 
ATOM   2989 C  CG  . ASP A 1 369 ? 9.948   -11.182 -7.658  1.00 66.32  ? 369  ASP A CG  1 
ATOM   2990 O  OD1 . ASP A 1 369 ? 9.035   -11.899 -8.136  1.00 62.46  ? 369  ASP A OD1 1 
ATOM   2991 O  OD2 . ASP A 1 369 ? 10.879  -10.723 -8.357  1.00 68.70  ? 369  ASP A OD2 1 
ATOM   2992 N  N   . ASP A 1 370 ? 8.641   -10.031 -3.295  1.00 50.64  ? 370  ASP A N   1 
ATOM   2993 C  CA  . ASP A 1 370 ? 8.869   -9.954  -1.856  1.00 54.01  ? 370  ASP A CA  1 
ATOM   2994 C  C   . ASP A 1 370 ? 7.659   -10.413 -1.037  1.00 50.70  ? 370  ASP A C   1 
ATOM   2995 O  O   . ASP A 1 370 ? 7.438   -9.912  0.071   1.00 48.13  ? 370  ASP A O   1 
ATOM   2996 C  CB  . ASP A 1 370 ? 9.228   -8.511  -1.480  1.00 46.28  ? 370  ASP A CB  1 
ATOM   2997 C  CG  . ASP A 1 370 ? 8.041   -7.574  -1.599  1.00 55.83  ? 370  ASP A CG  1 
ATOM   2998 O  OD1 . ASP A 1 370 ? 7.049   -7.982  -2.239  1.00 55.79  ? 370  ASP A OD1 1 
ATOM   2999 O  OD2 . ASP A 1 370 ? 8.094   -6.434  -1.079  1.00 55.65  ? 370  ASP A OD2 1 
ATOM   3000 N  N   . VAL A 1 371 ? 6.901   -11.386 -1.550  1.00 49.21  ? 371  VAL A N   1 
ATOM   3001 C  CA  . VAL A 1 371 ? 5.570   -11.671 -1.007  1.00 49.43  ? 371  VAL A CA  1 
ATOM   3002 C  C   . VAL A 1 371 ? 5.622   -12.175 0.435   1.00 48.41  ? 371  VAL A C   1 
ATOM   3003 O  O   . VAL A 1 371 ? 4.677   -11.949 1.213   1.00 45.01  ? 371  VAL A O   1 
ATOM   3004 C  CB  . VAL A 1 371 ? 4.827   -12.669 -1.915  1.00 45.92  ? 371  VAL A CB  1 
ATOM   3005 C  CG1 . VAL A 1 371 ? 5.502   -14.027 -1.888  1.00 50.16  ? 371  VAL A CG1 1 
ATOM   3006 C  CG2 . VAL A 1 371 ? 3.395   -12.789 -1.464  1.00 43.92  ? 371  VAL A CG2 1 
ATOM   3007 N  N   . GLU A 1 372 ? 6.691   -12.878 0.820   1.00 44.09  ? 372  GLU A N   1 
ATOM   3008 C  CA  . GLU A 1 372 ? 6.775   -13.418 2.169   1.00 49.00  ? 372  GLU A CA  1 
ATOM   3009 C  C   . GLU A 1 372 ? 7.248   -12.383 3.178   1.00 46.71  ? 372  GLU A C   1 
ATOM   3010 O  O   . GLU A 1 372 ? 7.212   -12.656 4.382   1.00 47.26  ? 372  GLU A O   1 
ATOM   3011 C  CB  . GLU A 1 372 ? 7.699   -14.642 2.202   1.00 47.35  ? 372  GLU A CB  1 
ATOM   3012 C  CG  . GLU A 1 372 ? 7.136   -15.883 1.514   1.00 47.58  ? 372  GLU A CG  1 
ATOM   3013 C  CD  . GLU A 1 372 ? 6.103   -16.631 2.363   1.00 50.04  ? 372  GLU A CD  1 
ATOM   3014 O  OE1 . GLU A 1 372 ? 6.197   -16.598 3.615   1.00 53.72  ? 372  GLU A OE1 1 
ATOM   3015 O  OE2 . GLU A 1 372 ? 5.203   -17.271 1.779   1.00 51.01  ? 372  GLU A OE2 1 
ATOM   3016 N  N   . GLU A 1 373 ? 7.666   -11.209 2.716   1.00 41.12  ? 373  GLU A N   1 
ATOM   3017 C  CA  . GLU A 1 373 ? 8.147   -10.140 3.574   1.00 43.95  ? 373  GLU A CA  1 
ATOM   3018 C  C   . GLU A 1 373 ? 6.980   -9.430  4.251   1.00 47.92  ? 373  GLU A C   1 
ATOM   3019 O  O   . GLU A 1 373 ? 5.894   -9.285  3.680   1.00 41.38  ? 373  GLU A O   1 
ATOM   3020 C  CB  . GLU A 1 373 ? 8.942   -9.132  2.749   1.00 48.01  ? 373  GLU A CB  1 
ATOM   3021 C  CG  . GLU A 1 373 ? 10.409  -9.450  2.622   1.00 55.60  ? 373  GLU A CG  1 
ATOM   3022 C  CD  . GLU A 1 373 ? 11.163  -8.323  1.950   1.00 62.55  ? 373  GLU A CD  1 
ATOM   3023 O  OE1 . GLU A 1 373 ? 11.004  -7.155  2.368   1.00 68.49  ? 373  GLU A OE1 1 
ATOM   3024 O  OE2 . GLU A 1 373 ? 11.886  -8.607  0.973   1.00 70.02  ? 373  GLU A OE2 1 
ATOM   3025 N  N   . PHE A 1 374 ? 7.224   -8.964  5.469   1.00 45.01  ? 374  PHE A N   1 
ATOM   3026 C  CA  . PHE A 1 374 ? 6.230   -8.213  6.227   1.00 42.40  ? 374  PHE A CA  1 
ATOM   3027 C  C   . PHE A 1 374 ? 6.459   -6.736  5.946   1.00 41.53  ? 374  PHE A C   1 
ATOM   3028 O  O   . PHE A 1 374 ? 7.371   -6.115  6.505   1.00 40.14  ? 374  PHE A O   1 
ATOM   3029 C  CB  . PHE A 1 374 ? 6.336   -8.516  7.718   1.00 37.89  ? 374  PHE A CB  1 
ATOM   3030 C  CG  . PHE A 1 374 ? 5.186   -7.996  8.525   1.00 35.93  ? 374  PHE A CG  1 
ATOM   3031 C  CD1 . PHE A 1 374 ? 3.988   -8.693  8.571   1.00 41.34  ? 374  PHE A CD1 1 
ATOM   3032 C  CD2 . PHE A 1 374 ? 5.293   -6.810  9.232   1.00 37.69  ? 374  PHE A CD2 1 
ATOM   3033 C  CE1 . PHE A 1 374 ? 2.907   -8.213  9.322   1.00 32.96  ? 374  PHE A CE1 1 
ATOM   3034 C  CE2 . PHE A 1 374 ? 4.227   -6.331  9.983   1.00 43.93  ? 374  PHE A CE2 1 
ATOM   3035 C  CZ  . PHE A 1 374 ? 3.026   -7.038  10.019  1.00 37.36  ? 374  PHE A CZ  1 
ATOM   3036 N  N   . ARG A 1 375 ? 5.623   -6.157  5.084   1.00 39.01  ? 375  ARG A N   1 
ATOM   3037 C  CA  . ARG A 1 375 ? 5.769   -4.757  4.692   1.00 37.69  ? 375  ARG A CA  1 
ATOM   3038 C  C   . ARG A 1 375 ? 4.408   -4.086  4.732   1.00 41.89  ? 375  ARG A C   1 
ATOM   3039 O  O   . ARG A 1 375 ? 3.673   -4.085  3.737   1.00 40.05  ? 375  ARG A O   1 
ATOM   3040 C  CB  . ARG A 1 375 ? 6.395   -4.628  3.300   1.00 41.85  ? 375  ARG A CB  1 
ATOM   3041 C  CG  . ARG A 1 375 ? 6.654   -3.189  2.899   1.00 47.30  ? 375  ARG A CG  1 
ATOM   3042 C  CD  . ARG A 1 375 ? 7.687   -3.086  1.778   1.00 55.07  ? 375  ARG A CD  1 
ATOM   3043 N  NE  . ARG A 1 375 ? 7.277   -3.849  0.604   1.00 51.25  ? 375  ARG A NE  1 
ATOM   3044 C  CZ  . ARG A 1 375 ? 6.437   -3.401  -0.319  1.00 54.90  ? 375  ARG A CZ  1 
ATOM   3045 N  NH1 . ARG A 1 375 ? 5.883   -2.202  -0.224  1.00 56.70  ? 375  ARG A NH1 1 
ATOM   3046 N  NH2 . ARG A 1 375 ? 6.135   -4.180  -1.355  1.00 56.01  ? 375  ARG A NH2 1 
ATOM   3047 N  N   . PRO A 1 376 ? 4.032   -3.509  5.875   1.00 41.08  ? 376  PRO A N   1 
ATOM   3048 C  CA  . PRO A 1 376 ? 2.702   -2.884  5.981   1.00 40.29  ? 376  PRO A CA  1 
ATOM   3049 C  C   . PRO A 1 376 ? 2.440   -1.833  4.917   1.00 41.10  ? 376  PRO A C   1 
ATOM   3050 O  O   . PRO A 1 376 ? 1.274   -1.580  4.589   1.00 39.35  ? 376  PRO A O   1 
ATOM   3051 C  CB  . PRO A 1 376 ? 2.722   -2.268  7.384   1.00 40.46  ? 376  PRO A CB  1 
ATOM   3052 C  CG  . PRO A 1 376 ? 3.685   -3.143  8.157   1.00 39.22  ? 376  PRO A CG  1 
ATOM   3053 C  CD  . PRO A 1 376 ? 4.755   -3.511  7.163   1.00 39.60  ? 376  PRO A CD  1 
ATOM   3054 N  N   . GLU A 1 377 ? 3.492   -1.219  4.368   1.00 39.34  ? 377  GLU A N   1 
ATOM   3055 C  CA  . GLU A 1 377 ? 3.332   -0.180  3.358   1.00 43.62  ? 377  GLU A CA  1 
ATOM   3056 C  C   . GLU A 1 377 ? 2.638   -0.680  2.093   1.00 40.03  ? 377  GLU A C   1 
ATOM   3057 O  O   . GLU A 1 377 ? 2.195   0.147   1.290   1.00 39.21  ? 377  GLU A O   1 
ATOM   3058 C  CB  . GLU A 1 377 ? 4.711   0.406   3.030   1.00 47.59  ? 377  GLU A CB  1 
ATOM   3059 C  CG  . GLU A 1 377 ? 5.329   1.199   4.193   1.00 48.42  ? 377  GLU A CG  1 
ATOM   3060 C  CD  . GLU A 1 377 ? 5.969   0.309   5.281   1.00 44.42  ? 377  GLU A CD  1 
ATOM   3061 O  OE1 . GLU A 1 377 ? 6.159   -0.909  5.055   1.00 43.76  ? 377  GLU A OE1 1 
ATOM   3062 O  OE2 . GLU A 1 377 ? 6.302   0.850   6.355   1.00 46.47  ? 377  GLU A OE2 1 
ATOM   3063 N  N   . ARG A 1 378 ? 2.532   -1.998  1.893   1.00 37.52  ? 378  ARG A N   1 
ATOM   3064 C  CA  . ARG A 1 378 ? 1.740   -2.507  0.775   1.00 41.42  ? 378  ARG A CA  1 
ATOM   3065 C  C   . ARG A 1 378 ? 0.326   -1.981  0.780   1.00 39.62  ? 378  ARG A C   1 
ATOM   3066 O  O   . ARG A 1 378 ? -0.334  -2.020  -0.267  1.00 38.94  ? 378  ARG A O   1 
ATOM   3067 C  CB  . ARG A 1 378 ? 1.608   -4.029  0.797   1.00 45.02  ? 378  ARG A CB  1 
ATOM   3068 C  CG  . ARG A 1 378 ? 2.858   -4.783  0.748   1.00 47.30  ? 378  ARG A CG  1 
ATOM   3069 C  CD  . ARG A 1 378 ? 2.548   -6.234  0.945   1.00 41.12  ? 378  ARG A CD  1 
ATOM   3070 N  NE  . ARG A 1 378 ? 3.752   -6.942  1.345   1.00 40.29  ? 378  ARG A NE  1 
ATOM   3071 C  CZ  . ARG A 1 378 ? 4.659   -7.419  0.509   1.00 47.14  ? 378  ARG A CZ  1 
ATOM   3072 N  NH1 . ARG A 1 378 ? 4.551   -7.252  -0.803  1.00 47.68  ? 378  ARG A NH1 1 
ATOM   3073 N  NH2 . ARG A 1 378 ? 5.689   -8.100  0.998   1.00 46.90  ? 378  ARG A NH2 1 
ATOM   3074 N  N   . PHE A 1 379 ? -0.174  -1.543  1.938   1.00 35.88  ? 379  PHE A N   1 
ATOM   3075 C  CA  . PHE A 1 379 ? -1.569  -1.148  2.095   1.00 37.62  ? 379  PHE A CA  1 
ATOM   3076 C  C   . PHE A 1 379 ? -1.748  0.363   2.096   1.00 38.74  ? 379  PHE A C   1 
ATOM   3077 O  O   . PHE A 1 379 ? -2.816  0.865   2.457   1.00 40.00  ? 379  PHE A O   1 
ATOM   3078 C  CB  . PHE A 1 379 ? -2.152  -1.796  3.362   1.00 35.80  ? 379  PHE A CB  1 
ATOM   3079 C  CG  . PHE A 1 379 ? -2.335  -3.282  3.213   1.00 35.92  ? 379  PHE A CG  1 
ATOM   3080 C  CD1 . PHE A 1 379 ? -3.484  -3.791  2.603   1.00 36.26  ? 379  PHE A CD1 1 
ATOM   3081 C  CD2 . PHE A 1 379 ? -1.348  -4.164  3.605   1.00 35.55  ? 379  PHE A CD2 1 
ATOM   3082 C  CE1 . PHE A 1 379 ? -3.651  -5.162  2.421   1.00 35.93  ? 379  PHE A CE1 1 
ATOM   3083 C  CE2 . PHE A 1 379 ? -1.501  -5.538  3.429   1.00 35.94  ? 379  PHE A CE2 1 
ATOM   3084 C  CZ  . PHE A 1 379 ? -2.652  -6.042  2.837   1.00 37.48  ? 379  PHE A CZ  1 
ATOM   3085 N  N   . GLU A 1 380 ? -0.742  1.098   1.628   1.00 36.84  ? 380  GLU A N   1 
ATOM   3086 C  CA  . GLU A 1 380 ? -0.822  2.544   1.697   1.00 38.38  ? 380  GLU A CA  1 
ATOM   3087 C  C   . GLU A 1 380 ? -1.911  3.074   0.772   1.00 38.95  ? 380  GLU A C   1 
ATOM   3088 O  O   . GLU A 1 380 ? -2.557  4.075   1.087   1.00 39.52  ? 380  GLU A O   1 
ATOM   3089 C  CB  . GLU A 1 380 ? 0.543   3.121   1.338   1.00 41.94  ? 380  GLU A CB  1 
ATOM   3090 C  CG  . GLU A 1 380 ? 1.030   4.142   2.348   1.00 54.79  ? 380  GLU A CG  1 
ATOM   3091 C  CD  . GLU A 1 380 ? 2.531   4.270   2.287   1.00 60.11  ? 380  GLU A CD  1 
ATOM   3092 O  OE1 . GLU A 1 380 ? 3.058   4.384   1.158   1.00 58.24  ? 380  GLU A OE1 1 
ATOM   3093 O  OE2 . GLU A 1 380 ? 3.185   4.163   3.348   1.00 58.68  ? 380  GLU A OE2 1 
ATOM   3094 N  N   . ASN A 1 381 ? -2.152  2.402   -0.352  1.00 38.68  ? 381  ASN A N   1 
ATOM   3095 C  CA  . ASN A 1 381 ? -3.144  2.845   -1.328  1.00 37.02  ? 381  ASN A CA  1 
ATOM   3096 C  C   . ASN A 1 381 ? -4.015  1.679   -1.777  1.00 39.48  ? 381  ASN A C   1 
ATOM   3097 O  O   . ASN A 1 381 ? -3.617  0.909   -2.666  1.00 36.05  ? 381  ASN A O   1 
ATOM   3098 C  CB  . ASN A 1 381 ? -2.468  3.496   -2.531  1.00 40.78  ? 381  ASN A CB  1 
ATOM   3099 C  CG  . ASN A 1 381 ? -3.467  4.048   -3.524  1.00 42.73  ? 381  ASN A CG  1 
ATOM   3100 O  OD1 . ASN A 1 381 ? -4.681  4.062   -3.270  1.00 39.55  ? 381  ASN A OD1 1 
ATOM   3101 N  ND2 . ASN A 1 381 ? -2.966  4.530   -4.658  1.00 41.62  ? 381  ASN A ND2 1 
ATOM   3102 N  N   . PRO A 1 382 ? -5.208  1.519   -1.199  1.00 38.51  ? 382  PRO A N   1 
ATOM   3103 C  CA  . PRO A 1 382 ? -6.090  0.429   -1.637  1.00 37.47  ? 382  PRO A CA  1 
ATOM   3104 C  C   . PRO A 1 382 ? -6.451  0.489   -3.103  1.00 37.99  ? 382  PRO A C   1 
ATOM   3105 O  O   . PRO A 1 382 ? -6.809  -0.552  -3.660  1.00 35.85  ? 382  PRO A O   1 
ATOM   3106 C  CB  . PRO A 1 382 ? -7.332  0.600   -0.748  1.00 38.20  ? 382  PRO A CB  1 
ATOM   3107 C  CG  . PRO A 1 382 ? -6.805  1.320   0.467   1.00 43.82  ? 382  PRO A CG  1 
ATOM   3108 C  CD  . PRO A 1 382 ? -5.793  2.283   -0.085  1.00 39.86  ? 382  PRO A CD  1 
ATOM   3109 N  N   . SER A 1 383 ? -6.368  1.659   -3.755  1.00 32.59  ? 383  SER A N   1 
ATOM   3110 C  CA  . SER A 1 383 ? -6.689  1.710   -5.177  1.00 34.39  ? 383  SER A CA  1 
ATOM   3111 C  C   . SER A 1 383 ? -5.612  1.071   -6.039  1.00 35.41  ? 383  SER A C   1 
ATOM   3112 O  O   . SER A 1 383 ? -5.866  0.785   -7.209  1.00 38.47  ? 383  SER A O   1 
ATOM   3113 C  CB  . SER A 1 383 ? -6.907  3.157   -5.641  1.00 34.67  ? 383  SER A CB  1 
ATOM   3114 O  OG  . SER A 1 383 ? -7.889  3.819   -4.851  1.00 36.83  ? 383  SER A OG  1 
ATOM   3115 N  N   . ALA A 1 384 ? -4.418  0.864   -5.504  1.00 34.30  ? 384  ALA A N   1 
ATOM   3116 C  CA  . ALA A 1 384 ? -3.363  0.196   -6.252  1.00 37.76  ? 384  ALA A CA  1 
ATOM   3117 C  C   . ALA A 1 384 ? -3.372  -1.315  -6.071  1.00 39.26  ? 384  ALA A C   1 
ATOM   3118 O  O   . ALA A 1 384 ? -2.515  -2.000  -6.638  1.00 39.48  ? 384  ALA A O   1 
ATOM   3119 C  CB  . ALA A 1 384 ? -1.999  0.765   -5.850  1.00 38.38  ? 384  ALA A CB  1 
ATOM   3120 N  N   . ILE A 1 385 ? -4.292  -1.851  -5.278  1.00 36.45  ? 385  ILE A N   1 
ATOM   3121 C  CA  . ILE A 1 385 ? -4.412  -3.289  -5.062  1.00 35.81  ? 385  ILE A CA  1 
ATOM   3122 C  C   . ILE A 1 385 ? -5.532  -3.812  -5.958  1.00 35.74  ? 385  ILE A C   1 
ATOM   3123 O  O   . ILE A 1 385 ? -6.662  -3.316  -5.860  1.00 35.77  ? 385  ILE A O   1 
ATOM   3124 C  CB  . ILE A 1 385 ? -4.699  -3.598  -3.587  1.00 37.35  ? 385  ILE A CB  1 
ATOM   3125 C  CG1 . ILE A 1 385 ? -3.581  -3.023  -2.700  1.00 39.75  ? 385  ILE A CG1 1 
ATOM   3126 C  CG2 . ILE A 1 385 ? -4.910  -5.107  -3.381  1.00 36.51  ? 385  ILE A CG2 1 
ATOM   3127 C  CD1 . ILE A 1 385 ? -3.884  -3.086  -1.206  1.00 41.05  ? 385  ILE A CD1 1 
ATOM   3128 N  N   . PRO A 1 386 ? -5.279  -4.801  -6.817  1.00 35.78  ? 386  PRO A N   1 
ATOM   3129 C  CA  . PRO A 1 386 ? -6.344  -5.310  -7.696  1.00 34.80  ? 386  PRO A CA  1 
ATOM   3130 C  C   . PRO A 1 386 ? -7.544  -5.847  -6.920  1.00 31.94  ? 386  PRO A C   1 
ATOM   3131 O  O   . PRO A 1 386 ? -7.460  -6.209  -5.743  1.00 33.88  ? 386  PRO A O   1 
ATOM   3132 C  CB  . PRO A 1 386 ? -5.651  -6.431  -8.486  1.00 36.49  ? 386  PRO A CB  1 
ATOM   3133 C  CG  . PRO A 1 386 ? -4.215  -6.042  -8.483  1.00 38.83  ? 386  PRO A CG  1 
ATOM   3134 C  CD  . PRO A 1 386 ? -3.959  -5.359  -7.166  1.00 38.56  ? 386  PRO A CD  1 
ATOM   3135 N  N   . GLN A 1 387 ? -8.677  -5.928  -7.623  1.00 33.53  ? 387  GLN A N   1 
ATOM   3136 C  CA  . GLN A 1 387 ? -9.909  -6.382  -6.986  1.00 33.10  ? 387  GLN A CA  1 
ATOM   3137 C  C   . GLN A 1 387 ? -9.752  -7.800  -6.452  1.00 33.81  ? 387  GLN A C   1 
ATOM   3138 O  O   . GLN A 1 387 ? -9.192  -8.675  -7.119  1.00 33.98  ? 387  GLN A O   1 
ATOM   3139 C  CB  . GLN A 1 387 ? -11.074 -6.344  -7.979  1.00 33.76  ? 387  GLN A CB  1 
ATOM   3140 C  CG  . GLN A 1 387 ? -11.592 -4.967  -8.295  1.00 32.81  ? 387  GLN A CG  1 
ATOM   3141 C  CD  . GLN A 1 387 ? -13.010 -5.011  -8.826  1.00 35.68  ? 387  GLN A CD  1 
ATOM   3142 O  OE1 . GLN A 1 387 ? -13.976 -4.997  -8.048  1.00 35.19  ? 387  GLN A OE1 1 
ATOM   3143 N  NE2 . GLN A 1 387 ? -13.148 -5.062  -10.149 1.00 37.11  ? 387  GLN A NE2 1 
ATOM   3144 N  N   . HIS A 1 388 ? -10.249 -8.019  -5.234  1.00 32.93  ? 388  HIS A N   1 
ATOM   3145 C  CA  . HIS A 1 388 ? -10.345 -9.339  -4.618  1.00 35.03  ? 388  HIS A CA  1 
ATOM   3146 C  C   . HIS A 1 388 ? -8.993  -9.988  -4.400  1.00 31.57  ? 388  HIS A C   1 
ATOM   3147 O  O   . HIS A 1 388 ? -8.909  -11.209 -4.217  1.00 33.95  ? 388  HIS A O   1 
ATOM   3148 C  CB  . HIS A 1 388 ? -11.259 -10.247 -5.431  1.00 34.19  ? 388  HIS A CB  1 
ATOM   3149 C  CG  . HIS A 1 388 ? -12.615 -9.653  -5.622  1.00 34.75  ? 388  HIS A CG  1 
ATOM   3150 N  ND1 . HIS A 1 388 ? -13.409 -9.296  -4.551  1.00 36.20  ? 388  HIS A ND1 1 
ATOM   3151 C  CD2 . HIS A 1 388 ? -13.285 -9.272  -6.736  1.00 36.07  ? 388  HIS A CD2 1 
ATOM   3152 C  CE1 . HIS A 1 388 ? -14.533 -8.761  -5.002  1.00 37.47  ? 388  HIS A CE1 1 
ATOM   3153 N  NE2 . HIS A 1 388 ? -14.480 -8.730  -6.323  1.00 38.47  ? 388  HIS A NE2 1 
ATOM   3154 N  N   . ALA A 1 389 ? -7.931  -9.184  -4.376  1.00 32.89  ? 389  ALA A N   1 
ATOM   3155 C  CA  . ALA A 1 389 ? -6.621  -9.702  -3.995  1.00 33.52  ? 389  ALA A CA  1 
ATOM   3156 C  C   . ALA A 1 389 ? -6.502  -10.000 -2.507  1.00 33.06  ? 389  ALA A C   1 
ATOM   3157 O  O   . ALA A 1 389 ? -5.609  -10.758 -2.119  1.00 34.39  ? 389  ALA A O   1 
ATOM   3158 C  CB  . ALA A 1 389 ? -5.534  -8.701  -4.357  1.00 32.86  ? 389  ALA A CB  1 
ATOM   3159 N  N   . PHE A 1 390 ? -7.352  -9.407  -1.669  1.00 30.85  ? 390  PHE A N   1 
ATOM   3160 C  CA  . PHE A 1 390 ? -7.159  -9.399  -0.221  1.00 29.58  ? 390  PHE A CA  1 
ATOM   3161 C  C   . PHE A 1 390 ? -8.517  -9.689  0.411   1.00 32.76  ? 390  PHE A C   1 
ATOM   3162 O  O   . PHE A 1 390 ? -9.391  -8.826  0.382   1.00 32.82  ? 390  PHE A O   1 
ATOM   3163 C  CB  . PHE A 1 390 ? -6.593  -8.044  0.213   1.00 32.45  ? 390  PHE A CB  1 
ATOM   3164 C  CG  . PHE A 1 390 ? -6.375  -7.888  1.703   1.00 34.98  ? 390  PHE A CG  1 
ATOM   3165 C  CD1 . PHE A 1 390 ? -5.395  -8.618  2.364   1.00 31.79  ? 390  PHE A CD1 1 
ATOM   3166 C  CD2 . PHE A 1 390 ? -7.123  -6.962  2.431   1.00 31.54  ? 390  PHE A CD2 1 
ATOM   3167 C  CE1 . PHE A 1 390 ? -5.193  -8.450  3.732   1.00 32.13  ? 390  PHE A CE1 1 
ATOM   3168 C  CE2 . PHE A 1 390 ? -6.922  -6.784  3.790   1.00 33.98  ? 390  PHE A CE2 1 
ATOM   3169 C  CZ  . PHE A 1 390 ? -5.948  -7.519  4.442   1.00 33.87  ? 390  PHE A CZ  1 
ATOM   3170 N  N   . LYS A 1 391 ? -8.709  -10.911 0.938   1.00 32.25  ? 391  LYS A N   1 
ATOM   3171 C  CA  . LYS A 1 391 ? -10.042 -11.367 1.351   1.00 29.96  ? 391  LYS A CA  1 
ATOM   3172 C  C   . LYS A 1 391 ? -10.084 -11.956 2.760   1.00 31.26  ? 391  LYS A C   1 
ATOM   3173 O  O   . LYS A 1 391 ? -10.754 -12.974 2.981   1.00 32.04  ? 391  LYS A O   1 
ATOM   3174 C  CB  . LYS A 1 391 ? -10.585 -12.415 0.379   1.00 31.70  ? 391  LYS A CB  1 
ATOM   3175 C  CG  . LYS A 1 391 ? -10.533 -12.057 -1.112  1.00 34.97  ? 391  LYS A CG  1 
ATOM   3176 C  CD  . LYS A 1 391 ? -11.418 -10.867 -1.461  1.00 33.88  ? 391  LYS A CD  1 
ATOM   3177 C  CE  . LYS A 1 391 ? -12.889 -11.146 -1.165  1.00 35.56  ? 391  LYS A CE  1 
ATOM   3178 N  NZ  . LYS A 1 391 ? -13.744 -10.048 -1.707  1.00 36.29  ? 391  LYS A NZ  1 
ATOM   3179 N  N   . PRO A 1 392 ? -9.416  -11.361 3.745   1.00 31.66  ? 392  PRO A N   1 
ATOM   3180 C  CA  . PRO A 1 392 ? -9.421  -11.972 5.084   1.00 30.27  ? 392  PRO A CA  1 
ATOM   3181 C  C   . PRO A 1 392 ? -10.766 -11.894 5.772   1.00 34.41  ? 392  PRO A C   1 
ATOM   3182 O  O   . PRO A 1 392 ? -10.959 -12.576 6.786   1.00 33.25  ? 392  PRO A O   1 
ATOM   3183 C  CB  . PRO A 1 392 ? -8.370  -11.163 5.834   1.00 31.66  ? 392  PRO A CB  1 
ATOM   3184 C  CG  . PRO A 1 392 ? -8.479  -9.823  5.249   1.00 32.20  ? 392  PRO A CG  1 
ATOM   3185 C  CD  . PRO A 1 392 ? -8.750  -10.044 3.761   1.00 31.82  ? 392  PRO A CD  1 
ATOM   3186 N  N   . HIS A 1 393 ? -11.691 -11.092 5.251   1.00 30.32  ? 393  HIS A N   1 
ATOM   3187 C  CA  . HIS A 1 393 ? -12.999 -10.903 5.868   1.00 33.43  ? 393  HIS A CA  1 
ATOM   3188 C  C   . HIS A 1 393 ? -14.103 -11.540 5.041   1.00 31.83  ? 393  HIS A C   1 
ATOM   3189 O  O   . HIS A 1 393 ? -15.284 -11.193 5.226   1.00 32.51  ? 393  HIS A O   1 
ATOM   3190 C  CB  . HIS A 1 393 ? -13.321 -9.412  6.017   1.00 36.07  ? 393  HIS A CB  1 
ATOM   3191 C  CG  . HIS A 1 393 ? -12.233 -8.598  6.635   1.00 41.50  ? 393  HIS A CG  1 
ATOM   3192 N  ND1 . HIS A 1 393 ? -11.829 -8.753  7.940   1.00 38.81  ? 393  HIS A ND1 1 
ATOM   3193 C  CD2 . HIS A 1 393 ? -11.485 -7.589  6.124   1.00 44.73  ? 393  HIS A CD2 1 
ATOM   3194 C  CE1 . HIS A 1 393 ? -10.874 -7.881  8.210   1.00 41.10  ? 393  HIS A CE1 1 
ATOM   3195 N  NE2 . HIS A 1 393 ? -10.648 -7.161  7.123   1.00 44.50  ? 393  HIS A NE2 1 
ATOM   3196 N  N   . GLY A 1 394 ? -13.756 -12.399 4.084   1.00 31.48  ? 394  GLY A N   1 
ATOM   3197 C  CA  . GLY A 1 394 ? -14.792 -12.987 3.255   1.00 31.71  ? 394  GLY A CA  1 
ATOM   3198 C  C   . GLY A 1 394 ? -15.229 -12.054 2.137   1.00 31.06  ? 394  GLY A C   1 
ATOM   3199 O  O   . GLY A 1 394 ? -14.488 -11.160 1.712   1.00 32.28  ? 394  GLY A O   1 
ATOM   3200 N  N   . ASN A 1 395 ? -16.457 -12.273 1.645   1.00 30.30  ? 395  ASN A N   1 
ATOM   3201 C  CA  . ASN A 1 395 ? -16.883 -11.633 0.407   1.00 31.29  ? 395  ASN A CA  1 
ATOM   3202 C  C   . ASN A 1 395 ? -18.350 -11.217 0.421   1.00 33.92  ? 395  ASN A C   1 
ATOM   3203 O  O   . ASN A 1 395 ? -19.221 -11.967 0.876   1.00 31.14  ? 395  ASN A O   1 
ATOM   3204 C  CB  . ASN A 1 395 ? -16.685 -12.551 -0.805  1.00 32.07  ? 395  ASN A CB  1 
ATOM   3205 C  CG  . ASN A 1 395 ? -16.983 -11.831 -2.121  1.00 32.06  ? 395  ASN A CG  1 
ATOM   3206 O  OD1 . ASN A 1 395 ? -16.261 -10.899 -2.500  1.00 33.55  ? 395  ASN A OD1 1 
ATOM   3207 N  ND2 . ASN A 1 395 ? -18.047 -12.250 -2.817  1.00 32.18  ? 395  ASN A ND2 1 
ATOM   3208 N  N   . GLY A 1 396 ? -18.614 -10.023 -0.123  1.00 33.58  ? 396  GLY A N   1 
ATOM   3209 C  CA  . GLY A 1 396 ? -19.971 -9.639  -0.478  1.00 33.41  ? 396  GLY A CA  1 
ATOM   3210 C  C   . GLY A 1 396 ? -20.889 -9.477  0.722   1.00 32.58  ? 396  GLY A C   1 
ATOM   3211 O  O   . GLY A 1 396 ? -20.470 -9.077  1.815   1.00 31.24  ? 396  GLY A O   1 
ATOM   3212 N  N   . GLN A 1 397 ? -22.177 -9.765  0.500   1.00 31.32  ? 397  GLN A N   1 
ATOM   3213 C  CA  . GLN A 1 397 ? -23.133 -9.624  1.590   1.00 32.86  ? 397  GLN A CA  1 
ATOM   3214 C  C   . GLN A 1 397 ? -22.868 -10.613 2.717   1.00 31.35  ? 397  GLN A C   1 
ATOM   3215 O  O   . GLN A 1 397 ? -23.337 -10.388 3.839   1.00 31.76  ? 397  GLN A O   1 
ATOM   3216 C  CB  . GLN A 1 397 ? -24.574 -9.782  1.082   1.00 32.81  ? 397  GLN A CB  1 
ATOM   3217 C  CG  . GLN A 1 397 ? -24.931 -11.172 0.561   1.00 34.22  ? 397  GLN A CG  1 
ATOM   3218 C  CD  . GLN A 1 397 ? -26.346 -11.222 -0.024  1.00 39.49  ? 397  GLN A CD  1 
ATOM   3219 O  OE1 . GLN A 1 397 ? -27.176 -10.360 0.266   1.00 37.15  ? 397  GLN A OE1 1 
ATOM   3220 N  NE2 . GLN A 1 397 ? -26.610 -12.210 -0.864  1.00 36.54  ? 397  GLN A NE2 1 
ATOM   3221 N  N   . ARG A 1 398 ? -22.103 -11.676 2.454   1.00 33.46  ? 398  ARG A N   1 
ATOM   3222 C  CA  . ARG A 1 398 ? -21.712 -12.634 3.482   1.00 33.07  ? 398  ARG A CA  1 
ATOM   3223 C  C   . ARG A 1 398 ? -20.324 -12.341 4.047   1.00 31.14  ? 398  ARG A C   1 
ATOM   3224 O  O   . ARG A 1 398 ? -19.727 -13.211 4.688   1.00 31.34  ? 398  ARG A O   1 
ATOM   3225 C  CB  . ARG A 1 398 ? -21.777 -14.069 2.946   1.00 32.11  ? 398  ARG A CB  1 
ATOM   3226 C  CG  . ARG A 1 398 ? -23.169 -14.533 2.473   1.00 30.36  ? 398  ARG A CG  1 
ATOM   3227 C  CD  . ARG A 1 398 ? -24.249 -14.309 3.518   1.00 29.36  ? 398  ARG A CD  1 
ATOM   3228 N  NE  . ARG A 1 398 ? -23.979 -14.978 4.792   1.00 29.00  ? 398  ARG A NE  1 
ATOM   3229 C  CZ  . ARG A 1 398 ? -24.301 -16.234 5.067   1.00 30.91  ? 398  ARG A CZ  1 
ATOM   3230 N  NH1 . ARG A 1 398 ? -24.895 -17.008 4.170   1.00 30.87  ? 398  ARG A NH1 1 
ATOM   3231 N  NH2 . ARG A 1 398 ? -24.017 -16.727 6.273   1.00 31.51  ? 398  ARG A NH2 1 
ATOM   3232 N  N   . ALA A 1 399 ? -19.795 -11.140 3.813   1.00 32.68  ? 399  ALA A N   1 
ATOM   3233 C  CA  . ALA A 1 399 ? -18.539 -10.762 4.427   1.00 29.58  ? 399  ALA A CA  1 
ATOM   3234 C  C   . ALA A 1 399 ? -18.729 -10.561 5.935   1.00 32.48  ? 399  ALA A C   1 
ATOM   3235 O  O   . ALA A 1 399 ? -19.848 -10.504 6.459   1.00 30.80  ? 399  ALA A O   1 
ATOM   3236 C  CB  . ALA A 1 399 ? -17.969 -9.490  3.782   1.00 33.40  ? 399  ALA A CB  1 
ATOM   3237 N  N   . CYS A 1 400 ? -17.604 -10.452 6.628   1.00 29.76  ? 400  CYS A N   1 
ATOM   3238 C  CA  . CYS A 1 400 ? -17.587 -10.367 8.084   1.00 30.81  ? 400  CYS A CA  1 
ATOM   3239 C  C   . CYS A 1 400 ? -18.396 -9.169  8.570   1.00 32.21  ? 400  CYS A C   1 
ATOM   3240 O  O   . CYS A 1 400 ? -18.118 -8.031  8.187   1.00 32.69  ? 400  CYS A O   1 
ATOM   3241 C  CB  . CYS A 1 400 ? -16.128 -10.264 8.536   1.00 28.26  ? 400  CYS A CB  1 
ATOM   3242 S  SG  . CYS A 1 400 ? -15.947 -10.022 10.298  1.00 30.81  ? 400  CYS A SG  1 
ATOM   3243 N  N   . ILE A 1 401 ? -19.404 -9.417  9.417   1.00 30.49  ? 401  ILE A N   1 
ATOM   3244 C  CA  . ILE A 1 401 ? -20.150 -8.304  9.996   1.00 29.95  ? 401  ILE A CA  1 
ATOM   3245 C  C   . ILE A 1 401 ? -19.377 -7.594  11.108  1.00 33.28  ? 401  ILE A C   1 
ATOM   3246 O  O   . ILE A 1 401 ? -19.681 -6.432  11.420  1.00 32.51  ? 401  ILE A O   1 
ATOM   3247 C  CB  . ILE A 1 401 ? -21.506 -8.801  10.531  1.00 28.18  ? 401  ILE A CB  1 
ATOM   3248 C  CG1 . ILE A 1 401 ? -22.495 -7.643  10.692  1.00 33.51  ? 401  ILE A CG1 1 
ATOM   3249 C  CG2 . ILE A 1 401 ? -21.295 -9.519  11.855  1.00 31.57  ? 401  ILE A CG2 1 
ATOM   3250 C  CD1 . ILE A 1 401 ? -23.882 -8.090  11.193  1.00 34.49  ? 401  ILE A CD1 1 
ATOM   3251 N  N   . GLY A 1 402 ? -18.389 -8.252  11.716  1.00 31.08  ? 402  GLY A N   1 
ATOM   3252 C  CA  . GLY A 1 402 ? -17.672 -7.711  12.852  1.00 33.33  ? 402  GLY A CA  1 
ATOM   3253 C  C   . GLY A 1 402 ? -16.319 -7.110  12.531  1.00 32.97  ? 402  GLY A C   1 
ATOM   3254 O  O   . GLY A 1 402 ? -15.559 -6.806  13.458  1.00 32.09  ? 402  GLY A O   1 
ATOM   3255 N  N   . GLN A 1 403 ? -16.016 -6.896  11.249  1.00 31.46  ? 403  GLN A N   1 
ATOM   3256 C  CA  . GLN A 1 403 ? -14.701 -6.419  10.831  1.00 34.01  ? 403  GLN A CA  1 
ATOM   3257 C  C   . GLN A 1 403 ? -14.287 -5.145  11.553  1.00 33.75  ? 403  GLN A C   1 
ATOM   3258 O  O   . GLN A 1 403 ? -13.131 -5.012  11.973  1.00 34.08  ? 403  GLN A O   1 
ATOM   3259 C  CB  . GLN A 1 403 ? -14.699 -6.184  9.314   1.00 36.88  ? 403  GLN A CB  1 
ATOM   3260 C  CG  . GLN A 1 403 ? -13.427 -5.526  8.822   1.00 44.92  ? 403  GLN A CG  1 
ATOM   3261 C  CD  . GLN A 1 403 ? -13.501 -5.132  7.362   1.00 48.62  ? 403  GLN A CD  1 
ATOM   3262 O  OE1 . GLN A 1 403 ? -14.414 -5.541  6.642   1.00 40.38  ? 403  GLN A OE1 1 
ATOM   3263 N  NE2 . GLN A 1 403 ? -12.546 -4.305  6.923   1.00 49.89  ? 403  GLN A NE2 1 
ATOM   3264 N  N   . GLN A 1 404 ? -15.200 -4.175  11.674  1.00 36.20  ? 404  GLN A N   1 
ATOM   3265 C  CA  . GLN A 1 404 ? -14.817 -2.909  12.293  1.00 37.94  ? 404  GLN A CA  1 
ATOM   3266 C  C   . GLN A 1 404 ? -14.560 -3.087  13.781  1.00 35.31  ? 404  GLN A C   1 
ATOM   3267 O  O   . GLN A 1 404 ? -13.649 -2.460  14.338  1.00 36.48  ? 404  GLN A O   1 
ATOM   3268 C  CB  . GLN A 1 404 ? -15.890 -1.843  12.066  1.00 35.86  ? 404  GLN A CB  1 
ATOM   3269 C  CG  . GLN A 1 404 ? -16.043 -1.451  10.605  1.00 43.90  ? 404  GLN A CG  1 
ATOM   3270 C  CD  . GLN A 1 404 ? -14.808 -0.759  10.085  1.00 53.21  ? 404  GLN A CD  1 
ATOM   3271 O  OE1 . GLN A 1 404 ? -14.179 -1.237  9.141   1.00 59.75  ? 404  GLN A OE1 1 
ATOM   3272 N  NE2 . GLN A 1 404 ? -14.415 0.337   10.733  1.00 51.86  ? 404  GLN A NE2 1 
ATOM   3273 N  N   . PHE A 1 405 ? -15.357 -3.933  14.436  1.00 31.80  ? 405  PHE A N   1 
ATOM   3274 C  CA  . PHE A 1 405 ? -15.133 -4.253  15.845  1.00 31.09  ? 405  PHE A CA  1 
ATOM   3275 C  C   . PHE A 1 405 ? -13.748 -4.847  16.036  1.00 34.40  ? 405  PHE A C   1 
ATOM   3276 O  O   . PHE A 1 405 ? -12.980 -4.404  16.903  1.00 33.95  ? 405  PHE A O   1 
ATOM   3277 C  CB  . PHE A 1 405 ? -16.219 -5.225  16.331  1.00 32.33  ? 405  PHE A CB  1 
ATOM   3278 C  CG  . PHE A 1 405 ? -16.228 -5.475  17.822  1.00 33.45  ? 405  PHE A CG  1 
ATOM   3279 C  CD1 . PHE A 1 405 ? -15.361 -6.397  18.388  1.00 31.44  ? 405  PHE A CD1 1 
ATOM   3280 C  CD2 . PHE A 1 405 ? -17.148 -4.833  18.655  1.00 32.96  ? 405  PHE A CD2 1 
ATOM   3281 C  CE1 . PHE A 1 405 ? -15.381 -6.659  19.752  1.00 35.79  ? 405  PHE A CE1 1 
ATOM   3282 C  CE2 . PHE A 1 405 ? -17.168 -5.089  20.035  1.00 33.78  ? 405  PHE A CE2 1 
ATOM   3283 C  CZ  . PHE A 1 405 ? -16.292 -6.014  20.576  1.00 31.66  ? 405  PHE A CZ  1 
ATOM   3284 N  N   . ALA A 1 406 ? -13.417 -5.863  15.232  1.00 33.09  ? 406  ALA A N   1 
ATOM   3285 C  CA  . ALA A 1 406 ? -12.122 -6.533  15.329  1.00 35.60  ? 406  ALA A CA  1 
ATOM   3286 C  C   . ALA A 1 406 ? -10.983 -5.551  15.125  1.00 34.26  ? 406  ALA A C   1 
ATOM   3287 O  O   . ALA A 1 406 ? -10.006 -5.542  15.887  1.00 33.08  ? 406  ALA A O   1 
ATOM   3288 C  CB  . ALA A 1 406 ? -12.027 -7.658  14.287  1.00 31.87  ? 406  ALA A CB  1 
ATOM   3289 N  N   . LEU A 1 407 ? -11.074 -4.735  14.079  1.00 33.37  ? 407  LEU A N   1 
ATOM   3290 C  CA  . LEU A 1 407 ? -9.942  -3.866  13.772  1.00 35.16  ? 407  LEU A CA  1 
ATOM   3291 C  C   . LEU A 1 407 ? -9.842  -2.712  14.762  1.00 33.51  ? 407  LEU A C   1 
ATOM   3292 O  O   . LEU A 1 407 ? -8.733  -2.287  15.101  1.00 35.91  ? 407  LEU A O   1 
ATOM   3293 C  CB  . LEU A 1 407 ? -10.033 -3.381  12.323  1.00 36.19  ? 407  LEU A CB  1 
ATOM   3294 C  CG  . LEU A 1 407 ? -9.731  -4.498  11.304  1.00 41.26  ? 407  LEU A CG  1 
ATOM   3295 C  CD1 . LEU A 1 407 ? -10.066 -4.091  9.855   1.00 45.38  ? 407  LEU A CD1 1 
ATOM   3296 C  CD2 . LEU A 1 407 ? -8.285  -4.981  11.410  1.00 41.46  ? 407  LEU A CD2 1 
ATOM   3297 N  N   . HIS A 1 408 ? -10.961 -2.222  15.295  1.00 34.04  ? 408  HIS A N   1 
ATOM   3298 C  CA  . HIS A 1 408 ? -10.847 -1.188  16.316  1.00 34.26  ? 408  HIS A CA  1 
ATOM   3299 C  C   . HIS A 1 408 ? -10.200 -1.756  17.573  1.00 32.55  ? 408  HIS A C   1 
ATOM   3300 O  O   . HIS A 1 408 ? -9.278  -1.153  18.147  1.00 34.48  ? 408  HIS A O   1 
ATOM   3301 C  CB  . HIS A 1 408 ? -12.222 -0.600  16.636  1.00 35.03  ? 408  HIS A CB  1 
ATOM   3302 C  CG  . HIS A 1 408 ? -12.167 0.633   17.485  1.00 36.50  ? 408  HIS A CG  1 
ATOM   3303 N  ND1 . HIS A 1 408 ? -12.015 1.895   16.950  1.00 35.43  ? 408  HIS A ND1 1 
ATOM   3304 C  CD2 . HIS A 1 408 ? -12.245 0.799   18.828  1.00 36.96  ? 408  HIS A CD2 1 
ATOM   3305 C  CE1 . HIS A 1 408 ? -12.018 2.786   17.928  1.00 37.77  ? 408  HIS A CE1 1 
ATOM   3306 N  NE2 . HIS A 1 408 ? -12.146 2.147   19.077  1.00 36.12  ? 408  HIS A NE2 1 
ATOM   3307 N  N   . GLU A 1 409 ? -10.670 -2.925  18.016  1.00 31.47  ? 409  GLU A N   1 
ATOM   3308 C  CA  . GLU A 1 409 ? -10.090 -3.554  19.200  1.00 29.98  ? 409  GLU A CA  1 
ATOM   3309 C  C   . GLU A 1 409 ? -8.605  -3.825  18.998  1.00 34.86  ? 409  GLU A C   1 
ATOM   3310 O  O   . GLU A 1 409 ? -7.770  -3.486  19.851  1.00 34.34  ? 409  GLU A O   1 
ATOM   3311 C  CB  . GLU A 1 409 ? -10.836 -4.851  19.512  1.00 32.27  ? 409  GLU A CB  1 
ATOM   3312 C  CG  . GLU A 1 409 ? -10.162 -5.685  20.594  1.00 30.77  ? 409  GLU A CG  1 
ATOM   3313 C  CD  . GLU A 1 409 ? -10.887 -6.986  20.861  1.00 32.93  ? 409  GLU A CD  1 
ATOM   3314 O  OE1 . GLU A 1 409 ? -11.825 -7.325  20.107  1.00 32.34  ? 409  GLU A OE1 1 
ATOM   3315 O  OE2 . GLU A 1 409 ? -10.535 -7.659  21.842  1.00 32.00  ? 409  GLU A OE2 1 
ATOM   3316 N  N   . ALA A 1 410 ? -8.251  -4.443  17.867  1.00 31.63  ? 410  ALA A N   1 
ATOM   3317 C  CA  . ALA A 1 410 ? -6.852  -4.811  17.653  1.00 32.87  ? 410  ALA A CA  1 
ATOM   3318 C  C   . ALA A 1 410 ? -5.976  -3.571  17.528  1.00 35.31  ? 410  ALA A C   1 
ATOM   3319 O  O   . ALA A 1 410 ? -4.841  -3.548  18.024  1.00 36.01  ? 410  ALA A O   1 
ATOM   3320 C  CB  . ALA A 1 410 ? -6.712  -5.703  16.415  1.00 32.51  ? 410  ALA A CB  1 
ATOM   3321 N  N   . THR A 1 411 ? -6.485  -2.525  16.876  1.00 34.53  ? 411  THR A N   1 
ATOM   3322 C  CA  . THR A 1 411 ? -5.702  -1.297  16.745  1.00 34.21  ? 411  THR A CA  1 
ATOM   3323 C  C   . THR A 1 411 ? -5.508  -0.623  18.105  1.00 35.00  ? 411  THR A C   1 
ATOM   3324 O  O   . THR A 1 411 ? -4.389  -0.212  18.454  1.00 35.57  ? 411  THR A O   1 
ATOM   3325 C  CB  . THR A 1 411 ? -6.391  -0.352  15.760  1.00 34.75  ? 411  THR A CB  1 
ATOM   3326 O  OG1 . THR A 1 411 ? -6.494  -0.982  14.467  1.00 33.43  ? 411  THR A OG1 1 
ATOM   3327 C  CG2 . THR A 1 411 ? -5.596  0.954   15.635  1.00 36.32  ? 411  THR A CG2 1 
ATOM   3328 N  N   . LEU A 1 412 ? -6.585  -0.515  18.895  1.00 32.80  ? 412  LEU A N   1 
ATOM   3329 C  CA  . LEU A 1 412 ? -6.471  0.008   20.257  1.00 31.51  ? 412  LEU A CA  1 
ATOM   3330 C  C   . LEU A 1 412 ? -5.415  -0.753  21.063  1.00 35.96  ? 412  LEU A C   1 
ATOM   3331 O  O   . LEU A 1 412 ? -4.521  -0.147  21.674  1.00 35.50  ? 412  LEU A O   1 
ATOM   3332 C  CB  . LEU A 1 412 ? -7.834  -0.066  20.962  1.00 33.78  ? 412  LEU A CB  1 
ATOM   3333 C  CG  . LEU A 1 412 ? -7.799  0.065   22.487  1.00 38.66  ? 412  LEU A CG  1 
ATOM   3334 C  CD1 . LEU A 1 412 ? -7.392  1.478   22.868  1.00 39.48  ? 412  LEU A CD1 1 
ATOM   3335 C  CD2 . LEU A 1 412 ? -9.149  -0.300  23.104  1.00 38.38  ? 412  LEU A CD2 1 
ATOM   3336 N  N   . VAL A 1 413 ? -5.511  -2.086  21.086  1.00 34.74  ? 413  VAL A N   1 
ATOM   3337 C  CA  . VAL A 1 413 ? -4.685  -2.885  21.996  1.00 33.65  ? 413  VAL A CA  1 
ATOM   3338 C  C   . VAL A 1 413 ? -3.228  -2.885  21.540  1.00 36.20  ? 413  VAL A C   1 
ATOM   3339 O  O   . VAL A 1 413 ? -2.305  -2.699  22.346  1.00 35.16  ? 413  VAL A O   1 
ATOM   3340 C  CB  . VAL A 1 413 ? -5.253  -4.316  22.105  1.00 36.42  ? 413  VAL A CB  1 
ATOM   3341 C  CG1 . VAL A 1 413 ? -4.351  -5.196  22.938  1.00 42.29  ? 413  VAL A CG1 1 
ATOM   3342 C  CG2 . VAL A 1 413 ? -6.662  -4.286  22.724  1.00 35.29  ? 413  VAL A CG2 1 
ATOM   3343 N  N   . LEU A 1 414 ? -2.992  -3.087  20.241  1.00 34.36  ? 414  LEU A N   1 
ATOM   3344 C  CA  . LEU A 1 414 ? -1.611  -3.045  19.755  1.00 36.23  ? 414  LEU A CA  1 
ATOM   3345 C  C   . LEU A 1 414 ? -1.010  -1.657  19.945  1.00 38.54  ? 414  LEU A C   1 
ATOM   3346 O  O   . LEU A 1 414 ? 0.184   -1.530  20.254  1.00 37.85  ? 414  LEU A O   1 
ATOM   3347 C  CB  . LEU A 1 414 ? -1.548  -3.473  18.278  1.00 36.05  ? 414  LEU A CB  1 
ATOM   3348 C  CG  . LEU A 1 414 ? -0.202  -3.807  17.629  1.00 41.38  ? 414  LEU A CG  1 
ATOM   3349 C  CD1 . LEU A 1 414 ? 0.587   -4.800  18.497  1.00 39.50  ? 414  LEU A CD1 1 
ATOM   3350 C  CD2 . LEU A 1 414 ? -0.392  -4.360  16.192  1.00 35.79  ? 414  LEU A CD2 1 
ATOM   3351 N  N   . GLY A 1 415 ? -1.824  -0.611  19.796  1.00 35.45  ? 415  GLY A N   1 
ATOM   3352 C  CA  . GLY A 1 415 ? -1.340  0.739   20.058  1.00 33.77  ? 415  GLY A CA  1 
ATOM   3353 C  C   . GLY A 1 415 ? -0.893  0.920   21.497  1.00 42.41  ? 415  GLY A C   1 
ATOM   3354 O  O   . GLY A 1 415 ? 0.186   1.456   21.768  1.00 41.18  ? 415  GLY A O   1 
ATOM   3355 N  N   . MET A 1 416 ? -1.714  0.466   22.443  1.00 37.26  ? 416  MET A N   1 
ATOM   3356 C  CA  . MET A 1 416 ? -1.314  0.568   23.844  1.00 36.03  ? 416  MET A CA  1 
ATOM   3357 C  C   . MET A 1 416 ? -0.103  -0.309  24.141  1.00 36.94  ? 416  MET A C   1 
ATOM   3358 O  O   . MET A 1 416 ? 0.785   0.086   24.910  1.00 38.82  ? 416  MET A O   1 
ATOM   3359 C  CB  . MET A 1 416 ? -2.483  0.216   24.758  1.00 36.89  ? 416  MET A CB  1 
ATOM   3360 C  CG  . MET A 1 416 ? -3.635  1.198   24.686  1.00 37.79  ? 416  MET A CG  1 
ATOM   3361 S  SD  . MET A 1 416 ? -4.976  0.767   25.812  1.00 41.44  ? 416  MET A SD  1 
ATOM   3362 C  CE  . MET A 1 416 ? -4.388  1.518   27.318  1.00 45.14  ? 416  MET A CE  1 
ATOM   3363 N  N   . MET A 1 417 ? -0.039  -1.490  23.533  1.00 36.75  ? 417  MET A N   1 
ATOM   3364 C  CA  . MET A 1 417 ? 1.108   -2.361  23.733  1.00 36.79  ? 417  MET A CA  1 
ATOM   3365 C  C   . MET A 1 417 ? 2.390   -1.655  23.318  1.00 41.92  ? 417  MET A C   1 
ATOM   3366 O  O   . MET A 1 417 ? 3.403   -1.700  24.026  1.00 37.26  ? 417  MET A O   1 
ATOM   3367 C  CB  . MET A 1 417 ? 0.911   -3.640  22.936  1.00 38.28  ? 417  MET A CB  1 
ATOM   3368 C  CG  . MET A 1 417 ? -0.211  -4.494  23.494  1.00 38.19  ? 417  MET A CG  1 
ATOM   3369 S  SD  . MET A 1 417 ? -0.582  -5.924  22.476  1.00 38.36  ? 417  MET A SD  1 
ATOM   3370 C  CE  . MET A 1 417 ? 1.028   -6.432  21.896  1.00 40.15  ? 417  MET A CE  1 
ATOM   3371 N  N   . LEU A 1 418 ? 2.362   -1.000  22.159  1.00 36.48  ? 418  LEU A N   1 
ATOM   3372 C  CA  . LEU A 1 418 ? 3.556   -0.339  21.647  1.00 37.19  ? 418  LEU A CA  1 
ATOM   3373 C  C   . LEU A 1 418 ? 3.840   0.972   22.362  1.00 37.20  ? 418  LEU A C   1 
ATOM   3374 O  O   . LEU A 1 418 ? 4.996   1.416   22.383  1.00 42.53  ? 418  LEU A O   1 
ATOM   3375 C  CB  . LEU A 1 418 ? 3.393   -0.102  20.139  1.00 38.55  ? 418  LEU A CB  1 
ATOM   3376 C  CG  . LEU A 1 418 ? 3.255   -1.383  19.304  1.00 42.44  ? 418  LEU A CG  1 
ATOM   3377 C  CD1 . LEU A 1 418 ? 2.912   -1.076  17.847  1.00 42.01  ? 418  LEU A CD1 1 
ATOM   3378 C  CD2 . LEU A 1 418 ? 4.508   -2.256  19.386  1.00 43.15  ? 418  LEU A CD2 1 
ATOM   3379 N  N   . LYS A 1 419 ? 2.817   1.601   22.942  1.00 37.40  ? 419  LYS A N   1 
ATOM   3380 C  CA  . LYS A 1 419 ? 3.042   2.793   23.749  1.00 38.89  ? 419  LYS A CA  1 
ATOM   3381 C  C   . LYS A 1 419 ? 3.732   2.442   25.060  1.00 42.08  ? 419  LYS A C   1 
ATOM   3382 O  O   . LYS A 1 419 ? 4.610   3.180   25.520  1.00 39.06  ? 419  LYS A O   1 
ATOM   3383 C  CB  . LYS A 1 419 ? 1.725   3.515   24.033  1.00 40.75  ? 419  LYS A CB  1 
ATOM   3384 C  CG  . LYS A 1 419 ? 1.852   4.657   25.058  1.00 41.91  ? 419  LYS A CG  1 
ATOM   3385 C  CD  . LYS A 1 419 ? 0.497   5.252   25.418  1.00 42.17  ? 419  LYS A CD  1 
ATOM   3386 C  CE  . LYS A 1 419 ? 0.638   6.400   26.403  1.00 43.11  ? 419  LYS A CE  1 
ATOM   3387 N  NZ  . LYS A 1 419 ? -0.638  7.131   26.613  1.00 46.79  ? 419  LYS A NZ  1 
ATOM   3388 N  N   . HIS A 1 420 ? 3.374   1.306   25.665  1.00 41.20  ? 420  HIS A N   1 
ATOM   3389 C  CA  . HIS A 1 420 ? 3.788   1.065   27.043  1.00 41.42  ? 420  HIS A CA  1 
ATOM   3390 C  C   . HIS A 1 420 ? 4.978   0.132   27.198  1.00 40.12  ? 420  HIS A C   1 
ATOM   3391 O  O   . HIS A 1 420 ? 5.557   0.093   28.290  1.00 41.57  ? 420  HIS A O   1 
ATOM   3392 C  CB  . HIS A 1 420 ? 2.609   0.522   27.860  1.00 38.60  ? 420  HIS A CB  1 
ATOM   3393 C  CG  . HIS A 1 420 ? 1.584   1.563   28.164  1.00 40.97  ? 420  HIS A CG  1 
ATOM   3394 N  ND1 . HIS A 1 420 ? 1.722   2.456   29.204  1.00 39.11  ? 420  HIS A ND1 1 
ATOM   3395 C  CD2 . HIS A 1 420 ? 0.422   1.879   27.547  1.00 38.47  ? 420  HIS A CD2 1 
ATOM   3396 C  CE1 . HIS A 1 420 ? 0.688   3.278   29.217  1.00 40.13  ? 420  HIS A CE1 1 
ATOM   3397 N  NE2 . HIS A 1 420 ? -0.118  2.947   28.223  1.00 42.34  ? 420  HIS A NE2 1 
ATOM   3398 N  N   . PHE A 1 421 ? 5.361   -0.622  26.173  1.00 40.30  ? 421  PHE A N   1 
ATOM   3399 C  CA  . PHE A 1 421 ? 6.402   -1.629  26.333  1.00 41.58  ? 421  PHE A CA  1 
ATOM   3400 C  C   . PHE A 1 421 ? 7.327   -1.673  25.128  1.00 45.71  ? 421  PHE A C   1 
ATOM   3401 O  O   . PHE A 1 421 ? 6.910   -1.454  23.988  1.00 43.95  ? 421  PHE A O   1 
ATOM   3402 C  CB  . PHE A 1 421 ? 5.828   -3.048  26.514  1.00 40.61  ? 421  PHE A CB  1 
ATOM   3403 C  CG  . PHE A 1 421 ? 4.824   -3.159  27.618  1.00 40.63  ? 421  PHE A CG  1 
ATOM   3404 C  CD1 . PHE A 1 421 ? 5.236   -3.382  28.920  1.00 40.57  ? 421  PHE A CD1 1 
ATOM   3405 C  CD2 . PHE A 1 421 ? 3.470   -3.047  27.355  1.00 40.76  ? 421  PHE A CD2 1 
ATOM   3406 C  CE1 . PHE A 1 421 ? 4.314   -3.481  29.954  1.00 39.89  ? 421  PHE A CE1 1 
ATOM   3407 C  CE2 . PHE A 1 421 ? 2.535   -3.145  28.388  1.00 37.23  ? 421  PHE A CE2 1 
ATOM   3408 C  CZ  . PHE A 1 421 ? 2.966   -3.359  29.694  1.00 39.33  ? 421  PHE A CZ  1 
ATOM   3409 N  N   . ASP A 1 422 ? 8.586   -2.000  25.397  1.00 43.57  ? 422  ASP A N   1 
ATOM   3410 C  CA  . ASP A 1 422 ? 9.454   -2.595  24.393  1.00 45.88  ? 422  ASP A CA  1 
ATOM   3411 C  C   . ASP A 1 422 ? 9.315   -4.103  24.476  1.00 45.25  ? 422  ASP A C   1 
ATOM   3412 O  O   . ASP A 1 422 ? 8.993   -4.651  25.533  1.00 44.88  ? 422  ASP A O   1 
ATOM   3413 C  CB  . ASP A 1 422 ? 10.919  -2.199  24.608  1.00 46.22  ? 422  ASP A CB  1 
ATOM   3414 C  CG  . ASP A 1 422 ? 11.173  -0.745  24.324  1.00 49.50  ? 422  ASP A CG  1 
ATOM   3415 O  OD1 . ASP A 1 422 ? 10.978  -0.321  23.163  1.00 50.75  ? 422  ASP A OD1 1 
ATOM   3416 O  OD2 . ASP A 1 422 ? 11.553  -0.021  25.262  1.00 48.68  ? 422  ASP A OD2 1 
ATOM   3417 N  N   . PHE A 1 423 ? 9.559   -4.775  23.357  1.00 41.17  ? 423  PHE A N   1 
ATOM   3418 C  CA  . PHE A 1 423 ? 9.375   -6.214  23.280  1.00 43.08  ? 423  PHE A CA  1 
ATOM   3419 C  C   . PHE A 1 423 ? 10.645  -6.893  22.803  1.00 47.26  ? 423  PHE A C   1 
ATOM   3420 O  O   . PHE A 1 423 ? 11.377  -6.378  21.954  1.00 45.83  ? 423  PHE A O   1 
ATOM   3421 C  CB  . PHE A 1 423 ? 8.213   -6.595  22.357  1.00 41.18  ? 423  PHE A CB  1 
ATOM   3422 C  CG  . PHE A 1 423 ? 6.891   -6.137  22.865  1.00 40.24  ? 423  PHE A CG  1 
ATOM   3423 C  CD1 . PHE A 1 423 ? 6.143   -6.955  23.699  1.00 43.89  ? 423  PHE A CD1 1 
ATOM   3424 C  CD2 . PHE A 1 423 ? 6.409   -4.876  22.547  1.00 43.05  ? 423  PHE A CD2 1 
ATOM   3425 C  CE1 . PHE A 1 423 ? 4.913   -6.536  24.191  1.00 41.63  ? 423  PHE A CE1 1 
ATOM   3426 C  CE2 . PHE A 1 423 ? 5.185   -4.445  23.037  1.00 39.77  ? 423  PHE A CE2 1 
ATOM   3427 C  CZ  . PHE A 1 423 ? 4.436   -5.279  23.861  1.00 43.30  ? 423  PHE A CZ  1 
ATOM   3428 N  N   . GLU A 1 424 ? 10.872  -8.079  23.351  1.00 41.73  ? 424  GLU A N   1 
ATOM   3429 C  CA  . GLU A 1 424 ? 12.060  -8.875  23.081  1.00 40.71  ? 424  GLU A CA  1 
ATOM   3430 C  C   . GLU A 1 424 ? 11.635  -10.277 22.693  1.00 42.32  ? 424  GLU A C   1 
ATOM   3431 O  O   . GLU A 1 424 ? 10.932  -10.951 23.453  1.00 41.40  ? 424  GLU A O   1 
ATOM   3432 C  CB  . GLU A 1 424 ? 12.986  -8.924  24.300  1.00 42.16  ? 424  GLU A CB  1 
ATOM   3433 C  CG  . GLU A 1 424 ? 14.319  -9.540  23.991  1.00 48.29  ? 424  GLU A CG  1 
ATOM   3434 C  CD  . GLU A 1 424 ? 15.068  -9.959  25.239  1.00 51.76  ? 424  GLU A CD  1 
ATOM   3435 O  OE1 . GLU A 1 424 ? 16.054  -10.707 25.097  1.00 54.43  ? 424  GLU A OE1 1 
ATOM   3436 O  OE2 . GLU A 1 424 ? 14.677  -9.539  26.352  1.00 51.37  ? 424  GLU A OE2 1 
ATOM   3437 N  N   . ASP A 1 425 ? 12.071  -10.717 21.516  1.00 40.25  ? 425  ASP A N   1 
ATOM   3438 C  CA  . ASP A 1 425 ? 11.894  -12.097 21.081  1.00 39.10  ? 425  ASP A CA  1 
ATOM   3439 C  C   . ASP A 1 425 ? 13.046  -12.902 21.681  1.00 43.32  ? 425  ASP A C   1 
ATOM   3440 O  O   . ASP A 1 425 ? 14.001  -13.300 21.010  1.00 44.00  ? 425  ASP A O   1 
ATOM   3441 C  CB  . ASP A 1 425 ? 11.853  -12.146 19.558  1.00 42.21  ? 425  ASP A CB  1 
ATOM   3442 C  CG  . ASP A 1 425 ? 11.871  -13.551 18.988  1.00 42.69  ? 425  ASP A CG  1 
ATOM   3443 O  OD1 . ASP A 1 425 ? 11.435  -14.517 19.651  1.00 43.41  ? 425  ASP A OD1 1 
ATOM   3444 O  OD2 . ASP A 1 425 ? 12.327  -13.682 17.831  1.00 42.03  ? 425  ASP A OD2 1 
ATOM   3445 N  N   . HIS A 1 426 ? 12.949  -13.117 22.998  1.00 46.43  ? 426  HIS A N   1 
ATOM   3446 C  CA  . HIS A 1 426 ? 14.089  -13.614 23.766  1.00 45.14  ? 426  HIS A CA  1 
ATOM   3447 C  C   . HIS A 1 426 ? 14.427  -15.067 23.464  1.00 44.97  ? 426  HIS A C   1 
ATOM   3448 O  O   . HIS A 1 426 ? 15.546  -15.497 23.769  1.00 45.91  ? 426  HIS A O   1 
ATOM   3449 C  CB  . HIS A 1 426 ? 13.829  -13.436 25.268  1.00 41.30  ? 426  HIS A CB  1 
ATOM   3450 C  CG  . HIS A 1 426 ? 12.671  -14.238 25.777  1.00 44.49  ? 426  HIS A CG  1 
ATOM   3451 N  ND1 . HIS A 1 426 ? 11.364  -13.957 25.434  1.00 41.14  ? 426  HIS A ND1 1 
ATOM   3452 C  CD2 . HIS A 1 426 ? 12.623  -15.322 26.590  1.00 47.66  ? 426  HIS A CD2 1 
ATOM   3453 C  CE1 . HIS A 1 426 ? 10.560  -14.830 26.019  1.00 45.39  ? 426  HIS A CE1 1 
ATOM   3454 N  NE2 . HIS A 1 426 ? 11.298  -15.668 26.730  1.00 49.47  ? 426  HIS A NE2 1 
ATOM   3455 N  N   . THR A 1 427 ? 13.503  -15.835 22.887  1.00 39.23  ? 427  THR A N   1 
ATOM   3456 C  CA  . THR A 1 427 ? 13.742  -17.235 22.546  1.00 41.04  ? 427  THR A CA  1 
ATOM   3457 C  C   . THR A 1 427 ? 14.047  -17.464 21.068  1.00 41.32  ? 427  THR A C   1 
ATOM   3458 O  O   . THR A 1 427 ? 14.182  -18.620 20.649  1.00 42.17  ? 427  THR A O   1 
ATOM   3459 C  CB  . THR A 1 427 ? 12.533  -18.090 22.934  1.00 45.06  ? 427  THR A CB  1 
ATOM   3460 O  OG1 . THR A 1 427 ? 11.455  -17.846 22.010  1.00 43.19  ? 427  THR A OG1 1 
ATOM   3461 C  CG2 . THR A 1 427 ? 12.081  -17.759 24.340  1.00 43.67  ? 427  THR A CG2 1 
ATOM   3462 N  N   . ASN A 1 428 ? 14.143  -16.406 20.272  1.00 43.93  ? 428  ASN A N   1 
ATOM   3463 C  CA  . ASN A 1 428 ? 14.202  -16.538 18.821  1.00 46.17  ? 428  ASN A CA  1 
ATOM   3464 C  C   . ASN A 1 428 ? 13.130  -17.519 18.350  1.00 43.34  ? 428  ASN A C   1 
ATOM   3465 O  O   . ASN A 1 428 ? 13.407  -18.582 17.788  1.00 40.20  ? 428  ASN A O   1 
ATOM   3466 C  CB  . ASN A 1 428 ? 15.598  -16.971 18.352  1.00 44.76  ? 428  ASN A CB  1 
ATOM   3467 C  CG  . ASN A 1 428 ? 15.832  -16.650 16.889  1.00 49.87  ? 428  ASN A CG  1 
ATOM   3468 O  OD1 . ASN A 1 428 ? 15.136  -15.807 16.321  1.00 51.39  ? 428  ASN A OD1 1 
ATOM   3469 N  ND2 . ASN A 1 428 ? 16.796  -17.330 16.263  1.00 50.51  ? 428  ASN A ND2 1 
ATOM   3470 N  N   . TYR A 1 429 ? 11.877  -17.142 18.602  1.00 40.68  ? 429  TYR A N   1 
ATOM   3471 C  CA  . TYR A 1 429 ? 10.768  -18.079 18.471  1.00 40.61  ? 429  TYR A CA  1 
ATOM   3472 C  C   . TYR A 1 429 ? 10.600  -18.559 17.034  1.00 39.99  ? 429  TYR A C   1 
ATOM   3473 O  O   . TYR A 1 429 ? 10.645  -17.767 16.090  1.00 43.01  ? 429  TYR A O   1 
ATOM   3474 C  CB  . TYR A 1 429 ? 9.484   -17.406 18.972  1.00 39.55  ? 429  TYR A CB  1 
ATOM   3475 C  CG  . TYR A 1 429 ? 8.214   -18.105 18.552  1.00 43.10  ? 429  TYR A CG  1 
ATOM   3476 C  CD1 . TYR A 1 429 ? 7.833   -19.303 19.135  1.00 39.80  ? 429  TYR A CD1 1 
ATOM   3477 C  CD2 . TYR A 1 429 ? 7.385   -17.556 17.572  1.00 42.14  ? 429  TYR A CD2 1 
ATOM   3478 C  CE1 . TYR A 1 429 ? 6.658   -19.947 18.748  1.00 39.63  ? 429  TYR A CE1 1 
ATOM   3479 C  CE2 . TYR A 1 429 ? 6.221   -18.184 17.187  1.00 37.65  ? 429  TYR A CE2 1 
ATOM   3480 C  CZ  . TYR A 1 429 ? 5.858   -19.371 17.773  1.00 40.68  ? 429  TYR A CZ  1 
ATOM   3481 O  OH  . TYR A 1 429 ? 4.698   -20.014 17.389  1.00 37.08  ? 429  TYR A OH  1 
ATOM   3482 N  N   . GLU A 1 430 ? 10.406  -19.864 16.871  1.00 42.30  ? 430  GLU A N   1 
ATOM   3483 C  CA  . GLU A 1 430 ? 10.126  -20.449 15.566  1.00 44.21  ? 430  GLU A CA  1 
ATOM   3484 C  C   . GLU A 1 430 ? 8.617   -20.541 15.367  1.00 40.83  ? 430  GLU A C   1 
ATOM   3485 O  O   . GLU A 1 430 ? 7.933   -21.251 16.118  1.00 41.66  ? 430  GLU A O   1 
ATOM   3486 C  CB  . GLU A 1 430 ? 10.755  -21.834 15.443  1.00 46.50  ? 430  GLU A CB  1 
ATOM   3487 C  CG  . GLU A 1 430 ? 10.982  -22.284 14.015  1.00 55.69  ? 430  GLU A CG  1 
ATOM   3488 C  CD  . GLU A 1 430 ? 11.767  -23.581 13.936  1.00 67.36  ? 430  GLU A CD  1 
ATOM   3489 O  OE1 . GLU A 1 430 ? 11.204  -24.588 13.457  1.00 74.73  ? 430  GLU A OE1 1 
ATOM   3490 O  OE2 . GLU A 1 430 ? 12.942  -23.599 14.362  1.00 75.30  ? 430  GLU A OE2 1 
ATOM   3491 N  N   . LEU A 1 431 ? 8.102   -19.854 14.343  1.00 40.35  ? 431  LEU A N   1 
ATOM   3492 C  CA  . LEU A 1 431 ? 6.657   -19.818 14.141  1.00 41.21  ? 431  LEU A CA  1 
ATOM   3493 C  C   . LEU A 1 431 ? 6.100   -21.229 14.007  1.00 38.25  ? 431  LEU A C   1 
ATOM   3494 O  O   . LEU A 1 431 ? 6.561   -22.035 13.192  1.00 42.14  ? 431  LEU A O   1 
ATOM   3495 C  CB  . LEU A 1 431 ? 6.299   -18.978 12.909  1.00 40.91  ? 431  LEU A CB  1 
ATOM   3496 C  CG  . LEU A 1 431 ? 4.797   -18.812 12.653  1.00 40.50  ? 431  LEU A CG  1 
ATOM   3497 C  CD1 . LEU A 1 431 ? 4.133   -18.116 13.842  1.00 39.41  ? 431  LEU A CD1 1 
ATOM   3498 C  CD2 . LEU A 1 431 ? 4.579   -18.029 11.363  1.00 43.60  ? 431  LEU A CD2 1 
ATOM   3499 N  N   . ASP A 1 432 ? 5.100   -21.520 14.824  1.00 36.17  ? 432  ASP A N   1 
ATOM   3500 C  CA  . ASP A 1 432 ? 4.414   -22.799 14.858  1.00 35.34  ? 432  ASP A CA  1 
ATOM   3501 C  C   . ASP A 1 432 ? 2.929   -22.477 14.889  1.00 38.48  ? 432  ASP A C   1 
ATOM   3502 O  O   . ASP A 1 432 ? 2.460   -21.860 15.852  1.00 36.92  ? 432  ASP A O   1 
ATOM   3503 C  CB  . ASP A 1 432 ? 4.829   -23.588 16.112  1.00 38.85  ? 432  ASP A CB  1 
ATOM   3504 C  CG  . ASP A 1 432 ? 4.190   -24.955 16.194  1.00 42.52  ? 432  ASP A CG  1 
ATOM   3505 O  OD1 . ASP A 1 432 ? 3.517   -25.367 15.236  1.00 47.45  ? 432  ASP A OD1 1 
ATOM   3506 O  OD2 . ASP A 1 432 ? 4.364   -25.627 17.232  1.00 49.10  ? 432  ASP A OD2 1 
ATOM   3507 N  N   . ILE A 1 433 ? 2.202   -22.862 13.846  1.00 37.16  ? 433  ILE A N   1 
ATOM   3508 C  CA  . ILE A 1 433 ? 0.821   -22.426 13.664  1.00 35.77  ? 433  ILE A CA  1 
ATOM   3509 C  C   . ILE A 1 433 ? -0.097  -23.593 13.987  1.00 33.59  ? 433  ILE A C   1 
ATOM   3510 O  O   . ILE A 1 433 ? -0.139  -24.594 13.263  1.00 36.40  ? 433  ILE A O   1 
ATOM   3511 C  CB  . ILE A 1 433 ? 0.573   -21.876 12.253  1.00 35.93  ? 433  ILE A CB  1 
ATOM   3512 C  CG1 . ILE A 1 433 ? 1.406   -20.603 12.071  1.00 38.02  ? 433  ILE A CG1 1 
ATOM   3513 C  CG2 . ILE A 1 433 ? -0.930  -21.580 12.057  1.00 36.30  ? 433  ILE A CG2 1 
ATOM   3514 C  CD1 . ILE A 1 433 ? 1.462   -20.083 10.640  1.00 36.55  ? 433  ILE A CD1 1 
ATOM   3515 N  N   . LYS A 1 434 ? -0.829  -23.450 15.092  1.00 34.33  ? 434  LYS A N   1 
ATOM   3516 C  CA  . LYS A 1 434 ? -1.832  -24.412 15.513  1.00 36.64  ? 434  LYS A CA  1 
ATOM   3517 C  C   . LYS A 1 434 ? -3.132  -24.191 14.758  1.00 32.75  ? 434  LYS A C   1 
ATOM   3518 O  O   . LYS A 1 434 ? -3.554  -23.051 14.542  1.00 36.31  ? 434  LYS A O   1 
ATOM   3519 C  CB  . LYS A 1 434 ? -2.083  -24.270 17.012  1.00 36.26  ? 434  LYS A CB  1 
ATOM   3520 C  CG  . LYS A 1 434 ? -3.134  -25.215 17.562  1.00 35.85  ? 434  LYS A CG  1 
ATOM   3521 C  CD  . LYS A 1 434 ? -3.224  -25.054 19.080  1.00 42.72  ? 434  LYS A CD  1 
ATOM   3522 C  CE  . LYS A 1 434 ? -4.355  -25.898 19.669  1.00 49.99  ? 434  LYS A CE  1 
ATOM   3523 N  NZ  . LYS A 1 434 ? -4.106  -27.354 19.510  1.00 49.79  ? 434  LYS A NZ  1 
ATOM   3524 N  N   . GLU A 1 435 ? -3.780  -25.287 14.375  1.00 33.54  ? 435  GLU A N   1 
ATOM   3525 C  CA  . GLU A 1 435 ? -5.017  -25.226 13.606  1.00 35.58  ? 435  GLU A CA  1 
ATOM   3526 C  C   . GLU A 1 435 ? -6.180  -25.721 14.454  1.00 35.21  ? 435  GLU A C   1 
ATOM   3527 O  O   . GLU A 1 435 ? -6.097  -26.787 15.074  1.00 34.72  ? 435  GLU A O   1 
ATOM   3528 C  CB  . GLU A 1 435 ? -4.891  -26.035 12.314  1.00 34.06  ? 435  GLU A CB  1 
ATOM   3529 C  CG  . GLU A 1 435 ? -3.773  -25.486 11.438  1.00 33.56  ? 435  GLU A CG  1 
ATOM   3530 C  CD  . GLU A 1 435 ? -3.924  -25.785 9.961   1.00 36.46  ? 435  GLU A CD  1 
ATOM   3531 O  OE1 . GLU A 1 435 ? -5.039  -26.134 9.515   1.00 38.01  ? 435  GLU A OE1 1 
ATOM   3532 O  OE2 . GLU A 1 435 ? -2.894  -25.662 9.251   1.00 35.69  ? 435  GLU A OE2 1 
ATOM   3533 N  N   . THR A 1 436 ? -7.247  -24.926 14.490  1.00 35.95  ? 436  THR A N   1 
ATOM   3534 C  CA  . THR A 1 436 ? -8.517  -25.266 15.123  1.00 35.03  ? 436  THR A CA  1 
ATOM   3535 C  C   . THR A 1 436 ? -9.639  -24.790 14.212  1.00 38.30  ? 436  THR A C   1 
ATOM   3536 O  O   . THR A 1 436 ? -10.569 -24.106 14.641  1.00 34.27  ? 436  THR A O   1 
ATOM   3537 C  CB  . THR A 1 436 ? -8.639  -24.640 16.518  1.00 35.82  ? 436  THR A CB  1 
ATOM   3538 O  OG1 . THR A 1 436 ? -8.449  -23.216 16.429  1.00 36.02  ? 436  THR A OG1 1 
ATOM   3539 C  CG2 . THR A 1 436 ? -7.592  -25.219 17.457  1.00 35.60  ? 436  THR A CG2 1 
ATOM   3540 N  N   . LEU A 1 437 ? -9.554  -25.177 12.932  1.00 33.84  ? 437  LEU A N   1 
ATOM   3541 C  CA  . LEU A 1 437 ? -10.233 -24.523 11.815  1.00 32.48  ? 437  LEU A CA  1 
ATOM   3542 C  C   . LEU A 1 437 ? -9.594  -23.151 11.603  1.00 36.06  ? 437  LEU A C   1 
ATOM   3543 O  O   . LEU A 1 437 ? -9.026  -22.879 10.532  1.00 33.10  ? 437  LEU A O   1 
ATOM   3544 C  CB  . LEU A 1 437 ? -11.757 -24.433 12.033  1.00 32.40  ? 437  LEU A CB  1 
ATOM   3545 C  CG  . LEU A 1 437 ? -12.492 -25.758 12.322  1.00 33.02  ? 437  LEU A CG  1 
ATOM   3546 C  CD1 . LEU A 1 437 ? -14.010 -25.530 12.448  1.00 33.48  ? 437  LEU A CD1 1 
ATOM   3547 C  CD2 . LEU A 1 437 ? -12.196 -26.798 11.256  1.00 34.76  ? 437  LEU A CD2 1 
ATOM   3548 N  N   . THR A 1 438 ? -9.646  -22.301 12.627  1.00 31.99  ? 438  THR A N   1 
ATOM   3549 C  CA  . THR A 1 438 ? -8.902  -21.054 12.650  1.00 32.32  ? 438  THR A CA  1 
ATOM   3550 C  C   . THR A 1 438 ? -7.407  -21.331 12.884  1.00 33.82  ? 438  THR A C   1 
ATOM   3551 O  O   . THR A 1 438 ? -6.996  -22.458 13.180  1.00 33.87  ? 438  THR A O   1 
ATOM   3552 C  CB  . THR A 1 438 ? -9.454  -20.136 13.743  1.00 34.46  ? 438  THR A CB  1 
ATOM   3553 O  OG1 . THR A 1 438 ? -9.426  -20.823 14.997  1.00 33.49  ? 438  THR A OG1 1 
ATOM   3554 C  CG2 . THR A 1 438 ? -10.911 -19.772 13.441  1.00 30.84  ? 438  THR A CG2 1 
ATOM   3555 N  N   . LEU A 1 439 ? -6.598  -20.278 12.744  1.00 31.45  ? 439  LEU A N   1 
ATOM   3556 C  CA  . LEU A 1 439 ? -5.140  -20.338 12.846  1.00 30.75  ? 439  LEU A CA  1 
ATOM   3557 C  C   . LEU A 1 439 ? -4.628  -19.410 13.939  1.00 35.04  ? 439  LEU A C   1 
ATOM   3558 O  O   . LEU A 1 439 ? -5.107  -18.278 14.084  1.00 33.42  ? 439  LEU A O   1 
ATOM   3559 C  CB  . LEU A 1 439 ? -4.496  -19.915 11.521  1.00 33.27  ? 439  LEU A CB  1 
ATOM   3560 C  CG  . LEU A 1 439 ? -4.957  -20.606 10.248  1.00 35.10  ? 439  LEU A CG  1 
ATOM   3561 C  CD1 . LEU A 1 439 ? -4.170  -20.015 9.065   1.00 34.97  ? 439  LEU A CD1 1 
ATOM   3562 C  CD2 . LEU A 1 439 ? -4.780  -22.114 10.327  1.00 35.22  ? 439  LEU A CD2 1 
ATOM   3563 N  N   . LYS A 1 440 ? -3.601  -19.863 14.677  1.00 32.46  ? 440  LYS A N   1 
ATOM   3564 C  CA  . LYS A 1 440 ? -3.023  -19.043 15.734  1.00 33.82  ? 440  LYS A CA  1 
ATOM   3565 C  C   . LYS A 1 440 ? -1.629  -19.560 16.044  1.00 33.59  ? 440  LYS A C   1 
ATOM   3566 O  O   . LYS A 1 440 ? -1.431  -20.782 16.023  1.00 35.29  ? 440  LYS A O   1 
ATOM   3567 C  CB  . LYS A 1 440 ? -3.898  -19.080 16.999  1.00 35.88  ? 440  LYS A CB  1 
ATOM   3568 C  CG  . LYS A 1 440 ? -3.610  -17.976 17.986  1.00 38.56  ? 440  LYS A CG  1 
ATOM   3569 C  CD  . LYS A 1 440 ? -4.366  -18.223 19.305  1.00 37.84  ? 440  LYS A CD  1 
ATOM   3570 C  CE  . LYS A 1 440 ? -5.858  -18.227 19.055  1.00 42.27  ? 440  LYS A CE  1 
ATOM   3571 N  NZ  . LYS A 1 440 ? -6.376  -19.620 18.942  1.00 42.73  ? 440  LYS A NZ  1 
ATOM   3572 N  N   . PRO A 1 441 ? -0.657  -18.691 16.333  1.00 34.90  ? 441  PRO A N   1 
ATOM   3573 C  CA  . PRO A 1 441 ? 0.646   -19.182 16.807  1.00 37.30  ? 441  PRO A CA  1 
ATOM   3574 C  C   . PRO A 1 441 ? 0.473   -19.997 18.078  1.00 39.86  ? 441  PRO A C   1 
ATOM   3575 O  O   . PRO A 1 441 ? -0.436  -19.758 18.877  1.00 34.83  ? 441  PRO A O   1 
ATOM   3576 C  CB  . PRO A 1 441 ? 1.444   -17.901 17.077  1.00 33.54  ? 441  PRO A CB  1 
ATOM   3577 C  CG  . PRO A 1 441 ? 0.770   -16.830 16.271  1.00 36.92  ? 441  PRO A CG  1 
ATOM   3578 C  CD  . PRO A 1 441 ? -0.693  -17.221 16.254  1.00 32.86  ? 441  PRO A CD  1 
ATOM   3579 N  N   . GLU A 1 442 ? 1.350   -20.978 18.253  1.00 35.57  ? 442  GLU A N   1 
ATOM   3580 C  CA  . GLU A 1 442 ? 1.395   -21.782 19.467  1.00 37.15  ? 442  GLU A CA  1 
ATOM   3581 C  C   . GLU A 1 442 ? 2.789   -21.682 20.062  1.00 41.35  ? 442  GLU A C   1 
ATOM   3582 O  O   . GLU A 1 442 ? 3.783   -21.723 19.332  1.00 38.94  ? 442  GLU A O   1 
ATOM   3583 C  CB  . GLU A 1 442 ? 1.048   -23.246 19.191  1.00 42.56  ? 442  GLU A CB  1 
ATOM   3584 C  CG  . GLU A 1 442 ? 1.217   -24.132 20.418  1.00 48.10  ? 442  GLU A CG  1 
ATOM   3585 C  CD  . GLU A 1 442 ? 0.725   -25.553 20.225  1.00 50.22  ? 442  GLU A CD  1 
ATOM   3586 O  OE1 . GLU A 1 442 ? 0.738   -26.065 19.088  1.00 50.60  ? 442  GLU A OE1 1 
ATOM   3587 O  OE2 . GLU A 1 442 ? 0.316   -26.168 21.233  1.00 58.58  ? 442  GLU A OE2 1 
ATOM   3588 N  N   . GLY A 1 443 ? 2.859   -21.552 21.383  1.00 37.96  ? 443  GLY A N   1 
ATOM   3589 C  CA  . GLY A 1 443 ? 4.148   -21.451 22.044  1.00 41.70  ? 443  GLY A CA  1 
ATOM   3590 C  C   . GLY A 1 443 ? 4.899   -20.165 21.812  1.00 38.63  ? 443  GLY A C   1 
ATOM   3591 O  O   . GLY A 1 443 ? 6.100   -20.113 22.092  1.00 42.22  ? 443  GLY A O   1 
ATOM   3592 N  N   . PHE A 1 444 ? 4.249   -19.132 21.278  1.00 39.48  ? 444  PHE A N   1 
ATOM   3593 C  CA  . PHE A 1 444 ? 4.893   -17.844 21.038  1.00 37.79  ? 444  PHE A CA  1 
ATOM   3594 C  C   . PHE A 1 444 ? 4.989   -17.067 22.349  1.00 41.20  ? 444  PHE A C   1 
ATOM   3595 O  O   . PHE A 1 444 ? 3.966   -16.745 22.964  1.00 36.98  ? 444  PHE A O   1 
ATOM   3596 C  CB  . PHE A 1 444 ? 4.099   -17.059 19.985  1.00 37.24  ? 444  PHE A CB  1 
ATOM   3597 C  CG  . PHE A 1 444 ? 4.589   -15.650 19.744  1.00 41.01  ? 444  PHE A CG  1 
ATOM   3598 C  CD1 . PHE A 1 444 ? 5.940   -15.340 19.761  1.00 37.23  ? 444  PHE A CD1 1 
ATOM   3599 C  CD2 . PHE A 1 444 ? 3.687   -14.634 19.462  1.00 36.14  ? 444  PHE A CD2 1 
ATOM   3600 C  CE1 . PHE A 1 444 ? 6.370   -14.037 19.543  1.00 36.95  ? 444  PHE A CE1 1 
ATOM   3601 C  CE2 . PHE A 1 444 ? 4.105   -13.327 19.238  1.00 37.41  ? 444  PHE A CE2 1 
ATOM   3602 C  CZ  . PHE A 1 444 ? 5.459   -13.023 19.274  1.00 37.79  ? 444  PHE A CZ  1 
ATOM   3603 N  N   . VAL A 1 445 ? 6.217   -16.770 22.781  1.00 36.33  ? 445  VAL A N   1 
ATOM   3604 C  CA  . VAL A 1 445 ? 6.480   -16.056 24.023  1.00 37.78  ? 445  VAL A CA  1 
ATOM   3605 C  C   . VAL A 1 445 ? 7.405   -14.888 23.723  1.00 36.82  ? 445  VAL A C   1 
ATOM   3606 O  O   . VAL A 1 445 ? 8.213   -14.941 22.790  1.00 39.46  ? 445  VAL A O   1 
ATOM   3607 C  CB  . VAL A 1 445 ? 7.100   -16.976 25.099  1.00 39.42  ? 445  VAL A CB  1 
ATOM   3608 C  CG1 . VAL A 1 445 ? 6.098   -18.041 25.521  1.00 38.15  ? 445  VAL A CG1 1 
ATOM   3609 C  CG2 . VAL A 1 445 ? 8.388   -17.614 24.579  1.00 40.98  ? 445  VAL A CG2 1 
ATOM   3610 N  N   . VAL A 1 446 ? 7.283   -13.826 24.519  1.00 36.11  ? 446  VAL A N   1 
ATOM   3611 C  CA  . VAL A 1 446 ? 8.156   -12.658 24.433  1.00 41.22  ? 446  VAL A CA  1 
ATOM   3612 C  C   . VAL A 1 446 ? 8.388   -12.121 25.840  1.00 40.57  ? 446  VAL A C   1 
ATOM   3613 O  O   . VAL A 1 446 ? 7.691   -12.477 26.794  1.00 40.03  ? 446  VAL A O   1 
ATOM   3614 C  CB  . VAL A 1 446 ? 7.575   -11.542 23.536  1.00 40.60  ? 446  VAL A CB  1 
ATOM   3615 C  CG1 . VAL A 1 446 ? 7.331   -12.064 22.116  1.00 38.62  ? 446  VAL A CG1 1 
ATOM   3616 C  CG2 . VAL A 1 446 ? 6.295   -10.970 24.145  1.00 40.52  ? 446  VAL A CG2 1 
ATOM   3617 N  N   . LYS A 1 447 ? 9.383   -11.246 25.961  1.00 39.40  ? 447  LYS A N   1 
ATOM   3618 C  CA  . LYS A 1 447 ? 9.555   -10.428 27.147  1.00 38.06  ? 447  LYS A CA  1 
ATOM   3619 C  C   . LYS A 1 447 ? 9.201   -8.988  26.817  1.00 43.58  ? 447  LYS A C   1 
ATOM   3620 O  O   . LYS A 1 447 ? 9.511   -8.495  25.729  1.00 45.20  ? 447  LYS A O   1 
ATOM   3621 C  CB  . LYS A 1 447 ? 10.987  -10.492 27.680  1.00 43.46  ? 447  LYS A CB  1 
ATOM   3622 C  CG  . LYS A 1 447 ? 11.294  -11.748 28.455  1.00 42.95  ? 447  LYS A CG  1 
ATOM   3623 C  CD  . LYS A 1 447 ? 12.782  -11.806 28.784  1.00 50.67  ? 447  LYS A CD  1 
ATOM   3624 C  CE  . LYS A 1 447 ? 13.028  -12.625 30.028  1.00 57.61  ? 447  LYS A CE  1 
ATOM   3625 N  NZ  . LYS A 1 447 ? 13.286  -14.049 29.673  1.00 59.67  ? 447  LYS A NZ  1 
ATOM   3626 N  N   . ALA A 1 448 ? 8.540   -8.322  27.750  1.00 39.80  ? 448  ALA A N   1 
ATOM   3627 C  CA  . ALA A 1 448 ? 8.227   -6.912  27.616  1.00 42.14  ? 448  ALA A CA  1 
ATOM   3628 C  C   . ALA A 1 448 ? 9.040   -6.130  28.634  1.00 50.98  ? 448  ALA A C   1 
ATOM   3629 O  O   . ALA A 1 448 ? 9.163   -6.543  29.793  1.00 54.23  ? 448  ALA A O   1 
ATOM   3630 C  CB  . ALA A 1 448 ? 6.727   -6.650  27.813  1.00 41.28  ? 448  ALA A CB  1 
ATOM   3631 N  N   . LYS A 1 449 ? 9.623   -5.020  28.193  1.00 46.37  ? 449  LYS A N   1 
ATOM   3632 C  CA  . LYS A 1 449 ? 10.281  -4.081  29.089  1.00 46.67  ? 449  LYS A CA  1 
ATOM   3633 C  C   . LYS A 1 449 ? 9.438   -2.819  29.169  1.00 43.70  ? 449  LYS A C   1 
ATOM   3634 O  O   . LYS A 1 449 ? 9.282   -2.109  28.171  1.00 44.71  ? 449  LYS A O   1 
ATOM   3635 C  CB  . LYS A 1 449 ? 11.701  -3.748  28.624  1.00 51.08  ? 449  LYS A CB  1 
ATOM   3636 C  CG  . LYS A 1 449 ? 12.681  -3.608  29.786  1.00 59.41  ? 449  LYS A CG  1 
ATOM   3637 C  CD  . LYS A 1 449 ? 13.736  -2.541  29.515  1.00 62.68  ? 449  LYS A CD  1 
ATOM   3638 C  CE  . LYS A 1 449 ? 15.096  -3.162  29.217  1.00 74.27  ? 449  LYS A CE  1 
ATOM   3639 N  NZ  . LYS A 1 449 ? 16.104  -2.150  28.778  1.00 74.52  ? 449  LYS A NZ  1 
ATOM   3640 N  N   . SER A 1 450 ? 8.907   -2.539  30.356  1.00 42.74  ? 450  SER A N   1 
ATOM   3641 C  CA  . SER A 1 450 ? 8.025   -1.398  30.533  1.00 44.18  ? 450  SER A CA  1 
ATOM   3642 C  C   . SER A 1 450 ? 8.736   -0.088  30.213  1.00 44.05  ? 450  SER A C   1 
ATOM   3643 O  O   . SER A 1 450 ? 9.884   0.129   30.604  1.00 48.36  ? 450  SER A O   1 
ATOM   3644 C  CB  . SER A 1 450 ? 7.490   -1.371  31.962  1.00 42.73  ? 450  SER A CB  1 
ATOM   3645 O  OG  . SER A 1 450 ? 6.714   -0.213  32.183  1.00 45.68  ? 450  SER A OG  1 
ATOM   3646 N  N   . LYS A 1 451 ? 8.041   0.789   29.485  1.00 43.69  ? 451  LYS A N   1 
ATOM   3647 C  CA  . LYS A 1 451 ? 8.479   2.167   29.315  1.00 47.40  ? 451  LYS A CA  1 
ATOM   3648 C  C   . LYS A 1 451 ? 8.085   3.046   30.493  1.00 50.12  ? 451  LYS A C   1 
ATOM   3649 O  O   . LYS A 1 451 ? 8.362   4.249   30.468  1.00 52.90  ? 451  LYS A O   1 
ATOM   3650 C  CB  . LYS A 1 451 ? 7.915   2.753   28.012  1.00 45.09  ? 451  LYS A CB  1 
ATOM   3651 C  CG  . LYS A 1 451 ? 8.448   2.072   26.760  1.00 46.05  ? 451  LYS A CG  1 
ATOM   3652 C  CD  . LYS A 1 451 ? 7.924   2.755   25.494  1.00 47.95  ? 451  LYS A CD  1 
ATOM   3653 C  CE  . LYS A 1 451 ? 8.481   2.107   24.241  1.00 48.64  ? 451  LYS A CE  1 
ATOM   3654 N  NZ  . LYS A 1 451 ? 9.908   2.475   23.991  1.00 53.94  ? 451  LYS A NZ  1 
ATOM   3655 N  N   . LYS A 1 452 ? 7.436   2.471   31.512  1.00 44.88  ? 452  LYS A N   1 
ATOM   3656 C  CA  . LYS A 1 452 ? 7.089   3.167   32.747  1.00 45.84  ? 452  LYS A CA  1 
ATOM   3657 C  C   . LYS A 1 452 ? 6.241   4.410   32.485  1.00 52.66  ? 452  LYS A C   1 
ATOM   3658 O  O   . LYS A 1 452 ? 6.456   5.473   33.072  1.00 48.68  ? 452  LYS A O   1 
ATOM   3659 C  CB  . LYS A 1 452 ? 8.348   3.518   33.543  1.00 51.44  ? 452  LYS A CB  1 
ATOM   3660 C  CG  . LYS A 1 452 ? 8.923   2.344   34.326  1.00 56.13  ? 452  LYS A CG  1 
ATOM   3661 C  CD  . LYS A 1 452 ? 10.437  2.468   34.480  1.00 62.85  ? 452  LYS A CD  1 
ATOM   3662 C  CE  . LYS A 1 452 ? 10.920  1.942   35.824  1.00 67.57  ? 452  LYS A CE  1 
ATOM   3663 N  NZ  . LYS A 1 452 ? 11.328  3.055   36.732  1.00 72.70  ? 452  LYS A NZ  1 
ATOM   3664 N  N   . ILE A 1 453 ? 5.245   4.270   31.621  1.00 43.44  ? 453  ILE A N   1 
ATOM   3665 C  CA  . ILE A 1 453 ? 4.322   5.358   31.314  1.00 43.76  ? 453  ILE A CA  1 
ATOM   3666 C  C   . ILE A 1 453 ? 3.012   5.095   32.049  1.00 50.33  ? 453  ILE A C   1 
ATOM   3667 O  O   . ILE A 1 453 ? 2.371   4.064   31.798  1.00 47.40  ? 453  ILE A O   1 
ATOM   3668 C  CB  . ILE A 1 453 ? 4.095   5.504   29.805  1.00 46.40  ? 453  ILE A CB  1 
ATOM   3669 C  CG1 . ILE A 1 453 ? 5.434   5.804   29.119  1.00 46.55  ? 453  ILE A CG1 1 
ATOM   3670 C  CG2 . ILE A 1 453 ? 3.066   6.585   29.555  1.00 42.17  ? 453  ILE A CG2 1 
ATOM   3671 C  CD1 . ILE A 1 453 ? 5.385   5.796   27.624  1.00 43.95  ? 453  ILE A CD1 1 
ATOM   3672 N  N   . PRO A 1 454 ? 2.582   5.983   32.942  1.00 52.48  ? 454  PRO A N   1 
ATOM   3673 C  CA  . PRO A 1 454 ? 1.408   5.692   33.772  1.00 53.39  ? 454  PRO A CA  1 
ATOM   3674 C  C   . PRO A 1 454 ? 0.124   5.615   32.962  1.00 52.87  ? 454  PRO A C   1 
ATOM   3675 O  O   . PRO A 1 454 ? -0.017  6.231   31.900  1.00 49.52  ? 454  PRO A O   1 
ATOM   3676 C  CB  . PRO A 1 454 ? 1.363   6.869   34.758  1.00 53.26  ? 454  PRO A CB  1 
ATOM   3677 C  CG  . PRO A 1 454 ? 2.726   7.503   34.691  1.00 54.93  ? 454  PRO A CG  1 
ATOM   3678 C  CD  . PRO A 1 454 ? 3.237   7.250   33.311  1.00 50.74  ? 454  PRO A CD  1 
ATOM   3679 N  N   . LEU A 1 455 ? -0.823  4.849   33.501  1.00 52.24  ? 455  LEU A N   1 
ATOM   3680 C  CA  . LEU A 1 455 ? -2.168  4.728   32.952  1.00 49.43  ? 455  LEU A CA  1 
ATOM   3681 C  C   . LEU A 1 455 ? -3.130  5.675   33.674  1.00 55.99  ? 455  LEU A C   1 
ATOM   3682 O  O   . LEU A 1 455 ? -2.720  6.426   34.568  1.00 59.72  ? 455  LEU A O   1 
ATOM   3683 C  CB  . LEU A 1 455 ? -2.655  3.281   33.073  1.00 50.46  ? 455  LEU A CB  1 
ATOM   3684 C  CG  . LEU A 1 455 ? -1.958  2.255   32.178  1.00 47.35  ? 455  LEU A CG  1 
ATOM   3685 C  CD1 . LEU A 1 455 ? -2.178  0.839   32.712  1.00 46.53  ? 455  LEU A CD1 1 
ATOM   3686 C  CD2 . LEU A 1 455 ? -2.476  2.374   30.751  1.00 45.81  ? 455  LEU A CD2 1 
ATOM   3687 O  OXT . LEU A 1 455 ? -4.335  5.714   33.397  1.00 52.58  ? 455  LEU A OXT 1 
ATOM   3688 N  N   . THR B 1 1   ? -1.681  -25.288 99.984  1.00 76.85  ? 1    THR B N   1 
ATOM   3689 C  CA  . THR B 1 1   ? -0.770  -24.399 99.264  1.00 78.43  ? 1    THR B CA  1 
ATOM   3690 C  C   . THR B 1 1   ? -0.412  -24.960 97.892  1.00 68.18  ? 1    THR B C   1 
ATOM   3691 O  O   . THR B 1 1   ? -0.906  -24.480 96.868  1.00 66.45  ? 1    THR B O   1 
ATOM   3692 C  CB  . THR B 1 1   ? 0.528   -24.152 100.061 1.00 81.80  ? 1    THR B CB  1 
ATOM   3693 O  OG1 . THR B 1 1   ? 0.229   -24.110 101.464 1.00 84.10  ? 1    THR B OG1 1 
ATOM   3694 C  CG2 . THR B 1 1   ? 1.188   -22.840 99.630  1.00 74.69  ? 1    THR B CG2 1 
ATOM   3695 N  N   . ILE B 1 2   ? 0.454   -25.973 97.882  1.00 68.52  ? 2    ILE B N   1 
ATOM   3696 C  CA  . ILE B 1 2   ? 0.811   -26.663 96.646  1.00 66.87  ? 2    ILE B CA  1 
ATOM   3697 C  C   . ILE B 1 2   ? -0.388  -27.482 96.178  1.00 68.19  ? 2    ILE B C   1 
ATOM   3698 O  O   . ILE B 1 2   ? -0.852  -28.391 96.880  1.00 68.69  ? 2    ILE B O   1 
ATOM   3699 C  CB  . ILE B 1 2   ? 2.042   -27.553 96.852  1.00 65.44  ? 2    ILE B CB  1 
ATOM   3700 C  CG1 . ILE B 1 2   ? 3.222   -26.730 97.383  1.00 67.32  ? 2    ILE B CG1 1 
ATOM   3701 C  CG2 . ILE B 1 2   ? 2.399   -28.280 95.556  1.00 61.84  ? 2    ILE B CG2 1 
ATOM   3702 C  CD1 . ILE B 1 2   ? 3.597   -25.540 96.524  1.00 64.47  ? 2    ILE B CD1 1 
ATOM   3703 N  N   . LYS B 1 3   ? -0.897  -27.159 94.992  1.00 63.86  ? 3    LYS B N   1 
ATOM   3704 C  CA  . LYS B 1 3   ? -2.052  -27.826 94.409  1.00 60.92  ? 3    LYS B CA  1 
ATOM   3705 C  C   . LYS B 1 3   ? -1.597  -28.844 93.373  1.00 60.07  ? 3    LYS B C   1 
ATOM   3706 O  O   . LYS B 1 3   ? -0.550  -28.685 92.737  1.00 59.45  ? 3    LYS B O   1 
ATOM   3707 C  CB  . LYS B 1 3   ? -2.995  -26.814 93.750  1.00 61.06  ? 3    LYS B CB  1 
ATOM   3708 C  CG  . LYS B 1 3   ? -3.313  -25.614 94.620  1.00 62.22  ? 3    LYS B CG  1 
ATOM   3709 C  CD  . LYS B 1 3   ? -4.798  -25.317 94.656  1.00 66.33  ? 3    LYS B CD  1 
ATOM   3710 C  CE  . LYS B 1 3   ? -5.349  -25.057 93.270  1.00 64.85  ? 3    LYS B CE  1 
ATOM   3711 N  NZ  . LYS B 1 3   ? -6.779  -24.646 93.357  1.00 68.07  ? 3    LYS B NZ  1 
ATOM   3712 N  N   . GLU B 1 4   ? -2.397  -29.891 93.201  1.00 57.34  ? 4    GLU B N   1 
ATOM   3713 C  CA  . GLU B 1 4   ? -2.164  -30.865 92.148  1.00 57.42  ? 4    GLU B CA  1 
ATOM   3714 C  C   . GLU B 1 4   ? -3.008  -30.498 90.935  1.00 51.52  ? 4    GLU B C   1 
ATOM   3715 O  O   . GLU B 1 4   ? -4.212  -30.257 91.049  1.00 51.63  ? 4    GLU B O   1 
ATOM   3716 C  CB  . GLU B 1 4   ? -2.483  -32.288 92.597  1.00 57.52  ? 4    GLU B CB  1 
ATOM   3717 C  CG  . GLU B 1 4   ? -2.270  -33.305 91.480  1.00 63.29  ? 4    GLU B CG  1 
ATOM   3718 C  CD  . GLU B 1 4   ? -2.754  -34.690 91.850  1.00 73.24  ? 4    GLU B CD  1 
ATOM   3719 O  OE1 . GLU B 1 4   ? -2.757  -35.573 90.965  1.00 74.63  ? 4    GLU B OE1 1 
ATOM   3720 O  OE2 . GLU B 1 4   ? -3.141  -34.890 93.023  1.00 76.23  ? 4    GLU B OE2 1 
ATOM   3721 N  N   . MET B 1 5   ? -2.391  -30.480 89.816  1.00 52.41  ? 5    MET B N   1 
ATOM   3722 C  CA  . MET B 1 5   ? -2.896  -29.970 88.561  1.00 48.19  ? 5    MET B CA  1 
ATOM   3723 C  C   . MET B 1 5   ? -3.782  -31.019 87.885  1.00 41.35  ? 5    MET B C   1 
ATOM   3724 O  O   . MET B 1 5   ? -3.421  -32.196 87.832  1.00 43.76  ? 5    MET B O   1 
ATOM   3725 C  CB  . MET B 1 5   ? -1.698  -29.624 87.692  1.00 51.93  ? 5    MET B CB  1 
ATOM   3726 C  CG  . MET B 1 5   ? -1.928  -28.914 86.446  1.00 46.84  ? 5    MET B CG  1 
ATOM   3727 S  SD  . MET B 1 5   ? -0.297  -28.900 85.687  1.00 41.76  ? 5    MET B SD  1 
ATOM   3728 C  CE  . MET B 1 5   ? 0.624   -27.850 86.836  1.00 43.72  ? 5    MET B CE  1 
ATOM   3729 N  N   . PRO B 1 6   ? -4.955  -30.644 87.381  1.00 38.48  ? 6    PRO B N   1 
ATOM   3730 C  CA  . PRO B 1 6   ? -5.789  -31.631 86.680  1.00 38.08  ? 6    PRO B CA  1 
ATOM   3731 C  C   . PRO B 1 6   ? -5.163  -32.058 85.357  1.00 40.55  ? 6    PRO B C   1 
ATOM   3732 O  O   . PRO B 1 6   ? -4.260  -31.412 84.822  1.00 37.55  ? 6    PRO B O   1 
ATOM   3733 C  CB  . PRO B 1 6   ? -7.110  -30.891 86.448  1.00 41.33  ? 6    PRO B CB  1 
ATOM   3734 C  CG  . PRO B 1 6   ? -6.743  -29.460 86.486  1.00 39.83  ? 6    PRO B CG  1 
ATOM   3735 C  CD  . PRO B 1 6   ? -5.626  -29.335 87.489  1.00 40.79  ? 6    PRO B CD  1 
ATOM   3736 N  N   . GLN B 1 7   ? -5.668  -33.173 84.830  1.00 39.89  ? 7    GLN B N   1 
ATOM   3737 C  CA  . GLN B 1 7   ? -5.162  -33.756 83.592  1.00 36.30  ? 7    GLN B CA  1 
ATOM   3738 C  C   . GLN B 1 7   ? -6.328  -34.345 82.812  1.00 39.83  ? 7    GLN B C   1 
ATOM   3739 O  O   . GLN B 1 7   ? -7.212  -34.982 83.411  1.00 38.16  ? 7    GLN B O   1 
ATOM   3740 C  CB  . GLN B 1 7   ? -4.116  -34.843 83.877  1.00 38.92  ? 7    GLN B CB  1 
ATOM   3741 C  CG  . GLN B 1 7   ? -3.426  -35.412 82.645  1.00 38.15  ? 7    GLN B CG  1 
ATOM   3742 C  CD  . GLN B 1 7   ? -2.375  -36.452 83.010  1.00 42.96  ? 7    GLN B CD  1 
ATOM   3743 O  OE1 . GLN B 1 7   ? -2.285  -36.881 84.164  1.00 46.64  ? 7    GLN B OE1 1 
ATOM   3744 N  NE2 . GLN B 1 7   ? -1.568  -36.853 82.028  1.00 40.34  ? 7    GLN B NE2 1 
ATOM   3745 N  N   . PRO B 1 8   ? -6.376  -34.144 81.489  1.00 36.11  ? 8    PRO B N   1 
ATOM   3746 C  CA  . PRO B 1 8   ? -7.455  -34.748 80.697  1.00 33.50  ? 8    PRO B CA  1 
ATOM   3747 C  C   . PRO B 1 8   ? -7.257  -36.245 80.532  1.00 35.19  ? 8    PRO B C   1 
ATOM   3748 O  O   . PRO B 1 8   ? -6.252  -36.796 80.987  1.00 35.70  ? 8    PRO B O   1 
ATOM   3749 C  CB  . PRO B 1 8   ? -7.365  -34.014 79.353  1.00 33.87  ? 8    PRO B CB  1 
ATOM   3750 C  CG  . PRO B 1 8   ? -5.912  -33.609 79.243  1.00 35.28  ? 8    PRO B CG  1 
ATOM   3751 C  CD  . PRO B 1 8   ? -5.493  -33.285 80.668  1.00 33.97  ? 8    PRO B CD  1 
ATOM   3752 N  N   . LYS B 1 9   ? -8.194  -36.904 79.859  1.00 34.19  ? 9    LYS B N   1 
ATOM   3753 C  CA  . LYS B 1 9   ? -8.237  -38.362 79.825  1.00 33.07  ? 9    LYS B CA  1 
ATOM   3754 C  C   . LYS B 1 9   ? -7.018  -38.951 79.113  1.00 35.83  ? 9    LYS B C   1 
ATOM   3755 O  O   . LYS B 1 9   ? -6.459  -38.357 78.184  1.00 36.59  ? 9    LYS B O   1 
ATOM   3756 C  CB  . LYS B 1 9   ? -9.529  -38.824 79.144  1.00 33.63  ? 9    LYS B CB  1 
ATOM   3757 C  CG  . LYS B 1 9   ? -9.656  -38.401 77.672  1.00 31.89  ? 9    LYS B CG  1 
ATOM   3758 C  CD  . LYS B 1 9   ? -11.047 -38.721 77.141  1.00 36.66  ? 9    LYS B CD  1 
ATOM   3759 C  CE  . LYS B 1 9   ? -11.237 -38.226 75.707  1.00 40.88  ? 9    LYS B CE  1 
ATOM   3760 N  NZ  . LYS B 1 9   ? -12.630 -38.481 75.195  1.00 45.35  ? 9    LYS B NZ  1 
ATOM   3761 N  N   . THR B 1 10  ? -6.632  -40.154 79.537  1.00 35.71  ? 10   THR B N   1 
ATOM   3762 C  CA  . THR B 1 10  ? -5.431  -40.829 79.065  1.00 34.42  ? 10   THR B CA  1 
ATOM   3763 C  C   . THR B 1 10  ? -5.771  -42.091 78.283  1.00 36.91  ? 10   THR B C   1 
ATOM   3764 O  O   . THR B 1 10  ? -6.871  -42.656 78.396  1.00 35.24  ? 10   THR B O   1 
ATOM   3765 C  CB  . THR B 1 10  ? -4.518  -41.192 80.237  1.00 36.68  ? 10   THR B CB  1 
ATOM   3766 O  OG1 . THR B 1 10  ? -5.246  -42.005 81.174  1.00 35.90  ? 10   THR B OG1 1 
ATOM   3767 C  CG2 . THR B 1 10  ? -4.042  -39.921 80.935  1.00 37.41  ? 10   THR B CG2 1 
ATOM   3768 N  N   . PHE B 1 11  ? -4.779  -42.531 77.505  1.00 33.46  ? 11   PHE B N   1 
ATOM   3769 C  CA  . PHE B 1 11  ? -4.879  -43.647 76.577  1.00 36.31  ? 11   PHE B CA  1 
ATOM   3770 C  C   . PHE B 1 11  ? -3.723  -44.623 76.839  1.00 38.86  ? 11   PHE B C   1 
ATOM   3771 O  O   . PHE B 1 11  ? -2.910  -44.912 75.963  1.00 38.08  ? 11   PHE B O   1 
ATOM   3772 C  CB  . PHE B 1 11  ? -4.833  -43.152 75.129  1.00 35.30  ? 11   PHE B CB  1 
ATOM   3773 C  CG  . PHE B 1 11  ? -5.985  -42.259 74.748  1.00 35.50  ? 11   PHE B CG  1 
ATOM   3774 C  CD1 . PHE B 1 11  ? -6.042  -40.943 75.188  1.00 35.97  ? 11   PHE B CD1 1 
ATOM   3775 C  CD2 . PHE B 1 11  ? -7.002  -42.732 73.923  1.00 34.68  ? 11   PHE B CD2 1 
ATOM   3776 C  CE1 . PHE B 1 11  ? -7.099  -40.111 74.837  1.00 35.16  ? 11   PHE B CE1 1 
ATOM   3777 C  CE2 . PHE B 1 11  ? -8.050  -41.895 73.553  1.00 36.85  ? 11   PHE B CE2 1 
ATOM   3778 C  CZ  . PHE B 1 11  ? -8.104  -40.590 74.010  1.00 35.08  ? 11   PHE B CZ  1 
ATOM   3779 N  N   . GLY B 1 12  ? -3.643  -45.125 78.070  1.00 37.45  ? 12   GLY B N   1 
ATOM   3780 C  CA  . GLY B 1 12  ? -2.578  -46.061 78.393  1.00 39.75  ? 12   GLY B CA  1 
ATOM   3781 C  C   . GLY B 1 12  ? -1.213  -45.424 78.209  1.00 39.74  ? 12   GLY B C   1 
ATOM   3782 O  O   . GLY B 1 12  ? -0.980  -44.267 78.577  1.00 36.43  ? 12   GLY B O   1 
ATOM   3783 N  N   . GLU B 1 13  ? -0.299  -46.181 77.600  1.00 41.20  ? 13   GLU B N   1 
ATOM   3784 C  CA  . GLU B 1 13  ? 1.071   -45.698 77.459  1.00 41.65  ? 13   GLU B CA  1 
ATOM   3785 C  C   . GLU B 1 13  ? 1.191   -44.534 76.478  1.00 40.97  ? 13   GLU B C   1 
ATOM   3786 O  O   . GLU B 1 13  ? 2.224   -43.856 76.475  1.00 42.65  ? 13   GLU B O   1 
ATOM   3787 C  CB  . GLU B 1 13  ? 1.995   -46.851 77.053  1.00 46.93  ? 13   GLU B CB  1 
ATOM   3788 C  CG  . GLU B 1 13  ? 2.118   -47.947 78.121  1.00 51.00  ? 13   GLU B CG  1 
ATOM   3789 C  CD  . GLU B 1 13  ? 2.963   -47.537 79.329  1.00 61.95  ? 13   GLU B CD  1 
ATOM   3790 O  OE1 . GLU B 1 13  ? 3.450   -46.381 79.384  1.00 64.92  ? 13   GLU B OE1 1 
ATOM   3791 O  OE2 . GLU B 1 13  ? 3.133   -48.379 80.238  1.00 68.88  ? 13   GLU B OE2 1 
ATOM   3792 N  N   . LEU B 1 14  ? 0.166   -44.268 75.658  1.00 38.61  ? 14   LEU B N   1 
ATOM   3793 C  CA  . LEU B 1 14  ? 0.182   -43.049 74.849  1.00 37.95  ? 14   LEU B CA  1 
ATOM   3794 C  C   . LEU B 1 14  ? -0.197  -41.808 75.653  1.00 39.43  ? 14   LEU B C   1 
ATOM   3795 O  O   . LEU B 1 14  ? -0.090  -40.689 75.131  1.00 40.88  ? 14   LEU B O   1 
ATOM   3796 C  CB  . LEU B 1 14  ? -0.747  -43.197 73.642  1.00 37.44  ? 14   LEU B CB  1 
ATOM   3797 C  CG  . LEU B 1 14  ? -0.406  -44.371 72.713  1.00 41.46  ? 14   LEU B CG  1 
ATOM   3798 C  CD1 . LEU B 1 14  ? -1.437  -44.528 71.621  1.00 41.77  ? 14   LEU B CD1 1 
ATOM   3799 C  CD2 . LEU B 1 14  ? 0.985   -44.176 72.134  1.00 45.10  ? 14   LEU B CD2 1 
ATOM   3800 N  N   . LYS B 1 15  ? -0.617  -41.980 76.900  1.00 37.43  ? 15   LYS B N   1 
ATOM   3801 C  CA  . LYS B 1 15  ? -0.910  -40.878 77.827  1.00 36.25  ? 15   LYS B CA  1 
ATOM   3802 C  C   . LYS B 1 15  ? -1.947  -39.978 77.158  1.00 37.06  ? 15   LYS B C   1 
ATOM   3803 O  O   . LYS B 1 15  ? -3.017  -40.480 76.765  1.00 36.29  ? 15   LYS B O   1 
ATOM   3804 C  CB  . LYS B 1 15  ? 0.404   -40.221 78.233  1.00 39.81  ? 15   LYS B CB  1 
ATOM   3805 C  CG  . LYS B 1 15  ? 1.292   -41.182 79.041  1.00 43.93  ? 15   LYS B CG  1 
ATOM   3806 C  CD  . LYS B 1 15  ? 2.636   -40.586 79.360  1.00 48.89  ? 15   LYS B CD  1 
ATOM   3807 C  CE  . LYS B 1 15  ? 3.459   -41.540 80.206  1.00 52.91  ? 15   LYS B CE  1 
ATOM   3808 N  NZ  . LYS B 1 15  ? 4.725   -40.886 80.617  1.00 56.81  ? 15   LYS B NZ  1 
ATOM   3809 N  N   . ASN B 1 16  ? -1.708  -38.672 77.019  1.00 36.04  ? 16   ASN B N   1 
ATOM   3810 C  CA  . ASN B 1 16  ? -2.717  -37.795 76.420  1.00 36.37  ? 16   ASN B CA  1 
ATOM   3811 C  C   . ASN B 1 16  ? -2.569  -37.633 74.908  1.00 38.73  ? 16   ASN B C   1 
ATOM   3812 O  O   . ASN B 1 16  ? -3.375  -36.920 74.304  1.00 35.75  ? 16   ASN B O   1 
ATOM   3813 C  CB  . ASN B 1 16  ? -2.684  -36.396 77.054  1.00 33.12  ? 16   ASN B CB  1 
ATOM   3814 C  CG  . ASN B 1 16  ? -2.996  -36.394 78.538  1.00 35.58  ? 16   ASN B CG  1 
ATOM   3815 O  OD1 . ASN B 1 16  ? -2.193  -35.934 79.331  1.00 35.51  ? 16   ASN B OD1 1 
ATOM   3816 N  ND2 . ASN B 1 16  ? -4.171  -36.910 78.921  1.00 36.57  ? 16   ASN B ND2 1 
ATOM   3817 N  N   . LEU B 1 17  ? -1.563  -38.247 74.280  1.00 35.23  ? 17   LEU B N   1 
ATOM   3818 C  CA  . LEU B 1 17  ? -1.274  -37.920 72.883  1.00 38.55  ? 17   LEU B CA  1 
ATOM   3819 C  C   . LEU B 1 17  ? -2.469  -38.096 71.954  1.00 34.28  ? 17   LEU B C   1 
ATOM   3820 O  O   . LEU B 1 17  ? -2.654  -37.247 71.065  1.00 36.15  ? 17   LEU B O   1 
ATOM   3821 C  CB  . LEU B 1 17  ? -0.084  -38.753 72.384  1.00 37.66  ? 17   LEU B CB  1 
ATOM   3822 C  CG  . LEU B 1 17  ? 0.519   -38.292 71.041  1.00 37.28  ? 17   LEU B CG  1 
ATOM   3823 C  CD1 . LEU B 1 17  ? 1.093   -36.881 71.125  1.00 39.95  ? 17   LEU B CD1 1 
ATOM   3824 C  CD2 . LEU B 1 17  ? 1.581   -39.280 70.567  1.00 42.66  ? 17   LEU B CD2 1 
ATOM   3825 N  N   . PRO B 1 18  ? -3.291  -39.139 72.068  1.00 36.99  ? 18   PRO B N   1 
ATOM   3826 C  CA  . PRO B 1 18  ? -4.399  -39.289 71.109  1.00 36.14  ? 18   PRO B CA  1 
ATOM   3827 C  C   . PRO B 1 18  ? -5.431  -38.156 71.165  1.00 32.63  ? 18   PRO B C   1 
ATOM   3828 O  O   . PRO B 1 18  ? -6.237  -38.048 70.238  1.00 34.40  ? 18   PRO B O   1 
ATOM   3829 C  CB  . PRO B 1 18  ? -5.010  -40.649 71.487  1.00 36.29  ? 18   PRO B CB  1 
ATOM   3830 C  CG  . PRO B 1 18  ? -3.835  -41.402 72.116  1.00 37.07  ? 18   PRO B CG  1 
ATOM   3831 C  CD  . PRO B 1 18  ? -3.136  -40.332 72.920  1.00 37.07  ? 18   PRO B CD  1 
ATOM   3832 N  N   . LEU B 1 19  ? -5.434  -37.317 72.203  1.00 34.87  ? 19   LEU B N   1 
ATOM   3833 C  CA  . LEU B 1 19  ? -6.292  -36.131 72.192  1.00 35.96  ? 19   LEU B CA  1 
ATOM   3834 C  C   . LEU B 1 19  ? -5.933  -35.179 71.062  1.00 35.29  ? 19   LEU B C   1 
ATOM   3835 O  O   . LEU B 1 19  ? -6.772  -34.364 70.661  1.00 36.48  ? 19   LEU B O   1 
ATOM   3836 C  CB  . LEU B 1 19  ? -6.210  -35.398 73.530  1.00 33.25  ? 19   LEU B CB  1 
ATOM   3837 C  CG  . LEU B 1 19  ? -6.725  -36.206 74.716  1.00 31.76  ? 19   LEU B CG  1 
ATOM   3838 C  CD1 . LEU B 1 19  ? -6.537  -35.431 75.976  1.00 33.59  ? 19   LEU B CD1 1 
ATOM   3839 C  CD2 . LEU B 1 19  ? -8.193  -36.557 74.529  1.00 36.09  ? 19   LEU B CD2 1 
ATOM   3840 N  N   . LEU B 1 20  ? -4.718  -35.276 70.526  1.00 34.71  ? 20   LEU B N   1 
ATOM   3841 C  CA  . LEU B 1 20  ? -4.311  -34.482 69.374  1.00 33.60  ? 20   LEU B CA  1 
ATOM   3842 C  C   . LEU B 1 20  ? -4.654  -35.138 68.046  1.00 34.43  ? 20   LEU B C   1 
ATOM   3843 O  O   . LEU B 1 20  ? -4.384  -34.552 66.993  1.00 36.61  ? 20   LEU B O   1 
ATOM   3844 C  CB  . LEU B 1 20  ? -2.798  -34.209 69.435  1.00 33.63  ? 20   LEU B CB  1 
ATOM   3845 C  CG  . LEU B 1 20  ? -2.357  -33.467 70.684  1.00 33.67  ? 20   LEU B CG  1 
ATOM   3846 C  CD1 . LEU B 1 20  ? -0.863  -33.191 70.629  1.00 36.50  ? 20   LEU B CD1 1 
ATOM   3847 C  CD2 . LEU B 1 20  ? -3.153  -32.177 70.838  1.00 36.88  ? 20   LEU B CD2 1 
ATOM   3848 N  N   . ASN B 1 21  ? -5.232  -36.338 68.061  1.00 32.39  ? 21   ASN B N   1 
ATOM   3849 C  CA  . ASN B 1 21  ? -5.584  -37.018 66.819  1.00 38.04  ? 21   ASN B CA  1 
ATOM   3850 C  C   . ASN B 1 21  ? -6.939  -36.487 66.359  1.00 39.71  ? 21   ASN B C   1 
ATOM   3851 O  O   . ASN B 1 21  ? -7.981  -37.138 66.469  1.00 37.46  ? 21   ASN B O   1 
ATOM   3852 C  CB  . ASN B 1 21  ? -5.599  -38.531 66.996  1.00 41.01  ? 21   ASN B CB  1 
ATOM   3853 C  CG  . ASN B 1 21  ? -5.817  -39.258 65.675  1.00 46.77  ? 21   ASN B CG  1 
ATOM   3854 O  OD1 . ASN B 1 21  ? -5.871  -38.632 64.609  1.00 44.59  ? 21   ASN B OD1 1 
ATOM   3855 N  ND2 . ASN B 1 21  ? -5.934  -40.577 65.734  1.00 47.66  ? 21   ASN B ND2 1 
ATOM   3856 N  N   . THR B 1 22  ? -6.901  -35.250 65.869  1.00 35.65  ? 22   THR B N   1 
ATOM   3857 C  CA  . THR B 1 22  ? -8.076  -34.537 65.394  1.00 33.90  ? 22   THR B CA  1 
ATOM   3858 C  C   . THR B 1 22  ? -7.617  -33.503 64.378  1.00 38.07  ? 22   THR B C   1 
ATOM   3859 O  O   . THR B 1 22  ? -6.469  -33.060 64.412  1.00 38.93  ? 22   THR B O   1 
ATOM   3860 C  CB  . THR B 1 22  ? -8.837  -33.850 66.533  1.00 38.22  ? 22   THR B CB  1 
ATOM   3861 O  OG1 . THR B 1 22  ? -9.811  -32.948 65.986  1.00 41.24  ? 22   THR B OG1 1 
ATOM   3862 C  CG2 . THR B 1 22  ? -7.876  -33.066 67.475  1.00 36.02  ? 22   THR B CG2 1 
ATOM   3863 N  N   . ASP B 1 23  ? -8.521  -33.122 63.469  1.00 38.17  ? 23   ASP B N   1 
ATOM   3864 C  CA  . ASP B 1 23  ? -8.176  -32.055 62.541  1.00 40.96  ? 23   ASP B CA  1 
ATOM   3865 C  C   . ASP B 1 23  ? -8.204  -30.689 63.210  1.00 33.23  ? 23   ASP B C   1 
ATOM   3866 O  O   . ASP B 1 23  ? -7.804  -29.707 62.580  1.00 33.64  ? 23   ASP B O   1 
ATOM   3867 C  CB  . ASP B 1 23  ? -9.127  -32.013 61.330  1.00 43.90  ? 23   ASP B CB  1 
ATOM   3868 C  CG  . ASP B 1 23  ? -10.605 -32.025 61.722  1.00 48.42  ? 23   ASP B CG  1 
ATOM   3869 O  OD1 . ASP B 1 23  ? -10.949 -32.411 62.855  1.00 51.27  ? 23   ASP B OD1 1 
ATOM   3870 O  OD2 . ASP B 1 23  ? -11.446 -31.649 60.871  1.00 56.50  ? 23   ASP B OD2 1 
ATOM   3871 N  N   . LYS B 1 24  ? -8.682  -30.605 64.453  1.00 35.36  ? 24   LYS B N   1 
ATOM   3872 C  CA  . LYS B 1 24  ? -8.906  -29.327 65.132  1.00 34.88  ? 24   LYS B CA  1 
ATOM   3873 C  C   . LYS B 1 24  ? -8.349  -29.395 66.545  1.00 32.60  ? 24   LYS B C   1 
ATOM   3874 O  O   . LYS B 1 24  ? -9.084  -29.302 67.537  1.00 31.55  ? 24   LYS B O   1 
ATOM   3875 C  CB  . LYS B 1 24  ? -10.393 -28.980 65.134  1.00 34.95  ? 24   LYS B CB  1 
ATOM   3876 C  CG  . LYS B 1 24  ? -10.903 -28.686 63.706  1.00 35.46  ? 24   LYS B CG  1 
ATOM   3877 C  CD  . LYS B 1 24  ? -12.389 -28.333 63.701  1.00 37.85  ? 24   LYS B CD  1 
ATOM   3878 C  CE  . LYS B 1 24  ? -12.887 -28.065 62.285  1.00 36.17  ? 24   LYS B CE  1 
ATOM   3879 N  NZ  . LYS B 1 24  ? -14.346 -27.704 62.346  1.00 37.55  ? 24   LYS B NZ  1 
ATOM   3880 N  N   . PRO B 1 25  ? -7.028  -29.543 66.671  1.00 30.08  ? 25   PRO B N   1 
ATOM   3881 C  CA  . PRO B 1 25  ? -6.452  -29.782 68.001  1.00 29.48  ? 25   PRO B CA  1 
ATOM   3882 C  C   . PRO B 1 25  ? -6.503  -28.582 68.930  1.00 32.20  ? 25   PRO B C   1 
ATOM   3883 O  O   . PRO B 1 25  ? -6.703  -28.763 70.137  1.00 32.39  ? 25   PRO B O   1 
ATOM   3884 C  CB  . PRO B 1 25  ? -5.004  -30.199 67.678  1.00 31.35  ? 25   PRO B CB  1 
ATOM   3885 C  CG  . PRO B 1 25  ? -4.723  -29.567 66.325  1.00 31.74  ? 25   PRO B CG  1 
ATOM   3886 C  CD  . PRO B 1 25  ? -6.041  -29.686 65.588  1.00 31.54  ? 25   PRO B CD  1 
ATOM   3887 N  N   . VAL B 1 26  ? -6.294  -27.362 68.426  1.00 31.52  ? 26   VAL B N   1 
ATOM   3888 C  CA  . VAL B 1 26  ? -6.399  -26.196 69.305  1.00 32.67  ? 26   VAL B CA  1 
ATOM   3889 C  C   . VAL B 1 26  ? -7.804  -26.085 69.859  1.00 30.59  ? 26   VAL B C   1 
ATOM   3890 O  O   . VAL B 1 26  ? -7.996  -25.840 71.053  1.00 32.59  ? 26   VAL B O   1 
ATOM   3891 C  CB  . VAL B 1 26  ? -5.996  -24.908 68.568  1.00 33.41  ? 26   VAL B CB  1 
ATOM   3892 C  CG1 . VAL B 1 26  ? -6.284  -23.706 69.451  1.00 32.20  ? 26   VAL B CG1 1 
ATOM   3893 C  CG2 . VAL B 1 26  ? -4.504  -24.963 68.191  1.00 32.17  ? 26   VAL B CG2 1 
ATOM   3894 N  N   . GLN B 1 27  ? -8.810  -26.271 69.002  1.00 31.73  ? 27   GLN B N   1 
ATOM   3895 C  CA  . GLN B 1 27  ? -10.186 -26.213 69.484  1.00 29.90  ? 27   GLN B CA  1 
ATOM   3896 C  C   . GLN B 1 27  ? -10.474 -27.326 70.486  1.00 31.95  ? 27   GLN B C   1 
ATOM   3897 O  O   . GLN B 1 27  ? -11.206 -27.115 71.464  1.00 31.15  ? 27   GLN B O   1 
ATOM   3898 C  CB  . GLN B 1 27  ? -11.147 -26.251 68.297  1.00 32.82  ? 27   GLN B CB  1 
ATOM   3899 C  CG  . GLN B 1 27  ? -11.069 -24.958 67.505  1.00 35.13  ? 27   GLN B CG  1 
ATOM   3900 C  CD  . GLN B 1 27  ? -11.670 -25.061 66.122  1.00 33.18  ? 27   GLN B CD  1 
ATOM   3901 O  OE1 . GLN B 1 27  ? -12.881 -24.854 65.935  1.00 34.52  ? 27   GLN B OE1 1 
ATOM   3902 N  NE2 . GLN B 1 27  ? -10.830 -25.360 65.138  1.00 33.44  ? 27   GLN B NE2 1 
ATOM   3903 N  N   . ALA B 1 28  ? -9.872  -28.509 70.293  1.00 32.83  ? 28   ALA B N   1 
ATOM   3904 C  CA  . ALA B 1 28  ? -10.007 -29.574 71.289  1.00 32.57  ? 28   ALA B CA  1 
ATOM   3905 C  C   . ALA B 1 28  ? -9.395  -29.163 72.623  1.00 35.15  ? 28   ALA B C   1 
ATOM   3906 O  O   . ALA B 1 28  ? -9.979  -29.400 73.690  1.00 32.83  ? 28   ALA B O   1 
ATOM   3907 C  CB  . ALA B 1 28  ? -9.357  -30.863 70.774  1.00 33.84  ? 28   ALA B CB  1 
ATOM   3908 N  N   . LEU B 1 29  ? -8.216  -28.536 72.585  1.00 33.27  ? 29   LEU B N   1 
ATOM   3909 C  CA  . LEU B 1 29  ? -7.583  -28.108 73.828  1.00 32.92  ? 29   LEU B CA  1 
ATOM   3910 C  C   . LEU B 1 29  ? -8.381  -27.005 74.512  1.00 36.64  ? 29   LEU B C   1 
ATOM   3911 O  O   . LEU B 1 29  ? -8.398  -26.928 75.750  1.00 32.79  ? 29   LEU B O   1 
ATOM   3912 C  CB  . LEU B 1 29  ? -6.152  -27.652 73.548  1.00 35.42  ? 29   LEU B CB  1 
ATOM   3913 C  CG  . LEU B 1 29  ? -5.196  -28.784 73.159  1.00 33.36  ? 29   LEU B CG  1 
ATOM   3914 C  CD1 . LEU B 1 29  ? -4.001  -28.262 72.358  1.00 31.50  ? 29   LEU B CD1 1 
ATOM   3915 C  CD2 . LEU B 1 29  ? -4.735  -29.501 74.424  1.00 34.93  ? 29   LEU B CD2 1 
ATOM   3916 N  N   . MET B 1 30  ? -9.024  -26.130 73.735  1.00 31.85  ? 30   MET B N   1 
ATOM   3917 C  CA  . MET B 1 30  ? -9.896  -25.136 74.342  1.00 33.77  ? 30   MET B CA  1 
ATOM   3918 C  C   . MET B 1 30  ? -11.022 -25.802 75.120  1.00 37.03  ? 30   MET B C   1 
ATOM   3919 O  O   . MET B 1 30  ? -11.347 -25.384 76.239  1.00 36.56  ? 30   MET B O   1 
ATOM   3920 C  CB  . MET B 1 30  ? -10.482 -24.181 73.300  1.00 34.64  ? 30   MET B CB  1 
ATOM   3921 C  CG  . MET B 1 30  ? -9.495  -23.132 72.762  1.00 32.33  ? 30   MET B CG  1 
ATOM   3922 S  SD  . MET B 1 30  ? -9.987  -22.382 71.207  1.00 34.48  ? 30   MET B SD  1 
ATOM   3923 C  CE  . MET B 1 30  ? -11.328 -21.376 71.865  1.00 35.35  ? 30   MET B CE  1 
ATOM   3924 N  N   . LYS B 1 31  ? -11.636 -26.837 74.541  1.00 33.74  ? 31   LYS B N   1 
ATOM   3925 C  CA  . LYS B 1 31  ? -12.709 -27.521 75.262  1.00 36.52  ? 31   LYS B CA  1 
ATOM   3926 C  C   . LYS B 1 31  ? -12.190 -28.188 76.530  1.00 36.78  ? 31   LYS B C   1 
ATOM   3927 O  O   . LYS B 1 31  ? -12.864 -28.170 77.563  1.00 34.30  ? 31   LYS B O   1 
ATOM   3928 C  CB  . LYS B 1 31  ? -13.396 -28.543 74.362  1.00 35.94  ? 31   LYS B CB  1 
ATOM   3929 C  CG  . LYS B 1 31  ? -14.518 -27.958 73.503  1.00 48.46  ? 31   LYS B CG  1 
ATOM   3930 C  CD  . LYS B 1 31  ? -14.702 -28.710 72.182  1.00 52.80  ? 31   LYS B CD  1 
ATOM   3931 C  CE  . LYS B 1 31  ? -15.272 -27.797 71.084  1.00 53.02  ? 31   LYS B CE  1 
ATOM   3932 N  NZ  . LYS B 1 31  ? -16.773 -27.771 71.123  1.00 63.89  ? 31   LYS B NZ  1 
ATOM   3933 N  N   . ILE B 1 32  ? -10.998 -28.791 76.474  1.00 34.03  ? 32   ILE B N   1 
ATOM   3934 C  CA  . ILE B 1 32  ? -10.404 -29.352 77.685  1.00 35.49  ? 32   ILE B CA  1 
ATOM   3935 C  C   . ILE B 1 32  ? -10.183 -28.256 78.720  1.00 37.30  ? 32   ILE B C   1 
ATOM   3936 O  O   . ILE B 1 32  ? -10.433 -28.457 79.915  1.00 33.87  ? 32   ILE B O   1 
ATOM   3937 C  CB  . ILE B 1 32  ? -9.092  -30.092 77.354  1.00 33.75  ? 32   ILE B CB  1 
ATOM   3938 C  CG1 . ILE B 1 32  ? -9.367  -31.325 76.483  1.00 34.14  ? 32   ILE B CG1 1 
ATOM   3939 C  CG2 . ILE B 1 32  ? -8.324  -30.463 78.652  1.00 30.42  ? 32   ILE B CG2 1 
ATOM   3940 C  CD1 . ILE B 1 32  ? -8.161  -31.825 75.721  1.00 34.00  ? 32   ILE B CD1 1 
ATOM   3941 N  N   . ALA B 1 33  ? -9.708  -27.085 78.283  1.00 34.85  ? 33   ALA B N   1 
ATOM   3942 C  CA  . ALA B 1 33  ? -9.504  -25.974 79.205  1.00 35.50  ? 33   ALA B CA  1 
ATOM   3943 C  C   . ALA B 1 33  ? -10.822 -25.520 79.818  1.00 34.85  ? 33   ALA B C   1 
ATOM   3944 O  O   . ALA B 1 33  ? -10.884 -25.196 81.009  1.00 35.95  ? 33   ALA B O   1 
ATOM   3945 C  CB  . ALA B 1 33  ? -8.811  -24.810 78.489  1.00 36.09  ? 33   ALA B CB  1 
ATOM   3946 N  N   . ASP B 1 34  ? -11.885 -25.469 79.021  1.00 36.05  ? 34   ASP B N   1 
ATOM   3947 C  CA  . ASP B 1 34  ? -13.183 -25.122 79.593  1.00 38.96  ? 34   ASP B CA  1 
ATOM   3948 C  C   . ASP B 1 34  ? -13.569 -26.094 80.689  1.00 40.68  ? 34   ASP B C   1 
ATOM   3949 O  O   . ASP B 1 34  ? -14.165 -25.703 81.702  1.00 42.36  ? 34   ASP B O   1 
ATOM   3950 C  CB  . ASP B 1 34  ? -14.251 -25.105 78.508  1.00 39.63  ? 34   ASP B CB  1 
ATOM   3951 C  CG  . ASP B 1 34  ? -14.206 -23.854 77.694  1.00 44.28  ? 34   ASP B CG  1 
ATOM   3952 O  OD1 . ASP B 1 34  ? -13.604 -22.872 78.171  1.00 50.11  ? 34   ASP B OD1 1 
ATOM   3953 O  OD2 . ASP B 1 34  ? -14.786 -23.844 76.595  1.00 47.74  ? 34   ASP B OD2 1 
ATOM   3954 N  N   . GLU B 1 35  ? -13.230 -27.366 80.508  1.00 35.29  ? 35   GLU B N   1 
ATOM   3955 C  CA  . GLU B 1 35  ? -13.595 -28.389 81.478  1.00 35.47  ? 35   GLU B CA  1 
ATOM   3956 C  C   . GLU B 1 35  ? -12.677 -28.379 82.700  1.00 39.44  ? 35   GLU B C   1 
ATOM   3957 O  O   . GLU B 1 35  ? -13.143 -28.548 83.836  1.00 37.47  ? 35   GLU B O   1 
ATOM   3958 C  CB  . GLU B 1 35  ? -13.577 -29.751 80.781  1.00 42.50  ? 35   GLU B CB  1 
ATOM   3959 C  CG  . GLU B 1 35  ? -13.730 -30.942 81.678  1.00 50.60  ? 35   GLU B CG  1 
ATOM   3960 C  CD  . GLU B 1 35  ? -13.737 -32.247 80.885  1.00 58.06  ? 35   GLU B CD  1 
ATOM   3961 O  OE1 . GLU B 1 35  ? -13.743 -32.189 79.631  1.00 61.61  ? 35   GLU B OE1 1 
ATOM   3962 O  OE2 . GLU B 1 35  ? -13.735 -33.323 81.525  1.00 64.68  ? 35   GLU B OE2 1 
ATOM   3963 N  N   . LEU B 1 36  ? -11.374 -28.168 82.504  1.00 35.28  ? 36   LEU B N   1 
ATOM   3964 C  CA  . LEU B 1 36  ? -10.434 -28.373 83.598  1.00 35.48  ? 36   LEU B CA  1 
ATOM   3965 C  C   . LEU B 1 36  ? -9.979  -27.094 84.284  1.00 35.64  ? 36   LEU B C   1 
ATOM   3966 O  O   . LEU B 1 36  ? -9.529  -27.162 85.437  1.00 35.65  ? 36   LEU B O   1 
ATOM   3967 C  CB  . LEU B 1 36  ? -9.200  -29.132 83.101  1.00 34.65  ? 36   LEU B CB  1 
ATOM   3968 C  CG  . LEU B 1 36  ? -9.462  -30.538 82.572  1.00 39.81  ? 36   LEU B CG  1 
ATOM   3969 C  CD1 . LEU B 1 36  ? -8.128  -31.234 82.241  1.00 34.27  ? 36   LEU B CD1 1 
ATOM   3970 C  CD2 . LEU B 1 36  ? -10.273 -31.330 83.591  1.00 38.58  ? 36   LEU B CD2 1 
ATOM   3971 N  N   . GLY B 1 37  ? -10.064 -25.954 83.621  1.00 34.94  ? 37   GLY B N   1 
ATOM   3972 C  CA  . GLY B 1 37  ? -9.763  -24.684 84.253  1.00 35.77  ? 37   GLY B CA  1 
ATOM   3973 C  C   . GLY B 1 37  ? -8.457  -24.077 83.770  1.00 36.84  ? 37   GLY B C   1 
ATOM   3974 O  O   . GLY B 1 37  ? -7.978  -24.338 82.662  1.00 38.25  ? 37   GLY B O   1 
ATOM   3975 N  N   . GLU B 1 38  ? -7.879  -23.237 84.629  1.00 33.35  ? 38   GLU B N   1 
ATOM   3976 C  CA  . GLU B 1 38  ? -6.804  -22.346 84.210  1.00 37.80  ? 38   GLU B CA  1 
ATOM   3977 C  C   . GLU B 1 38  ? -5.493  -23.068 83.932  1.00 36.41  ? 38   GLU B C   1 
ATOM   3978 O  O   . GLU B 1 38  ? -4.602  -22.477 83.310  1.00 34.39  ? 38   GLU B O   1 
ATOM   3979 C  CB  . GLU B 1 38  ? -6.576  -21.285 85.278  1.00 38.33  ? 38   GLU B CB  1 
ATOM   3980 C  CG  . GLU B 1 38  ? -6.097  -21.883 86.588  1.00 38.64  ? 38   GLU B CG  1 
ATOM   3981 C  CD  . GLU B 1 38  ? -5.831  -20.843 87.666  1.00 43.18  ? 38   GLU B CD  1 
ATOM   3982 O  OE1 . GLU B 1 38  ? -5.781  -19.628 87.362  1.00 37.32  ? 38   GLU B OE1 1 
ATOM   3983 O  OE2 . GLU B 1 38  ? -5.679  -21.259 88.835  1.00 40.85  ? 38   GLU B OE2 1 
ATOM   3984 N  N   . ILE B 1 39  ? -5.331  -24.306 84.390  1.00 33.62  ? 39   ILE B N   1 
ATOM   3985 C  CA  . ILE B 1 39  ? -4.085  -25.032 84.127  1.00 35.40  ? 39   ILE B CA  1 
ATOM   3986 C  C   . ILE B 1 39  ? -4.378  -26.524 84.073  1.00 36.29  ? 39   ILE B C   1 
ATOM   3987 O  O   . ILE B 1 39  ? -5.134  -27.050 84.891  1.00 35.16  ? 39   ILE B O   1 
ATOM   3988 C  CB  . ILE B 1 39  ? -3.009  -24.708 85.183  1.00 35.73  ? 39   ILE B CB  1 
ATOM   3989 C  CG1 . ILE B 1 39  ? -1.702  -25.438 84.868  1.00 36.63  ? 39   ILE B CG1 1 
ATOM   3990 C  CG2 . ILE B 1 39  ? -3.500  -25.062 86.613  1.00 37.56  ? 39   ILE B CG2 1 
ATOM   3991 C  CD1 . ILE B 1 39  ? -0.503  -24.918 85.675  1.00 36.75  ? 39   ILE B CD1 1 
ATOM   3992 N  N   . PHE B 1 40  ? -3.779  -27.210 83.103  1.00 34.22  ? 40   PHE B N   1 
ATOM   3993 C  CA  . PHE B 1 40  ? -3.825  -28.667 83.112  1.00 34.72  ? 40   PHE B CA  1 
ATOM   3994 C  C   . PHE B 1 40  ? -2.519  -29.217 82.565  1.00 35.00  ? 40   PHE B C   1 
ATOM   3995 O  O   . PHE B 1 40  ? -1.837  -28.571 81.764  1.00 35.43  ? 40   PHE B O   1 
ATOM   3996 C  CB  . PHE B 1 40  ? -5.036  -29.255 82.350  1.00 35.41  ? 40   PHE B CB  1 
ATOM   3997 C  CG  . PHE B 1 40  ? -5.110  -28.903 80.873  1.00 33.11  ? 40   PHE B CG  1 
ATOM   3998 C  CD1 . PHE B 1 40  ? -4.541  -29.722 79.908  1.00 32.60  ? 40   PHE B CD1 1 
ATOM   3999 C  CD2 . PHE B 1 40  ? -5.835  -27.783 80.451  1.00 32.87  ? 40   PHE B CD2 1 
ATOM   4000 C  CE1 . PHE B 1 40  ? -4.641  -29.406 78.552  1.00 34.08  ? 40   PHE B CE1 1 
ATOM   4001 C  CE2 . PHE B 1 40  ? -5.941  -27.455 79.096  1.00 34.24  ? 40   PHE B CE2 1 
ATOM   4002 C  CZ  . PHE B 1 40  ? -5.349  -28.276 78.140  1.00 35.37  ? 40   PHE B CZ  1 
ATOM   4003 N  N   . LYS B 1 41  ? -2.153  -30.386 83.079  1.00 35.23  ? 41   LYS B N   1 
ATOM   4004 C  CA  . LYS B 1 41  ? -0.993  -31.122 82.612  1.00 35.55  ? 41   LYS B CA  1 
ATOM   4005 C  C   . LYS B 1 41  ? -1.360  -31.929 81.378  1.00 36.17  ? 41   LYS B C   1 
ATOM   4006 O  O   . LYS B 1 41  ? -2.449  -32.504 81.299  1.00 36.63  ? 41   LYS B O   1 
ATOM   4007 C  CB  . LYS B 1 41  ? -0.502  -32.062 83.717  1.00 40.41  ? 41   LYS B CB  1 
ATOM   4008 C  CG  . LYS B 1 41  ? 0.737   -32.870 83.363  1.00 43.92  ? 41   LYS B CG  1 
ATOM   4009 C  CD  . LYS B 1 41  ? 0.792   -34.079 84.287  1.00 45.78  ? 41   LYS B CD  1 
ATOM   4010 C  CE  . LYS B 1 41  ? 1.992   -34.066 85.202  1.00 60.71  ? 41   LYS B CE  1 
ATOM   4011 N  NZ  . LYS B 1 41  ? 2.591   -35.432 85.318  1.00 60.87  ? 41   LYS B NZ  1 
ATOM   4012 N  N   . PHE B 1 42  ? -0.449  -31.973 80.409  1.00 34.23  ? 42   PHE B N   1 
ATOM   4013 C  CA  . PHE B 1 42  ? -0.644  -32.746 79.194  1.00 35.12  ? 42   PHE B CA  1 
ATOM   4014 C  C   . PHE B 1 42  ? 0.615   -33.564 78.970  1.00 34.98  ? 42   PHE B C   1 
ATOM   4015 O  O   . PHE B 1 42  ? 1.711   -32.999 78.900  1.00 34.19  ? 42   PHE B O   1 
ATOM   4016 C  CB  . PHE B 1 42  ? -0.925  -31.831 77.995  1.00 34.28  ? 42   PHE B CB  1 
ATOM   4017 C  CG  . PHE B 1 42  ? -1.366  -32.567 76.759  1.00 34.78  ? 42   PHE B CG  1 
ATOM   4018 C  CD1 . PHE B 1 42  ? -0.439  -33.168 75.917  1.00 38.25  ? 42   PHE B CD1 1 
ATOM   4019 C  CD2 . PHE B 1 42  ? -2.715  -32.668 76.441  1.00 37.01  ? 42   PHE B CD2 1 
ATOM   4020 C  CE1 . PHE B 1 42  ? -0.848  -33.855 74.777  1.00 38.58  ? 42   PHE B CE1 1 
ATOM   4021 C  CE2 . PHE B 1 42  ? -3.125  -33.342 75.301  1.00 34.75  ? 42   PHE B CE2 1 
ATOM   4022 C  CZ  . PHE B 1 42  ? -2.191  -33.927 74.468  1.00 36.24  ? 42   PHE B CZ  1 
ATOM   4023 N  N   . GLU B 1 43  ? 0.461   -34.880 78.862  1.00 37.10  ? 43   GLU B N   1 
ATOM   4024 C  CA  . GLU B 1 43  ? 1.586   -35.802 78.740  1.00 40.40  ? 43   GLU B CA  1 
ATOM   4025 C  C   . GLU B 1 43  ? 1.511   -36.582 77.437  1.00 38.99  ? 43   GLU B C   1 
ATOM   4026 O  O   . GLU B 1 43  ? 0.433   -37.009 77.007  1.00 38.71  ? 43   GLU B O   1 
ATOM   4027 C  CB  . GLU B 1 43  ? 1.635   -36.804 79.903  1.00 38.63  ? 43   GLU B CB  1 
ATOM   4028 C  CG  . GLU B 1 43  ? 1.983   -36.208 81.224  1.00 45.42  ? 43   GLU B CG  1 
ATOM   4029 C  CD  . GLU B 1 43  ? 2.065   -37.268 82.295  1.00 53.19  ? 43   GLU B CD  1 
ATOM   4030 O  OE1 . GLU B 1 43  ? 1.119   -38.076 82.393  1.00 49.06  ? 43   GLU B OE1 1 
ATOM   4031 O  OE2 . GLU B 1 43  ? 3.068   -37.293 83.028  1.00 58.94  ? 43   GLU B OE2 1 
ATOM   4032 N  N   . ALA B 1 44  ? 2.663   -36.763 76.810  1.00 40.35  ? 44   ALA B N   1 
ATOM   4033 C  CA  . ALA B 1 44  ? 2.858   -37.689 75.707  1.00 36.49  ? 44   ALA B CA  1 
ATOM   4034 C  C   . ALA B 1 44  ? 4.062   -38.541 76.057  1.00 37.46  ? 44   ALA B C   1 
ATOM   4035 O  O   . ALA B 1 44  ? 4.806   -38.222 76.990  1.00 38.34  ? 44   ALA B O   1 
ATOM   4036 C  CB  . ALA B 1 44  ? 3.085   -36.939 74.386  1.00 37.16  ? 44   ALA B CB  1 
ATOM   4037 N  N   . PRO B 1 45  ? 4.263   -39.659 75.368  1.00 37.32  ? 45   PRO B N   1 
ATOM   4038 C  CA  . PRO B 1 45  ? 5.461   -40.463 75.652  1.00 40.47  ? 45   PRO B CA  1 
ATOM   4039 C  C   . PRO B 1 45  ? 6.700   -39.595 75.586  1.00 42.52  ? 45   PRO B C   1 
ATOM   4040 O  O   . PRO B 1 45  ? 6.988   -39.011 74.537  1.00 44.90  ? 45   PRO B O   1 
ATOM   4041 C  CB  . PRO B 1 45  ? 5.448   -41.527 74.548  1.00 38.61  ? 45   PRO B CB  1 
ATOM   4042 C  CG  . PRO B 1 45  ? 3.971   -41.683 74.202  1.00 40.16  ? 45   PRO B CG  1 
ATOM   4043 C  CD  . PRO B 1 45  ? 3.413   -40.274 74.330  1.00 37.62  ? 45   PRO B CD  1 
ATOM   4044 N  N   . GLY B 1 46  ? 7.402   -39.462 76.706  1.00 46.20  ? 46   GLY B N   1 
ATOM   4045 C  CA  . GLY B 1 46  ? 8.650   -38.726 76.734  1.00 47.20  ? 46   GLY B CA  1 
ATOM   4046 C  C   . GLY B 1 46  ? 8.546   -37.219 76.818  1.00 48.50  ? 46   GLY B C   1 
ATOM   4047 O  O   . GLY B 1 46  ? 9.547   -36.534 76.589  1.00 47.06  ? 46   GLY B O   1 
ATOM   4048 N  N   . ARG B 1 47  ? 7.372   -36.671 77.135  1.00 41.62  ? 47   ARG B N   1 
ATOM   4049 C  CA  . ARG B 1 47  ? 7.228   -35.225 77.227  1.00 41.88  ? 47   ARG B CA  1 
ATOM   4050 C  C   . ARG B 1 47  ? 6.053   -34.866 78.125  1.00 43.26  ? 47   ARG B C   1 
ATOM   4051 O  O   . ARG B 1 47  ? 5.046   -35.577 78.176  1.00 41.77  ? 47   ARG B O   1 
ATOM   4052 C  CB  . ARG B 1 47  ? 7.045   -34.572 75.849  1.00 39.91  ? 47   ARG B CB  1 
ATOM   4053 C  CG  . ARG B 1 47  ? 6.654   -33.091 75.950  1.00 51.49  ? 47   ARG B CG  1 
ATOM   4054 C  CD  . ARG B 1 47  ? 6.677   -32.350 74.616  1.00 48.44  ? 47   ARG B CD  1 
ATOM   4055 N  NE  . ARG B 1 47  ? 6.256   -30.951 74.723  1.00 44.08  ? 47   ARG B NE  1 
ATOM   4056 C  CZ  . ARG B 1 47  ? 5.520   -30.354 73.790  1.00 44.39  ? 47   ARG B CZ  1 
ATOM   4057 N  NH1 . ARG B 1 47  ? 5.204   -30.980 72.666  1.00 45.11  ? 47   ARG B NH1 1 
ATOM   4058 N  NH2 . ARG B 1 47  ? 5.079   -29.113 73.991  1.00 34.70  ? 47   ARG B NH2 1 
ATOM   4059 N  N   . VAL B 1 48  ? 6.197   -33.746 78.824  1.00 42.92  ? 48   VAL B N   1 
ATOM   4060 C  CA  . VAL B 1 48  ? 5.097   -33.149 79.568  1.00 37.58  ? 48   VAL B CA  1 
ATOM   4061 C  C   . VAL B 1 48  ? 5.092   -31.653 79.280  1.00 37.66  ? 48   VAL B C   1 
ATOM   4062 O  O   . VAL B 1 48  ? 6.139   -31.031 79.069  1.00 41.65  ? 48   VAL B O   1 
ATOM   4063 C  CB  . VAL B 1 48  ? 5.208   -33.437 81.082  1.00 44.61  ? 48   VAL B CB  1 
ATOM   4064 C  CG1 . VAL B 1 48  ? 6.607   -33.165 81.560  1.00 46.11  ? 48   VAL B CG1 1 
ATOM   4065 C  CG2 . VAL B 1 48  ? 4.197   -32.634 81.878  1.00 43.13  ? 48   VAL B CG2 1 
ATOM   4066 N  N   . THR B 1 49  ? 3.896   -31.076 79.234  1.00 34.92  ? 49   THR B N   1 
ATOM   4067 C  CA  . THR B 1 49  ? 3.756   -29.629 79.246  1.00 34.39  ? 49   THR B CA  1 
ATOM   4068 C  C   . THR B 1 49  ? 2.509   -29.299 80.058  1.00 36.00  ? 49   THR B C   1 
ATOM   4069 O  O   . THR B 1 49  ? 1.765   -30.191 80.484  1.00 36.97  ? 49   THR B O   1 
ATOM   4070 C  CB  . THR B 1 49  ? 3.705   -29.039 77.820  1.00 35.64  ? 49   THR B CB  1 
ATOM   4071 O  OG1 . THR B 1 49  ? 3.884   -27.610 77.876  1.00 33.74  ? 49   THR B OG1 1 
ATOM   4072 C  CG2 . THR B 1 49  ? 2.358   -29.352 77.140  1.00 35.54  ? 49   THR B CG2 1 
ATOM   4073 N  N   . ARG B 1 50  ? 2.307   -28.009 80.301  1.00 33.21  ? 50   ARG B N   1 
ATOM   4074 C  CA  . ARG B 1 50  ? 1.176   -27.515 81.085  1.00 35.41  ? 50   ARG B CA  1 
ATOM   4075 C  C   . ARG B 1 50  ? 0.500   -26.399 80.301  1.00 36.01  ? 50   ARG B C   1 
ATOM   4076 O  O   . ARG B 1 50  ? 1.157   -25.428 79.910  1.00 33.65  ? 50   ARG B O   1 
ATOM   4077 C  CB  . ARG B 1 50  ? 1.645   -27.015 82.456  1.00 37.08  ? 50   ARG B CB  1 
ATOM   4078 C  CG  . ARG B 1 50  ? 2.463   -28.062 83.203  1.00 36.62  ? 50   ARG B CG  1 
ATOM   4079 C  CD  . ARG B 1 50  ? 3.714   -27.485 83.821  1.00 40.08  ? 50   ARG B CD  1 
ATOM   4080 N  NE  . ARG B 1 50  ? 4.559   -28.568 84.314  1.00 42.60  ? 50   ARG B NE  1 
ATOM   4081 C  CZ  . ARG B 1 50  ? 5.516   -29.150 83.601  1.00 44.44  ? 50   ARG B CZ  1 
ATOM   4082 N  NH1 . ARG B 1 50  ? 5.852   -28.715 82.395  1.00 37.64  ? 50   ARG B NH1 1 
ATOM   4083 N  NH2 . ARG B 1 50  ? 6.156   -30.202 84.105  1.00 42.13  ? 50   ARG B NH2 1 
ATOM   4084 N  N   . TYR B 1 51  ? -0.800  -26.541 80.060  1.00 32.94  ? 51   TYR B N   1 
ATOM   4085 C  CA  . TYR B 1 51  ? -1.558  -25.558 79.289  1.00 33.79  ? 51   TYR B CA  1 
ATOM   4086 C  C   . TYR B 1 51  ? -2.183  -24.531 80.224  1.00 31.90  ? 51   TYR B C   1 
ATOM   4087 O  O   . TYR B 1 51  ? -2.926  -24.893 81.140  1.00 33.74  ? 51   TYR B O   1 
ATOM   4088 C  CB  . TYR B 1 51  ? -2.654  -26.230 78.463  1.00 33.49  ? 51   TYR B CB  1 
ATOM   4089 C  CG  . TYR B 1 51  ? -2.120  -26.924 77.227  1.00 30.94  ? 51   TYR B CG  1 
ATOM   4090 C  CD1 . TYR B 1 51  ? -1.605  -28.214 77.306  1.00 31.76  ? 51   TYR B CD1 1 
ATOM   4091 C  CD2 . TYR B 1 51  ? -2.093  -26.271 75.998  1.00 32.39  ? 51   TYR B CD2 1 
ATOM   4092 C  CE1 . TYR B 1 51  ? -1.092  -28.847 76.186  1.00 32.28  ? 51   TYR B CE1 1 
ATOM   4093 C  CE2 . TYR B 1 51  ? -1.566  -26.889 74.871  1.00 34.26  ? 51   TYR B CE2 1 
ATOM   4094 C  CZ  . TYR B 1 51  ? -1.069  -28.178 74.976  1.00 33.15  ? 51   TYR B CZ  1 
ATOM   4095 O  OH  . TYR B 1 51  ? -0.546  -28.802 73.862  1.00 33.66  ? 51   TYR B OH  1 
ATOM   4096 N  N   . LEU B 1 52  ? -1.904  -23.259 79.970  1.00 32.96  ? 52   LEU B N   1 
ATOM   4097 C  CA  . LEU B 1 52  ? -2.372  -22.158 80.801  1.00 33.54  ? 52   LEU B CA  1 
ATOM   4098 C  C   . LEU B 1 52  ? -3.456  -21.367 80.082  1.00 34.68  ? 52   LEU B C   1 
ATOM   4099 O  O   . LEU B 1 52  ? -3.317  -21.034 78.898  1.00 32.87  ? 52   LEU B O   1 
ATOM   4100 C  CB  . LEU B 1 52  ? -1.225  -21.216 81.166  1.00 33.13  ? 52   LEU B CB  1 
ATOM   4101 C  CG  . LEU B 1 52  ? 0.030   -21.815 81.802  1.00 32.94  ? 52   LEU B CG  1 
ATOM   4102 C  CD1 . LEU B 1 52  ? 1.026   -20.684 82.094  1.00 34.75  ? 52   LEU B CD1 1 
ATOM   4103 C  CD2 . LEU B 1 52  ? -0.339  -22.554 83.065  1.00 36.92  ? 52   LEU B CD2 1 
ATOM   4104 N  N   . SER B 1 53  ? -4.519  -21.033 80.820  1.00 31.58  ? 53   SER B N   1 
ATOM   4105 C  CA  . SER B 1 53  ? -5.669  -20.348 80.258  1.00 32.79  ? 53   SER B CA  1 
ATOM   4106 C  C   . SER B 1 53  ? -6.086  -19.080 80.995  1.00 34.60  ? 53   SER B C   1 
ATOM   4107 O  O   . SER B 1 53  ? -6.955  -18.372 80.479  1.00 35.15  ? 53   SER B O   1 
ATOM   4108 C  CB  . SER B 1 53  ? -6.889  -21.288 80.230  1.00 34.50  ? 53   SER B CB  1 
ATOM   4109 O  OG  . SER B 1 53  ? -6.708  -22.312 79.277  1.00 37.84  ? 53   SER B OG  1 
ATOM   4110 N  N   . SER B 1 54  ? -5.559  -18.795 82.194  1.00 33.55  ? 54   SER B N   1 
ATOM   4111 C  CA  . SER B 1 54  ? -6.008  -17.630 82.958  1.00 31.80  ? 54   SER B CA  1 
ATOM   4112 C  C   . SER B 1 54  ? -5.001  -16.491 82.872  1.00 34.20  ? 54   SER B C   1 
ATOM   4113 O  O   . SER B 1 54  ? -3.792  -16.712 82.763  1.00 34.98  ? 54   SER B O   1 
ATOM   4114 C  CB  . SER B 1 54  ? -6.252  -17.982 84.432  1.00 34.85  ? 54   SER B CB  1 
ATOM   4115 O  OG  . SER B 1 54  ? -5.036  -18.343 85.070  1.00 32.09  ? 54   SER B OG  1 
ATOM   4116 N  N   . GLN B 1 55  ? -5.513  -15.260 82.928  1.00 37.43  ? 55   GLN B N   1 
ATOM   4117 C  CA  . GLN B 1 55  ? -4.617  -14.111 82.988  1.00 36.78  ? 55   GLN B CA  1 
ATOM   4118 C  C   . GLN B 1 55  ? -3.730  -14.190 84.224  1.00 33.81  ? 55   GLN B C   1 
ATOM   4119 O  O   . GLN B 1 55  ? -2.544  -13.833 84.172  1.00 34.26  ? 55   GLN B O   1 
ATOM   4120 C  CB  . GLN B 1 55  ? -5.430  -12.819 82.970  1.00 36.81  ? 55   GLN B CB  1 
ATOM   4121 C  CG  . GLN B 1 55  ? -4.602  -11.542 82.845  1.00 39.25  ? 55   GLN B CG  1 
ATOM   4122 C  CD  . GLN B 1 55  ? -4.207  -10.978 84.200  1.00 41.15  ? 55   GLN B CD  1 
ATOM   4123 O  OE1 . GLN B 1 55  ? -4.598  -11.508 85.248  1.00 39.13  ? 55   GLN B OE1 1 
ATOM   4124 N  NE2 . GLN B 1 55  ? -3.422  -9.898  84.188  1.00 42.23  ? 55   GLN B NE2 1 
ATOM   4125 N  N   . ARG B 1 56  ? -4.281  -14.687 85.336  1.00 34.97  ? 56   ARG B N   1 
ATOM   4126 C  CA  . ARG B 1 56  ? -3.524  -14.790 86.585  1.00 34.71  ? 56   ARG B CA  1 
ATOM   4127 C  C   . ARG B 1 56  ? -2.208  -15.536 86.383  1.00 38.29  ? 56   ARG B C   1 
ATOM   4128 O  O   . ARG B 1 56  ? -1.144  -15.076 86.812  1.00 38.31  ? 56   ARG B O   1 
ATOM   4129 C  CB  . ARG B 1 56  ? -4.383  -15.495 87.649  1.00 40.13  ? 56   ARG B CB  1 
ATOM   4130 C  CG  . ARG B 1 56  ? -3.655  -15.806 88.963  1.00 47.40  ? 56   ARG B CG  1 
ATOM   4131 C  CD  . ARG B 1 56  ? -4.563  -16.546 89.960  1.00 42.99  ? 56   ARG B CD  1 
ATOM   4132 N  NE  . ARG B 1 56  ? -4.430  -17.997 89.868  1.00 44.11  ? 56   ARG B NE  1 
ATOM   4133 C  CZ  . ARG B 1 56  ? -3.619  -18.725 90.627  1.00 46.96  ? 56   ARG B CZ  1 
ATOM   4134 N  NH1 . ARG B 1 56  ? -2.841  -18.165 91.540  1.00 45.50  ? 56   ARG B NH1 1 
ATOM   4135 N  NH2 . ARG B 1 56  ? -3.604  -20.051 90.483  1.00 43.42  ? 56   ARG B NH2 1 
ATOM   4136 N  N   . LEU B 1 57  ? -2.264  -16.704 85.742  1.00 33.97  ? 57   LEU B N   1 
ATOM   4137 C  CA  . LEU B 1 57  ? -1.052  -17.495 85.548  1.00 31.31  ? 57   LEU B CA  1 
ATOM   4138 C  C   . LEU B 1 57  ? -0.261  -17.043 84.331  1.00 32.17  ? 57   LEU B C   1 
ATOM   4139 O  O   . LEU B 1 57  ? 0.975   -17.119 84.333  1.00 32.44  ? 57   LEU B O   1 
ATOM   4140 C  CB  . LEU B 1 57  ? -1.407  -18.973 85.409  1.00 35.49  ? 57   LEU B CB  1 
ATOM   4141 C  CG  . LEU B 1 57  ? -2.102  -19.594 86.625  1.00 35.24  ? 57   LEU B CG  1 
ATOM   4142 C  CD1 . LEU B 1 57  ? -2.447  -21.050 86.355  1.00 36.10  ? 57   LEU B CD1 1 
ATOM   4143 C  CD2 . LEU B 1 57  ? -1.195  -19.476 87.838  1.00 38.44  ? 57   LEU B CD2 1 
ATOM   4144 N  N   . ILE B 1 58  ? -0.940  -16.586 83.280  1.00 35.15  ? 58   ILE B N   1 
ATOM   4145 C  CA  . ILE B 1 58  ? -0.199  -16.225 82.073  1.00 34.06  ? 58   ILE B CA  1 
ATOM   4146 C  C   . ILE B 1 58  ? 0.631   -14.966 82.301  1.00 33.43  ? 58   ILE B C   1 
ATOM   4147 O  O   . ILE B 1 58  ? 1.717   -14.816 81.727  1.00 34.16  ? 58   ILE B O   1 
ATOM   4148 C  CB  . ILE B 1 58  ? -1.179  -16.106 80.885  1.00 33.40  ? 58   ILE B CB  1 
ATOM   4149 C  CG1 . ILE B 1 58  ? -1.639  -17.507 80.448  1.00 32.45  ? 58   ILE B CG1 1 
ATOM   4150 C  CG2 . ILE B 1 58  ? -0.528  -15.385 79.705  1.00 33.74  ? 58   ILE B CG2 1 
ATOM   4151 C  CD1 . ILE B 1 58  ? -2.900  -17.528 79.538  1.00 31.19  ? 58   ILE B CD1 1 
ATOM   4152 N  N   . LYS B 1 59  ? 0.173   -14.056 83.162  1.00 33.39  ? 59   LYS B N   1 
ATOM   4153 C  CA  . LYS B 1 59  ? 0.996   -12.879 83.435  1.00 37.96  ? 59   LYS B CA  1 
ATOM   4154 C  C   . LYS B 1 59  ? 2.311   -13.268 84.096  1.00 36.10  ? 59   LYS B C   1 
ATOM   4155 O  O   . LYS B 1 59  ? 3.339   -12.628 83.848  1.00 35.34  ? 59   LYS B O   1 
ATOM   4156 C  CB  . LYS B 1 59  ? 0.245   -11.872 84.307  1.00 36.65  ? 59   LYS B CB  1 
ATOM   4157 C  CG  . LYS B 1 59  ? 0.041   -12.304 85.737  1.00 41.88  ? 59   LYS B CG  1 
ATOM   4158 C  CD  . LYS B 1 59  ? -0.738  -11.250 86.515  1.00 43.36  ? 59   LYS B CD  1 
ATOM   4159 C  CE  . LYS B 1 59  ? -0.898  -11.671 87.976  1.00 49.96  ? 59   LYS B CE  1 
ATOM   4160 N  NZ  . LYS B 1 59  ? -1.789  -10.725 88.718  1.00 57.45  ? 59   LYS B NZ  1 
ATOM   4161 N  N   . GLU B 1 60  ? 2.306   -14.314 84.926  1.00 35.20  ? 60   GLU B N   1 
ATOM   4162 C  CA  . GLU B 1 60  ? 3.563   -14.824 85.471  1.00 37.25  ? 60   GLU B CA  1 
ATOM   4163 C  C   . GLU B 1 60  ? 4.398   -15.505 84.396  1.00 38.25  ? 60   GLU B C   1 
ATOM   4164 O  O   . GLU B 1 60  ? 5.625   -15.347 84.360  1.00 36.18  ? 60   GLU B O   1 
ATOM   4165 C  CB  . GLU B 1 60  ? 3.301   -15.793 86.622  1.00 37.45  ? 60   GLU B CB  1 
ATOM   4166 C  CG  . GLU B 1 60  ? 2.772   -15.126 87.873  1.00 38.47  ? 60   GLU B CG  1 
ATOM   4167 C  CD  . GLU B 1 60  ? 2.721   -16.075 89.049  1.00 45.20  ? 60   GLU B CD  1 
ATOM   4168 O  OE1 . GLU B 1 60  ? 3.613   -16.947 89.170  1.00 40.60  ? 60   GLU B OE1 1 
ATOM   4169 O  OE2 . GLU B 1 60  ? 1.792   -15.929 89.867  1.00 46.89  ? 60   GLU B OE2 1 
ATOM   4170 N  N   . ALA B 1 61  ? 3.759   -16.292 83.529  1.00 34.11  ? 61   ALA B N   1 
ATOM   4171 C  CA  . ALA B 1 61  ? 4.494   -16.927 82.444  1.00 34.66  ? 61   ALA B CA  1 
ATOM   4172 C  C   . ALA B 1 61  ? 5.201   -15.896 81.574  1.00 36.07  ? 61   ALA B C   1 
ATOM   4173 O  O   . ALA B 1 61  ? 6.241   -16.201 80.978  1.00 35.66  ? 61   ALA B O   1 
ATOM   4174 C  CB  . ALA B 1 61  ? 3.544   -17.774 81.591  1.00 38.15  ? 61   ALA B CB  1 
ATOM   4175 N  N   . CYS B 1 62  ? 4.651   -14.680 81.490  1.00 35.64  ? 62   CYS B N   1 
ATOM   4176 C  CA  . CYS B 1 62  ? 5.166   -13.604 80.653  1.00 34.44  ? 62   CYS B CA  1 
ATOM   4177 C  C   . CYS B 1 62  ? 6.244   -12.789 81.347  1.00 35.95  ? 62   CYS B C   1 
ATOM   4178 O  O   . CYS B 1 62  ? 6.740   -11.813 80.775  1.00 37.06  ? 62   CYS B O   1 
ATOM   4179 C  CB  . CYS B 1 62  ? 4.018   -12.692 80.209  1.00 36.64  ? 62   CYS B CB  1 
ATOM   4180 S  SG  . CYS B 1 62  ? 2.920   -13.451 78.960  1.00 36.53  ? 62   CYS B SG  1 
ATOM   4181 N  N   . ASP B 1 63  ? 6.618   -13.175 82.556  1.00 35.34  ? 63   ASP B N   1 
ATOM   4182 C  CA  . ASP B 1 63  ? 7.746   -12.567 83.246  1.00 36.66  ? 63   ASP B CA  1 
ATOM   4183 C  C   . ASP B 1 63  ? 9.018   -13.104 82.609  1.00 34.10  ? 63   ASP B C   1 
ATOM   4184 O  O   . ASP B 1 63  ? 9.368   -14.271 82.803  1.00 34.29  ? 63   ASP B O   1 
ATOM   4185 C  CB  . ASP B 1 63  ? 7.669   -12.897 84.733  1.00 36.91  ? 63   ASP B CB  1 
ATOM   4186 C  CG  . ASP B 1 63  ? 8.749   -12.216 85.548  1.00 41.50  ? 63   ASP B CG  1 
ATOM   4187 O  OD1 . ASP B 1 63  ? 9.782   -11.777 84.985  1.00 36.84  ? 63   ASP B OD1 1 
ATOM   4188 O  OD2 . ASP B 1 63  ? 8.551   -12.138 86.771  1.00 42.84  ? 63   ASP B OD2 1 
ATOM   4189 N  N   . GLU B 1 64  ? 9.710   -12.255 81.839  1.00 36.11  ? 64   GLU B N   1 
ATOM   4190 C  CA  . GLU B 1 64  ? 10.879  -12.705 81.090  1.00 35.10  ? 64   GLU B CA  1 
ATOM   4191 C  C   . GLU B 1 64  ? 12.080  -13.000 81.979  1.00 37.93  ? 64   GLU B C   1 
ATOM   4192 O  O   . GLU B 1 64  ? 13.044  -13.621 81.506  1.00 37.60  ? 64   GLU B O   1 
ATOM   4193 C  CB  . GLU B 1 64  ? 11.276  -11.655 80.052  1.00 40.72  ? 64   GLU B CB  1 
ATOM   4194 C  CG  . GLU B 1 64  ? 10.265  -11.474 78.942  1.00 35.15  ? 64   GLU B CG  1 
ATOM   4195 C  CD  . GLU B 1 64  ? 10.668  -10.355 78.006  1.00 41.24  ? 64   GLU B CD  1 
ATOM   4196 O  OE1 . GLU B 1 64  ? 10.492  -9.177  78.374  1.00 46.06  ? 64   GLU B OE1 1 
ATOM   4197 O  OE2 . GLU B 1 64  ? 11.181  -10.653 76.913  1.00 36.51  ? 64   GLU B OE2 1 
ATOM   4198 N  N   . SER B 1 65  ? 12.067  -12.543 83.236  1.00 35.54  ? 65   SER B N   1 
ATOM   4199 C  CA  . SER B 1 65  ? 13.130  -12.939 84.151  1.00 37.88  ? 65   SER B CA  1 
ATOM   4200 C  C   . SER B 1 65  ? 12.955  -14.371 84.606  1.00 37.58  ? 65   SER B C   1 
ATOM   4201 O  O   . SER B 1 65  ? 13.919  -14.981 85.077  1.00 41.09  ? 65   SER B O   1 
ATOM   4202 C  CB  . SER B 1 65  ? 13.185  -12.006 85.370  1.00 41.98  ? 65   SER B CB  1 
ATOM   4203 O  OG  . SER B 1 65  ? 12.110  -12.243 86.276  1.00 41.67  ? 65   SER B OG  1 
ATOM   4204 N  N   . ARG B 1 66  ? 11.749  -14.923 84.464  1.00 36.19  ? 66   ARG B N   1 
ATOM   4205 C  CA  . ARG B 1 66  ? 11.463  -16.272 84.921  1.00 37.21  ? 66   ARG B CA  1 
ATOM   4206 C  C   . ARG B 1 66  ? 11.260  -17.274 83.798  1.00 34.90  ? 66   ARG B C   1 
ATOM   4207 O  O   . ARG B 1 66  ? 11.546  -18.456 83.992  1.00 35.02  ? 66   ARG B O   1 
ATOM   4208 C  CB  . ARG B 1 66  ? 10.217  -16.267 85.811  1.00 37.91  ? 66   ARG B CB  1 
ATOM   4209 C  CG  . ARG B 1 66  ? 10.378  -15.400 87.061  1.00 38.57  ? 66   ARG B CG  1 
ATOM   4210 C  CD  . ARG B 1 66  ? 9.028   -15.217 87.748  1.00 40.76  ? 66   ARG B CD  1 
ATOM   4211 N  NE  . ARG B 1 66  ? 8.533   -16.486 88.258  1.00 40.78  ? 66   ARG B NE  1 
ATOM   4212 C  CZ  . ARG B 1 66  ? 7.282   -16.709 88.638  1.00 38.91  ? 66   ARG B CZ  1 
ATOM   4213 N  NH1 . ARG B 1 66  ? 6.350   -15.774 88.531  1.00 38.40  ? 66   ARG B NH1 1 
ATOM   4214 N  NH2 . ARG B 1 66  ? 6.958   -17.901 89.126  1.00 41.60  ? 66   ARG B NH2 1 
ATOM   4215 N  N   . PHE B 1 67  ? 10.774  -16.835 82.634  1.00 32.56  ? 67   PHE B N   1 
ATOM   4216 C  CA  . PHE B 1 67  ? 10.432  -17.725 81.532  1.00 33.38  ? 67   PHE B CA  1 
ATOM   4217 C  C   . PHE B 1 67  ? 10.925  -17.134 80.221  1.00 33.48  ? 67   PHE B C   1 
ATOM   4218 O  O   . PHE B 1 67  ? 10.800  -15.927 79.996  1.00 35.00  ? 67   PHE B O   1 
ATOM   4219 C  CB  . PHE B 1 67  ? 8.908   -17.957 81.446  1.00 33.58  ? 67   PHE B CB  1 
ATOM   4220 C  CG  . PHE B 1 67  ? 8.322   -18.543 82.703  1.00 34.35  ? 67   PHE B CG  1 
ATOM   4221 C  CD1 . PHE B 1 67  ? 8.319   -19.912 82.897  1.00 35.46  ? 67   PHE B CD1 1 
ATOM   4222 C  CD2 . PHE B 1 67  ? 7.815   -17.723 83.697  1.00 37.30  ? 67   PHE B CD2 1 
ATOM   4223 C  CE1 . PHE B 1 67  ? 7.800   -20.467 84.068  1.00 36.07  ? 67   PHE B CE1 1 
ATOM   4224 C  CE2 . PHE B 1 67  ? 7.288   -18.270 84.882  1.00 35.97  ? 67   PHE B CE2 1 
ATOM   4225 C  CZ  . PHE B 1 67  ? 7.288   -19.647 85.053  1.00 35.81  ? 67   PHE B CZ  1 
ATOM   4226 N  N   . ASP B 1 68  ? 11.461  -17.996 79.352  1.00 34.67  ? 68   ASP B N   1 
ATOM   4227 C  CA  . ASP B 1 68  ? 11.916  -17.635 78.013  1.00 33.50  ? 68   ASP B CA  1 
ATOM   4228 C  C   . ASP B 1 68  ? 11.090  -18.396 76.975  1.00 33.89  ? 68   ASP B C   1 
ATOM   4229 O  O   . ASP B 1 68  ? 10.440  -19.395 77.285  1.00 30.86  ? 68   ASP B O   1 
ATOM   4230 C  CB  . ASP B 1 68  ? 13.423  -17.956 77.884  1.00 33.79  ? 68   ASP B CB  1 
ATOM   4231 C  CG  . ASP B 1 68  ? 14.019  -17.587 76.541  1.00 35.74  ? 68   ASP B CG  1 
ATOM   4232 O  OD1 . ASP B 1 68  ? 13.516  -16.675 75.834  1.00 33.19  ? 68   ASP B OD1 1 
ATOM   4233 O  OD2 . ASP B 1 68  ? 15.041  -18.238 76.194  1.00 34.12  ? 68   ASP B OD2 1 
ATOM   4234 N  N   . LYS B 1 69  ? 11.111  -17.918 75.729  1.00 34.39  ? 69   LYS B N   1 
ATOM   4235 C  CA  . LYS B 1 69  ? 10.402  -18.609 74.650  1.00 32.90  ? 69   LYS B CA  1 
ATOM   4236 C  C   . LYS B 1 69  ? 10.911  -20.036 74.459  1.00 34.44  ? 69   LYS B C   1 
ATOM   4237 O  O   . LYS B 1 69  ? 12.119  -20.277 74.369  1.00 33.82  ? 69   LYS B O   1 
ATOM   4238 C  CB  . LYS B 1 69  ? 10.552  -17.840 73.332  1.00 32.07  ? 69   LYS B CB  1 
ATOM   4239 C  CG  . LYS B 1 69  ? 10.206  -18.688 72.101  1.00 33.95  ? 69   LYS B CG  1 
ATOM   4240 C  CD  . LYS B 1 69  ? 9.828   -17.808 70.904  1.00 30.95  ? 69   LYS B CD  1 
ATOM   4241 C  CE  . LYS B 1 69  ? 9.695   -18.647 69.618  1.00 31.49  ? 69   LYS B CE  1 
ATOM   4242 N  NZ  . LYS B 1 69  ? 8.808   -18.004 68.545  1.00 28.95  ? 69   LYS B NZ  1 
ATOM   4243 N  N   . ASN B 1 70  ? 9.979   -20.980 74.336  1.00 31.29  ? 70   ASN B N   1 
ATOM   4244 C  CA  . ASN B 1 70  ? 10.283  -22.367 74.033  1.00 31.10  ? 70   ASN B CA  1 
ATOM   4245 C  C   . ASN B 1 70  ? 9.805   -22.689 72.622  1.00 31.60  ? 70   ASN B C   1 
ATOM   4246 O  O   . ASN B 1 70  ? 8.821   -22.122 72.141  1.00 33.01  ? 70   ASN B O   1 
ATOM   4247 C  CB  . ASN B 1 70  ? 9.610   -23.301 75.054  1.00 33.62  ? 70   ASN B CB  1 
ATOM   4248 C  CG  . ASN B 1 70  ? 9.881   -24.763 74.772  1.00 37.88  ? 70   ASN B CG  1 
ATOM   4249 O  OD1 . ASN B 1 70  ? 11.032  -25.176 74.635  1.00 35.27  ? 70   ASN B OD1 1 
ATOM   4250 N  ND2 . ASN B 1 70  ? 8.824   -25.550 74.658  1.00 35.27  ? 70   ASN B ND2 1 
ATOM   4251 N  N   . LEU B 1 71  ? 10.515  -23.587 71.943  1.00 32.50  ? 71   LEU B N   1 
ATOM   4252 C  CA  . LEU B 1 71  ? 10.015  -24.153 70.695  1.00 30.78  ? 71   LEU B CA  1 
ATOM   4253 C  C   . LEU B 1 71  ? 9.098   -25.314 71.059  1.00 31.88  ? 71   LEU B C   1 
ATOM   4254 O  O   . LEU B 1 71  ? 9.561   -26.359 71.529  1.00 32.07  ? 71   LEU B O   1 
ATOM   4255 C  CB  . LEU B 1 71  ? 11.161  -24.614 69.793  1.00 31.74  ? 71   LEU B CB  1 
ATOM   4256 C  CG  . LEU B 1 71  ? 12.179  -23.541 69.369  1.00 31.00  ? 71   LEU B CG  1 
ATOM   4257 C  CD1 . LEU B 1 71  ? 13.120  -24.086 68.281  1.00 33.12  ? 71   LEU B CD1 1 
ATOM   4258 C  CD2 . LEU B 1 71  ? 11.511  -22.236 68.882  1.00 34.14  ? 71   LEU B CD2 1 
ATOM   4259 N  N   . SER B 1 72  ? 7.792   -25.111 70.881  1.00 32.82  ? 72   SER B N   1 
ATOM   4260 C  CA  . SER B 1 72  ? 6.829   -26.203 70.893  1.00 34.16  ? 72   SER B CA  1 
ATOM   4261 C  C   . SER B 1 72  ? 7.207   -27.259 69.858  1.00 32.21  ? 72   SER B C   1 
ATOM   4262 O  O   . SER B 1 72  ? 8.011   -27.019 68.958  1.00 33.78  ? 72   SER B O   1 
ATOM   4263 C  CB  . SER B 1 72  ? 5.430   -25.665 70.580  1.00 29.63  ? 72   SER B CB  1 
ATOM   4264 O  OG  . SER B 1 72  ? 5.447   -25.006 69.313  1.00 31.07  ? 72   SER B OG  1 
ATOM   4265 N  N   . GLN B 1 73  ? 6.619   -28.451 69.982  1.00 32.49  ? 73   GLN B N   1 
ATOM   4266 C  CA  . GLN B 1 73  ? 6.828   -29.438 68.927  1.00 34.12  ? 73   GLN B CA  1 
ATOM   4267 C  C   . GLN B 1 73  ? 6.444   -28.864 67.570  1.00 32.29  ? 73   GLN B C   1 
ATOM   4268 O  O   . GLN B 1 73  ? 7.145   -29.072 66.569  1.00 32.79  ? 73   GLN B O   1 
ATOM   4269 C  CB  . GLN B 1 73  ? 6.040   -30.719 69.211  1.00 36.83  ? 73   GLN B CB  1 
ATOM   4270 C  CG  . GLN B 1 73  ? 6.534   -31.886 68.392  1.00 42.41  ? 73   GLN B CG  1 
ATOM   4271 C  CD  . GLN B 1 73  ? 7.988   -32.184 68.677  1.00 45.98  ? 73   GLN B CD  1 
ATOM   4272 O  OE1 . GLN B 1 73  ? 8.357   -32.487 69.817  1.00 43.08  ? 73   GLN B OE1 1 
ATOM   4273 N  NE2 . GLN B 1 73  ? 8.833   -32.045 67.656  1.00 43.74  ? 73   GLN B NE2 1 
ATOM   4274 N  N   . ALA B 1 74  ? 5.342   -28.113 67.511  1.00 29.96  ? 74   ALA B N   1 
ATOM   4275 C  CA  . ALA B 1 74  ? 4.947   -27.504 66.247  1.00 33.60  ? 74   ALA B CA  1 
ATOM   4276 C  C   . ALA B 1 74  ? 6.080   -26.661 65.667  1.00 32.80  ? 74   ALA B C   1 
ATOM   4277 O  O   . ALA B 1 74  ? 6.400   -26.760 64.477  1.00 31.92  ? 74   ALA B O   1 
ATOM   4278 C  CB  . ALA B 1 74  ? 3.695   -26.653 66.446  1.00 33.66  ? 74   ALA B CB  1 
ATOM   4279 N  N   . LEU B 1 75  ? 6.685   -25.810 66.494  1.00 31.80  ? 75   LEU B N   1 
ATOM   4280 C  CA  . LEU B 1 75  ? 7.737   -24.951 65.961  1.00 29.01  ? 75   LEU B CA  1 
ATOM   4281 C  C   . LEU B 1 75  ? 8.997   -25.759 65.658  1.00 30.53  ? 75   LEU B C   1 
ATOM   4282 O  O   . LEU B 1 75  ? 9.743   -25.410 64.738  1.00 31.56  ? 75   LEU B O   1 
ATOM   4283 C  CB  . LEU B 1 75  ? 8.056   -23.808 66.930  1.00 32.24  ? 75   LEU B CB  1 
ATOM   4284 C  CG  . LEU B 1 75  ? 6.998   -22.707 67.149  1.00 32.71  ? 75   LEU B CG  1 
ATOM   4285 C  CD1 . LEU B 1 75  ? 7.629   -21.542 67.935  1.00 32.84  ? 75   LEU B CD1 1 
ATOM   4286 C  CD2 . LEU B 1 75  ? 6.378   -22.220 65.826  1.00 30.90  ? 75   LEU B CD2 1 
ATOM   4287 N  N   . LYS B 1 76  ? 9.262   -26.829 66.419  1.00 30.31  ? 76   LYS B N   1 
ATOM   4288 C  CA  . LYS B 1 76  ? 10.397  -27.676 66.055  1.00 34.02  ? 76   LYS B CA  1 
ATOM   4289 C  C   . LYS B 1 76  ? 10.191  -28.275 64.667  1.00 34.02  ? 76   LYS B C   1 
ATOM   4290 O  O   . LYS B 1 76  ? 11.132  -28.354 63.858  1.00 34.03  ? 76   LYS B O   1 
ATOM   4291 C  CB  . LYS B 1 76  ? 10.605  -28.769 67.104  1.00 34.87  ? 76   LYS B CB  1 
ATOM   4292 C  CG  . LYS B 1 76  ? 11.149  -28.223 68.423  1.00 35.90  ? 76   LYS B CG  1 
ATOM   4293 C  CD  . LYS B 1 76  ? 11.343  -29.327 69.429  1.00 38.16  ? 76   LYS B CD  1 
ATOM   4294 C  CE  . LYS B 1 76  ? 11.919  -28.772 70.714  1.00 44.14  ? 76   LYS B CE  1 
ATOM   4295 N  NZ  . LYS B 1 76  ? 11.847  -29.779 71.791  1.00 49.45  ? 76   LYS B NZ  1 
ATOM   4296 N  N   . PHE B 1 77  ? 8.949   -28.665 64.357  1.00 33.12  ? 77   PHE B N   1 
ATOM   4297 C  CA  . PHE B 1 77  ? 8.652   -29.225 63.042  1.00 35.70  ? 77   PHE B CA  1 
ATOM   4298 C  C   . PHE B 1 77  ? 8.732   -28.160 61.954  1.00 36.21  ? 77   PHE B C   1 
ATOM   4299 O  O   . PHE B 1 77  ? 9.268   -28.413 60.870  1.00 35.29  ? 77   PHE B O   1 
ATOM   4300 C  CB  . PHE B 1 77  ? 7.263   -29.877 63.059  1.00 33.32  ? 77   PHE B CB  1 
ATOM   4301 C  CG  . PHE B 1 77  ? 7.199   -31.162 63.846  1.00 36.13  ? 77   PHE B CG  1 
ATOM   4302 C  CD1 . PHE B 1 77  ? 8.342   -31.906 64.088  1.00 40.86  ? 77   PHE B CD1 1 
ATOM   4303 C  CD2 . PHE B 1 77  ? 5.993   -31.638 64.321  1.00 36.69  ? 77   PHE B CD2 1 
ATOM   4304 C  CE1 . PHE B 1 77  ? 8.274   -33.099 64.789  1.00 41.84  ? 77   PHE B CE1 1 
ATOM   4305 C  CE2 . PHE B 1 77  ? 5.918   -32.823 65.034  1.00 39.79  ? 77   PHE B CE2 1 
ATOM   4306 C  CZ  . PHE B 1 77  ? 7.061   -33.552 65.268  1.00 44.34  ? 77   PHE B CZ  1 
ATOM   4307 N  N   . VAL B 1 78  ? 8.191   -26.968 62.217  1.00 32.14  ? 78   VAL B N   1 
ATOM   4308 C  CA  . VAL B 1 78  ? 8.268   -25.883 61.244  1.00 31.97  ? 78   VAL B CA  1 
ATOM   4309 C  C   . VAL B 1 78  ? 9.722   -25.481 61.022  1.00 33.71  ? 78   VAL B C   1 
ATOM   4310 O  O   . VAL B 1 78  ? 10.091  -25.023 59.940  1.00 32.41  ? 78   VAL B O   1 
ATOM   4311 C  CB  . VAL B 1 78  ? 7.401   -24.701 61.724  1.00 37.42  ? 78   VAL B CB  1 
ATOM   4312 C  CG1 . VAL B 1 78  ? 7.870   -23.401 61.114  1.00 40.59  ? 78   VAL B CG1 1 
ATOM   4313 C  CG2 . VAL B 1 78  ? 5.933   -24.973 61.392  1.00 39.52  ? 78   VAL B CG2 1 
ATOM   4314 N  N   . ARG B 1 79  ? 10.569  -25.669 62.034  1.00 33.24  ? 79   ARG B N   1 
ATOM   4315 C  CA  . ARG B 1 79  ? 11.983  -25.317 61.901  1.00 34.04  ? 79   ARG B CA  1 
ATOM   4316 C  C   . ARG B 1 79  ? 12.685  -26.148 60.826  1.00 38.90  ? 79   ARG B C   1 
ATOM   4317 O  O   . ARG B 1 79  ? 13.759  -25.750 60.339  1.00 34.72  ? 79   ARG B O   1 
ATOM   4318 C  CB  . ARG B 1 79  ? 12.676  -25.487 63.264  1.00 32.20  ? 79   ARG B CB  1 
ATOM   4319 C  CG  . ARG B 1 79  ? 14.183  -25.242 63.226  1.00 34.04  ? 79   ARG B CG  1 
ATOM   4320 C  CD  . ARG B 1 79  ? 14.733  -24.915 64.605  1.00 34.20  ? 79   ARG B CD  1 
ATOM   4321 N  NE  . ARG B 1 79  ? 16.190  -24.843 64.555  1.00 38.09  ? 79   ARG B NE  1 
ATOM   4322 C  CZ  . ARG B 1 79  ? 16.922  -23.937 65.191  1.00 40.03  ? 79   ARG B CZ  1 
ATOM   4323 N  NH1 . ARG B 1 79  ? 16.365  -23.003 65.941  1.00 34.54  ? 79   ARG B NH1 1 
ATOM   4324 N  NH2 . ARG B 1 79  ? 18.250  -23.970 65.064  1.00 38.78  ? 79   ARG B NH2 1 
ATOM   4325 N  N   . ASP B 1 80  ? 12.107  -27.288 60.427  1.00 34.03  ? 80   ASP B N   1 
ATOM   4326 C  CA  . ASP B 1 80  ? 12.725  -28.065 59.362  1.00 36.45  ? 80   ASP B CA  1 
ATOM   4327 C  C   . ASP B 1 80  ? 12.813  -27.269 58.069  1.00 37.61  ? 80   ASP B C   1 
ATOM   4328 O  O   . ASP B 1 80  ? 13.690  -27.548 57.241  1.00 38.02  ? 80   ASP B O   1 
ATOM   4329 C  CB  . ASP B 1 80  ? 11.965  -29.379 59.121  1.00 36.29  ? 80   ASP B CB  1 
ATOM   4330 C  CG  . ASP B 1 80  ? 12.194  -30.401 60.223  1.00 45.30  ? 80   ASP B CG  1 
ATOM   4331 O  OD1 . ASP B 1 80  ? 13.130  -30.227 61.030  1.00 43.48  ? 80   ASP B OD1 1 
ATOM   4332 O  OD2 . ASP B 1 80  ? 11.427  -31.383 60.291  1.00 46.80  ? 80   ASP B OD2 1 
ATOM   4333 N  N   . PHE B 1 81  ? 11.933  -26.280 57.870  1.00 34.04  ? 81   PHE B N   1 
ATOM   4334 C  CA  . PHE B 1 81  ? 12.082  -25.372 56.742  1.00 36.50  ? 81   PHE B CA  1 
ATOM   4335 C  C   . PHE B 1 81  ? 12.311  -23.913 57.134  1.00 35.04  ? 81   PHE B C   1 
ATOM   4336 O  O   . PHE B 1 81  ? 12.844  -23.162 56.312  1.00 34.95  ? 81   PHE B O   1 
ATOM   4337 C  CB  . PHE B 1 81  ? 10.878  -25.481 55.780  1.00 34.55  ? 81   PHE B CB  1 
ATOM   4338 C  CG  . PHE B 1 81  ? 9.516   -25.262 56.413  1.00 34.11  ? 81   PHE B CG  1 
ATOM   4339 C  CD1 . PHE B 1 81  ? 8.987   -23.988 56.529  1.00 33.83  ? 81   PHE B CD1 1 
ATOM   4340 C  CD2 . PHE B 1 81  ? 8.739   -26.343 56.824  1.00 35.38  ? 81   PHE B CD2 1 
ATOM   4341 C  CE1 . PHE B 1 81  ? 7.720   -23.779 57.080  1.00 34.92  ? 81   PHE B CE1 1 
ATOM   4342 C  CE2 . PHE B 1 81  ? 7.460   -26.143 57.378  1.00 35.07  ? 81   PHE B CE2 1 
ATOM   4343 C  CZ  . PHE B 1 81  ? 6.958   -24.860 57.504  1.00 37.15  ? 81   PHE B CZ  1 
ATOM   4344 N  N   . ALA B 1 82  ? 11.991  -23.499 58.367  1.00 34.23  ? 82   ALA B N   1 
ATOM   4345 C  CA  . ALA B 1 82  ? 12.249  -22.120 58.771  1.00 35.63  ? 82   ALA B CA  1 
ATOM   4346 C  C   . ALA B 1 82  ? 13.561  -21.940 59.532  1.00 33.96  ? 82   ALA B C   1 
ATOM   4347 O  O   . ALA B 1 82  ? 13.946  -20.797 59.787  1.00 34.56  ? 82   ALA B O   1 
ATOM   4348 C  CB  . ALA B 1 82  ? 11.090  -21.575 59.629  1.00 33.02  ? 82   ALA B CB  1 
ATOM   4349 N  N   . GLY B 1 83  ? 14.233  -23.023 59.909  1.00 33.00  ? 83   GLY B N   1 
ATOM   4350 C  CA  . GLY B 1 83  ? 15.593  -22.954 60.430  1.00 32.03  ? 83   GLY B CA  1 
ATOM   4351 C  C   . GLY B 1 83  ? 15.732  -22.057 61.647  1.00 34.81  ? 83   GLY B C   1 
ATOM   4352 O  O   . GLY B 1 83  ? 14.886  -22.050 62.551  1.00 32.50  ? 83   GLY B O   1 
ATOM   4353 N  N   . ASP B 1 84  ? 16.822  -21.284 61.685  1.00 33.89  ? 84   ASP B N   1 
ATOM   4354 C  CA  . ASP B 1 84  ? 16.997  -20.309 62.761  1.00 31.67  ? 84   ASP B CA  1 
ATOM   4355 C  C   . ASP B 1 84  ? 16.590  -18.910 62.323  1.00 34.51  ? 84   ASP B C   1 
ATOM   4356 O  O   . ASP B 1 84  ? 17.204  -17.918 62.726  1.00 32.71  ? 84   ASP B O   1 
ATOM   4357 C  CB  . ASP B 1 84  ? 18.427  -20.338 63.321  1.00 31.52  ? 84   ASP B CB  1 
ATOM   4358 C  CG  . ASP B 1 84  ? 19.490  -20.034 62.286  1.00 34.73  ? 84   ASP B CG  1 
ATOM   4359 O  OD1 . ASP B 1 84  ? 19.191  -19.953 61.082  1.00 34.27  ? 84   ASP B OD1 1 
ATOM   4360 O  OD2 . ASP B 1 84  ? 20.667  -19.895 62.702  1.00 37.13  ? 84   ASP B OD2 1 
ATOM   4361 N  N   . GLY B 1 85  ? 15.533  -18.814 61.506  1.00 30.63  ? 85   GLY B N   1 
ATOM   4362 C  CA  . GLY B 1 85  ? 14.839  -17.549 61.320  1.00 31.48  ? 85   GLY B CA  1 
ATOM   4363 C  C   . GLY B 1 85  ? 14.250  -17.054 62.634  1.00 34.05  ? 85   GLY B C   1 
ATOM   4364 O  O   . GLY B 1 85  ? 14.255  -17.746 63.650  1.00 32.21  ? 85   GLY B O   1 
ATOM   4365 N  N   . LEU B 1 86  ? 13.704  -15.828 62.604  1.00 30.23  ? 86   LEU B N   1 
ATOM   4366 C  CA  . LEU B 1 86  ? 13.307  -15.176 63.855  1.00 29.07  ? 86   LEU B CA  1 
ATOM   4367 C  C   . LEU B 1 86  ? 12.224  -15.963 64.585  1.00 30.32  ? 86   LEU B C   1 
ATOM   4368 O  O   . LEU B 1 86  ? 12.186  -15.983 65.820  1.00 30.79  ? 86   LEU B O   1 
ATOM   4369 C  CB  . LEU B 1 86  ? 12.824  -13.746 63.574  1.00 31.52  ? 86   LEU B CB  1 
ATOM   4370 C  CG  . LEU B 1 86  ? 13.953  -12.727 63.388  1.00 32.21  ? 86   LEU B CG  1 
ATOM   4371 C  CD1 . LEU B 1 86  ? 13.347  -11.385 63.028  1.00 36.03  ? 86   LEU B CD1 1 
ATOM   4372 C  CD2 . LEU B 1 86  ? 14.766  -12.625 64.689  1.00 32.22  ? 86   LEU B CD2 1 
ATOM   4373 N  N   . PHE B 1 87  ? 11.311  -16.593 63.839  1.00 32.21  ? 87   PHE B N   1 
ATOM   4374 C  CA  . PHE B 1 87  ? 10.170  -17.241 64.493  1.00 30.72  ? 87   PHE B CA  1 
ATOM   4375 C  C   . PHE B 1 87  ? 10.563  -18.550 65.181  1.00 32.29  ? 87   PHE B C   1 
ATOM   4376 O  O   . PHE B 1 87  ? 9.947   -18.936 66.182  1.00 31.86  ? 87   PHE B O   1 
ATOM   4377 C  CB  . PHE B 1 87  ? 9.060   -17.484 63.464  1.00 30.75  ? 87   PHE B CB  1 
ATOM   4378 C  CG  . PHE B 1 87  ? 7.637   -17.452 64.044  1.00 30.57  ? 87   PHE B CG  1 
ATOM   4379 C  CD1 . PHE B 1 87  ? 7.176   -18.496 64.823  1.00 32.94  ? 87   PHE B CD1 1 
ATOM   4380 C  CD2 . PHE B 1 87  ? 6.781   -16.388 63.772  1.00 32.78  ? 87   PHE B CD2 1 
ATOM   4381 C  CE1 . PHE B 1 87  ? 5.874   -18.499 65.345  1.00 35.05  ? 87   PHE B CE1 1 
ATOM   4382 C  CE2 . PHE B 1 87  ? 5.460   -16.373 64.299  1.00 32.24  ? 87   PHE B CE2 1 
ATOM   4383 C  CZ  . PHE B 1 87  ? 5.023   -17.426 65.080  1.00 32.68  ? 87   PHE B CZ  1 
ATOM   4384 N  N   . THR B 1 88  ? 11.584  -19.249 64.677  1.00 31.37  ? 88   THR B N   1 
ATOM   4385 C  CA  . THR B 1 88  ? 11.892  -20.597 65.143  1.00 31.70  ? 88   THR B CA  1 
ATOM   4386 C  C   . THR B 1 88  ? 13.291  -20.727 65.737  1.00 31.65  ? 88   THR B C   1 
ATOM   4387 O  O   . THR B 1 88  ? 13.768  -21.849 65.938  1.00 32.92  ? 88   THR B O   1 
ATOM   4388 C  CB  . THR B 1 88  ? 11.715  -21.603 64.005  1.00 32.40  ? 88   THR B CB  1 
ATOM   4389 O  OG1 . THR B 1 88  ? 12.374  -21.127 62.820  1.00 31.85  ? 88   THR B OG1 1 
ATOM   4390 C  CG2 . THR B 1 88  ? 10.226  -21.756 63.705  1.00 32.37  ? 88   THR B CG2 1 
ATOM   4391 N  N   . SER B 1 89  ? 13.948  -19.616 66.029  1.00 33.34  ? 89   SER B N   1 
ATOM   4392 C  CA  . SER B 1 89  ? 15.222  -19.630 66.742  1.00 30.19  ? 89   SER B CA  1 
ATOM   4393 C  C   . SER B 1 89  ? 15.016  -19.541 68.254  1.00 32.69  ? 89   SER B C   1 
ATOM   4394 O  O   . SER B 1 89  ? 14.027  -18.986 68.749  1.00 32.62  ? 89   SER B O   1 
ATOM   4395 C  CB  . SER B 1 89  ? 16.102  -18.469 66.267  1.00 34.08  ? 89   SER B CB  1 
ATOM   4396 O  OG  . SER B 1 89  ? 15.356  -17.259 66.267  1.00 38.25  ? 89   SER B OG  1 
ATOM   4397 N  N   . TRP B 1 90  ? 15.970  -20.101 68.993  1.00 32.62  ? 90   TRP B N   1 
ATOM   4398 C  CA  . TRP B 1 90  ? 16.008  -19.921 70.433  1.00 30.52  ? 90   TRP B CA  1 
ATOM   4399 C  C   . TRP B 1 90  ? 16.610  -18.555 70.744  1.00 32.91  ? 90   TRP B C   1 
ATOM   4400 O  O   . TRP B 1 90  ? 17.438  -18.034 69.989  1.00 32.14  ? 90   TRP B O   1 
ATOM   4401 C  CB  . TRP B 1 90  ? 16.849  -21.012 71.104  1.00 31.16  ? 90   TRP B CB  1 
ATOM   4402 C  CG  . TRP B 1 90  ? 16.376  -22.411 70.856  1.00 34.50  ? 90   TRP B CG  1 
ATOM   4403 C  CD1 . TRP B 1 90  ? 16.759  -23.241 69.845  1.00 32.10  ? 90   TRP B CD1 1 
ATOM   4404 C  CD2 . TRP B 1 90  ? 15.443  -23.151 71.652  1.00 34.11  ? 90   TRP B CD2 1 
ATOM   4405 N  NE1 . TRP B 1 90  ? 16.133  -24.457 69.963  1.00 33.22  ? 90   TRP B NE1 1 
ATOM   4406 C  CE2 . TRP B 1 90  ? 15.309  -24.425 71.060  1.00 35.14  ? 90   TRP B CE2 1 
ATOM   4407 C  CE3 . TRP B 1 90  ? 14.711  -22.862 72.814  1.00 36.35  ? 90   TRP B CE3 1 
ATOM   4408 C  CZ2 . TRP B 1 90  ? 14.470  -25.412 71.590  1.00 35.11  ? 90   TRP B CZ2 1 
ATOM   4409 C  CZ3 . TRP B 1 90  ? 13.871  -23.845 73.338  1.00 34.37  ? 90   TRP B CZ3 1 
ATOM   4410 C  CH2 . TRP B 1 90  ? 13.764  -25.103 72.726  1.00 34.35  ? 90   TRP B CH2 1 
ATOM   4411 N  N   . THR B 1 91  ? 16.171  -17.970 71.853  1.00 30.94  ? 91   THR B N   1 
ATOM   4412 C  CA  . THR B 1 91  ? 16.650  -16.641 72.216  1.00 32.40  ? 91   THR B CA  1 
ATOM   4413 C  C   . THR B 1 91  ? 18.166  -16.617 72.372  1.00 33.93  ? 91   THR B C   1 
ATOM   4414 O  O   . THR B 1 91  ? 18.791  -15.576 72.141  1.00 34.07  ? 91   THR B O   1 
ATOM   4415 C  CB  . THR B 1 91  ? 15.957  -16.177 73.498  1.00 31.84  ? 91   THR B CB  1 
ATOM   4416 O  OG1 . THR B 1 91  ? 14.533  -16.252 73.308  1.00 33.39  ? 91   THR B OG1 1 
ATOM   4417 C  CG2 . THR B 1 91  ? 16.367  -14.739 73.860  1.00 35.18  ? 91   THR B CG2 1 
ATOM   4418 N  N   . HIS B 1 92  ? 18.770  -17.751 72.745  1.00 32.95  ? 92   HIS B N   1 
ATOM   4419 C  CA  . HIS B 1 92  ? 20.203  -17.812 73.002  1.00 32.98  ? 92   HIS B CA  1 
ATOM   4420 C  C   . HIS B 1 92  ? 21.030  -18.153 71.768  1.00 35.73  ? 92   HIS B C   1 
ATOM   4421 O  O   . HIS B 1 92  ? 22.269  -18.116 71.842  1.00 34.13  ? 92   HIS B O   1 
ATOM   4422 C  CB  . HIS B 1 92  ? 20.474  -18.832 74.114  1.00 34.38  ? 92   HIS B CB  1 
ATOM   4423 C  CG  . HIS B 1 92  ? 19.848  -20.170 73.863  1.00 32.76  ? 92   HIS B CG  1 
ATOM   4424 N  ND1 . HIS B 1 92  ? 20.396  -21.091 72.999  1.00 35.94  ? 92   HIS B ND1 1 
ATOM   4425 C  CD2 . HIS B 1 92  ? 18.728  -20.748 74.372  1.00 33.88  ? 92   HIS B CD2 1 
ATOM   4426 C  CE1 . HIS B 1 92  ? 19.640  -22.176 72.979  1.00 34.53  ? 92   HIS B CE1 1 
ATOM   4427 N  NE2 . HIS B 1 92  ? 18.629  -22.000 73.812  1.00 34.47  ? 92   HIS B NE2 1 
ATOM   4428 N  N   . GLU B 1 93  ? 20.399  -18.462 70.632  1.00 31.86  ? 93   GLU B N   1 
ATOM   4429 C  CA  . GLU B 1 93  ? 21.157  -18.626 69.401  1.00 30.22  ? 93   GLU B CA  1 
ATOM   4430 C  C   . GLU B 1 93  ? 21.625  -17.268 68.896  1.00 31.34  ? 93   GLU B C   1 
ATOM   4431 O  O   . GLU B 1 93  ? 20.859  -16.303 68.868  1.00 32.04  ? 93   GLU B O   1 
ATOM   4432 C  CB  . GLU B 1 93  ? 20.307  -19.314 68.333  1.00 33.17  ? 93   GLU B CB  1 
ATOM   4433 C  CG  . GLU B 1 93  ? 20.075  -20.793 68.619  1.00 32.74  ? 93   GLU B CG  1 
ATOM   4434 C  CD  . GLU B 1 93  ? 19.225  -21.441 67.539  1.00 36.79  ? 93   GLU B CD  1 
ATOM   4435 O  OE1 . GLU B 1 93  ? 17.998  -21.243 67.536  1.00 35.39  ? 93   GLU B OE1 1 
ATOM   4436 O  OE2 . GLU B 1 93  ? 19.803  -22.131 66.681  1.00 36.14  ? 93   GLU B OE2 1 
ATOM   4437 N  N   . LYS B 1 94  ? 22.890  -17.203 68.469  1.00 33.00  ? 94   LYS B N   1 
ATOM   4438 C  CA  . LYS B 1 94  ? 23.456  -15.930 68.027  1.00 34.99  ? 94   LYS B CA  1 
ATOM   4439 C  C   . LYS B 1 94  ? 22.572  -15.258 66.980  1.00 31.33  ? 94   LYS B C   1 
ATOM   4440 O  O   . LYS B 1 94  ? 22.371  -14.037 67.018  1.00 35.19  ? 94   LYS B O   1 
ATOM   4441 C  CB  . LYS B 1 94  ? 24.881  -16.154 67.489  1.00 34.90  ? 94   LYS B CB  1 
ATOM   4442 C  CG  . LYS B 1 94  ? 25.509  -14.930 66.810  1.00 35.85  ? 94   LYS B CG  1 
ATOM   4443 C  CD  . LYS B 1 94  ? 26.977  -15.210 66.438  1.00 35.75  ? 94   LYS B CD  1 
ATOM   4444 C  CE  . LYS B 1 94  ? 27.585  -14.059 65.661  1.00 38.60  ? 94   LYS B CE  1 
ATOM   4445 N  NZ  . LYS B 1 94  ? 29.033  -14.291 65.337  1.00 43.34  ? 94   LYS B NZ  1 
ATOM   4446 N  N   . ASN B 1 95  ? 22.012  -16.042 66.055  1.00 32.46  ? 95   ASN B N   1 
ATOM   4447 C  CA  . ASN B 1 95  ? 21.234  -15.459 64.968  1.00 34.16  ? 95   ASN B CA  1 
ATOM   4448 C  C   . ASN B 1 95  ? 19.891  -14.876 65.411  1.00 34.31  ? 95   ASN B C   1 
ATOM   4449 O  O   . ASN B 1 95  ? 19.289  -14.123 64.632  1.00 33.03  ? 95   ASN B O   1 
ATOM   4450 C  CB  . ASN B 1 95  ? 21.006  -16.500 63.870  1.00 33.84  ? 95   ASN B CB  1 
ATOM   4451 C  CG  . ASN B 1 95  ? 22.163  -16.574 62.880  1.00 35.41  ? 95   ASN B CG  1 
ATOM   4452 O  OD1 . ASN B 1 95  ? 22.919  -15.619 62.721  1.00 38.60  ? 95   ASN B OD1 1 
ATOM   4453 N  ND2 . ASN B 1 95  ? 22.301  -17.716 62.211  1.00 31.64  ? 95   ASN B ND2 1 
ATOM   4454 N  N   . TRP B 1 96  ? 19.397  -15.165 66.617  1.00 31.35  ? 96   TRP B N   1 
ATOM   4455 C  CA  . TRP B 1 96  ? 18.151  -14.506 67.012  1.00 32.10  ? 96   TRP B CA  1 
ATOM   4456 C  C   . TRP B 1 96  ? 18.382  -13.011 67.235  1.00 33.34  ? 96   TRP B C   1 
ATOM   4457 O  O   . TRP B 1 96  ? 17.838  -12.170 66.507  1.00 33.93  ? 96   TRP B O   1 
ATOM   4458 C  CB  . TRP B 1 96  ? 17.497  -15.142 68.258  1.00 33.19  ? 96   TRP B CB  1 
ATOM   4459 C  CG  . TRP B 1 96  ? 16.304  -14.285 68.524  1.00 32.32  ? 96   TRP B CG  1 
ATOM   4460 C  CD1 . TRP B 1 96  ? 15.153  -14.217 67.747  1.00 32.69  ? 96   TRP B CD1 1 
ATOM   4461 C  CD2 . TRP B 1 96  ? 16.188  -13.230 69.492  1.00 32.84  ? 96   TRP B CD2 1 
ATOM   4462 N  NE1 . TRP B 1 96  ? 14.330  -13.218 68.221  1.00 31.61  ? 96   TRP B NE1 1 
ATOM   4463 C  CE2 . TRP B 1 96  ? 14.936  -12.602 69.287  1.00 31.27  ? 96   TRP B CE2 1 
ATOM   4464 C  CE3 . TRP B 1 96  ? 17.000  -12.783 70.543  1.00 32.91  ? 96   TRP B CE3 1 
ATOM   4465 C  CZ2 . TRP B 1 96  ? 14.490  -11.539 70.088  1.00 35.58  ? 96   TRP B CZ2 1 
ATOM   4466 C  CZ3 . TRP B 1 96  ? 16.558  -11.724 71.333  1.00 33.92  ? 96   TRP B CZ3 1 
ATOM   4467 C  CH2 . TRP B 1 96  ? 15.305  -11.118 71.103  1.00 37.30  ? 96   TRP B CH2 1 
ATOM   4468 N  N   . LYS B 1 97  ? 19.225  -12.652 68.210  1.00 31.95  ? 97   LYS B N   1 
ATOM   4469 C  CA  . LYS B 1 97  ? 19.395  -11.230 68.500  1.00 31.25  ? 97   LYS B CA  1 
ATOM   4470 C  C   . LYS B 1 97  ? 19.981  -10.501 67.303  1.00 30.08  ? 97   LYS B C   1 
ATOM   4471 O  O   . LYS B 1 97  ? 19.638  -9.341  67.042  1.00 33.75  ? 97   LYS B O   1 
ATOM   4472 C  CB  . LYS B 1 97  ? 20.291  -11.024 69.725  1.00 29.02  ? 97   LYS B CB  1 
ATOM   4473 C  CG  . LYS B 1 97  ? 20.302  -9.571  70.238  1.00 35.81  ? 97   LYS B CG  1 
ATOM   4474 C  CD  . LYS B 1 97  ? 18.891  -9.087  70.613  1.00 39.62  ? 97   LYS B CD  1 
ATOM   4475 C  CE  . LYS B 1 97  ? 18.873  -7.638  71.139  1.00 45.39  ? 97   LYS B CE  1 
ATOM   4476 N  NZ  . LYS B 1 97  ? 19.674  -7.495  72.389  1.00 50.48  ? 97   LYS B NZ  1 
ATOM   4477 N  N   . LYS B 1 98  ? 20.858  -11.171 66.566  1.00 32.28  ? 98   LYS B N   1 
ATOM   4478 C  CA  . LYS B 1 98  ? 21.498  -10.541 65.422  1.00 33.28  ? 98   LYS B CA  1 
ATOM   4479 C  C   . LYS B 1 98  ? 20.473  -10.155 64.361  1.00 36.17  ? 98   LYS B C   1 
ATOM   4480 O  O   . LYS B 1 98  ? 20.460  -9.015  63.871  1.00 32.47  ? 98   LYS B O   1 
ATOM   4481 C  CB  . LYS B 1 98  ? 22.553  -11.494 64.869  1.00 34.47  ? 98   LYS B CB  1 
ATOM   4482 C  CG  . LYS B 1 98  ? 23.218  -11.022 63.625  1.00 36.82  ? 98   LYS B CG  1 
ATOM   4483 C  CD  . LYS B 1 98  ? 24.300  -12.019 63.206  1.00 35.24  ? 98   LYS B CD  1 
ATOM   4484 C  CE  . LYS B 1 98  ? 24.876  -11.660 61.880  1.00 33.80  ? 98   LYS B CE  1 
ATOM   4485 N  NZ  . LYS B 1 98  ? 25.963  -12.612 61.560  1.00 35.68  ? 98   LYS B NZ  1 
ATOM   4486 N  N   . ALA B 1 99  ? 19.609  -11.099 63.981  1.00 34.27  ? 99   ALA B N   1 
ATOM   4487 C  CA  . ALA B 1 99  ? 18.588  -10.795 62.979  1.00 32.23  ? 99   ALA B CA  1 
ATOM   4488 C  C   . ALA B 1 99  ? 17.553  -9.816  63.518  1.00 33.36  ? 99   ALA B C   1 
ATOM   4489 O  O   . ALA B 1 99  ? 17.046  -8.966  62.773  1.00 33.98  ? 99   ALA B O   1 
ATOM   4490 C  CB  . ALA B 1 99  ? 17.911  -12.079 62.510  1.00 33.54  ? 99   ALA B CB  1 
ATOM   4491 N  N   . HIS B 1 100 ? 17.219  -9.928  64.805  1.00 34.11  ? 100  HIS B N   1 
ATOM   4492 C  CA  . HIS B 1 100 ? 16.294  -8.985  65.419  1.00 33.43  ? 100  HIS B CA  1 
ATOM   4493 C  C   . HIS B 1 100 ? 16.813  -7.558  65.292  1.00 36.07  ? 100  HIS B C   1 
ATOM   4494 O  O   . HIS B 1 100 ? 16.085  -6.657  64.874  1.00 34.56  ? 100  HIS B O   1 
ATOM   4495 C  CB  . HIS B 1 100 ? 16.075  -9.348  66.888  1.00 33.57  ? 100  HIS B CB  1 
ATOM   4496 C  CG  . HIS B 1 100 ? 15.272  -8.339  67.644  1.00 42.26  ? 100  HIS B CG  1 
ATOM   4497 N  ND1 . HIS B 1 100 ? 13.894  -8.307  67.595  1.00 39.55  ? 100  HIS B ND1 1 
ATOM   4498 C  CD2 . HIS B 1 100 ? 15.644  -7.333  68.472  1.00 46.61  ? 100  HIS B CD2 1 
ATOM   4499 C  CE1 . HIS B 1 100 ? 13.452  -7.324  68.361  1.00 47.39  ? 100  HIS B CE1 1 
ATOM   4500 N  NE2 . HIS B 1 100 ? 14.493  -6.723  68.911  1.00 48.12  ? 100  HIS B NE2 1 
ATOM   4501 N  N   . ASN B 1 101 ? 18.076  -7.328  65.666  1.00 33.47  ? 101  ASN B N   1 
ATOM   4502 C  CA  . ASN B 1 101 ? 18.639  -5.983  65.553  1.00 37.98  ? 101  ASN B CA  1 
ATOM   4503 C  C   . ASN B 1 101 ? 18.645  -5.501  64.110  1.00 32.01  ? 101  ASN B C   1 
ATOM   4504 O  O   . ASN B 1 101 ? 18.410  -4.316  63.839  1.00 38.07  ? 101  ASN B O   1 
ATOM   4505 C  CB  . ASN B 1 101 ? 20.066  -5.948  66.121  1.00 32.11  ? 101  ASN B CB  1 
ATOM   4506 C  CG  . ASN B 1 101 ? 20.099  -6.067  67.640  1.00 37.84  ? 101  ASN B CG  1 
ATOM   4507 O  OD1 . ASN B 1 101 ? 19.102  -5.808  68.326  1.00 35.54  ? 101  ASN B OD1 1 
ATOM   4508 N  ND2 . ASN B 1 101 ? 21.255  -6.458  68.179  1.00 35.66  ? 101  ASN B ND2 1 
ATOM   4509 N  N   . ILE B 1 102 ? 18.928  -6.400  63.175  1.00 32.27  ? 102  ILE B N   1 
ATOM   4510 C  CA  . ILE B 1 102 ? 19.082  -6.021  61.777  1.00 34.14  ? 102  ILE B CA  1 
ATOM   4511 C  C   . ILE B 1 102 ? 17.732  -5.678  61.170  1.00 35.35  ? 102  ILE B C   1 
ATOM   4512 O  O   . ILE B 1 102 ? 17.621  -4.765  60.345  1.00 35.31  ? 102  ILE B O   1 
ATOM   4513 C  CB  . ILE B 1 102 ? 19.784  -7.151  60.997  1.00 34.89  ? 102  ILE B CB  1 
ATOM   4514 C  CG1 . ILE B 1 102 ? 21.285  -7.188  61.331  1.00 35.48  ? 102  ILE B CG1 1 
ATOM   4515 C  CG2 . ILE B 1 102 ? 19.540  -7.033  59.486  1.00 34.69  ? 102  ILE B CG2 1 
ATOM   4516 C  CD1 . ILE B 1 102 ? 22.016  -8.395  60.753  1.00 34.33  ? 102  ILE B CD1 1 
ATOM   4517 N  N   . LEU B 1 103 ? 16.690  -6.398  61.566  1.00 34.34  ? 103  LEU B N   1 
ATOM   4518 C  CA  . LEU B 1 103 ? 15.416  -6.297  60.870  1.00 32.73  ? 103  LEU B CA  1 
ATOM   4519 C  C   . LEU B 1 103 ? 14.394  -5.427  61.581  1.00 37.39  ? 103  LEU B C   1 
ATOM   4520 O  O   . LEU B 1 103 ? 13.425  -5.014  60.941  1.00 35.54  ? 103  LEU B O   1 
ATOM   4521 C  CB  . LEU B 1 103 ? 14.829  -7.699  60.646  1.00 34.75  ? 103  LEU B CB  1 
ATOM   4522 C  CG  . LEU B 1 103 ? 15.707  -8.590  59.751  1.00 32.62  ? 103  LEU B CG  1 
ATOM   4523 C  CD1 . LEU B 1 103 ? 15.101  -9.997  59.628  1.00 35.96  ? 103  LEU B CD1 1 
ATOM   4524 C  CD2 . LEU B 1 103 ? 15.908  -7.966  58.355  1.00 36.62  ? 103  LEU B CD2 1 
ATOM   4525 N  N   . LEU B 1 104 ? 14.571  -5.134  62.864  1.00 35.07  ? 104  LEU B N   1 
ATOM   4526 C  CA  . LEU B 1 104 ? 13.629  -4.252  63.547  1.00 39.49  ? 104  LEU B CA  1 
ATOM   4527 C  C   . LEU B 1 104 ? 13.422  -2.926  62.822  1.00 42.21  ? 104  LEU B C   1 
ATOM   4528 O  O   . LEU B 1 104 ? 12.268  -2.473  62.742  1.00 39.83  ? 104  LEU B O   1 
ATOM   4529 C  CB  . LEU B 1 104 ? 14.091  -4.009  64.993  1.00 42.72  ? 104  LEU B CB  1 
ATOM   4530 C  CG  . LEU B 1 104 ? 13.031  -3.428  65.930  1.00 43.80  ? 104  LEU B CG  1 
ATOM   4531 C  CD1 . LEU B 1 104 ? 11.802  -4.321  66.067  1.00 43.58  ? 104  LEU B CD1 1 
ATOM   4532 C  CD2 . LEU B 1 104 ? 13.649  -3.157  67.295  1.00 46.35  ? 104  LEU B CD2 1 
ATOM   4533 N  N   . PRO B 1 105 ? 14.448  -2.277  62.267  1.00 43.95  ? 105  PRO B N   1 
ATOM   4534 C  CA  . PRO B 1 105 ? 14.214  -1.006  61.553  1.00 46.47  ? 105  PRO B CA  1 
ATOM   4535 C  C   . PRO B 1 105 ? 13.282  -1.123  60.353  1.00 44.77  ? 105  PRO B C   1 
ATOM   4536 O  O   . PRO B 1 105 ? 12.766  -0.096  59.897  1.00 45.62  ? 105  PRO B O   1 
ATOM   4537 C  CB  . PRO B 1 105 ? 15.623  -0.589  61.116  1.00 45.41  ? 105  PRO B CB  1 
ATOM   4538 C  CG  . PRO B 1 105 ? 16.517  -1.217  62.152  1.00 47.90  ? 105  PRO B CG  1 
ATOM   4539 C  CD  . PRO B 1 105 ? 15.886  -2.558  62.429  1.00 44.88  ? 105  PRO B CD  1 
ATOM   4540 N  N   . SER B 1 106 ? 13.074  -2.327  59.813  1.00 39.57  ? 106  SER B N   1 
ATOM   4541 C  CA  . SER B 1 106 ? 12.129  -2.534  58.717  1.00 37.67  ? 106  SER B CA  1 
ATOM   4542 C  C   . SER B 1 106 ? 10.682  -2.358  59.135  1.00 39.45  ? 106  SER B C   1 
ATOM   4543 O  O   . SER B 1 106 ? 9.792   -2.415  58.273  1.00 39.32  ? 106  SER B O   1 
ATOM   4544 C  CB  . SER B 1 106 ? 12.269  -3.937  58.142  1.00 38.19  ? 106  SER B CB  1 
ATOM   4545 O  OG  . SER B 1 106 ? 13.521  -4.090  57.533  1.00 46.52  ? 106  SER B OG  1 
ATOM   4546 N  N   . PHE B 1 107 ? 10.421  -2.201  60.425  1.00 38.47  ? 107  PHE B N   1 
ATOM   4547 C  CA  . PHE B 1 107 ? 9.065   -2.030  60.917  1.00 39.67  ? 107  PHE B CA  1 
ATOM   4548 C  C   . PHE B 1 107 ? 8.939   -0.744  61.723  1.00 42.11  ? 107  PHE B C   1 
ATOM   4549 O  O   . PHE B 1 107 ? 8.026   -0.604  62.531  1.00 47.32  ? 107  PHE B O   1 
ATOM   4550 C  CB  . PHE B 1 107 ? 8.656   -3.275  61.704  1.00 40.46  ? 107  PHE B CB  1 
ATOM   4551 C  CG  . PHE B 1 107 ? 8.711   -4.515  60.867  1.00 41.17  ? 107  PHE B CG  1 
ATOM   4552 C  CD1 . PHE B 1 107 ? 7.655   -4.846  60.027  1.00 36.56  ? 107  PHE B CD1 1 
ATOM   4553 C  CD2 . PHE B 1 107 ? 9.856   -5.282  60.823  1.00 34.94  ? 107  PHE B CD2 1 
ATOM   4554 C  CE1 . PHE B 1 107 ? 7.723   -5.965  59.214  1.00 37.77  ? 107  PHE B CE1 1 
ATOM   4555 C  CE2 . PHE B 1 107 ? 9.948   -6.397  59.993  1.00 34.37  ? 107  PHE B CE2 1 
ATOM   4556 C  CZ  . PHE B 1 107 ? 8.875   -6.741  59.187  1.00 39.69  ? 107  PHE B CZ  1 
ATOM   4557 N  N   . SER B 1 108 ? 9.826   0.215   61.478  1.00 45.69  ? 108  SER B N   1 
ATOM   4558 C  CA  . SER B 1 108 ? 9.671   1.540   62.058  1.00 48.45  ? 108  SER B CA  1 
ATOM   4559 C  C   . SER B 1 108 ? 8.494   2.262   61.403  1.00 50.26  ? 108  SER B C   1 
ATOM   4560 O  O   . SER B 1 108 ? 7.969   1.844   60.365  1.00 46.84  ? 108  SER B O   1 
ATOM   4561 C  CB  . SER B 1 108 ? 10.944  2.358   61.866  1.00 46.72  ? 108  SER B CB  1 
ATOM   4562 O  OG  . SER B 1 108 ? 11.152  2.633   60.489  1.00 49.13  ? 108  SER B OG  1 
ATOM   4563 N  N   . GLN B 1 109 ? 8.084   3.381   62.004  1.00 49.21  ? 109  GLN B N   1 
ATOM   4564 C  CA  . GLN B 1 109 ? 6.998   4.136   61.387  1.00 51.87  ? 109  GLN B CA  1 
ATOM   4565 C  C   . GLN B 1 109 ? 7.409   4.671   60.022  1.00 46.28  ? 109  GLN B C   1 
ATOM   4566 O  O   . GLN B 1 109 ? 6.612   4.646   59.076  1.00 49.27  ? 109  GLN B O   1 
ATOM   4567 C  CB  . GLN B 1 109 ? 6.517   5.259   62.309  1.00 55.14  ? 109  GLN B CB  1 
ATOM   4568 C  CG  . GLN B 1 109 ? 5.796   4.731   63.540  1.00 58.22  ? 109  GLN B CG  1 
ATOM   4569 C  CD  . GLN B 1 109 ? 4.395   4.234   63.210  1.00 65.54  ? 109  GLN B CD  1 
ATOM   4570 O  OE1 . GLN B 1 109 ? 4.077   3.057   63.420  1.00 67.03  ? 109  GLN B OE1 1 
ATOM   4571 N  NE2 . GLN B 1 109 ? 3.559   5.119   62.655  1.00 61.49  ? 109  GLN B NE2 1 
ATOM   4572 N  N   . GLN B 1 110 ? 8.661   5.127   59.884  1.00 46.11  ? 110  GLN B N   1 
ATOM   4573 C  CA  . GLN B 1 110 ? 9.137   5.570   58.578  1.00 48.53  ? 110  GLN B CA  1 
ATOM   4574 C  C   . GLN B 1 110 ? 9.083   4.442   57.556  1.00 47.30  ? 110  GLN B C   1 
ATOM   4575 O  O   . GLN B 1 110 ? 8.712   4.663   56.396  1.00 43.83  ? 110  GLN B O   1 
ATOM   4576 C  CB  . GLN B 1 110 ? 10.560  6.127   58.673  1.00 52.58  ? 110  GLN B CB  1 
ATOM   4577 C  CG  . GLN B 1 110 ? 11.031  6.732   57.340  1.00 53.79  ? 110  GLN B CG  1 
ATOM   4578 C  CD  . GLN B 1 110 ? 12.443  7.307   57.389  1.00 71.01  ? 110  GLN B CD  1 
ATOM   4579 O  OE1 . GLN B 1 110 ? 13.380  6.737   56.824  1.00 73.32  ? 110  GLN B OE1 1 
ATOM   4580 N  NE2 . GLN B 1 110 ? 12.593  8.457   58.045  1.00 73.71  ? 110  GLN B NE2 1 
ATOM   4581 N  N   . ALA B 1 111 ? 9.480   3.229   57.956  1.00 45.01  ? 111  ALA B N   1 
ATOM   4582 C  CA  . ALA B 1 111 ? 9.343   2.087   57.060  1.00 44.11  ? 111  ALA B CA  1 
ATOM   4583 C  C   . ALA B 1 111 ? 7.882   1.849   56.703  1.00 39.63  ? 111  ALA B C   1 
ATOM   4584 O  O   . ALA B 1 111 ? 7.558   1.573   55.544  1.00 41.79  ? 111  ALA B O   1 
ATOM   4585 C  CB  . ALA B 1 111 ? 9.948   0.834   57.695  1.00 44.41  ? 111  ALA B CB  1 
ATOM   4586 N  N   . MET B 1 112 ? 6.988   1.946   57.683  1.00 39.49  ? 112  MET B N   1 
ATOM   4587 C  CA  . MET B 1 112 ? 5.585   1.676   57.400  1.00 42.35  ? 112  MET B CA  1 
ATOM   4588 C  C   . MET B 1 112 ? 5.001   2.703   56.440  1.00 43.12  ? 112  MET B C   1 
ATOM   4589 O  O   . MET B 1 112 ? 4.236   2.351   55.531  1.00 38.84  ? 112  MET B O   1 
ATOM   4590 C  CB  . MET B 1 112 ? 4.799   1.618   58.700  1.00 44.02  ? 112  MET B CB  1 
ATOM   4591 C  CG  . MET B 1 112 ? 5.249   0.428   59.510  1.00 52.37  ? 112  MET B CG  1 
ATOM   4592 S  SD  . MET B 1 112 ? 4.444   -1.083  58.937  1.00 42.74  ? 112  MET B SD  1 
ATOM   4593 C  CE  . MET B 1 112 ? 3.000   -0.445  58.122  1.00 44.39  ? 112  MET B CE  1 
ATOM   4594 N  N   . LYS B 1 113 ? 5.357   3.977   56.611  1.00 38.86  ? 113  LYS B N   1 
ATOM   4595 C  CA  . LYS B 1 113 ? 4.938   4.975   55.635  1.00 40.84  ? 113  LYS B CA  1 
ATOM   4596 C  C   . LYS B 1 113 ? 5.400   4.593   54.242  1.00 40.60  ? 113  LYS B C   1 
ATOM   4597 O  O   . LYS B 1 113 ? 4.667   4.786   53.262  1.00 41.38  ? 113  LYS B O   1 
ATOM   4598 C  CB  . LYS B 1 113 ? 5.455   6.359   56.031  1.00 40.37  ? 113  LYS B CB  1 
ATOM   4599 C  CG  . LYS B 1 113 ? 4.880   6.822   57.356  1.00 41.47  ? 113  LYS B CG  1 
ATOM   4600 C  CD  . LYS B 1 113 ? 5.474   8.135   57.849  1.00 43.16  ? 113  LYS B CD  1 
ATOM   4601 C  CE  . LYS B 1 113 ? 4.748   8.619   59.108  1.00 50.23  ? 113  LYS B CE  1 
ATOM   4602 N  NZ  . LYS B 1 113 ? 5.368   9.860   59.665  1.00 50.46  ? 113  LYS B NZ  1 
ATOM   4603 N  N   . GLY B 1 114 ? 6.597   4.013   54.137  1.00 39.04  ? 114  GLY B N   1 
ATOM   4604 C  CA  . GLY B 1 114 ? 7.122   3.636   52.842  1.00 37.62  ? 114  GLY B CA  1 
ATOM   4605 C  C   . GLY B 1 114 ? 6.459   2.408   52.246  1.00 41.04  ? 114  GLY B C   1 
ATOM   4606 O  O   . GLY B 1 114 ? 6.465   2.238   51.024  1.00 43.37  ? 114  GLY B O   1 
ATOM   4607 N  N   . TYR B 1 115 ? 5.904   1.523   53.092  1.00 39.12  ? 115  TYR B N   1 
ATOM   4608 C  CA  . TYR B 1 115 ? 5.183   0.347   52.602  1.00 37.83  ? 115  TYR B CA  1 
ATOM   4609 C  C   . TYR B 1 115 ? 3.785   0.694   52.120  1.00 37.19  ? 115  TYR B C   1 
ATOM   4610 O  O   . TYR B 1 115 ? 3.198   -0.072  51.341  1.00 37.62  ? 115  TYR B O   1 
ATOM   4611 C  CB  . TYR B 1 115 ? 5.033   -0.730  53.696  1.00 34.95  ? 115  TYR B CB  1 
ATOM   4612 C  CG  . TYR B 1 115 ? 6.328   -1.327  54.224  1.00 35.76  ? 115  TYR B CG  1 
ATOM   4613 C  CD1 . TYR B 1 115 ? 7.390   -1.578  53.380  1.00 39.50  ? 115  TYR B CD1 1 
ATOM   4614 C  CD2 . TYR B 1 115 ? 6.469   -1.646  55.567  1.00 36.22  ? 115  TYR B CD2 1 
ATOM   4615 C  CE1 . TYR B 1 115 ? 8.571   -2.129  53.857  1.00 39.05  ? 115  TYR B CE1 1 
ATOM   4616 C  CE2 . TYR B 1 115 ? 7.644   -2.205  56.058  1.00 36.58  ? 115  TYR B CE2 1 
ATOM   4617 C  CZ  . TYR B 1 115 ? 8.690   -2.440  55.192  1.00 40.06  ? 115  TYR B CZ  1 
ATOM   4618 O  OH  . TYR B 1 115 ? 9.862   -2.986  55.657  1.00 43.68  ? 115  TYR B OH  1 
ATOM   4619 N  N   . HIS B 1 116 ? 3.251   1.825   52.568  1.00 35.90  ? 116  HIS B N   1 
ATOM   4620 C  CA  . HIS B 1 116 ? 1.830   2.108   52.404  1.00 33.79  ? 116  HIS B CA  1 
ATOM   4621 C  C   . HIS B 1 116 ? 1.382   2.045   50.946  1.00 36.67  ? 116  HIS B C   1 
ATOM   4622 O  O   . HIS B 1 116 ? 0.341   1.455   50.636  1.00 35.26  ? 116  HIS B O   1 
ATOM   4623 C  CB  . HIS B 1 116 ? 1.499   3.466   53.005  1.00 36.52  ? 116  HIS B CB  1 
ATOM   4624 C  CG  . HIS B 1 116 ? 0.069   3.837   52.826  1.00 34.20  ? 116  HIS B CG  1 
ATOM   4625 N  ND1 . HIS B 1 116 ? -0.911  3.451   53.711  1.00 34.50  ? 116  HIS B ND1 1 
ATOM   4626 C  CD2 . HIS B 1 116 ? -0.562  4.485   51.818  1.00 35.92  ? 116  HIS B CD2 1 
ATOM   4627 C  CE1 . HIS B 1 116 ? -2.084  3.873   53.277  1.00 35.09  ? 116  HIS B CE1 1 
ATOM   4628 N  NE2 . HIS B 1 116 ? -1.899  4.502   52.128  1.00 34.46  ? 116  HIS B NE2 1 
ATOM   4629 N  N   . ALA B 1 117 ? 2.126   2.680   50.033  1.00 34.20  ? 117  ALA B N   1 
ATOM   4630 C  CA  . ALA B 1 117 ? 1.670   2.721   48.645  1.00 38.54  ? 117  ALA B CA  1 
ATOM   4631 C  C   . ALA B 1 117 ? 1.590   1.320   48.047  1.00 33.21  ? 117  ALA B C   1 
ATOM   4632 O  O   . ALA B 1 117 ? 0.711   1.032   47.229  1.00 35.37  ? 117  ALA B O   1 
ATOM   4633 C  CB  . ALA B 1 117 ? 2.592   3.601   47.801  1.00 37.56  ? 117  ALA B CB  1 
ATOM   4634 N  N   . MET B 1 118 ? 2.526   0.443   48.405  1.00 34.71  ? 118  MET B N   1 
ATOM   4635 C  CA  . MET B 1 118 ? 2.465   -0.904  47.858  1.00 34.99  ? 118  MET B CA  1 
ATOM   4636 C  C   . MET B 1 118 ? 1.335   -1.714  48.483  1.00 33.96  ? 118  MET B C   1 
ATOM   4637 O  O   . MET B 1 118 ? 0.780   -2.603  47.829  1.00 32.77  ? 118  MET B O   1 
ATOM   4638 C  CB  . MET B 1 118 ? 3.804   -1.621  48.035  1.00 37.25  ? 118  MET B CB  1 
ATOM   4639 C  CG  . MET B 1 118 ? 4.858   -1.252  47.000  1.00 39.36  ? 118  MET B CG  1 
ATOM   4640 S  SD  . MET B 1 118 ? 6.525   -1.726  47.552  1.00 50.28  ? 118  MET B SD  1 
ATOM   4641 C  CE  . MET B 1 118 ? 7.417   -1.783  45.993  1.00 50.80  ? 118  MET B CE  1 
ATOM   4642 N  N   . MET B 1 119 ? 0.976   -1.437  49.739  1.00 31.84  ? 119  MET B N   1 
ATOM   4643 C  CA  . MET B 1 119 ? -0.207  -2.095  50.283  1.00 30.50  ? 119  MET B CA  1 
ATOM   4644 C  C   . MET B 1 119 ? -1.447  -1.661  49.508  1.00 32.13  ? 119  MET B C   1 
ATOM   4645 O  O   . MET B 1 119 ? -2.327  -2.475  49.200  1.00 31.40  ? 119  MET B O   1 
ATOM   4646 C  CB  . MET B 1 119 ? -0.382  -1.754  51.757  1.00 30.53  ? 119  MET B CB  1 
ATOM   4647 C  CG  . MET B 1 119 ? 0.687   -2.376  52.664  1.00 32.55  ? 119  MET B CG  1 
ATOM   4648 S  SD  . MET B 1 119 ? 0.277   -2.031  54.366  1.00 33.17  ? 119  MET B SD  1 
ATOM   4649 C  CE  . MET B 1 119 ? 1.583   -2.951  55.204  1.00 34.99  ? 119  MET B CE  1 
ATOM   4650 N  N   . VAL B 1 120 ? -1.538  -0.365  49.200  1.00 31.93  ? 120  VAL B N   1 
ATOM   4651 C  CA  . VAL B 1 120 ? -2.682  0.130   48.437  1.00 33.97  ? 120  VAL B CA  1 
ATOM   4652 C  C   . VAL B 1 120 ? -2.737  -0.548  47.071  1.00 33.65  ? 120  VAL B C   1 
ATOM   4653 O  O   . VAL B 1 120 ? -3.817  -0.888  46.570  1.00 34.97  ? 120  VAL B O   1 
ATOM   4654 C  CB  . VAL B 1 120 ? -2.618  1.669   48.317  1.00 32.47  ? 120  VAL B CB  1 
ATOM   4655 C  CG1 . VAL B 1 120 ? -3.699  2.175   47.370  1.00 35.71  ? 120  VAL B CG1 1 
ATOM   4656 C  CG2 . VAL B 1 120 ? -2.780  2.319   49.696  1.00 32.87  ? 120  VAL B CG2 1 
ATOM   4657 N  N   . ASP B 1 121 ? -1.572  -0.778  46.460  1.00 30.09  ? 121  ASP B N   1 
ATOM   4658 C  CA  . ASP B 1 121 ? -1.518  -1.448  45.160  1.00 31.90  ? 121  ASP B CA  1 
ATOM   4659 C  C   . ASP B 1 121 ? -2.260  -2.785  45.189  1.00 33.64  ? 121  ASP B C   1 
ATOM   4660 O  O   . ASP B 1 121 ? -3.115  -3.057  44.335  1.00 33.23  ? 121  ASP B O   1 
ATOM   4661 C  CB  . ASP B 1 121 ? -0.049  -1.632  44.750  1.00 31.98  ? 121  ASP B CB  1 
ATOM   4662 C  CG  . ASP B 1 121 ? 0.114   -2.255  43.362  1.00 39.16  ? 121  ASP B CG  1 
ATOM   4663 O  OD1 . ASP B 1 121 ? -0.389  -3.382  43.141  1.00 34.92  ? 121  ASP B OD1 1 
ATOM   4664 O  OD2 . ASP B 1 121 ? 0.774   -1.628  42.499  1.00 36.12  ? 121  ASP B OD2 1 
ATOM   4665 N  N   . ILE B 1 122 ? -1.994  -3.611  46.207  1.00 30.36  ? 122  ILE B N   1 
ATOM   4666 C  CA  . ILE B 1 122 ? -2.624  -4.929  46.261  1.00 29.88  ? 122  ILE B CA  1 
ATOM   4667 C  C   . ILE B 1 122 ? -4.087  -4.800  46.686  1.00 32.49  ? 122  ILE B C   1 
ATOM   4668 O  O   . ILE B 1 122 ? -4.964  -5.528  46.185  1.00 32.62  ? 122  ILE B O   1 
ATOM   4669 C  CB  . ILE B 1 122 ? -1.834  -5.870  47.199  1.00 33.07  ? 122  ILE B CB  1 
ATOM   4670 C  CG1 . ILE B 1 122 ? -0.341  -5.950  46.802  1.00 30.46  ? 122  ILE B CG1 1 
ATOM   4671 C  CG2 . ILE B 1 122 ? -2.461  -7.260  47.210  1.00 28.99  ? 122  ILE B CG2 1 
ATOM   4672 C  CD1 . ILE B 1 122 ? -0.075  -6.335  45.319  1.00 31.63  ? 122  ILE B CD1 1 
ATOM   4673 N  N   . ALA B 1 123 ? -4.374  -3.871  47.602  1.00 30.68  ? 123  ALA B N   1 
ATOM   4674 C  CA  . ALA B 1 123 ? -5.750  -3.674  48.059  1.00 31.24  ? 123  ALA B CA  1 
ATOM   4675 C  C   . ALA B 1 123 ? -6.652  -3.245  46.912  1.00 33.00  ? 123  ALA B C   1 
ATOM   4676 O  O   . ALA B 1 123 ? -7.797  -3.704  46.808  1.00 33.97  ? 123  ALA B O   1 
ATOM   4677 C  CB  . ALA B 1 123 ? -5.797  -2.643  49.193  1.00 35.11  ? 123  ALA B CB  1 
ATOM   4678 N  N   . VAL B 1 124 ? -6.161  -2.358  46.048  1.00 34.50  ? 124  VAL B N   1 
ATOM   4679 C  CA  . VAL B 1 124 ? -6.936  -1.954  44.875  1.00 32.76  ? 124  VAL B CA  1 
ATOM   4680 C  C   . VAL B 1 124 ? -7.193  -3.152  43.964  1.00 32.67  ? 124  VAL B C   1 
ATOM   4681 O  O   . VAL B 1 124 ? -8.306  -3.332  43.455  1.00 34.50  ? 124  VAL B O   1 
ATOM   4682 C  CB  . VAL B 1 124 ? -6.224  -0.804  44.139  1.00 32.72  ? 124  VAL B CB  1 
ATOM   4683 C  CG1 . VAL B 1 124 ? -6.879  -0.551  42.776  1.00 33.01  ? 124  VAL B CG1 1 
ATOM   4684 C  CG2 . VAL B 1 124 ? -6.266  0.467   44.989  1.00 35.57  ? 124  VAL B CG2 1 
ATOM   4685 N  N   . GLN B 1 125 ? -6.184  -4.011  43.773  1.00 32.19  ? 125  GLN B N   1 
ATOM   4686 C  CA  . GLN B 1 125 ? -6.415  -5.236  43.007  1.00 33.84  ? 125  GLN B CA  1 
ATOM   4687 C  C   . GLN B 1 125 ? -7.546  -6.061  43.607  1.00 35.33  ? 125  GLN B C   1 
ATOM   4688 O  O   . GLN B 1 125 ? -8.352  -6.644  42.870  1.00 34.43  ? 125  GLN B O   1 
ATOM   4689 C  CB  . GLN B 1 125 ? -5.136  -6.070  42.918  1.00 32.27  ? 125  GLN B CB  1 
ATOM   4690 C  CG  . GLN B 1 125 ? -4.039  -5.402  42.097  1.00 31.70  ? 125  GLN B CG  1 
ATOM   4691 C  CD  . GLN B 1 125 ? -2.910  -6.370  41.796  1.00 33.86  ? 125  GLN B CD  1 
ATOM   4692 O  OE1 . GLN B 1 125 ? -3.148  -7.505  41.365  1.00 32.35  ? 125  GLN B OE1 1 
ATOM   4693 N  NE2 . GLN B 1 125 ? -1.674  -5.923  42.006  1.00 32.61  ? 125  GLN B NE2 1 
ATOM   4694 N  N   . LEU B 1 126 ? -7.632  -6.116  44.948  1.00 32.80  ? 126  LEU B N   1 
ATOM   4695 C  CA  . LEU B 1 126 ? -8.718  -6.847  45.597  1.00 30.30  ? 126  LEU B CA  1 
ATOM   4696 C  C   . LEU B 1 126 ? -10.068 -6.214  45.281  1.00 31.30  ? 126  LEU B C   1 
ATOM   4697 O  O   . LEU B 1 126 ? -11.013 -6.903  44.875  1.00 34.01  ? 126  LEU B O   1 
ATOM   4698 C  CB  . LEU B 1 126 ? -8.510  -6.883  47.116  1.00 29.45  ? 126  LEU B CB  1 
ATOM   4699 C  CG  . LEU B 1 126 ? -9.706  -7.515  47.850  1.00 33.15  ? 126  LEU B CG  1 
ATOM   4700 C  CD1 . LEU B 1 126 ? -9.777  -8.991  47.535  1.00 32.59  ? 126  LEU B CD1 1 
ATOM   4701 C  CD2 . LEU B 1 126 ? -9.617  -7.316  49.363  1.00 37.48  ? 126  LEU B CD2 1 
ATOM   4702 N  N   . VAL B 1 127 ? -10.184 -4.902  45.484  1.00 31.72  ? 127  VAL B N   1 
ATOM   4703 C  CA  . VAL B 1 127 ? -11.460 -4.226  45.258  1.00 32.43  ? 127  VAL B CA  1 
ATOM   4704 C  C   . VAL B 1 127 ? -11.887 -4.381  43.796  1.00 34.09  ? 127  VAL B C   1 
ATOM   4705 O  O   . VAL B 1 127 ? -13.060 -4.643  43.493  1.00 32.29  ? 127  VAL B O   1 
ATOM   4706 C  CB  . VAL B 1 127 ? -11.351 -2.746  45.689  1.00 33.22  ? 127  VAL B CB  1 
ATOM   4707 C  CG1 . VAL B 1 127 ? -12.580 -1.946  45.261  1.00 32.95  ? 127  VAL B CG1 1 
ATOM   4708 C  CG2 . VAL B 1 127 ? -11.160 -2.638  47.204  1.00 34.03  ? 127  VAL B CG2 1 
ATOM   4709 N  N   . GLN B 1 128 ? -10.934 -4.260  42.869  1.00 33.07  ? 128  GLN B N   1 
ATOM   4710 C  CA  . GLN B 1 128 ? -11.263 -4.372  41.453  1.00 32.74  ? 128  GLN B CA  1 
ATOM   4711 C  C   . GLN B 1 128 ? -11.740 -5.778  41.108  1.00 32.97  ? 128  GLN B C   1 
ATOM   4712 O  O   . GLN B 1 128 ? -12.658 -5.943  40.294  1.00 33.18  ? 128  GLN B O   1 
ATOM   4713 C  CB  . GLN B 1 128 ? -10.041 -3.981  40.617  1.00 30.92  ? 128  GLN B CB  1 
ATOM   4714 C  CG  . GLN B 1 128 ? -9.828  -2.477  40.640  1.00 34.88  ? 128  GLN B CG  1 
ATOM   4715 C  CD  . GLN B 1 128 ? -8.822  -1.988  39.645  1.00 47.88  ? 128  GLN B CD  1 
ATOM   4716 O  OE1 . GLN B 1 128 ? -7.764  -2.591  39.463  1.00 50.22  ? 128  GLN B OE1 1 
ATOM   4717 N  NE2 . GLN B 1 128 ? -9.133  -0.867  39.002  1.00 52.34  ? 128  GLN B NE2 1 
ATOM   4718 N  N   . LYS B 1 129 ? -11.130 -6.812  41.703  1.00 31.43  ? 129  LYS B N   1 
ATOM   4719 C  CA  . LYS B 1 129 ? -11.624 -8.163  41.463  1.00 31.96  ? 129  LYS B CA  1 
ATOM   4720 C  C   . LYS B 1 129 ? -13.100 -8.273  41.835  1.00 32.10  ? 129  LYS B C   1 
ATOM   4721 O  O   . LYS B 1 129 ? -13.917 -8.785  41.061  1.00 32.11  ? 129  LYS B O   1 
ATOM   4722 C  CB  . LYS B 1 129 ? -10.806 -9.192  42.245  1.00 32.37  ? 129  LYS B CB  1 
ATOM   4723 C  CG  . LYS B 1 129 ? -11.459 -10.577 42.206  1.00 35.07  ? 129  LYS B CG  1 
ATOM   4724 C  CD  . LYS B 1 129 ? -10.557 -11.684 42.719  1.00 35.83  ? 129  LYS B CD  1 
ATOM   4725 C  CE  . LYS B 1 129 ? -11.249 -13.047 42.688  1.00 37.71  ? 129  LYS B CE  1 
ATOM   4726 N  NZ  . LYS B 1 129 ? -10.342 -14.175 43.104  1.00 35.50  ? 129  LYS B NZ  1 
ATOM   4727 N  N   . TRP B 1 130 ? -13.459 -7.786  43.016  1.00 32.08  ? 130  TRP B N   1 
ATOM   4728 C  CA  . TRP B 1 130 ? -14.843 -7.901  43.476  1.00 30.79  ? 130  TRP B CA  1 
ATOM   4729 C  C   . TRP B 1 130 ? -15.786 -6.986  42.701  1.00 30.87  ? 130  TRP B C   1 
ATOM   4730 O  O   . TRP B 1 130 ? -16.954 -7.350  42.483  1.00 32.59  ? 130  TRP B O   1 
ATOM   4731 C  CB  . TRP B 1 130 ? -14.907 -7.597  44.978  1.00 31.41  ? 130  TRP B CB  1 
ATOM   4732 C  CG  . TRP B 1 130 ? -14.200 -8.600  45.831  1.00 33.00  ? 130  TRP B CG  1 
ATOM   4733 C  CD1 . TRP B 1 130 ? -13.579 -9.753  45.419  1.00 34.59  ? 130  TRP B CD1 1 
ATOM   4734 C  CD2 . TRP B 1 130 ? -14.037 -8.545  47.255  1.00 30.48  ? 130  TRP B CD2 1 
ATOM   4735 N  NE1 . TRP B 1 130 ? -13.046 -10.416 46.504  1.00 34.03  ? 130  TRP B NE1 1 
ATOM   4736 C  CE2 . TRP B 1 130 ? -13.318 -9.699  47.641  1.00 32.97  ? 130  TRP B CE2 1 
ATOM   4737 C  CE3 . TRP B 1 130 ? -14.445 -7.639  48.243  1.00 30.56  ? 130  TRP B CE3 1 
ATOM   4738 C  CZ2 . TRP B 1 130 ? -12.988 -9.961  48.970  1.00 33.99  ? 130  TRP B CZ2 1 
ATOM   4739 C  CZ3 . TRP B 1 130 ? -14.113 -7.905  49.572  1.00 31.53  ? 130  TRP B CZ3 1 
ATOM   4740 C  CH2 . TRP B 1 130 ? -13.395 -9.052  49.918  1.00 32.37  ? 130  TRP B CH2 1 
ATOM   4741 N  N   . GLU B 1 131 ? -15.324 -5.792  42.298  1.00 30.80  ? 131  GLU B N   1 
ATOM   4742 C  CA  . GLU B 1 131 ? -16.158 -4.947  41.441  1.00 33.97  ? 131  GLU B CA  1 
ATOM   4743 C  C   . GLU B 1 131 ? -16.510 -5.646  40.139  1.00 35.94  ? 131  GLU B C   1 
ATOM   4744 O  O   . GLU B 1 131 ? -17.548 -5.344  39.533  1.00 34.24  ? 131  GLU B O   1 
ATOM   4745 C  CB  . GLU B 1 131 ? -15.469 -3.626  41.097  1.00 32.36  ? 131  GLU B CB  1 
ATOM   4746 C  CG  . GLU B 1 131 ? -15.194 -2.701  42.293  1.00 36.91  ? 131  GLU B CG  1 
ATOM   4747 C  CD  . GLU B 1 131 ? -16.413 -1.895  42.715  1.00 39.15  ? 131  GLU B CD  1 
ATOM   4748 O  OE1 . GLU B 1 131 ? -17.563 -2.318  42.420  1.00 38.77  ? 131  GLU B OE1 1 
ATOM   4749 O  OE2 . GLU B 1 131 ? -16.215 -0.833  43.347  1.00 40.69  ? 131  GLU B OE2 1 
ATOM   4750 N  N   . ARG B 1 132 ? -15.655 -6.555  39.683  1.00 31.55  ? 132  ARG B N   1 
ATOM   4751 C  CA  . ARG B 1 132 ? -15.786 -7.134  38.351  1.00 34.29  ? 132  ARG B CA  1 
ATOM   4752 C  C   . ARG B 1 132 ? -16.547 -8.445  38.342  1.00 36.13  ? 132  ARG B C   1 
ATOM   4753 O  O   . ARG B 1 132 ? -16.704 -9.043  37.272  1.00 34.84  ? 132  ARG B O   1 
ATOM   4754 C  CB  . ARG B 1 132 ? -14.392 -7.316  37.729  1.00 31.58  ? 132  ARG B CB  1 
ATOM   4755 C  CG  . ARG B 1 132 ? -13.796 -5.981  37.316  1.00 33.29  ? 132  ARG B CG  1 
ATOM   4756 C  CD  . ARG B 1 132 ? -12.305 -6.056  37.005  1.00 35.27  ? 132  ARG B CD  1 
ATOM   4757 N  NE  . ARG B 1 132 ? -11.821 -4.753  36.575  1.00 32.74  ? 132  ARG B NE  1 
ATOM   4758 C  CZ  . ARG B 1 132 ? -10.543 -4.409  36.464  1.00 35.85  ? 132  ARG B CZ  1 
ATOM   4759 N  NH1 . ARG B 1 132 ? -9.573  -5.237  36.809  1.00 32.01  ? 132  ARG B NH1 1 
ATOM   4760 N  NH2 . ARG B 1 132 ? -10.235 -3.202  35.991  1.00 37.97  ? 132  ARG B NH2 1 
ATOM   4761 N  N   . LEU B 1 133 ? -17.037 -8.898  39.492  1.00 32.04  ? 133  LEU B N   1 
ATOM   4762 C  CA  . LEU B 1 133 ? -17.834 -10.113 39.524  1.00 32.77  ? 133  LEU B CA  1 
ATOM   4763 C  C   . LEU B 1 133 ? -19.192 -9.876  38.871  1.00 33.74  ? 133  LEU B C   1 
ATOM   4764 O  O   . LEU B 1 133 ? -19.732 -8.768  38.892  1.00 38.13  ? 133  LEU B O   1 
ATOM   4765 C  CB  . LEU B 1 133 ? -18.043 -10.597 40.965  1.00 36.72  ? 133  LEU B CB  1 
ATOM   4766 C  CG  . LEU B 1 133 ? -16.786 -10.943 41.766  1.00 34.15  ? 133  LEU B CG  1 
ATOM   4767 C  CD1 . LEU B 1 133 ? -17.147 -11.336 43.197  1.00 36.31  ? 133  LEU B CD1 1 
ATOM   4768 C  CD2 . LEU B 1 133 ? -15.977 -12.048 41.062  1.00 36.77  ? 133  LEU B CD2 1 
ATOM   4769 N  N   . ASN B 1 134 ? -19.744 -10.938 38.300  1.00 34.51  ? 134  ASN B N   1 
ATOM   4770 C  CA  . ASN B 1 134 ? -21.051 -10.883 37.666  1.00 34.34  ? 134  ASN B CA  1 
ATOM   4771 C  C   . ASN B 1 134 ? -22.166 -11.110 38.677  1.00 41.21  ? 134  ASN B C   1 
ATOM   4772 O  O   . ASN B 1 134 ? -21.945 -11.548 39.805  1.00 37.86  ? 134  ASN B O   1 
ATOM   4773 C  CB  . ASN B 1 134 ? -21.157 -11.927 36.563  1.00 33.31  ? 134  ASN B CB  1 
ATOM   4774 C  CG  . ASN B 1 134 ? -20.100 -11.749 35.509  1.00 34.18  ? 134  ASN B CG  1 
ATOM   4775 O  OD1 . ASN B 1 134 ? -20.099 -10.750 34.780  1.00 34.57  ? 134  ASN B OD1 1 
ATOM   4776 N  ND2 . ASN B 1 134 ? -19.190 -12.706 35.424  1.00 33.79  ? 134  ASN B ND2 1 
ATOM   4777 N  N   . ALA B 1 135 ? -23.388 -10.839 38.226  1.00 42.42  ? 135  ALA B N   1 
ATOM   4778 C  CA  . ALA B 1 135 ? -24.591 -11.055 39.014  1.00 47.35  ? 135  ALA B CA  1 
ATOM   4779 C  C   . ALA B 1 135 ? -24.523 -12.366 39.780  1.00 43.07  ? 135  ALA B C   1 
ATOM   4780 O  O   . ALA B 1 135 ? -24.297 -13.435 39.200  1.00 39.63  ? 135  ALA B O   1 
ATOM   4781 C  CB  . ALA B 1 135 ? -25.814 -11.048 38.091  1.00 43.81  ? 135  ALA B CB  1 
ATOM   4782 N  N   . ASP B 1 136 ? -24.688 -12.268 41.092  1.00 46.98  ? 136  ASP B N   1 
ATOM   4783 C  CA  . ASP B 1 136 ? -24.847 -13.383 42.018  1.00 48.36  ? 136  ASP B CA  1 
ATOM   4784 C  C   . ASP B 1 136 ? -23.641 -14.311 42.098  1.00 45.04  ? 136  ASP B C   1 
ATOM   4785 O  O   . ASP B 1 136 ? -23.729 -15.377 42.720  1.00 47.43  ? 136  ASP B O   1 
ATOM   4786 C  CB  . ASP B 1 136 ? -26.119 -14.167 41.707  1.00 55.81  ? 136  ASP B CB  1 
ATOM   4787 C  CG  . ASP B 1 136 ? -27.354 -13.411 42.152  1.00 59.11  ? 136  ASP B CG  1 
ATOM   4788 O  OD1 . ASP B 1 136 ? -27.430 -13.099 43.370  1.00 58.04  ? 136  ASP B OD1 1 
ATOM   4789 O  OD2 . ASP B 1 136 ? -28.212 -13.097 41.300  1.00 59.62  ? 136  ASP B OD2 1 
ATOM   4790 N  N   . GLU B 1 137 ? -22.501 -13.928 41.534  1.00 38.44  ? 137  GLU B N   1 
ATOM   4791 C  CA  . GLU B 1 137 ? -21.280 -14.627 41.903  1.00 36.68  ? 137  GLU B CA  1 
ATOM   4792 C  C   . GLU B 1 137 ? -20.901 -14.260 43.330  1.00 37.86  ? 137  GLU B C   1 
ATOM   4793 O  O   . GLU B 1 137 ? -21.317 -13.230 43.865  1.00 41.03  ? 137  GLU B O   1 
ATOM   4794 C  CB  . GLU B 1 137 ? -20.148 -14.286 40.942  1.00 35.15  ? 137  GLU B CB  1 
ATOM   4795 C  CG  . GLU B 1 137 ? -20.551 -14.585 39.504  1.00 36.49  ? 137  GLU B CG  1 
ATOM   4796 C  CD  . GLU B 1 137 ? -19.463 -14.301 38.492  1.00 38.97  ? 137  GLU B CD  1 
ATOM   4797 O  OE1 . GLU B 1 137 ? -18.559 -13.479 38.765  1.00 35.42  ? 137  GLU B OE1 1 
ATOM   4798 O  OE2 . GLU B 1 137 ? -19.550 -14.885 37.397  1.00 38.10  ? 137  GLU B OE2 1 
ATOM   4799 N  N   . HIS B 1 138 ? -20.111 -15.117 43.957  1.00 37.04  ? 138  HIS B N   1 
ATOM   4800 C  CA  . HIS B 1 138 ? -19.766 -14.892 45.352  1.00 36.17  ? 138  HIS B CA  1 
ATOM   4801 C  C   . HIS B 1 138 ? -18.255 -14.817 45.501  1.00 33.99  ? 138  HIS B C   1 
ATOM   4802 O  O   . HIS B 1 138 ? -17.496 -15.007 44.543  1.00 32.02  ? 138  HIS B O   1 
ATOM   4803 C  CB  . HIS B 1 138 ? -20.356 -15.988 46.244  1.00 34.55  ? 138  HIS B CB  1 
ATOM   4804 C  CG  . HIS B 1 138 ? -19.821 -17.353 45.960  1.00 38.89  ? 138  HIS B CG  1 
ATOM   4805 N  ND1 . HIS B 1 138 ? -20.447 -18.233 45.103  1.00 42.35  ? 138  HIS B ND1 1 
ATOM   4806 C  CD2 . HIS B 1 138 ? -18.729 -18.000 46.435  1.00 38.40  ? 138  HIS B CD2 1 
ATOM   4807 C  CE1 . HIS B 1 138 ? -19.751 -19.354 45.046  1.00 46.05  ? 138  HIS B CE1 1 
ATOM   4808 N  NE2 . HIS B 1 138 ? -18.705 -19.240 45.847  1.00 42.54  ? 138  HIS B NE2 1 
ATOM   4809 N  N   . ILE B 1 139 ? -17.848 -14.518 46.728  1.00 34.95  ? 139  ILE B N   1 
ATOM   4810 C  CA  . ILE B 1 139 ? -16.455 -14.313 47.105  1.00 33.80  ? 139  ILE B CA  1 
ATOM   4811 C  C   . ILE B 1 139 ? -16.051 -15.457 48.022  1.00 33.70  ? 139  ILE B C   1 
ATOM   4812 O  O   . ILE B 1 139 ? -16.778 -15.782 48.969  1.00 34.47  ? 139  ILE B O   1 
ATOM   4813 C  CB  . ILE B 1 139 ? -16.263 -12.966 47.828  1.00 36.03  ? 139  ILE B CB  1 
ATOM   4814 C  CG1 . ILE B 1 139 ? -16.446 -11.782 46.862  1.00 34.69  ? 139  ILE B CG1 1 
ATOM   4815 C  CG2 . ILE B 1 139 ? -14.905 -12.954 48.603  1.00 31.91  ? 139  ILE B CG2 1 
ATOM   4816 C  CD1 . ILE B 1 139 ? -16.928 -10.517 47.536  1.00 36.28  ? 139  ILE B CD1 1 
ATOM   4817 N  N   . GLU B 1 140 ? -14.890 -16.058 47.746  1.00 34.16  ? 140  GLU B N   1 
ATOM   4818 C  CA  . GLU B 1 140 ? -14.264 -17.040 48.634  1.00 35.96  ? 140  GLU B CA  1 
ATOM   4819 C  C   . GLU B 1 140 ? -13.326 -16.264 49.552  1.00 34.23  ? 140  GLU B C   1 
ATOM   4820 O  O   . GLU B 1 140 ? -12.266 -15.795 49.125  1.00 32.85  ? 140  GLU B O   1 
ATOM   4821 C  CB  . GLU B 1 140 ? -13.534 -18.104 47.821  1.00 37.09  ? 140  GLU B CB  1 
ATOM   4822 C  CG  . GLU B 1 140 ? -14.483 -18.862 46.886  1.00 36.74  ? 140  GLU B CG  1 
ATOM   4823 C  CD  . GLU B 1 140 ? -13.774 -19.946 46.105  1.00 46.96  ? 140  GLU B CD  1 
ATOM   4824 O  OE1 . GLU B 1 140 ? -12.550 -19.837 45.927  1.00 45.22  ? 140  GLU B OE1 1 
ATOM   4825 O  OE2 . GLU B 1 140 ? -14.438 -20.907 45.683  1.00 43.42  ? 140  GLU B OE2 1 
ATOM   4826 N  N   . VAL B 1 141 ? -13.740 -16.075 50.797  1.00 30.89  ? 141  VAL B N   1 
ATOM   4827 C  CA  . VAL B 1 141 ? -13.141 -15.029 51.625  1.00 31.39  ? 141  VAL B CA  1 
ATOM   4828 C  C   . VAL B 1 141 ? -11.712 -15.398 52.017  1.00 29.90  ? 141  VAL B C   1 
ATOM   4829 O  O   . VAL B 1 141 ? -10.789 -14.650 51.668  1.00 33.09  ? 141  VAL B O   1 
ATOM   4830 C  CB  . VAL B 1 141 ? -13.998 -14.722 52.860  1.00 31.72  ? 141  VAL B CB  1 
ATOM   4831 C  CG1 . VAL B 1 141 ? -13.226 -13.790 53.794  1.00 32.04  ? 141  VAL B CG1 1 
ATOM   4832 C  CG2 . VAL B 1 141 ? -15.339 -14.082 52.431  1.00 31.76  ? 141  VAL B CG2 1 
ATOM   4833 N  N   . PRO B 1 142 ? -11.463 -16.505 52.719  1.00 31.35  ? 142  PRO B N   1 
ATOM   4834 C  CA  . PRO B 1 142 ? -10.063 -16.798 53.093  1.00 31.50  ? 142  PRO B CA  1 
ATOM   4835 C  C   . PRO B 1 142 ? -9.170  -16.940 51.883  1.00 32.74  ? 142  PRO B C   1 
ATOM   4836 O  O   . PRO B 1 142 ? -7.978  -16.603 51.945  1.00 30.96  ? 142  PRO B O   1 
ATOM   4837 C  CB  . PRO B 1 142 ? -10.160 -18.110 53.884  1.00 35.04  ? 142  PRO B CB  1 
ATOM   4838 C  CG  . PRO B 1 142 ? -11.491 -18.710 53.505  1.00 36.06  ? 142  PRO B CG  1 
ATOM   4839 C  CD  . PRO B 1 142 ? -12.397 -17.517 53.246  1.00 33.97  ? 142  PRO B CD  1 
ATOM   4840 N  N   . GLU B 1 143 ? -9.721  -17.425 50.775  1.00 30.53  ? 143  GLU B N   1 
ATOM   4841 C  CA  . GLU B 1 143 ? -8.923  -17.574 49.565  1.00 31.68  ? 143  GLU B CA  1 
ATOM   4842 C  C   . GLU B 1 143 ? -8.457  -16.221 49.040  1.00 32.20  ? 143  GLU B C   1 
ATOM   4843 O  O   . GLU B 1 143 ? -7.288  -16.054 48.678  1.00 32.85  ? 143  GLU B O   1 
ATOM   4844 C  CB  . GLU B 1 143 ? -9.738  -18.320 48.504  1.00 30.95  ? 143  GLU B CB  1 
ATOM   4845 C  CG  . GLU B 1 143 ? -9.885  -19.802 48.775  1.00 39.05  ? 143  GLU B CG  1 
ATOM   4846 C  CD  . GLU B 1 143 ? -10.929 -20.140 49.840  1.00 41.18  ? 143  GLU B CD  1 
ATOM   4847 O  OE1 . GLU B 1 143 ? -11.759 -19.274 50.196  1.00 35.55  ? 143  GLU B OE1 1 
ATOM   4848 O  OE2 . GLU B 1 143 ? -10.909 -21.292 50.325  1.00 45.07  ? 143  GLU B OE2 1 
ATOM   4849 N  N   . ASP B 1 144 ? -9.365  -15.249 48.952  1.00 29.91  ? 144  ASP B N   1 
ATOM   4850 C  CA  . ASP B 1 144 ? -8.979  -13.928 48.466  1.00 29.45  ? 144  ASP B CA  1 
ATOM   4851 C  C   . ASP B 1 144 ? -8.176  -13.162 49.511  1.00 32.14  ? 144  ASP B C   1 
ATOM   4852 O  O   . ASP B 1 144 ? -7.345  -12.318 49.150  1.00 30.96  ? 144  ASP B O   1 
ATOM   4853 C  CB  . ASP B 1 144 ? -10.223 -13.131 48.076  1.00 33.60  ? 144  ASP B CB  1 
ATOM   4854 C  CG  . ASP B 1 144 ? -10.627 -13.350 46.646  1.00 34.47  ? 144  ASP B CG  1 
ATOM   4855 O  OD1 . ASP B 1 144 ? -9.818  -13.907 45.880  1.00 33.59  ? 144  ASP B OD1 1 
ATOM   4856 O  OD2 . ASP B 1 144 ? -11.763 -12.963 46.274  1.00 33.54  ? 144  ASP B OD2 1 
ATOM   4857 N  N   . MET B 1 145 ? -8.423  -13.424 50.806  1.00 30.07  ? 145  MET B N   1 
ATOM   4858 C  CA  . MET B 1 145 ? -7.629  -12.754 51.825  1.00 30.76  ? 145  MET B CA  1 
ATOM   4859 C  C   . MET B 1 145 ? -6.190  -13.232 51.738  1.00 30.79  ? 145  MET B C   1 
ATOM   4860 O  O   . MET B 1 145 ? -5.266  -12.453 51.958  1.00 32.38  ? 145  MET B O   1 
ATOM   4861 C  CB  . MET B 1 145 ? -8.198  -13.029 53.233  1.00 29.41  ? 145  MET B CB  1 
ATOM   4862 C  CG  . MET B 1 145 ? -9.486  -12.266 53.581  1.00 31.56  ? 145  MET B CG  1 
ATOM   4863 S  SD  . MET B 1 145 ? -9.569  -10.535 53.081  1.00 31.96  ? 145  MET B SD  1 
ATOM   4864 C  CE  . MET B 1 145 ? -10.352 -10.655 51.481  1.00 35.20  ? 145  MET B CE  1 
ATOM   4865 N  N   . THR B 1 146 ? -5.980  -14.515 51.441  1.00 28.88  ? 146  THR B N   1 
ATOM   4866 C  CA  . THR B 1 146 ? -4.612  -15.020 51.272  1.00 30.97  ? 146  THR B CA  1 
ATOM   4867 C  C   . THR B 1 146 ? -3.961  -14.476 49.997  1.00 30.97  ? 146  THR B C   1 
ATOM   4868 O  O   . THR B 1 146 ? -2.754  -14.174 49.980  1.00 30.31  ? 146  THR B O   1 
ATOM   4869 C  CB  . THR B 1 146 ? -4.630  -16.550 51.264  1.00 33.21  ? 146  THR B CB  1 
ATOM   4870 O  OG1 . THR B 1 146 ? -4.865  -17.019 52.597  1.00 34.78  ? 146  THR B OG1 1 
ATOM   4871 C  CG2 . THR B 1 146 ? -3.318  -17.124 50.751  1.00 32.34  ? 146  THR B CG2 1 
ATOM   4872 N  N   . ARG B 1 147 ? -4.735  -14.341 48.912  1.00 30.42  ? 147  ARG B N   1 
ATOM   4873 C  CA  . ARG B 1 147 ? -4.211  -13.662 47.727  1.00 30.19  ? 147  ARG B CA  1 
ATOM   4874 C  C   . ARG B 1 147 ? -3.674  -12.281 48.103  1.00 33.80  ? 147  ARG B C   1 
ATOM   4875 O  O   . ARG B 1 147 ? -2.542  -11.920 47.757  1.00 32.35  ? 147  ARG B O   1 
ATOM   4876 C  CB  . ARG B 1 147 ? -5.300  -13.533 46.643  1.00 31.12  ? 147  ARG B CB  1 
ATOM   4877 C  CG  . ARG B 1 147 ? -5.657  -14.841 45.924  1.00 33.76  ? 147  ARG B CG  1 
ATOM   4878 C  CD  . ARG B 1 147 ? -6.634  -14.567 44.757  1.00 30.99  ? 147  ARG B CD  1 
ATOM   4879 N  NE  . ARG B 1 147 ? -6.895  -15.775 43.975  1.00 35.32  ? 147  ARG B NE  1 
ATOM   4880 C  CZ  . ARG B 1 147 ? -7.811  -16.694 44.267  1.00 39.74  ? 147  ARG B CZ  1 
ATOM   4881 N  NH1 . ARG B 1 147 ? -8.652  -16.544 45.286  1.00 32.61  ? 147  ARG B NH1 1 
ATOM   4882 N  NH2 . ARG B 1 147 ? -7.863  -17.810 43.540  1.00 39.78  ? 147  ARG B NH2 1 
ATOM   4883 N  N   . LEU B 1 148 ? -4.471  -11.512 48.859  1.00 30.96  ? 148  LEU B N   1 
ATOM   4884 C  CA  . LEU B 1 148 ? -4.068  -10.168 49.262  1.00 32.18  ? 148  LEU B CA  1 
ATOM   4885 C  C   . LEU B 1 148 ? -2.834  -10.185 50.153  1.00 30.75  ? 148  LEU B C   1 
ATOM   4886 O  O   . LEU B 1 148 ? -1.867  -9.458  49.903  1.00 32.89  ? 148  LEU B O   1 
ATOM   4887 C  CB  . LEU B 1 148 ? -5.208  -9.455  49.993  1.00 34.84  ? 148  LEU B CB  1 
ATOM   4888 C  CG  . LEU B 1 148 ? -4.717  -8.037  50.339  1.00 35.40  ? 148  LEU B CG  1 
ATOM   4889 C  CD1 . LEU B 1 148 ? -5.509  -6.918  49.704  1.00 35.86  ? 148  LEU B CD1 1 
ATOM   4890 C  CD2 . LEU B 1 148 ? -4.626  -7.886  51.880  1.00 37.40  ? 148  LEU B CD2 1 
ATOM   4891 N  N   . THR B 1 149 ? -2.864  -10.968 51.229  1.00 31.47  ? 149  THR B N   1 
ATOM   4892 C  CA  . THR B 1 149 ? -1.801  -10.816 52.216  1.00 29.63  ? 149  THR B CA  1 
ATOM   4893 C  C   . THR B 1 149 ? -0.472  -11.360 51.695  1.00 31.22  ? 149  THR B C   1 
ATOM   4894 O  O   . THR B 1 149 ? 0.584   -10.770 51.959  1.00 30.14  ? 149  THR B O   1 
ATOM   4895 C  CB  . THR B 1 149 ? -2.190  -11.487 53.532  1.00 31.96  ? 149  THR B CB  1 
ATOM   4896 O  OG1 . THR B 1 149 ? -2.490  -12.867 53.302  1.00 31.34  ? 149  THR B OG1 1 
ATOM   4897 C  CG2 . THR B 1 149 ? -3.433  -10.790 54.159  1.00 31.49  ? 149  THR B CG2 1 
ATOM   4898 N  N   . LEU B 1 150 ? -0.491  -12.482 50.965  1.00 30.80  ? 150  LEU B N   1 
ATOM   4899 C  CA  . LEU B 1 150 ? 0.756   -12.972 50.368  1.00 31.89  ? 150  LEU B CA  1 
ATOM   4900 C  C   . LEU B 1 150 ? 1.334   -11.940 49.406  1.00 31.52  ? 150  LEU B C   1 
ATOM   4901 O  O   . LEU B 1 150 ? 2.534   -11.637 49.427  1.00 32.25  ? 150  LEU B O   1 
ATOM   4902 C  CB  . LEU B 1 150 ? 0.520   -14.284 49.621  1.00 32.11  ? 150  LEU B CB  1 
ATOM   4903 C  CG  . LEU B 1 150 ? 1.782   -14.793 48.932  1.00 33.85  ? 150  LEU B CG  1 
ATOM   4904 C  CD1 . LEU B 1 150 ? 2.771   -15.265 49.993  1.00 38.09  ? 150  LEU B CD1 1 
ATOM   4905 C  CD2 . LEU B 1 150 ? 1.440   -15.911 47.952  1.00 38.11  ? 150  LEU B CD2 1 
ATOM   4906 N  N   . ASP B 1 151 ? 0.496   -11.391 48.538  1.00 32.56  ? 151  ASP B N   1 
ATOM   4907 C  CA  . ASP B 1 151 ? 1.017   -10.411 47.595  1.00 30.68  ? 151  ASP B CA  1 
ATOM   4908 C  C   . ASP B 1 151 ? 1.517   -9.160  48.299  1.00 31.00  ? 151  ASP B C   1 
ATOM   4909 O  O   . ASP B 1 151 ? 2.479   -8.535  47.849  1.00 31.19  ? 151  ASP B O   1 
ATOM   4910 C  CB  . ASP B 1 151 ? -0.055  -10.044 46.577  1.00 32.45  ? 151  ASP B CB  1 
ATOM   4911 C  CG  . ASP B 1 151 ? -0.190  -11.085 45.510  1.00 31.16  ? 151  ASP B CG  1 
ATOM   4912 O  OD1 . ASP B 1 151 ? 0.172   -12.248 45.771  1.00 34.79  ? 151  ASP B OD1 1 
ATOM   4913 O  OD2 . ASP B 1 151 ? -0.646  -10.727 44.415  1.00 34.14  ? 151  ASP B OD2 1 
ATOM   4914 N  N   . THR B 1 152 ? 0.873   -8.769  49.390  1.00 30.39  ? 152  THR B N   1 
ATOM   4915 C  CA  . THR B 1 152 ? 1.324   -7.588  50.122  1.00 31.32  ? 152  THR B CA  1 
ATOM   4916 C  C   . THR B 1 152 ? 2.707   -7.797  50.743  1.00 32.82  ? 152  THR B C   1 
ATOM   4917 O  O   . THR B 1 152 ? 3.584   -6.938  50.601  1.00 31.33  ? 152  THR B O   1 
ATOM   4918 C  CB  . THR B 1 152 ? 0.282   -7.196  51.171  1.00 31.99  ? 152  THR B CB  1 
ATOM   4919 O  OG1 . THR B 1 152 ? -0.944  -6.889  50.489  1.00 31.80  ? 152  THR B OG1 1 
ATOM   4920 C  CG2 . THR B 1 152 ? 0.731   -5.934  51.932  1.00 31.65  ? 152  THR B CG2 1 
ATOM   4921 N  N   . ILE B 1 153 ? 2.940   -8.926  51.428  1.00 32.11  ? 153  ILE B N   1 
ATOM   4922 C  CA  . ILE B 1 153 ? 4.276   -9.120  51.997  1.00 32.71  ? 153  ILE B CA  1 
ATOM   4923 C  C   . ILE B 1 153 ? 5.298   -9.309  50.875  1.00 32.93  ? 153  ILE B C   1 
ATOM   4924 O  O   . ILE B 1 153 ? 6.433   -8.822  50.962  1.00 31.87  ? 153  ILE B O   1 
ATOM   4925 C  CB  . ILE B 1 153 ? 4.306   -10.279 53.021  1.00 30.78  ? 153  ILE B CB  1 
ATOM   4926 C  CG1 . ILE B 1 153 ? 5.669   -10.327 53.742  1.00 32.06  ? 153  ILE B CG1 1 
ATOM   4927 C  CG2 . ILE B 1 153 ? 4.042   -11.633 52.345  1.00 31.12  ? 153  ILE B CG2 1 
ATOM   4928 C  CD1 . ILE B 1 153 ? 5.953   -9.105  54.596  1.00 33.17  ? 153  ILE B CD1 1 
ATOM   4929 N  N   . GLY B 1 154 ? 4.913   -9.993  49.794  1.00 30.93  ? 154  GLY B N   1 
ATOM   4930 C  CA  . GLY B 1 154 ? 5.837   -10.161 48.678  1.00 31.28  ? 154  GLY B CA  1 
ATOM   4931 C  C   . GLY B 1 154 ? 6.289   -8.832  48.094  1.00 32.94  ? 154  GLY B C   1 
ATOM   4932 O  O   . GLY B 1 154 ? 7.481   -8.606  47.856  1.00 33.54  ? 154  GLY B O   1 
ATOM   4933 N  N   . LEU B 1 155 ? 5.342   -7.934  47.849  1.00 31.73  ? 155  LEU B N   1 
ATOM   4934 C  CA  . LEU B 1 155 ? 5.677   -6.656  47.230  1.00 31.48  ? 155  LEU B CA  1 
ATOM   4935 C  C   . LEU B 1 155 ? 6.328   -5.696  48.226  1.00 33.93  ? 155  LEU B C   1 
ATOM   4936 O  O   . LEU B 1 155 ? 7.402   -5.147  47.950  1.00 33.23  ? 155  LEU B O   1 
ATOM   4937 C  CB  . LEU B 1 155 ? 4.414   -6.043  46.608  1.00 33.99  ? 155  LEU B CB  1 
ATOM   4938 C  CG  . LEU B 1 155 ? 4.562   -4.732  45.823  1.00 36.15  ? 155  LEU B CG  1 
ATOM   4939 C  CD1 . LEU B 1 155 ? 5.540   -4.884  44.670  1.00 33.38  ? 155  LEU B CD1 1 
ATOM   4940 C  CD2 . LEU B 1 155 ? 3.189   -4.242  45.307  1.00 33.10  ? 155  LEU B CD2 1 
ATOM   4941 N  N   . CYS B 1 156 ? 5.709   -5.486  49.396  1.00 32.84  ? 156  CYS B N   1 
ATOM   4942 C  CA  . CYS B 1 156 ? 6.287   -4.573  50.382  1.00 34.23  ? 156  CYS B CA  1 
ATOM   4943 C  C   . CYS B 1 156 ? 7.629   -5.083  50.884  1.00 35.80  ? 156  CYS B C   1 
ATOM   4944 O  O   . CYS B 1 156 ? 8.571   -4.302  51.063  1.00 36.16  ? 156  CYS B O   1 
ATOM   4945 C  CB  . CYS B 1 156 ? 5.348   -4.380  51.577  1.00 34.03  ? 156  CYS B CB  1 
ATOM   4946 S  SG  . CYS B 1 156 ? 3.735   -3.661  51.158  1.00 36.68  ? 156  CYS B SG  1 
ATOM   4947 N  N   . GLY B 1 157 ? 7.728   -6.386  51.133  1.00 32.94  ? 157  GLY B N   1 
ATOM   4948 C  CA  . GLY B 1 157 ? 8.917   -6.930  51.770  1.00 32.90  ? 157  GLY B CA  1 
ATOM   4949 C  C   . GLY B 1 157 ? 10.054  -7.176  50.799  1.00 36.47  ? 157  GLY B C   1 
ATOM   4950 O  O   . GLY B 1 157 ? 11.227  -6.952  51.125  1.00 35.33  ? 157  GLY B O   1 
ATOM   4951 N  N   . PHE B 1 158 ? 9.721   -7.624  49.589  1.00 31.98  ? 158  PHE B N   1 
ATOM   4952 C  CA  . PHE B 1 158 ? 10.732  -8.156  48.689  1.00 31.67  ? 158  PHE B CA  1 
ATOM   4953 C  C   . PHE B 1 158 ? 10.655  -7.573  47.284  1.00 35.43  ? 158  PHE B C   1 
ATOM   4954 O  O   . PHE B 1 158 ? 11.409  -8.009  46.405  1.00 35.10  ? 158  PHE B O   1 
ATOM   4955 C  CB  . PHE B 1 158 ? 10.630  -9.685  48.667  1.00 33.75  ? 158  PHE B CB  1 
ATOM   4956 C  CG  . PHE B 1 158 ? 10.702  -10.294 50.053  1.00 34.26  ? 158  PHE B CG  1 
ATOM   4957 C  CD1 . PHE B 1 158 ? 11.921  -10.653 50.607  1.00 33.67  ? 158  PHE B CD1 1 
ATOM   4958 C  CD2 . PHE B 1 158 ? 9.553   -10.448 50.822  1.00 32.47  ? 158  PHE B CD2 1 
ATOM   4959 C  CE1 . PHE B 1 158 ? 12.005  -11.182 51.902  1.00 37.55  ? 158  PHE B CE1 1 
ATOM   4960 C  CE2 . PHE B 1 158 ? 9.622   -10.979 52.119  1.00 31.87  ? 158  PHE B CE2 1 
ATOM   4961 C  CZ  . PHE B 1 158 ? 10.857  -11.349 52.664  1.00 32.98  ? 158  PHE B CZ  1 
ATOM   4962 N  N   . ASN B 1 159 ? 9.809   -6.571  47.065  1.00 32.84  ? 159  ASN B N   1 
ATOM   4963 C  CA  . ASN B 1 159 ? 9.581   -6.019  45.727  1.00 35.49  ? 159  ASN B CA  1 
ATOM   4964 C  C   . ASN B 1 159 ? 9.344   -7.126  44.699  1.00 37.03  ? 159  ASN B C   1 
ATOM   4965 O  O   . ASN B 1 159 ? 9.830   -7.077  43.560  1.00 38.97  ? 159  ASN B O   1 
ATOM   4966 C  CB  . ASN B 1 159 ? 10.745  -5.114  45.302  1.00 37.87  ? 159  ASN B CB  1 
ATOM   4967 C  CG  . ASN B 1 159 ? 10.349  -4.134  44.213  1.00 49.71  ? 159  ASN B CG  1 
ATOM   4968 O  OD1 . ASN B 1 159 ? 9.159   -3.927  43.955  1.00 39.16  ? 159  ASN B OD1 1 
ATOM   4969 N  ND2 . ASN B 1 159 ? 11.342  -3.526  43.570  1.00 51.30  ? 159  ASN B ND2 1 
ATOM   4970 N  N   . TYR B 1 160 ? 8.579   -8.143  45.090  1.00 34.98  ? 160  TYR B N   1 
ATOM   4971 C  CA  . TYR B 1 160 ? 8.341   -9.293  44.231  1.00 32.49  ? 160  TYR B CA  1 
ATOM   4972 C  C   . TYR B 1 160 ? 6.840   -9.474  44.077  1.00 34.40  ? 160  TYR B C   1 
ATOM   4973 O  O   . TYR B 1 160 ? 6.124   -9.499  45.079  1.00 32.47  ? 160  TYR B O   1 
ATOM   4974 C  CB  . TYR B 1 160 ? 8.957   -10.555 44.813  1.00 35.85  ? 160  TYR B CB  1 
ATOM   4975 C  CG  . TYR B 1 160 ? 8.841   -11.762 43.914  1.00 37.89  ? 160  TYR B CG  1 
ATOM   4976 C  CD1 . TYR B 1 160 ? 9.788   -11.996 42.917  1.00 40.02  ? 160  TYR B CD1 1 
ATOM   4977 C  CD2 . TYR B 1 160 ? 7.794   -12.676 44.065  1.00 40.68  ? 160  TYR B CD2 1 
ATOM   4978 C  CE1 . TYR B 1 160 ? 9.696   -13.105 42.093  1.00 45.57  ? 160  TYR B CE1 1 
ATOM   4979 C  CE2 . TYR B 1 160 ? 7.696   -13.789 43.250  1.00 43.62  ? 160  TYR B CE2 1 
ATOM   4980 C  CZ  . TYR B 1 160 ? 8.646   -13.993 42.258  1.00 45.17  ? 160  TYR B CZ  1 
ATOM   4981 O  OH  . TYR B 1 160 ? 8.558   -15.108 41.440  1.00 52.90  ? 160  TYR B OH  1 
ATOM   4982 N  N   . ARG B 1 161 ? 6.360   -9.625  42.836  1.00 35.49  ? 161  ARG B N   1 
ATOM   4983 C  CA  . ARG B 1 161 ? 4.917   -9.735  42.582  1.00 34.52  ? 161  ARG B CA  1 
ATOM   4984 C  C   . ARG B 1 161 ? 4.507   -11.203 42.426  1.00 33.07  ? 161  ARG B C   1 
ATOM   4985 O  O   . ARG B 1 161 ? 4.860   -11.857 41.442  1.00 35.30  ? 161  ARG B O   1 
ATOM   4986 C  CB  . ARG B 1 161 ? 4.522   -8.889  41.366  1.00 35.05  ? 161  ARG B CB  1 
ATOM   4987 C  CG  . ARG B 1 161 ? 4.522   -7.398  41.722  1.00 38.24  ? 161  ARG B CG  1 
ATOM   4988 C  CD  . ARG B 1 161 ? 3.955   -6.498  40.652  1.00 36.78  ? 161  ARG B CD  1 
ATOM   4989 N  NE  . ARG B 1 161 ? 4.002   -5.090  41.033  1.00 37.27  ? 161  ARG B NE  1 
ATOM   4990 C  CZ  . ARG B 1 161 ? 2.989   -4.403  41.542  1.00 34.56  ? 161  ARG B CZ  1 
ATOM   4991 N  NH1 . ARG B 1 161 ? 1.818   -4.975  41.785  1.00 32.88  ? 161  ARG B NH1 1 
ATOM   4992 N  NH2 . ARG B 1 161 ? 3.152   -3.106  41.814  1.00 34.24  ? 161  ARG B NH2 1 
ATOM   4993 N  N   . PHE B 1 162 ? 3.768   -11.729 43.420  1.00 32.43  ? 162  PHE B N   1 
ATOM   4994 C  CA  . PHE B 1 162 ? 3.217   -13.076 43.314  1.00 33.56  ? 162  PHE B CA  1 
ATOM   4995 C  C   . PHE B 1 162 ? 2.047   -13.138 42.338  1.00 33.54  ? 162  PHE B C   1 
ATOM   4996 O  O   . PHE B 1 162 ? 1.694   -14.227 41.868  1.00 34.47  ? 162  PHE B O   1 
ATOM   4997 C  CB  . PHE B 1 162 ? 2.743   -13.584 44.684  1.00 35.67  ? 162  PHE B CB  1 
ATOM   4998 C  CG  . PHE B 1 162 ? 3.860   -13.938 45.629  1.00 36.41  ? 162  PHE B CG  1 
ATOM   4999 C  CD1 . PHE B 1 162 ? 4.556   -15.126 45.474  1.00 43.34  ? 162  PHE B CD1 1 
ATOM   5000 C  CD2 . PHE B 1 162 ? 4.180   -13.108 46.685  1.00 35.86  ? 162  PHE B CD2 1 
ATOM   5001 C  CE1 . PHE B 1 162 ? 5.579   -15.470 46.345  1.00 47.97  ? 162  PHE B CE1 1 
ATOM   5002 C  CE2 . PHE B 1 162 ? 5.208   -13.436 47.561  1.00 38.63  ? 162  PHE B CE2 1 
ATOM   5003 C  CZ  . PHE B 1 162 ? 5.910   -14.625 47.387  1.00 40.87  ? 162  PHE B CZ  1 
ATOM   5004 N  N   . ASN B 1 163 ? 1.440   -11.994 42.048  1.00 31.41  ? 163  ASN B N   1 
ATOM   5005 C  CA  . ASN B 1 163 ? 0.317   -11.886 41.117  1.00 31.57  ? 163  ASN B CA  1 
ATOM   5006 C  C   . ASN B 1 163 ? -0.761  -12.928 41.420  1.00 32.03  ? 163  ASN B C   1 
ATOM   5007 O  O   . ASN B 1 163 ? -1.284  -13.608 40.537  1.00 31.97  ? 163  ASN B O   1 
ATOM   5008 C  CB  . ASN B 1 163 ? 0.816   -11.967 39.675  1.00 34.35  ? 163  ASN B CB  1 
ATOM   5009 C  CG  . ASN B 1 163 ? 1.618   -10.739 39.292  1.00 33.73  ? 163  ASN B CG  1 
ATOM   5010 O  OD1 . ASN B 1 163 ? 1.179   -9.601  39.520  1.00 35.85  ? 163  ASN B OD1 1 
ATOM   5011 N  ND2 . ASN B 1 163 ? 2.818   -10.951 38.746  1.00 36.00  ? 163  ASN B ND2 1 
ATOM   5012 N  N   . SER B 1 164 ? -1.122  -13.015 42.703  1.00 31.82  ? 164  SER B N   1 
ATOM   5013 C  CA  . SER B 1 164 ? -2.117  -13.990 43.135  1.00 35.02  ? 164  SER B CA  1 
ATOM   5014 C  C   . SER B 1 164 ? -3.492  -13.707 42.544  1.00 35.22  ? 164  SER B C   1 
ATOM   5015 O  O   . SER B 1 164 ? -4.295  -14.637 42.396  1.00 33.75  ? 164  SER B O   1 
ATOM   5016 C  CB  . SER B 1 164 ? -2.208  -14.010 44.660  1.00 32.53  ? 164  SER B CB  1 
ATOM   5017 O  OG  . SER B 1 164 ? -0.968  -14.382 45.229  1.00 34.15  ? 164  SER B OG  1 
ATOM   5018 N  N   . PHE B 1 165 ? -3.799  -12.444 42.246  1.00 32.27  ? 165  PHE B N   1 
ATOM   5019 C  CA  . PHE B 1 165 ? -5.112  -12.137 41.684  1.00 34.72  ? 165  PHE B CA  1 
ATOM   5020 C  C   . PHE B 1 165 ? -5.195  -12.451 40.200  1.00 36.18  ? 165  PHE B C   1 
ATOM   5021 O  O   . PHE B 1 165 ? -6.292  -12.370 39.631  1.00 35.60  ? 165  PHE B O   1 
ATOM   5022 C  CB  . PHE B 1 165 ? -5.490  -10.673 41.946  1.00 32.57  ? 165  PHE B CB  1 
ATOM   5023 C  CG  . PHE B 1 165 ? -5.864  -10.415 43.385  1.00 35.44  ? 165  PHE B CG  1 
ATOM   5024 C  CD1 . PHE B 1 165 ? -7.026  -10.975 43.925  1.00 33.77  ? 165  PHE B CD1 1 
ATOM   5025 C  CD2 . PHE B 1 165 ? -5.042  -9.659  44.210  1.00 31.73  ? 165  PHE B CD2 1 
ATOM   5026 C  CE1 . PHE B 1 165 ? -7.372  -10.766 45.261  1.00 35.21  ? 165  PHE B CE1 1 
ATOM   5027 C  CE2 . PHE B 1 165 ? -5.376  -9.446  45.555  1.00 34.28  ? 165  PHE B CE2 1 
ATOM   5028 C  CZ  . PHE B 1 165 ? -6.550  -9.996  46.077  1.00 33.73  ? 165  PHE B CZ  1 
ATOM   5029 N  N   . TYR B 1 166 ? -4.082  -12.850 39.582  1.00 34.29  ? 166  TYR B N   1 
ATOM   5030 C  CA  . TYR B 1 166 ? -4.077  -13.375 38.218  1.00 33.85  ? 166  TYR B CA  1 
ATOM   5031 C  C   . TYR B 1 166 ? -4.232  -14.891 38.171  1.00 37.86  ? 166  TYR B C   1 
ATOM   5032 O  O   . TYR B 1 166 ? -4.058  -15.487 37.103  1.00 37.19  ? 166  TYR B O   1 
ATOM   5033 C  CB  . TYR B 1 166 ? -2.787  -12.944 37.505  1.00 34.08  ? 166  TYR B CB  1 
ATOM   5034 C  CG  . TYR B 1 166 ? -2.774  -11.464 37.331  1.00 33.78  ? 166  TYR B CG  1 
ATOM   5035 C  CD1 . TYR B 1 166 ? -2.359  -10.626 38.362  1.00 33.17  ? 166  TYR B CD1 1 
ATOM   5036 C  CD2 . TYR B 1 166 ? -3.251  -10.887 36.157  1.00 34.06  ? 166  TYR B CD2 1 
ATOM   5037 C  CE1 . TYR B 1 166 ? -2.383  -9.255  38.212  1.00 31.34  ? 166  TYR B CE1 1 
ATOM   5038 C  CE2 . TYR B 1 166 ? -3.288  -9.531  35.998  1.00 30.55  ? 166  TYR B CE2 1 
ATOM   5039 C  CZ  . TYR B 1 166 ? -2.850  -8.710  37.023  1.00 33.82  ? 166  TYR B CZ  1 
ATOM   5040 O  OH  . TYR B 1 166 ? -2.893  -7.347  36.861  1.00 34.22  ? 166  TYR B OH  1 
ATOM   5041 N  N   . ARG B 1 167 ? -4.563  -15.524 39.299  1.00 36.86  ? 167  ARG B N   1 
ATOM   5042 C  CA  . ARG B 1 167 ? -4.668  -16.974 39.394  1.00 36.27  ? 167  ARG B CA  1 
ATOM   5043 C  C   . ARG B 1 167 ? -6.019  -17.365 39.972  1.00 41.84  ? 167  ARG B C   1 
ATOM   5044 O  O   . ARG B 1 167 ? -6.445  -16.809 40.984  1.00 39.07  ? 167  ARG B O   1 
ATOM   5045 C  CB  . ARG B 1 167 ? -3.569  -17.552 40.287  1.00 41.29  ? 167  ARG B CB  1 
ATOM   5046 C  CG  . ARG B 1 167 ? -2.189  -17.170 39.867  1.00 42.43  ? 167  ARG B CG  1 
ATOM   5047 C  CD  . ARG B 1 167 ? -1.187  -17.537 40.935  1.00 45.17  ? 167  ARG B CD  1 
ATOM   5048 N  NE  . ARG B 1 167 ? 0.037   -16.778 40.734  1.00 49.28  ? 167  ARG B NE  1 
ATOM   5049 C  CZ  . ARG B 1 167 ? 1.105   -17.268 40.123  1.00 51.92  ? 167  ARG B CZ  1 
ATOM   5050 N  NH1 . ARG B 1 167 ? 1.138   -18.524 39.695  1.00 48.33  ? 167  ARG B NH1 1 
ATOM   5051 N  NH2 . ARG B 1 167 ? 2.154   -16.475 39.914  1.00 45.69  ? 167  ARG B NH2 1 
ATOM   5052 N  N   . ASP B 1 168 ? -6.675  -18.331 39.341  1.00 40.99  ? 168  ASP B N   1 
ATOM   5053 C  CA  . ASP B 1 168 ? -7.903  -18.909 39.876  1.00 43.47  ? 168  ASP B CA  1 
ATOM   5054 C  C   . ASP B 1 168 ? -7.645  -20.028 40.876  1.00 45.38  ? 168  ASP B C   1 
ATOM   5055 O  O   . ASP B 1 168 ? -8.520  -20.319 41.699  1.00 45.85  ? 168  ASP B O   1 
ATOM   5056 C  CB  . ASP B 1 168 ? -8.784  -19.399 38.711  1.00 41.98  ? 168  ASP B CB  1 
ATOM   5057 C  CG  . ASP B 1 168 ? -8.105  -20.483 37.880  1.00 50.01  ? 168  ASP B CG  1 
ATOM   5058 O  OD1 . ASP B 1 168 ? -8.191  -21.683 38.216  1.00 58.60  ? 168  ASP B OD1 1 
ATOM   5059 O  OD2 . ASP B 1 168 ? -7.431  -20.122 36.894  1.00 54.76  ? 168  ASP B OD2 1 
ATOM   5060 N  N   . GLN B 1 169 ? -6.473  -20.639 40.835  1.00 43.69  ? 169  GLN B N   1 
ATOM   5061 C  CA  . GLN B 1 169 ? -6.019  -21.623 41.796  1.00 49.40  ? 169  GLN B CA  1 
ATOM   5062 C  C   . GLN B 1 169 ? -5.080  -20.969 42.798  1.00 48.11  ? 169  GLN B C   1 
ATOM   5063 O  O   . GLN B 1 169 ? -4.573  -19.869 42.558  1.00 45.26  ? 169  GLN B O   1 
ATOM   5064 C  CB  . GLN B 1 169 ? -5.306  -22.769 41.073  1.00 55.07  ? 169  GLN B CB  1 
ATOM   5065 C  CG  . GLN B 1 169 ? -6.074  -24.091 41.109  1.00 66.47  ? 169  GLN B CG  1 
ATOM   5066 C  CD  . GLN B 1 169 ? -5.171  -25.304 40.924  1.00 74.23  ? 169  GLN B CD  1 
ATOM   5067 O  OE1 . GLN B 1 169 ? -4.988  -25.789 39.803  1.00 74.81  ? 169  GLN B OE1 1 
ATOM   5068 N  NE2 . GLN B 1 169 ? -4.597  -25.794 42.025  1.00 68.88  ? 169  GLN B NE2 1 
ATOM   5069 N  N   . PRO B 1 170 ? -4.840  -21.595 43.950  1.00 47.97  ? 170  PRO B N   1 
ATOM   5070 C  CA  . PRO B 1 170 ? -3.889  -21.012 44.900  1.00 48.89  ? 170  PRO B CA  1 
ATOM   5071 C  C   . PRO B 1 170 ? -2.511  -20.937 44.271  1.00 44.70  ? 170  PRO B C   1 
ATOM   5072 O  O   . PRO B 1 170 ? -2.134  -21.774 43.443  1.00 42.60  ? 170  PRO B O   1 
ATOM   5073 C  CB  . PRO B 1 170 ? -3.909  -21.986 46.088  1.00 46.32  ? 170  PRO B CB  1 
ATOM   5074 C  CG  . PRO B 1 170 ? -5.102  -22.819 45.904  1.00 49.17  ? 170  PRO B CG  1 
ATOM   5075 C  CD  . PRO B 1 170 ? -5.372  -22.879 44.430  1.00 46.05  ? 170  PRO B CD  1 
ATOM   5076 N  N   . HIS B 1 171 ? -1.760  -19.914 44.662  1.00 45.79  ? 171  HIS B N   1 
ATOM   5077 C  CA  . HIS B 1 171 ? -0.369  -19.831 44.244  1.00 43.34  ? 171  HIS B CA  1 
ATOM   5078 C  C   . HIS B 1 171 ? 0.374   -21.093 44.684  1.00 45.66  ? 171  HIS B C   1 
ATOM   5079 O  O   . HIS B 1 171 ? 0.139   -21.597 45.789  1.00 39.94  ? 171  HIS B O   1 
ATOM   5080 C  CB  . HIS B 1 171 ? 0.301   -18.589 44.840  1.00 43.85  ? 171  HIS B CB  1 
ATOM   5081 C  CG  . HIS B 1 171 ? 1.646   -18.292 44.251  1.00 43.98  ? 171  HIS B CG  1 
ATOM   5082 N  ND1 . HIS B 1 171 ? 2.768   -19.041 44.533  1.00 44.63  ? 171  HIS B ND1 1 
ATOM   5083 C  CD2 . HIS B 1 171 ? 2.042   -17.338 43.374  1.00 47.48  ? 171  HIS B CD2 1 
ATOM   5084 C  CE1 . HIS B 1 171 ? 3.801   -18.555 43.869  1.00 46.28  ? 171  HIS B CE1 1 
ATOM   5085 N  NE2 . HIS B 1 171 ? 3.388   -17.521 43.156  1.00 46.51  ? 171  HIS B NE2 1 
ATOM   5086 N  N   . PRO B 1 172 ? 1.269   -21.634 43.849  1.00 41.74  ? 172  PRO B N   1 
ATOM   5087 C  CA  . PRO B 1 172 ? 2.001   -22.855 44.233  1.00 42.54  ? 172  PRO B CA  1 
ATOM   5088 C  C   . PRO B 1 172 ? 2.710   -22.751 45.576  1.00 43.02  ? 172  PRO B C   1 
ATOM   5089 O  O   . PRO B 1 172 ? 2.822   -23.753 46.304  1.00 37.69  ? 172  PRO B O   1 
ATOM   5090 C  CB  . PRO B 1 172 ? 3.008   -23.025 43.090  1.00 45.36  ? 172  PRO B CB  1 
ATOM   5091 C  CG  . PRO B 1 172 ? 2.387   -22.345 41.924  1.00 44.37  ? 172  PRO B CG  1 
ATOM   5092 C  CD  . PRO B 1 172 ? 1.568   -21.204 42.468  1.00 47.41  ? 172  PRO B CD  1 
ATOM   5093 N  N   . PHE B 1 173 ? 3.231   -21.571 45.918  1.00 41.94  ? 173  PHE B N   1 
ATOM   5094 C  CA  . PHE B 1 173 ? 3.841   -21.423 47.231  1.00 39.08  ? 173  PHE B CA  1 
ATOM   5095 C  C   . PHE B 1 173 ? 2.812   -21.696 48.309  1.00 35.22  ? 173  PHE B C   1 
ATOM   5096 O  O   . PHE B 1 173 ? 3.108   -22.343 49.315  1.00 37.13  ? 173  PHE B O   1 
ATOM   5097 C  CB  . PHE B 1 173 ? 4.442   -20.025 47.392  1.00 39.84  ? 173  PHE B CB  1 
ATOM   5098 C  CG  . PHE B 1 173 ? 5.168   -19.819 48.703  1.00 39.24  ? 173  PHE B CG  1 
ATOM   5099 C  CD1 . PHE B 1 173 ? 4.493   -19.358 49.818  1.00 37.53  ? 173  PHE B CD1 1 
ATOM   5100 C  CD2 . PHE B 1 173 ? 6.527   -20.070 48.806  1.00 35.66  ? 173  PHE B CD2 1 
ATOM   5101 C  CE1 . PHE B 1 173 ? 5.163   -19.165 51.032  1.00 35.85  ? 173  PHE B CE1 1 
ATOM   5102 C  CE2 . PHE B 1 173 ? 7.204   -19.866 50.001  1.00 37.41  ? 173  PHE B CE2 1 
ATOM   5103 C  CZ  . PHE B 1 173 ? 6.518   -19.420 51.118  1.00 39.21  ? 173  PHE B CZ  1 
ATOM   5104 N  N   . ILE B 1 174 ? 1.581   -21.238 48.095  1.00 35.16  ? 174  ILE B N   1 
ATOM   5105 C  CA  . ILE B 1 174 ? 0.540   -21.435 49.091  1.00 37.43  ? 174  ILE B CA  1 
ATOM   5106 C  C   . ILE B 1 174 ? 0.194   -22.911 49.202  1.00 34.64  ? 174  ILE B C   1 
ATOM   5107 O  O   . ILE B 1 174 ? 0.049   -23.449 50.303  1.00 37.93  ? 174  ILE B O   1 
ATOM   5108 C  CB  . ILE B 1 174 ? -0.703  -20.595 48.757  1.00 35.85  ? 174  ILE B CB  1 
ATOM   5109 C  CG1 . ILE B 1 174 ? -0.389  -19.092 48.847  1.00 37.77  ? 174  ILE B CG1 1 
ATOM   5110 C  CG2 . ILE B 1 174 ? -1.839  -20.991 49.682  1.00 36.95  ? 174  ILE B CG2 1 
ATOM   5111 C  CD1 . ILE B 1 174 ? 0.088   -18.607 50.244  1.00 34.62  ? 174  ILE B CD1 1 
ATOM   5112 N  N   . THR B 1 175 ? 0.045   -23.585 48.059  1.00 35.06  ? 175  THR B N   1 
ATOM   5113 C  CA  . THR B 1 175 ? -0.270  -25.009 48.085  1.00 36.22  ? 175  THR B CA  1 
ATOM   5114 C  C   . THR B 1 175 ? 0.745   -25.784 48.915  1.00 36.69  ? 175  THR B C   1 
ATOM   5115 O  O   . THR B 1 175 ? 0.378   -26.616 49.753  1.00 37.23  ? 175  THR B O   1 
ATOM   5116 C  CB  . THR B 1 175 ? -0.330  -25.561 46.663  1.00 37.32  ? 175  THR B CB  1 
ATOM   5117 O  OG1 . THR B 1 175 ? -1.404  -24.922 45.968  1.00 40.97  ? 175  THR B OG1 1 
ATOM   5118 C  CG2 . THR B 1 175 ? -0.550  -27.074 46.706  1.00 36.98  ? 175  THR B CG2 1 
ATOM   5119 N  N   . SER B 1 176 ? 2.034   -25.507 48.706  1.00 36.48  ? 176  SER B N   1 
ATOM   5120 C  CA  . SER B 1 176 ? 3.065   -26.249 49.415  1.00 36.44  ? 176  SER B CA  1 
ATOM   5121 C  C   . SER B 1 176 ? 3.185   -25.804 50.868  1.00 34.11  ? 176  SER B C   1 
ATOM   5122 O  O   . SER B 1 176 ? 3.442   -26.631 51.746  1.00 32.90  ? 176  SER B O   1 
ATOM   5123 C  CB  . SER B 1 176 ? 4.400   -26.094 48.690  1.00 36.20  ? 176  SER B CB  1 
ATOM   5124 O  OG  . SER B 1 176 ? 4.435   -26.933 47.548  1.00 38.51  ? 176  SER B OG  1 
ATOM   5125 N  N   . MET B 1 177 ? 3.000   -24.509 51.134  1.00 33.63  ? 177  MET B N   1 
ATOM   5126 C  CA  . MET B 1 177 ? 3.046   -24.025 52.511  1.00 32.90  ? 177  MET B CA  1 
ATOM   5127 C  C   . MET B 1 177 ? 1.919   -24.627 53.336  1.00 34.46  ? 177  MET B C   1 
ATOM   5128 O  O   . MET B 1 177 ? 2.138   -25.091 54.458  1.00 32.82  ? 177  MET B O   1 
ATOM   5129 C  CB  . MET B 1 177 ? 2.978   -22.497 52.552  1.00 32.72  ? 177  MET B CB  1 
ATOM   5130 C  CG  . MET B 1 177 ? 2.816   -21.976 53.991  1.00 34.95  ? 177  MET B CG  1 
ATOM   5131 S  SD  . MET B 1 177 ? 2.090   -20.325 54.142  1.00 35.91  ? 177  MET B SD  1 
ATOM   5132 C  CE  . MET B 1 177 ? 0.355   -20.626 53.847  1.00 33.60  ? 177  MET B CE  1 
ATOM   5133 N  N   . VAL B 1 178 ? 0.697   -24.623 52.795  1.00 36.32  ? 178  VAL B N   1 
ATOM   5134 C  CA  . VAL B 1 178 ? -0.429  -25.206 53.519  1.00 36.51  ? 178  VAL B CA  1 
ATOM   5135 C  C   . VAL B 1 178 ? -0.192  -26.686 53.786  1.00 37.28  ? 178  VAL B C   1 
ATOM   5136 O  O   . VAL B 1 178 ? -0.429  -27.178 54.897  1.00 36.21  ? 178  VAL B O   1 
ATOM   5137 C  CB  . VAL B 1 178 ? -1.731  -24.972 52.740  1.00 34.65  ? 178  VAL B CB  1 
ATOM   5138 C  CG1 . VAL B 1 178 ? -2.865  -25.835 53.316  1.00 37.81  ? 178  VAL B CG1 1 
ATOM   5139 C  CG2 . VAL B 1 178 ? -2.077  -23.477 52.762  1.00 34.80  ? 178  VAL B CG2 1 
ATOM   5140 N  N   . ARG B 1 179 ? 0.283   -27.420 52.780  1.00 36.71  ? 179  ARG B N   1 
ATOM   5141 C  CA  . ARG B 1 179 ? 0.518   -28.850 52.960  1.00 34.48  ? 179  ARG B CA  1 
ATOM   5142 C  C   . ARG B 1 179 ? 1.619   -29.111 53.978  1.00 36.45  ? 179  ARG B C   1 
ATOM   5143 O  O   . ARG B 1 179 ? 1.538   -30.086 54.733  1.00 36.50  ? 179  ARG B O   1 
ATOM   5144 C  CB  . ARG B 1 179 ? 0.855   -29.494 51.612  1.00 39.41  ? 179  ARG B CB  1 
ATOM   5145 C  CG  . ARG B 1 179 ? 0.566   -30.984 51.522  1.00 43.96  ? 179  ARG B CG  1 
ATOM   5146 C  CD  . ARG B 1 179 ? 0.304   -31.407 50.061  1.00 42.92  ? 179  ARG B CD  1 
ATOM   5147 N  NE  . ARG B 1 179 ? 1.344   -30.914 49.160  1.00 41.83  ? 179  ARG B NE  1 
ATOM   5148 C  CZ  . ARG B 1 179 ? 1.146   -30.590 47.889  1.00 48.65  ? 179  ARG B CZ  1 
ATOM   5149 N  NH1 . ARG B 1 179 ? -0.036  -30.753 47.307  1.00 46.39  ? 179  ARG B NH1 1 
ATOM   5150 N  NH2 . ARG B 1 179 ? 2.153   -30.078 47.185  1.00 44.65  ? 179  ARG B NH2 1 
ATOM   5151 N  N   . ALA B 1 180 ? 2.638   -28.243 54.034  1.00 33.84  ? 180  ALA B N   1 
ATOM   5152 C  CA  . ALA B 1 180 ? 3.704   -28.397 55.021  1.00 35.36  ? 180  ALA B CA  1 
ATOM   5153 C  C   . ALA B 1 180 ? 3.202   -28.114 56.438  1.00 35.40  ? 180  ALA B C   1 
ATOM   5154 O  O   . ALA B 1 180 ? 3.545   -28.838 57.382  1.00 32.80  ? 180  ALA B O   1 
ATOM   5155 C  CB  . ALA B 1 180 ? 4.874   -27.469 54.670  1.00 36.92  ? 180  ALA B CB  1 
ATOM   5156 N  N   . LEU B 1 181 ? 2.418   -27.045 56.612  1.00 33.00  ? 181  LEU B N   1 
ATOM   5157 C  CA  . LEU B 1 181 ? 1.808   -26.770 57.910  1.00 34.47  ? 181  LEU B CA  1 
ATOM   5158 C  C   . LEU B 1 181 ? 0.870   -27.897 58.328  1.00 35.43  ? 181  LEU B C   1 
ATOM   5159 O  O   . LEU B 1 181 ? 0.823   -28.269 59.505  1.00 34.42  ? 181  LEU B O   1 
ATOM   5160 C  CB  . LEU B 1 181 ? 1.046   -25.439 57.857  1.00 31.38  ? 181  LEU B CB  1 
ATOM   5161 C  CG  . LEU B 1 181 ? 1.898   -24.194 57.606  1.00 28.69  ? 181  LEU B CG  1 
ATOM   5162 C  CD1 . LEU B 1 181 ? 0.990   -22.972 57.460  1.00 36.18  ? 181  LEU B CD1 1 
ATOM   5163 C  CD2 . LEU B 1 181 ? 2.950   -24.022 58.719  1.00 35.32  ? 181  LEU B CD2 1 
ATOM   5164 N  N   . ASP B 1 182 ? 0.082   -28.416 57.377  1.00 36.44  ? 182  ASP B N   1 
ATOM   5165 C  CA  . ASP B 1 182 ? -0.781  -29.573 57.619  1.00 37.27  ? 182  ASP B CA  1 
ATOM   5166 C  C   . ASP B 1 182 ? 0.023   -30.730 58.184  1.00 36.64  ? 182  ASP B C   1 
ATOM   5167 O  O   . ASP B 1 182 ? -0.396  -31.408 59.132  1.00 37.87  ? 182  ASP B O   1 
ATOM   5168 C  CB  . ASP B 1 182 ? -1.416  -30.052 56.313  1.00 40.53  ? 182  ASP B CB  1 
ATOM   5169 C  CG  . ASP B 1 182 ? -2.581  -29.231 55.873  1.00 48.09  ? 182  ASP B CG  1 
ATOM   5170 O  OD1 . ASP B 1 182 ? -3.187  -28.528 56.705  1.00 49.60  ? 182  ASP B OD1 1 
ATOM   5171 O  OD2 . ASP B 1 182 ? -2.908  -29.334 54.668  1.00 46.46  ? 182  ASP B OD2 1 
ATOM   5172 N  N   . GLU B 1 183 ? 1.157   -31.002 57.553  1.00 36.04  ? 183  GLU B N   1 
ATOM   5173 C  CA  . GLU B 1 183 ? 1.982   -32.132 57.938  1.00 36.86  ? 183  GLU B CA  1 
ATOM   5174 C  C   . GLU B 1 183 ? 2.582   -31.901 59.314  1.00 34.83  ? 183  GLU B C   1 
ATOM   5175 O  O   . GLU B 1 183 ? 2.580   -32.806 60.152  1.00 33.87  ? 183  GLU B O   1 
ATOM   5176 C  CB  . GLU B 1 183 ? 3.063   -32.351 56.872  1.00 36.06  ? 183  GLU B CB  1 
ATOM   5177 C  CG  . GLU B 1 183 ? 4.184   -33.294 57.291  1.00 39.06  ? 183  GLU B CG  1 
ATOM   5178 C  CD  . GLU B 1 183 ? 3.754   -34.761 57.400  1.00 41.51  ? 183  GLU B CD  1 
ATOM   5179 O  OE1 . GLU B 1 183 ? 2.580   -35.085 57.099  1.00 39.79  ? 183  GLU B OE1 1 
ATOM   5180 O  OE2 . GLU B 1 183 ? 4.607   -35.581 57.809  1.00 40.58  ? 183  GLU B OE2 1 
ATOM   5181 N  N   . ALA B 1 184 ? 3.072   -30.681 59.574  1.00 33.22  ? 184  ALA B N   1 
ATOM   5182 C  CA  . ALA B 1 184 ? 3.586   -30.364 60.900  1.00 31.48  ? 184  ALA B CA  1 
ATOM   5183 C  C   . ALA B 1 184 ? 2.516   -30.588 61.966  1.00 35.03  ? 184  ALA B C   1 
ATOM   5184 O  O   . ALA B 1 184 ? 2.797   -31.170 63.021  1.00 35.64  ? 184  ALA B O   1 
ATOM   5185 C  CB  . ALA B 1 184 ? 4.101   -28.919 60.940  1.00 35.82  ? 184  ALA B CB  1 
ATOM   5186 N  N   . MET B 1 185 ? 1.274   -30.150 61.705  1.00 33.37  ? 185  MET B N   1 
ATOM   5187 C  CA  . MET B 1 185 ? 0.194   -30.373 62.670  1.00 32.65  ? 185  MET B CA  1 
ATOM   5188 C  C   . MET B 1 185 ? -0.122  -31.857 62.850  1.00 33.70  ? 185  MET B C   1 
ATOM   5189 O  O   . MET B 1 185 ? -0.309  -32.326 63.979  1.00 34.56  ? 185  MET B O   1 
ATOM   5190 C  CB  . MET B 1 185 ? -1.077  -29.662 62.237  1.00 32.40  ? 185  MET B CB  1 
ATOM   5191 C  CG  . MET B 1 185 ? -2.061  -29.470 63.378  1.00 31.50  ? 185  MET B CG  1 
ATOM   5192 S  SD  . MET B 1 185 ? -3.572  -28.668 62.845  1.00 35.24  ? 185  MET B SD  1 
ATOM   5193 C  CE  . MET B 1 185 ? -4.265  -29.988 61.794  1.00 35.70  ? 185  MET B CE  1 
ATOM   5194 N  N   . ASN B 1 186 ? -0.263  -32.595 61.740  1.00 34.99  ? 186  ASN B N   1 
ATOM   5195 C  CA  . ASN B 1 186 ? -0.551  -34.026 61.828  1.00 36.89  ? 186  ASN B CA  1 
ATOM   5196 C  C   . ASN B 1 186 ? 0.584   -34.795 62.493  1.00 39.24  ? 186  ASN B C   1 
ATOM   5197 O  O   . ASN B 1 186 ? 0.340   -35.789 63.188  1.00 39.23  ? 186  ASN B O   1 
ATOM   5198 C  CB  . ASN B 1 186 ? -0.846  -34.599 60.430  1.00 39.54  ? 186  ASN B CB  1 
ATOM   5199 C  CG  . ASN B 1 186 ? -1.403  -36.027 60.483  1.00 47.06  ? 186  ASN B CG  1 
ATOM   5200 O  OD1 . ASN B 1 186 ? -0.647  -37.002 60.457  1.00 48.44  ? 186  ASN B OD1 1 
ATOM   5201 N  ND2 . ASN B 1 186 ? -2.724  -36.150 60.616  1.00 48.05  ? 186  ASN B ND2 1 
ATOM   5202 N  N   . LYS B 1 187 ? 1.824   -34.349 62.293  1.00 34.29  ? 187  LYS B N   1 
ATOM   5203 C  CA  . LYS B 1 187 ? 2.963   -35.009 62.912  1.00 37.28  ? 187  LYS B CA  1 
ATOM   5204 C  C   . LYS B 1 187 ? 2.884   -34.947 64.439  1.00 37.45  ? 187  LYS B C   1 
ATOM   5205 O  O   . LYS B 1 187 ? 3.402   -35.839 65.122  1.00 36.14  ? 187  LYS B O   1 
ATOM   5206 C  CB  . LYS B 1 187 ? 4.249   -34.359 62.388  1.00 39.54  ? 187  LYS B CB  1 
ATOM   5207 C  CG  . LYS B 1 187 ? 5.351   -35.318 62.033  1.00 47.54  ? 187  LYS B CG  1 
ATOM   5208 C  CD  . LYS B 1 187 ? 6.633   -34.578 61.606  1.00 46.92  ? 187  LYS B CD  1 
ATOM   5209 C  CE  . LYS B 1 187 ? 7.850   -35.193 62.305  1.00 50.74  ? 187  LYS B CE  1 
ATOM   5210 N  NZ  . LYS B 1 187 ? 9.163   -34.789 61.710  1.00 56.47  ? 187  LYS B NZ  1 
ATOM   5211 N  N   . LEU B 1 188 ? 2.191   -33.939 64.990  1.00 37.37  ? 188  LEU B N   1 
ATOM   5212 C  CA  . LEU B 1 188 ? 2.149   -33.769 66.443  1.00 39.03  ? 188  LEU B CA  1 
ATOM   5213 C  C   . LEU B 1 188 ? 1.581   -34.991 67.145  1.00 35.88  ? 188  LEU B C   1 
ATOM   5214 O  O   . LEU B 1 188 ? 2.008   -35.319 68.256  1.00 38.32  ? 188  LEU B O   1 
ATOM   5215 C  CB  . LEU B 1 188 ? 1.309   -32.547 66.829  1.00 37.74  ? 188  LEU B CB  1 
ATOM   5216 C  CG  . LEU B 1 188 ? 1.821   -31.214 66.309  1.00 35.99  ? 188  LEU B CG  1 
ATOM   5217 C  CD1 . LEU B 1 188 ? 0.781   -30.121 66.562  1.00 35.11  ? 188  LEU B CD1 1 
ATOM   5218 C  CD2 . LEU B 1 188 ? 3.127   -30.909 67.010  1.00 38.98  ? 188  LEU B CD2 1 
ATOM   5219 N  N   . GLN B 1 189 ? 0.615   -35.663 66.531  1.00 38.19  ? 189  GLN B N   1 
ATOM   5220 C  CA  . GLN B 1 189 ? -0.076  -36.765 67.184  1.00 41.93  ? 189  GLN B CA  1 
ATOM   5221 C  C   . GLN B 1 189 ? 0.483   -38.141 66.832  1.00 42.96  ? 189  GLN B C   1 
ATOM   5222 O  O   . GLN B 1 189 ? -0.057  -39.145 67.306  1.00 41.84  ? 189  GLN B O   1 
ATOM   5223 C  CB  . GLN B 1 189 ? -1.575  -36.716 66.846  1.00 40.71  ? 189  GLN B CB  1 
ATOM   5224 C  CG  . GLN B 1 189 ? -1.890  -36.612 65.364  1.00 41.58  ? 189  GLN B CG  1 
ATOM   5225 C  CD  . GLN B 1 189 ? -2.071  -37.971 64.708  1.00 48.14  ? 189  GLN B CD  1 
ATOM   5226 O  OE1 . GLN B 1 189 ? -2.959  -38.741 65.083  1.00 50.61  ? 189  GLN B OE1 1 
ATOM   5227 N  NE2 . GLN B 1 189 ? -1.239  -38.267 63.710  1.00 46.25  ? 189  GLN B NE2 1 
ATOM   5228 N  N   . ARG B 1 190 ? 1.531   -38.231 66.012  1.00 40.56  ? 190  ARG B N   1 
ATOM   5229 C  CA  . ARG B 1 190 ? 2.012   -39.545 65.578  1.00 41.68  ? 190  ARG B CA  1 
ATOM   5230 C  C   . ARG B 1 190 ? 2.826   -40.179 66.699  1.00 44.83  ? 190  ARG B C   1 
ATOM   5231 O  O   . ARG B 1 190 ? 3.891   -39.677 67.061  1.00 40.93  ? 190  ARG B O   1 
ATOM   5232 C  CB  . ARG B 1 190 ? 2.845   -39.436 64.304  1.00 40.72  ? 190  ARG B CB  1 
ATOM   5233 C  CG  . ARG B 1 190 ? 2.070   -38.931 63.111  1.00 40.55  ? 190  ARG B CG  1 
ATOM   5234 C  CD  . ARG B 1 190 ? 2.921   -38.815 61.850  1.00 39.49  ? 190  ARG B CD  1 
ATOM   5235 N  NE  . ARG B 1 190 ? 2.110   -38.150 60.840  1.00 37.56  ? 190  ARG B NE  1 
ATOM   5236 C  CZ  . ARG B 1 190 ? 2.577   -37.550 59.756  1.00 41.12  ? 190  ARG B CZ  1 
ATOM   5237 N  NH1 . ARG B 1 190 ? 3.867   -37.579 59.446  1.00 38.17  ? 190  ARG B NH1 1 
ATOM   5238 N  NH2 . ARG B 1 190 ? 1.733   -36.885 58.977  1.00 41.94  ? 190  ARG B NH2 1 
ATOM   5239 N  N   . ALA B 1 191 ? 2.327   -41.282 67.259  1.00 46.40  ? 191  ALA B N   1 
ATOM   5240 C  CA  . ALA B 1 191 ? 3.093   -41.988 68.282  1.00 47.75  ? 191  ALA B CA  1 
ATOM   5241 C  C   . ALA B 1 191 ? 4.349   -42.619 67.690  1.00 50.81  ? 191  ALA B C   1 
ATOM   5242 O  O   . ALA B 1 191 ? 5.407   -42.638 68.334  1.00 49.29  ? 191  ALA B O   1 
ATOM   5243 C  CB  . ALA B 1 191 ? 2.222   -43.051 68.948  1.00 49.32  ? 191  ALA B CB  1 
ATOM   5244 N  N   . ASN B 1 192 ? 4.261   -43.127 66.462  1.00 47.61  ? 192  ASN B N   1 
ATOM   5245 C  CA  . ASN B 1 192 ? 5.391   -43.756 65.781  1.00 46.44  ? 192  ASN B CA  1 
ATOM   5246 C  C   . ASN B 1 192 ? 5.650   -42.977 64.501  1.00 45.40  ? 192  ASN B C   1 
ATOM   5247 O  O   . ASN B 1 192 ? 5.137   -43.337 63.429  1.00 48.26  ? 192  ASN B O   1 
ATOM   5248 C  CB  . ASN B 1 192 ? 5.114   -45.228 65.482  1.00 49.94  ? 192  ASN B CB  1 
ATOM   5249 C  CG  . ASN B 1 192 ? 4.407   -45.926 66.620  1.00 54.78  ? 192  ASN B CG  1 
ATOM   5250 O  OD1 . ASN B 1 192 ? 4.949   -46.038 67.711  1.00 55.83  ? 192  ASN B OD1 1 
ATOM   5251 N  ND2 . ASN B 1 192 ? 3.187   -46.395 66.372  1.00 56.44  ? 192  ASN B ND2 1 
ATOM   5252 N  N   . PRO B 1 193 ? 6.434   -41.901 64.569  1.00 46.23  ? 193  PRO B N   1 
ATOM   5253 C  CA  . PRO B 1 193 ? 6.659   -41.076 63.374  1.00 46.50  ? 193  PRO B CA  1 
ATOM   5254 C  C   . PRO B 1 193 ? 7.290   -41.842 62.231  1.00 50.95  ? 193  PRO B C   1 
ATOM   5255 O  O   . PRO B 1 193 ? 7.171   -41.412 61.074  1.00 46.27  ? 193  PRO B O   1 
ATOM   5256 C  CB  . PRO B 1 193 ? 7.594   -39.964 63.875  1.00 48.60  ? 193  PRO B CB  1 
ATOM   5257 C  CG  . PRO B 1 193 ? 7.552   -40.032 65.370  1.00 51.40  ? 193  PRO B CG  1 
ATOM   5258 C  CD  . PRO B 1 193 ? 7.199   -41.434 65.738  1.00 51.88  ? 193  PRO B CD  1 
ATOM   5259 N  N   . ASP B 1 194 ? 7.962   -42.958 62.514  1.00 49.98  ? 194  ASP B N   1 
ATOM   5260 C  CA  . ASP B 1 194 ? 8.704   -43.680 61.494  1.00 51.05  ? 194  ASP B CA  1 
ATOM   5261 C  C   . ASP B 1 194 ? 7.952   -44.893 60.969  1.00 52.28  ? 194  ASP B C   1 
ATOM   5262 O  O   . ASP B 1 194 ? 8.496   -45.636 60.146  1.00 53.24  ? 194  ASP B O   1 
ATOM   5263 C  CB  . ASP B 1 194 ? 10.071  -44.084 62.040  1.00 56.24  ? 194  ASP B CB  1 
ATOM   5264 C  CG  . ASP B 1 194 ? 10.985  -42.888 62.213  1.00 57.67  ? 194  ASP B CG  1 
ATOM   5265 O  OD1 . ASP B 1 194 ? 10.837  -41.909 61.445  1.00 54.31  ? 194  ASP B OD1 1 
ATOM   5266 O  OD2 . ASP B 1 194 ? 11.841  -42.916 63.120  1.00 66.71  ? 194  ASP B OD2 1 
ATOM   5267 N  N   . ASP B 1 195 ? 6.723   -45.105 61.425  1.00 49.37  ? 195  ASP B N   1 
ATOM   5268 C  CA  . ASP B 1 195 ? 5.820   -46.040 60.777  1.00 49.94  ? 195  ASP B CA  1 
ATOM   5269 C  C   . ASP B 1 195 ? 5.839   -45.813 59.262  1.00 53.97  ? 195  ASP B C   1 
ATOM   5270 O  O   . ASP B 1 195 ? 5.805   -44.657 58.812  1.00 50.01  ? 195  ASP B O   1 
ATOM   5271 C  CB  . ASP B 1 195 ? 4.412   -45.844 61.346  1.00 52.68  ? 195  ASP B CB  1 
ATOM   5272 C  CG  . ASP B 1 195 ? 3.396   -46.846 60.815  1.00 55.83  ? 195  ASP B CG  1 
ATOM   5273 O  OD1 . ASP B 1 195 ? 3.472   -47.260 59.637  1.00 57.34  ? 195  ASP B OD1 1 
ATOM   5274 O  OD2 . ASP B 1 195 ? 2.487   -47.204 61.595  1.00 62.95  ? 195  ASP B OD2 1 
ATOM   5275 N  N   . PRO B 1 196 ? 5.911   -46.873 58.451  1.00 52.52  ? 196  PRO B N   1 
ATOM   5276 C  CA  . PRO B 1 196 ? 5.967   -46.682 56.989  1.00 50.85  ? 196  PRO B CA  1 
ATOM   5277 C  C   . PRO B 1 196 ? 4.728   -46.024 56.421  1.00 49.78  ? 196  PRO B C   1 
ATOM   5278 O  O   . PRO B 1 196 ? 4.767   -45.520 55.291  1.00 52.08  ? 196  PRO B O   1 
ATOM   5279 C  CB  . PRO B 1 196 ? 6.129   -48.112 56.452  1.00 55.76  ? 196  PRO B CB  1 
ATOM   5280 C  CG  . PRO B 1 196 ? 6.697   -48.890 57.603  1.00 54.75  ? 196  PRO B CG  1 
ATOM   5281 C  CD  . PRO B 1 196 ? 6.097   -48.283 58.837  1.00 54.99  ? 196  PRO B CD  1 
ATOM   5282 N  N   . ALA B 1 197 ? 3.622   -46.019 57.161  1.00 50.93  ? 197  ALA B N   1 
ATOM   5283 C  CA  . ALA B 1 197 ? 2.436   -45.314 56.699  1.00 48.79  ? 197  ALA B CA  1 
ATOM   5284 C  C   . ALA B 1 197 ? 2.702   -43.828 56.469  1.00 47.38  ? 197  ALA B C   1 
ATOM   5285 O  O   . ALA B 1 197 ? 1.914   -43.170 55.783  1.00 48.96  ? 197  ALA B O   1 
ATOM   5286 C  CB  . ALA B 1 197 ? 1.298   -45.502 57.706  1.00 51.71  ? 197  ALA B CB  1 
ATOM   5287 N  N   . TYR B 1 198 ? 3.785   -43.285 57.026  1.00 45.01  ? 198  TYR B N   1 
ATOM   5288 C  CA  . TYR B 1 198 ? 4.116   -41.870 56.883  1.00 44.54  ? 198  TYR B CA  1 
ATOM   5289 C  C   . TYR B 1 198 ? 5.226   -41.610 55.868  1.00 46.48  ? 198  TYR B C   1 
ATOM   5290 O  O   . TYR B 1 198 ? 5.664   -40.459 55.730  1.00 41.87  ? 198  TYR B O   1 
ATOM   5291 C  CB  . TYR B 1 198 ? 4.509   -41.286 58.248  1.00 39.91  ? 198  TYR B CB  1 
ATOM   5292 C  CG  . TYR B 1 198 ? 3.473   -41.527 59.331  1.00 43.42  ? 198  TYR B CG  1 
ATOM   5293 C  CD1 . TYR B 1 198 ? 2.152   -41.134 59.157  1.00 41.24  ? 198  TYR B CD1 1 
ATOM   5294 C  CD2 . TYR B 1 198 ? 3.810   -42.181 60.502  1.00 42.54  ? 198  TYR B CD2 1 
ATOM   5295 C  CE1 . TYR B 1 198 ? 1.200   -41.365 60.136  1.00 45.54  ? 198  TYR B CE1 1 
ATOM   5296 C  CE2 . TYR B 1 198 ? 2.869   -42.423 61.482  1.00 45.54  ? 198  TYR B CE2 1 
ATOM   5297 C  CZ  . TYR B 1 198 ? 1.564   -42.013 61.296  1.00 45.59  ? 198  TYR B CZ  1 
ATOM   5298 O  OH  . TYR B 1 198 ? 0.633   -42.248 62.285  1.00 51.54  ? 198  TYR B OH  1 
ATOM   5299 N  N   . ASP B 1 199 ? 5.699   -42.644 55.162  1.00 43.73  ? 199  ASP B N   1 
ATOM   5300 C  CA  . ASP B 1 199 ? 6.784   -42.435 54.204  1.00 47.07  ? 199  ASP B CA  1 
ATOM   5301 C  C   . ASP B 1 199 ? 6.380   -41.428 53.141  1.00 41.84  ? 199  ASP B C   1 
ATOM   5302 O  O   . ASP B 1 199 ? 7.162   -40.542 52.783  1.00 43.61  ? 199  ASP B O   1 
ATOM   5303 C  CB  . ASP B 1 199 ? 7.181   -43.753 53.533  1.00 48.33  ? 199  ASP B CB  1 
ATOM   5304 C  CG  . ASP B 1 199 ? 7.926   -44.683 54.462  1.00 50.85  ? 199  ASP B CG  1 
ATOM   5305 O  OD1 . ASP B 1 199 ? 8.384   -44.224 55.531  1.00 52.91  ? 199  ASP B OD1 1 
ATOM   5306 O  OD2 . ASP B 1 199 ? 8.069   -45.875 54.109  1.00 53.40  ? 199  ASP B OD2 1 
ATOM   5307 N  N   . GLU B 1 200 ? 5.162   -41.558 52.614  1.00 45.06  ? 200  GLU B N   1 
ATOM   5308 C  CA  . GLU B 1 200 ? 4.708   -40.633 51.585  1.00 46.05  ? 200  GLU B CA  1 
ATOM   5309 C  C   . GLU B 1 200 ? 4.542   -39.224 52.146  1.00 44.04  ? 200  GLU B C   1 
ATOM   5310 O  O   . GLU B 1 200 ? 4.894   -38.245 51.474  1.00 44.19  ? 200  GLU B O   1 
ATOM   5311 C  CB  . GLU B 1 200 ? 3.407   -41.139 50.962  1.00 49.53  ? 200  GLU B CB  1 
ATOM   5312 C  CG  . GLU B 1 200 ? 2.798   -40.198 49.938  1.00 50.82  ? 200  GLU B CG  1 
ATOM   5313 C  CD  . GLU B 1 200 ? 3.733   -39.863 48.778  1.00 54.14  ? 200  GLU B CD  1 
ATOM   5314 O  OE1 . GLU B 1 200 ? 4.752   -40.561 48.579  1.00 58.45  ? 200  GLU B OE1 1 
ATOM   5315 O  OE2 . GLU B 1 200 ? 3.442   -38.883 48.061  1.00 64.19  ? 200  GLU B OE2 1 
ATOM   5316 N  N   . ASN B 1 201 ? 4.020   -39.097 53.372  1.00 42.38  ? 201  ASN B N   1 
ATOM   5317 C  CA  . ASN B 1 201 ? 3.959   -37.781 54.010  1.00 40.43  ? 201  ASN B CA  1 
ATOM   5318 C  C   . ASN B 1 201 ? 5.333   -37.128 54.022  1.00 42.48  ? 201  ASN B C   1 
ATOM   5319 O  O   . ASN B 1 201 ? 5.480   -35.936 53.720  1.00 41.50  ? 201  ASN B O   1 
ATOM   5320 C  CB  . ASN B 1 201 ? 3.430   -37.887 55.445  1.00 43.20  ? 201  ASN B CB  1 
ATOM   5321 C  CG  . ASN B 1 201 ? 2.032   -38.453 55.519  1.00 45.76  ? 201  ASN B CG  1 
ATOM   5322 O  OD1 . ASN B 1 201 ? 1.824   -39.540 56.047  1.00 53.09  ? 201  ASN B OD1 1 
ATOM   5323 N  ND2 . ASN B 1 201 ? 1.066   -37.723 54.976  1.00 48.65  ? 201  ASN B ND2 1 
ATOM   5324 N  N   . LYS B 1 202 ? 6.359   -37.901 54.373  1.00 41.41  ? 202  LYS B N   1 
ATOM   5325 C  CA  . LYS B 1 202 ? 7.700   -37.337 54.452  1.00 41.28  ? 202  LYS B CA  1 
ATOM   5326 C  C   . LYS B 1 202 ? 8.221   -36.948 53.074  1.00 42.63  ? 202  LYS B C   1 
ATOM   5327 O  O   . LYS B 1 202 ? 8.851   -35.894 52.920  1.00 40.30  ? 202  LYS B O   1 
ATOM   5328 C  CB  . LYS B 1 202 ? 8.642   -38.323 55.136  1.00 45.66  ? 202  LYS B CB  1 
ATOM   5329 C  CG  . LYS B 1 202 ? 8.297   -38.585 56.601  1.00 42.03  ? 202  LYS B CG  1 
ATOM   5330 C  CD  . LYS B 1 202 ? 9.131   -39.740 57.140  1.00 47.19  ? 202  LYS B CD  1 
ATOM   5331 C  CE  . LYS B 1 202 ? 8.877   -39.963 58.620  1.00 45.31  ? 202  LYS B CE  1 
ATOM   5332 N  NZ  . LYS B 1 202 ? 9.520   -41.218 59.061  1.00 50.69  ? 202  LYS B NZ  1 
ATOM   5333 N  N   . ARG B 1 203 ? 7.979   -37.787 52.062  1.00 43.09  ? 203  ARG B N   1 
ATOM   5334 C  CA  . ARG B 1 203 ? 8.350   -37.430 50.693  1.00 43.03  ? 203  ARG B CA  1 
ATOM   5335 C  C   . ARG B 1 203 ? 7.687   -36.124 50.275  1.00 41.55  ? 203  ARG B C   1 
ATOM   5336 O  O   . ARG B 1 203 ? 8.339   -35.218 49.745  1.00 40.85  ? 203  ARG B O   1 
ATOM   5337 C  CB  . ARG B 1 203 ? 7.948   -38.547 49.728  1.00 44.39  ? 203  ARG B CB  1 
ATOM   5338 C  CG  . ARG B 1 203 ? 8.429   -38.313 48.298  1.00 53.01  ? 203  ARG B CG  1 
ATOM   5339 C  CD  . ARG B 1 203 ? 7.611   -39.106 47.286  1.00 56.39  ? 203  ARG B CD  1 
ATOM   5340 N  NE  . ARG B 1 203 ? 6.298   -38.483 47.148  1.00 59.55  ? 203  ARG B NE  1 
ATOM   5341 C  CZ  . ARG B 1 203 ? 6.077   -37.310 46.564  1.00 58.86  ? 203  ARG B CZ  1 
ATOM   5342 N  NH1 . ARG B 1 203 ? 7.055   -36.629 45.983  1.00 59.88  ? 203  ARG B NH1 1 
ATOM   5343 N  NH2 . ARG B 1 203 ? 4.849   -36.796 46.581  1.00 57.44  ? 203  ARG B NH2 1 
ATOM   5344 N  N   . GLN B 1 204 ? 6.374   -36.024 50.488  1.00 39.18  ? 204  GLN B N   1 
ATOM   5345 C  CA  . GLN B 1 204 ? 5.647   -34.818 50.114  1.00 41.23  ? 204  GLN B CA  1 
ATOM   5346 C  C   . GLN B 1 204 ? 6.164   -33.608 50.876  1.00 39.35  ? 204  GLN B C   1 
ATOM   5347 O  O   . GLN B 1 204 ? 6.227   -32.500 50.333  1.00 38.39  ? 204  GLN B O   1 
ATOM   5348 C  CB  . GLN B 1 204 ? 4.159   -35.009 50.375  1.00 40.03  ? 204  GLN B CB  1 
ATOM   5349 C  CG  . GLN B 1 204 ? 3.346   -33.783 50.060  1.00 42.59  ? 204  GLN B CG  1 
ATOM   5350 C  CD  . GLN B 1 204 ? 3.351   -33.474 48.580  1.00 44.18  ? 204  GLN B CD  1 
ATOM   5351 O  OE1 . GLN B 1 204 ? 4.057   -32.573 48.115  1.00 43.61  ? 204  GLN B OE1 1 
ATOM   5352 N  NE2 . GLN B 1 204 ? 2.586   -34.241 47.825  1.00 48.60  ? 204  GLN B NE2 1 
ATOM   5353 N  N   . PHE B 1 205 ? 6.509   -33.801 52.151  1.00 36.25  ? 205  PHE B N   1 
ATOM   5354 C  CA  . PHE B 1 205 ? 7.034   -32.704 52.961  1.00 37.29  ? 205  PHE B CA  1 
ATOM   5355 C  C   . PHE B 1 205 ? 8.315   -32.145 52.350  1.00 39.12  ? 205  PHE B C   1 
ATOM   5356 O  O   . PHE B 1 205 ? 8.464   -30.926 52.193  1.00 39.17  ? 205  PHE B O   1 
ATOM   5357 C  CB  . PHE B 1 205 ? 7.267   -33.203 54.384  1.00 38.35  ? 205  PHE B CB  1 
ATOM   5358 C  CG  . PHE B 1 205 ? 7.537   -32.111 55.396  1.00 38.34  ? 205  PHE B CG  1 
ATOM   5359 C  CD1 . PHE B 1 205 ? 6.584   -31.146 55.675  1.00 34.91  ? 205  PHE B CD1 1 
ATOM   5360 C  CD2 . PHE B 1 205 ? 8.731   -32.094 56.109  1.00 40.73  ? 205  PHE B CD2 1 
ATOM   5361 C  CE1 . PHE B 1 205 ? 6.829   -30.163 56.634  1.00 33.56  ? 205  PHE B CE1 1 
ATOM   5362 C  CE2 . PHE B 1 205 ? 8.982   -31.124 57.066  1.00 39.37  ? 205  PHE B CE2 1 
ATOM   5363 C  CZ  . PHE B 1 205 ? 8.037   -30.149 57.320  1.00 38.25  ? 205  PHE B CZ  1 
ATOM   5364 N  N   . GLN B 1 206 ? 9.252   -33.024 51.990  1.00 38.78  ? 206  GLN B N   1 
ATOM   5365 C  CA  . GLN B 1 206 ? 10.488  -32.554 51.374  1.00 42.31  ? 206  GLN B CA  1 
ATOM   5366 C  C   . GLN B 1 206 ? 10.199  -31.843 50.064  1.00 40.20  ? 206  GLN B C   1 
ATOM   5367 O  O   . GLN B 1 206 ? 10.832  -30.832 49.742  1.00 42.15  ? 206  GLN B O   1 
ATOM   5368 C  CB  . GLN B 1 206 ? 11.457  -33.719 51.156  1.00 43.25  ? 206  GLN B CB  1 
ATOM   5369 C  CG  . GLN B 1 206 ? 11.988  -34.317 52.445  1.00 47.21  ? 206  GLN B CG  1 
ATOM   5370 C  CD  . GLN B 1 206 ? 12.597  -33.277 53.378  1.00 50.04  ? 206  GLN B CD  1 
ATOM   5371 O  OE1 . GLN B 1 206 ? 12.206  -33.171 54.547  1.00 50.80  ? 206  GLN B OE1 1 
ATOM   5372 N  NE2 . GLN B 1 206 ? 13.556  -32.507 52.869  1.00 48.83  ? 206  GLN B NE2 1 
ATOM   5373 N  N   . GLU B 1 207 ? 9.231   -32.350 49.300  1.00 39.46  ? 207  GLU B N   1 
ATOM   5374 C  CA  . GLU B 1 207 ? 8.894   -31.713 48.033  1.00 39.42  ? 207  GLU B CA  1 
ATOM   5375 C  C   . GLU B 1 207 ? 8.316   -30.320 48.258  1.00 41.72  ? 207  GLU B C   1 
ATOM   5376 O  O   . GLU B 1 207 ? 8.631   -29.381 47.515  1.00 35.86  ? 207  GLU B O   1 
ATOM   5377 C  CB  . GLU B 1 207 ? 7.923   -32.602 47.256  1.00 42.31  ? 207  GLU B CB  1 
ATOM   5378 C  CG  . GLU B 1 207 ? 7.344   -31.972 45.998  1.00 47.54  ? 207  GLU B CG  1 
ATOM   5379 C  CD  . GLU B 1 207 ? 6.154   -32.763 45.459  1.00 54.79  ? 207  GLU B CD  1 
ATOM   5380 O  OE1 . GLU B 1 207 ? 5.135   -32.140 45.072  1.00 57.05  ? 207  GLU B OE1 1 
ATOM   5381 O  OE2 . GLU B 1 207 ? 6.243   -34.011 45.424  1.00 61.19  ? 207  GLU B OE2 1 
ATOM   5382 N  N   . ASP B 1 208 ? 7.471   -30.167 49.281  1.00 38.45  ? 208  ASP B N   1 
ATOM   5383 C  CA  . ASP B 1 208 ? 6.906   -28.853 49.563  1.00 37.04  ? 208  ASP B CA  1 
ATOM   5384 C  C   . ASP B 1 208 ? 7.976   -27.896 50.065  1.00 35.68  ? 208  ASP B C   1 
ATOM   5385 O  O   . ASP B 1 208 ? 7.948   -26.702 49.737  1.00 37.65  ? 208  ASP B O   1 
ATOM   5386 C  CB  . ASP B 1 208 ? 5.760   -28.976 50.567  1.00 34.73  ? 208  ASP B CB  1 
ATOM   5387 C  CG  . ASP B 1 208 ? 4.528   -29.599 49.951  1.00 37.48  ? 208  ASP B CG  1 
ATOM   5388 O  OD1 . ASP B 1 208 ? 4.264   -29.332 48.754  1.00 41.15  ? 208  ASP B OD1 1 
ATOM   5389 O  OD2 . ASP B 1 208 ? 3.834   -30.365 50.655  1.00 38.49  ? 208  ASP B OD2 1 
ATOM   5390 N  N   . ILE B 1 209 ? 8.938   -28.396 50.845  1.00 35.74  ? 209  ILE B N   1 
ATOM   5391 C  CA  . ILE B 1 209 ? 10.042  -27.539 51.269  1.00 36.26  ? 209  ILE B CA  1 
ATOM   5392 C  C   . ILE B 1 209 ? 10.851  -27.062 50.062  1.00 39.33  ? 209  ILE B C   1 
ATOM   5393 O  O   . ILE B 1 209 ? 11.274  -25.902 50.003  1.00 38.67  ? 209  ILE B O   1 
ATOM   5394 C  CB  . ILE B 1 209 ? 10.919  -28.265 52.307  1.00 39.03  ? 209  ILE B CB  1 
ATOM   5395 C  CG1 . ILE B 1 209 ? 10.130  -28.465 53.602  1.00 38.14  ? 209  ILE B CG1 1 
ATOM   5396 C  CG2 . ILE B 1 209 ? 12.194  -27.483 52.577  1.00 39.86  ? 209  ILE B CG2 1 
ATOM   5397 C  CD1 . ILE B 1 209 ? 10.841  -29.318 54.632  1.00 39.23  ? 209  ILE B CD1 1 
ATOM   5398 N  N   . LYS B 1 210 ? 11.055  -27.937 49.072  1.00 37.67  ? 210  LYS B N   1 
ATOM   5399 C  CA  . LYS B 1 210 ? 11.802  -27.542 47.877  1.00 37.54  ? 210  LYS B CA  1 
ATOM   5400 C  C   . LYS B 1 210 ? 11.048  -26.484 47.078  1.00 39.43  ? 210  LYS B C   1 
ATOM   5401 O  O   . LYS B 1 210 ? 11.652  -25.528 46.572  1.00 41.47  ? 210  LYS B O   1 
ATOM   5402 C  CB  . LYS B 1 210 ? 12.098  -28.773 47.018  1.00 40.51  ? 210  LYS B CB  1 
ATOM   5403 C  CG  . LYS B 1 210 ? 13.099  -28.536 45.865  1.00 47.34  ? 210  LYS B CG  1 
ATOM   5404 C  CD  . LYS B 1 210 ? 12.417  -28.294 44.530  1.00 56.65  ? 210  LYS B CD  1 
ATOM   5405 C  CE  . LYS B 1 210 ? 13.383  -28.535 43.369  1.00 54.11  ? 210  LYS B CE  1 
ATOM   5406 N  NZ  . LYS B 1 210 ? 12.620  -28.938 42.152  1.00 63.41  ? 210  LYS B NZ  1 
ATOM   5407 N  N   . VAL B 1 211 ? 9.729   -26.629 46.957  1.00 36.72  ? 211  VAL B N   1 
ATOM   5408 C  CA  . VAL B 1 211 ? 8.933   -25.609 46.280  1.00 37.44  ? 211  VAL B CA  1 
ATOM   5409 C  C   . VAL B 1 211 ? 9.100   -24.261 46.964  1.00 39.01  ? 211  VAL B C   1 
ATOM   5410 O  O   . VAL B 1 211 ? 9.244   -23.219 46.306  1.00 39.18  ? 211  VAL B O   1 
ATOM   5411 C  CB  . VAL B 1 211 ? 7.453   -26.036 46.229  1.00 38.39  ? 211  VAL B CB  1 
ATOM   5412 C  CG1 . VAL B 1 211 ? 6.583   -24.875 45.787  1.00 40.50  ? 211  VAL B CG1 1 
ATOM   5413 C  CG2 . VAL B 1 211 ? 7.277   -27.214 45.284  1.00 39.89  ? 211  VAL B CG2 1 
ATOM   5414 N  N   . MET B 1 212 ? 9.082   -24.248 48.297  1.00 36.78  ? 212  MET B N   1 
ATOM   5415 C  CA  . MET B 1 212 ? 9.207   -22.963 48.974  1.00 37.19  ? 212  MET B CA  1 
ATOM   5416 C  C   . MET B 1 212 ? 10.594  -22.371 48.749  1.00 36.70  ? 212  MET B C   1 
ATOM   5417 O  O   . MET B 1 212 ? 10.721  -21.176 48.459  1.00 40.98  ? 212  MET B O   1 
ATOM   5418 C  CB  . MET B 1 212 ? 8.896   -23.105 50.466  1.00 38.42  ? 212  MET B CB  1 
ATOM   5419 C  CG  . MET B 1 212 ? 7.407   -23.352 50.700  1.00 36.24  ? 212  MET B CG  1 
ATOM   5420 S  SD  . MET B 1 212 ? 6.812   -23.324 52.421  1.00 40.90  ? 212  MET B SD  1 
ATOM   5421 C  CE  . MET B 1 212 ? 7.479   -24.846 53.091  1.00 40.42  ? 212  MET B CE  1 
ATOM   5422 N  N   . ASN B 1 213 ? 11.644  -23.198 48.854  1.00 37.97  ? 213  ASN B N   1 
ATOM   5423 C  CA  . ASN B 1 213 ? 13.002  -22.713 48.616  1.00 36.49  ? 213  ASN B CA  1 
ATOM   5424 C  C   . ASN B 1 213 ? 13.233  -22.285 47.174  1.00 40.08  ? 213  ASN B C   1 
ATOM   5425 O  O   . ASN B 1 213 ? 14.002  -21.351 46.937  1.00 44.76  ? 213  ASN B O   1 
ATOM   5426 C  CB  . ASN B 1 213 ? 14.048  -23.755 49.014  1.00 38.80  ? 213  ASN B CB  1 
ATOM   5427 C  CG  . ASN B 1 213 ? 14.332  -23.751 50.501  1.00 46.34  ? 213  ASN B CG  1 
ATOM   5428 O  OD1 . ASN B 1 213 ? 13.783  -24.536 51.272  1.00 45.76  ? 213  ASN B OD1 1 
ATOM   5429 N  ND2 . ASN B 1 213 ? 15.211  -22.848 50.910  1.00 50.86  ? 213  ASN B ND2 1 
ATOM   5430 N  N   . ASP B 1 214 ? 12.606  -22.952 46.205  1.00 40.28  ? 214  ASP B N   1 
ATOM   5431 C  CA  . ASP B 1 214 ? 12.741  -22.511 44.816  1.00 43.38  ? 214  ASP B CA  1 
ATOM   5432 C  C   . ASP B 1 214 ? 12.248  -21.074 44.641  1.00 43.31  ? 214  ASP B C   1 
ATOM   5433 O  O   . ASP B 1 214 ? 12.885  -20.263 43.953  1.00 42.72  ? 214  ASP B O   1 
ATOM   5434 C  CB  . ASP B 1 214 ? 11.978  -23.457 43.892  1.00 44.57  ? 214  ASP B CB  1 
ATOM   5435 C  CG  . ASP B 1 214 ? 12.686  -24.790 43.696  1.00 46.20  ? 214  ASP B CG  1 
ATOM   5436 O  OD1 . ASP B 1 214 ? 13.854  -24.932 44.124  1.00 46.75  ? 214  ASP B OD1 1 
ATOM   5437 O  OD2 . ASP B 1 214 ? 12.067  -25.697 43.103  1.00 50.60  ? 214  ASP B OD2 1 
ATOM   5438 N  N   . LEU B 1 215 ? 11.118  -20.740 45.265  1.00 39.18  ? 215  LEU B N   1 
ATOM   5439 C  CA  . LEU B 1 215 ? 10.625  -19.368 45.220  1.00 37.39  ? 215  LEU B CA  1 
ATOM   5440 C  C   . LEU B 1 215 ? 11.576  -18.409 45.919  1.00 41.17  ? 215  LEU B C   1 
ATOM   5441 O  O   . LEU B 1 215 ? 11.811  -17.292 45.438  1.00 39.51  ? 215  LEU B O   1 
ATOM   5442 C  CB  . LEU B 1 215 ? 9.232   -19.293 45.836  1.00 41.07  ? 215  LEU B CB  1 
ATOM   5443 C  CG  . LEU B 1 215 ? 8.771   -17.843 45.862  1.00 42.85  ? 215  LEU B CG  1 
ATOM   5444 C  CD1 . LEU B 1 215 ? 8.272   -17.455 44.469  1.00 46.42  ? 215  LEU B CD1 1 
ATOM   5445 C  CD2 . LEU B 1 215 ? 7.680   -17.687 46.859  1.00 47.53  ? 215  LEU B CD2 1 
ATOM   5446 N  N   . VAL B 1 216 ? 12.125  -18.819 47.066  1.00 40.33  ? 216  VAL B N   1 
ATOM   5447 C  CA  . VAL B 1 216 ? 13.145  -18.010 47.726  1.00 38.78  ? 216  VAL B CA  1 
ATOM   5448 C  C   . VAL B 1 216 ? 14.321  -17.756 46.784  1.00 44.17  ? 216  VAL B C   1 
ATOM   5449 O  O   . VAL B 1 216 ? 14.857  -16.643 46.725  1.00 43.57  ? 216  VAL B O   1 
ATOM   5450 C  CB  . VAL B 1 216 ? 13.599  -18.687 49.030  1.00 40.41  ? 216  VAL B CB  1 
ATOM   5451 C  CG1 . VAL B 1 216 ? 14.854  -18.002 49.562  1.00 40.82  ? 216  VAL B CG1 1 
ATOM   5452 C  CG2 . VAL B 1 216 ? 12.475  -18.666 50.059  1.00 38.13  ? 216  VAL B CG2 1 
ATOM   5453 N  N   . ASP B 1 217 ? 14.747  -18.784 46.040  1.00 44.35  ? 217  ASP B N   1 
ATOM   5454 C  CA  . ASP B 1 217 ? 15.817  -18.592 45.062  1.00 46.28  ? 217  ASP B CA  1 
ATOM   5455 C  C   . ASP B 1 217 ? 15.459  -17.492 44.069  1.00 47.18  ? 217  ASP B C   1 
ATOM   5456 O  O   . ASP B 1 217 ? 16.297  -16.642 43.736  1.00 47.15  ? 217  ASP B O   1 
ATOM   5457 C  CB  . ASP B 1 217 ? 16.095  -19.886 44.289  1.00 50.06  ? 217  ASP B CB  1 
ATOM   5458 C  CG  . ASP B 1 217 ? 16.691  -20.991 45.144  1.00 52.28  ? 217  ASP B CG  1 
ATOM   5459 O  OD1 . ASP B 1 217 ? 17.200  -20.727 46.257  1.00 52.56  ? 217  ASP B OD1 1 
ATOM   5460 O  OD2 . ASP B 1 217 ? 16.660  -22.148 44.664  1.00 57.72  ? 217  ASP B OD2 1 
ATOM   5461 N  N   . LYS B 1 218 ? 14.220  -17.502 43.573  1.00 44.70  ? 218  LYS B N   1 
ATOM   5462 C  CA  . LYS B 1 218 ? 13.822  -16.529 42.567  1.00 45.97  ? 218  LYS B CA  1 
ATOM   5463 C  C   . LYS B 1 218 ? 13.836  -15.118 43.134  1.00 47.60  ? 218  LYS B C   1 
ATOM   5464 O  O   . LYS B 1 218 ? 14.230  -14.168 42.446  1.00 44.30  ? 218  LYS B O   1 
ATOM   5465 C  CB  . LYS B 1 218 ? 12.437  -16.877 42.023  1.00 48.60  ? 218  LYS B CB  1 
ATOM   5466 C  CG  . LYS B 1 218 ? 12.469  -17.887 40.890  1.00 50.95  ? 218  LYS B CG  1 
ATOM   5467 C  CD  . LYS B 1 218 ? 11.272  -17.738 39.983  1.00 61.14  ? 218  LYS B CD  1 
ATOM   5468 C  CE  . LYS B 1 218 ? 10.196  -18.744 40.332  1.00 59.65  ? 218  LYS B CE  1 
ATOM   5469 N  NZ  . LYS B 1 218 ? 9.454   -19.177 39.115  1.00 67.71  ? 218  LYS B NZ  1 
ATOM   5470 N  N   . ILE B 1 219 ? 13.403  -14.961 44.385  1.00 38.98  ? 219  ILE B N   1 
ATOM   5471 C  CA  . ILE B 1 219 ? 13.379  -13.638 44.998  1.00 35.52  ? 219  ILE B CA  1 
ATOM   5472 C  C   . ILE B 1 219 ? 14.791  -13.096 45.131  1.00 40.86  ? 219  ILE B C   1 
ATOM   5473 O  O   . ILE B 1 219 ? 15.057  -11.924 44.837  1.00 38.75  ? 219  ILE B O   1 
ATOM   5474 C  CB  . ILE B 1 219 ? 12.663  -13.702 46.361  1.00 36.70  ? 219  ILE B CB  1 
ATOM   5475 C  CG1 . ILE B 1 219 ? 11.172  -13.971 46.146  1.00 39.08  ? 219  ILE B CG1 1 
ATOM   5476 C  CG2 . ILE B 1 219 ? 12.897  -12.424 47.156  1.00 36.78  ? 219  ILE B CG2 1 
ATOM   5477 C  CD1 . ILE B 1 219 ? 10.395  -14.204 47.425  1.00 37.37  ? 219  ILE B CD1 1 
ATOM   5478 N  N   . ILE B 1 220 ? 15.715  -13.939 45.593  1.00 38.03  ? 220  ILE B N   1 
ATOM   5479 C  CA  . ILE B 1 220 ? 17.102  -13.520 45.767  1.00 39.77  ? 220  ILE B CA  1 
ATOM   5480 C  C   . ILE B 1 220 ? 17.720  -13.158 44.422  1.00 43.24  ? 220  ILE B C   1 
ATOM   5481 O  O   . ILE B 1 220 ? 18.392  -12.126 44.286  1.00 45.42  ? 220  ILE B O   1 
ATOM   5482 C  CB  . ILE B 1 220 ? 17.900  -14.624 46.482  1.00 42.41  ? 220  ILE B CB  1 
ATOM   5483 C  CG1 . ILE B 1 220 ? 17.415  -14.759 47.926  1.00 43.08  ? 220  ILE B CG1 1 
ATOM   5484 C  CG2 . ILE B 1 220 ? 19.412  -14.347 46.387  1.00 42.57  ? 220  ILE B CG2 1 
ATOM   5485 C  CD1 . ILE B 1 220 ? 17.947  -15.996 48.655  1.00 48.19  ? 220  ILE B CD1 1 
ATOM   5486 N  N   . ALA B 1 221 ? 17.482  -13.988 43.405  1.00 47.64  ? 221  ALA B N   1 
ATOM   5487 C  CA  . ALA B 1 221 ? 18.002  -13.703 42.068  1.00 49.63  ? 221  ALA B CA  1 
ATOM   5488 C  C   . ALA B 1 221 ? 17.428  -12.404 41.512  1.00 51.62  ? 221  ALA B C   1 
ATOM   5489 O  O   . ALA B 1 221 ? 18.170  -11.550 41.009  1.00 56.14  ? 221  ALA B O   1 
ATOM   5490 C  CB  . ALA B 1 221 ? 17.699  -14.873 41.127  1.00 50.48  ? 221  ALA B CB  1 
ATOM   5491 N  N   . ASP B 1 222 ? 16.099  -12.251 41.569  1.00 48.95  ? 222  ASP B N   1 
ATOM   5492 C  CA  . ASP B 1 222 ? 15.456  -11.013 41.136  1.00 47.60  ? 222  ASP B CA  1 
ATOM   5493 C  C   . ASP B 1 222 ? 16.162  -9.800  41.733  1.00 52.46  ? 222  ASP B C   1 
ATOM   5494 O  O   . ASP B 1 222 ? 16.545  -8.868  41.015  1.00 54.91  ? 222  ASP B O   1 
ATOM   5495 C  CB  . ASP B 1 222 ? 13.968  -11.042 41.526  1.00 50.00  ? 222  ASP B CB  1 
ATOM   5496 C  CG  . ASP B 1 222 ? 13.201  -9.788  41.094  1.00 53.49  ? 222  ASP B CG  1 
ATOM   5497 O  OD1 . ASP B 1 222 ? 13.271  -8.766  41.814  1.00 57.34  ? 222  ASP B OD1 1 
ATOM   5498 O  OD2 . ASP B 1 222 ? 12.495  -9.825  40.059  1.00 52.78  ? 222  ASP B OD2 1 
ATOM   5499 N  N   . ARG B 1 223 ? 16.376  -9.812  43.049  1.00 45.82  ? 223  ARG B N   1 
ATOM   5500 C  CA  . ARG B 1 223 ? 17.007  -8.674  43.706  1.00 44.45  ? 223  ARG B CA  1 
ATOM   5501 C  C   . ARG B 1 223 ? 18.451  -8.505  43.251  1.00 51.79  ? 223  ARG B C   1 
ATOM   5502 O  O   . ARG B 1 223 ? 18.882  -7.391  42.943  1.00 51.04  ? 223  ARG B O   1 
ATOM   5503 C  CB  . ARG B 1 223 ? 16.940  -8.840  45.227  1.00 41.01  ? 223  ARG B CB  1 
ATOM   5504 C  CG  . ARG B 1 223 ? 17.599  -7.718  46.017  1.00 40.60  ? 223  ARG B CG  1 
ATOM   5505 C  CD  . ARG B 1 223 ? 16.977  -6.369  45.700  1.00 42.02  ? 223  ARG B CD  1 
ATOM   5506 N  NE  . ARG B 1 223 ? 15.536  -6.373  45.933  1.00 44.44  ? 223  ARG B NE  1 
ATOM   5507 C  CZ  . ARG B 1 223 ? 14.944  -5.872  47.010  1.00 40.25  ? 223  ARG B CZ  1 
ATOM   5508 N  NH1 . ARG B 1 223 ? 15.631  -5.256  47.956  1.00 37.00  ? 223  ARG B NH1 1 
ATOM   5509 N  NH2 . ARG B 1 223 ? 13.623  -5.995  47.144  1.00 40.57  ? 223  ARG B NH2 1 
ATOM   5510 N  N   . LYS B 1 224 ? 19.219  -9.598  43.216  1.00 53.57  ? 224  LYS B N   1 
ATOM   5511 C  CA  . LYS B 1 224 ? 20.620  -9.486  42.814  1.00 57.63  ? 224  LYS B CA  1 
ATOM   5512 C  C   . LYS B 1 224 ? 20.744  -8.919  41.406  1.00 60.16  ? 224  LYS B C   1 
ATOM   5513 O  O   . LYS B 1 224 ? 21.666  -8.148  41.115  1.00 64.99  ? 224  LYS B O   1 
ATOM   5514 C  CB  . LYS B 1 224 ? 21.313  -10.845 42.905  1.00 58.61  ? 224  LYS B CB  1 
ATOM   5515 C  CG  . LYS B 1 224 ? 22.828  -10.762 42.737  1.00 70.94  ? 224  LYS B CG  1 
ATOM   5516 C  CD  . LYS B 1 224 ? 23.531  -11.997 43.289  1.00 75.11  ? 224  LYS B CD  1 
ATOM   5517 C  CE  . LYS B 1 224 ? 23.825  -13.004 42.189  1.00 79.83  ? 224  LYS B CE  1 
ATOM   5518 N  NZ  . LYS B 1 224 ? 22.569  -13.478 41.547  1.00 79.77  ? 224  LYS B NZ  1 
ATOM   5519 N  N   . ALA B 1 225 ? 19.824  -9.285  40.521  1.00 58.75  ? 225  ALA B N   1 
ATOM   5520 C  CA  . ALA B 1 225 ? 19.821  -8.797  39.151  1.00 61.11  ? 225  ALA B CA  1 
ATOM   5521 C  C   . ALA B 1 225 ? 19.213  -7.413  39.023  1.00 65.40  ? 225  ALA B C   1 
ATOM   5522 O  O   . ALA B 1 225 ? 19.241  -6.839  37.930  1.00 67.90  ? 225  ALA B O   1 
ATOM   5523 C  CB  . ALA B 1 225 ? 19.055  -9.771  38.255  1.00 59.00  ? 225  ALA B CB  1 
ATOM   5524 N  N   . SER B 1 226 ? 18.670  -6.869  40.107  1.00 63.64  ? 226  SER B N   1 
ATOM   5525 C  CA  . SER B 1 226 ? 17.885  -5.643  40.050  1.00 67.20  ? 226  SER B CA  1 
ATOM   5526 C  C   . SER B 1 226 ? 18.807  -4.440  39.913  1.00 76.64  ? 226  SER B C   1 
ATOM   5527 O  O   . SER B 1 226 ? 19.599  -4.151  40.817  1.00 76.59  ? 226  SER B O   1 
ATOM   5528 C  CB  . SER B 1 226 ? 17.018  -5.513  41.301  1.00 69.76  ? 226  SER B CB  1 
ATOM   5529 O  OG  . SER B 1 226 ? 16.360  -4.261  41.326  1.00 78.34  ? 226  SER B OG  1 
ATOM   5530 N  N   . GLY B 1 227 ? 18.709  -3.747  38.775  1.00 84.65  ? 227  GLY B N   1 
ATOM   5531 C  CA  . GLY B 1 227 ? 19.375  -2.464  38.637  1.00 87.58  ? 227  GLY B CA  1 
ATOM   5532 C  C   . GLY B 1 227 ? 18.655  -1.358  39.376  1.00 89.36  ? 227  GLY B C   1 
ATOM   5533 O  O   . GLY B 1 227 ? 19.281  -0.375  39.788  1.00 92.81  ? 227  GLY B O   1 
ATOM   5534 N  N   . GLU B 1 228 ? 17.343  -1.499  39.550  1.00 87.29  ? 228  GLU B N   1 
ATOM   5535 C  CA  . GLU B 1 228 ? 16.582  -0.590  40.394  1.00 88.07  ? 228  GLU B CA  1 
ATOM   5536 C  C   . GLU B 1 228 ? 17.017  -0.743  41.847  1.00 88.08  ? 228  GLU B C   1 
ATOM   5537 O  O   . GLU B 1 228 ? 17.301  -1.849  42.316  1.00 88.31  ? 228  GLU B O   1 
ATOM   5538 C  CB  . GLU B 1 228 ? 15.085  -0.879  40.253  1.00 86.17  ? 228  GLU B CB  1 
ATOM   5539 C  CG  . GLU B 1 228 ? 14.287  -0.765  41.546  1.00 85.94  ? 228  GLU B CG  1 
ATOM   5540 C  CD  . GLU B 1 228 ? 12.822  -1.148  41.366  1.00 86.37  ? 228  GLU B CD  1 
ATOM   5541 O  OE1 . GLU B 1 228 ? 12.522  -1.954  40.457  1.00 84.78  ? 228  GLU B OE1 1 
ATOM   5542 O  OE2 . GLU B 1 228 ? 11.969  -0.639  42.128  1.00 84.92  ? 228  GLU B OE2 1 
ATOM   5543 N  N   . GLN B 1 229 ? 17.077  0.374   42.564  1.00 86.41  ? 229  GLN B N   1 
ATOM   5544 C  CA  . GLN B 1 229 ? 17.460  0.360   43.969  1.00 86.31  ? 229  GLN B CA  1 
ATOM   5545 C  C   . GLN B 1 229 ? 16.212  0.340   44.843  1.00 81.58  ? 229  GLN B C   1 
ATOM   5546 O  O   . GLN B 1 229 ? 15.265  1.099   44.608  1.00 82.59  ? 229  GLN B O   1 
ATOM   5547 C  CB  . GLN B 1 229 ? 18.344  1.560   44.314  1.00 89.07  ? 229  GLN B CB  1 
ATOM   5548 C  CG  . GLN B 1 229 ? 17.798  2.913   43.892  1.00 95.51  ? 229  GLN B CG  1 
ATOM   5549 C  CD  . GLN B 1 229 ? 18.773  4.039   44.193  1.00 103.90 ? 229  GLN B CD  1 
ATOM   5550 O  OE1 . GLN B 1 229 ? 19.866  4.096   43.626  1.00 106.36 ? 229  GLN B OE1 1 
ATOM   5551 N  NE2 . GLN B 1 229 ? 18.388  4.934   45.099  1.00 101.24 ? 229  GLN B NE2 1 
ATOM   5552 N  N   . SER B 1 230 ? 16.211  -0.542  45.838  1.00 74.15  ? 230  SER B N   1 
ATOM   5553 C  CA  . SER B 1 230 ? 15.117  -0.682  46.786  1.00 65.73  ? 230  SER B CA  1 
ATOM   5554 C  C   . SER B 1 230 ? 15.615  -0.386  48.201  1.00 66.03  ? 230  SER B C   1 
ATOM   5555 O  O   . SER B 1 230 ? 16.822  -0.319  48.471  1.00 59.67  ? 230  SER B O   1 
ATOM   5556 C  CB  . SER B 1 230 ? 14.501  -2.089  46.712  1.00 63.66  ? 230  SER B CB  1 
ATOM   5557 O  OG  . SER B 1 230 ? 13.795  -2.304  45.497  1.00 61.31  ? 230  SER B OG  1 
ATOM   5558 N  N   . ASP B 1 231 ? 14.660  -0.188  49.115  1.00 56.86  ? 231  ASP B N   1 
ATOM   5559 C  CA  . ASP B 1 231 ? 14.990  0.027   50.518  1.00 55.05  ? 231  ASP B CA  1 
ATOM   5560 C  C   . ASP B 1 231 ? 13.879  -0.616  51.353  1.00 57.28  ? 231  ASP B C   1 
ATOM   5561 O  O   . ASP B 1 231 ? 13.086  0.044   52.019  1.00 59.93  ? 231  ASP B O   1 
ATOM   5562 C  CB  . ASP B 1 231 ? 15.161  1.510   50.847  1.00 59.46  ? 231  ASP B CB  1 
ATOM   5563 C  CG  . ASP B 1 231 ? 15.653  1.732   52.261  1.00 69.34  ? 231  ASP B CG  1 
ATOM   5564 O  OD1 . ASP B 1 231 ? 16.193  0.768   52.850  1.00 66.96  ? 231  ASP B OD1 1 
ATOM   5565 O  OD2 . ASP B 1 231 ? 15.512  2.865   52.782  1.00 72.47  ? 231  ASP B OD2 1 
ATOM   5566 N  N   . ASP B 1 232 ? 13.825  -1.950  51.320  1.00 49.24  ? 232  ASP B N   1 
ATOM   5567 C  CA  . ASP B 1 232 ? 12.754  -2.689  51.968  1.00 43.99  ? 232  ASP B CA  1 
ATOM   5568 C  C   . ASP B 1 232 ? 13.303  -3.762  52.901  1.00 43.63  ? 232  ASP B C   1 
ATOM   5569 O  O   . ASP B 1 232 ? 14.486  -3.736  53.273  1.00 39.04  ? 232  ASP B O   1 
ATOM   5570 C  CB  . ASP B 1 232 ? 11.840  -3.299  50.900  1.00 38.67  ? 232  ASP B CB  1 
ATOM   5571 C  CG  . ASP B 1 232 ? 12.600  -4.168  49.907  1.00 41.39  ? 232  ASP B CG  1 
ATOM   5572 O  OD1 . ASP B 1 232 ? 13.782  -4.481  50.174  1.00 41.03  ? 232  ASP B OD1 1 
ATOM   5573 O  OD2 . ASP B 1 232 ? 12.045  -4.509  48.838  1.00 38.82  ? 232  ASP B OD2 1 
ATOM   5574 N  N   . LEU B 1 233 ? 12.440  -4.698  53.299  1.00 40.35  ? 233  LEU B N   1 
ATOM   5575 C  CA  . LEU B 1 233 ? 12.855  -5.757  54.217  1.00 40.51  ? 233  LEU B CA  1 
ATOM   5576 C  C   . LEU B 1 233 ? 14.023  -6.562  53.642  1.00 38.29  ? 233  LEU B C   1 
ATOM   5577 O  O   . LEU B 1 233 ? 15.018  -6.821  54.333  1.00 38.22  ? 233  LEU B O   1 
ATOM   5578 C  CB  . LEU B 1 233 ? 11.654  -6.652  54.539  1.00 40.65  ? 233  LEU B CB  1 
ATOM   5579 C  CG  . LEU B 1 233 ? 11.820  -7.843  55.471  1.00 36.45  ? 233  LEU B CG  1 
ATOM   5580 C  CD1 . LEU B 1 233 ? 12.186  -7.397  56.905  1.00 37.89  ? 233  LEU B CD1 1 
ATOM   5581 C  CD2 . LEU B 1 233 ? 10.533  -8.674  55.478  1.00 35.55  ? 233  LEU B CD2 1 
ATOM   5582 N  N   . LEU B 1 234 ? 13.932  -6.952  52.364  1.00 37.54  ? 234  LEU B N   1 
ATOM   5583 C  CA  . LEU B 1 234 ? 15.021  -7.706  51.748  1.00 33.93  ? 234  LEU B CA  1 
ATOM   5584 C  C   . LEU B 1 234 ? 16.309  -6.890  51.714  1.00 36.53  ? 234  LEU B C   1 
ATOM   5585 O  O   . LEU B 1 234 ? 17.404  -7.449  51.860  1.00 37.02  ? 234  LEU B O   1 
ATOM   5586 C  CB  . LEU B 1 234 ? 14.623  -8.135  50.333  1.00 35.78  ? 234  LEU B CB  1 
ATOM   5587 C  CG  . LEU B 1 234 ? 15.639  -8.999  49.572  1.00 33.89  ? 234  LEU B CG  1 
ATOM   5588 C  CD1 . LEU B 1 234 ? 16.016  -10.254 50.357  1.00 35.02  ? 234  LEU B CD1 1 
ATOM   5589 C  CD2 . LEU B 1 234 ? 15.084  -9.389  48.210  1.00 36.05  ? 234  LEU B CD2 1 
ATOM   5590 N  N   . THR B 1 235 ? 16.198  -5.571  51.533  1.00 34.03  ? 235  THR B N   1 
ATOM   5591 C  CA  . THR B 1 235 ? 17.387  -4.721  51.536  1.00 36.77  ? 235  THR B CA  1 
ATOM   5592 C  C   . THR B 1 235 ? 18.126  -4.840  52.859  1.00 37.97  ? 235  THR B C   1 
ATOM   5593 O  O   . THR B 1 235 ? 19.353  -4.985  52.881  1.00 38.51  ? 235  THR B O   1 
ATOM   5594 C  CB  . THR B 1 235 ? 17.027  -3.256  51.286  1.00 40.81  ? 235  THR B CB  1 
ATOM   5595 O  OG1 . THR B 1 235 ? 16.284  -3.124  50.072  1.00 40.86  ? 235  THR B OG1 1 
ATOM   5596 C  CG2 . THR B 1 235 ? 18.302  -2.425  51.172  1.00 42.98  ? 235  THR B CG2 1 
ATOM   5597 N  N   . HIS B 1 236 ? 17.387  -4.759  53.975  1.00 36.18  ? 236  HIS B N   1 
ATOM   5598 C  CA  . HIS B 1 236 ? 18.006  -4.865  55.293  1.00 40.28  ? 236  HIS B CA  1 
ATOM   5599 C  C   . HIS B 1 236 ? 18.591  -6.252  55.495  1.00 40.16  ? 236  HIS B C   1 
ATOM   5600 O  O   . HIS B 1 236 ? 19.693  -6.405  56.037  1.00 39.14  ? 236  HIS B O   1 
ATOM   5601 C  CB  . HIS B 1 236 ? 16.980  -4.545  56.387  1.00 40.49  ? 236  HIS B CB  1 
ATOM   5602 C  CG  . HIS B 1 236 ? 16.568  -3.105  56.445  1.00 42.19  ? 236  HIS B CG  1 
ATOM   5603 N  ND1 . HIS B 1 236 ? 15.653  -2.549  55.576  1.00 48.13  ? 236  HIS B ND1 1 
ATOM   5604 C  CD2 . HIS B 1 236 ? 16.939  -2.109  57.285  1.00 49.54  ? 236  HIS B CD2 1 
ATOM   5605 C  CE1 . HIS B 1 236 ? 15.492  -1.270  55.864  1.00 49.81  ? 236  HIS B CE1 1 
ATOM   5606 N  NE2 . HIS B 1 236 ? 16.256  -0.979  56.902  1.00 54.61  ? 236  HIS B NE2 1 
ATOM   5607 N  N   . MET B 1 237 ? 17.858  -7.273  55.058  1.00 37.84  ? 237  MET B N   1 
ATOM   5608 C  CA  . MET B 1 237 ? 18.336  -8.648  55.116  1.00 35.75  ? 237  MET B CA  1 
ATOM   5609 C  C   . MET B 1 237 ? 19.699  -8.777  54.457  1.00 40.92  ? 237  MET B C   1 
ATOM   5610 O  O   . MET B 1 237 ? 20.628  -9.355  55.032  1.00 40.71  ? 237  MET B O   1 
ATOM   5611 C  CB  . MET B 1 237 ? 17.304  -9.526  54.412  1.00 36.34  ? 237  MET B CB  1 
ATOM   5612 C  CG  . MET B 1 237 ? 16.174  -9.967  55.299  1.00 36.64  ? 237  MET B CG  1 
ATOM   5613 S  SD  . MET B 1 237 ? 15.260  -11.274 54.463  1.00 37.94  ? 237  MET B SD  1 
ATOM   5614 C  CE  . MET B 1 237 ? 13.719  -11.174 55.393  1.00 36.07  ? 237  MET B CE  1 
ATOM   5615 N  N   . LEU B 1 238 ? 19.835  -8.228  53.246  1.00 41.27  ? 238  LEU B N   1 
ATOM   5616 C  CA  . LEU B 1 238 ? 21.053  -8.373  52.458  1.00 36.38  ? 238  LEU B CA  1 
ATOM   5617 C  C   . LEU B 1 238 ? 22.164  -7.420  52.879  1.00 42.76  ? 238  LEU B C   1 
ATOM   5618 O  O   . LEU B 1 238 ? 23.338  -7.725  52.648  1.00 51.43  ? 238  LEU B O   1 
ATOM   5619 C  CB  . LEU B 1 238 ? 20.746  -8.152  50.972  1.00 42.53  ? 238  LEU B CB  1 
ATOM   5620 C  CG  . LEU B 1 238 ? 19.788  -9.157  50.339  1.00 42.03  ? 238  LEU B CG  1 
ATOM   5621 C  CD1 . LEU B 1 238 ? 19.398  -8.696  48.930  1.00 40.03  ? 238  LEU B CD1 1 
ATOM   5622 C  CD2 . LEU B 1 238 ? 20.378  -10.570 50.307  1.00 46.06  ? 238  LEU B CD2 1 
ATOM   5623 N  N   . ASN B 1 239 ? 21.845  -6.282  53.483  1.00 40.65  ? 239  ASN B N   1 
ATOM   5624 C  CA  . ASN B 1 239 ? 22.858  -5.254  53.693  1.00 44.38  ? 239  ASN B CA  1 
ATOM   5625 C  C   . ASN B 1 239 ? 22.982  -4.758  55.118  1.00 45.38  ? 239  ASN B C   1 
ATOM   5626 O  O   . ASN B 1 239 ? 23.994  -4.122  55.430  1.00 45.37  ? 239  ASN B O   1 
ATOM   5627 C  CB  . ASN B 1 239 ? 22.587  -4.041  52.789  1.00 44.74  ? 239  ASN B CB  1 
ATOM   5628 C  CG  . ASN B 1 239 ? 22.591  -4.407  51.318  1.00 49.99  ? 239  ASN B CG  1 
ATOM   5629 O  OD1 . ASN B 1 239 ? 23.647  -4.520  50.698  1.00 52.91  ? 239  ASN B OD1 1 
ATOM   5630 N  ND2 . ASN B 1 239 ? 21.406  -4.605  50.753  1.00 45.73  ? 239  ASN B ND2 1 
ATOM   5631 N  N   . GLY B 1 240 ? 22.002  -4.997  55.988  1.00 40.25  ? 240  GLY B N   1 
ATOM   5632 C  CA  . GLY B 1 240 ? 22.036  -4.390  57.306  1.00 40.82  ? 240  GLY B CA  1 
ATOM   5633 C  C   . GLY B 1 240 ? 23.051  -5.084  58.201  1.00 37.86  ? 240  GLY B C   1 
ATOM   5634 O  O   . GLY B 1 240 ? 23.277  -6.289  58.098  1.00 41.34  ? 240  GLY B O   1 
ATOM   5635 N  N   . LYS B 1 241 ? 23.690  -4.300  59.063  1.00 40.38  ? 241  LYS B N   1 
ATOM   5636 C  CA  . LYS B 1 241 ? 24.678  -4.813  60.003  1.00 42.32  ? 241  LYS B CA  1 
ATOM   5637 C  C   . LYS B 1 241 ? 24.139  -4.713  61.417  1.00 38.21  ? 241  LYS B C   1 
ATOM   5638 O  O   . LYS B 1 241 ? 23.587  -3.681  61.814  1.00 37.42  ? 241  LYS B O   1 
ATOM   5639 C  CB  . LYS B 1 241 ? 26.008  -4.050  59.915  1.00 41.59  ? 241  LYS B CB  1 
ATOM   5640 C  CG  . LYS B 1 241 ? 26.481  -3.795  58.506  1.00 46.90  ? 241  LYS B CG  1 
ATOM   5641 C  CD  . LYS B 1 241 ? 27.220  -4.979  57.941  1.00 48.99  ? 241  LYS B CD  1 
ATOM   5642 C  CE  . LYS B 1 241 ? 28.215  -4.527  56.863  1.00 52.01  ? 241  LYS B CE  1 
ATOM   5643 N  NZ  . LYS B 1 241 ? 29.092  -3.420  57.338  1.00 62.86  ? 241  LYS B NZ  1 
ATOM   5644 N  N   . ASP B 1 242 ? 24.323  -5.783  62.171  1.00 35.87  ? 242  ASP B N   1 
ATOM   5645 C  CA  . ASP B 1 242 ? 23.950  -5.804  63.567  1.00 36.37  ? 242  ASP B CA  1 
ATOM   5646 C  C   . ASP B 1 242 ? 24.910  -4.930  64.356  1.00 37.02  ? 242  ASP B C   1 
ATOM   5647 O  O   . ASP B 1 242 ? 26.119  -5.203  64.353  1.00 37.01  ? 242  ASP B O   1 
ATOM   5648 C  CB  . ASP B 1 242 ? 23.988  -7.234  64.078  1.00 33.48  ? 242  ASP B CB  1 
ATOM   5649 C  CG  . ASP B 1 242 ? 23.984  -7.319  65.593  1.00 34.52  ? 242  ASP B CG  1 
ATOM   5650 O  OD1 . ASP B 1 242 ? 23.403  -6.431  66.246  1.00 35.88  ? 242  ASP B OD1 1 
ATOM   5651 O  OD2 . ASP B 1 242 ? 24.539  -8.309  66.118  1.00 35.78  ? 242  ASP B OD2 1 
ATOM   5652 N  N   . PRO B 1 243 ? 24.435  -3.895  65.045  1.00 36.83  ? 243  PRO B N   1 
ATOM   5653 C  CA  . PRO B 1 243 ? 25.362  -3.020  65.781  1.00 36.46  ? 243  PRO B CA  1 
ATOM   5654 C  C   . PRO B 1 243 ? 26.143  -3.740  66.853  1.00 39.11  ? 243  PRO B C   1 
ATOM   5655 O  O   . PRO B 1 243 ? 27.228  -3.272  67.225  1.00 40.84  ? 243  PRO B O   1 
ATOM   5656 C  CB  . PRO B 1 243 ? 24.436  -1.965  66.406  1.00 44.38  ? 243  PRO B CB  1 
ATOM   5657 C  CG  . PRO B 1 243 ? 23.163  -2.051  65.627  1.00 46.83  ? 243  PRO B CG  1 
ATOM   5658 C  CD  . PRO B 1 243 ? 23.032  -3.473  65.200  1.00 41.49  ? 243  PRO B CD  1 
ATOM   5659 N  N   . GLU B 1 244 ? 25.614  -4.843  67.390  1.00 36.39  ? 244  GLU B N   1 
ATOM   5660 C  CA  . GLU B 1 244 ? 26.296  -5.519  68.488  1.00 37.42  ? 244  GLU B CA  1 
ATOM   5661 C  C   . GLU B 1 244 ? 27.492  -6.306  67.964  1.00 39.46  ? 244  GLU B C   1 
ATOM   5662 O  O   . GLU B 1 244 ? 28.640  -5.987  68.282  1.00 37.69  ? 244  GLU B O   1 
ATOM   5663 C  CB  . GLU B 1 244 ? 25.336  -6.443  69.244  1.00 37.73  ? 244  GLU B CB  1 
ATOM   5664 C  CG  . GLU B 1 244 ? 26.025  -7.228  70.347  1.00 43.88  ? 244  GLU B CG  1 
ATOM   5665 C  CD  . GLU B 1 244 ? 25.156  -8.319  70.982  1.00 51.02  ? 244  GLU B CD  1 
ATOM   5666 O  OE1 . GLU B 1 244 ? 23.934  -8.390  70.714  1.00 42.61  ? 244  GLU B OE1 1 
ATOM   5667 O  OE2 . GLU B 1 244 ? 25.716  -9.115  71.765  1.00 59.11  ? 244  GLU B OE2 1 
ATOM   5668 N  N   . THR B 1 245 ? 27.233  -7.332  67.141  1.00 37.19  ? 245  THR B N   1 
ATOM   5669 C  CA  . THR B 1 245 ? 28.313  -8.094  66.518  1.00 39.10  ? 245  THR B CA  1 
ATOM   5670 C  C   . THR B 1 245 ? 29.010  -7.315  65.416  1.00 41.46  ? 245  THR B C   1 
ATOM   5671 O  O   . THR B 1 245 ? 30.152  -7.646  65.074  1.00 40.99  ? 245  THR B O   1 
ATOM   5672 C  CB  . THR B 1 245 ? 27.794  -9.409  65.922  1.00 40.24  ? 245  THR B CB  1 
ATOM   5673 O  OG1 . THR B 1 245 ? 26.894  -9.134  64.831  1.00 37.67  ? 245  THR B OG1 1 
ATOM   5674 C  CG2 . THR B 1 245 ? 27.090  -10.251 66.982  1.00 39.39  ? 245  THR B CG2 1 
ATOM   5675 N  N   . GLY B 1 246 ? 28.341  -6.314  64.838  1.00 37.64  ? 246  GLY B N   1 
ATOM   5676 C  CA  . GLY B 1 246 ? 28.823  -5.624  63.664  1.00 35.26  ? 246  GLY B CA  1 
ATOM   5677 C  C   . GLY B 1 246 ? 28.682  -6.389  62.369  1.00 35.57  ? 246  GLY B C   1 
ATOM   5678 O  O   . GLY B 1 246 ? 29.109  -5.884  61.324  1.00 37.19  ? 246  GLY B O   1 
ATOM   5679 N  N   . GLU B 1 247 ? 28.066  -7.620  62.392  1.00 36.98  ? 247  GLU B N   1 
ATOM   5680 C  CA  . GLU B 1 247 ? 27.988  -8.493  61.225  1.00 33.50  ? 247  GLU B CA  1 
ATOM   5681 C  C   . GLU B 1 247 ? 26.644  -8.350  60.519  1.00 36.23  ? 247  GLU B C   1 
ATOM   5682 O  O   . GLU B 1 247 ? 25.635  -8.040  61.153  1.00 35.65  ? 247  GLU B O   1 
ATOM   5683 C  CB  . GLU B 1 247 ? 28.152  -9.957  61.634  1.00 34.16  ? 247  GLU B CB  1 
ATOM   5684 C  CG  . GLU B 1 247 ? 29.378  -10.245 62.483  1.00 39.22  ? 247  GLU B CG  1 
ATOM   5685 C  CD  . GLU B 1 247 ? 29.256  -11.578 63.191  1.00 39.51  ? 247  GLU B CD  1 
ATOM   5686 O  OE1 . GLU B 1 247 ? 28.273  -12.308 62.928  1.00 37.03  ? 247  GLU B OE1 1 
ATOM   5687 O  OE2 . GLU B 1 247 ? 30.118  -11.883 64.036  1.00 37.67  ? 247  GLU B OE2 1 
ATOM   5688 N  N   . PRO B 1 248 ? 26.610  -8.583  59.217  1.00 37.97  ? 248  PRO B N   1 
ATOM   5689 C  CA  . PRO B 1 248 ? 25.337  -8.767  58.519  1.00 37.93  ? 248  PRO B CA  1 
ATOM   5690 C  C   . PRO B 1 248 ? 24.937  -10.234 58.604  1.00 38.21  ? 248  PRO B C   1 
ATOM   5691 O  O   . PRO B 1 248 ? 25.716  -11.087 59.015  1.00 35.30  ? 248  PRO B O   1 
ATOM   5692 C  CB  . PRO B 1 248 ? 25.688  -8.388  57.077  1.00 40.68  ? 248  PRO B CB  1 
ATOM   5693 C  CG  . PRO B 1 248 ? 27.086  -8.937  56.931  1.00 39.55  ? 248  PRO B CG  1 
ATOM   5694 C  CD  . PRO B 1 248 ? 27.757  -8.683  58.291  1.00 36.23  ? 248  PRO B CD  1 
ATOM   5695 N  N   . LEU B 1 249 ? 23.713  -10.526 58.167  1.00 38.47  ? 249  LEU B N   1 
ATOM   5696 C  CA  . LEU B 1 249 ? 23.317  -11.928 58.121  1.00 35.86  ? 249  LEU B CA  1 
ATOM   5697 C  C   . LEU B 1 249 ? 24.094  -12.682 57.046  1.00 38.95  ? 249  LEU B C   1 
ATOM   5698 O  O   . LEU B 1 249 ? 24.462  -12.128 56.006  1.00 39.33  ? 249  LEU B O   1 
ATOM   5699 C  CB  . LEU B 1 249 ? 21.827  -12.069 57.831  1.00 37.62  ? 249  LEU B CB  1 
ATOM   5700 C  CG  . LEU B 1 249 ? 20.895  -11.337 58.773  1.00 36.63  ? 249  LEU B CG  1 
ATOM   5701 C  CD1 . LEU B 1 249 ? 19.467  -11.474 58.220  1.00 34.95  ? 249  LEU B CD1 1 
ATOM   5702 C  CD2 . LEU B 1 249 ? 21.024  -11.869 60.184  1.00 34.66  ? 249  LEU B CD2 1 
ATOM   5703 N  N   . ASP B 1 250 ? 24.313  -13.969 57.286  1.00 37.43  ? 250  ASP B N   1 
ATOM   5704 C  CA  . ASP B 1 250 ? 24.913  -14.816 56.262  1.00 39.18  ? 250  ASP B CA  1 
ATOM   5705 C  C   . ASP B 1 250 ? 23.833  -15.420 55.361  1.00 42.04  ? 250  ASP B C   1 
ATOM   5706 O  O   . ASP B 1 250 ? 22.632  -15.321 55.624  1.00 38.15  ? 250  ASP B O   1 
ATOM   5707 C  CB  . ASP B 1 250 ? 25.815  -15.879 56.904  1.00 43.89  ? 250  ASP B CB  1 
ATOM   5708 C  CG  . ASP B 1 250 ? 25.056  -16.913 57.724  1.00 47.37  ? 250  ASP B CG  1 
ATOM   5709 O  OD1 . ASP B 1 250 ? 23.972  -17.377 57.313  1.00 42.02  ? 250  ASP B OD1 1 
ATOM   5710 O  OD2 . ASP B 1 250 ? 25.547  -17.230 58.832  1.00 56.92  ? 250  ASP B OD2 1 
ATOM   5711 N  N   . ASP B 1 251 ? 24.282  -16.019 54.251  1.00 41.63  ? 251  ASP B N   1 
ATOM   5712 C  CA  . ASP B 1 251 ? 23.353  -16.417 53.197  1.00 43.52  ? 251  ASP B CA  1 
ATOM   5713 C  C   . ASP B 1 251 ? 22.355  -17.455 53.695  1.00 40.09  ? 251  ASP B C   1 
ATOM   5714 O  O   . ASP B 1 251 ? 21.161  -17.392 53.363  1.00 39.54  ? 251  ASP B O   1 
ATOM   5715 C  CB  . ASP B 1 251 ? 24.138  -16.946 51.992  1.00 42.80  ? 251  ASP B CB  1 
ATOM   5716 C  CG  . ASP B 1 251 ? 24.731  -15.826 51.143  1.00 53.54  ? 251  ASP B CG  1 
ATOM   5717 O  OD1 . ASP B 1 251 ? 24.367  -14.651 51.360  1.00 49.98  ? 251  ASP B OD1 1 
ATOM   5718 O  OD2 . ASP B 1 251 ? 25.565  -16.123 50.261  1.00 55.03  ? 251  ASP B OD2 1 
ATOM   5719 N  N   . GLU B 1 252 ? 22.823  -18.423 54.484  1.00 36.20  ? 252  GLU B N   1 
ATOM   5720 C  CA  . GLU B 1 252 ? 21.935  -19.479 54.966  1.00 37.79  ? 252  GLU B CA  1 
ATOM   5721 C  C   . GLU B 1 252 ? 20.813  -18.898 55.821  1.00 36.23  ? 252  GLU B C   1 
ATOM   5722 O  O   . GLU B 1 252 ? 19.638  -19.255 55.652  1.00 36.66  ? 252  GLU B O   1 
ATOM   5723 C  CB  . GLU B 1 252 ? 22.735  -20.518 55.755  1.00 44.23  ? 252  GLU B CB  1 
ATOM   5724 C  CG  . GLU B 1 252 ? 21.918  -21.722 56.220  1.00 45.96  ? 252  GLU B CG  1 
ATOM   5725 C  CD  . GLU B 1 252 ? 22.618  -22.517 57.314  1.00 57.27  ? 252  GLU B CD  1 
ATOM   5726 O  OE1 . GLU B 1 252 ? 23.723  -23.031 57.041  1.00 67.79  ? 252  GLU B OE1 1 
ATOM   5727 O  OE2 . GLU B 1 252 ? 22.073  -22.621 58.445  1.00 56.96  ? 252  GLU B OE2 1 
ATOM   5728 N  N   . ASN B 1 253 ? 21.155  -17.995 56.741  1.00 35.29  ? 253  ASN B N   1 
ATOM   5729 C  CA  . ASN B 1 253 ? 20.120  -17.405 57.588  1.00 34.37  ? 253  ASN B CA  1 
ATOM   5730 C  C   . ASN B 1 253 ? 19.190  -16.504 56.778  1.00 33.17  ? 253  ASN B C   1 
ATOM   5731 O  O   . ASN B 1 253 ? 17.981  -16.458 57.036  1.00 33.08  ? 253  ASN B O   1 
ATOM   5732 C  CB  . ASN B 1 253 ? 20.746  -16.621 58.741  1.00 34.92  ? 253  ASN B CB  1 
ATOM   5733 C  CG  . ASN B 1 253 ? 19.710  -16.113 59.727  1.00 32.09  ? 253  ASN B CG  1 
ATOM   5734 O  OD1 . ASN B 1 253 ? 19.429  -14.913 59.802  1.00 33.71  ? 253  ASN B OD1 1 
ATOM   5735 N  ND2 . ASN B 1 253 ? 19.119  -17.029 60.482  1.00 32.89  ? 253  ASN B ND2 1 
ATOM   5736 N  N   . ILE B 1 254 ? 19.726  -15.775 55.801  1.00 32.43  ? 254  ILE B N   1 
ATOM   5737 C  CA  . ILE B 1 254 ? 18.860  -14.949 54.953  1.00 33.38  ? 254  ILE B CA  1 
ATOM   5738 C  C   . ILE B 1 254 ? 17.754  -15.801 54.333  1.00 36.64  ? 254  ILE B C   1 
ATOM   5739 O  O   . ILE B 1 254 ? 16.576  -15.408 54.315  1.00 32.00  ? 254  ILE B O   1 
ATOM   5740 C  CB  . ILE B 1 254 ? 19.690  -14.228 53.874  1.00 33.21  ? 254  ILE B CB  1 
ATOM   5741 C  CG1 . ILE B 1 254 ? 20.480  -13.070 54.494  1.00 36.92  ? 254  ILE B CG1 1 
ATOM   5742 C  CG2 . ILE B 1 254 ? 18.767  -13.709 52.759  1.00 35.88  ? 254  ILE B CG2 1 
ATOM   5743 C  CD1 . ILE B 1 254 ? 21.640  -12.602 53.617  1.00 41.27  ? 254  ILE B CD1 1 
ATOM   5744 N  N   . ARG B 1 255 ? 18.120  -16.977 53.806  1.00 33.15  ? 255  ARG B N   1 
ATOM   5745 C  CA  . ARG B 1 255 ? 17.124  -17.859 53.190  1.00 34.72  ? 255  ARG B CA  1 
ATOM   5746 C  C   . ARG B 1 255 ? 16.053  -18.267 54.197  1.00 33.79  ? 255  ARG B C   1 
ATOM   5747 O  O   . ARG B 1 255 ? 14.863  -18.302 53.865  1.00 34.58  ? 255  ARG B O   1 
ATOM   5748 C  CB  . ARG B 1 255 ? 17.796  -19.101 52.597  1.00 38.60  ? 255  ARG B CB  1 
ATOM   5749 C  CG  . ARG B 1 255 ? 18.746  -18.823 51.429  1.00 41.38  ? 255  ARG B CG  1 
ATOM   5750 C  CD  . ARG B 1 255 ? 19.317  -20.130 50.849  1.00 47.05  ? 255  ARG B CD  1 
ATOM   5751 N  NE  . ARG B 1 255 ? 18.237  -20.954 50.321  1.00 52.36  ? 255  ARG B NE  1 
ATOM   5752 C  CZ  . ARG B 1 255 ? 17.711  -20.843 49.107  1.00 52.49  ? 255  ARG B CZ  1 
ATOM   5753 N  NH1 . ARG B 1 255 ? 18.195  -19.993 48.208  1.00 53.01  ? 255  ARG B NH1 1 
ATOM   5754 N  NH2 . ARG B 1 255 ? 16.652  -21.582 48.794  1.00 46.13  ? 255  ARG B NH2 1 
ATOM   5755 N  N   . TYR B 1 256 ? 16.456  -18.576 55.434  1.00 30.93  ? 256  TYR B N   1 
ATOM   5756 C  CA  . TYR B 1 256 ? 15.468  -18.882 56.469  1.00 34.50  ? 256  TYR B CA  1 
ATOM   5757 C  C   . TYR B 1 256 ? 14.594  -17.669 56.798  1.00 35.23  ? 256  TYR B C   1 
ATOM   5758 O  O   . TYR B 1 256 ? 13.389  -17.818 57.061  1.00 32.32  ? 256  TYR B O   1 
ATOM   5759 C  CB  . TYR B 1 256 ? 16.156  -19.388 57.742  1.00 31.67  ? 256  TYR B CB  1 
ATOM   5760 C  CG  . TYR B 1 256 ? 16.737  -20.782 57.645  1.00 32.90  ? 256  TYR B CG  1 
ATOM   5761 C  CD1 . TYR B 1 256 ? 16.036  -21.816 57.032  1.00 32.86  ? 256  TYR B CD1 1 
ATOM   5762 C  CD2 . TYR B 1 256 ? 17.995  -21.065 58.166  1.00 34.07  ? 256  TYR B CD2 1 
ATOM   5763 C  CE1 . TYR B 1 256 ? 16.578  -23.106 56.949  1.00 36.42  ? 256  TYR B CE1 1 
ATOM   5764 C  CE2 . TYR B 1 256 ? 18.541  -22.346 58.088  1.00 37.39  ? 256  TYR B CE2 1 
ATOM   5765 C  CZ  . TYR B 1 256 ? 17.838  -23.354 57.476  1.00 40.55  ? 256  TYR B CZ  1 
ATOM   5766 O  OH  . TYR B 1 256 ? 18.388  -24.618 57.404  1.00 40.80  ? 256  TYR B OH  1 
ATOM   5767 N  N   . GLN B 1 257 ? 15.183  -16.468 56.837  1.00 32.59  ? 257  GLN B N   1 
ATOM   5768 C  CA  . GLN B 1 257 ? 14.366  -15.290 57.133  1.00 32.41  ? 257  GLN B CA  1 
ATOM   5769 C  C   . GLN B 1 257 ? 13.338  -15.048 56.038  1.00 32.14  ? 257  GLN B C   1 
ATOM   5770 O  O   . GLN B 1 257 ? 12.203  -14.654 56.332  1.00 33.03  ? 257  GLN B O   1 
ATOM   5771 C  CB  . GLN B 1 257 ? 15.220  -14.036 57.324  1.00 33.46  ? 257  GLN B CB  1 
ATOM   5772 C  CG  . GLN B 1 257 ? 16.290  -14.145 58.421  1.00 31.83  ? 257  GLN B CG  1 
ATOM   5773 C  CD  . GLN B 1 257 ? 15.743  -14.364 59.827  1.00 34.06  ? 257  GLN B CD  1 
ATOM   5774 O  OE1 . GLN B 1 257 ? 14.526  -14.344 60.068  1.00 30.52  ? 257  GLN B OE1 1 
ATOM   5775 N  NE2 . GLN B 1 257 ? 16.656  -14.551 60.785  1.00 32.40  ? 257  GLN B NE2 1 
ATOM   5776 N  N   . ILE B 1 258 ? 13.714  -15.247 54.772  1.00 32.13  ? 258  ILE B N   1 
ATOM   5777 C  CA  . ILE B 1 258 ? 12.754  -15.009 53.689  1.00 34.05  ? 258  ILE B CA  1 
ATOM   5778 C  C   . ILE B 1 258 ? 11.578  -15.974 53.794  1.00 34.02  ? 258  ILE B C   1 
ATOM   5779 O  O   . ILE B 1 258 ? 10.411  -15.571 53.707  1.00 31.64  ? 258  ILE B O   1 
ATOM   5780 C  CB  . ILE B 1 258 ? 13.444  -15.096 52.315  1.00 32.54  ? 258  ILE B CB  1 
ATOM   5781 C  CG1 . ILE B 1 258 ? 14.511  -14.009 52.219  1.00 33.49  ? 258  ILE B CG1 1 
ATOM   5782 C  CG2 . ILE B 1 258 ? 12.393  -14.975 51.166  1.00 31.45  ? 258  ILE B CG2 1 
ATOM   5783 C  CD1 . ILE B 1 258 ? 15.338  -14.082 50.917  1.00 36.53  ? 258  ILE B CD1 1 
ATOM   5784 N  N   . ILE B 1 259 ? 11.861  -17.266 53.965  1.00 32.28  ? 259  ILE B N   1 
ATOM   5785 C  CA  . ILE B 1 259 ? 10.789  -18.238 54.189  1.00 33.53  ? 259  ILE B CA  1 
ATOM   5786 C  C   . ILE B 1 259 ? 9.942   -17.828 55.392  1.00 35.00  ? 259  ILE B C   1 
ATOM   5787 O  O   . ILE B 1 259 ? 8.699   -17.811 55.331  1.00 30.88  ? 259  ILE B O   1 
ATOM   5788 C  CB  . ILE B 1 259 ? 11.387  -19.647 54.371  1.00 35.38  ? 259  ILE B CB  1 
ATOM   5789 C  CG1 . ILE B 1 259 ? 11.966  -20.137 53.036  1.00 39.52  ? 259  ILE B CG1 1 
ATOM   5790 C  CG2 . ILE B 1 259 ? 10.351  -20.618 54.920  1.00 38.74  ? 259  ILE B CG2 1 
ATOM   5791 C  CD1 . ILE B 1 259 ? 12.885  -21.327 53.174  1.00 42.61  ? 259  ILE B CD1 1 
ATOM   5792 N  N   . THR B 1 260 ? 10.604  -17.474 56.498  1.00 30.98  ? 260  THR B N   1 
ATOM   5793 C  CA  . THR B 1 260 ? 9.887   -17.071 57.709  1.00 32.19  ? 260  THR B CA  1 
ATOM   5794 C  C   . THR B 1 260 ? 8.958   -15.890 57.437  1.00 33.78  ? 260  THR B C   1 
ATOM   5795 O  O   . THR B 1 260 ? 7.765   -15.925 57.780  1.00 30.99  ? 260  THR B O   1 
ATOM   5796 C  CB  . THR B 1 260 ? 10.894  -16.721 58.808  1.00 32.24  ? 260  THR B CB  1 
ATOM   5797 O  OG1 . THR B 1 260 ? 11.652  -17.883 59.130  1.00 31.66  ? 260  THR B OG1 1 
ATOM   5798 C  CG2 . THR B 1 260 ? 10.197  -16.224 60.067  1.00 31.27  ? 260  THR B CG2 1 
ATOM   5799 N  N   . PHE B 1 261 ? 9.482   -14.835 56.806  1.00 30.17  ? 261  PHE B N   1 
ATOM   5800 C  CA  . PHE B 1 261 ? 8.666   -13.638 56.619  1.00 31.64  ? 261  PHE B CA  1 
ATOM   5801 C  C   . PHE B 1 261 ? 7.590   -13.827 55.545  1.00 33.24  ? 261  PHE B C   1 
ATOM   5802 O  O   . PHE B 1 261 ? 6.506   -13.236 55.662  1.00 33.15  ? 261  PHE B O   1 
ATOM   5803 C  CB  . PHE B 1 261 ? 9.568   -12.437 56.321  1.00 33.17  ? 261  PHE B CB  1 
ATOM   5804 C  CG  . PHE B 1 261 ? 10.101  -11.796 57.570  1.00 32.01  ? 261  PHE B CG  1 
ATOM   5805 C  CD1 . PHE B 1 261 ? 11.302  -12.214 58.129  1.00 31.57  ? 261  PHE B CD1 1 
ATOM   5806 C  CD2 . PHE B 1 261 ? 9.370   -10.812 58.217  1.00 32.57  ? 261  PHE B CD2 1 
ATOM   5807 C  CE1 . PHE B 1 261 ? 11.762  -11.637 59.306  1.00 32.57  ? 261  PHE B CE1 1 
ATOM   5808 C  CE2 . PHE B 1 261 ? 9.816   -10.235 59.392  1.00 32.47  ? 261  PHE B CE2 1 
ATOM   5809 C  CZ  . PHE B 1 261 ? 11.017  -10.641 59.939  1.00 33.38  ? 261  PHE B CZ  1 
ATOM   5810 N  N   . LEU B 1 262 ? 7.841   -14.635 54.511  1.00 30.37  ? 262  LEU B N   1 
ATOM   5811 C  CA  . LEU B 1 262 ? 6.764   -14.909 53.553  1.00 32.74  ? 262  LEU B CA  1 
ATOM   5812 C  C   . LEU B 1 262 ? 5.588   -15.604 54.234  1.00 34.78  ? 262  LEU B C   1 
ATOM   5813 O  O   . LEU B 1 262 ? 4.421   -15.334 53.906  1.00 33.62  ? 262  LEU B O   1 
ATOM   5814 C  CB  . LEU B 1 262 ? 7.265   -15.772 52.388  1.00 31.12  ? 262  LEU B CB  1 
ATOM   5815 C  CG  . LEU B 1 262 ? 8.177   -15.042 51.392  1.00 32.45  ? 262  LEU B CG  1 
ATOM   5816 C  CD1 . LEU B 1 262 ? 8.737   -16.000 50.345  1.00 33.22  ? 262  LEU B CD1 1 
ATOM   5817 C  CD2 . LEU B 1 262 ? 7.481   -13.839 50.760  1.00 31.75  ? 262  LEU B CD2 1 
ATOM   5818 N  N   . ILE B 1 263 ? 5.873   -16.517 55.169  1.00 32.61  ? 263  ILE B N   1 
ATOM   5819 C  CA  . ILE B 1 263 ? 4.809   -17.273 55.834  1.00 31.90  ? 263  ILE B CA  1 
ATOM   5820 C  C   . ILE B 1 263 ? 4.225   -16.489 57.001  1.00 31.36  ? 263  ILE B C   1 
ATOM   5821 O  O   . ILE B 1 263 ? 3.026   -16.183 57.035  1.00 30.99  ? 263  ILE B O   1 
ATOM   5822 C  CB  . ILE B 1 263 ? 5.326   -18.642 56.302  1.00 31.76  ? 263  ILE B CB  1 
ATOM   5823 C  CG1 . ILE B 1 263 ? 5.735   -19.489 55.102  1.00 31.92  ? 263  ILE B CG1 1 
ATOM   5824 C  CG2 . ILE B 1 263 ? 4.265   -19.338 57.173  1.00 33.24  ? 263  ILE B CG2 1 
ATOM   5825 C  CD1 . ILE B 1 263 ? 6.355   -20.800 55.504  1.00 33.93  ? 263  ILE B CD1 1 
ATOM   5826 N  N   . ALA B 1 264 ? 5.062   -16.164 57.991  1.00 29.11  ? 264  ALA B N   1 
ATOM   5827 C  CA  . ALA B 1 264 ? 4.564   -15.420 59.138  1.00 31.60  ? 264  ALA B CA  1 
ATOM   5828 C  C   . ALA B 1 264 ? 4.045   -14.055 58.718  1.00 29.97  ? 264  ALA B C   1 
ATOM   5829 O  O   . ALA B 1 264 ? 3.148   -13.510 59.364  1.00 32.34  ? 264  ALA B O   1 
ATOM   5830 C  CB  . ALA B 1 264 ? 5.663   -15.282 60.198  1.00 29.97  ? 264  ALA B CB  1 
ATOM   5831 N  N   . GLY B 1 265 ? 4.546   -13.516 57.609  1.00 31.01  ? 265  GLY B N   1 
ATOM   5832 C  CA  . GLY B 1 265 ? 4.115   -12.205 57.183  1.00 31.97  ? 265  GLY B CA  1 
ATOM   5833 C  C   . GLY B 1 265 ? 2.816   -12.153 56.400  1.00 33.26  ? 265  GLY B C   1 
ATOM   5834 O  O   . GLY B 1 265 ? 2.428   -11.060 55.985  1.00 33.18  ? 265  GLY B O   1 
ATOM   5835 N  N   . HIS B 1 266 ? 2.134   -13.279 56.173  1.00 32.43  ? 266  HIS B N   1 
ATOM   5836 C  CA  . HIS B 1 266 ? 0.829   -13.212 55.505  1.00 32.00  ? 266  HIS B CA  1 
ATOM   5837 C  C   . HIS B 1 266 ? -0.222  -14.145 56.100  1.00 33.35  ? 266  HIS B C   1 
ATOM   5838 O  O   . HIS B 1 266 ? -1.404  -13.791 56.127  1.00 31.70  ? 266  HIS B O   1 
ATOM   5839 C  CB  . HIS B 1 266 ? 0.961   -13.488 53.997  1.00 31.51  ? 266  HIS B CB  1 
ATOM   5840 C  CG  . HIS B 1 266 ? 0.715   -14.915 53.614  1.00 31.72  ? 266  HIS B CG  1 
ATOM   5841 N  ND1 . HIS B 1 266 ? 1.710   -15.870 53.638  1.00 31.25  ? 266  HIS B ND1 1 
ATOM   5842 C  CD2 . HIS B 1 266 ? -0.412  -15.559 53.217  1.00 31.27  ? 266  HIS B CD2 1 
ATOM   5843 C  CE1 . HIS B 1 266 ? 1.209   -17.041 53.280  1.00 31.78  ? 266  HIS B CE1 1 
ATOM   5844 N  NE2 . HIS B 1 266 ? -0.079  -16.881 53.025  1.00 32.04  ? 266  HIS B NE2 1 
ATOM   5845 N  N   . GLU B 1 267 ? 0.168   -15.333 56.570  1.00 30.98  ? 267  GLU B N   1 
ATOM   5846 C  CA  . GLU B 1 267 ? -0.833  -16.370 56.830  1.00 31.23  ? 267  GLU B CA  1 
ATOM   5847 C  C   . GLU B 1 267 ? -1.808  -15.950 57.926  1.00 32.49  ? 267  GLU B C   1 
ATOM   5848 O  O   . GLU B 1 267 ? -3.034  -16.038 57.757  1.00 29.67  ? 267  GLU B O   1 
ATOM   5849 C  CB  . GLU B 1 267 ? -0.139  -17.687 57.177  1.00 33.52  ? 267  GLU B CB  1 
ATOM   5850 C  CG  . GLU B 1 267 ? -0.974  -18.615 58.054  1.00 33.01  ? 267  GLU B CG  1 
ATOM   5851 C  CD  . GLU B 1 267 ? -2.159  -19.215 57.317  1.00 37.30  ? 267  GLU B CD  1 
ATOM   5852 O  OE1 . GLU B 1 267 ? -2.109  -19.360 56.086  1.00 35.44  ? 267  GLU B OE1 1 
ATOM   5853 O  OE2 . GLU B 1 267 ? -3.161  -19.541 57.985  1.00 41.17  ? 267  GLU B OE2 1 
ATOM   5854 N  N   . THR B 1 268 ? -1.283  -15.468 59.046  1.00 30.78  ? 268  THR B N   1 
ATOM   5855 C  CA  . THR B 1 268 ? -2.116  -15.040 60.165  1.00 31.28  ? 268  THR B CA  1 
ATOM   5856 C  C   . THR B 1 268 ? -2.877  -13.756 59.881  1.00 31.35  ? 268  THR B C   1 
ATOM   5857 O  O   . THR B 1 268 ? -3.923  -13.527 60.498  1.00 32.95  ? 268  THR B O   1 
ATOM   5858 C  CB  . THR B 1 268 ? -1.238  -14.865 61.402  1.00 32.60  ? 268  THR B CB  1 
ATOM   5859 O  OG1 . THR B 1 268 ? -0.057  -14.137 61.033  1.00 31.55  ? 268  THR B OG1 1 
ATOM   5860 C  CG2 . THR B 1 268 ? -0.818  -16.243 61.946  1.00 31.54  ? 268  THR B CG2 1 
ATOM   5861 N  N   . THR B 1 269 ? -2.387  -12.917 58.966  1.00 29.19  ? 269  THR B N   1 
ATOM   5862 C  CA  . THR B 1 269 ? -3.145  -11.732 58.597  1.00 30.54  ? 269  THR B CA  1 
ATOM   5863 C  C   . THR B 1 269 ? -4.312  -12.101 57.687  1.00 31.12  ? 269  THR B C   1 
ATOM   5864 O  O   . THR B 1 269 ? -5.381  -11.474 57.756  1.00 31.46  ? 269  THR B O   1 
ATOM   5865 C  CB  . THR B 1 269 ? -2.221  -10.707 57.923  1.00 31.57  ? 269  THR B CB  1 
ATOM   5866 O  OG1 . THR B 1 269 ? -1.129  -10.389 58.808  1.00 29.12  ? 269  THR B OG1 1 
ATOM   5867 C  CG2 . THR B 1 269 ? -2.984  -9.426  57.585  1.00 30.31  ? 269  THR B CG2 1 
ATOM   5868 N  N   . SER B 1 270 ? -4.136  -13.125 56.850  1.00 31.31  ? 270  SER B N   1 
ATOM   5869 C  CA  . SER B 1 270 ? -5.273  -13.646 56.092  1.00 30.96  ? 270  SER B CA  1 
ATOM   5870 C  C   . SER B 1 270 ? -6.334  -14.199 57.037  1.00 31.82  ? 270  SER B C   1 
ATOM   5871 O  O   . SER B 1 270 ? -7.539  -13.962 56.849  1.00 32.25  ? 270  SER B O   1 
ATOM   5872 C  CB  . SER B 1 270 ? -4.805  -14.738 55.122  1.00 30.08  ? 270  SER B CB  1 
ATOM   5873 O  OG  . SER B 1 270 ? -5.928  -15.413 54.579  1.00 36.50  ? 270  SER B OG  1 
ATOM   5874 N  N   . GLY B 1 271 ? -5.902  -14.947 58.056  1.00 31.05  ? 271  GLY B N   1 
ATOM   5875 C  CA  . GLY B 1 271 ? -6.838  -15.423 59.060  1.00 30.57  ? 271  GLY B CA  1 
ATOM   5876 C  C   . GLY B 1 271 ? -7.580  -14.283 59.729  1.00 31.67  ? 271  GLY B C   1 
ATOM   5877 O  O   . GLY B 1 271 ? -8.804  -14.326 59.876  1.00 32.23  ? 271  GLY B O   1 
ATOM   5878 N  N   . LEU B 1 272 ? -6.849  -13.250 60.152  1.00 30.34  ? 272  LEU B N   1 
ATOM   5879 C  CA  . LEU B 1 272 ? -7.483  -12.123 60.840  1.00 32.88  ? 272  LEU B CA  1 
ATOM   5880 C  C   . LEU B 1 272 ? -8.558  -11.472 59.975  1.00 31.65  ? 272  LEU B C   1 
ATOM   5881 O  O   . LEU B 1 272 ? -9.693  -11.249 60.421  1.00 30.77  ? 272  LEU B O   1 
ATOM   5882 C  CB  . LEU B 1 272 ? -6.422  -11.096 61.228  1.00 30.80  ? 272  LEU B CB  1 
ATOM   5883 C  CG  . LEU B 1 272 ? -6.921  -9.727  61.720  1.00 28.37  ? 272  LEU B CG  1 
ATOM   5884 C  CD1 . LEU B 1 272 ? -7.856  -9.887  62.937  1.00 29.09  ? 272  LEU B CD1 1 
ATOM   5885 C  CD2 . LEU B 1 272 ? -5.729  -8.836  62.082  1.00 32.33  ? 272  LEU B CD2 1 
ATOM   5886 N  N   . LEU B 1 273 ? -8.219  -11.137 58.732  1.00 29.45  ? 273  LEU B N   1 
ATOM   5887 C  CA  . LEU B 1 273 ? -9.199  -10.482 57.874  1.00 30.50  ? 273  LEU B CA  1 
ATOM   5888 C  C   . LEU B 1 273 ? -10.411 -11.375 57.658  1.00 32.42  ? 273  LEU B C   1 
ATOM   5889 O  O   . LEU B 1 273 ? -11.548 -10.888 57.619  1.00 31.93  ? 273  LEU B O   1 
ATOM   5890 C  CB  . LEU B 1 273 ? -8.561  -10.104 56.529  1.00 29.46  ? 273  LEU B CB  1 
ATOM   5891 C  CG  . LEU B 1 273 ? -7.671  -8.857  56.575  1.00 31.48  ? 273  LEU B CG  1 
ATOM   5892 C  CD1 . LEU B 1 273 ? -6.761  -8.733  55.332  1.00 28.88  ? 273  LEU B CD1 1 
ATOM   5893 C  CD2 . LEU B 1 273 ? -8.561  -7.615  56.701  1.00 33.21  ? 273  LEU B CD2 1 
ATOM   5894 N  N   . SER B 1 274 ? -10.184 -12.687 57.500  1.00 31.13  ? 274  SER B N   1 
ATOM   5895 C  CA  . SER B 1 274 ? -11.294 -13.613 57.305  1.00 29.89  ? 274  SER B CA  1 
ATOM   5896 C  C   . SER B 1 274 ? -12.196 -13.655 58.535  1.00 30.12  ? 274  SER B C   1 
ATOM   5897 O  O   . SER B 1 274 ? -13.423 -13.572 58.413  1.00 31.89  ? 274  SER B O   1 
ATOM   5898 C  CB  . SER B 1 274 ? -10.768 -15.018 56.970  1.00 31.94  ? 274  SER B CB  1 
ATOM   5899 O  OG  . SER B 1 274 ? -9.976  -15.026 55.779  1.00 32.08  ? 274  SER B OG  1 
ATOM   5900 N  N   . PHE B 1 275 ? -11.611 -13.799 59.735  1.00 30.17  ? 275  PHE B N   1 
ATOM   5901 C  CA  . PHE B 1 275 ? -12.427 -13.780 60.950  1.00 32.09  ? 275  PHE B CA  1 
ATOM   5902 C  C   . PHE B 1 275 ? -13.127 -12.436 61.116  1.00 32.14  ? 275  PHE B C   1 
ATOM   5903 O  O   . PHE B 1 275 ? -14.287 -12.377 61.550  1.00 32.32  ? 275  PHE B O   1 
ATOM   5904 C  CB  . PHE B 1 275 ? -11.570 -14.061 62.188  1.00 28.54  ? 275  PHE B CB  1 
ATOM   5905 C  CG  . PHE B 1 275 ? -11.300 -15.524 62.444  1.00 31.19  ? 275  PHE B CG  1 
ATOM   5906 C  CD1 . PHE B 1 275 ? -12.332 -16.389 62.819  1.00 33.46  ? 275  PHE B CD1 1 
ATOM   5907 C  CD2 . PHE B 1 275 ? -10.011 -16.025 62.343  1.00 30.24  ? 275  PHE B CD2 1 
ATOM   5908 C  CE1 . PHE B 1 275 ? -12.087 -17.730 63.073  1.00 30.64  ? 275  PHE B CE1 1 
ATOM   5909 C  CE2 . PHE B 1 275 ? -9.746  -17.365 62.605  1.00 32.05  ? 275  PHE B CE2 1 
ATOM   5910 C  CZ  . PHE B 1 275 ? -10.784 -18.230 62.962  1.00 34.87  ? 275  PHE B CZ  1 
ATOM   5911 N  N   . ALA B 1 276 ? -12.428 -11.341 60.807  1.00 30.48  ? 276  ALA B N   1 
ATOM   5912 C  CA  . ALA B 1 276 ? -13.033 -10.018 60.968  1.00 32.33  ? 276  ALA B CA  1 
ATOM   5913 C  C   . ALA B 1 276 ? -14.280 -9.886  60.097  1.00 32.99  ? 276  ALA B C   1 
ATOM   5914 O  O   . ALA B 1 276 ? -15.347 -9.465  60.569  1.00 31.87  ? 276  ALA B O   1 
ATOM   5915 C  CB  . ALA B 1 276 ? -12.007 -8.925  60.632  1.00 30.78  ? 276  ALA B CB  1 
ATOM   5916 N  N   . LEU B 1 277 ? -14.175 -10.276 58.824  1.00 31.42  ? 277  LEU B N   1 
ATOM   5917 C  CA  . LEU B 1 277 ? -15.337 -10.177 57.944  1.00 29.26  ? 277  LEU B CA  1 
ATOM   5918 C  C   . LEU B 1 277 ? -16.450 -11.109 58.401  1.00 32.09  ? 277  LEU B C   1 
ATOM   5919 O  O   . LEU B 1 277 ? -17.638 -10.755 58.314  1.00 33.21  ? 277  LEU B O   1 
ATOM   5920 C  CB  . LEU B 1 277 ? -14.938 -10.459 56.494  1.00 30.75  ? 277  LEU B CB  1 
ATOM   5921 C  CG  . LEU B 1 277 ? -16.082 -10.231 55.502  1.00 33.21  ? 277  LEU B CG  1 
ATOM   5922 C  CD1 . LEU B 1 277 ? -16.556 -8.778  55.532  1.00 33.78  ? 277  LEU B CD1 1 
ATOM   5923 C  CD2 . LEU B 1 277 ? -15.660 -10.650 54.099  1.00 32.80  ? 277  LEU B CD2 1 
ATOM   5924 N  N   . TYR B 1 278 ? -16.094 -12.305 58.875  1.00 30.43  ? 278  TYR B N   1 
ATOM   5925 C  CA  . TYR B 1 278 ? -17.093 -13.197 59.463  1.00 29.70  ? 278  TYR B CA  1 
ATOM   5926 C  C   . TYR B 1 278 ? -17.843 -12.494 60.586  1.00 34.79  ? 278  TYR B C   1 
ATOM   5927 O  O   . TYR B 1 278 ? -19.080 -12.471 60.615  1.00 31.93  ? 278  TYR B O   1 
ATOM   5928 C  CB  . TYR B 1 278 ? -16.429 -14.470 59.988  1.00 30.08  ? 278  TYR B CB  1 
ATOM   5929 C  CG  . TYR B 1 278 ? -17.335 -15.275 60.870  1.00 32.05  ? 278  TYR B CG  1 
ATOM   5930 C  CD1 . TYR B 1 278 ? -18.250 -16.169 60.315  1.00 33.68  ? 278  TYR B CD1 1 
ATOM   5931 C  CD2 . TYR B 1 278 ? -17.303 -15.123 62.253  1.00 32.50  ? 278  TYR B CD2 1 
ATOM   5932 C  CE1 . TYR B 1 278 ? -19.105 -16.905 61.126  1.00 31.57  ? 278  TYR B CE1 1 
ATOM   5933 C  CE2 . TYR B 1 278 ? -18.148 -15.850 63.070  1.00 36.05  ? 278  TYR B CE2 1 
ATOM   5934 C  CZ  . TYR B 1 278 ? -19.046 -16.735 62.502  1.00 35.37  ? 278  TYR B CZ  1 
ATOM   5935 O  OH  . TYR B 1 278 ? -19.898 -17.437 63.327  1.00 34.96  ? 278  TYR B OH  1 
ATOM   5936 N  N   . PHE B 1 279 ? -17.107 -11.938 61.548  1.00 31.95  ? 279  PHE B N   1 
ATOM   5937 C  CA  . PHE B 1 279 ? -17.797 -11.326 62.677  1.00 31.73  ? 279  PHE B CA  1 
ATOM   5938 C  C   . PHE B 1 279 ? -18.631 -10.129 62.237  1.00 33.65  ? 279  PHE B C   1 
ATOM   5939 O  O   . PHE B 1 279 ? -19.728 -9.913  62.764  1.00 32.98  ? 279  PHE B O   1 
ATOM   5940 C  CB  . PHE B 1 279 ? -16.788 -10.956 63.763  1.00 31.68  ? 279  PHE B CB  1 
ATOM   5941 C  CG  . PHE B 1 279 ? -16.376 -12.140 64.604  1.00 33.45  ? 279  PHE B CG  1 
ATOM   5942 C  CD1 . PHE B 1 279 ? -17.336 -12.866 65.320  1.00 32.60  ? 279  PHE B CD1 1 
ATOM   5943 C  CD2 . PHE B 1 279 ? -15.044 -12.534 64.690  1.00 34.64  ? 279  PHE B CD2 1 
ATOM   5944 C  CE1 . PHE B 1 279 ? -16.976 -13.962 66.091  1.00 35.67  ? 279  PHE B CE1 1 
ATOM   5945 C  CE2 . PHE B 1 279 ? -14.675 -13.628 65.479  1.00 34.73  ? 279  PHE B CE2 1 
ATOM   5946 C  CZ  . PHE B 1 279 ? -15.642 -14.344 66.178  1.00 32.42  ? 279  PHE B CZ  1 
ATOM   5947 N  N   . LEU B 1 280 ? -18.171 -9.382  61.242  1.00 31.85  ? 280  LEU B N   1 
ATOM   5948 C  CA  . LEU B 1 280 ? -18.955 -8.235  60.789  1.00 32.15  ? 280  LEU B CA  1 
ATOM   5949 C  C   . LEU B 1 280 ? -20.291 -8.677  60.188  1.00 32.97  ? 280  LEU B C   1 
ATOM   5950 O  O   . LEU B 1 280 ? -21.345 -8.127  60.532  1.00 34.05  ? 280  LEU B O   1 
ATOM   5951 C  CB  . LEU B 1 280 ? -18.153 -7.407  59.790  1.00 32.61  ? 280  LEU B CB  1 
ATOM   5952 C  CG  . LEU B 1 280 ? -16.998 -6.621  60.397  1.00 31.49  ? 280  LEU B CG  1 
ATOM   5953 C  CD1 . LEU B 1 280 ? -16.256 -5.910  59.268  1.00 33.10  ? 280  LEU B CD1 1 
ATOM   5954 C  CD2 . LEU B 1 280 ? -17.445 -5.629  61.463  1.00 37.49  ? 280  LEU B CD2 1 
ATOM   5955 N  N   . VAL B 1 281 ? -20.275 -9.670  59.294  1.00 34.27  ? 281  VAL B N   1 
ATOM   5956 C  CA  . VAL B 1 281 ? -21.551 -10.066 58.691  1.00 31.71  ? 281  VAL B CA  1 
ATOM   5957 C  C   . VAL B 1 281 ? -22.457 -10.757 59.708  1.00 34.71  ? 281  VAL B C   1 
ATOM   5958 O  O   . VAL B 1 281 ? -23.681 -10.774 59.521  1.00 36.37  ? 281  VAL B O   1 
ATOM   5959 C  CB  . VAL B 1 281 ? -21.358 -10.929 57.420  1.00 32.18  ? 281  VAL B CB  1 
ATOM   5960 C  CG1 . VAL B 1 281 ? -20.512 -10.188 56.391  1.00 37.92  ? 281  VAL B CG1 1 
ATOM   5961 C  CG2 . VAL B 1 281 ? -20.773 -12.323 57.726  1.00 32.33  ? 281  VAL B CG2 1 
ATOM   5962 N  N   . LYS B 1 282 ? -21.912 -11.298 60.801  1.00 30.18  ? 282  LYS B N   1 
ATOM   5963 C  CA  . LYS B 1 282 ? -22.762 -11.867 61.848  1.00 32.99  ? 282  LYS B CA  1 
ATOM   5964 C  C   . LYS B 1 282 ? -23.248 -10.834 62.863  1.00 34.93  ? 282  LYS B C   1 
ATOM   5965 O  O   . LYS B 1 282 ? -24.073 -11.175 63.719  1.00 34.96  ? 282  LYS B O   1 
ATOM   5966 C  CB  . LYS B 1 282 ? -22.025 -12.995 62.596  1.00 33.65  ? 282  LYS B CB  1 
ATOM   5967 C  CG  . LYS B 1 282 ? -21.640 -14.212 61.714  1.00 34.60  ? 282  LYS B CG  1 
ATOM   5968 C  CD  . LYS B 1 282 ? -22.873 -14.864 61.071  1.00 35.85  ? 282  LYS B CD  1 
ATOM   5969 C  CE  . LYS B 1 282 ? -22.497 -16.219 60.437  1.00 34.06  ? 282  LYS B CE  1 
ATOM   5970 N  NZ  . LYS B 1 282 ? -23.688 -16.896 59.801  1.00 32.70  ? 282  LYS B NZ  1 
ATOM   5971 N  N   . ASN B 1 283 ? -22.771 -9.595  62.785  1.00 33.31  ? 283  ASN B N   1 
ATOM   5972 C  CA  . ASN B 1 283 ? -23.063 -8.568  63.791  1.00 33.65  ? 283  ASN B CA  1 
ATOM   5973 C  C   . ASN B 1 283 ? -23.368 -7.269  63.068  1.00 33.07  ? 283  ASN B C   1 
ATOM   5974 O  O   . ASN B 1 283 ? -22.557 -6.336  63.042  1.00 33.58  ? 283  ASN B O   1 
ATOM   5975 C  CB  . ASN B 1 283 ? -21.904 -8.420  64.786  1.00 33.75  ? 283  ASN B CB  1 
ATOM   5976 C  CG  . ASN B 1 283 ? -21.761 -9.637  65.658  1.00 34.61  ? 283  ASN B CG  1 
ATOM   5977 O  OD1 . ASN B 1 283 ? -22.490 -9.792  66.651  1.00 34.22  ? 283  ASN B OD1 1 
ATOM   5978 N  ND2 . ASN B 1 283 ? -20.847 -10.545 65.276  1.00 31.61  ? 283  ASN B ND2 1 
ATOM   5979 N  N   . PRO B 1 284 ? -24.553 -7.176  62.460  1.00 32.86  ? 284  PRO B N   1 
ATOM   5980 C  CA  . PRO B 1 284 ? -24.857 -6.026  61.592  1.00 32.87  ? 284  PRO B CA  1 
ATOM   5981 C  C   . PRO B 1 284 ? -24.726 -4.674  62.276  1.00 33.65  ? 284  PRO B C   1 
ATOM   5982 O  O   . PRO B 1 284 ? -24.395 -3.696  61.597  1.00 34.52  ? 284  PRO B O   1 
ATOM   5983 C  CB  . PRO B 1 284 ? -26.308 -6.275  61.149  1.00 37.56  ? 284  PRO B CB  1 
ATOM   5984 C  CG  . PRO B 1 284 ? -26.700 -7.636  61.658  1.00 38.14  ? 284  PRO B CG  1 
ATOM   5985 C  CD  . PRO B 1 284 ? -25.571 -8.237  62.428  1.00 34.41  ? 284  PRO B CD  1 
ATOM   5986 N  N   . HIS B 1 285 ? -24.985 -4.576  63.585  1.00 31.07  ? 285  HIS B N   1 
ATOM   5987 C  CA  . HIS B 1 285 ? -24.798 -3.295  64.268  1.00 31.02  ? 285  HIS B CA  1 
ATOM   5988 C  C   . HIS B 1 285 ? -23.344 -2.862  64.189  1.00 32.90  ? 285  HIS B C   1 
ATOM   5989 O  O   . HIS B 1 285 ? -23.037 -1.689  63.945  1.00 33.64  ? 285  HIS B O   1 
ATOM   5990 C  CB  . HIS B 1 285 ? -25.206 -3.399  65.739  1.00 35.42  ? 285  HIS B CB  1 
ATOM   5991 C  CG  . HIS B 1 285 ? -26.685 -3.463  65.964  1.00 35.34  ? 285  HIS B CG  1 
ATOM   5992 N  ND1 . HIS B 1 285 ? -27.558 -2.513  65.480  1.00 40.97  ? 285  HIS B ND1 1 
ATOM   5993 C  CD2 . HIS B 1 285 ? -27.438 -4.365  66.634  1.00 35.28  ? 285  HIS B CD2 1 
ATOM   5994 C  CE1 . HIS B 1 285 ? -28.791 -2.830  65.846  1.00 34.35  ? 285  HIS B CE1 1 
ATOM   5995 N  NE2 . HIS B 1 285 ? -28.745 -3.948  66.543  1.00 36.75  ? 285  HIS B NE2 1 
ATOM   5996 N  N   . VAL B 1 286 ? -22.440 -3.807  64.421  1.00 31.86  ? 286  VAL B N   1 
ATOM   5997 C  CA  . VAL B 1 286 ? -21.016 -3.504  64.369  1.00 32.00  ? 286  VAL B CA  1 
ATOM   5998 C  C   . VAL B 1 286 ? -20.589 -3.188  62.942  1.00 32.64  ? 286  VAL B C   1 
ATOM   5999 O  O   . VAL B 1 286 ? -19.811 -2.253  62.700  1.00 33.07  ? 286  VAL B O   1 
ATOM   6000 C  CB  . VAL B 1 286 ? -20.223 -4.684  64.949  1.00 32.20  ? 286  VAL B CB  1 
ATOM   6001 C  CG1 . VAL B 1 286 ? -18.715 -4.438  64.790  1.00 33.06  ? 286  VAL B CG1 1 
ATOM   6002 C  CG2 . VAL B 1 286 ? -20.625 -4.940  66.400  1.00 31.63  ? 286  VAL B CG2 1 
ATOM   6003 N  N   . LEU B 1 287 ? -21.071 -3.969  61.979  1.00 32.32  ? 287  LEU B N   1 
ATOM   6004 C  CA  . LEU B 1 287 ? -20.772 -3.678  60.584  1.00 33.02  ? 287  LEU B CA  1 
ATOM   6005 C  C   . LEU B 1 287 ? -21.173 -2.254  60.225  1.00 34.88  ? 287  LEU B C   1 
ATOM   6006 O  O   . LEU B 1 287 ? -20.411 -1.525  59.581  1.00 33.60  ? 287  LEU B O   1 
ATOM   6007 C  CB  . LEU B 1 287 ? -21.469 -4.697  59.683  1.00 33.84  ? 287  LEU B CB  1 
ATOM   6008 C  CG  . LEU B 1 287 ? -21.399 -4.460  58.182  1.00 38.84  ? 287  LEU B CG  1 
ATOM   6009 C  CD1 . LEU B 1 287 ? -19.983 -4.219  57.756  1.00 38.79  ? 287  LEU B CD1 1 
ATOM   6010 C  CD2 . LEU B 1 287 ? -21.980 -5.678  57.457  1.00 44.30  ? 287  LEU B CD2 1 
ATOM   6011 N  N   . GLN B 1 288 ? -22.365 -1.830  60.641  1.00 35.32  ? 288  GLN B N   1 
ATOM   6012 C  CA  . GLN B 1 288 ? -22.804 -0.480  60.308  1.00 35.30  ? 288  GLN B CA  1 
ATOM   6013 C  C   . GLN B 1 288 ? -21.861 0.564   60.890  1.00 34.75  ? 288  GLN B C   1 
ATOM   6014 O  O   . GLN B 1 288 ? -21.507 1.534   60.207  1.00 34.95  ? 288  GLN B O   1 
ATOM   6015 C  CB  . GLN B 1 288 ? -24.233 -0.250  60.796  1.00 38.90  ? 288  GLN B CB  1 
ATOM   6016 C  CG  . GLN B 1 288 ? -24.742 1.172   60.599  1.00 42.21  ? 288  GLN B CG  1 
ATOM   6017 C  CD  . GLN B 1 288 ? -26.208 1.304   60.983  1.00 58.53  ? 288  GLN B CD  1 
ATOM   6018 O  OE1 . GLN B 1 288 ? -26.538 1.818   62.054  1.00 63.47  ? 288  GLN B OE1 1 
ATOM   6019 N  NE2 . GLN B 1 288 ? -27.095 0.825   60.113  1.00 62.56  ? 288  GLN B NE2 1 
ATOM   6020 N  N   . LYS B 1 289 ? -21.418 0.372   62.141  1.00 33.88  ? 289  LYS B N   1 
ATOM   6021 C  CA  . LYS B 1 289 ? -20.527 1.361   62.748  1.00 32.61  ? 289  LYS B CA  1 
ATOM   6022 C  C   . LYS B 1 289 ? -19.190 1.395   62.022  1.00 32.65  ? 289  LYS B C   1 
ATOM   6023 O  O   . LYS B 1 289 ? -18.620 2.469   61.814  1.00 33.16  ? 289  LYS B O   1 
ATOM   6024 C  CB  . LYS B 1 289 ? -20.309 1.073   64.238  1.00 33.96  ? 289  LYS B CB  1 
ATOM   6025 C  CG  . LYS B 1 289 ? -21.453 1.566   65.146  1.00 40.49  ? 289  LYS B CG  1 
ATOM   6026 C  CD  . LYS B 1 289 ? -21.269 1.136   66.614  1.00 37.17  ? 289  LYS B CD  1 
ATOM   6027 C  CE  . LYS B 1 289 ? -20.198 1.942   67.362  1.00 36.38  ? 289  LYS B CE  1 
ATOM   6028 N  NZ  . LYS B 1 289 ? -20.395 1.882   68.872  1.00 34.19  ? 289  LYS B NZ  1 
ATOM   6029 N  N   . ALA B 1 290 ? -18.672 0.226   61.627  1.00 33.79  ? 290  ALA B N   1 
ATOM   6030 C  CA  . ALA B 1 290 ? -17.393 0.206   60.931  1.00 30.37  ? 290  ALA B CA  1 
ATOM   6031 C  C   . ALA B 1 290 ? -17.520 0.816   59.544  1.00 32.01  ? 290  ALA B C   1 
ATOM   6032 O  O   . ALA B 1 290 ? -16.634 1.553   59.090  1.00 33.09  ? 290  ALA B O   1 
ATOM   6033 C  CB  . ALA B 1 290 ? -16.870 -1.232  60.841  1.00 34.48  ? 290  ALA B CB  1 
ATOM   6034 N  N   . ALA B 1 291 ? -18.618 0.519   58.847  1.00 31.42  ? 291  ALA B N   1 
ATOM   6035 C  CA  . ALA B 1 291 ? -18.793 1.057   57.506  1.00 33.43  ? 291  ALA B CA  1 
ATOM   6036 C  C   . ALA B 1 291 ? -18.990 2.571   57.539  1.00 31.80  ? 291  ALA B C   1 
ATOM   6037 O  O   . ALA B 1 291 ? -18.494 3.282   56.664  1.00 31.52  ? 291  ALA B O   1 
ATOM   6038 C  CB  . ALA B 1 291 ? -19.966 0.354   56.813  1.00 35.16  ? 291  ALA B CB  1 
ATOM   6039 N  N   . GLU B 1 292 ? -19.697 3.084   58.546  1.00 32.80  ? 292  GLU B N   1 
ATOM   6040 C  CA  . GLU B 1 292 ? -19.813 4.531   58.710  1.00 34.60  ? 292  GLU B CA  1 
ATOM   6041 C  C   . GLU B 1 292 ? -18.439 5.171   58.772  1.00 33.42  ? 292  GLU B C   1 
ATOM   6042 O  O   . GLU B 1 292 ? -18.173 6.177   58.107  1.00 32.00  ? 292  GLU B O   1 
ATOM   6043 C  CB  . GLU B 1 292 ? -20.596 4.868   59.984  1.00 36.44  ? 292  GLU B CB  1 
ATOM   6044 C  CG  . GLU B 1 292 ? -20.954 6.373   60.108  1.00 36.30  ? 292  GLU B CG  1 
ATOM   6045 C  CD  . GLU B 1 292 ? -19.786 7.280   60.556  1.00 37.50  ? 292  GLU B CD  1 
ATOM   6046 O  OE1 . GLU B 1 292 ? -18.885 6.833   61.308  1.00 36.95  ? 292  GLU B OE1 1 
ATOM   6047 O  OE2 . GLU B 1 292 ? -19.785 8.466   60.156  1.00 39.28  ? 292  GLU B OE2 1 
ATOM   6048 N  N   . GLU B 1 293 ? -17.552 4.596   59.583  1.00 32.43  ? 293  GLU B N   1 
ATOM   6049 C  CA  . GLU B 1 293 ? -16.230 5.189   59.742  1.00 32.61  ? 293  GLU B CA  1 
ATOM   6050 C  C   . GLU B 1 293 ? -15.443 5.126   58.446  1.00 33.87  ? 293  GLU B C   1 
ATOM   6051 O  O   . GLU B 1 293 ? -14.820 6.116   58.040  1.00 32.09  ? 293  GLU B O   1 
ATOM   6052 C  CB  . GLU B 1 293 ? -15.469 4.482   60.855  1.00 30.36  ? 293  GLU B CB  1 
ATOM   6053 C  CG  . GLU B 1 293 ? -14.118 5.093   61.129  1.00 32.46  ? 293  GLU B CG  1 
ATOM   6054 C  CD  . GLU B 1 293 ? -13.401 4.339   62.231  1.00 33.81  ? 293  GLU B CD  1 
ATOM   6055 O  OE1 . GLU B 1 293 ? -12.820 3.267   61.938  1.00 32.84  ? 293  GLU B OE1 1 
ATOM   6056 O  OE2 . GLU B 1 293 ? -13.448 4.808   63.384  1.00 34.17  ? 293  GLU B OE2 1 
ATOM   6057 N  N   . ALA B 1 294 ? -15.433 3.952   57.803  1.00 30.98  ? 294  ALA B N   1 
ATOM   6058 C  CA  . ALA B 1 294 ? -14.717 3.802   56.541  1.00 34.43  ? 294  ALA B CA  1 
ATOM   6059 C  C   . ALA B 1 294 ? -15.192 4.828   55.520  1.00 34.71  ? 294  ALA B C   1 
ATOM   6060 O  O   . ALA B 1 294 ? -14.382 5.470   54.840  1.00 34.70  ? 294  ALA B O   1 
ATOM   6061 C  CB  . ALA B 1 294 ? -14.895 2.381   56.003  1.00 34.55  ? 294  ALA B CB  1 
ATOM   6062 N  N   . ALA B 1 295 ? -16.512 4.975   55.379  1.00 34.77  ? 295  ALA B N   1 
ATOM   6063 C  CA  . ALA B 1 295 ? -17.047 5.909   54.391  1.00 38.45  ? 295  ALA B CA  1 
ATOM   6064 C  C   . ALA B 1 295 ? -16.649 7.347   54.712  1.00 37.86  ? 295  ALA B C   1 
ATOM   6065 O  O   . ALA B 1 295 ? -16.341 8.134   53.809  1.00 38.89  ? 295  ALA B O   1 
ATOM   6066 C  CB  . ALA B 1 295 ? -18.568 5.770   54.325  1.00 36.76  ? 295  ALA B CB  1 
ATOM   6067 N  N   . ARG B 1 296 ? -16.636 7.705   55.998  1.00 35.04  ? 296  ARG B N   1 
ATOM   6068 C  CA  . ARG B 1 296 ? -16.383 9.085   56.392  1.00 37.76  ? 296  ARG B CA  1 
ATOM   6069 C  C   . ARG B 1 296 ? -14.903 9.437   56.329  1.00 38.77  ? 296  ARG B C   1 
ATOM   6070 O  O   . ARG B 1 296 ? -14.547 10.567  55.972  1.00 38.41  ? 296  ARG B O   1 
ATOM   6071 C  CB  . ARG B 1 296 ? -16.927 9.319   57.800  1.00 37.38  ? 296  ARG B CB  1 
ATOM   6072 C  CG  . ARG B 1 296 ? -16.366 10.536  58.500  1.00 39.90  ? 296  ARG B CG  1 
ATOM   6073 C  CD  . ARG B 1 296 ? -17.218 10.848  59.726  1.00 40.16  ? 296  ARG B CD  1 
ATOM   6074 N  NE  . ARG B 1 296 ? -17.339 9.698   60.621  1.00 36.92  ? 296  ARG B NE  1 
ATOM   6075 C  CZ  . ARG B 1 296 ? -16.466 9.408   61.580  1.00 40.24  ? 296  ARG B CZ  1 
ATOM   6076 N  NH1 . ARG B 1 296 ? -15.379 10.143  61.769  1.00 41.10  ? 296  ARG B NH1 1 
ATOM   6077 N  NH2 . ARG B 1 296 ? -16.680 8.349   62.361  1.00 38.31  ? 296  ARG B NH2 1 
ATOM   6078 N  N   . VAL B 1 297 ? -14.035 8.489   56.664  1.00 33.95  ? 297  VAL B N   1 
ATOM   6079 C  CA  . VAL B 1 297 ? -12.600 8.759   56.758  1.00 35.39  ? 297  VAL B CA  1 
ATOM   6080 C  C   . VAL B 1 297 ? -11.913 8.630   55.402  1.00 35.36  ? 297  VAL B C   1 
ATOM   6081 O  O   . VAL B 1 297 ? -11.063 9.458   55.044  1.00 35.05  ? 297  VAL B O   1 
ATOM   6082 C  CB  . VAL B 1 297 ? -11.991 7.804   57.798  1.00 33.97  ? 297  VAL B CB  1 
ATOM   6083 C  CG1 . VAL B 1 297 ? -10.451 7.809   57.724  1.00 36.17  ? 297  VAL B CG1 1 
ATOM   6084 C  CG2 . VAL B 1 297 ? -12.449 8.190   59.193  1.00 34.56  ? 297  VAL B CG2 1 
ATOM   6085 N  N   . LEU B 1 298 ? -12.263 7.592   54.634  1.00 33.68  ? 298  LEU B N   1 
ATOM   6086 C  CA  . LEU B 1 298 ? -11.583 7.288   53.371  1.00 35.86  ? 298  LEU B CA  1 
ATOM   6087 C  C   . LEU B 1 298 ? -12.220 8.091   52.237  1.00 35.22  ? 298  LEU B C   1 
ATOM   6088 O  O   . LEU B 1 298 ? -12.895 7.565   51.355  1.00 37.24  ? 298  LEU B O   1 
ATOM   6089 C  CB  . LEU B 1 298 ? -11.633 5.792   53.092  1.00 34.85  ? 298  LEU B CB  1 
ATOM   6090 C  CG  . LEU B 1 298 ? -10.968 4.928   54.157  1.00 36.15  ? 298  LEU B CG  1 
ATOM   6091 C  CD1 . LEU B 1 298 ? -10.987 3.467   53.729  1.00 38.18  ? 298  LEU B CD1 1 
ATOM   6092 C  CD2 . LEU B 1 298 ? -9.549  5.393   54.391  1.00 32.93  ? 298  LEU B CD2 1 
ATOM   6093 N  N   . VAL B 1 299 ? -11.984 9.409   52.275  1.00 36.76  ? 299  VAL B N   1 
ATOM   6094 C  CA  . VAL B 1 299 ? -12.667 10.312  51.346  1.00 36.17  ? 299  VAL B CA  1 
ATOM   6095 C  C   . VAL B 1 299 ? -12.003 10.382  49.984  1.00 40.07  ? 299  VAL B C   1 
ATOM   6096 O  O   . VAL B 1 299 ? -12.567 10.987  49.063  1.00 40.94  ? 299  VAL B O   1 
ATOM   6097 C  CB  . VAL B 1 299 ? -12.753 11.736  51.931  1.00 38.89  ? 299  VAL B CB  1 
ATOM   6098 C  CG1 . VAL B 1 299 ? -13.608 11.710  53.182  1.00 42.97  ? 299  VAL B CG1 1 
ATOM   6099 C  CG2 . VAL B 1 299 ? -11.368 12.283  52.216  1.00 39.30  ? 299  VAL B CG2 1 
ATOM   6100 N  N   . ASP B 1 300 ? -10.830 9.791   49.827  1.00 38.44  ? 300  ASP B N   1 
ATOM   6101 C  CA  . ASP B 1 300 ? -10.119 9.836   48.559  1.00 42.37  ? 300  ASP B CA  1 
ATOM   6102 C  C   . ASP B 1 300 ? -10.092 8.461   47.907  1.00 40.47  ? 300  ASP B C   1 
ATOM   6103 O  O   . ASP B 1 300 ? -10.092 7.440   48.604  1.00 37.47  ? 300  ASP B O   1 
ATOM   6104 C  CB  . ASP B 1 300 ? -8.676  10.319  48.748  1.00 40.62  ? 300  ASP B CB  1 
ATOM   6105 C  CG  . ASP B 1 300 ? -8.596  11.700  49.377  1.00 43.06  ? 300  ASP B CG  1 
ATOM   6106 O  OD1 . ASP B 1 300 ? -9.372  12.581  48.966  1.00 44.04  ? 300  ASP B OD1 1 
ATOM   6107 O  OD2 . ASP B 1 300 ? -7.749  11.914  50.269  1.00 44.57  ? 300  ASP B OD2 1 
ATOM   6108 N  N   . PRO B 1 301 ? -10.020 8.404   46.572  1.00 39.42  ? 301  PRO B N   1 
ATOM   6109 C  CA  . PRO B 1 301 ? -9.950  7.097   45.898  1.00 42.01  ? 301  PRO B CA  1 
ATOM   6110 C  C   . PRO B 1 301 ? -8.749  6.269   46.314  1.00 39.74  ? 301  PRO B C   1 
ATOM   6111 O  O   . PRO B 1 301 ? -8.844  5.038   46.339  1.00 41.79  ? 301  PRO B O   1 
ATOM   6112 C  CB  . PRO B 1 301 ? -9.886  7.467   44.406  1.00 42.95  ? 301  PRO B CB  1 
ATOM   6113 C  CG  . PRO B 1 301 ? -10.365 8.887   44.326  1.00 47.52  ? 301  PRO B CG  1 
ATOM   6114 C  CD  . PRO B 1 301 ? -10.019 9.534   45.629  1.00 44.51  ? 301  PRO B CD  1 
ATOM   6115 N  N   . VAL B 1 302 ? -7.627  6.902   46.645  1.00 38.46  ? 302  VAL B N   1 
ATOM   6116 C  CA  . VAL B 1 302 ? -6.432  6.224   47.137  1.00 41.92  ? 302  VAL B CA  1 
ATOM   6117 C  C   . VAL B 1 302 ? -6.286  6.574   48.618  1.00 41.96  ? 302  VAL B C   1 
ATOM   6118 O  O   . VAL B 1 302 ? -5.970  7.725   48.944  1.00 42.36  ? 302  VAL B O   1 
ATOM   6119 C  CB  . VAL B 1 302 ? -5.188  6.641   46.340  1.00 42.86  ? 302  VAL B CB  1 
ATOM   6120 C  CG1 . VAL B 1 302 ? -3.973  5.828   46.745  1.00 43.36  ? 302  VAL B CG1 1 
ATOM   6121 C  CG2 . VAL B 1 302 ? -5.446  6.511   44.826  1.00 45.09  ? 302  VAL B CG2 1 
ATOM   6122 N  N   . PRO B 1 303 ? -6.510  5.636   49.541  1.00 39.78  ? 303  PRO B N   1 
ATOM   6123 C  CA  . PRO B 1 303 ? -6.335  5.953   50.969  1.00 39.81  ? 303  PRO B CA  1 
ATOM   6124 C  C   . PRO B 1 303 ? -4.896  6.339   51.276  1.00 36.98  ? 303  PRO B C   1 
ATOM   6125 O  O   . PRO B 1 303 ? -3.954  5.762   50.731  1.00 36.41  ? 303  PRO B O   1 
ATOM   6126 C  CB  . PRO B 1 303 ? -6.723  4.648   51.675  1.00 42.66  ? 303  PRO B CB  1 
ATOM   6127 C  CG  . PRO B 1 303 ? -7.571  3.907   50.671  1.00 42.59  ? 303  PRO B CG  1 
ATOM   6128 C  CD  . PRO B 1 303 ? -7.003  4.262   49.332  1.00 40.56  ? 303  PRO B CD  1 
ATOM   6129 N  N   . SER B 1 304 ? -4.732  7.321   52.161  1.00 35.46  ? 304  SER B N   1 
ATOM   6130 C  CA  . SER B 1 304 ? -3.414  7.729   52.633  1.00 38.82  ? 304  SER B CA  1 
ATOM   6131 C  C   . SER B 1 304 ? -3.055  7.031   53.944  1.00 32.58  ? 304  SER B C   1 
ATOM   6132 O  O   . SER B 1 304 ? -3.909  6.521   54.666  1.00 32.80  ? 304  SER B O   1 
ATOM   6133 C  CB  . SER B 1 304 ? -3.351  9.248   52.852  1.00 38.80  ? 304  SER B CB  1 
ATOM   6134 O  OG  . SER B 1 304 ? -4.192  9.623   53.940  1.00 36.87  ? 304  SER B OG  1 
ATOM   6135 N  N   . TYR B 1 305 ? -1.761  7.057   54.260  1.00 34.57  ? 305  TYR B N   1 
ATOM   6136 C  CA  . TYR B 1 305 ? -1.292  6.534   55.535  1.00 35.28  ? 305  TYR B CA  1 
ATOM   6137 C  C   . TYR B 1 305 ? -2.021  7.190   56.703  1.00 37.43  ? 305  TYR B C   1 
ATOM   6138 O  O   . TYR B 1 305 ? -2.495  6.505   57.618  1.00 36.22  ? 305  TYR B O   1 
ATOM   6139 C  CB  . TYR B 1 305 ? 0.214   6.762   55.634  1.00 38.75  ? 305  TYR B CB  1 
ATOM   6140 C  CG  . TYR B 1 305 ? 0.840   6.223   56.886  1.00 39.73  ? 305  TYR B CG  1 
ATOM   6141 C  CD1 . TYR B 1 305 ? 0.901   6.994   58.035  1.00 44.71  ? 305  TYR B CD1 1 
ATOM   6142 C  CD2 . TYR B 1 305 ? 1.379   4.944   56.916  1.00 40.11  ? 305  TYR B CD2 1 
ATOM   6143 C  CE1 . TYR B 1 305 ? 1.477   6.510   59.177  1.00 46.29  ? 305  TYR B CE1 1 
ATOM   6144 C  CE2 . TYR B 1 305 ? 1.961   4.452   58.054  1.00 42.66  ? 305  TYR B CE2 1 
ATOM   6145 C  CZ  . TYR B 1 305 ? 2.003   5.238   59.182  1.00 47.73  ? 305  TYR B CZ  1 
ATOM   6146 O  OH  . TYR B 1 305 ? 2.585   4.757   60.326  1.00 52.20  ? 305  TYR B OH  1 
ATOM   6147 N  N   . LYS B 1 306 ? -2.132  8.525   56.681  1.00 33.97  ? 306  LYS B N   1 
ATOM   6148 C  CA  . LYS B 1 306 ? -2.815  9.225   57.764  1.00 39.63  ? 306  LYS B CA  1 
ATOM   6149 C  C   . LYS B 1 306 ? -4.268  8.795   57.870  1.00 34.13  ? 306  LYS B C   1 
ATOM   6150 O  O   . LYS B 1 306 ? -4.794  8.664   58.974  1.00 35.40  ? 306  LYS B O   1 
ATOM   6151 C  CB  . LYS B 1 306 ? -2.728  10.741  57.569  1.00 45.45  ? 306  LYS B CB  1 
ATOM   6152 C  CG  . LYS B 1 306 ? -1.590  11.398  58.350  1.00 49.86  ? 306  LYS B CG  1 
ATOM   6153 C  CD  . LYS B 1 306 ? -1.217  12.760  57.773  1.00 55.57  ? 306  LYS B CD  1 
ATOM   6154 C  CE  . LYS B 1 306 ? 0.293   12.984  57.796  1.00 60.60  ? 306  LYS B CE  1 
ATOM   6155 N  NZ  . LYS B 1 306 ? 0.654   14.433  57.768  1.00 69.34  ? 306  LYS B NZ  1 
ATOM   6156 N  N   . GLN B 1 307 ? -4.934  8.554   56.735  1.00 35.73  ? 307  GLN B N   1 
ATOM   6157 C  CA  . GLN B 1 307 ? -6.344  8.171   56.810  1.00 35.83  ? 307  GLN B CA  1 
ATOM   6158 C  C   . GLN B 1 307 ? -6.514  6.792   57.437  1.00 34.29  ? 307  GLN B C   1 
ATOM   6159 O  O   . GLN B 1 307 ? -7.442  6.577   58.228  1.00 33.91  ? 307  GLN B O   1 
ATOM   6160 C  CB  . GLN B 1 307 ? -6.988  8.223   55.419  1.00 35.46  ? 307  GLN B CB  1 
ATOM   6161 C  CG  . GLN B 1 307 ? -7.291  9.643   54.945  1.00 36.35  ? 307  GLN B CG  1 
ATOM   6162 C  CD  . GLN B 1 307 ? -7.528  9.720   53.445  1.00 39.42  ? 307  GLN B CD  1 
ATOM   6163 O  OE1 . GLN B 1 307 ? -7.242  8.770   52.709  1.00 38.39  ? 307  GLN B OE1 1 
ATOM   6164 N  NE2 . GLN B 1 307 ? -8.033  10.861  52.983  1.00 41.05  ? 307  GLN B NE2 1 
ATOM   6165 N  N   . VAL B 1 308 ? -5.617  5.846   57.126  1.00 32.48  ? 308  VAL B N   1 
ATOM   6166 C  CA  . VAL B 1 308 ? -5.724  4.525   57.747  1.00 31.77  ? 308  VAL B CA  1 
ATOM   6167 C  C   . VAL B 1 308 ? -5.562  4.645   59.257  1.00 33.76  ? 308  VAL B C   1 
ATOM   6168 O  O   . VAL B 1 308 ? -6.259  3.980   60.032  1.00 34.46  ? 308  VAL B O   1 
ATOM   6169 C  CB  . VAL B 1 308 ? -4.703  3.543   57.139  1.00 32.93  ? 308  VAL B CB  1 
ATOM   6170 C  CG1 . VAL B 1 308 ? -4.736  2.202   57.898  1.00 35.55  ? 308  VAL B CG1 1 
ATOM   6171 C  CG2 . VAL B 1 308 ? -4.983  3.313   55.639  1.00 34.38  ? 308  VAL B CG2 1 
ATOM   6172 N  N   . LYS B 1 309 ? -4.649  5.506   59.700  1.00 33.63  ? 309  LYS B N   1 
ATOM   6173 C  CA  . LYS B 1 309 ? -4.478  5.714   61.131  1.00 35.61  ? 309  LYS B CA  1 
ATOM   6174 C  C   . LYS B 1 309 ? -5.735  6.239   61.810  1.00 36.25  ? 309  LYS B C   1 
ATOM   6175 O  O   . LYS B 1 309 ? -5.879  6.066   63.026  1.00 37.65  ? 309  LYS B O   1 
ATOM   6176 C  CB  . LYS B 1 309 ? -3.317  6.673   61.381  1.00 36.92  ? 309  LYS B CB  1 
ATOM   6177 C  CG  . LYS B 1 309 ? -1.987  6.102   60.916  1.00 40.69  ? 309  LYS B CG  1 
ATOM   6178 C  CD  . LYS B 1 309 ? -1.710  4.800   61.633  1.00 49.62  ? 309  LYS B CD  1 
ATOM   6179 C  CE  . LYS B 1 309 ? -0.281  4.334   61.457  1.00 52.62  ? 309  LYS B CE  1 
ATOM   6180 N  NZ  . LYS B 1 309 ? -0.028  3.112   62.277  1.00 58.94  ? 309  LYS B NZ  1 
ATOM   6181 N  N   . GLN B 1 310 ? -6.632  6.883   61.073  1.00 32.87  ? 310  GLN B N   1 
ATOM   6182 C  CA  . GLN B 1 310 ? -7.864  7.409   61.653  1.00 33.88  ? 310  GLN B CA  1 
ATOM   6183 C  C   . GLN B 1 310 ? -8.982  6.381   61.724  1.00 34.67  ? 310  GLN B C   1 
ATOM   6184 O  O   . GLN B 1 310 ? -10.052 6.707   62.253  1.00 35.99  ? 310  GLN B O   1 
ATOM   6185 C  CB  . GLN B 1 310 ? -8.387  8.613   60.851  1.00 36.41  ? 310  GLN B CB  1 
ATOM   6186 C  CG  . GLN B 1 310 ? -7.588  9.908   60.943  1.00 39.18  ? 310  GLN B CG  1 
ATOM   6187 C  CD  . GLN B 1 310 ? -8.064  10.919  59.897  1.00 41.56  ? 310  GLN B CD  1 
ATOM   6188 O  OE1 . GLN B 1 310 ? -7.867  10.724  58.698  1.00 43.64  ? 310  GLN B OE1 1 
ATOM   6189 N  NE2 . GLN B 1 310 ? -8.696  11.988  60.348  1.00 46.98  ? 310  GLN B NE2 1 
ATOM   6190 N  N   . LEU B 1 311 ? -8.792  5.172   61.191  1.00 32.42  ? 311  LEU B N   1 
ATOM   6191 C  CA  . LEU B 1 311 ? -9.828  4.136   61.234  1.00 33.54  ? 311  LEU B CA  1 
ATOM   6192 C  C   . LEU B 1 311 ? -9.789  3.432   62.595  1.00 35.26  ? 311  LEU B C   1 
ATOM   6193 O  O   . LEU B 1 311 ? -9.467  2.246   62.721  1.00 33.91  ? 311  LEU B O   1 
ATOM   6194 C  CB  . LEU B 1 311 ? -9.646  3.153   60.083  1.00 30.78  ? 311  LEU B CB  1 
ATOM   6195 C  CG  . LEU B 1 311 ? -9.825  3.758   58.693  1.00 34.63  ? 311  LEU B CG  1 
ATOM   6196 C  CD1 . LEU B 1 311 ? -9.402  2.766   57.636  1.00 33.25  ? 311  LEU B CD1 1 
ATOM   6197 C  CD2 . LEU B 1 311 ? -11.278 4.216   58.511  1.00 33.21  ? 311  LEU B CD2 1 
ATOM   6198 N  N   . LYS B 1 312 ? -10.159 4.194   63.633  1.00 34.67  ? 312  LYS B N   1 
ATOM   6199 C  CA  . LYS B 1 312 ? -10.051 3.706   65.006  1.00 34.94  ? 312  LYS B CA  1 
ATOM   6200 C  C   . LYS B 1 312 ? -10.991 2.529   65.258  1.00 32.67  ? 312  LYS B C   1 
ATOM   6201 O  O   . LYS B 1 312 ? -10.598 1.522   65.859  1.00 32.96  ? 312  LYS B O   1 
ATOM   6202 C  CB  . LYS B 1 312 ? -10.338 4.855   65.977  1.00 34.42  ? 312  LYS B CB  1 
ATOM   6203 C  CG  . LYS B 1 312 ? -10.341 4.455   67.447  1.00 44.86  ? 312  LYS B CG  1 
ATOM   6204 C  CD  . LYS B 1 312 ? -11.045 5.506   68.300  1.00 53.78  ? 312  LYS B CD  1 
ATOM   6205 C  CE  . LYS B 1 312 ? -10.354 5.693   69.662  1.00 55.56  ? 312  LYS B CE  1 
ATOM   6206 N  NZ  . LYS B 1 312 ? -10.247 4.449   70.469  1.00 49.21  ? 312  LYS B NZ  1 
ATOM   6207 N  N   . TYR B 1 313 ? -12.249 2.648   64.828  1.00 30.42  ? 313  TYR B N   1 
ATOM   6208 C  CA  . TYR B 1 313 ? -13.206 1.577   65.082  1.00 31.30  ? 313  TYR B CA  1 
ATOM   6209 C  C   . TYR B 1 313 ? -12.912 0.354   64.225  1.00 32.94  ? 313  TYR B C   1 
ATOM   6210 O  O   . TYR B 1 313 ? -13.137 -0.778  64.663  1.00 32.90  ? 313  TYR B O   1 
ATOM   6211 C  CB  . TYR B 1 313 ? -14.638 2.071   64.849  1.00 33.11  ? 313  TYR B CB  1 
ATOM   6212 C  CG  . TYR B 1 313 ? -15.694 1.104   65.363  1.00 32.88  ? 313  TYR B CG  1 
ATOM   6213 C  CD1 . TYR B 1 313 ? -16.134 1.157   66.680  1.00 33.62  ? 313  TYR B CD1 1 
ATOM   6214 C  CD2 . TYR B 1 313 ? -16.252 0.138   64.524  1.00 32.14  ? 313  TYR B CD2 1 
ATOM   6215 C  CE1 . TYR B 1 313 ? -17.086 0.273   67.149  1.00 33.94  ? 313  TYR B CE1 1 
ATOM   6216 C  CE2 . TYR B 1 313 ? -17.219 -0.756  64.994  1.00 32.70  ? 313  TYR B CE2 1 
ATOM   6217 C  CZ  . TYR B 1 313 ? -17.631 -0.672  66.303  1.00 33.87  ? 313  TYR B CZ  1 
ATOM   6218 O  OH  . TYR B 1 313 ? -18.576 -1.552  66.773  1.00 33.94  ? 313  TYR B OH  1 
ATOM   6219 N  N   . VAL B 1 314 ? -12.449 0.554   62.986  1.00 30.35  ? 314  VAL B N   1 
ATOM   6220 C  CA  . VAL B 1 314 ? -11.989 -0.591  62.208  1.00 30.64  ? 314  VAL B CA  1 
ATOM   6221 C  C   . VAL B 1 314 ? -10.882 -1.308  62.973  1.00 31.80  ? 314  VAL B C   1 
ATOM   6222 O  O   . VAL B 1 314 ? -10.877 -2.539  63.086  1.00 30.91  ? 314  VAL B O   1 
ATOM   6223 C  CB  . VAL B 1 314 ? -11.531 -0.151  60.802  1.00 33.87  ? 314  VAL B CB  1 
ATOM   6224 C  CG1 . VAL B 1 314 ? -10.982 -1.339  60.036  1.00 31.21  ? 314  VAL B CG1 1 
ATOM   6225 C  CG2 . VAL B 1 314 ? -12.696 0.473   60.008  1.00 32.06  ? 314  VAL B CG2 1 
ATOM   6226 N  N   . GLY B 1 315 ? -9.949  -0.541  63.546  1.00 33.05  ? 315  GLY B N   1 
ATOM   6227 C  CA  . GLY B 1 315 ? -8.916  -1.141  64.384  1.00 33.11  ? 315  GLY B CA  1 
ATOM   6228 C  C   . GLY B 1 315 ? -9.477  -1.905  65.576  1.00 33.04  ? 315  GLY B C   1 
ATOM   6229 O  O   . GLY B 1 315 ? -8.958  -2.963  65.952  1.00 32.57  ? 315  GLY B O   1 
ATOM   6230 N  N   . MET B 1 316 ? -10.524 -1.373  66.208  1.00 32.32  ? 316  MET B N   1 
ATOM   6231 C  CA  . MET B 1 316 ? -11.138 -2.113  67.309  1.00 33.13  ? 316  MET B CA  1 
ATOM   6232 C  C   . MET B 1 316 ? -11.807 -3.399  66.831  1.00 31.05  ? 316  MET B C   1 
ATOM   6233 O  O   . MET B 1 316 ? -11.795 -4.409  67.542  1.00 32.07  ? 316  MET B O   1 
ATOM   6234 C  CB  . MET B 1 316 ? -12.133 -1.226  68.065  1.00 33.97  ? 316  MET B CB  1 
ATOM   6235 C  CG  . MET B 1 316 ? -11.535 0.093   68.592  1.00 33.40  ? 316  MET B CG  1 
ATOM   6236 S  SD  . MET B 1 316 ? -12.742 1.408   68.962  1.00 40.01  ? 316  MET B SD  1 
ATOM   6237 C  CE  . MET B 1 316 ? -14.062 0.535   69.753  1.00 40.46  ? 316  MET B CE  1 
ATOM   6238 N  N   . VAL B 1 317 ? -12.431 -3.373  65.654  1.00 30.58  ? 317  VAL B N   1 
ATOM   6239 C  CA  . VAL B 1 317 ? -12.972 -4.604  65.082  1.00 29.38  ? 317  VAL B CA  1 
ATOM   6240 C  C   . VAL B 1 317 ? -11.871 -5.657  64.966  1.00 32.38  ? 317  VAL B C   1 
ATOM   6241 O  O   . VAL B 1 317 ? -12.052 -6.814  65.356  1.00 31.22  ? 317  VAL B O   1 
ATOM   6242 C  CB  . VAL B 1 317 ? -13.622 -4.327  63.713  1.00 30.66  ? 317  VAL B CB  1 
ATOM   6243 C  CG1 . VAL B 1 317 ? -13.878 -5.658  62.992  1.00 31.03  ? 317  VAL B CG1 1 
ATOM   6244 C  CG2 . VAL B 1 317 ? -14.934 -3.512  63.877  1.00 29.91  ? 317  VAL B CG2 1 
ATOM   6245 N  N   . LEU B 1 318 ? -10.713 -5.269  64.413  1.00 31.19  ? 318  LEU B N   1 
ATOM   6246 C  CA  . LEU B 1 318 ? -9.626  -6.229  64.223  1.00 33.32  ? 318  LEU B CA  1 
ATOM   6247 C  C   . LEU B 1 318 ? -9.102  -6.759  65.557  1.00 33.38  ? 318  LEU B C   1 
ATOM   6248 O  O   . LEU B 1 318 ? -8.847  -7.964  65.699  1.00 32.39  ? 318  LEU B O   1 
ATOM   6249 C  CB  . LEU B 1 318 ? -8.504  -5.583  63.414  1.00 31.15  ? 318  LEU B CB  1 
ATOM   6250 C  CG  . LEU B 1 318 ? -8.921  -5.281  61.963  1.00 32.82  ? 318  LEU B CG  1 
ATOM   6251 C  CD1 . LEU B 1 318 ? -7.946  -4.269  61.375  1.00 33.28  ? 318  LEU B CD1 1 
ATOM   6252 C  CD2 . LEU B 1 318 ? -8.943  -6.551  61.109  1.00 30.68  ? 318  LEU B CD2 1 
ATOM   6253 N  N   . ASN B 1 319 ? -8.967  -5.886  66.559  1.00 31.33  ? 319  ASN B N   1 
ATOM   6254 C  CA  . ASN B 1 319 ? -8.517  -6.356  67.864  1.00 30.74  ? 319  ASN B CA  1 
ATOM   6255 C  C   . ASN B 1 319 ? -9.528  -7.307  68.496  1.00 31.26  ? 319  ASN B C   1 
ATOM   6256 O  O   . ASN B 1 319 ? -9.148  -8.305  69.118  1.00 30.70  ? 319  ASN B O   1 
ATOM   6257 C  CB  . ASN B 1 319 ? -8.232  -5.167  68.782  1.00 33.06  ? 319  ASN B CB  1 
ATOM   6258 C  CG  . ASN B 1 319 ? -6.842  -4.616  68.568  1.00 40.26  ? 319  ASN B CG  1 
ATOM   6259 O  OD1 . ASN B 1 319 ? -5.931  -5.366  68.219  1.00 36.93  ? 319  ASN B OD1 1 
ATOM   6260 N  ND2 . ASN B 1 319 ? -6.673  -3.309  68.742  1.00 42.49  ? 319  ASN B ND2 1 
ATOM   6261 N  N   . GLU B 1 320 ? -10.826 -7.026  68.329  1.00 31.39  ? 320  GLU B N   1 
ATOM   6262 C  CA  . GLU B 1 320 ? -11.834 -7.932  68.871  1.00 32.51  ? 320  GLU B CA  1 
ATOM   6263 C  C   . GLU B 1 320 ? -11.839 -9.268  68.129  1.00 29.91  ? 320  GLU B C   1 
ATOM   6264 O  O   . GLU B 1 320 ? -12.110 -10.316 68.738  1.00 30.90  ? 320  GLU B O   1 
ATOM   6265 C  CB  . GLU B 1 320 ? -13.216 -7.258  68.826  1.00 31.32  ? 320  GLU B CB  1 
ATOM   6266 C  CG  . GLU B 1 320 ? -14.379 -8.099  69.364  1.00 31.82  ? 320  GLU B CG  1 
ATOM   6267 C  CD  . GLU B 1 320 ? -14.360 -8.295  70.888  1.00 36.21  ? 320  GLU B CD  1 
ATOM   6268 O  OE1 . GLU B 1 320 ? -13.302 -8.107  71.515  1.00 31.96  ? 320  GLU B OE1 1 
ATOM   6269 O  OE2 . GLU B 1 320 ? -15.420 -8.644  71.461  1.00 32.73  ? 320  GLU B OE2 1 
ATOM   6270 N  N   . ALA B 1 321 ? -11.540 -9.266  66.825  1.00 31.80  ? 321  ALA B N   1 
ATOM   6271 C  CA  . ALA B 1 321 ? -11.401 -10.534 66.110  1.00 31.10  ? 321  ALA B CA  1 
ATOM   6272 C  C   . ALA B 1 321 ? -10.159 -11.293 66.574  1.00 31.84  ? 321  ALA B C   1 
ATOM   6273 O  O   . ALA B 1 321 ? -10.195 -12.520 66.718  1.00 30.74  ? 321  ALA B O   1 
ATOM   6274 C  CB  . ALA B 1 321 ? -11.365 -10.300 64.593  1.00 30.66  ? 321  ALA B CB  1 
ATOM   6275 N  N   . LEU B 1 322 ? -9.063  -10.577 66.837  1.00 31.63  ? 322  LEU B N   1 
ATOM   6276 C  CA  . LEU B 1 322 ? -7.894  -11.196 67.459  1.00 32.30  ? 322  LEU B CA  1 
ATOM   6277 C  C   . LEU B 1 322 ? -8.185  -11.683 68.877  1.00 32.73  ? 322  LEU B C   1 
ATOM   6278 O  O   . LEU B 1 322 ? -7.580  -12.669 69.325  1.00 33.32  ? 322  LEU B O   1 
ATOM   6279 C  CB  . LEU B 1 322 ? -6.728  -10.209 67.484  1.00 31.47  ? 322  LEU B CB  1 
ATOM   6280 C  CG  . LEU B 1 322 ? -6.025  -9.966  66.142  1.00 33.91  ? 322  LEU B CG  1 
ATOM   6281 C  CD1 . LEU B 1 322 ? -4.898  -8.968  66.353  1.00 33.96  ? 322  LEU B CD1 1 
ATOM   6282 C  CD2 . LEU B 1 322 ? -5.484  -11.290 65.586  1.00 31.90  ? 322  LEU B CD2 1 
ATOM   6283 N  N   . ARG B 1 323 ? -9.085  -11.020 69.609  1.00 30.60  ? 323  ARG B N   1 
ATOM   6284 C  CA  . ARG B 1 323 ? -9.423  -11.522 70.939  1.00 30.00  ? 323  ARG B CA  1 
ATOM   6285 C  C   . ARG B 1 323 ? -10.062 -12.896 70.825  1.00 31.57  ? 323  ARG B C   1 
ATOM   6286 O  O   . ARG B 1 323 ? -9.623  -13.854 71.459  1.00 31.07  ? 323  ARG B O   1 
ATOM   6287 C  CB  . ARG B 1 323 ? -10.367 -10.554 71.684  1.00 30.86  ? 323  ARG B CB  1 
ATOM   6288 C  CG  . ARG B 1 323 ? -10.519 -10.924 73.189  1.00 31.28  ? 323  ARG B CG  1 
ATOM   6289 C  CD  . ARG B 1 323 ? -11.532 -10.032 73.940  1.00 31.00  ? 323  ARG B CD  1 
ATOM   6290 N  NE  . ARG B 1 323 ? -12.864 -10.132 73.351  1.00 32.29  ? 323  ARG B NE  1 
ATOM   6291 C  CZ  . ARG B 1 323 ? -13.712 -11.128 73.579  1.00 34.53  ? 323  ARG B CZ  1 
ATOM   6292 N  NH1 . ARG B 1 323 ? -13.419 -12.112 74.419  1.00 34.41  ? 323  ARG B NH1 1 
ATOM   6293 N  NH2 . ARG B 1 323 ? -14.886 -11.135 72.958  1.00 32.65  ? 323  ARG B NH2 1 
ATOM   6294 N  N   . LEU B 1 324 ? -11.095 -13.014 69.999  1.00 32.82  ? 324  LEU B N   1 
ATOM   6295 C  CA  . LEU B 1 324 ? -11.830 -14.270 69.964  1.00 31.85  ? 324  LEU B CA  1 
ATOM   6296 C  C   . LEU B 1 324 ? -11.051 -15.365 69.249  1.00 30.78  ? 324  LEU B C   1 
ATOM   6297 O  O   . LEU B 1 324 ? -11.026 -16.508 69.714  1.00 32.14  ? 324  LEU B O   1 
ATOM   6298 C  CB  . LEU B 1 324 ? -13.202 -14.054 69.336  1.00 31.98  ? 324  LEU B CB  1 
ATOM   6299 C  CG  . LEU B 1 324 ? -14.194 -13.394 70.306  1.00 32.19  ? 324  LEU B CG  1 
ATOM   6300 C  CD1 . LEU B 1 324 ? -15.444 -12.922 69.548  1.00 35.50  ? 324  LEU B CD1 1 
ATOM   6301 C  CD2 . LEU B 1 324 ? -14.606 -14.335 71.460  1.00 34.40  ? 324  LEU B CD2 1 
ATOM   6302 N  N   . TRP B 1 325 ? -10.384 -15.055 68.136  1.00 32.28  ? 325  TRP B N   1 
ATOM   6303 C  CA  . TRP B 1 325 ? -9.691  -16.082 67.354  1.00 30.41  ? 325  TRP B CA  1 
ATOM   6304 C  C   . TRP B 1 325 ? -8.295  -15.609 66.973  1.00 30.39  ? 325  TRP B C   1 
ATOM   6305 O  O   . TRP B 1 325 ? -8.007  -15.344 65.799  1.00 33.35  ? 325  TRP B O   1 
ATOM   6306 C  CB  . TRP B 1 325 ? -10.516 -16.486 66.127  1.00 30.22  ? 325  TRP B CB  1 
ATOM   6307 C  CG  . TRP B 1 325 ? -11.707 -17.258 66.601  1.00 30.74  ? 325  TRP B CG  1 
ATOM   6308 C  CD1 . TRP B 1 325 ? -13.016 -16.855 66.583  1.00 34.91  ? 325  TRP B CD1 1 
ATOM   6309 C  CD2 . TRP B 1 325 ? -11.684 -18.529 67.269  1.00 31.00  ? 325  TRP B CD2 1 
ATOM   6310 N  NE1 . TRP B 1 325 ? -13.811 -17.817 67.177  1.00 32.02  ? 325  TRP B NE1 1 
ATOM   6311 C  CE2 . TRP B 1 325 ? -13.019 -18.856 67.599  1.00 33.61  ? 325  TRP B CE2 1 
ATOM   6312 C  CE3 . TRP B 1 325 ? -10.665 -19.430 67.608  1.00 30.85  ? 325  TRP B CE3 1 
ATOM   6313 C  CZ2 . TRP B 1 325 ? -13.357 -20.047 68.245  1.00 36.60  ? 325  TRP B CZ2 1 
ATOM   6314 C  CZ3 . TRP B 1 325 ? -10.998 -20.615 68.244  1.00 32.77  ? 325  TRP B CZ3 1 
ATOM   6315 C  CH2 . TRP B 1 325 ? -12.334 -20.913 68.560  1.00 34.50  ? 325  TRP B CH2 1 
ATOM   6316 N  N   . PRO B 1 326 ? -7.387  -15.539 67.944  1.00 29.94  ? 326  PRO B N   1 
ATOM   6317 C  CA  . PRO B 1 326 ? -5.999  -15.179 67.616  1.00 28.67  ? 326  PRO B CA  1 
ATOM   6318 C  C   . PRO B 1 326 ? -5.416  -16.237 66.683  1.00 30.37  ? 326  PRO B C   1 
ATOM   6319 O  O   . PRO B 1 326 ? -5.467  -17.437 66.966  1.00 31.87  ? 326  PRO B O   1 
ATOM   6320 C  CB  . PRO B 1 326 ? -5.308  -15.168 68.987  1.00 31.06  ? 326  PRO B CB  1 
ATOM   6321 C  CG  . PRO B 1 326 ? -6.114  -16.148 69.825  1.00 30.03  ? 326  PRO B CG  1 
ATOM   6322 C  CD  . PRO B 1 326 ? -7.546  -15.926 69.361  1.00 29.96  ? 326  PRO B CD  1 
ATOM   6323 N  N   . THR B 1 327 ? -4.886  -15.791 65.543  1.00 29.73  ? 327  THR B N   1 
ATOM   6324 C  CA  . THR B 1 327 ? -4.669  -16.713 64.434  1.00 30.41  ? 327  THR B CA  1 
ATOM   6325 C  C   . THR B 1 327 ? -3.353  -17.474 64.545  1.00 32.02  ? 327  THR B C   1 
ATOM   6326 O  O   . THR B 1 327 ? -3.163  -18.458 63.817  1.00 30.86  ? 327  THR B O   1 
ATOM   6327 C  CB  . THR B 1 327 ? -4.755  -15.968 63.099  1.00 29.91  ? 327  THR B CB  1 
ATOM   6328 O  OG1 . THR B 1 327 ? -3.968  -14.773 63.156  1.00 31.93  ? 327  THR B OG1 1 
ATOM   6329 C  CG2 . THR B 1 327 ? -6.222  -15.565 62.788  1.00 29.11  ? 327  THR B CG2 1 
ATOM   6330 N  N   . ALA B 1 328 ? -2.456  -17.054 65.442  1.00 30.11  ? 328  ALA B N   1 
ATOM   6331 C  CA  . ALA B 1 328 ? -1.351  -17.894 65.898  1.00 31.94  ? 328  ALA B CA  1 
ATOM   6332 C  C   . ALA B 1 328 ? -1.691  -18.223 67.344  1.00 27.33  ? 328  ALA B C   1 
ATOM   6333 O  O   . ALA B 1 328 ? -1.345  -17.461 68.256  1.00 31.92  ? 328  ALA B O   1 
ATOM   6334 C  CB  . ALA B 1 328 ? -0.003  -17.176 65.790  1.00 31.00  ? 328  ALA B CB  1 
ATOM   6335 N  N   . PRO B 1 329 ? -2.408  -19.321 67.606  1.00 30.19  ? 329  PRO B N   1 
ATOM   6336 C  CA  . PRO B 1 329 ? -3.223  -19.404 68.830  1.00 33.33  ? 329  PRO B CA  1 
ATOM   6337 C  C   . PRO B 1 329 ? -2.494  -19.858 70.085  1.00 31.85  ? 329  PRO B C   1 
ATOM   6338 O  O   . PRO B 1 329 ? -3.123  -19.949 71.148  1.00 31.51  ? 329  PRO B O   1 
ATOM   6339 C  CB  . PRO B 1 329 ? -4.317  -20.410 68.436  1.00 33.19  ? 329  PRO B CB  1 
ATOM   6340 C  CG  . PRO B 1 329 ? -3.688  -21.276 67.420  1.00 33.01  ? 329  PRO B CG  1 
ATOM   6341 C  CD  . PRO B 1 329 ? -2.763  -20.364 66.628  1.00 32.72  ? 329  PRO B CD  1 
ATOM   6342 N  N   . ALA B 1 330 ? -1.191  -20.087 70.042  1.00 29.20  ? 330  ALA B N   1 
ATOM   6343 C  CA  . ALA B 1 330 ? -0.507  -20.459 71.270  1.00 30.68  ? 330  ALA B CA  1 
ATOM   6344 C  C   . ALA B 1 330 ? 0.945   -20.084 71.106  1.00 30.40  ? 330  ALA B C   1 
ATOM   6345 O  O   . ALA B 1 330 ? 1.440   -19.930 69.982  1.00 32.20  ? 330  ALA B O   1 
ATOM   6346 C  CB  . ALA B 1 330 ? -0.638  -21.957 71.562  1.00 32.51  ? 330  ALA B CB  1 
ATOM   6347 N  N   . PHE B 1 331 ? 1.615   -19.938 72.240  1.00 30.77  ? 331  PHE B N   1 
ATOM   6348 C  CA  . PHE B 1 331 ? 3.065   -19.902 72.254  1.00 31.45  ? 331  PHE B CA  1 
ATOM   6349 C  C   . PHE B 1 331 ? 3.540   -20.645 73.490  1.00 33.36  ? 331  PHE B C   1 
ATOM   6350 O  O   . PHE B 1 331 ? 2.775   -20.897 74.431  1.00 33.79  ? 331  PHE B O   1 
ATOM   6351 C  CB  . PHE B 1 331 ? 3.637   -18.469 72.193  1.00 30.74  ? 331  PHE B CB  1 
ATOM   6352 C  CG  . PHE B 1 331 ? 3.118   -17.516 73.250  1.00 32.04  ? 331  PHE B CG  1 
ATOM   6353 C  CD1 . PHE B 1 331 ? 1.939   -16.793 73.058  1.00 33.47  ? 331  PHE B CD1 1 
ATOM   6354 C  CD2 . PHE B 1 331 ? 3.855   -17.274 74.392  1.00 36.01  ? 331  PHE B CD2 1 
ATOM   6355 C  CE1 . PHE B 1 331 ? 1.484   -15.896 74.025  1.00 34.24  ? 331  PHE B CE1 1 
ATOM   6356 C  CE2 . PHE B 1 331 ? 3.410   -16.378 75.365  1.00 36.26  ? 331  PHE B CE2 1 
ATOM   6357 C  CZ  . PHE B 1 331 ? 2.223   -15.692 75.184  1.00 34.29  ? 331  PHE B CZ  1 
ATOM   6358 N  N   . SER B 1 332 ? 4.822   -20.991 73.477  1.00 32.87  ? 332  SER B N   1 
ATOM   6359 C  CA  . SER B 1 332 ? 5.395   -21.880 74.470  1.00 32.31  ? 332  SER B CA  1 
ATOM   6360 C  C   . SER B 1 332 ? 6.538   -21.193 75.204  1.00 31.57  ? 332  SER B C   1 
ATOM   6361 O  O   . SER B 1 332 ? 7.266   -20.389 74.620  1.00 31.87  ? 332  SER B O   1 
ATOM   6362 C  CB  . SER B 1 332 ? 5.886   -23.159 73.782  1.00 32.13  ? 332  SER B CB  1 
ATOM   6363 O  OG  . SER B 1 332 ? 6.234   -24.113 74.747  1.00 33.12  ? 332  SER B OG  1 
ATOM   6364 N  N   . LEU B 1 333 ? 6.694   -21.538 76.487  1.00 32.27  ? 333  LEU B N   1 
ATOM   6365 C  CA  . LEU B 1 333 ? 7.719   -20.996 77.374  1.00 33.07  ? 333  LEU B CA  1 
ATOM   6366 C  C   . LEU B 1 333 ? 8.391   -22.132 78.137  1.00 34.46  ? 333  LEU B C   1 
ATOM   6367 O  O   . LEU B 1 333 ? 7.817   -23.210 78.312  1.00 36.21  ? 333  LEU B O   1 
ATOM   6368 C  CB  . LEU B 1 333 ? 7.108   -19.998 78.364  1.00 36.07  ? 333  LEU B CB  1 
ATOM   6369 C  CG  . LEU B 1 333 ? 6.320   -18.902 77.650  1.00 37.74  ? 333  LEU B CG  1 
ATOM   6370 C  CD1 . LEU B 1 333 ? 5.193   -18.380 78.531  1.00 39.12  ? 333  LEU B CD1 1 
ATOM   6371 C  CD2 . LEU B 1 333 ? 7.255   -17.789 77.182  1.00 34.41  ? 333  LEU B CD2 1 
ATOM   6372 N  N   . TYR B 1 334 ? 9.626   -21.891 78.594  1.00 33.22  ? 334  TYR B N   1 
ATOM   6373 C  CA  . TYR B 1 334 ? 10.284  -22.802 79.526  1.00 33.70  ? 334  TYR B CA  1 
ATOM   6374 C  C   . TYR B 1 334 ? 10.809  -22.017 80.725  1.00 33.01  ? 334  TYR B C   1 
ATOM   6375 O  O   . TYR B 1 334 ? 11.158  -20.835 80.621  1.00 32.76  ? 334  TYR B O   1 
ATOM   6376 C  CB  . TYR B 1 334 ? 11.444  -23.611 78.873  1.00 36.83  ? 334  TYR B CB  1 
ATOM   6377 C  CG  . TYR B 1 334 ? 12.640  -22.764 78.524  1.00 34.89  ? 334  TYR B CG  1 
ATOM   6378 C  CD1 . TYR B 1 334 ? 12.730  -22.136 77.287  1.00 34.19  ? 334  TYR B CD1 1 
ATOM   6379 C  CD2 . TYR B 1 334 ? 13.683  -22.581 79.436  1.00 34.86  ? 334  TYR B CD2 1 
ATOM   6380 C  CE1 . TYR B 1 334 ? 13.819  -21.341 76.958  1.00 33.24  ? 334  TYR B CE1 1 
ATOM   6381 C  CE2 . TYR B 1 334 ? 14.768  -21.791 79.123  1.00 36.59  ? 334  TYR B CE2 1 
ATOM   6382 C  CZ  . TYR B 1 334 ? 14.831  -21.173 77.879  1.00 38.59  ? 334  TYR B CZ  1 
ATOM   6383 O  OH  . TYR B 1 334 ? 15.905  -20.383 77.559  1.00 39.87  ? 334  TYR B OH  1 
ATOM   6384 N  N   . ALA B 1 335 ? 10.838  -22.688 81.873  1.00 34.16  ? 335  ALA B N   1 
ATOM   6385 C  CA  . ALA B 1 335 ? 11.289  -22.059 83.110  1.00 34.31  ? 335  ALA B CA  1 
ATOM   6386 C  C   . ALA B 1 335 ? 12.807  -21.915 83.091  1.00 33.61  ? 335  ALA B C   1 
ATOM   6387 O  O   . ALA B 1 335 ? 13.517  -22.909 82.928  1.00 35.38  ? 335  ALA B O   1 
ATOM   6388 C  CB  . ALA B 1 335 ? 10.847  -22.891 84.312  1.00 35.38  ? 335  ALA B CB  1 
ATOM   6389 N  N   . LYS B 1 336 ? 13.299  -20.681 83.257  1.00 34.63  ? 336  LYS B N   1 
ATOM   6390 C  CA  . LYS B 1 336 ? 14.744  -20.442 83.268  1.00 39.68  ? 336  LYS B CA  1 
ATOM   6391 C  C   . LYS B 1 336 ? 15.413  -21.046 84.502  1.00 40.85  ? 336  LYS B C   1 
ATOM   6392 O  O   . LYS B 1 336 ? 16.575  -21.470 84.441  1.00 38.25  ? 336  LYS B O   1 
ATOM   6393 C  CB  . LYS B 1 336 ? 15.014  -18.937 83.201  1.00 37.06  ? 336  LYS B CB  1 
ATOM   6394 C  CG  . LYS B 1 336 ? 14.697  -18.324 81.825  1.00 38.71  ? 336  LYS B CG  1 
ATOM   6395 C  CD  . LYS B 1 336 ? 14.533  -16.810 81.897  1.00 41.46  ? 336  LYS B CD  1 
ATOM   6396 C  CE  . LYS B 1 336 ? 15.815  -16.107 82.361  1.00 43.62  ? 336  LYS B CE  1 
ATOM   6397 N  NZ  . LYS B 1 336 ? 16.929  -16.252 81.384  1.00 44.23  ? 336  LYS B NZ  1 
ATOM   6398 N  N   . GLU B 1 337 ? 14.705  -21.067 85.625  1.00 38.25  ? 337  GLU B N   1 
ATOM   6399 C  CA  . GLU B 1 337 ? 15.186  -21.661 86.866  1.00 41.15  ? 337  GLU B CA  1 
ATOM   6400 C  C   . GLU B 1 337 ? 13.991  -22.277 87.576  1.00 40.29  ? 337  GLU B C   1 
ATOM   6401 O  O   . GLU B 1 337 ? 12.841  -22.039 87.205  1.00 38.61  ? 337  GLU B O   1 
ATOM   6402 C  CB  . GLU B 1 337 ? 15.867  -20.620 87.774  1.00 40.05  ? 337  GLU B CB  1 
ATOM   6403 C  CG  . GLU B 1 337 ? 17.067  -19.884 87.165  1.00 41.77  ? 337  GLU B CG  1 
ATOM   6404 C  CD  . GLU B 1 337 ? 18.283  -20.767 86.887  1.00 45.91  ? 337  GLU B CD  1 
ATOM   6405 O  OE1 . GLU B 1 337 ? 18.347  -21.917 87.371  1.00 43.92  ? 337  GLU B OE1 1 
ATOM   6406 O  OE2 . GLU B 1 337 ? 19.189  -20.302 86.164  1.00 48.54  ? 337  GLU B OE2 1 
ATOM   6407 N  N   . ASP B 1 338 ? 14.261  -23.074 88.611  1.00 39.67  ? 338  ASP B N   1 
ATOM   6408 C  CA  . ASP B 1 338 ? 13.178  -23.521 89.480  1.00 41.39  ? 338  ASP B CA  1 
ATOM   6409 C  C   . ASP B 1 338 ? 12.365  -22.312 89.925  1.00 41.44  ? 338  ASP B C   1 
ATOM   6410 O  O   . ASP B 1 338 ? 12.922  -21.268 90.268  1.00 42.86  ? 338  ASP B O   1 
ATOM   6411 C  CB  . ASP B 1 338 ? 13.713  -24.244 90.724  1.00 38.79  ? 338  ASP B CB  1 
ATOM   6412 C  CG  . ASP B 1 338 ? 14.479  -25.522 90.415  1.00 42.14  ? 338  ASP B CG  1 
ATOM   6413 O  OD1 . ASP B 1 338 ? 14.442  -26.057 89.290  1.00 40.26  ? 338  ASP B OD1 1 
ATOM   6414 O  OD2 . ASP B 1 338 ? 15.149  -26.010 91.350  1.00 49.13  ? 338  ASP B OD2 1 
ATOM   6415 N  N   . THR B 1 339 ? 11.038  -22.451 89.927  1.00 39.52  ? 339  THR B N   1 
ATOM   6416 C  CA  . THR B 1 339 ? 10.177  -21.342 90.321  1.00 40.56  ? 339  THR B CA  1 
ATOM   6417 C  C   . THR B 1 339 ? 8.782   -21.888 90.600  1.00 41.46  ? 339  THR B C   1 
ATOM   6418 O  O   . THR B 1 339 ? 8.429   -22.981 90.152  1.00 44.37  ? 339  THR B O   1 
ATOM   6419 C  CB  . THR B 1 339 ? 10.135  -20.256 89.237  1.00 40.02  ? 339  THR B CB  1 
ATOM   6420 O  OG1 . THR B 1 339 ? 9.587   -19.047 89.771  1.00 42.13  ? 339  THR B OG1 1 
ATOM   6421 C  CG2 . THR B 1 339 ? 9.282   -20.713 88.050  1.00 40.00  ? 339  THR B CG2 1 
ATOM   6422 N  N   . VAL B 1 340 ? 7.990   -21.125 91.347  1.00 40.68  ? 340  VAL B N   1 
ATOM   6423 C  CA  . VAL B 1 340 ? 6.642   -21.550 91.715  1.00 40.65  ? 340  VAL B CA  1 
ATOM   6424 C  C   . VAL B 1 340 ? 5.635   -20.698 90.960  1.00 39.29  ? 340  VAL B C   1 
ATOM   6425 O  O   . VAL B 1 340 ? 5.599   -19.471 91.121  1.00 42.67  ? 340  VAL B O   1 
ATOM   6426 C  CB  . VAL B 1 340 ? 6.394   -21.465 93.227  1.00 43.87  ? 340  VAL B CB  1 
ATOM   6427 C  CG1 . VAL B 1 340 ? 4.959   -21.889 93.516  1.00 42.91  ? 340  VAL B CG1 1 
ATOM   6428 C  CG2 . VAL B 1 340 ? 7.367   -22.356 93.957  1.00 41.66  ? 340  VAL B CG2 1 
ATOM   6429 N  N   . LEU B 1 341 ? 4.788   -21.356 90.173  1.00 40.72  ? 341  LEU B N   1 
ATOM   6430 C  CA  . LEU B 1 341 ? 3.793   -20.671 89.361  1.00 41.99  ? 341  LEU B CA  1 
ATOM   6431 C  C   . LEU B 1 341 ? 2.538   -20.420 90.193  1.00 42.61  ? 341  LEU B C   1 
ATOM   6432 O  O   . LEU B 1 341 ? 1.936   -21.361 90.727  1.00 41.15  ? 341  LEU B O   1 
ATOM   6433 C  CB  . LEU B 1 341 ? 3.472   -21.492 88.111  1.00 37.41  ? 341  LEU B CB  1 
ATOM   6434 C  CG  . LEU B 1 341 ? 2.696   -20.747 87.037  1.00 40.25  ? 341  LEU B CG  1 
ATOM   6435 C  CD1 . LEU B 1 341 ? 3.525   -19.591 86.458  1.00 38.11  ? 341  LEU B CD1 1 
ATOM   6436 C  CD2 . LEU B 1 341 ? 2.305   -21.738 85.957  1.00 39.85  ? 341  LEU B CD2 1 
ATOM   6437 N  N   . GLY B 1 342 ? 2.150   -19.152 90.299  1.00 40.82  ? 342  GLY B N   1 
ATOM   6438 C  CA  . GLY B 1 342 ? 0.903   -18.790 90.953  1.00 43.01  ? 342  GLY B CA  1 
ATOM   6439 C  C   . GLY B 1 342 ? 0.816   -19.170 92.411  1.00 47.86  ? 342  GLY B C   1 
ATOM   6440 O  O   . GLY B 1 342 ? -0.288  -19.386 92.919  1.00 42.49  ? 342  GLY B O   1 
ATOM   6441 N  N   . GLY B 1 343 ? 1.952   -19.260 93.101  1.00 43.65  ? 343  GLY B N   1 
ATOM   6442 C  CA  . GLY B 1 343 ? 1.965   -19.678 94.492  1.00 44.21  ? 343  GLY B CA  1 
ATOM   6443 C  C   . GLY B 1 343 ? 1.508   -21.094 94.747  1.00 46.66  ? 343  GLY B C   1 
ATOM   6444 O  O   . GLY B 1 343 ? 1.372   -21.482 95.911  1.00 48.87  ? 343  GLY B O   1 
ATOM   6445 N  N   . GLU B 1 344 ? 1.285   -21.894 93.702  1.00 43.98  ? 344  GLU B N   1 
ATOM   6446 C  CA  . GLU B 1 344 ? 0.671   -23.207 93.876  1.00 46.49  ? 344  GLU B CA  1 
ATOM   6447 C  C   . GLU B 1 344 ? 1.326   -24.336 93.088  1.00 46.45  ? 344  GLU B C   1 
ATOM   6448 O  O   . GLU B 1 344 ? 1.219   -25.491 93.516  1.00 44.91  ? 344  GLU B O   1 
ATOM   6449 C  CB  . GLU B 1 344 ? -0.814  -23.128 93.495  1.00 48.67  ? 344  GLU B CB  1 
ATOM   6450 C  CG  . GLU B 1 344 ? -1.593  -22.158 94.369  1.00 53.71  ? 344  GLU B CG  1 
ATOM   6451 C  CD  . GLU B 1 344 ? -2.976  -21.844 93.832  1.00 58.63  ? 344  GLU B CD  1 
ATOM   6452 O  OE1 . GLU B 1 344 ? -3.234  -22.101 92.637  1.00 52.67  ? 344  GLU B OE1 1 
ATOM   6453 O  OE2 . GLU B 1 344 ? -3.804  -21.322 94.608  1.00 64.27  ? 344  GLU B OE2 1 
ATOM   6454 N  N   . TYR B 1 345 ? 1.983   -24.063 91.961  1.00 41.02  ? 345  TYR B N   1 
ATOM   6455 C  CA  . TYR B 1 345 ? 2.483   -25.105 91.063  1.00 40.33  ? 345  TYR B CA  1 
ATOM   6456 C  C   . TYR B 1 345 ? 3.998   -25.002 90.929  1.00 43.23  ? 345  TYR B C   1 
ATOM   6457 O  O   . TYR B 1 345 ? 4.504   -24.172 90.149  1.00 40.63  ? 345  TYR B O   1 
ATOM   6458 C  CB  . TYR B 1 345 ? 1.806   -24.986 89.699  1.00 42.43  ? 345  TYR B CB  1 
ATOM   6459 C  CG  . TYR B 1 345 ? 0.296   -25.038 89.806  1.00 35.53  ? 345  TYR B CG  1 
ATOM   6460 C  CD1 . TYR B 1 345 ? -0.356  -26.244 90.017  1.00 41.10  ? 345  TYR B CD1 1 
ATOM   6461 C  CD2 . TYR B 1 345 ? -0.462  -23.882 89.753  1.00 39.75  ? 345  TYR B CD2 1 
ATOM   6462 C  CE1 . TYR B 1 345 ? -1.733  -26.308 90.133  1.00 41.77  ? 345  TYR B CE1 1 
ATOM   6463 C  CE2 . TYR B 1 345 ? -1.838  -23.930 89.875  1.00 43.12  ? 345  TYR B CE2 1 
ATOM   6464 C  CZ  . TYR B 1 345 ? -2.469  -25.151 90.069  1.00 43.55  ? 345  TYR B CZ  1 
ATOM   6465 O  OH  . TYR B 1 345 ? -3.843  -25.212 90.191  1.00 46.25  ? 345  TYR B OH  1 
ATOM   6466 N  N   . PRO B 1 346 ? 4.759   -25.804 91.670  1.00 44.55  ? 346  PRO B N   1 
ATOM   6467 C  CA  . PRO B 1 346 ? 6.221   -25.737 91.558  1.00 45.08  ? 346  PRO B CA  1 
ATOM   6468 C  C   . PRO B 1 346 ? 6.685   -26.245 90.204  1.00 40.54  ? 346  PRO B C   1 
ATOM   6469 O  O   . PRO B 1 346 ? 6.195   -27.257 89.695  1.00 41.26  ? 346  PRO B O   1 
ATOM   6470 C  CB  . PRO B 1 346 ? 6.713   -26.647 92.695  1.00 46.21  ? 346  PRO B CB  1 
ATOM   6471 C  CG  . PRO B 1 346 ? 5.505   -26.871 93.576  1.00 47.21  ? 346  PRO B CG  1 
ATOM   6472 C  CD  . PRO B 1 346 ? 4.333   -26.823 92.642  1.00 45.37  ? 346  PRO B CD  1 
ATOM   6473 N  N   . LEU B 1 347 ? 7.650   -25.534 89.627  1.00 38.62  ? 347  LEU B N   1 
ATOM   6474 C  CA  . LEU B 1 347 ? 8.246   -25.911 88.356  1.00 40.60  ? 347  LEU B CA  1 
ATOM   6475 C  C   . LEU B 1 347 ? 9.753   -26.021 88.524  1.00 39.36  ? 347  LEU B C   1 
ATOM   6476 O  O   . LEU B 1 347 ? 10.363  -25.263 89.288  1.00 41.90  ? 347  LEU B O   1 
ATOM   6477 C  CB  . LEU B 1 347 ? 7.929   -24.886 87.244  1.00 38.85  ? 347  LEU B CB  1 
ATOM   6478 C  CG  . LEU B 1 347 ? 6.459   -24.632 86.912  1.00 39.93  ? 347  LEU B CG  1 
ATOM   6479 C  CD1 . LEU B 1 347 ? 6.346   -23.539 85.856  1.00 38.41  ? 347  LEU B CD1 1 
ATOM   6480 C  CD2 . LEU B 1 347 ? 5.771   -25.918 86.436  1.00 36.38  ? 347  LEU B CD2 1 
ATOM   6481 N  N   . GLU B 1 348 ? 10.336  -26.971 87.814  1.00 39.47  ? 348  GLU B N   1 
ATOM   6482 C  CA  . GLU B 1 348 ? 11.776  -27.135 87.753  1.00 40.42  ? 348  GLU B CA  1 
ATOM   6483 C  C   . GLU B 1 348 ? 12.317  -26.438 86.514  1.00 41.83  ? 348  GLU B C   1 
ATOM   6484 O  O   . GLU B 1 348 ? 11.626  -26.309 85.497  1.00 38.18  ? 348  GLU B O   1 
ATOM   6485 C  CB  . GLU B 1 348 ? 12.146  -28.613 87.712  1.00 42.48  ? 348  GLU B CB  1 
ATOM   6486 C  CG  . GLU B 1 348 ? 11.756  -29.353 88.974  1.00 50.21  ? 348  GLU B CG  1 
ATOM   6487 C  CD  . GLU B 1 348 ? 12.147  -30.804 88.909  1.00 57.04  ? 348  GLU B CD  1 
ATOM   6488 O  OE1 . GLU B 1 348 ? 13.255  -31.139 89.379  1.00 65.20  ? 348  GLU B OE1 1 
ATOM   6489 O  OE2 . GLU B 1 348 ? 11.356  -31.601 88.362  1.00 59.28  ? 348  GLU B OE2 1 
ATOM   6490 N  N   . LYS B 1 349 ? 13.558  -25.984 86.616  1.00 38.82  ? 349  LYS B N   1 
ATOM   6491 C  CA  . LYS B 1 349 ? 14.273  -25.454 85.467  1.00 38.38  ? 349  LYS B CA  1 
ATOM   6492 C  C   . LYS B 1 349 ? 14.048  -26.346 84.259  1.00 39.38  ? 349  LYS B C   1 
ATOM   6493 O  O   . LYS B 1 349 ? 14.184  -27.570 84.343  1.00 41.03  ? 349  LYS B O   1 
ATOM   6494 C  CB  . LYS B 1 349 ? 15.764  -25.356 85.795  1.00 44.10  ? 349  LYS B CB  1 
ATOM   6495 C  CG  . LYS B 1 349 ? 16.642  -24.975 84.616  1.00 41.54  ? 349  LYS B CG  1 
ATOM   6496 C  CD  . LYS B 1 349 ? 18.108  -24.966 85.022  1.00 46.49  ? 349  LYS B CD  1 
ATOM   6497 C  CE  . LYS B 1 349 ? 18.933  -24.161 84.036  1.00 48.14  ? 349  LYS B CE  1 
ATOM   6498 N  NZ  . LYS B 1 349 ? 20.371  -24.167 84.429  1.00 56.33  ? 349  LYS B NZ  1 
ATOM   6499 N  N   . GLY B 1 350 ? 13.670  -25.728 83.138  1.00 39.07  ? 350  GLY B N   1 
ATOM   6500 C  CA  . GLY B 1 350 ? 13.420  -26.441 81.910  1.00 37.39  ? 350  GLY B CA  1 
ATOM   6501 C  C   . GLY B 1 350 ? 11.979  -26.861 81.678  1.00 36.99  ? 350  GLY B C   1 
ATOM   6502 O  O   . GLY B 1 350 ? 11.637  -27.223 80.549  1.00 38.90  ? 350  GLY B O   1 
ATOM   6503 N  N   . ASP B 1 351 ? 11.135  -26.845 82.716  1.00 35.00  ? 351  ASP B N   1 
ATOM   6504 C  CA  . ASP B 1 351 ? 9.735   -27.230 82.561  1.00 35.77  ? 351  ASP B CA  1 
ATOM   6505 C  C   . ASP B 1 351 ? 9.028   -26.306 81.571  1.00 38.89  ? 351  ASP B C   1 
ATOM   6506 O  O   . ASP B 1 351 ? 9.221   -25.091 81.595  1.00 35.76  ? 351  ASP B O   1 
ATOM   6507 C  CB  . ASP B 1 351 ? 9.015   -27.173 83.918  1.00 36.85  ? 351  ASP B CB  1 
ATOM   6508 C  CG  . ASP B 1 351 ? 9.283   -28.395 84.797  1.00 38.99  ? 351  ASP B CG  1 
ATOM   6509 O  OD1 . ASP B 1 351 ? 9.974   -29.324 84.340  1.00 38.14  ? 351  ASP B OD1 1 
ATOM   6510 O  OD2 . ASP B 1 351 ? 8.784   -28.414 85.951  1.00 41.06  ? 351  ASP B OD2 1 
ATOM   6511 N  N   . GLU B 1 352 ? 8.171   -26.882 80.727  1.00 35.03  ? 352  GLU B N   1 
ATOM   6512 C  CA  . GLU B 1 352 ? 7.536   -26.154 79.640  1.00 37.09  ? 352  GLU B CA  1 
ATOM   6513 C  C   . GLU B 1 352 ? 6.102   -25.751 79.993  1.00 36.30  ? 352  GLU B C   1 
ATOM   6514 O  O   . GLU B 1 352 ? 5.433   -26.410 80.794  1.00 35.46  ? 352  GLU B O   1 
ATOM   6515 C  CB  . GLU B 1 352 ? 7.521   -27.018 78.385  1.00 38.40  ? 352  GLU B CB  1 
ATOM   6516 C  CG  . GLU B 1 352 ? 8.904   -27.266 77.838  1.00 46.11  ? 352  GLU B CG  1 
ATOM   6517 C  CD  . GLU B 1 352 ? 8.899   -28.149 76.614  1.00 51.79  ? 352  GLU B CD  1 
ATOM   6518 O  OE1 . GLU B 1 352 ? 7.800   -28.499 76.118  1.00 45.68  ? 352  GLU B OE1 1 
ATOM   6519 O  OE2 . GLU B 1 352 ? 10.007  -28.541 76.193  1.00 56.22  ? 352  GLU B OE2 1 
ATOM   6520 N  N   . LEU B 1 353 ? 5.637   -24.670 79.354  1.00 34.11  ? 353  LEU B N   1 
ATOM   6521 C  CA  . LEU B 1 353 ? 4.271   -24.170 79.441  1.00 34.30  ? 353  LEU B CA  1 
ATOM   6522 C  C   . LEU B 1 353 ? 3.763   -23.898 78.033  1.00 34.60  ? 353  LEU B C   1 
ATOM   6523 O  O   . LEU B 1 353 ? 4.531   -23.530 77.138  1.00 34.06  ? 353  LEU B O   1 
ATOM   6524 C  CB  . LEU B 1 353 ? 4.182   -22.856 80.240  1.00 29.73  ? 353  LEU B CB  1 
ATOM   6525 C  CG  . LEU B 1 353 ? 4.765   -22.881 81.655  1.00 32.52  ? 353  LEU B CG  1 
ATOM   6526 C  CD1 . LEU B 1 353 ? 4.925   -21.478 82.188  1.00 37.03  ? 353  LEU B CD1 1 
ATOM   6527 C  CD2 . LEU B 1 353 ? 3.843   -23.713 82.552  1.00 34.30  ? 353  LEU B CD2 1 
ATOM   6528 N  N   . MET B 1 354 ? 2.458   -24.072 77.848  1.00 34.71  ? 354  MET B N   1 
ATOM   6529 C  CA  . MET B 1 354 ? 1.757   -23.663 76.633  1.00 32.82  ? 354  MET B CA  1 
ATOM   6530 C  C   . MET B 1 354 ? 0.748   -22.593 77.017  1.00 32.60  ? 354  MET B C   1 
ATOM   6531 O  O   . MET B 1 354 ? -0.057  -22.800 77.932  1.00 35.03  ? 354  MET B O   1 
ATOM   6532 C  CB  . MET B 1 354 ? 1.041   -24.843 75.985  1.00 33.41  ? 354  MET B CB  1 
ATOM   6533 C  CG  . MET B 1 354 ? 1.894   -25.943 75.385  1.00 32.08  ? 354  MET B CG  1 
ATOM   6534 S  SD  . MET B 1 354 ? 3.041   -25.367 74.094  1.00 36.69  ? 354  MET B SD  1 
ATOM   6535 C  CE  . MET B 1 354 ? 1.833   -24.959 72.819  1.00 36.82  ? 354  MET B CE  1 
ATOM   6536 N  N   . VAL B 1 355 ? 0.801   -21.456 76.338  1.00 34.26  ? 355  VAL B N   1 
ATOM   6537 C  CA  . VAL B 1 355 ? -0.157  -20.381 76.554  1.00 32.01  ? 355  VAL B CA  1 
ATOM   6538 C  C   . VAL B 1 355 ? -1.268  -20.541 75.524  1.00 30.73  ? 355  VAL B C   1 
ATOM   6539 O  O   . VAL B 1 355 ? -1.031  -20.436 74.318  1.00 31.45  ? 355  VAL B O   1 
ATOM   6540 C  CB  . VAL B 1 355 ? 0.516   -19.010 76.441  1.00 33.77  ? 355  VAL B CB  1 
ATOM   6541 C  CG1 . VAL B 1 355 ? -0.538  -17.896 76.504  1.00 34.24  ? 355  VAL B CG1 1 
ATOM   6542 C  CG2 . VAL B 1 355 ? 1.524   -18.834 77.561  1.00 34.48  ? 355  VAL B CG2 1 
ATOM   6543 N  N   . LEU B 1 356 ? -2.482  -20.796 75.998  1.00 31.59  ? 356  LEU B N   1 
ATOM   6544 C  CA  . LEU B 1 356 ? -3.616  -21.029 75.117  1.00 34.06  ? 356  LEU B CA  1 
ATOM   6545 C  C   . LEU B 1 356 ? -4.320  -19.688 74.935  1.00 32.91  ? 356  LEU B C   1 
ATOM   6546 O  O   . LEU B 1 356 ? -5.197  -19.324 75.716  1.00 32.90  ? 356  LEU B O   1 
ATOM   6547 C  CB  . LEU B 1 356 ? -4.525  -22.097 75.716  1.00 36.90  ? 356  LEU B CB  1 
ATOM   6548 C  CG  . LEU B 1 356 ? -5.474  -22.946 74.888  1.00 41.60  ? 356  LEU B CG  1 
ATOM   6549 C  CD1 . LEU B 1 356 ? -4.799  -23.543 73.646  1.00 40.33  ? 356  LEU B CD1 1 
ATOM   6550 C  CD2 . LEU B 1 356 ? -5.942  -24.069 75.817  1.00 39.40  ? 356  LEU B CD2 1 
ATOM   6551 N  N   . ILE B 1 357 ? -3.936  -18.954 73.878  1.00 30.95  ? 357  ILE B N   1 
ATOM   6552 C  CA  . ILE B 1 357 ? -4.356  -17.552 73.760  1.00 33.30  ? 357  ILE B CA  1 
ATOM   6553 C  C   . ILE B 1 357 ? -5.870  -17.426 73.666  1.00 31.16  ? 357  ILE B C   1 
ATOM   6554 O  O   . ILE B 1 357 ? -6.432  -16.526 74.307  1.00 30.74  ? 357  ILE B O   1 
ATOM   6555 C  CB  . ILE B 1 357 ? -3.632  -16.873 72.590  1.00 31.66  ? 357  ILE B CB  1 
ATOM   6556 C  CG1 . ILE B 1 357 ? -2.123  -17.134 72.653  1.00 31.19  ? 357  ILE B CG1 1 
ATOM   6557 C  CG2 . ILE B 1 357 ? -3.915  -15.358 72.612  1.00 32.34  ? 357  ILE B CG2 1 
ATOM   6558 C  CD1 . ILE B 1 357 ? -1.400  -16.645 71.427  1.00 32.56  ? 357  ILE B CD1 1 
ATOM   6559 N  N   . PRO B 1 358 ? -6.588  -18.256 72.899  1.00 32.15  ? 358  PRO B N   1 
ATOM   6560 C  CA  . PRO B 1 358 ? -8.050  -18.092 72.851  1.00 32.32  ? 358  PRO B CA  1 
ATOM   6561 C  C   . PRO B 1 358 ? -8.698  -18.219 74.211  1.00 35.02  ? 358  PRO B C   1 
ATOM   6562 O  O   . PRO B 1 358 ? -9.692  -17.530 74.476  1.00 33.41  ? 358  PRO B O   1 
ATOM   6563 C  CB  . PRO B 1 358 ? -8.505  -19.211 71.899  1.00 32.63  ? 358  PRO B CB  1 
ATOM   6564 C  CG  . PRO B 1 358 ? -7.273  -19.504 71.045  1.00 29.73  ? 358  PRO B CG  1 
ATOM   6565 C  CD  . PRO B 1 358 ? -6.142  -19.373 72.050  1.00 30.38  ? 358  PRO B CD  1 
ATOM   6566 N  N   . GLN B 1 359 ? -8.151  -19.061 75.095  1.00 34.18  ? 359  GLN B N   1 
ATOM   6567 C  CA  . GLN B 1 359 ? -8.726  -19.186 76.432  1.00 34.74  ? 359  GLN B CA  1 
ATOM   6568 C  C   . GLN B 1 359 ? -8.383  -17.986 77.299  1.00 34.02  ? 359  GLN B C   1 
ATOM   6569 O  O   . GLN B 1 359 ? -9.244  -17.474 78.019  1.00 34.21  ? 359  GLN B O   1 
ATOM   6570 C  CB  . GLN B 1 359 ? -8.259  -20.479 77.102  1.00 35.71  ? 359  GLN B CB  1 
ATOM   6571 C  CG  . GLN B 1 359 ? -8.859  -21.726 76.477  1.00 38.62  ? 359  GLN B CG  1 
ATOM   6572 C  CD  . GLN B 1 359 ? -10.390 -21.700 76.442  1.00 36.72  ? 359  GLN B CD  1 
ATOM   6573 O  OE1 . GLN B 1 359 ? -10.989 -21.610 75.375  1.00 39.01  ? 359  GLN B OE1 1 
ATOM   6574 N  NE2 . GLN B 1 359 ? -11.020 -21.798 77.604  1.00 41.74  ? 359  GLN B NE2 1 
ATOM   6575 N  N   . LEU B 1 360 ? -7.136  -17.512 77.232  1.00 31.14  ? 360  LEU B N   1 
ATOM   6576 C  CA  . LEU B 1 360 ? -6.782  -16.271 77.908  1.00 30.38  ? 360  LEU B CA  1 
ATOM   6577 C  C   . LEU B 1 360 ? -7.794  -15.181 77.583  1.00 31.99  ? 360  LEU B C   1 
ATOM   6578 O  O   . LEU B 1 360 ? -8.262  -14.459 78.470  1.00 32.04  ? 360  LEU B O   1 
ATOM   6579 C  CB  . LEU B 1 360 ? -5.374  -15.825 77.480  1.00 30.97  ? 360  LEU B CB  1 
ATOM   6580 C  CG  . LEU B 1 360 ? -4.945  -14.424 77.963  1.00 33.88  ? 360  LEU B CG  1 
ATOM   6581 C  CD1 . LEU B 1 360 ? -4.715  -14.376 79.461  1.00 33.31  ? 360  LEU B CD1 1 
ATOM   6582 C  CD2 . LEU B 1 360 ? -3.675  -13.961 77.250  1.00 30.79  ? 360  LEU B CD2 1 
ATOM   6583 N  N   . HIS B 1 361 ? -8.141  -15.055 76.300  1.00 30.77  ? 361  HIS B N   1 
ATOM   6584 C  CA  . HIS B 1 361 ? -9.000  -13.987 75.810  1.00 31.44  ? 361  HIS B CA  1 
ATOM   6585 C  C   . HIS B 1 361 ? -10.462 -14.211 76.173  1.00 35.02  ? 361  HIS B C   1 
ATOM   6586 O  O   . HIS B 1 361 ? -11.310 -13.363 75.849  1.00 33.38  ? 361  HIS B O   1 
ATOM   6587 C  CB  . HIS B 1 361 ? -8.832  -13.862 74.292  1.00 28.85  ? 361  HIS B CB  1 
ATOM   6588 C  CG  . HIS B 1 361 ? -7.488  -13.332 73.875  1.00 29.98  ? 361  HIS B CG  1 
ATOM   6589 N  ND1 . HIS B 1 361 ? -7.067  -13.314 72.563  1.00 31.44  ? 361  HIS B ND1 1 
ATOM   6590 C  CD2 . HIS B 1 361 ? -6.473  -12.802 74.604  1.00 34.30  ? 361  HIS B CD2 1 
ATOM   6591 C  CE1 . HIS B 1 361 ? -5.853  -12.784 72.497  1.00 30.74  ? 361  HIS B CE1 1 
ATOM   6592 N  NE2 . HIS B 1 361 ? -5.468  -12.472 73.722  1.00 32.19  ? 361  HIS B NE2 1 
ATOM   6593 N  N   . ARG B 1 362 ? -10.763 -15.335 76.831  1.00 32.01  ? 362  ARG B N   1 
ATOM   6594 C  CA  . ARG B 1 362 ? -12.103 -15.630 77.329  1.00 33.73  ? 362  ARG B CA  1 
ATOM   6595 C  C   . ARG B 1 362 ? -12.144 -15.690 78.854  1.00 33.11  ? 362  ARG B C   1 
ATOM   6596 O  O   . ARG B 1 362 ? -13.102 -16.223 79.434  1.00 35.19  ? 362  ARG B O   1 
ATOM   6597 C  CB  . ARG B 1 362 ? -12.603 -16.944 76.722  1.00 32.95  ? 362  ARG B CB  1 
ATOM   6598 C  CG  . ARG B 1 362 ? -12.953 -16.844 75.225  1.00 33.33  ? 362  ARG B CG  1 
ATOM   6599 C  CD  . ARG B 1 362 ? -13.063 -18.237 74.592  1.00 34.79  ? 362  ARG B CD  1 
ATOM   6600 N  NE  . ARG B 1 362 ? -13.588 -18.207 73.228  1.00 35.24  ? 362  ARG B NE  1 
ATOM   6601 C  CZ  . ARG B 1 362 ? -12.902 -17.814 72.160  1.00 36.50  ? 362  ARG B CZ  1 
ATOM   6602 N  NH1 . ARG B 1 362 ? -11.645 -17.395 72.254  1.00 32.34  ? 362  ARG B NH1 1 
ATOM   6603 N  NH2 . ARG B 1 362 ? -13.492 -17.828 70.972  1.00 34.56  ? 362  ARG B NH2 1 
ATOM   6604 N  N   . ASP B 1 363 ? -11.106 -15.174 79.515  1.00 35.30  ? 363  ASP B N   1 
ATOM   6605 C  CA  . ASP B 1 363 ? -11.041 -15.122 80.977  1.00 31.84  ? 363  ASP B CA  1 
ATOM   6606 C  C   . ASP B 1 363 ? -12.097 -14.138 81.484  1.00 33.64  ? 363  ASP B C   1 
ATOM   6607 O  O   . ASP B 1 363 ? -11.957 -12.922 81.319  1.00 34.42  ? 363  ASP B O   1 
ATOM   6608 C  CB  . ASP B 1 363 ? -9.627  -14.719 81.407  1.00 33.85  ? 363  ASP B CB  1 
ATOM   6609 C  CG  . ASP B 1 363 ? -9.394  -14.835 82.912  1.00 34.87  ? 363  ASP B CG  1 
ATOM   6610 O  OD1 . ASP B 1 363 ? -10.366 -14.778 83.681  1.00 33.49  ? 363  ASP B OD1 1 
ATOM   6611 O  OD2 . ASP B 1 363 ? -8.224  -14.942 83.338  1.00 34.09  ? 363  ASP B OD2 1 
ATOM   6612 N  N   . LYS B 1 364 ? -13.178 -14.666 82.064  1.00 35.71  ? 364  LYS B N   1 
ATOM   6613 C  CA  . LYS B 1 364 ? -14.283 -13.814 82.499  1.00 35.60  ? 364  LYS B CA  1 
ATOM   6614 C  C   . LYS B 1 364 ? -13.896 -12.892 83.649  1.00 37.65  ? 364  LYS B C   1 
ATOM   6615 O  O   . LYS B 1 364 ? -14.528 -11.841 83.825  1.00 34.90  ? 364  LYS B O   1 
ATOM   6616 C  CB  . LYS B 1 364 ? -15.482 -14.681 82.898  1.00 38.85  ? 364  LYS B CB  1 
ATOM   6617 C  CG  . LYS B 1 364 ? -16.060 -15.467 81.726  1.00 38.64  ? 364  LYS B CG  1 
ATOM   6618 C  CD  . LYS B 1 364 ? -17.329 -16.213 82.101  1.00 48.50  ? 364  LYS B CD  1 
ATOM   6619 C  CE  . LYS B 1 364 ? -18.029 -16.734 80.840  1.00 52.98  ? 364  LYS B CE  1 
ATOM   6620 N  NZ  . LYS B 1 364 ? -19.167 -17.641 81.162  1.00 57.81  ? 364  LYS B NZ  1 
ATOM   6621 N  N   . THR B 1 365 ? -12.883 -13.249 84.439  1.00 37.08  ? 365  THR B N   1 
ATOM   6622 C  CA  . THR B 1 365 ? -12.479 -12.352 85.518  1.00 38.98  ? 365  THR B CA  1 
ATOM   6623 C  C   . THR B 1 365 ? -11.810 -11.093 84.977  1.00 39.50  ? 365  THR B C   1 
ATOM   6624 O  O   . THR B 1 365 ? -11.708 -10.095 85.699  1.00 41.43  ? 365  THR B O   1 
ATOM   6625 C  CB  . THR B 1 365 ? -11.546 -13.068 86.502  1.00 38.67  ? 365  THR B CB  1 
ATOM   6626 O  OG1 . THR B 1 365 ? -10.262 -13.222 85.895  1.00 38.71  ? 365  THR B OG1 1 
ATOM   6627 C  CG2 . THR B 1 365 ? -12.100 -14.437 86.873  1.00 39.77  ? 365  THR B CG2 1 
ATOM   6628 N  N   . ILE B 1 366 ? -11.378 -11.121 83.721  1.00 34.48  ? 366  ILE B N   1 
ATOM   6629 C  CA  . ILE B 1 366 ? -10.806 -9.970  83.038  1.00 36.22  ? 366  ILE B CA  1 
ATOM   6630 C  C   . ILE B 1 366 ? -11.844 -9.251  82.195  1.00 36.27  ? 366  ILE B C   1 
ATOM   6631 O  O   . ILE B 1 366 ? -12.026 -8.040  82.315  1.00 40.23  ? 366  ILE B O   1 
ATOM   6632 C  CB  . ILE B 1 366 ? -9.617  -10.415 82.152  1.00 36.88  ? 366  ILE B CB  1 
ATOM   6633 C  CG1 . ILE B 1 366 ? -8.468  -10.954 83.014  1.00 36.39  ? 366  ILE B CG1 1 
ATOM   6634 C  CG2 . ILE B 1 366 ? -9.200  -9.272  81.227  1.00 39.90  ? 366  ILE B CG2 1 
ATOM   6635 C  CD1 . ILE B 1 366 ? -7.844  -9.926  83.955  1.00 43.53  ? 366  ILE B CD1 1 
ATOM   6636 N  N   . TRP B 1 367 ? -12.525 -9.992  81.324  1.00 37.49  ? 367  TRP B N   1 
ATOM   6637 C  CA  . TRP B 1 367 ? -13.332 -9.418  80.258  1.00 33.69  ? 367  TRP B CA  1 
ATOM   6638 C  C   . TRP B 1 367 ? -14.813 -9.291  80.607  1.00 39.43  ? 367  TRP B C   1 
ATOM   6639 O  O   . TRP B 1 367 ? -15.546 -8.605  79.886  1.00 40.67  ? 367  TRP B O   1 
ATOM   6640 C  CB  . TRP B 1 367 ? -13.175 -10.265 78.988  1.00 36.87  ? 367  TRP B CB  1 
ATOM   6641 C  CG  . TRP B 1 367 ? -11.739 -10.310 78.494  1.00 33.88  ? 367  TRP B CG  1 
ATOM   6642 C  CD1 . TRP B 1 367 ? -10.801 -11.261 78.764  1.00 33.79  ? 367  TRP B CD1 1 
ATOM   6643 C  CD2 . TRP B 1 367 ? -11.099 -9.328  77.667  1.00 34.14  ? 367  TRP B CD2 1 
ATOM   6644 N  NE1 . TRP B 1 367 ? -9.611  -10.943 78.130  1.00 31.86  ? 367  TRP B NE1 1 
ATOM   6645 C  CE2 . TRP B 1 367 ? -9.769  -9.756  77.461  1.00 32.47  ? 367  TRP B CE2 1 
ATOM   6646 C  CE3 . TRP B 1 367 ? -11.527 -8.127  77.078  1.00 36.14  ? 367  TRP B CE3 1 
ATOM   6647 C  CZ2 . TRP B 1 367 ? -8.860  -9.030  76.680  1.00 33.07  ? 367  TRP B CZ2 1 
ATOM   6648 C  CZ3 . TRP B 1 367 ? -10.624 -7.401  76.313  1.00 32.64  ? 367  TRP B CZ3 1 
ATOM   6649 C  CH2 . TRP B 1 367 ? -9.300  -7.853  76.126  1.00 32.91  ? 367  TRP B CH2 1 
ATOM   6650 N  N   . GLY B 1 368 ? -15.271 -9.925  81.678  1.00 38.73  ? 368  GLY B N   1 
ATOM   6651 C  CA  . GLY B 1 368 ? -16.680 -9.905  82.025  1.00 37.78  ? 368  GLY B CA  1 
ATOM   6652 C  C   . GLY B 1 368 ? -17.391 -11.139 81.512  1.00 43.80  ? 368  GLY B C   1 
ATOM   6653 O  O   . GLY B 1 368 ? -16.808 -12.025 80.881  1.00 40.80  ? 368  GLY B O   1 
ATOM   6654 N  N   . ASP B 1 369 ? -18.700 -11.183 81.769  1.00 42.63  ? 369  ASP B N   1 
ATOM   6655 C  CA  . ASP B 1 369 ? -19.458 -12.391 81.467  1.00 44.89  ? 369  ASP B CA  1 
ATOM   6656 C  C   . ASP B 1 369 ? -19.700 -12.588 79.976  1.00 43.69  ? 369  ASP B C   1 
ATOM   6657 O  O   . ASP B 1 369 ? -19.953 -13.717 79.552  1.00 49.87  ? 369  ASP B O   1 
ATOM   6658 C  CB  . ASP B 1 369 ? -20.798 -12.355 82.198  1.00 53.60  ? 369  ASP B CB  1 
ATOM   6659 C  CG  . ASP B 1 369 ? -20.633 -12.344 83.696  1.00 52.01  ? 369  ASP B CG  1 
ATOM   6660 O  OD1 . ASP B 1 369 ? -19.823 -13.149 84.200  1.00 53.82  ? 369  ASP B OD1 1 
ATOM   6661 O  OD2 . ASP B 1 369 ? -21.280 -11.502 84.352  1.00 57.44  ? 369  ASP B OD2 1 
ATOM   6662 N  N   . ASP B 1 370 ? -19.641 -11.527 79.178  1.00 39.00  ? 370  ASP B N   1 
ATOM   6663 C  CA  . ASP B 1 370 ? -20.057 -11.595 77.778  1.00 40.76  ? 370  ASP B CA  1 
ATOM   6664 C  C   . ASP B 1 370 ? -18.903 -11.935 76.832  1.00 38.32  ? 370  ASP B C   1 
ATOM   6665 O  O   . ASP B 1 370 ? -18.869 -11.405 75.712  1.00 38.63  ? 370  ASP B O   1 
ATOM   6666 C  CB  . ASP B 1 370 ? -20.705 -10.267 77.391  1.00 40.11  ? 370  ASP B CB  1 
ATOM   6667 C  CG  . ASP B 1 370 ? -19.738 -9.094  77.484  1.00 44.06  ? 370  ASP B CG  1 
ATOM   6668 O  OD1 . ASP B 1 370 ? -18.599 -9.285  77.975  1.00 42.34  ? 370  ASP B OD1 1 
ATOM   6669 O  OD2 . ASP B 1 370 ? -20.118 -7.972  77.079  1.00 49.65  ? 370  ASP B OD2 1 
ATOM   6670 N  N   . VAL B 1 371 ? -17.982 -12.829 77.231  1.00 37.63  ? 371  VAL B N   1 
ATOM   6671 C  CA  . VAL B 1 371 ? -16.713 -12.996 76.509  1.00 35.43  ? 371  VAL B CA  1 
ATOM   6672 C  C   . VAL B 1 371 ? -16.926 -13.557 75.115  1.00 38.08  ? 371  VAL B C   1 
ATOM   6673 O  O   . VAL B 1 371 ? -16.073 -13.373 74.233  1.00 36.25  ? 371  VAL B O   1 
ATOM   6674 C  CB  . VAL B 1 371 ? -15.734 -13.914 77.277  1.00 41.24  ? 371  VAL B CB  1 
ATOM   6675 C  CG1 . VAL B 1 371 ? -15.060 -13.172 78.433  1.00 45.21  ? 371  VAL B CG1 1 
ATOM   6676 C  CG2 . VAL B 1 371 ? -16.415 -15.210 77.730  1.00 41.84  ? 371  VAL B CG2 1 
ATOM   6677 N  N   . GLU B 1 372 ? -18.007 -14.307 74.898  1.00 32.59  ? 372  GLU B N   1 
ATOM   6678 C  CA  . GLU B 1 372 ? -18.233 -14.885 73.578  1.00 35.91  ? 372  GLU B CA  1 
ATOM   6679 C  C   . GLU B 1 372 ? -18.837 -13.895 72.588  1.00 35.38  ? 372  GLU B C   1 
ATOM   6680 O  O   . GLU B 1 372 ? -18.860 -14.183 71.387  1.00 35.65  ? 372  GLU B O   1 
ATOM   6681 C  CB  . GLU B 1 372 ? -19.134 -16.119 73.694  1.00 36.76  ? 372  GLU B CB  1 
ATOM   6682 C  CG  . GLU B 1 372 ? -18.465 -17.275 74.431  1.00 38.55  ? 372  GLU B CG  1 
ATOM   6683 C  CD  . GLU B 1 372 ? -17.379 -17.940 73.583  1.00 42.85  ? 372  GLU B CD  1 
ATOM   6684 O  OE1 . GLU B 1 372 ? -17.522 -17.986 72.336  1.00 45.36  ? 372  GLU B OE1 1 
ATOM   6685 O  OE2 . GLU B 1 372 ? -16.395 -18.422 74.172  1.00 47.67  ? 372  GLU B OE2 1 
ATOM   6686 N  N   . GLU B 1 373 ? -19.296 -12.732 73.044  1.00 34.37  ? 373  GLU B N   1 
ATOM   6687 C  CA  . GLU B 1 373 ? -19.918 -11.775 72.140  1.00 33.75  ? 373  GLU B CA  1 
ATOM   6688 C  C   . GLU B 1 373 ? -18.853 -10.921 71.459  1.00 33.64  ? 373  GLU B C   1 
ATOM   6689 O  O   . GLU B 1 373 ? -17.776 -10.681 72.011  1.00 34.82  ? 373  GLU B O   1 
ATOM   6690 C  CB  . GLU B 1 373 ? -20.922 -10.901 72.902  1.00 37.79  ? 373  GLU B CB  1 
ATOM   6691 C  CG  . GLU B 1 373 ? -22.139 -11.715 73.337  1.00 40.65  ? 373  GLU B CG  1 
ATOM   6692 C  CD  . GLU B 1 373 ? -23.126 -10.959 74.211  1.00 50.04  ? 373  GLU B CD  1 
ATOM   6693 O  OE1 . GLU B 1 373 ? -22.851 -9.798  74.599  1.00 45.28  ? 373  GLU B OE1 1 
ATOM   6694 O  OE2 . GLU B 1 373 ? -24.189 -11.552 74.518  1.00 53.02  ? 373  GLU B OE2 1 
ATOM   6695 N  N   . PHE B 1 374 ? -19.162 -10.488 70.234  1.00 33.29  ? 374  PHE B N   1 
ATOM   6696 C  CA  . PHE B 1 374 ? -18.256 -9.690  69.413  1.00 32.32  ? 374  PHE B CA  1 
ATOM   6697 C  C   . PHE B 1 374 ? -18.589 -8.219  69.642  1.00 34.36  ? 374  PHE B C   1 
ATOM   6698 O  O   . PHE B 1 374 ? -19.583 -7.698  69.121  1.00 34.00  ? 374  PHE B O   1 
ATOM   6699 C  CB  . PHE B 1 374 ? -18.374 -10.077 67.939  1.00 32.39  ? 374  PHE B CB  1 
ATOM   6700 C  CG  . PHE B 1 374 ? -17.339 -9.445  67.080  1.00 30.57  ? 374  PHE B CG  1 
ATOM   6701 C  CD1 . PHE B 1 374 ? -16.057 -9.987  67.014  1.00 31.38  ? 374  PHE B CD1 1 
ATOM   6702 C  CD2 . PHE B 1 374 ? -17.612 -8.285  66.364  1.00 30.97  ? 374  PHE B CD2 1 
ATOM   6703 C  CE1 . PHE B 1 374 ? -15.084 -9.378  66.246  1.00 28.95  ? 374  PHE B CE1 1 
ATOM   6704 C  CE2 . PHE B 1 374 ? -16.626 -7.684  65.580  1.00 33.05  ? 374  PHE B CE2 1 
ATOM   6705 C  CZ  . PHE B 1 374 ? -15.362 -8.230  65.541  1.00 32.77  ? 374  PHE B CZ  1 
ATOM   6706 N  N   . ARG B 1 375 ? -17.762 -7.553  70.441  1.00 32.14  ? 375  ARG B N   1 
ATOM   6707 C  CA  . ARG B 1 375 ? -18.038 -6.192  70.903  1.00 32.56  ? 375  ARG B CA  1 
ATOM   6708 C  C   . ARG B 1 375 ? -16.758 -5.387  70.792  1.00 33.26  ? 375  ARG B C   1 
ATOM   6709 O  O   . ARG B 1 375 ? -15.988 -5.280  71.757  1.00 32.76  ? 375  ARG B O   1 
ATOM   6710 C  CB  . ARG B 1 375 ? -18.570 -6.189  72.341  1.00 32.55  ? 375  ARG B CB  1 
ATOM   6711 C  CG  . ARG B 1 375 ? -19.888 -6.923  72.493  1.00 35.47  ? 375  ARG B CG  1 
ATOM   6712 C  CD  . ARG B 1 375 ? -20.452 -6.826  73.912  1.00 40.34  ? 375  ARG B CD  1 
ATOM   6713 N  NE  . ARG B 1 375 ? -21.785 -7.421  73.960  1.00 42.36  ? 375  ARG B NE  1 
ATOM   6714 C  CZ  . ARG B 1 375 ? -22.876 -6.818  73.504  1.00 47.62  ? 375  ARG B CZ  1 
ATOM   6715 N  NH1 . ARG B 1 375 ? -22.835 -5.581  73.027  1.00 44.73  ? 375  ARG B NH1 1 
ATOM   6716 N  NH2 . ARG B 1 375 ? -24.039 -7.466  73.535  1.00 45.12  ? 375  ARG B NH2 1 
ATOM   6717 N  N   . PRO B 1 376 ? -16.489 -4.813  69.616  1.00 34.53  ? 376  PRO B N   1 
ATOM   6718 C  CA  . PRO B 1 376 ? -15.280 -3.990  69.465  1.00 32.41  ? 376  PRO B CA  1 
ATOM   6719 C  C   . PRO B 1 376 ? -15.187 -2.869  70.491  1.00 33.36  ? 376  PRO B C   1 
ATOM   6720 O  O   . PRO B 1 376 ? -14.078 -2.401  70.771  1.00 34.14  ? 376  PRO B O   1 
ATOM   6721 C  CB  . PRO B 1 376 ? -15.408 -3.441  68.038  1.00 32.43  ? 376  PRO B CB  1 
ATOM   6722 C  CG  . PRO B 1 376 ? -16.258 -4.480  67.325  1.00 33.90  ? 376  PRO B CG  1 
ATOM   6723 C  CD  . PRO B 1 376 ? -17.268 -4.883  68.363  1.00 31.53  ? 376  PRO B CD  1 
ATOM   6724 N  N   . GLU B 1 377 ? -16.318 -2.437  71.059  1.00 35.92  ? 377  GLU B N   1 
ATOM   6725 C  CA  . GLU B 1 377 ? -16.314 -1.368  72.050  1.00 39.22  ? 377  GLU B CA  1 
ATOM   6726 C  C   . GLU B 1 377 ? -15.459 -1.705  73.272  1.00 36.29  ? 377  GLU B C   1 
ATOM   6727 O  O   . GLU B 1 377 ? -15.049 -0.790  73.997  1.00 36.00  ? 377  GLU B O   1 
ATOM   6728 C  CB  . GLU B 1 377 ? -17.755 -1.068  72.472  1.00 39.17  ? 377  GLU B CB  1 
ATOM   6729 C  CG  . GLU B 1 377 ? -18.575 -0.381  71.381  1.00 34.68  ? 377  GLU B CG  1 
ATOM   6730 C  CD  . GLU B 1 377 ? -19.055 -1.335  70.293  1.00 33.90  ? 377  GLU B CD  1 
ATOM   6731 O  OE1 . GLU B 1 377 ? -19.075 -2.576  70.505  1.00 34.29  ? 377  GLU B OE1 1 
ATOM   6732 O  OE2 . GLU B 1 377 ? -19.458 -0.827  69.225  1.00 35.42  ? 377  GLU B OE2 1 
ATOM   6733 N  N   . ARG B 1 378 ? -15.183 -2.994  73.514  1.00 35.16  ? 378  ARG B N   1 
ATOM   6734 C  CA  . ARG B 1 378 ? -14.241 -3.384  74.567  1.00 38.28  ? 378  ARG B CA  1 
ATOM   6735 C  C   . ARG B 1 378 ? -12.918 -2.658  74.447  1.00 38.28  ? 378  ARG B C   1 
ATOM   6736 O  O   . ARG B 1 378 ? -12.209 -2.490  75.444  1.00 39.09  ? 378  ARG B O   1 
ATOM   6737 C  CB  . ARG B 1 378 ? -13.913 -4.878  74.498  1.00 35.91  ? 378  ARG B CB  1 
ATOM   6738 C  CG  . ARG B 1 378 ? -14.985 -5.801  74.883  1.00 39.57  ? 378  ARG B CG  1 
ATOM   6739 C  CD  . ARG B 1 378 ? -14.468 -7.185  74.574  1.00 33.79  ? 378  ARG B CD  1 
ATOM   6740 N  NE  . ARG B 1 378 ? -15.574 -8.019  74.159  1.00 33.94  ? 378  ARG B NE  1 
ATOM   6741 C  CZ  . ARG B 1 378 ? -16.455 -8.532  74.998  1.00 38.13  ? 378  ARG B CZ  1 
ATOM   6742 N  NH1 . ARG B 1 378 ? -16.380 -8.302  76.305  1.00 38.54  ? 378  ARG B NH1 1 
ATOM   6743 N  NH2 . ARG B 1 378 ? -17.436 -9.286  74.520  1.00 36.06  ? 378  ARG B NH2 1 
ATOM   6744 N  N   . PHE B 1 379 ? -12.522 -2.311  73.226  1.00 33.82  ? 379  PHE B N   1 
ATOM   6745 C  CA  . PHE B 1 379 ? -11.220 -1.719  72.975  1.00 34.34  ? 379  PHE B CA  1 
ATOM   6746 C  C   . PHE B 1 379 ? -11.282 -0.205  72.814  1.00 38.82  ? 379  PHE B C   1 
ATOM   6747 O  O   . PHE B 1 379 ? -10.291 0.402   72.387  1.00 40.36  ? 379  PHE B O   1 
ATOM   6748 C  CB  . PHE B 1 379 ? -10.591 -2.371  71.741  1.00 36.47  ? 379  PHE B CB  1 
ATOM   6749 C  CG  . PHE B 1 379 ? -10.182 -3.804  71.963  1.00 36.25  ? 379  PHE B CG  1 
ATOM   6750 C  CD1 . PHE B 1 379 ? -8.914  -4.108  72.460  1.00 36.18  ? 379  PHE B CD1 1 
ATOM   6751 C  CD2 . PHE B 1 379 ? -11.061 -4.847  71.700  1.00 36.10  ? 379  PHE B CD2 1 
ATOM   6752 C  CE1 . PHE B 1 379 ? -8.528  -5.429  72.683  1.00 35.26  ? 379  PHE B CE1 1 
ATOM   6753 C  CE2 . PHE B 1 379 ? -10.689 -6.178  71.920  1.00 33.24  ? 379  PHE B CE2 1 
ATOM   6754 C  CZ  . PHE B 1 379 ? -9.412  -6.472  72.417  1.00 33.75  ? 379  PHE B CZ  1 
ATOM   6755 N  N   . GLU B 1 380 ? -12.420 0.416   73.139  1.00 40.06  ? 380  GLU B N   1 
ATOM   6756 C  CA  . GLU B 1 380 ? -12.556 1.859   72.943  1.00 40.96  ? 380  GLU B CA  1 
ATOM   6757 C  C   . GLU B 1 380 ? -11.462 2.612   73.682  1.00 48.01  ? 380  GLU B C   1 
ATOM   6758 O  O   . GLU B 1 380 ? -10.855 3.549   73.143  1.00 46.39  ? 380  GLU B O   1 
ATOM   6759 C  CB  . GLU B 1 380 ? -13.921 2.346   73.433  1.00 44.24  ? 380  GLU B CB  1 
ATOM   6760 C  CG  . GLU B 1 380 ? -15.092 2.197   72.487  1.00 49.37  ? 380  GLU B CG  1 
ATOM   6761 C  CD  . GLU B 1 380 ? -16.418 2.492   73.191  1.00 47.93  ? 380  GLU B CD  1 
ATOM   6762 O  OE1 . GLU B 1 380 ? -16.387 2.836   74.396  1.00 60.18  ? 380  GLU B OE1 1 
ATOM   6763 O  OE2 . GLU B 1 380 ? -17.480 2.408   72.543  1.00 57.68  ? 380  GLU B OE2 1 
ATOM   6764 N  N   . ASN B 1 381 ? -11.229 2.227   74.936  1.00 43.36  ? 381  ASN B N   1 
ATOM   6765 C  CA  . ASN B 1 381 ? -10.243 2.813   75.840  1.00 46.71  ? 381  ASN B CA  1 
ATOM   6766 C  C   . ASN B 1 381 ? -9.106  1.828   76.064  1.00 41.97  ? 381  ASN B C   1 
ATOM   6767 O  O   . ASN B 1 381 ? -9.227  0.917   76.898  1.00 46.48  ? 381  ASN B O   1 
ATOM   6768 C  CB  . ASN B 1 381 ? -10.913 3.184   77.166  1.00 45.93  ? 381  ASN B CB  1 
ATOM   6769 C  CG  . ASN B 1 381 ? -9.989  3.935   78.109  1.00 52.12  ? 381  ASN B CG  1 
ATOM   6770 O  OD1 . ASN B 1 381 ? -8.806  4.157   77.816  1.00 48.31  ? 381  ASN B OD1 1 
ATOM   6771 N  ND2 . ASN B 1 381 ? -10.539 4.352   79.248  1.00 49.33  ? 381  ASN B ND2 1 
ATOM   6772 N  N   . PRO B 1 382 ? -7.985  1.972   75.359  1.00 48.53  ? 382  PRO B N   1 
ATOM   6773 C  CA  . PRO B 1 382 ? -6.924  0.958   75.447  1.00 49.92  ? 382  PRO B CA  1 
ATOM   6774 C  C   . PRO B 1 382 ? -6.351  0.820   76.839  1.00 55.55  ? 382  PRO B C   1 
ATOM   6775 O  O   . PRO B 1 382 ? -5.930  -0.280  77.224  1.00 48.64  ? 382  PRO B O   1 
ATOM   6776 C  CB  . PRO B 1 382 ? -5.869  1.467   74.456  1.00 54.57  ? 382  PRO B CB  1 
ATOM   6777 C  CG  . PRO B 1 382 ? -6.144  2.932   74.326  1.00 55.01  ? 382  PRO B CG  1 
ATOM   6778 C  CD  . PRO B 1 382 ? -7.628  3.087   74.466  1.00 53.54  ? 382  PRO B CD  1 
ATOM   6779 N  N   . SER B 1 383 ? -6.324  1.913   77.609  1.00 49.27  ? 383  SER B N   1 
ATOM   6780 C  CA  . SER B 1 383 ? -5.760  1.865   78.950  1.00 53.18  ? 383  SER B CA  1 
ATOM   6781 C  C   . SER B 1 383 ? -6.639  1.074   79.906  1.00 53.02  ? 383  SER B C   1 
ATOM   6782 O  O   . SER B 1 383 ? -6.168  0.657   80.971  1.00 55.21  ? 383  SER B O   1 
ATOM   6783 C  CB  . SER B 1 383 ? -5.520  3.294   79.449  1.00 49.69  ? 383  SER B CB  1 
ATOM   6784 O  OG  . SER B 1 383 ? -6.636  3.766   80.175  1.00 59.42  ? 383  SER B OG  1 
ATOM   6785 N  N   . ALA B 1 384 ? -7.891  0.821   79.531  1.00 51.84  ? 384  ALA B N   1 
ATOM   6786 C  CA  . ALA B 1 384 ? -8.765  -0.005  80.346  1.00 50.24  ? 384  ALA B CA  1 
ATOM   6787 C  C   . ALA B 1 384 ? -8.424  -1.494  80.275  1.00 55.84  ? 384  ALA B C   1 
ATOM   6788 O  O   . ALA B 1 384 ? -8.934  -2.258  81.100  1.00 53.18  ? 384  ALA B O   1 
ATOM   6789 C  CB  . ALA B 1 384 ? -10.220 0.229   79.929  1.00 50.94  ? 384  ALA B CB  1 
ATOM   6790 N  N   . ILE B 1 385 ? -7.588  -1.927  79.331  1.00 52.09  ? 385  ILE B N   1 
ATOM   6791 C  CA  . ILE B 1 385 ? -7.252  -3.346  79.188  1.00 49.25  ? 385  ILE B CA  1 
ATOM   6792 C  C   . ILE B 1 385 ? -6.137  -3.706  80.163  1.00 47.29  ? 385  ILE B C   1 
ATOM   6793 O  O   . ILE B 1 385 ? -5.044  -3.132  80.077  1.00 48.30  ? 385  ILE B O   1 
ATOM   6794 C  CB  . ILE B 1 385 ? -6.810  -3.689  77.754  1.00 49.99  ? 385  ILE B CB  1 
ATOM   6795 C  CG1 . ILE B 1 385 ? -7.773  -3.110  76.708  1.00 49.99  ? 385  ILE B CG1 1 
ATOM   6796 C  CG2 . ILE B 1 385 ? -6.668  -5.199  77.600  1.00 47.34  ? 385  ILE B CG2 1 
ATOM   6797 C  CD1 . ILE B 1 385 ? -9.034  -3.910  76.513  1.00 45.46  ? 385  ILE B CD1 1 
ATOM   6798 N  N   . PRO B 1 386 ? -6.342  -4.663  81.070  1.00 47.06  ? 386  PRO B N   1 
ATOM   6799 C  CA  . PRO B 1 386 ? -5.282  -5.011  82.030  1.00 45.64  ? 386  PRO B CA  1 
ATOM   6800 C  C   . PRO B 1 386 ? -4.048  -5.593  81.352  1.00 49.53  ? 386  PRO B C   1 
ATOM   6801 O  O   . PRO B 1 386 ? -4.127  -6.202  80.285  1.00 41.45  ? 386  PRO B O   1 
ATOM   6802 C  CB  . PRO B 1 386 ? -5.956  -6.045  82.944  1.00 48.22  ? 386  PRO B CB  1 
ATOM   6803 C  CG  . PRO B 1 386 ? -7.426  -5.842  82.745  1.00 46.66  ? 386  PRO B CG  1 
ATOM   6804 C  CD  . PRO B 1 386 ? -7.593  -5.394  81.324  1.00 46.96  ? 386  PRO B CD  1 
ATOM   6805 N  N   . GLN B 1 387 ? -2.892  -5.419  81.998  1.00 50.50  ? 387  GLN B N   1 
ATOM   6806 C  CA  . GLN B 1 387 ? -1.644  -5.940  81.447  1.00 47.22  ? 387  GLN B CA  1 
ATOM   6807 C  C   . GLN B 1 387 ? -1.706  -7.457  81.284  1.00 42.63  ? 387  GLN B C   1 
ATOM   6808 O  O   . GLN B 1 387 ? -2.186  -8.172  82.166  1.00 49.62  ? 387  GLN B O   1 
ATOM   6809 C  CB  . GLN B 1 387 ? -0.467  -5.576  82.357  1.00 55.49  ? 387  GLN B CB  1 
ATOM   6810 C  CG  . GLN B 1 387 ? 0.896   -5.954  81.782  1.00 58.26  ? 387  GLN B CG  1 
ATOM   6811 C  CD  . GLN B 1 387 ? 2.049   -5.584  82.707  1.00 66.19  ? 387  GLN B CD  1 
ATOM   6812 O  OE1 . GLN B 1 387 ? 3.196   -5.967  82.469  1.00 68.49  ? 387  GLN B OE1 1 
ATOM   6813 N  NE2 . GLN B 1 387 ? 1.742   -4.861  83.784  1.00 64.37  ? 387  GLN B NE2 1 
ATOM   6814 N  N   . HIS B 1 388 ? -1.186  -7.951  80.161  1.00 42.94  ? 388  HIS B N   1 
ATOM   6815 C  CA  . HIS B 1 388 ? -1.106  -9.376  79.837  1.00 42.57  ? 388  HIS B CA  1 
ATOM   6816 C  C   . HIS B 1 388 ? -2.478  -10.035 79.683  1.00 36.97  ? 388  HIS B C   1 
ATOM   6817 O  O   . HIS B 1 388 ? -2.561  -11.265 79.641  1.00 40.03  ? 388  HIS B O   1 
ATOM   6818 C  CB  . HIS B 1 388 ? -0.279  -10.149 80.881  1.00 44.43  ? 388  HIS B CB  1 
ATOM   6819 C  CG  . HIS B 1 388 ? 1.144   -9.692  80.981  1.00 44.79  ? 388  HIS B CG  1 
ATOM   6820 N  ND1 . HIS B 1 388 ? 1.966   -9.577  79.879  1.00 47.69  ? 388  HIS B ND1 1 
ATOM   6821 C  CD2 . HIS B 1 388 ? 1.886   -9.307  82.045  1.00 51.35  ? 388  HIS B CD2 1 
ATOM   6822 C  CE1 . HIS B 1 388 ? 3.156   -9.149  80.263  1.00 51.09  ? 388  HIS B CE1 1 
ATOM   6823 N  NE2 . HIS B 1 388 ? 3.132   -8.974  81.572  1.00 51.39  ? 388  HIS B NE2 1 
ATOM   6824 N  N   . ALA B 1 389 ? -3.557  -9.254  79.578  1.00 37.88  ? 389  ALA B N   1 
ATOM   6825 C  CA  . ALA B 1 389 ? -4.873  -9.834  79.304  1.00 35.71  ? 389  ALA B CA  1 
ATOM   6826 C  C   . ALA B 1 389 ? -5.084  -10.146 77.827  1.00 32.65  ? 389  ALA B C   1 
ATOM   6827 O  O   . ALA B 1 389 ? -5.885  -11.028 77.495  1.00 33.15  ? 389  ALA B O   1 
ATOM   6828 C  CB  . ALA B 1 389 ? -5.980  -8.891  79.776  1.00 39.69  ? 389  ALA B CB  1 
ATOM   6829 N  N   . PHE B 1 390 ? -4.361  -9.470  76.937  1.00 33.00  ? 390  PHE B N   1 
ATOM   6830 C  CA  . PHE B 1 390 ? -4.600  -9.532  75.497  1.00 31.70  ? 390  PHE B CA  1 
ATOM   6831 C  C   . PHE B 1 390 ? -3.250  -9.766  74.834  1.00 33.35  ? 390  PHE B C   1 
ATOM   6832 O  O   . PHE B 1 390 ? -2.397  -8.872  74.840  1.00 32.95  ? 390  PHE B O   1 
ATOM   6833 C  CB  . PHE B 1 390 ? -5.252  -8.230  75.036  1.00 31.63  ? 390  PHE B CB  1 
ATOM   6834 C  CG  . PHE B 1 390 ? -5.562  -8.162  73.559  1.00 33.36  ? 390  PHE B CG  1 
ATOM   6835 C  CD1 . PHE B 1 390 ? -6.448  -9.053  72.971  1.00 33.33  ? 390  PHE B CD1 1 
ATOM   6836 C  CD2 . PHE B 1 390 ? -4.992  -7.176  72.775  1.00 30.86  ? 390  PHE B CD2 1 
ATOM   6837 C  CE1 . PHE B 1 390 ? -6.745  -8.964  71.625  1.00 31.10  ? 390  PHE B CE1 1 
ATOM   6838 C  CE2 . PHE B 1 390 ? -5.282  -7.073  71.406  1.00 31.98  ? 390  PHE B CE2 1 
ATOM   6839 C  CZ  . PHE B 1 390 ? -6.159  -7.966  70.832  1.00 32.05  ? 390  PHE B CZ  1 
ATOM   6840 N  N   . LYS B 1 391 ? -3.034  -10.981 74.313  1.00 34.67  ? 391  LYS B N   1 
ATOM   6841 C  CA  . LYS B 1 391 ? -1.702  -11.369 73.849  1.00 33.35  ? 391  LYS B CA  1 
ATOM   6842 C  C   . LYS B 1 391 ? -1.689  -12.020 72.469  1.00 32.86  ? 391  LYS B C   1 
ATOM   6843 O  O   . LYS B 1 391 ? -0.984  -13.025 72.277  1.00 31.93  ? 391  LYS B O   1 
ATOM   6844 C  CB  . LYS B 1 391 ? -1.057  -12.343 74.845  1.00 32.47  ? 391  LYS B CB  1 
ATOM   6845 C  CG  . LYS B 1 391 ? -0.999  -11.841 76.292  1.00 38.28  ? 391  LYS B CG  1 
ATOM   6846 C  CD  . LYS B 1 391 ? -0.045  -10.675 76.416  1.00 41.69  ? 391  LYS B CD  1 
ATOM   6847 C  CE  . LYS B 1 391 ? 1.414   -11.148 76.406  1.00 41.37  ? 391  LYS B CE  1 
ATOM   6848 N  NZ  . LYS B 1 391 ? 2.359   -10.029 76.725  1.00 45.14  ? 391  LYS B NZ  1 
ATOM   6849 N  N   . PRO B 1 392 ? -2.435  -11.510 71.484  1.00 32.95  ? 392  PRO B N   1 
ATOM   6850 C  CA  . PRO B 1 392 ? -2.408  -12.151 70.164  1.00 32.04  ? 392  PRO B CA  1 
ATOM   6851 C  C   . PRO B 1 392 ? -1.065  -12.024 69.475  1.00 32.46  ? 392  PRO B C   1 
ATOM   6852 O  O   . PRO B 1 392 ? -0.848  -12.702 68.463  1.00 32.46  ? 392  PRO B O   1 
ATOM   6853 C  CB  . PRO B 1 392 ? -3.493  -11.406 69.383  1.00 32.43  ? 392  PRO B CB  1 
ATOM   6854 C  CG  . PRO B 1 392 ? -3.467  -10.029 69.970  1.00 35.07  ? 392  PRO B CG  1 
ATOM   6855 C  CD  . PRO B 1 392 ? -3.176  -10.235 71.462  1.00 32.80  ? 392  PRO B CD  1 
ATOM   6856 N  N   . HIS B 1 393 ? -0.174  -11.175 69.981  1.00 30.55  ? 393  HIS B N   1 
ATOM   6857 C  CA  . HIS B 1 393 ? 1.115   -10.975 69.331  1.00 32.91  ? 393  HIS B CA  1 
ATOM   6858 C  C   . HIS B 1 393 ? 2.269   -11.539 70.153  1.00 34.56  ? 393  HIS B C   1 
ATOM   6859 O  O   . HIS B 1 393 ? 3.418   -11.121 69.964  1.00 32.47  ? 393  HIS B O   1 
ATOM   6860 C  CB  . HIS B 1 393 ? 1.365   -9.489  69.086  1.00 35.06  ? 393  HIS B CB  1 
ATOM   6861 C  CG  . HIS B 1 393 ? 0.233   -8.796  68.401  1.00 43.77  ? 393  HIS B CG  1 
ATOM   6862 N  ND1 . HIS B 1 393 ? -0.123  -9.048  67.097  1.00 42.66  ? 393  HIS B ND1 1 
ATOM   6863 C  CD2 . HIS B 1 393 ? -0.593  -7.815  68.836  1.00 50.02  ? 393  HIS B CD2 1 
ATOM   6864 C  CE1 . HIS B 1 393 ? -1.150  -8.284  66.771  1.00 40.47  ? 393  HIS B CE1 1 
ATOM   6865 N  NE2 . HIS B 1 393 ? -1.444  -7.515  67.803  1.00 48.36  ? 393  HIS B NE2 1 
ATOM   6866 N  N   . GLY B 1 394 ? 1.997   -12.452 71.074  1.00 32.74  ? 394  GLY B N   1 
ATOM   6867 C  CA  . GLY B 1 394 ? 3.099   -13.011 71.845  1.00 33.03  ? 394  GLY B CA  1 
ATOM   6868 C  C   . GLY B 1 394 ? 3.530   -12.082 72.969  1.00 35.54  ? 394  GLY B C   1 
ATOM   6869 O  O   . GLY B 1 394 ? 2.766   -11.227 73.447  1.00 34.03  ? 394  GLY B O   1 
ATOM   6870 N  N   . ASN B 1 395 ? 4.786   -12.256 73.405  1.00 31.60  ? 395  ASN B N   1 
ATOM   6871 C  CA  . ASN B 1 395 ? 5.223   -11.604 74.629  1.00 35.03  ? 395  ASN B CA  1 
ATOM   6872 C  C   . ASN B 1 395 ? 6.676   -11.153 74.561  1.00 32.79  ? 395  ASN B C   1 
ATOM   6873 O  O   . ASN B 1 395 ? 7.541   -11.889 74.079  1.00 32.57  ? 395  ASN B O   1 
ATOM   6874 C  CB  . ASN B 1 395 ? 5.073   -12.528 75.832  1.00 32.90  ? 395  ASN B CB  1 
ATOM   6875 C  CG  . ASN B 1 395 ? 5.454   -11.839 77.119  1.00 36.67  ? 395  ASN B CG  1 
ATOM   6876 O  OD1 . ASN B 1 395 ? 4.755   -10.935 77.574  1.00 38.81  ? 395  ASN B OD1 1 
ATOM   6877 N  ND2 . ASN B 1 395 ? 6.569   -12.248 77.706  1.00 34.56  ? 395  ASN B ND2 1 
ATOM   6878 N  N   . GLY B 1 396 ? 6.929   -9.948  75.086  1.00 33.02  ? 396  GLY B N   1 
ATOM   6879 C  CA  . GLY B 1 396 ? 8.283   -9.520  75.434  1.00 34.23  ? 396  GLY B CA  1 
ATOM   6880 C  C   . GLY B 1 396 ? 9.182   -9.313  74.225  1.00 31.78  ? 396  GLY B C   1 
ATOM   6881 O  O   . GLY B 1 396 ? 8.742   -8.929  73.147  1.00 33.51  ? 396  GLY B O   1 
ATOM   6882 N  N   . GLN B 1 397 ? 10.482  -9.561  74.423  1.00 32.09  ? 397  GLN B N   1 
ATOM   6883 C  CA  . GLN B 1 397 ? 11.422  -9.435  73.315  1.00 33.00  ? 397  GLN B CA  1 
ATOM   6884 C  C   . GLN B 1 397 ? 11.149  -10.454 72.215  1.00 33.33  ? 397  GLN B C   1 
ATOM   6885 O  O   . GLN B 1 397 ? 11.600  -10.259 71.081  1.00 34.14  ? 397  GLN B O   1 
ATOM   6886 C  CB  . GLN B 1 397 ? 12.861  -9.570  73.827  1.00 33.49  ? 397  GLN B CB  1 
ATOM   6887 C  CG  . GLN B 1 397 ? 13.256  -10.972 74.283  1.00 32.42  ? 397  GLN B CG  1 
ATOM   6888 C  CD  . GLN B 1 397 ? 14.662  -11.012 74.894  1.00 37.29  ? 397  GLN B CD  1 
ATOM   6889 O  OE1 . GLN B 1 397 ? 15.492  -10.154 74.611  1.00 38.90  ? 397  GLN B OE1 1 
ATOM   6890 N  NE2 . GLN B 1 397 ? 14.933  -12.028 75.714  1.00 36.50  ? 397  GLN B NE2 1 
ATOM   6891 N  N   . ARG B 1 398 ? 10.424  -11.534 72.517  1.00 32.68  ? 398  ARG B N   1 
ATOM   6892 C  CA  . ARG B 1 398 ? 10.035  -12.507 71.505  1.00 32.67  ? 398  ARG B CA  1 
ATOM   6893 C  C   . ARG B 1 398 ? 8.631   -12.232 70.957  1.00 31.27  ? 398  ARG B C   1 
ATOM   6894 O  O   . ARG B 1 398 ? 8.024   -13.111 70.338  1.00 32.18  ? 398  ARG B O   1 
ATOM   6895 C  CB  . ARG B 1 398 ? 10.141  -13.932 72.056  1.00 32.84  ? 398  ARG B CB  1 
ATOM   6896 C  CG  . ARG B 1 398 ? 11.573  -14.346 72.513  1.00 29.27  ? 398  ARG B CG  1 
ATOM   6897 C  CD  . ARG B 1 398 ? 12.630  -14.100 71.409  1.00 30.37  ? 398  ARG B CD  1 
ATOM   6898 N  NE  . ARG B 1 398 ? 12.321  -14.772 70.152  1.00 29.39  ? 398  ARG B NE  1 
ATOM   6899 C  CZ  . ARG B 1 398 ? 12.720  -15.993 69.823  1.00 30.58  ? 398  ARG B CZ  1 
ATOM   6900 N  NH1 . ARG B 1 398 ? 13.440  -16.741 70.656  1.00 29.58  ? 398  ARG B NH1 1 
ATOM   6901 N  NH2 . ARG B 1 398 ? 12.412  -16.472 68.618  1.00 30.84  ? 398  ARG B NH2 1 
ATOM   6902 N  N   . ALA B 1 399 ? 8.111   -11.030 71.180  1.00 32.43  ? 399  ALA B N   1 
ATOM   6903 C  CA  . ALA B 1 399 ? 6.814   -10.657 70.638  1.00 31.98  ? 399  ALA B CA  1 
ATOM   6904 C  C   . ALA B 1 399 ? 6.892   -10.503 69.116  1.00 30.77  ? 399  ALA B C   1 
ATOM   6905 O  O   . ALA B 1 399 ? 7.969   -10.424 68.517  1.00 32.88  ? 399  ALA B O   1 
ATOM   6906 C  CB  . ALA B 1 399 ? 6.321   -9.363  71.283  1.00 33.35  ? 399  ALA B CB  1 
ATOM   6907 N  N   . CYS B 1 400 ? 5.722   -10.445 68.488  1.00 31.54  ? 400  CYS B N   1 
ATOM   6908 C  CA  . CYS B 1 400 ? 5.613   -10.314 67.035  1.00 30.89  ? 400  CYS B CA  1 
ATOM   6909 C  C   . CYS B 1 400 ? 6.346   -9.074  66.519  1.00 32.07  ? 400  CYS B C   1 
ATOM   6910 O  O   . CYS B 1 400 ? 6.044   -7.945  66.918  1.00 33.23  ? 400  CYS B O   1 
ATOM   6911 C  CB  . CYS B 1 400 ? 4.127   -10.257 66.656  1.00 30.37  ? 400  CYS B CB  1 
ATOM   6912 S  SG  . CYS B 1 400 ? 3.879   -10.060 64.880  1.00 32.03  ? 400  CYS B SG  1 
ATOM   6913 N  N   . ILE B 1 401 ? 7.301   -9.273  65.606  1.00 29.83  ? 401  ILE B N   1 
ATOM   6914 C  CA  . ILE B 1 401 ? 7.993   -8.130  65.017  1.00 31.97  ? 401  ILE B CA  1 
ATOM   6915 C  C   . ILE B 1 401 ? 7.141   -7.405  63.975  1.00 36.18  ? 401  ILE B C   1 
ATOM   6916 O  O   . ILE B 1 401 ? 7.364   -6.214  63.720  1.00 34.31  ? 401  ILE B O   1 
ATOM   6917 C  CB  . ILE B 1 401 ? 9.338   -8.573  64.405  1.00 31.09  ? 401  ILE B CB  1 
ATOM   6918 C  CG1 . ILE B 1 401 ? 10.279  -7.373  64.291  1.00 34.16  ? 401  ILE B CG1 1 
ATOM   6919 C  CG2 . ILE B 1 401 ? 9.136   -9.228  63.028  1.00 32.24  ? 401  ILE B CG2 1 
ATOM   6920 C  CD1 . ILE B 1 401 ? 11.670  -7.728  63.786  1.00 37.71  ? 401  ILE B CD1 1 
ATOM   6921 N  N   . GLY B 1 402 ? 6.143   -8.069  63.398  1.00 34.55  ? 402  GLY B N   1 
ATOM   6922 C  CA  . GLY B 1 402 ? 5.416   -7.496  62.271  1.00 30.74  ? 402  GLY B CA  1 
ATOM   6923 C  C   . GLY B 1 402 ? 4.026   -6.998  62.618  1.00 33.68  ? 402  GLY B C   1 
ATOM   6924 O  O   . GLY B 1 402 ? 3.214   -6.747  61.727  1.00 34.62  ? 402  GLY B O   1 
ATOM   6925 N  N   . GLN B 1 403 ? 3.747   -6.831  63.915  1.00 31.00  ? 403  GLN B N   1 
ATOM   6926 C  CA  . GLN B 1 403 ? 2.374   -6.572  64.334  1.00 32.19  ? 403  GLN B CA  1 
ATOM   6927 C  C   . GLN B 1 403 ? 1.850   -5.242  63.771  1.00 35.03  ? 403  GLN B C   1 
ATOM   6928 O  O   . GLN B 1 403 ? 0.694   -5.165  63.327  1.00 34.06  ? 403  GLN B O   1 
ATOM   6929 C  CB  . GLN B 1 403 ? 2.268   -6.644  65.865  1.00 37.85  ? 403  GLN B CB  1 
ATOM   6930 C  CG  . GLN B 1 403 ? 3.097   -5.683  66.656  1.00 38.77  ? 403  GLN B CG  1 
ATOM   6931 C  CD  . GLN B 1 403 ? 3.112   -6.029  68.160  1.00 44.41  ? 403  GLN B CD  1 
ATOM   6932 O  OE1 . GLN B 1 403 ? 2.221   -5.572  68.874  1.00 42.10  ? 403  GLN B OE1 1 
ATOM   6933 N  NE2 . GLN B 1 403 ? 4.185   -6.702  68.663  1.00 37.45  ? 403  GLN B NE2 1 
ATOM   6934 N  N   . GLN B 1 404 ? 2.693   -4.202  63.728  1.00 35.78  ? 404  GLN B N   1 
ATOM   6935 C  CA  . GLN B 1 404 ? 2.281   -2.939  63.111  1.00 38.42  ? 404  GLN B CA  1 
ATOM   6936 C  C   . GLN B 1 404 ? 2.000   -3.104  61.619  1.00 38.32  ? 404  GLN B C   1 
ATOM   6937 O  O   . GLN B 1 404 ? 1.040   -2.527  61.090  1.00 35.10  ? 404  GLN B O   1 
ATOM   6938 C  CB  . GLN B 1 404 ? 3.353   -1.867  63.329  1.00 42.30  ? 404  GLN B CB  1 
ATOM   6939 C  CG  . GLN B 1 404 ? 3.563   -1.509  64.782  1.00 50.33  ? 404  GLN B CG  1 
ATOM   6940 C  CD  . GLN B 1 404 ? 2.272   -1.083  65.431  1.00 53.67  ? 404  GLN B CD  1 
ATOM   6941 O  OE1 . GLN B 1 404 ? 1.670   -0.081  65.036  1.00 60.99  ? 404  GLN B OE1 1 
ATOM   6942 N  NE2 . GLN B 1 404 ? 1.823   -1.849  66.423  1.00 58.63  ? 404  GLN B NE2 1 
ATOM   6943 N  N   . PHE B 1 405 ? 2.845   -3.867  60.921  1.00 34.07  ? 405  PHE B N   1 
ATOM   6944 C  CA  . PHE B 1 405 ? 2.619   -4.170  59.507  1.00 35.21  ? 405  PHE B CA  1 
ATOM   6945 C  C   . PHE B 1 405 ? 1.266   -4.843  59.300  1.00 34.04  ? 405  PHE B C   1 
ATOM   6946 O  O   . PHE B 1 405 ? 0.444   -4.400  58.480  1.00 32.00  ? 405  PHE B O   1 
ATOM   6947 C  CB  . PHE B 1 405 ? 3.764   -5.062  59.006  1.00 32.53  ? 405  PHE B CB  1 
ATOM   6948 C  CG  . PHE B 1 405 ? 3.770   -5.293  57.523  1.00 32.51  ? 405  PHE B CG  1 
ATOM   6949 C  CD1 . PHE B 1 405 ? 2.968   -6.273  56.952  1.00 32.82  ? 405  PHE B CD1 1 
ATOM   6950 C  CD2 . PHE B 1 405 ? 4.607   -4.555  56.689  1.00 35.66  ? 405  PHE B CD2 1 
ATOM   6951 C  CE1 . PHE B 1 405 ? 2.977   -6.490  55.576  1.00 34.70  ? 405  PHE B CE1 1 
ATOM   6952 C  CE2 . PHE B 1 405 ? 4.616   -4.770  55.309  1.00 34.90  ? 405  PHE B CE2 1 
ATOM   6953 C  CZ  . PHE B 1 405 ? 3.809   -5.737  54.752  1.00 34.93  ? 405  PHE B CZ  1 
ATOM   6954 N  N   . ALA B 1 406 ? 1.023   -5.928  60.033  1.00 31.32  ? 406  ALA B N   1 
ATOM   6955 C  CA  . ALA B 1 406 ? -0.235  -6.660  59.903  1.00 31.79  ? 406  ALA B CA  1 
ATOM   6956 C  C   . ALA B 1 406 ? -1.435  -5.760  60.174  1.00 35.93  ? 406  ALA B C   1 
ATOM   6957 O  O   . ALA B 1 406 ? -2.434  -5.806  59.444  1.00 33.94  ? 406  ALA B O   1 
ATOM   6958 C  CB  . ALA B 1 406 ? -0.245  -7.850  60.867  1.00 33.47  ? 406  ALA B CB  1 
ATOM   6959 N  N   . LEU B 1 407 ? -1.372  -4.946  61.231  1.00 33.37  ? 407  LEU B N   1 
ATOM   6960 C  CA  . LEU B 1 407 ? -2.558  -4.164  61.583  1.00 33.28  ? 407  LEU B CA  1 
ATOM   6961 C  C   . LEU B 1 407 ? -2.784  -3.003  60.613  1.00 34.23  ? 407  LEU B C   1 
ATOM   6962 O  O   . LEU B 1 407 ? -3.940  -2.652  60.328  1.00 34.06  ? 407  LEU B O   1 
ATOM   6963 C  CB  . LEU B 1 407 ? -2.454  -3.675  63.028  1.00 36.21  ? 407  LEU B CB  1 
ATOM   6964 C  CG  . LEU B 1 407 ? -2.740  -4.791  64.045  1.00 39.88  ? 407  LEU B CG  1 
ATOM   6965 C  CD1 . LEU B 1 407 ? -2.512  -4.294  65.471  1.00 43.61  ? 407  LEU B CD1 1 
ATOM   6966 C  CD2 . LEU B 1 407 ? -4.152  -5.371  63.871  1.00 43.65  ? 407  LEU B CD2 1 
ATOM   6967 N  N   . HIS B 1 408 ? -1.712  -2.406  60.076  1.00 32.82  ? 408  HIS B N   1 
ATOM   6968 C  CA  . HIS B 1 408 ? -1.898  -1.358  59.076  1.00 32.51  ? 408  HIS B CA  1 
ATOM   6969 C  C   . HIS B 1 408 ? -2.491  -1.943  57.799  1.00 32.18  ? 408  HIS B C   1 
ATOM   6970 O  O   . HIS B 1 408 ? -3.463  -1.412  57.240  1.00 33.11  ? 408  HIS B O   1 
ATOM   6971 C  CB  . HIS B 1 408 ? -0.564  -0.662  58.784  1.00 34.44  ? 408  HIS B CB  1 
ATOM   6972 C  CG  . HIS B 1 408 ? -0.715  0.588   57.973  1.00 32.96  ? 408  HIS B CG  1 
ATOM   6973 N  ND1 . HIS B 1 408 ? -1.082  1.795   58.528  1.00 36.44  ? 408  HIS B ND1 1 
ATOM   6974 C  CD2 . HIS B 1 408 ? -0.609  0.802   56.642  1.00 32.56  ? 408  HIS B CD2 1 
ATOM   6975 C  CE1 . HIS B 1 408 ? -1.180  2.705   57.576  1.00 37.32  ? 408  HIS B CE1 1 
ATOM   6976 N  NE2 . HIS B 1 408 ? -0.887  2.132   56.422  1.00 33.37  ? 408  HIS B NE2 1 
ATOM   6977 N  N   . GLU B 1 409 ? -1.934  -3.062  57.343  1.00 29.66  ? 409  GLU B N   1 
ATOM   6978 C  CA  . GLU B 1 409 ? -2.472  -3.727  56.161  1.00 30.70  ? 409  GLU B CA  1 
ATOM   6979 C  C   . GLU B 1 409 ? -3.939  -4.068  56.363  1.00 30.45  ? 409  GLU B C   1 
ATOM   6980 O  O   . GLU B 1 409 ? -4.791  -3.773  55.505  1.00 31.61  ? 409  GLU B O   1 
ATOM   6981 C  CB  . GLU B 1 409 ? -1.670  -4.995  55.869  1.00 32.40  ? 409  GLU B CB  1 
ATOM   6982 C  CG  . GLU B 1 409 ? -2.237  -5.790  54.697  1.00 30.75  ? 409  GLU B CG  1 
ATOM   6983 C  CD  . GLU B 1 409 ? -1.476  -7.078  54.457  1.00 32.80  ? 409  GLU B CD  1 
ATOM   6984 O  OE1 . GLU B 1 409 ? -0.517  -7.357  55.213  1.00 33.13  ? 409  GLU B OE1 1 
ATOM   6985 O  OE2 . GLU B 1 409 ? -1.793  -7.780  53.477  1.00 31.33  ? 409  GLU B OE2 1 
ATOM   6986 N  N   . ALA B 1 410 ? -4.252  -4.709  57.493  1.00 32.06  ? 410  ALA B N   1 
ATOM   6987 C  CA  . ALA B 1 410 ? -5.615  -5.198  57.704  1.00 33.36  ? 410  ALA B CA  1 
ATOM   6988 C  C   . ALA B 1 410 ? -6.593  -4.046  57.881  1.00 33.47  ? 410  ALA B C   1 
ATOM   6989 O  O   . ALA B 1 410 ? -7.752  -4.141  57.462  1.00 32.60  ? 410  ALA B O   1 
ATOM   6990 C  CB  . ALA B 1 410 ? -5.663  -6.141  58.916  1.00 31.12  ? 410  ALA B CB  1 
ATOM   6991 N  N   . THR B 1 411 ? -6.161  -2.966  58.530  1.00 32.25  ? 411  THR B N   1 
ATOM   6992 C  CA  . THR B 1 411 ? -7.040  -1.807  58.683  1.00 31.28  ? 411  THR B CA  1 
ATOM   6993 C  C   . THR B 1 411 ? -7.297  -1.132  57.340  1.00 32.06  ? 411  THR B C   1 
ATOM   6994 O  O   . THR B 1 411 ? -8.441  -0.785  57.017  1.00 34.53  ? 411  THR B O   1 
ATOM   6995 C  CB  . THR B 1 411 ? -6.445  -0.816  59.681  1.00 32.94  ? 411  THR B CB  1 
ATOM   6996 O  OG1 . THR B 1 411 ? -6.195  -1.493  60.933  1.00 31.36  ? 411  THR B OG1 1 
ATOM   6997 C  CG2 . THR B 1 411 ? -7.419  0.346   59.891  1.00 32.61  ? 411  THR B CG2 1 
ATOM   6998 N  N   . LEU B 1 412 ? -6.249  -0.965  56.534  1.00 32.45  ? 412  LEU B N   1 
ATOM   6999 C  CA  . LEU B 1 412 ? -6.411  -0.396  55.199  1.00 31.05  ? 412  LEU B CA  1 
ATOM   7000 C  C   . LEU B 1 412 ? -7.383  -1.222  54.376  1.00 33.78  ? 412  LEU B C   1 
ATOM   7001 O  O   . LEU B 1 412 ? -8.310  -0.690  53.743  1.00 33.18  ? 412  LEU B O   1 
ATOM   7002 C  CB  . LEU B 1 412 ? -5.048  -0.352  54.501  1.00 28.40  ? 412  LEU B CB  1 
ATOM   7003 C  CG  . LEU B 1 412 ? -5.094  -0.186  52.973  1.00 36.70  ? 412  LEU B CG  1 
ATOM   7004 C  CD1 . LEU B 1 412 ? -5.549  1.234   52.616  1.00 33.61  ? 412  LEU B CD1 1 
ATOM   7005 C  CD2 . LEU B 1 412 ? -3.739  -0.492  52.359  1.00 36.96  ? 412  LEU B CD2 1 
ATOM   7006 N  N   . VAL B 1 413 ? -7.159  -2.533  54.347  1.00 31.59  ? 413  VAL B N   1 
ATOM   7007 C  CA  . VAL B 1 413 ? -7.916  -3.405  53.459  1.00 33.41  ? 413  VAL B CA  1 
ATOM   7008 C  C   . VAL B 1 413 ? -9.360  -3.509  53.929  1.00 32.71  ? 413  VAL B C   1 
ATOM   7009 O  O   . VAL B 1 413 ? -10.300 -3.359  53.135  1.00 32.39  ? 413  VAL B O   1 
ATOM   7010 C  CB  . VAL B 1 413 ? -7.226  -4.782  53.380  1.00 36.40  ? 413  VAL B CB  1 
ATOM   7011 C  CG1 . VAL B 1 413 ? -8.125  -5.821  52.742  1.00 39.12  ? 413  VAL B CG1 1 
ATOM   7012 C  CG2 . VAL B 1 413 ? -5.903  -4.650  52.593  1.00 35.90  ? 413  VAL B CG2 1 
ATOM   7013 N  N   . LEU B 1 414 ? -9.563  -3.752  55.227  1.00 31.23  ? 414  LEU B N   1 
ATOM   7014 C  CA  . LEU B 1 414 ? -10.931 -3.828  55.736  1.00 31.82  ? 414  LEU B CA  1 
ATOM   7015 C  C   . LEU B 1 414 ? -11.638 -2.486  55.570  1.00 34.08  ? 414  LEU B C   1 
ATOM   7016 O  O   . LEU B 1 414 ? -12.820 -2.438  55.206  1.00 32.40  ? 414  LEU B O   1 
ATOM   7017 C  CB  . LEU B 1 414 ? -10.934 -4.277  57.202  1.00 33.16  ? 414  LEU B CB  1 
ATOM   7018 C  CG  . LEU B 1 414 ? -12.295 -4.582  57.835  1.00 34.24  ? 414  LEU B CG  1 
ATOM   7019 C  CD1 . LEU B 1 414 ? -13.080 -5.557  56.968  1.00 33.96  ? 414  LEU B CD1 1 
ATOM   7020 C  CD2 . LEU B 1 414 ? -12.082 -5.191  59.227  1.00 29.45  ? 414  LEU B CD2 1 
ATOM   7021 N  N   . GLY B 1 415 ? -10.921 -1.385  55.806  1.00 34.45  ? 415  GLY B N   1 
ATOM   7022 C  CA  . GLY B 1 415 ? -11.474 -0.071  55.507  1.00 34.74  ? 415  GLY B CA  1 
ATOM   7023 C  C   . GLY B 1 415 ? -11.937 0.039   54.064  1.00 35.41  ? 415  GLY B C   1 
ATOM   7024 O  O   . GLY B 1 415 ? -13.057 0.477   53.780  1.00 32.70  ? 415  GLY B O   1 
ATOM   7025 N  N   . MET B 1 416 ? -11.089 -0.371  53.116  1.00 32.60  ? 416  MET B N   1 
ATOM   7026 C  CA  . MET B 1 416 ? -11.499 -0.225  51.726  1.00 32.91  ? 416  MET B CA  1 
ATOM   7027 C  C   . MET B 1 416 ? -12.661 -1.158  51.400  1.00 30.71  ? 416  MET B C   1 
ATOM   7028 O  O   . MET B 1 416 ? -13.571 -0.779  50.649  1.00 33.20  ? 416  MET B O   1 
ATOM   7029 C  CB  . MET B 1 416 ? -10.335 -0.490  50.762  1.00 31.92  ? 416  MET B CB  1 
ATOM   7030 C  CG  . MET B 1 416 ? -9.520  0.751   50.514  1.00 36.86  ? 416  MET B CG  1 
ATOM   7031 S  SD  . MET B 1 416 ? -7.961  0.367   49.681  1.00 38.01  ? 416  MET B SD  1 
ATOM   7032 C  CE  . MET B 1 416 ? -8.662  0.545   48.023  1.00 38.59  ? 416  MET B CE  1 
ATOM   7033 N  N   . MET B 1 417 ? -12.658 -2.386  51.948  1.00 30.52  ? 417  MET B N   1 
ATOM   7034 C  CA  . MET B 1 417 ? -13.774 -3.288  51.689  1.00 32.93  ? 417  MET B CA  1 
ATOM   7035 C  C   . MET B 1 417 ? -15.092 -2.679  52.139  1.00 36.56  ? 417  MET B C   1 
ATOM   7036 O  O   . MET B 1 417 ? -16.087 -2.718  51.402  1.00 31.95  ? 417  MET B O   1 
ATOM   7037 C  CB  . MET B 1 417 ? -13.576 -4.660  52.340  1.00 32.29  ? 417  MET B CB  1 
ATOM   7038 C  CG  . MET B 1 417 ? -12.352 -5.428  51.841  1.00 34.25  ? 417  MET B CG  1 
ATOM   7039 S  SD  . MET B 1 417 ? -11.785 -6.749  52.942  1.00 35.91  ? 417  MET B SD  1 
ATOM   7040 C  CE  . MET B 1 417 ? -13.303 -7.569  53.416  1.00 36.84  ? 417  MET B CE  1 
ATOM   7041 N  N   . LEU B 1 418 ? -15.110 -2.085  53.336  1.00 35.15  ? 418  LEU B N   1 
ATOM   7042 C  CA  . LEU B 1 418 ? -16.352 -1.532  53.876  1.00 34.10  ? 418  LEU B CA  1 
ATOM   7043 C  C   . LEU B 1 418 ? -16.763 -0.249  53.173  1.00 35.75  ? 418  LEU B C   1 
ATOM   7044 O  O   . LEU B 1 418 ? -17.948 0.112   53.185  1.00 34.28  ? 418  LEU B O   1 
ATOM   7045 C  CB  . LEU B 1 418 ? -16.188 -1.268  55.372  1.00 32.38  ? 418  LEU B CB  1 
ATOM   7046 C  CG  . LEU B 1 418 ? -15.965 -2.544  56.183  1.00 36.56  ? 418  LEU B CG  1 
ATOM   7047 C  CD1 . LEU B 1 418 ? -15.794 -2.140  57.623  1.00 38.65  ? 418  LEU B CD1 1 
ATOM   7048 C  CD2 . LEU B 1 418 ? -17.136 -3.518  56.037  1.00 38.51  ? 418  LEU B CD2 1 
ATOM   7049 N  N   . LYS B 1 419 ? -15.798 0.478   52.619  1.00 32.77  ? 419  LYS B N   1 
ATOM   7050 C  CA  . LYS B 1 419 ? -16.109 1.661   51.827  1.00 32.36  ? 419  LYS B CA  1 
ATOM   7051 C  C   . LYS B 1 419 ? -16.838 1.290   50.539  1.00 35.81  ? 419  LYS B C   1 
ATOM   7052 O  O   . LYS B 1 419 ? -17.802 1.960   50.140  1.00 35.08  ? 419  LYS B O   1 
ATOM   7053 C  CB  . LYS B 1 419 ? -14.818 2.415   51.493  1.00 33.19  ? 419  LYS B CB  1 
ATOM   7054 C  CG  . LYS B 1 419 ? -15.014 3.580   50.520  1.00 35.11  ? 419  LYS B CG  1 
ATOM   7055 C  CD  . LYS B 1 419 ? -13.687 4.267   50.182  1.00 36.89  ? 419  LYS B CD  1 
ATOM   7056 C  CE  . LYS B 1 419 ? -13.882 5.408   49.194  1.00 36.47  ? 419  LYS B CE  1 
ATOM   7057 N  NZ  . LYS B 1 419 ? -12.609 6.116   48.907  1.00 36.78  ? 419  LYS B NZ  1 
ATOM   7058 N  N   . HIS B 1 420 ? -16.386 0.229   49.872  1.00 34.79  ? 420  HIS B N   1 
ATOM   7059 C  CA  . HIS B 1 420 ? -16.760 -0.001  48.485  1.00 32.69  ? 420  HIS B CA  1 
ATOM   7060 C  C   . HIS B 1 420 ? -17.891 -1.008  48.302  1.00 32.96  ? 420  HIS B C   1 
ATOM   7061 O  O   . HIS B 1 420 ? -18.441 -1.089  47.202  1.00 35.51  ? 420  HIS B O   1 
ATOM   7062 C  CB  . HIS B 1 420 ? -15.533 -0.469  47.699  1.00 35.49  ? 420  HIS B CB  1 
ATOM   7063 C  CG  . HIS B 1 420 ? -14.584 0.636   47.358  1.00 35.81  ? 420  HIS B CG  1 
ATOM   7064 N  ND1 . HIS B 1 420 ? -14.803 1.507   46.307  1.00 35.69  ? 420  HIS B ND1 1 
ATOM   7065 C  CD2 . HIS B 1 420 ? -13.415 1.017   47.928  1.00 34.43  ? 420  HIS B CD2 1 
ATOM   7066 C  CE1 . HIS B 1 420 ? -13.805 2.373   46.244  1.00 38.45  ? 420  HIS B CE1 1 
ATOM   7067 N  NE2 . HIS B 1 420 ? -12.949 2.095   47.214  1.00 35.51  ? 420  HIS B NE2 1 
ATOM   7068 N  N   . PHE B 1 421 ? -18.250 -1.777  49.329  1.00 32.23  ? 421  PHE B N   1 
ATOM   7069 C  CA  . PHE B 1 421 ? -19.239 -2.836  49.165  1.00 34.08  ? 421  PHE B CA  1 
ATOM   7070 C  C   . PHE B 1 421 ? -20.138 -2.938  50.388  1.00 37.89  ? 421  PHE B C   1 
ATOM   7071 O  O   . PHE B 1 421 ? -19.729 -2.633  51.511  1.00 34.48  ? 421  PHE B O   1 
ATOM   7072 C  CB  . PHE B 1 421 ? -18.585 -4.212  48.944  1.00 35.04  ? 421  PHE B CB  1 
ATOM   7073 C  CG  . PHE B 1 421 ? -17.609 -4.246  47.797  1.00 34.90  ? 421  PHE B CG  1 
ATOM   7074 C  CD1 . PHE B 1 421 ? -18.056 -4.437  46.509  1.00 34.15  ? 421  PHE B CD1 1 
ATOM   7075 C  CD2 . PHE B 1 421 ? -16.253 -4.048  48.012  1.00 31.18  ? 421  PHE B CD2 1 
ATOM   7076 C  CE1 . PHE B 1 421 ? -17.161 -4.458  45.441  1.00 35.60  ? 421  PHE B CE1 1 
ATOM   7077 C  CE2 . PHE B 1 421 ? -15.345 -4.066  46.954  1.00 31.15  ? 421  PHE B CE2 1 
ATOM   7078 C  CZ  . PHE B 1 421 ? -15.802 -4.265  45.665  1.00 33.13  ? 421  PHE B CZ  1 
ATOM   7079 N  N   . ASP B 1 422 ? -21.363 -3.402  50.153  1.00 35.61  ? 422  ASP B N   1 
ATOM   7080 C  CA  . ASP B 1 422 ? -22.189 -3.996  51.198  1.00 36.53  ? 422  ASP B CA  1 
ATOM   7081 C  C   . ASP B 1 422 ? -22.003 -5.507  51.127  1.00 38.81  ? 422  ASP B C   1 
ATOM   7082 O  O   . ASP B 1 422 ? -21.818 -6.058  50.040  1.00 39.34  ? 422  ASP B O   1 
ATOM   7083 C  CB  . ASP B 1 422 ? -23.668 -3.639  51.002  1.00 38.60  ? 422  ASP B CB  1 
ATOM   7084 C  CG  . ASP B 1 422 ? -23.970 -2.204  51.354  1.00 42.70  ? 422  ASP B CG  1 
ATOM   7085 O  OD1 . ASP B 1 422 ? -23.802 -1.849  52.533  1.00 43.33  ? 422  ASP B OD1 1 
ATOM   7086 O  OD2 . ASP B 1 422 ? -24.343 -1.431  50.447  1.00 48.23  ? 422  ASP B OD2 1 
ATOM   7087 N  N   . PHE B 1 423 ? -22.035 -6.178  52.272  1.00 33.76  ? 423  PHE B N   1 
ATOM   7088 C  CA  . PHE B 1 423 ? -21.747 -7.607  52.306  1.00 35.40  ? 423  PHE B CA  1 
ATOM   7089 C  C   . PHE B 1 423 ? -22.949 -8.388  52.801  1.00 38.11  ? 423  PHE B C   1 
ATOM   7090 O  O   . PHE B 1 423 ? -23.633 -7.961  53.738  1.00 40.68  ? 423  PHE B O   1 
ATOM   7091 C  CB  . PHE B 1 423 ? -20.530 -7.897  53.179  1.00 35.81  ? 423  PHE B CB  1 
ATOM   7092 C  CG  . PHE B 1 423 ? -19.253 -7.362  52.607  1.00 37.06  ? 423  PHE B CG  1 
ATOM   7093 C  CD1 . PHE B 1 423 ? -18.539 -8.096  51.681  1.00 37.17  ? 423  PHE B CD1 1 
ATOM   7094 C  CD2 . PHE B 1 423 ? -18.795 -6.102  52.959  1.00 37.88  ? 423  PHE B CD2 1 
ATOM   7095 C  CE1 . PHE B 1 423 ? -17.370 -7.597  51.130  1.00 38.31  ? 423  PHE B CE1 1 
ATOM   7096 C  CE2 . PHE B 1 423 ? -17.632 -5.601  52.424  1.00 37.32  ? 423  PHE B CE2 1 
ATOM   7097 C  CZ  . PHE B 1 423 ? -16.914 -6.344  51.503  1.00 37.48  ? 423  PHE B CZ  1 
ATOM   7098 N  N   . GLU B 1 424 ? -23.200 -9.529  52.158  1.00 36.56  ? 424  GLU B N   1 
ATOM   7099 C  CA  . GLU B 1 424 ? -24.316 -10.402 52.496  1.00 38.50  ? 424  GLU B CA  1 
ATOM   7100 C  C   . GLU B 1 424 ? -23.796 -11.798 52.826  1.00 37.46  ? 424  GLU B C   1 
ATOM   7101 O  O   . GLU B 1 424 ? -23.028 -12.378 52.046  1.00 36.58  ? 424  GLU B O   1 
ATOM   7102 C  CB  . GLU B 1 424 ? -25.325 -10.470 51.340  1.00 37.13  ? 424  GLU B CB  1 
ATOM   7103 C  CG  . GLU B 1 424 ? -26.471 -11.456 51.589  1.00 44.43  ? 424  GLU B CG  1 
ATOM   7104 C  CD  . GLU B 1 424 ? -27.335 -11.702 50.357  1.00 48.28  ? 424  GLU B CD  1 
ATOM   7105 O  OE1 . GLU B 1 424 ? -26.967 -11.250 49.249  1.00 47.29  ? 424  GLU B OE1 1 
ATOM   7106 O  OE2 . GLU B 1 424 ? -28.392 -12.345 50.506  1.00 52.47  ? 424  GLU B OE2 1 
ATOM   7107 N  N   . ASP B 1 425 ? -24.206 -12.317 53.990  1.00 34.20  ? 425  ASP B N   1 
ATOM   7108 C  CA  . ASP B 1 425 ? -23.954 -13.695 54.419  1.00 33.13  ? 425  ASP B CA  1 
ATOM   7109 C  C   . ASP B 1 425 ? -25.051 -14.572 53.815  1.00 34.03  ? 425  ASP B C   1 
ATOM   7110 O  O   . ASP B 1 425 ? -25.980 -15.034 54.484  1.00 36.13  ? 425  ASP B O   1 
ATOM   7111 C  CB  . ASP B 1 425 ? -23.912 -13.749 55.943  1.00 32.56  ? 425  ASP B CB  1 
ATOM   7112 C  CG  . ASP B 1 425 ? -23.809 -15.156 56.510  1.00 35.47  ? 425  ASP B CG  1 
ATOM   7113 O  OD1 . ASP B 1 425 ? -23.270 -16.074 55.856  1.00 35.23  ? 425  ASP B OD1 1 
ATOM   7114 O  OD2 . ASP B 1 425 ? -24.276 -15.329 57.660  1.00 37.11  ? 425  ASP B OD2 1 
ATOM   7115 N  N   . HIS B 1 426 ? -24.934 -14.781 52.503  1.00 39.03  ? 426  HIS B N   1 
ATOM   7116 C  CA  . HIS B 1 426 ? -26.042 -15.336 51.731  1.00 40.48  ? 426  HIS B CA  1 
ATOM   7117 C  C   . HIS B 1 426 ? -26.274 -16.815 52.009  1.00 39.60  ? 426  HIS B C   1 
ATOM   7118 O  O   . HIS B 1 426 ? -27.387 -17.301 51.783  1.00 38.39  ? 426  HIS B O   1 
ATOM   7119 C  CB  . HIS B 1 426 ? -25.814 -15.110 50.230  1.00 39.73  ? 426  HIS B CB  1 
ATOM   7120 C  CG  . HIS B 1 426 ? -24.622 -15.828 49.684  1.00 36.94  ? 426  HIS B CG  1 
ATOM   7121 N  ND1 . HIS B 1 426 ? -23.328 -15.528 50.065  1.00 35.96  ? 426  HIS B ND1 1 
ATOM   7122 C  CD2 . HIS B 1 426 ? -24.528 -16.842 48.794  1.00 37.72  ? 426  HIS B CD2 1 
ATOM   7123 C  CE1 . HIS B 1 426 ? -22.490 -16.328 49.429  1.00 39.66  ? 426  HIS B CE1 1 
ATOM   7124 N  NE2 . HIS B 1 426 ? -23.192 -17.131 48.648  1.00 36.93  ? 426  HIS B NE2 1 
ATOM   7125 N  N   . THR B 1 427 ? -25.273 -17.540 52.512  1.00 36.79  ? 427  THR B N   1 
ATOM   7126 C  CA  . THR B 1 427 ? -25.459 -18.940 52.874  1.00 35.11  ? 427  THR B CA  1 
ATOM   7127 C  C   . THR B 1 427 ? -25.742 -19.144 54.358  1.00 35.34  ? 427  THR B C   1 
ATOM   7128 O  O   . THR B 1 427 ? -25.900 -20.287 54.787  1.00 37.88  ? 427  THR B O   1 
ATOM   7129 C  CB  . THR B 1 427 ? -24.232 -19.774 52.481  1.00 36.69  ? 427  THR B CB  1 
ATOM   7130 O  OG1 . THR B 1 427 ? -23.152 -19.525 53.400  1.00 36.86  ? 427  THR B OG1 1 
ATOM   7131 C  CG2 . THR B 1 427 ? -23.804 -19.477 51.035  1.00 35.69  ? 427  THR B CG2 1 
ATOM   7132 N  N   . ASN B 1 428 ? -25.853 -18.076 55.140  1.00 36.63  ? 428  ASN B N   1 
ATOM   7133 C  CA  . ASN B 1 428 ? -25.908 -18.190 56.598  1.00 34.80  ? 428  ASN B CA  1 
ATOM   7134 C  C   . ASN B 1 428 ? -24.802 -19.123 57.088  1.00 36.54  ? 428  ASN B C   1 
ATOM   7135 O  O   . ASN B 1 428 ? -25.029 -20.170 57.709  1.00 37.27  ? 428  ASN B O   1 
ATOM   7136 C  CB  . ASN B 1 428 ? -27.287 -18.667 57.077  1.00 38.64  ? 428  ASN B CB  1 
ATOM   7137 C  CG  . ASN B 1 428 ? -27.387 -18.677 58.576  1.00 46.65  ? 428  ASN B CG  1 
ATOM   7138 O  OD1 . ASN B 1 428 ? -26.657 -17.950 59.256  1.00 47.22  ? 428  ASN B OD1 1 
ATOM   7139 N  ND2 . ASN B 1 428 ? -28.290 -19.498 59.113  1.00 54.00  ? 428  ASN B ND2 1 
ATOM   7140 N  N   . TYR B 1 429 ? -23.576 -18.706 56.790  1.00 32.28  ? 429  TYR B N   1 
ATOM   7141 C  CA  . TYR B 1 429 ? -22.414 -19.562 56.939  1.00 34.81  ? 429  TYR B CA  1 
ATOM   7142 C  C   . TYR B 1 429 ? -22.228 -20.019 58.383  1.00 33.84  ? 429  TYR B C   1 
ATOM   7143 O  O   . TYR B 1 429 ? -22.295 -19.216 59.319  1.00 34.29  ? 429  TYR B O   1 
ATOM   7144 C  CB  . TYR B 1 429 ? -21.189 -18.789 56.448  1.00 33.38  ? 429  TYR B CB  1 
ATOM   7145 C  CG  . TYR B 1 429 ? -19.854 -19.377 56.862  1.00 33.11  ? 429  TYR B CG  1 
ATOM   7146 C  CD1 . TYR B 1 429 ? -19.378 -20.538 56.268  1.00 33.29  ? 429  TYR B CD1 1 
ATOM   7147 C  CD2 . TYR B 1 429 ? -19.080 -18.769 57.853  1.00 33.85  ? 429  TYR B CD2 1 
ATOM   7148 C  CE1 . TYR B 1 429 ? -18.148 -21.085 56.640  1.00 32.13  ? 429  TYR B CE1 1 
ATOM   7149 C  CE2 . TYR B 1 429 ? -17.854 -19.303 58.230  1.00 33.13  ? 429  TYR B CE2 1 
ATOM   7150 C  CZ  . TYR B 1 429 ? -17.400 -20.464 57.615  1.00 33.89  ? 429  TYR B CZ  1 
ATOM   7151 O  OH  . TYR B 1 429 ? -16.188 -21.012 57.978  1.00 32.86  ? 429  TYR B OH  1 
ATOM   7152 N  N   . GLU B 1 430 ? -21.956 -21.311 58.564  1.00 33.66  ? 430  GLU B N   1 
ATOM   7153 C  CA  . GLU B 1 430 ? -21.674 -21.858 59.887  1.00 35.26  ? 430  GLU B CA  1 
ATOM   7154 C  C   . GLU B 1 430 ? -20.165 -21.892 60.084  1.00 35.65  ? 430  GLU B C   1 
ATOM   7155 O  O   . GLU B 1 430 ? -19.450 -22.542 59.313  1.00 36.10  ? 430  GLU B O   1 
ATOM   7156 C  CB  . GLU B 1 430 ? -22.257 -23.261 60.047  1.00 38.97  ? 430  GLU B CB  1 
ATOM   7157 C  CG  . GLU B 1 430 ? -21.962 -23.857 61.413  1.00 45.89  ? 430  GLU B CG  1 
ATOM   7158 C  CD  . GLU B 1 430 ? -22.375 -25.308 61.505  1.00 61.43  ? 430  GLU B CD  1 
ATOM   7159 O  OE1 . GLU B 1 430 ? -23.473 -25.647 61.002  1.00 63.16  ? 430  GLU B OE1 1 
ATOM   7160 O  OE2 . GLU B 1 430 ? -21.600 -26.106 62.080  1.00 67.96  ? 430  GLU B OE2 1 
ATOM   7161 N  N   . LEU B 1 431 ? -19.686 -21.208 61.114  1.00 34.59  ? 431  LEU B N   1 
ATOM   7162 C  CA  . LEU B 1 431 ? -18.249 -21.070 61.294  1.00 33.16  ? 431  LEU B CA  1 
ATOM   7163 C  C   . LEU B 1 431 ? -17.601 -22.441 61.360  1.00 33.73  ? 431  LEU B C   1 
ATOM   7164 O  O   . LEU B 1 431 ? -18.018 -23.304 62.138  1.00 36.90  ? 431  LEU B O   1 
ATOM   7165 C  CB  . LEU B 1 431 ? -17.943 -20.269 62.560  1.00 36.74  ? 431  LEU B CB  1 
ATOM   7166 C  CG  . LEU B 1 431 ? -16.467 -19.988 62.850  1.00 37.11  ? 431  LEU B CG  1 
ATOM   7167 C  CD1 . LEU B 1 431 ? -15.844 -19.291 61.659  1.00 34.93  ? 431  LEU B CD1 1 
ATOM   7168 C  CD2 . LEU B 1 431 ? -16.339 -19.149 64.112  1.00 37.10  ? 431  LEU B CD2 1 
ATOM   7169 N  N   . ASP B 1 432 ? -16.575 -22.630 60.533  1.00 31.42  ? 432  ASP B N   1 
ATOM   7170 C  CA  . ASP B 1 432 ? -15.796 -23.860 60.474  1.00 32.86  ? 432  ASP B CA  1 
ATOM   7171 C  C   . ASP B 1 432 ? -14.340 -23.421 60.468  1.00 31.60  ? 432  ASP B C   1 
ATOM   7172 O  O   . ASP B 1 432 ? -13.887 -22.796 59.501  1.00 31.88  ? 432  ASP B O   1 
ATOM   7173 C  CB  . ASP B 1 432 ? -16.171 -24.655 59.220  1.00 34.20  ? 432  ASP B CB  1 
ATOM   7174 C  CG  . ASP B 1 432 ? -15.455 -25.984 59.109  1.00 40.11  ? 432  ASP B CG  1 
ATOM   7175 O  OD1 . ASP B 1 432 ? -14.729 -26.376 60.039  1.00 40.71  ? 432  ASP B OD1 1 
ATOM   7176 O  OD2 . ASP B 1 432 ? -15.637 -26.650 58.061  1.00 40.36  ? 432  ASP B OD2 1 
ATOM   7177 N  N   . ILE B 1 433 ? -13.627 -23.673 61.562  1.00 32.75  ? 433  ILE B N   1 
ATOM   7178 C  CA  . ILE B 1 433 ? -12.275 -23.142 61.721  1.00 30.82  ? 433  ILE B CA  1 
ATOM   7179 C  C   . ILE B 1 433 ? -11.291 -24.240 61.357  1.00 33.78  ? 433  ILE B C   1 
ATOM   7180 O  O   . ILE B 1 433 ? -11.151 -25.225 62.092  1.00 35.37  ? 433  ILE B O   1 
ATOM   7181 C  CB  . ILE B 1 433 ? -12.030 -22.618 63.140  1.00 31.44  ? 433  ILE B CB  1 
ATOM   7182 C  CG1 . ILE B 1 433 ? -12.957 -21.434 63.430  1.00 32.30  ? 433  ILE B CG1 1 
ATOM   7183 C  CG2 . ILE B 1 433 ? -10.573 -22.169 63.276  1.00 32.87  ? 433  ILE B CG2 1 
ATOM   7184 C  CD1 . ILE B 1 433 ? -12.919 -20.983 64.880  1.00 32.14  ? 433  ILE B CD1 1 
ATOM   7185 N  N   . LYS B 1 434 ? -10.604 -24.055 60.221  1.00 31.93  ? 434  LYS B N   1 
ATOM   7186 C  CA  . LYS B 1 434 ? -9.571  -24.974 59.767  1.00 34.15  ? 434  LYS B CA  1 
ATOM   7187 C  C   . LYS B 1 434 ? -8.279  -24.699 60.518  1.00 33.72  ? 434  LYS B C   1 
ATOM   7188 O  O   . LYS B 1 434 ? -7.918  -23.543 60.750  1.00 34.19  ? 434  LYS B O   1 
ATOM   7189 C  CB  . LYS B 1 434 ? -9.331  -24.819 58.264  1.00 31.04  ? 434  LYS B CB  1 
ATOM   7190 C  CG  . LYS B 1 434 ? -8.307  -25.812 57.680  1.00 33.92  ? 434  LYS B CG  1 
ATOM   7191 C  CD  . LYS B 1 434 ? -8.151  -25.571 56.166  1.00 40.22  ? 434  LYS B CD  1 
ATOM   7192 C  CE  . LYS B 1 434 ? -7.010  -26.387 55.552  1.00 48.32  ? 434  LYS B CE  1 
ATOM   7193 N  NZ  . LYS B 1 434 ? -7.238  -27.858 55.725  1.00 51.80  ? 434  LYS B NZ  1 
ATOM   7194 N  N   . GLU B 1 435 ? -7.586  -25.764 60.897  1.00 31.95  ? 435  GLU B N   1 
ATOM   7195 C  CA  . GLU B 1 435 ? -6.373  -25.644 61.691  1.00 32.70  ? 435  GLU B CA  1 
ATOM   7196 C  C   . GLU B 1 435 ? -5.186  -26.103 60.861  1.00 33.25  ? 435  GLU B C   1 
ATOM   7197 O  O   . GLU B 1 435 ? -5.215  -27.201 60.291  1.00 32.91  ? 435  GLU B O   1 
ATOM   7198 C  CB  . GLU B 1 435 ? -6.486  -26.454 62.984  1.00 31.59  ? 435  GLU B CB  1 
ATOM   7199 C  CG  . GLU B 1 435 ? -7.603  -25.919 63.905  1.00 29.55  ? 435  GLU B CG  1 
ATOM   7200 C  CD  . GLU B 1 435 ? -7.394  -26.280 65.362  1.00 33.27  ? 435  GLU B CD  1 
ATOM   7201 O  OE1 . GLU B 1 435 ? -6.246  -26.592 65.747  1.00 31.56  ? 435  GLU B OE1 1 
ATOM   7202 O  OE2 . GLU B 1 435 ? -8.375  -26.233 66.133  1.00 31.72  ? 435  GLU B OE2 1 
ATOM   7203 N  N   . THR B 1 436 ? -4.161  -25.247 60.790  1.00 31.63  ? 436  THR B N   1 
ATOM   7204 C  CA  . THR B 1 436 ? -2.884  -25.525 60.136  1.00 32.66  ? 436  THR B CA  1 
ATOM   7205 C  C   . THR B 1 436 ? -1.772  -25.008 61.040  1.00 30.86  ? 436  THR B C   1 
ATOM   7206 O  O   . THR B 1 436 ? -0.872  -24.288 60.603  1.00 33.44  ? 436  THR B O   1 
ATOM   7207 C  CB  . THR B 1 436 ? -2.790  -24.886 58.745  1.00 32.86  ? 436  THR B CB  1 
ATOM   7208 O  OG1 . THR B 1 436 ? -3.060  -23.477 58.838  1.00 34.03  ? 436  THR B OG1 1 
ATOM   7209 C  CG2 . THR B 1 436 ? -3.783  -25.556 57.757  1.00 32.73  ? 436  THR B CG2 1 
ATOM   7210 N  N   . LEU B 1 437 ? -1.867  -25.361 62.327  1.00 29.39  ? 437  LEU B N   1 
ATOM   7211 C  CA  . LEU B 1 437 ? -1.183  -24.683 63.429  1.00 32.00  ? 437  LEU B CA  1 
ATOM   7212 C  C   . LEU B 1 437 ? -1.864  -23.333 63.653  1.00 33.18  ? 437  LEU B C   1 
ATOM   7213 O  O   . LEU B 1 437 ? -2.371  -23.046 64.752  1.00 31.61  ? 437  LEU B O   1 
ATOM   7214 C  CB  . LEU B 1 437 ? 0.327   -24.522 63.160  1.00 31.73  ? 437  LEU B CB  1 
ATOM   7215 C  CG  . LEU B 1 437 ? 1.108   -25.816 62.835  1.00 32.37  ? 437  LEU B CG  1 
ATOM   7216 C  CD1 . LEU B 1 437 ? 2.607   -25.520 62.667  1.00 33.10  ? 437  LEU B CD1 1 
ATOM   7217 C  CD2 . LEU B 1 437 ? 0.885   -26.941 63.878  1.00 30.79  ? 437  LEU B CD2 1 
ATOM   7218 N  N   . THR B 1 438 ? -1.897  -22.516 62.607  1.00 33.62  ? 438  THR B N   1 
ATOM   7219 C  CA  . THR B 1 438 ? -2.693  -21.297 62.573  1.00 31.33  ? 438  THR B CA  1 
ATOM   7220 C  C   . THR B 1 438 ? -4.171  -21.631 62.362  1.00 31.65  ? 438  THR B C   1 
ATOM   7221 O  O   . THR B 1 438 ? -4.540  -22.769 62.058  1.00 32.72  ? 438  THR B O   1 
ATOM   7222 C  CB  . THR B 1 438 ? -2.197  -20.387 61.459  1.00 33.61  ? 438  THR B CB  1 
ATOM   7223 O  OG1 . THR B 1 438 ? -2.236  -21.095 60.216  1.00 31.69  ? 438  THR B OG1 1 
ATOM   7224 C  CG2 . THR B 1 438 ? -0.744  -19.966 61.736  1.00 31.18  ? 438  THR B CG2 1 
ATOM   7225 N  N   . LEU B 1 439 ? -5.022  -20.617 62.535  1.00 32.52  ? 439  LEU B N   1 
ATOM   7226 C  CA  . LEU B 1 439 ? -6.469  -20.768 62.471  1.00 31.16  ? 439  LEU B CA  1 
ATOM   7227 C  C   . LEU B 1 439 ? -7.039  -19.871 61.388  1.00 32.29  ? 439  LEU B C   1 
ATOM   7228 O  O   . LEU B 1 439 ? -6.627  -18.713 61.251  1.00 31.38  ? 439  LEU B O   1 
ATOM   7229 C  CB  . LEU B 1 439 ? -7.113  -20.401 63.804  1.00 28.77  ? 439  LEU B CB  1 
ATOM   7230 C  CG  . LEU B 1 439 ? -6.603  -21.120 65.057  1.00 31.72  ? 439  LEU B CG  1 
ATOM   7231 C  CD1 . LEU B 1 439 ? -7.352  -20.625 66.296  1.00 31.85  ? 439  LEU B CD1 1 
ATOM   7232 C  CD2 . LEU B 1 439 ? -6.767  -22.618 64.891  1.00 32.76  ? 439  LEU B CD2 1 
ATOM   7233 N  N   . LYS B 1 440 ? -8.032  -20.388 60.647  1.00 31.68  ? 440  LYS B N   1 
ATOM   7234 C  CA  . LYS B 1 440 ? -8.675  -19.581 59.611  1.00 29.91  ? 440  LYS B CA  1 
ATOM   7235 C  C   . LYS B 1 440 ? -10.042 -20.180 59.304  1.00 32.55  ? 440  LYS B C   1 
ATOM   7236 O  O   . LYS B 1 440 ? -10.159 -21.412 59.278  1.00 32.68  ? 440  LYS B O   1 
ATOM   7237 C  CB  . LYS B 1 440 ? -7.799  -19.545 58.341  1.00 33.38  ? 440  LYS B CB  1 
ATOM   7238 C  CG  . LYS B 1 440 ? -8.224  -18.516 57.293  1.00 36.15  ? 440  LYS B CG  1 
ATOM   7239 C  CD  . LYS B 1 440 ? -7.344  -18.588 56.029  1.00 37.75  ? 440  LYS B CD  1 
ATOM   7240 C  CE  . LYS B 1 440 ? -5.866  -18.505 56.378  1.00 40.16  ? 440  LYS B CE  1 
ATOM   7241 N  NZ  . LYS B 1 440 ? -5.221  -19.858 56.266  1.00 41.11  ? 440  LYS B NZ  1 
ATOM   7242 N  N   . PRO B 1 441 ? -11.082 -19.378 59.060  1.00 32.78  ? 441  PRO B N   1 
ATOM   7243 C  CA  . PRO B 1 441 ? -12.340 -19.972 58.585  1.00 33.41  ? 441  PRO B CA  1 
ATOM   7244 C  C   . PRO B 1 441 ? -12.134 -20.714 57.273  1.00 33.99  ? 441  PRO B C   1 
ATOM   7245 O  O   . PRO B 1 441 ? -11.362 -20.292 56.406  1.00 32.25  ? 441  PRO B O   1 
ATOM   7246 C  CB  . PRO B 1 441 ? -13.264 -18.766 58.392  1.00 32.78  ? 441  PRO B CB  1 
ATOM   7247 C  CG  . PRO B 1 441 ? -12.693 -17.675 59.251  1.00 33.09  ? 441  PRO B CG  1 
ATOM   7248 C  CD  . PRO B 1 441 ? -11.184 -17.910 59.162  1.00 32.12  ? 441  PRO B CD  1 
ATOM   7249 N  N   . GLU B 1 442 ? -12.839 -21.830 57.132  1.00 32.74  ? 442  GLU B N   1 
ATOM   7250 C  CA  . GLU B 1 442 ? -12.909 -22.584 55.890  1.00 31.68  ? 442  GLU B CA  1 
ATOM   7251 C  C   . GLU B 1 442 ? -14.315 -22.521 55.303  1.00 31.78  ? 442  GLU B C   1 
ATOM   7252 O  O   . GLU B 1 442 ? -15.305 -22.583 56.037  1.00 33.95  ? 442  GLU B O   1 
ATOM   7253 C  CB  . GLU B 1 442 ? -12.482 -24.033 56.135  1.00 36.30  ? 442  GLU B CB  1 
ATOM   7254 C  CG  . GLU B 1 442 ? -12.644 -24.937 54.958  1.00 41.11  ? 442  GLU B CG  1 
ATOM   7255 C  CD  . GLU B 1 442 ? -11.950 -26.258 55.173  1.00 44.96  ? 442  GLU B CD  1 
ATOM   7256 O  OE1 . GLU B 1 442 ? -12.039 -26.829 56.278  1.00 43.77  ? 442  GLU B OE1 1 
ATOM   7257 O  OE2 . GLU B 1 442 ? -11.367 -26.749 54.188  1.00 54.63  ? 442  GLU B OE2 1 
ATOM   7258 N  N   . GLY B 1 443 ? -14.393 -22.396 53.982  1.00 33.89  ? 443  GLY B N   1 
ATOM   7259 C  CA  . GLY B 1 443 ? -15.683 -22.414 53.318  1.00 34.84  ? 443  GLY B CA  1 
ATOM   7260 C  C   . GLY B 1 443 ? -16.499 -21.162 53.517  1.00 35.49  ? 443  GLY B C   1 
ATOM   7261 O  O   . GLY B 1 443 ? -17.688 -21.156 53.186  1.00 35.83  ? 443  GLY B O   1 
ATOM   7262 N  N   . PHE B 1 444 ? -15.902 -20.111 54.066  1.00 35.15  ? 444  PHE B N   1 
ATOM   7263 C  CA  . PHE B 1 444 ? -16.607 -18.858 54.303  1.00 35.72  ? 444  PHE B CA  1 
ATOM   7264 C  C   . PHE B 1 444 ? -16.733 -18.109 52.980  1.00 35.05  ? 444  PHE B C   1 
ATOM   7265 O  O   . PHE B 1 444 ? -15.727 -17.794 52.336  1.00 33.12  ? 444  PHE B O   1 
ATOM   7266 C  CB  . PHE B 1 444 ? -15.851 -18.041 55.351  1.00 35.06  ? 444  PHE B CB  1 
ATOM   7267 C  CG  . PHE B 1 444 ? -16.447 -16.681 55.641  1.00 33.31  ? 444  PHE B CG  1 
ATOM   7268 C  CD1 . PHE B 1 444 ? -17.822 -16.488 55.671  1.00 32.49  ? 444  PHE B CD1 1 
ATOM   7269 C  CD2 . PHE B 1 444 ? -15.620 -15.600 55.908  1.00 30.28  ? 444  PHE B CD2 1 
ATOM   7270 C  CE1 . PHE B 1 444 ? -18.346 -15.232 55.945  1.00 32.64  ? 444  PHE B CE1 1 
ATOM   7271 C  CE2 . PHE B 1 444 ? -16.126 -14.356 56.182  1.00 31.48  ? 444  PHE B CE2 1 
ATOM   7272 C  CZ  . PHE B 1 444 ? -17.501 -14.161 56.202  1.00 32.71  ? 444  PHE B CZ  1 
ATOM   7273 N  N   . VAL B 1 445 ? -17.966 -17.855 52.563  1.00 34.36  ? 445  VAL B N   1 
ATOM   7274 C  CA  . VAL B 1 445 ? -18.274 -17.152 51.333  1.00 32.11  ? 445  VAL B CA  1 
ATOM   7275 C  C   . VAL B 1 445 ? -19.290 -16.061 51.651  1.00 33.82  ? 445  VAL B C   1 
ATOM   7276 O  O   . VAL B 1 445 ? -20.092 -16.190 52.584  1.00 35.57  ? 445  VAL B O   1 
ATOM   7277 C  CB  . VAL B 1 445 ? -18.824 -18.108 50.252  1.00 35.68  ? 445  VAL B CB  1 
ATOM   7278 C  CG1 . VAL B 1 445 ? -17.742 -19.094 49.811  1.00 35.27  ? 445  VAL B CG1 1 
ATOM   7279 C  CG2 . VAL B 1 445 ? -20.048 -18.865 50.796  1.00 38.74  ? 445  VAL B CG2 1 
ATOM   7280 N  N   . VAL B 1 446 ? -19.262 -14.991 50.848  1.00 32.84  ? 446  VAL B N   1 
ATOM   7281 C  CA  . VAL B 1 446 ? -20.187 -13.871 50.974  1.00 36.96  ? 446  VAL B CA  1 
ATOM   7282 C  C   . VAL B 1 446 ? -20.498 -13.351 49.575  1.00 36.01  ? 446  VAL B C   1 
ATOM   7283 O  O   . VAL B 1 446 ? -19.802 -13.656 48.604  1.00 36.00  ? 446  VAL B O   1 
ATOM   7284 C  CB  . VAL B 1 446 ? -19.625 -12.728 51.851  1.00 33.96  ? 446  VAL B CB  1 
ATOM   7285 C  CG1 . VAL B 1 446 ? -19.320 -13.226 53.280  1.00 35.06  ? 446  VAL B CG1 1 
ATOM   7286 C  CG2 . VAL B 1 446 ? -18.369 -12.103 51.202  1.00 33.99  ? 446  VAL B CG2 1 
ATOM   7287 N  N   . LYS B 1 447 ? -21.558 -12.553 49.479  1.00 34.87  ? 447  LYS B N   1 
ATOM   7288 C  CA  . LYS B 1 447 ? -21.805 -11.746 48.294  1.00 33.89  ? 447  LYS B CA  1 
ATOM   7289 C  C   . LYS B 1 447 ? -21.555 -10.282 48.629  1.00 36.68  ? 447  LYS B C   1 
ATOM   7290 O  O   . LYS B 1 447 ? -21.887 -9.815  49.727  1.00 36.91  ? 447  LYS B O   1 
ATOM   7291 C  CB  . LYS B 1 447 ? -23.234 -11.937 47.756  1.00 36.15  ? 447  LYS B CB  1 
ATOM   7292 C  CG  . LYS B 1 447 ? -23.465 -13.321 47.162  1.00 40.11  ? 447  LYS B CG  1 
ATOM   7293 C  CD  . LYS B 1 447 ? -24.887 -13.474 46.638  1.00 41.11  ? 447  LYS B CD  1 
ATOM   7294 C  CE  . LYS B 1 447 ? -25.047 -14.792 45.899  1.00 44.28  ? 447  LYS B CE  1 
ATOM   7295 N  NZ  . LYS B 1 447 ? -26.446 -14.922 45.401  1.00 50.39  ? 447  LYS B NZ  1 
ATOM   7296 N  N   . ALA B 1 448 ? -20.936 -9.575  47.692  1.00 35.64  ? 448  ALA B N   1 
ATOM   7297 C  CA  . ALA B 1 448 ? -20.623 -8.166  47.841  1.00 39.52  ? 448  ALA B CA  1 
ATOM   7298 C  C   . ALA B 1 448 ? -21.466 -7.394  46.847  1.00 46.18  ? 448  ALA B C   1 
ATOM   7299 O  O   . ALA B 1 448 ? -21.496 -7.730  45.659  1.00 49.91  ? 448  ALA B O   1 
ATOM   7300 C  CB  . ALA B 1 448 ? -19.131 -7.892  47.617  1.00 41.24  ? 448  ALA B CB  1 
ATOM   7301 N  N   . LYS B 1 449 ? -22.173 -6.394  47.332  1.00 39.93  ? 449  LYS B N   1 
ATOM   7302 C  CA  . LYS B 1 449 ? -22.934 -5.500  46.473  1.00 41.84  ? 449  LYS B CA  1 
ATOM   7303 C  C   . LYS B 1 449 ? -22.181 -4.181  46.423  1.00 37.55  ? 449  LYS B C   1 
ATOM   7304 O  O   . LYS B 1 449 ? -22.066 -3.494  47.441  1.00 37.68  ? 449  LYS B O   1 
ATOM   7305 C  CB  . LYS B 1 449 ? -24.350 -5.313  47.002  1.00 46.08  ? 449  LYS B CB  1 
ATOM   7306 C  CG  . LYS B 1 449 ? -25.386 -5.072  45.928  1.00 53.33  ? 449  LYS B CG  1 
ATOM   7307 C  CD  . LYS B 1 449 ? -26.225 -3.853  46.263  1.00 57.89  ? 449  LYS B CD  1 
ATOM   7308 C  CE  . LYS B 1 449 ? -27.143 -3.473  45.108  1.00 62.05  ? 449  LYS B CE  1 
ATOM   7309 N  NZ  . LYS B 1 449 ? -28.078 -2.381  45.508  1.00 69.18  ? 449  LYS B NZ  1 
ATOM   7310 N  N   . SER B 1 450 ? -21.663 -3.843  45.249  1.00 39.32  ? 450  SER B N   1 
ATOM   7311 C  CA  . SER B 1 450 ? -20.866 -2.637  45.085  1.00 38.29  ? 450  SER B CA  1 
ATOM   7312 C  C   . SER B 1 450 ? -21.665 -1.392  45.441  1.00 40.93  ? 450  SER B C   1 
ATOM   7313 O  O   . SER B 1 450 ? -22.835 -1.251  45.064  1.00 41.57  ? 450  SER B O   1 
ATOM   7314 C  CB  . SER B 1 450 ? -20.377 -2.526  43.641  1.00 39.08  ? 450  SER B CB  1 
ATOM   7315 O  OG  . SER B 1 450 ? -19.609 -1.357  43.465  1.00 37.23  ? 450  SER B OG  1 
ATOM   7316 N  N   . LYS B 1 451 ? -21.028 -0.484  46.172  1.00 37.88  ? 451  LYS B N   1 
ATOM   7317 C  CA  . LYS B 1 451 ? -21.583 0.851   46.347  1.00 40.70  ? 451  LYS B CA  1 
ATOM   7318 C  C   . LYS B 1 451 ? -21.225 1.773   45.189  1.00 42.00  ? 451  LYS B C   1 
ATOM   7319 O  O   . LYS B 1 451 ? -21.567 2.959   45.233  1.00 44.86  ? 451  LYS B O   1 
ATOM   7320 C  CB  . LYS B 1 451 ? -21.111 1.449   47.676  1.00 39.60  ? 451  LYS B CB  1 
ATOM   7321 C  CG  . LYS B 1 451 ? -21.447 0.584   48.885  1.00 42.24  ? 451  LYS B CG  1 
ATOM   7322 C  CD  . LYS B 1 451 ? -20.846 1.165   50.157  1.00 41.56  ? 451  LYS B CD  1 
ATOM   7323 C  CE  . LYS B 1 451 ? -21.451 0.526   51.386  1.00 44.24  ? 451  LYS B CE  1 
ATOM   7324 N  NZ  . LYS B 1 451 ? -22.793 1.096   51.661  1.00 53.43  ? 451  LYS B NZ  1 
ATOM   7325 N  N   . LYS B 1 452 ? -20.545 1.251   44.166  1.00 38.84  ? 452  LYS B N   1 
ATOM   7326 C  CA  . LYS B 1 452 ? -20.229 1.991   42.937  1.00 43.62  ? 452  LYS B CA  1 
ATOM   7327 C  C   . LYS B 1 452 ? -19.489 3.290   43.240  1.00 46.27  ? 452  LYS B C   1 
ATOM   7328 O  O   . LYS B 1 452 ? -19.805 4.357   42.703  1.00 45.17  ? 452  LYS B O   1 
ATOM   7329 C  CB  . LYS B 1 452 ? -21.490 2.269   42.107  1.00 41.96  ? 452  LYS B CB  1 
ATOM   7330 C  CG  . LYS B 1 452 ? -22.240 1.029   41.621  1.00 45.58  ? 452  LYS B CG  1 
ATOM   7331 C  CD  . LYS B 1 452 ? -21.440 0.193   40.632  1.00 49.45  ? 452  LYS B CD  1 
ATOM   7332 C  CE  . LYS B 1 452 ? -22.221 -1.066  40.238  1.00 52.44  ? 452  LYS B CE  1 
ATOM   7333 N  NZ  . LYS B 1 452 ? -21.378 -2.094  39.556  1.00 51.46  ? 452  LYS B NZ  1 
ATOM   7334 N  N   . ILE B 1 453 ? -18.475 3.193   44.091  1.00 40.91  ? 453  ILE B N   1 
ATOM   7335 C  CA  . ILE B 1 453 ? -17.619 4.324   44.435  1.00 39.47  ? 453  ILE B CA  1 
ATOM   7336 C  C   . ILE B 1 453 ? -16.323 4.177   43.647  1.00 41.51  ? 453  ILE B C   1 
ATOM   7337 O  O   . ILE B 1 453 ? -15.640 3.148   43.792  1.00 41.39  ? 453  ILE B O   1 
ATOM   7338 C  CB  . ILE B 1 453 ? -17.340 4.385   45.946  1.00 41.57  ? 453  ILE B CB  1 
ATOM   7339 C  CG1 . ILE B 1 453 ? -18.651 4.487   46.717  1.00 43.21  ? 453  ILE B CG1 1 
ATOM   7340 C  CG2 . ILE B 1 453 ? -16.452 5.584   46.269  1.00 40.04  ? 453  ILE B CG2 1 
ATOM   7341 C  CD1 . ILE B 1 453 ? -18.482 4.385   48.218  1.00 44.35  ? 453  ILE B CD1 1 
ATOM   7342 N  N   . PRO B 1 454 ? -15.956 5.146   42.809  1.00 44.56  ? 454  PRO B N   1 
ATOM   7343 C  CA  . PRO B 1 454 ? -14.801 4.962   41.924  1.00 46.18  ? 454  PRO B CA  1 
ATOM   7344 C  C   . PRO B 1 454 ? -13.494 4.840   42.686  1.00 45.70  ? 454  PRO B C   1 
ATOM   7345 O  O   . PRO B 1 454 ? -13.331 5.374   43.789  1.00 46.13  ? 454  PRO B O   1 
ATOM   7346 C  CB  . PRO B 1 454 ? -14.812 6.231   41.059  1.00 45.78  ? 454  PRO B CB  1 
ATOM   7347 C  CG  . PRO B 1 454 ? -16.220 6.710   41.109  1.00 46.89  ? 454  PRO B CG  1 
ATOM   7348 C  CD  . PRO B 1 454 ? -16.719 6.364   42.477  1.00 48.00  ? 454  PRO B CD  1 
ATOM   7349 N  N   . LEU B 1 455 ? -12.559 4.115   42.074  1.00 41.45  ? 455  LEU B N   1 
ATOM   7350 C  CA  . LEU B 1 455 ? -11.176 4.030   42.546  1.00 43.88  ? 455  LEU B CA  1 
ATOM   7351 C  C   . LEU B 1 455 ? -10.295 5.025   41.804  1.00 47.36  ? 455  LEU B C   1 
ATOM   7352 O  O   . LEU B 1 455 ? -10.757 5.767   40.932  1.00 50.41  ? 455  LEU B O   1 
ATOM   7353 C  CB  . LEU B 1 455 ? -10.617 2.623   42.351  1.00 41.89  ? 455  LEU B CB  1 
ATOM   7354 C  CG  . LEU B 1 455 ? -11.109 1.566   43.327  1.00 44.07  ? 455  LEU B CG  1 
ATOM   7355 C  CD1 . LEU B 1 455 ? -10.765 0.164   42.808  1.00 42.44  ? 455  LEU B CD1 1 
ATOM   7356 C  CD2 . LEU B 1 455 ? -10.473 1.832   44.680  1.00 43.05  ? 455  LEU B CD2 1 
ATOM   7357 O  OXT . LEU B 1 455 ? -9.093  5.092   42.057  1.00 48.16  ? 455  LEU B OXT 1 
HETATM 7358 C  CHA . HEM C 2 .   ? -17.916 -13.882 8.862   1.00 30.83  ? 501  HEM A CHA 1 
HETATM 7359 C  CHB . HEM C 2 .   ? -13.106 -13.324 9.210   1.00 32.72  ? 501  HEM A CHB 1 
HETATM 7360 C  CHC . HEM C 2 .   ? -13.700 -10.983 13.513  1.00 29.94  ? 501  HEM A CHC 1 
HETATM 7361 C  CHD . HEM C 2 .   ? -18.479 -11.844 13.279  1.00 32.59  ? 501  HEM A CHD 1 
HETATM 7362 C  C1A . HEM C 2 .   ? -16.554 -13.914 8.596   1.00 28.42  ? 501  HEM A C1A 1 
HETATM 7363 C  C2A . HEM C 2 .   ? -15.981 -14.477 7.411   1.00 31.06  ? 501  HEM A C2A 1 
HETATM 7364 C  C3A . HEM C 2 .   ? -14.631 -14.330 7.516   1.00 30.10  ? 501  HEM A C3A 1 
HETATM 7365 C  C4A . HEM C 2 .   ? -14.370 -13.664 8.741   1.00 29.65  ? 501  HEM A C4A 1 
HETATM 7366 C  CMA . HEM C 2 .   ? -13.595 -14.791 6.496   1.00 30.34  ? 501  HEM A CMA 1 
HETATM 7367 C  CAA . HEM C 2 .   ? -16.695 -15.147 6.249   1.00 31.37  ? 501  HEM A CAA 1 
HETATM 7368 C  CBA . HEM C 2 .   ? -16.921 -16.648 6.534   1.00 30.65  ? 501  HEM A CBA 1 
HETATM 7369 C  CGA . HEM C 2 .   ? -17.475 -17.424 5.352   1.00 29.55  ? 501  HEM A CGA 1 
HETATM 7370 O  O1A . HEM C 2 .   ? -17.746 -18.643 5.477   1.00 32.22  ? 501  HEM A O1A 1 
HETATM 7371 O  O2A . HEM C 2 .   ? -17.656 -16.888 4.235   1.00 30.18  ? 501  HEM A O2A 1 
HETATM 7372 C  C1B . HEM C 2 .   ? -12.892 -12.654 10.432  1.00 33.33  ? 501  HEM A C1B 1 
HETATM 7373 C  C2B . HEM C 2 .   ? -11.585 -12.315 10.914  1.00 30.02  ? 501  HEM A C2B 1 
HETATM 7374 C  C3B . HEM C 2 .   ? -11.747 -11.670 12.113  1.00 28.85  ? 501  HEM A C3B 1 
HETATM 7375 C  C4B . HEM C 2 .   ? -13.192 -11.596 12.363  1.00 30.63  ? 501  HEM A C4B 1 
HETATM 7376 C  CMB . HEM C 2 .   ? -10.248 -12.628 10.238  1.00 31.67  ? 501  HEM A CMB 1 
HETATM 7377 C  CAB . HEM C 2 .   ? -10.760 -11.099 13.062  1.00 31.80  ? 501  HEM A CAB 1 
HETATM 7378 C  CBB . HEM C 2 .   ? -9.595  -10.597 12.644  1.00 34.81  ? 501  HEM A CBB 1 
HETATM 7379 C  C1C . HEM C 2 .   ? -15.067 -10.996 13.830  1.00 27.49  ? 501  HEM A C1C 1 
HETATM 7380 C  C2C . HEM C 2 .   ? -15.662 -10.420 14.979  1.00 29.65  ? 501  HEM A C2C 1 
HETATM 7381 C  C3C . HEM C 2 .   ? -17.022 -10.681 14.911  1.00 30.76  ? 501  HEM A C3C 1 
HETATM 7382 C  C4C . HEM C 2 .   ? -17.244 -11.392 13.690  1.00 33.81  ? 501  HEM A C4C 1 
HETATM 7383 C  CMC . HEM C 2 .   ? -14.950 -9.692  16.081  1.00 33.31  ? 501  HEM A CMC 1 
HETATM 7384 C  CAC . HEM C 2 .   ? -18.072 -10.275 15.878  1.00 27.67  ? 501  HEM A CAC 1 
HETATM 7385 C  CBC . HEM C 2 .   ? -17.985 -9.193  16.647  1.00 32.09  ? 501  HEM A CBC 1 
HETATM 7386 C  C1D . HEM C 2 .   ? -18.646 -12.493 12.047  1.00 30.45  ? 501  HEM A C1D 1 
HETATM 7387 C  C2D . HEM C 2 .   ? -19.975 -12.954 11.641  1.00 31.06  ? 501  HEM A C2D 1 
HETATM 7388 C  C3D . HEM C 2 .   ? -19.829 -13.518 10.425  1.00 29.44  ? 501  HEM A C3D 1 
HETATM 7389 C  C4D . HEM C 2 .   ? -18.400 -13.389 10.075  1.00 28.49  ? 501  HEM A C4D 1 
HETATM 7390 C  CMD . HEM C 2 .   ? -21.281 -12.832 12.411  1.00 29.64  ? 501  HEM A CMD 1 
HETATM 7391 C  CAD . HEM C 2 .   ? -20.954 -14.078 9.592   1.00 29.68  ? 501  HEM A CAD 1 
HETATM 7392 C  CBD . HEM C 2 .   ? -21.485 -12.893 8.759   1.00 31.70  ? 501  HEM A CBD 1 
HETATM 7393 C  CGD . HEM C 2 .   ? -22.659 -13.214 7.854   1.00 32.12  ? 501  HEM A CGD 1 
HETATM 7394 O  O1D . HEM C 2 .   ? -22.549 -14.060 6.928   1.00 31.29  ? 501  HEM A O1D 1 
HETATM 7395 O  O2D . HEM C 2 .   ? -23.741 -12.586 7.995   1.00 33.75  ? 501  HEM A O2D 1 
HETATM 7396 N  NA  . HEM C 2 .   ? -15.554 -13.380 9.395   1.00 31.57  ? 501  HEM A NA  1 
HETATM 7397 N  NB  . HEM C 2 .   ? -13.800 -12.207 11.329  1.00 29.29  ? 501  HEM A NB  1 
HETATM 7398 N  NC  . HEM C 2 .   ? -16.030 -11.581 13.051  1.00 30.57  ? 501  HEM A NC  1 
HETATM 7399 N  ND  . HEM C 2 .   ? -17.739 -12.769 11.078  1.00 26.49  ? 501  HEM A ND  1 
HETATM 7400 FE FE  . HEM C 2 .   ? -15.867 -12.335 11.096  1.00 30.64  ? 501  HEM A FE  1 
HETATM 7401 C  C1  . D0L D 3 .   ? -12.919 -30.600 1.733   1.00 41.09  ? 502  D0L A C1  1 
HETATM 7402 C  C2  . D0L D 3 .   ? -12.908 -30.757 3.119   1.00 36.95  ? 502  D0L A C2  1 
HETATM 7403 C  C15 . D0L D 3 .   ? -11.454 -24.447 6.295   1.00 36.75  ? 502  D0L A C15 1 
HETATM 7404 C  C14 . D0L D 3 .   ? -10.357 -25.817 7.957   1.00 35.37  ? 502  D0L A C14 1 
HETATM 7405 C  C7  . D0L D 3 .   ? -12.214 -29.758 4.022   1.00 38.39  ? 502  D0L A C7  1 
HETATM 7406 C  C12 . D0L D 3 .   ? -9.167  -27.283 6.455   1.00 35.18  ? 502  D0L A C12 1 
HETATM 7407 C  C10 . D0L D 3 .   ? -10.829 -26.978 4.580   1.00 37.10  ? 502  D0L A C10 1 
HETATM 7408 C  C3  . D0L D 3 .   ? -13.511 -31.884 3.680   1.00 39.37  ? 502  D0L A C3  1 
HETATM 7409 C  C13 . D0L D 3 .   ? -9.544  -27.105 7.925   1.00 35.78  ? 502  D0L A C13 1 
HETATM 7410 C  C11 . D0L D 3 .   ? -10.094 -26.323 5.706   1.00 37.19  ? 502  D0L A C11 1 
HETATM 7411 C  C6  . D0L D 3 .   ? -13.562 -31.544 0.934   1.00 40.93  ? 502  D0L A C6  1 
HETATM 7412 C  C8  . D0L D 3 .   ? -12.796 -28.335 3.978   1.00 38.48  ? 502  D0L A C8  1 
HETATM 7413 C  C5  . D0L D 3 .   ? -14.168 -32.665 1.497   1.00 44.52  ? 502  D0L A C5  1 
HETATM 7414 C  C9  . D0L D 3 .   ? -14.214 -28.353 4.469   1.00 38.63  ? 502  D0L A C9  1 
HETATM 7415 C  C4  . D0L D 3 .   ? -14.145 -32.833 2.879   1.00 42.22  ? 502  D0L A C4  1 
HETATM 7416 O  O2  . D0L D 3 .   ? -14.408 -28.084 5.681   1.00 37.84  ? 502  D0L A O2  1 
HETATM 7417 O  O3  . D0L D 3 .   ? -10.347 -26.977 3.457   1.00 39.68  ? 502  D0L A O3  1 
HETATM 7418 O  O1  . D0L D 3 .   ? -15.140 -28.634 3.679   1.00 34.24  ? 502  D0L A O1  1 
HETATM 7419 N  N2  . D0L D 3 .   ? -11.073 -25.822 6.681   1.00 37.92  ? 502  D0L A N2  1 
HETATM 7420 C  C16 . D0L D 3 .   ? -12.603 -23.919 7.159   1.00 40.86  ? 502  D0L A C16 1 
HETATM 7421 C  C17 . D0L D 3 .   ? -12.198 -22.609 7.832   1.00 40.76  ? 502  D0L A C17 1 
HETATM 7422 C  C18 . D0L D 3 .   ? -13.313 -22.023 8.708   1.00 39.10  ? 502  D0L A C18 1 
HETATM 7423 C  C19 . D0L D 3 .   ? -12.763 -20.945 9.638   1.00 38.30  ? 502  D0L A C19 1 
HETATM 7424 C  C20 . D0L D 3 .   ? -13.862 -20.287 10.484  1.00 38.46  ? 502  D0L A C20 1 
HETATM 7425 C  C21 . D0L D 3 .   ? -14.555 -21.280 11.399  1.00 40.67  ? 502  D0L A C21 1 
HETATM 7426 N  N1  . D0L D 3 .   ? -12.003 -27.523 4.885   1.00 35.07  ? 502  D0L A N1  1 
HETATM 7427 C  CAF A SYN E 4 .   ? -16.604 -20.389 14.634  0.36 36.86  ? 503  SYN A CAF 1 
HETATM 7428 C  CAF B SYN E 4 .   ? -16.360 -20.630 14.788  0.59 36.89  ? 503  SYN A CAF 1 
HETATM 7429 C  CAD A SYN E 4 .   ? -17.570 -21.215 15.183  0.36 38.07  ? 503  SYN A CAD 1 
HETATM 7430 C  CAD B SYN E 4 .   ? -14.985 -20.591 14.944  0.59 38.70  ? 503  SYN A CAD 1 
HETATM 7431 C  CAC A SYN E 4 .   ? -18.891 -20.834 15.173  0.36 38.02  ? 503  SYN A CAC 1 
HETATM 7432 C  CAC B SYN E 4 .   ? -14.270 -19.492 14.524  0.59 33.87  ? 503  SYN A CAC 1 
HETATM 7433 C  CAE A SYN E 4 .   ? -19.256 -19.632 14.609  0.36 36.60  ? 503  SYN A CAE 1 
HETATM 7434 C  CAE B SYN E 4 .   ? -14.922 -18.430 13.941  0.59 34.72  ? 503  SYN A CAE 1 
HETATM 7435 C  CAG A SYN E 4 .   ? -18.294 -18.804 14.056  0.36 36.82  ? 503  SYN A CAG 1 
HETATM 7436 C  CAG B SYN E 4 .   ? -16.296 -18.467 13.776  0.59 35.25  ? 503  SYN A CAG 1 
HETATM 7437 C  CAH A SYN E 4 .   ? -16.947 -19.165 14.060  0.36 36.70  ? 503  SYN A CAH 1 
HETATM 7438 C  CAH B SYN E 4 .   ? -17.043 -19.564 14.204  0.59 36.78  ? 503  SYN A CAH 1 
HETATM 7439 C  CAB A SYN E 4 .   ? -15.921 -18.282 13.475  0.36 34.91  ? 503  SYN A CAB 1 
HETATM 7440 C  CAB B SYN E 4 .   ? -18.508 -19.593 14.037  0.59 37.30  ? 503  SYN A CAB 1 
HETATM 7441 C  CAA A SYN E 4 .   ? -14.633 -18.443 13.517  0.36 34.75  ? 503  SYN A CAA 1 
HETATM 7442 C  CAA B SYN E 4 .   ? -19.343 -20.465 14.518  0.59 39.56  ? 503  SYN A CAA 1 
HETATM 7443 C  C1  . GOL F 5 .   ? -30.326 -25.573 13.546  1.00 49.36  ? 504  GOL A C1  1 
HETATM 7444 O  O1  . GOL F 5 .   ? -29.274 -26.082 12.788  1.00 47.70  ? 504  GOL A O1  1 
HETATM 7445 C  C2  . GOL F 5 .   ? -31.276 -24.802 12.584  1.00 52.74  ? 504  GOL A C2  1 
HETATM 7446 O  O2  . GOL F 5 .   ? -31.645 -25.535 11.471  1.00 54.82  ? 504  GOL A O2  1 
HETATM 7447 C  C3  . GOL F 5 .   ? -32.433 -24.451 13.522  1.00 53.47  ? 504  GOL A C3  1 
HETATM 7448 O  O3  . GOL F 5 .   ? -33.540 -24.221 12.723  1.00 60.78  ? 504  GOL A O3  1 
HETATM 7449 H  H11 . GOL F 5 .   ? -30.022 -24.970 14.242  1.00 59.24  ? 504  GOL A H11 1 
HETATM 7450 H  H12 . GOL F 5 .   ? -30.828 -26.269 13.997  1.00 59.24  ? 504  GOL A H12 1 
HETATM 7451 H  HO1 . GOL F 5 .   ? -29.557 -26.117 11.992  1.00 57.26  ? 504  GOL A HO1 1 
HETATM 7452 H  H2  . GOL F 5 .   ? -30.862 -24.017 12.193  1.00 63.30  ? 504  GOL A H2  1 
HETATM 7453 H  HO2 . GOL F 5 .   ? -32.382 -25.878 11.629  1.00 65.80  ? 504  GOL A HO2 1 
HETATM 7454 H  H31 . GOL F 5 .   ? -32.180 -23.684 14.060  1.00 64.18  ? 504  GOL A H31 1 
HETATM 7455 H  H32 . GOL F 5 .   ? -32.558 -25.177 14.154  1.00 64.18  ? 504  GOL A H32 1 
HETATM 7456 H  HO3 . GOL F 5 .   ? -33.231 -24.020 11.953  1.00 72.95  ? 504  GOL A HO3 1 
HETATM 7457 C  C1  . GOL G 5 .   ? -13.898 -30.199 -12.374 1.00 58.58  ? 505  GOL A C1  1 
HETATM 7458 O  O1  . GOL G 5 .   ? -14.446 -28.947 -11.990 1.00 52.26  ? 505  GOL A O1  1 
HETATM 7459 C  C2  . GOL G 5 .   ? -15.038 -31.139 -12.887 1.00 59.32  ? 505  GOL A C2  1 
HETATM 7460 O  O2  . GOL G 5 .   ? -14.625 -32.479 -12.905 1.00 67.21  ? 505  GOL A O2  1 
HETATM 7461 C  C3  . GOL G 5 .   ? -16.229 -30.869 -11.964 1.00 53.17  ? 505  GOL A C3  1 
HETATM 7462 O  O3  . GOL G 5 .   ? -16.831 -32.093 -11.691 1.00 60.09  ? 505  GOL A O3  1 
HETATM 7463 H  H11 . GOL G 5 .   ? -13.444 -30.638 -11.638 1.00 70.32  ? 505  GOL A H11 1 
HETATM 7464 H  H12 . GOL G 5 .   ? -13.236 -30.106 -13.077 1.00 70.32  ? 505  GOL A H12 1 
HETATM 7465 H  HO1 . GOL G 5 .   ? -15.044 -28.756 -12.562 1.00 62.73  ? 505  GOL A HO1 1 
HETATM 7466 H  H2  . GOL G 5 .   ? -15.285 -30.933 -13.802 1.00 71.20  ? 505  GOL A H2  1 
HETATM 7467 H  HO2 . GOL G 5 .   ? -14.516 -32.745 -12.105 1.00 80.67  ? 505  GOL A HO2 1 
HETATM 7468 H  H31 . GOL G 5 .   ? -16.823 -30.239 -12.400 1.00 63.82  ? 505  GOL A H31 1 
HETATM 7469 H  H32 . GOL G 5 .   ? -15.909 -30.414 -11.170 1.00 63.82  ? 505  GOL A H32 1 
HETATM 7470 H  HO3 . GOL G 5 .   ? -16.711 -32.581 -12.386 1.00 72.13  ? 505  GOL A HO3 1 
HETATM 7471 C  C1  . GOL H 5 .   ? 2.218   -1.390  38.340  1.00 55.21  ? 506  GOL A C1  1 
HETATM 7472 O  O1  . GOL H 5 .   ? 2.353   -0.654  37.145  1.00 60.10  ? 506  GOL A O1  1 
HETATM 7473 C  C2  . GOL H 5 .   ? 0.712   -1.407  38.679  1.00 55.42  ? 506  GOL A C2  1 
HETATM 7474 O  O2  . GOL H 5 .   ? 0.435   -2.095  39.849  1.00 40.96  ? 506  GOL A O2  1 
HETATM 7475 C  C3  . GOL H 5 .   ? 0.340   0.081   38.746  1.00 58.25  ? 506  GOL A C3  1 
HETATM 7476 O  O3  . GOL H 5 .   ? -0.921  0.174   39.356  1.00 62.16  ? 506  GOL A O3  1 
HETATM 7477 H  H11 . GOL H 5 .   ? 2.711   -1.000  39.079  1.00 66.27  ? 506  GOL A H11 1 
HETATM 7478 H  H12 . GOL H 5 .   ? 2.541   -2.301  38.257  1.00 66.27  ? 506  GOL A H12 1 
HETATM 7479 H  HO1 . GOL H 5 .   ? 3.159   -0.364  37.127  1.00 72.14  ? 506  GOL A HO1 1 
HETATM 7480 H  H2  . GOL H 5 .   ? 0.199   -1.871  37.999  1.00 66.53  ? 506  GOL A H2  1 
HETATM 7481 H  HO2 . GOL H 5 .   ? 0.535   -1.564  40.487  1.00 49.17  ? 506  GOL A HO2 1 
HETATM 7482 H  H31 . GOL H 5 .   ? 0.359   0.448   37.848  1.00 69.92  ? 506  GOL A H31 1 
HETATM 7483 H  H32 . GOL H 5 .   ? 1.036   0.554   39.230  1.00 69.92  ? 506  GOL A H32 1 
HETATM 7484 H  HO3 . GOL H 5 .   ? -1.117  -0.608  39.651  1.00 74.61  ? 506  GOL A HO3 1 
HETATM 7485 C  CHA . HEM I 2 .   ? 6.086   -13.759 66.257  1.00 31.66  ? 501  HEM B CHA 1 
HETATM 7486 C  CHB . HEM I 2 .   ? 1.265   -13.446 65.996  1.00 30.19  ? 501  HEM B CHB 1 
HETATM 7487 C  CHC . HEM I 2 .   ? 1.652   -11.015 61.738  1.00 32.14  ? 501  HEM B CHC 1 
HETATM 7488 C  CHD . HEM I 2 .   ? 6.469   -11.659 61.851  1.00 31.01  ? 501  HEM B CHD 1 
HETATM 7489 C  C1A . HEM I 2 .   ? 4.751   -13.850 66.556  1.00 29.74  ? 501  HEM B C1A 1 
HETATM 7490 C  C2A . HEM I 2 .   ? 4.230   -14.466 67.734  1.00 31.73  ? 501  HEM B C2A 1 
HETATM 7491 C  C3A . HEM I 2 .   ? 2.870   -14.382 67.645  1.00 30.18  ? 501  HEM B C3A 1 
HETATM 7492 C  C4A . HEM I 2 .   ? 2.552   -13.714 66.437  1.00 29.14  ? 501  HEM B C4A 1 
HETATM 7493 C  CMA . HEM I 2 .   ? 1.873   -14.884 68.659  1.00 30.36  ? 501  HEM B CMA 1 
HETATM 7494 C  CAA . HEM I 2 .   ? 4.988   -15.105 68.889  1.00 31.14  ? 501  HEM B CAA 1 
HETATM 7495 C  CBA . HEM I 2 .   ? 5.166   -16.606 68.627  1.00 29.52  ? 501  HEM B CBA 1 
HETATM 7496 C  CGA . HEM I 2 .   ? 5.874   -17.353 69.739  1.00 29.56  ? 501  HEM B CGA 1 
HETATM 7497 O  O1A . HEM I 2 .   ? 6.189   -18.555 69.549  1.00 31.62  ? 501  HEM B O1A 1 
HETATM 7498 O  O2A . HEM I 2 .   ? 6.145   -16.806 70.837  1.00 31.72  ? 501  HEM B O2A 1 
HETATM 7499 C  C1B . HEM I 2 .   ? 0.987   -12.764 64.784  1.00 33.88  ? 501  HEM B C1B 1 
HETATM 7500 C  C2B . HEM I 2 .   ? -0.339  -12.493 64.336  1.00 32.80  ? 501  HEM B C2B 1 
HETATM 7501 C  C3B . HEM I 2 .   ? -0.259  -11.824 63.149  1.00 29.77  ? 501  HEM B C3B 1 
HETATM 7502 C  C4B . HEM I 2 .   ? 1.186   -11.669 62.874  1.00 32.43  ? 501  HEM B C4B 1 
HETATM 7503 C  CMB . HEM I 2 .   ? -1.607  -12.903 65.048  1.00 30.65  ? 501  HEM B CMB 1 
HETATM 7504 C  CAB . HEM I 2 .   ? -1.334  -11.311 62.274  1.00 29.62  ? 501  HEM B CAB 1 
HETATM 7505 C  CBB . HEM I 2 .   ? -2.489  -10.857 62.778  1.00 35.02  ? 501  HEM B CBB 1 
HETATM 7506 C  C1C . HEM I 2 .   ? 3.002   -10.970 61.396  1.00 32.00  ? 501  HEM B C1C 1 
HETATM 7507 C  C2C . HEM I 2 .   ? 3.523   -10.347 60.251  1.00 32.80  ? 501  HEM B C2C 1 
HETATM 7508 C  C3C . HEM I 2 .   ? 4.898   -10.552 60.261  1.00 31.86  ? 501  HEM B C3C 1 
HETATM 7509 C  C4C . HEM I 2 .   ? 5.202   -11.256 61.476  1.00 31.73  ? 501  HEM B C4C 1 
HETATM 7510 C  CMC . HEM I 2 .   ? 2.704   -9.648  59.184  1.00 31.95  ? 501  HEM B CMC 1 
HETATM 7511 C  CAC . HEM I 2 .   ? 5.893   -10.079 59.265  1.00 29.96  ? 501  HEM B CAC 1 
HETATM 7512 C  CBC . HEM I 2 .   ? 5.737   -9.002  58.487  1.00 31.91  ? 501  HEM B CBC 1 
HETATM 7513 C  C1D . HEM I 2 .   ? 6.692   -12.308 63.077  1.00 33.51  ? 501  HEM B C1D 1 
HETATM 7514 C  C2D . HEM I 2 .   ? 8.056   -12.718 63.477  1.00 30.12  ? 501  HEM B C2D 1 
HETATM 7515 C  C3D . HEM I 2 .   ? 7.948   -13.289 64.694  1.00 29.06  ? 501  HEM B C3D 1 
HETATM 7516 C  C4D . HEM I 2 .   ? 6.512   -13.240 65.040  1.00 29.46  ? 501  HEM B C4D 1 
HETATM 7517 C  CMD . HEM I 2 .   ? 9.351   -12.515 62.703  1.00 32.30  ? 501  HEM B CMD 1 
HETATM 7518 C  CAD . HEM I 2 .   ? 9.102   -13.814 65.538  1.00 30.82  ? 501  HEM B CAD 1 
HETATM 7519 C  CBD . HEM I 2 .   ? 9.623   -12.641 66.416  1.00 31.20  ? 501  HEM B CBD 1 
HETATM 7520 C  CGD . HEM I 2 .   ? 10.872  -13.008 67.199  1.00 31.71  ? 501  HEM B CGD 1 
HETATM 7521 O  O1D . HEM I 2 .   ? 10.836  -13.941 68.028  1.00 32.24  ? 501  HEM B O1D 1 
HETATM 7522 O  O2D . HEM I 2 .   ? 11.954  -12.390 67.009  1.00 33.74  ? 501  HEM B O2D 1 
HETATM 7523 N  NA  . HEM I 2 .   ? 3.708   -13.364 65.762  1.00 31.42  ? 501  HEM B NA  1 
HETATM 7524 N  NB  . HEM I 2 .   ? 1.832   -12.258 63.881  1.00 29.72  ? 501  HEM B NB  1 
HETATM 7525 N  NC  . HEM I 2 .   ? 4.013   -11.510 62.143  1.00 31.71  ? 501  HEM B NC  1 
HETATM 7526 N  ND  . HEM I 2 .   ? 5.808   -12.634 64.048  1.00 28.20  ? 501  HEM B ND  1 
HETATM 7527 FE FE  . HEM I 2 .   ? 3.908   -12.292 64.080  1.00 31.09  ? 501  HEM B FE  1 
HETATM 7528 C  C1  . D0L J 3 .   ? 1.895   -30.927 73.269  1.00 37.25  ? 502  D0L B C1  1 
HETATM 7529 C  C2  . D0L J 3 .   ? 1.856   -31.108 71.889  1.00 35.71  ? 502  D0L B C2  1 
HETATM 7530 C  C15 . D0L J 3 .   ? 0.190   -24.679 68.923  1.00 34.89  ? 502  D0L B C15 1 
HETATM 7531 C  C14 . D0L J 3 .   ? -0.945  -25.967 67.232  1.00 34.31  ? 502  D0L B C14 1 
HETATM 7532 C  C7  . D0L J 3 .   ? 1.197   -30.091 70.968  1.00 37.19  ? 502  D0L B C7  1 
HETATM 7533 C  C12 . D0L J 3 .   ? -1.981  -27.590 68.712  1.00 35.18  ? 502  D0L B C12 1 
HETATM 7534 C  C10 . D0L J 3 .   ? -0.299  -27.323 70.558  1.00 32.66  ? 502  D0L B C10 1 
HETATM 7535 C  C3  . D0L J 3 .   ? 2.416   -32.260 71.345  1.00 36.18  ? 502  D0L B C3  1 
HETATM 7536 C  C13 . D0L J 3 .   ? -1.741  -27.270 67.233  1.00 37.49  ? 502  D0L B C13 1 
HETATM 7537 C  C11 . D0L J 3 .   ? -1.082  -26.630 69.480  1.00 32.72  ? 502  D0L B C11 1 
HETATM 7538 C  C6  . D0L J 3 .   ? 2.500   -31.880 74.095  1.00 41.98  ? 502  D0L B C6  1 
HETATM 7539 C  C8  . D0L J 3 .   ? 1.722   -28.653 71.084  1.00 32.35  ? 502  D0L B C8  1 
HETATM 7540 C  C5  . D0L J 3 .   ? 3.069   -33.028 73.551  1.00 38.55  ? 502  D0L B C5  1 
HETATM 7541 C  C9  . D0L J 3 .   ? 3.153   -28.584 70.597  1.00 33.46  ? 502  D0L B C9  1 
HETATM 7542 C  C4  . D0L J 3 .   ? 3.027   -33.209 72.172  1.00 40.54  ? 502  D0L B C4  1 
HETATM 7543 O  O2  . D0L J 3 .   ? 4.104   -28.871 71.359  1.00 32.17  ? 502  D0L B O2  1 
HETATM 7544 O  O3  . D0L J 3 .   ? -0.769  -27.429 71.695  1.00 34.97  ? 502  D0L B O3  1 
HETATM 7545 O  O1  . D0L J 3 .   ? 3.351   -28.245 69.412  1.00 34.12  ? 502  D0L B O1  1 
HETATM 7546 N  N2  . D0L J 3 .   ? -0.182  -26.028 68.472  1.00 34.17  ? 502  D0L B N2  1 
HETATM 7547 C  C16 . D0L J 3 .   ? 1.267   -24.090 68.012  1.00 36.88  ? 502  D0L B C16 1 
HETATM 7548 C  C17 . D0L J 3 .   ? 0.799   -22.770 67.412  1.00 35.52  ? 502  D0L B C17 1 
HETATM 7549 C  C18 . D0L J 3 .   ? 1.874   -22.169 66.499  1.00 33.94  ? 502  D0L B C18 1 
HETATM 7550 C  C19 . D0L J 3 .   ? 1.307   -21.078 65.602  1.00 36.09  ? 502  D0L B C19 1 
HETATM 7551 C  C20 . D0L J 3 .   ? 2.379   -20.360 64.776  1.00 35.55  ? 502  D0L B C20 1 
HETATM 7552 C  C21 . D0L J 3 .   ? 2.960   -21.233 63.679  1.00 38.92  ? 502  D0L B C21 1 
HETATM 7553 N  N1  . D0L J 3 .   ? 0.914   -27.784 70.230  1.00 32.88  ? 502  D0L B N1  1 
HETATM 7554 C  CAF A SYN K 4 .   ? 6.462   -18.485 61.046  0.33 37.46  ? 503  SYN B CAF 1 
HETATM 7555 C  CAF B SYN K 4 .   ? 4.666   -18.407 61.225  0.63 34.53  ? 503  SYN B CAF 1 
HETATM 7556 C  CAD A SYN K 4 .   ? 7.519   -19.250 60.584  0.33 33.79  ? 503  SYN B CAD 1 
HETATM 7557 C  CAD B SYN K 4 .   ? 3.287   -18.520 61.168  0.63 36.09  ? 503  SYN B CAD 1 
HETATM 7558 C  CAC A SYN K 4 .   ? 7.287   -20.501 60.061  0.33 37.34  ? 503  SYN B CAC 1 
HETATM 7559 C  CAC B SYN K 4 .   ? 2.710   -19.662 60.665  0.63 35.88  ? 503  SYN B CAC 1 
HETATM 7560 C  CAE A SYN K 4 .   ? 6.003   -20.993 59.998  0.33 37.10  ? 503  SYN B CAE 1 
HETATM 7561 C  CAE B SYN K 4 .   ? 3.505   -20.689 60.211  0.63 36.05  ? 503  SYN B CAE 1 
HETATM 7562 C  CAG A SYN K 4 .   ? 4.943   -20.232 60.460  0.33 36.56  ? 503  SYN B CAG 1 
HETATM 7563 C  CAG B SYN K 4 .   ? 4.883   -20.579 60.262  0.63 37.53  ? 503  SYN B CAG 1 
HETATM 7564 C  CAH A SYN K 4 .   ? 5.152   -18.962 60.996  0.33 34.58  ? 503  SYN B CAH 1 
HETATM 7565 C  CAH B SYN K 4 .   ? 5.493   -19.437 60.776  0.63 34.91  ? 503  SYN B CAH 1 
HETATM 7566 C  CAB A SYN K 4 .   ? 4.025   -18.146 61.484  0.33 35.88  ? 503  SYN B CAB 1 
HETATM 7567 C  CAB B SYN K 4 .   ? 6.962   -19.306 60.824  0.63 35.04  ? 503  SYN B CAB 1 
HETATM 7568 C  CAA A SYN K 4 .   ? 2.758   -18.422 61.386  0.33 35.44  ? 503  SYN B CAA 1 
HETATM 7569 C  CAA B SYN K 4 .   ? 7.843   -20.085 60.282  0.63 37.59  ? 503  SYN B CAA 1 
HETATM 7570 C  C1  . GOL L 5 .   ? -4.583  2.045   62.275  1.00 48.89  ? 504  GOL B C1  1 
HETATM 7571 O  O1  . GOL L 5 .   ? -3.618  2.036   63.275  1.00 60.18  ? 504  GOL B O1  1 
HETATM 7572 C  C2  . GOL L 5 .   ? -5.775  1.121   62.667  1.00 51.23  ? 504  GOL B C2  1 
HETATM 7573 O  O2  . GOL L 5 .   ? -5.479  -0.064  63.296  1.00 43.47  ? 504  GOL B O2  1 
HETATM 7574 C  C3  . GOL L 5 .   ? -6.716  1.969   63.585  1.00 45.51  ? 504  GOL B C3  1 
HETATM 7575 O  O3  . GOL L 5 .   ? -5.917  2.573   64.584  1.00 59.86  ? 504  GOL B O3  1 
HETATM 7576 H  H11 . GOL L 5 .   ? -4.228  1.741   61.425  1.00 58.69  ? 504  GOL B H11 1 
HETATM 7577 H  H12 . GOL L 5 .   ? -4.929  2.937   62.114  1.00 58.69  ? 504  GOL B H12 1 
HETATM 7578 H  HO1 . GOL L 5 .   ? -3.743  2.746   63.730  1.00 72.23  ? 504  GOL B HO1 1 
HETATM 7579 H  H2  . GOL L 5 .   ? -6.170  0.862   61.820  1.00 61.49  ? 504  GOL B H2  1 
HETATM 7580 H  HO2 . GOL L 5 .   ? -6.134  -0.252  63.806  1.00 52.18  ? 504  GOL B HO2 1 
HETATM 7581 H  H31 . GOL L 5 .   ? -7.403  1.387   63.946  1.00 54.63  ? 504  GOL B H31 1 
HETATM 7582 H  H32 . GOL L 5 .   ? -7.188  2.612   63.033  1.00 54.63  ? 504  GOL B H32 1 
HETATM 7583 H  HO3 . GOL L 5 .   ? -5.473  1.940   64.980  1.00 71.85  ? 504  GOL B HO3 1 
HETATM 7584 C  C1  . GOL M 5 .   ? 21.125  -23.645 61.856  1.00 60.25  ? 505  GOL B C1  1 
HETATM 7585 O  O1  . GOL M 5 .   ? 22.280  -23.929 62.614  1.00 60.92  ? 505  GOL B O1  1 
HETATM 7586 C  C2  . GOL M 5 .   ? 20.272  -24.927 61.855  1.00 60.30  ? 505  GOL B C2  1 
HETATM 7587 O  O2  . GOL M 5 .   ? 20.029  -25.386 63.142  1.00 59.65  ? 505  GOL B O2  1 
HETATM 7588 C  C3  . GOL M 5 .   ? 18.992  -24.546 61.097  1.00 51.21  ? 505  GOL B C3  1 
HETATM 7589 O  O3  . GOL M 5 .   ? 17.962  -25.380 61.594  1.00 53.73  ? 505  GOL B O3  1 
HETATM 7590 H  H11 . GOL M 5 .   ? 21.330  -23.393 60.942  1.00 72.31  ? 505  GOL B H11 1 
HETATM 7591 H  H12 . GOL M 5 .   ? 20.606  -22.913 62.224  1.00 72.31  ? 505  GOL B H12 1 
HETATM 7592 H  HO1 . GOL M 5 .   ? 22.182  -24.719 62.918  1.00 73.12  ? 505  GOL B HO1 1 
HETATM 7593 H  H2  . GOL M 5 .   ? 20.730  -25.653 61.403  1.00 72.37  ? 505  GOL B H2  1 
HETATM 7594 H  HO2 . GOL M 5 .   ? 19.495  -24.864 63.499  1.00 71.60  ? 505  GOL B HO2 1 
HETATM 7595 H  H31 . GOL M 5 .   ? 19.147  -24.650 60.145  1.00 61.47  ? 505  GOL B H31 1 
HETATM 7596 H  H32 . GOL M 5 .   ? 18.819  -23.600 61.227  1.00 61.47  ? 505  GOL B H32 1 
HETATM 7597 H  HO3 . GOL M 5 .   ? 18.329  -25.930 62.139  1.00 64.49  ? 505  GOL B HO3 1 
HETATM 7598 C  C1  . GOL N 5 .   ? -4.230  -3.546  72.679  1.00 58.28  ? 506  GOL B C1  1 
HETATM 7599 O  O1  . GOL N 5 .   ? -3.308  -4.099  71.717  1.00 60.22  ? 506  GOL B O1  1 
HETATM 7600 C  C2  . GOL N 5 .   ? -5.172  -2.514  71.981  1.00 56.33  ? 506  GOL B C2  1 
HETATM 7601 O  O2  . GOL N 5 .   ? -5.772  -1.662  72.898  1.00 52.59  ? 506  GOL B O2  1 
HETATM 7602 C  C3  . GOL N 5 .   ? -4.246  -1.806  70.973  1.00 62.95  ? 506  GOL B C3  1 
HETATM 7603 O  O3  . GOL N 5 .   ? -4.752  -0.519  70.776  1.00 67.68  ? 506  GOL B O3  1 
HETATM 7604 H  H11 . GOL N 5 .   ? -3.770  -3.098  73.407  1.00 69.95  ? 506  GOL B H11 1 
HETATM 7605 H  H12 . GOL N 5 .   ? -4.778  -4.231  73.093  1.00 69.95  ? 506  GOL B H12 1 
HETATM 7606 H  HO1 . GOL N 5 .   ? -3.747  -4.267  71.015  1.00 72.29  ? 506  GOL B HO1 1 
HETATM 7607 H  H2  . GOL N 5 .   ? -5.914  -2.940  71.524  1.00 67.61  ? 506  GOL B H2  1 
HETATM 7608 H  HO2 . GOL N 5 .   ? -5.161  -1.288  73.336  1.00 63.12  ? 506  GOL B HO2 1 
HETATM 7609 H  H31 . GOL N 5 .   ? -4.210  -2.333  70.159  1.00 75.56  ? 506  GOL B H31 1 
HETATM 7610 H  H32 . GOL N 5 .   ? -3.341  -1.813  71.323  1.00 75.56  ? 506  GOL B H32 1 
HETATM 7611 H  HO3 . GOL N 5 .   ? -5.461  -0.469  71.244  1.00 81.23  ? 506  GOL B HO3 1 
HETATM 7612 C  C1  . GOL O 5 .   ? 5.463   -30.997 86.891  1.00 57.31  ? 507  GOL B C1  1 
HETATM 7613 O  O1  . GOL O 5 .   ? 5.651   -32.319 87.287  1.00 69.11  ? 507  GOL B O1  1 
HETATM 7614 C  C2  . GOL O 5 .   ? 4.041   -30.532 87.321  1.00 58.12  ? 507  GOL B C2  1 
HETATM 7615 O  O2  . GOL O 5 .   ? 3.821   -29.227 86.931  1.00 48.73  ? 507  GOL B O2  1 
HETATM 7616 C  C3  . GOL O 5 .   ? 3.102   -31.549 86.675  1.00 60.52  ? 507  GOL B C3  1 
HETATM 7617 O  O3  . GOL O 5 .   ? 2.853   -32.516 87.686  1.00 64.45  ? 507  GOL B O3  1 
HETATM 7618 H  H11 . GOL O 5 .   ? 5.549   -30.887 85.931  1.00 68.79  ? 507  GOL B H11 1 
HETATM 7619 H  H12 . GOL O 5 .   ? 6.118   -30.400 87.286  1.00 68.79  ? 507  GOL B H12 1 
HETATM 7620 H  HO1 . GOL O 5 .   ? 5.967   -32.287 88.077  1.00 82.95  ? 507  GOL B HO1 1 
HETATM 7621 H  H2  . GOL O 5 .   ? 3.916   -30.539 88.283  1.00 69.77  ? 507  GOL B H2  1 
HETATM 7622 H  HO2 . GOL O 5 .   ? 4.548   -28.924 86.640  1.00 58.49  ? 507  GOL B HO2 1 
HETATM 7623 H  H31 . GOL O 5 .   ? 3.519   -31.915 85.879  1.00 72.64  ? 507  GOL B H31 1 
HETATM 7624 H  H32 . GOL O 5 .   ? 2.303   -31.098 86.361  1.00 72.64  ? 507  GOL B H32 1 
HETATM 7625 H  HO3 . GOL O 5 .   ? 3.623   -32.810 87.952  1.00 77.35  ? 507  GOL B HO3 1 
HETATM 7626 C  C1  . GOL P 5 .   ? 18.525  -17.303 77.034  1.00 49.12  ? 508  GOL B C1  1 
HETATM 7627 O  O1  . GOL P 5 .   ? 19.456  -18.275 77.417  1.00 53.60  ? 508  GOL B O1  1 
HETATM 7628 C  C2  . GOL P 5 .   ? 17.923  -16.695 78.314  1.00 53.53  ? 508  GOL B C2  1 
HETATM 7629 O  O2  . GOL P 5 .   ? 18.822  -15.941 79.020  1.00 52.44  ? 508  GOL B O2  1 
HETATM 7630 C  C3  . GOL P 5 .   ? 16.744  -15.893 77.733  1.00 46.88  ? 508  GOL B C3  1 
HETATM 7631 O  O3  . GOL P 5 .   ? 16.051  -15.414 78.806  1.00 45.47  ? 508  GOL B O3  1 
HETATM 7632 H  H11 . GOL P 5 .   ? 17.810  -17.669 76.490  1.00 58.96  ? 508  GOL B H11 1 
HETATM 7633 H  H12 . GOL P 5 .   ? 18.925  -16.595 76.505  1.00 58.96  ? 508  GOL B H12 1 
HETATM 7634 H  HO1 . GOL P 5 .   ? 19.914  -18.450 76.725  1.00 64.33  ? 508  GOL B HO1 1 
HETATM 7635 H  H2  . GOL P 5 .   ? 17.640  -17.361 78.960  1.00 64.25  ? 508  GOL B H2  1 
HETATM 7636 H  HO2 . GOL P 5 .   ? 18.477  -15.194 79.149  1.00 62.94  ? 508  GOL B HO2 1 
HETATM 7637 H  H31 . GOL P 5 .   ? 16.219  -16.471 77.158  1.00 56.28  ? 508  GOL B H31 1 
HETATM 7638 H  H32 . GOL P 5 .   ? 17.089  -15.197 77.151  1.00 56.28  ? 508  GOL B H32 1 
HETATM 7639 H  HO3 . GOL P 5 .   ? 16.127  -15.990 79.394  1.00 54.58  ? 508  GOL B HO3 1 
HETATM 7640 O  O   . HOH Q 6 .   ? -16.289 -6.777  6.365   1.00 42.68  ? 601  HOH A O   1 
HETATM 7641 O  O   . HOH Q 6 .   ? -12.471 -9.464  9.997   1.00 43.85  ? 602  HOH A O   1 
HETATM 7642 O  O   . HOH Q 6 .   ? -16.801 -27.000 -0.945  1.00 40.58  ? 603  HOH A O   1 
HETATM 7643 O  O   . HOH Q 6 .   ? -27.651 -23.298 -14.382 1.00 54.05  ? 604  HOH A O   1 
HETATM 7644 O  O   . HOH Q 6 .   ? -38.834 -15.995 25.862  1.00 62.60  ? 605  HOH A O   1 
HETATM 7645 O  O   . HOH Q 6 .   ? -34.565 -22.132 12.367  1.00 54.87  ? 606  HOH A O   1 
HETATM 7646 O  O   . HOH Q 6 .   ? -12.710 2.869   10.868  1.00 65.09  ? 607  HOH A O   1 
HETATM 7647 O  O   . HOH Q 6 .   ? -1.648  -18.966 32.720  1.00 54.45  ? 608  HOH A O   1 
HETATM 7648 O  O   . HOH Q 6 .   ? 8.027   -21.318 22.826  1.00 51.73  ? 609  HOH A O   1 
HETATM 7649 O  O   . HOH Q 6 .   ? -11.093 1.708   14.218  1.00 42.55  ? 610  HOH A O   1 
HETATM 7650 O  O   . HOH Q 6 .   ? -8.427  12.870  24.528  1.00 58.59  ? 611  HOH A O   1 
HETATM 7651 O  O   . HOH Q 6 .   ? -20.239 -30.803 3.037   1.00 53.03  ? 612  HOH A O   1 
HETATM 7652 O  O   . HOH Q 6 .   ? 10.805  -15.490 21.976  1.00 39.54  ? 613  HOH A O   1 
HETATM 7653 O  O   . HOH Q 6 .   ? -4.835  -23.138 -14.460 1.00 50.78  ? 614  HOH A O   1 
HETATM 7654 O  O   . HOH Q 6 .   ? -21.176 8.616   15.357  1.00 55.86  ? 615  HOH A O   1 
HETATM 7655 O  O   . HOH Q 6 .   ? -6.146  -10.991 -12.484 1.00 48.63  ? 616  HOH A O   1 
HETATM 7656 O  O   . HOH Q 6 .   ? 5.220   -17.877 -0.622  1.00 53.14  ? 617  HOH A O   1 
HETATM 7657 O  O   . HOH Q 6 .   ? 1.530   1.687   32.848  1.00 49.75  ? 618  HOH A O   1 
HETATM 7658 O  O   . HOH Q 6 .   ? -23.978 -9.820  8.105   1.00 42.78  ? 619  HOH A O   1 
HETATM 7659 O  O   . HOH Q 6 .   ? 7.573   7.782   12.434  1.00 59.09  ? 620  HOH A O   1 
HETATM 7660 O  O   . HOH Q 6 .   ? -24.226 -10.649 35.213  1.00 48.18  ? 621  HOH A O   1 
HETATM 7661 O  O   . HOH Q 6 .   ? -8.449  9.946   25.960  1.00 52.47  ? 622  HOH A O   1 
HETATM 7662 O  O   . HOH Q 6 .   ? -22.122 -17.326 -15.796 1.00 53.24  ? 623  HOH A O   1 
HETATM 7663 O  O   . HOH Q 6 .   ? 0.139   -32.923 -5.054  1.00 52.83  ? 624  HOH A O   1 
HETATM 7664 O  O   . HOH Q 6 .   ? 9.511   0.084   21.165  1.00 47.65  ? 625  HOH A O   1 
HETATM 7665 O  O   . HOH Q 6 .   ? 9.810   -17.966 12.714  1.00 42.23  ? 626  HOH A O   1 
HETATM 7666 O  O   . HOH Q 6 .   ? -34.292 -7.018  3.824   1.00 50.78  ? 627  HOH A O   1 
HETATM 7667 O  O   . HOH Q 6 .   ? -8.494  -29.468 22.866  1.00 56.74  ? 628  HOH A O   1 
HETATM 7668 O  O   . HOH Q 6 .   ? -20.470 -15.361 6.301   1.00 32.40  ? 629  HOH A O   1 
HETATM 7669 O  O   . HOH Q 6 .   ? -28.425 -27.192 17.789  1.00 56.32  ? 630  HOH A O   1 
HETATM 7670 O  O   . HOH Q 6 .   ? 4.276   1.647   30.520  1.00 40.57  ? 631  HOH A O   1 
HETATM 7671 O  O   . HOH Q 6 .   ? -14.987 -26.702 29.693  1.00 48.13  ? 632  HOH A O   1 
HETATM 7672 O  O   . HOH Q 6 .   ? -32.167 -14.764 4.280   1.00 36.66  ? 633  HOH A O   1 
HETATM 7673 O  O   . HOH Q 6 .   ? -29.347 -18.716 -7.149  1.00 48.42  ? 634  HOH A O   1 
HETATM 7674 O  O   . HOH Q 6 .   ? 0.898   -26.188 16.547  1.00 46.07  ? 635  HOH A O   1 
HETATM 7675 O  O   . HOH Q 6 .   ? -15.597 -35.045 5.850   1.00 51.63  ? 636  HOH A O   1 
HETATM 7676 O  O   . HOH Q 6 .   ? -23.132 -29.548 -8.979  1.00 51.10  ? 637  HOH A O   1 
HETATM 7677 O  O   . HOH Q 6 .   ? 6.362   -7.309  31.446  1.00 46.99  ? 638  HOH A O   1 
HETATM 7678 O  O   . HOH Q 6 .   ? 11.003  -16.505 31.376  1.00 55.91  ? 639  HOH A O   1 
HETATM 7679 O  O   . HOH Q 6 .   ? -7.775  -6.870  40.216  1.00 34.10  ? 640  HOH A O   1 
HETATM 7680 O  O   . HOH Q 6 .   ? -13.977 0.543   33.046  1.00 50.38  ? 641  HOH A O   1 
HETATM 7681 O  O   . HOH Q 6 .   ? 0.615   -21.747 23.017  1.00 40.74  ? 642  HOH A O   1 
HETATM 7682 O  O   . HOH Q 6 .   ? 8.904   -7.536  40.599  1.00 52.46  ? 643  HOH A O   1 
HETATM 7683 O  O   . HOH Q 6 .   ? -9.528  -18.427 21.626  1.00 43.66  ? 644  HOH A O   1 
HETATM 7684 O  O   . HOH Q 6 .   ? 2.111   9.210   24.022  1.00 49.04  ? 645  HOH A O   1 
HETATM 7685 O  O   . HOH Q 6 .   ? -5.012  -23.933 -5.403  1.00 37.34  ? 646  HOH A O   1 
HETATM 7686 O  O   . HOH Q 6 .   ? -32.897 -18.986 25.580  1.00 52.72  ? 647  HOH A O   1 
HETATM 7687 O  O   . HOH Q 6 .   ? 2.278   -25.021 4.052   1.00 44.94  ? 648  HOH A O   1 
HETATM 7688 O  O   . HOH Q 6 .   ? -2.307  4.672   27.450  1.00 45.51  ? 649  HOH A O   1 
HETATM 7689 O  O   . HOH Q 6 .   ? -13.277 -2.455  35.450  1.00 37.75  ? 650  HOH A O   1 
HETATM 7690 O  O   . HOH Q 6 .   ? -3.541  -14.367 -10.257 1.00 38.35  ? 651  HOH A O   1 
HETATM 7691 O  O   . HOH Q 6 .   ? -19.122 -30.034 -12.926 1.00 51.35  ? 652  HOH A O   1 
HETATM 7692 O  O   . HOH Q 6 .   ? 3.359   -23.336 7.788   1.00 46.66  ? 653  HOH A O   1 
HETATM 7693 O  O   . HOH Q 6 .   ? -10.148 -14.334 -14.502 1.00 45.23  ? 654  HOH A O   1 
HETATM 7694 O  O   . HOH Q 6 .   ? -10.662 -24.664 31.717  1.00 54.20  ? 655  HOH A O   1 
HETATM 7695 O  O   . HOH Q 6 .   ? 1.778   7.249   11.235  1.00 49.58  ? 656  HOH A O   1 
HETATM 7696 O  O   . HOH Q 6 .   ? -9.434  12.384  21.903  1.00 46.41  ? 657  HOH A O   1 
HETATM 7697 O  O   . HOH Q 6 .   ? -4.673  2.100   8.244   1.00 42.39  ? 658  HOH A O   1 
HETATM 7698 O  O   . HOH Q 6 .   ? -13.874 -9.592  31.762  1.00 31.50  ? 659  HOH A O   1 
HETATM 7699 O  O   . HOH Q 6 .   ? -14.317 -14.610 13.294  1.00 30.34  ? 660  HOH A O   1 
HETATM 7700 O  O   . HOH Q 6 .   ? -17.632 -16.739 33.779  1.00 47.94  ? 661  HOH A O   1 
HETATM 7701 O  O   . HOH Q 6 .   ? -2.771  -27.970 14.960  1.00 39.22  ? 662  HOH A O   1 
HETATM 7702 O  O   . HOH Q 6 .   ? -6.701  -4.655  36.414  1.00 37.82  ? 663  HOH A O   1 
HETATM 7703 O  O   . HOH Q 6 .   ? -20.013 -31.941 14.471  1.00 49.98  ? 664  HOH A O   1 
HETATM 7704 O  O   . HOH Q 6 .   ? -33.213 -24.121 7.202   1.00 41.01  ? 665  HOH A O   1 
HETATM 7705 O  O   . HOH Q 6 .   ? -8.966  -4.919  6.222   1.00 40.17  ? 666  HOH A O   1 
HETATM 7706 O  O   . HOH Q 6 .   ? -18.936 -29.676 -5.975  1.00 40.59  ? 667  HOH A O   1 
HETATM 7707 O  O   . HOH Q 6 .   ? -1.646  -34.005 4.316   1.00 48.00  ? 668  HOH A O   1 
HETATM 7708 O  O   . HOH Q 6 .   ? -13.031 -9.599  20.800  1.00 31.03  ? 669  HOH A O   1 
HETATM 7709 O  O   . HOH Q 6 .   ? -13.439 -15.251 -17.402 1.00 51.02  ? 670  HOH A O   1 
HETATM 7710 O  O   . HOH Q 6 .   ? -8.587  -15.357 -16.612 1.00 51.16  ? 671  HOH A O   1 
HETATM 7711 O  O   . HOH Q 6 .   ? -6.400  -2.633  9.660   1.00 44.81  ? 672  HOH A O   1 
HETATM 7712 O  O   . HOH Q 6 .   ? -11.131 -7.298  1.667   1.00 47.64  ? 673  HOH A O   1 
HETATM 7713 O  O   . HOH Q 6 .   ? -5.889  -28.585 21.252  1.00 62.24  ? 674  HOH A O   1 
HETATM 7714 O  O   . HOH Q 6 .   ? -9.752  10.455  14.473  1.00 47.89  ? 675  HOH A O   1 
HETATM 7715 O  O   . HOH Q 6 .   ? -0.479  -15.851 33.195  1.00 44.00  ? 676  HOH A O   1 
HETATM 7716 O  O   . HOH Q 6 .   ? -18.285 0.809   26.474  1.00 40.18  ? 677  HOH A O   1 
HETATM 7717 O  O   . HOH Q 6 .   ? 4.767   -18.220 5.159   1.00 47.56  ? 678  HOH A O   1 
HETATM 7718 O  O   . HOH Q 6 .   ? -6.919  0.313   12.185  1.00 41.85  ? 679  HOH A O   1 
HETATM 7719 O  O   . HOH Q 6 .   ? -7.797  -2.008  35.545  1.00 39.21  ? 680  HOH A O   1 
HETATM 7720 O  O   . HOH Q 6 .   ? -12.064 -28.351 -16.010 1.00 54.92  ? 681  HOH A O   1 
HETATM 7721 O  O   . HOH Q 6 .   ? 6.210   -15.035 5.768   1.00 48.44  ? 682  HOH A O   1 
HETATM 7722 O  O   . HOH Q 6 .   ? -29.840 -3.136  9.217   1.00 49.71  ? 683  HOH A O   1 
HETATM 7723 O  O   . HOH Q 6 .   ? -16.406 -36.861 8.305   1.00 53.05  ? 684  HOH A O   1 
HETATM 7724 O  O   . HOH Q 6 .   ? -11.665 -34.759 18.959  1.00 50.01  ? 685  HOH A O   1 
HETATM 7725 O  O   . HOH Q 6 .   ? -9.586  -27.463 25.298  1.00 45.79  ? 686  HOH A O   1 
HETATM 7726 O  O   . HOH Q 6 .   ? -33.256 -21.428 9.551   1.00 43.05  ? 687  HOH A O   1 
HETATM 7727 O  O   . HOH Q 6 .   ? -5.082  -2.031  39.913  1.00 39.97  ? 688  HOH A O   1 
HETATM 7728 O  O   . HOH Q 6 .   ? -10.178 -48.136 -1.280  1.00 55.58  ? 689  HOH A O   1 
HETATM 7729 O  O   . HOH Q 6 .   ? -6.599  -44.050 -5.592  1.00 37.69  ? 690  HOH A O   1 
HETATM 7730 O  O   . HOH Q 6 .   ? 8.459   -1.622  6.223   1.00 51.56  ? 691  HOH A O   1 
HETATM 7731 O  O   . HOH Q 6 .   ? -15.776 -10.005 29.696  1.00 31.33  ? 692  HOH A O   1 
HETATM 7732 O  O   . HOH Q 6 .   ? -0.959  0.388   -1.652  1.00 50.14  ? 693  HOH A O   1 
HETATM 7733 O  O   . HOH Q 6 .   ? -0.270  3.758   35.883  1.00 55.44  ? 694  HOH A O   1 
HETATM 7734 O  O   . HOH Q 6 .   ? 5.860   3.901   21.881  1.00 48.31  ? 695  HOH A O   1 
HETATM 7735 O  O   . HOH Q 6 .   ? -42.615 -7.865  15.303  1.00 54.36  ? 696  HOH A O   1 
HETATM 7736 O  O   . HOH Q 6 .   ? -9.408  -14.775 7.600   1.00 33.16  ? 697  HOH A O   1 
HETATM 7737 O  O   . HOH Q 6 .   ? -29.522 -20.892 -3.862  1.00 45.62  ? 698  HOH A O   1 
HETATM 7738 O  O   . HOH Q 6 .   ? 3.925   -13.391 37.678  1.00 45.09  ? 699  HOH A O   1 
HETATM 7739 O  O   . HOH Q 6 .   ? -3.611  -25.595 -10.943 1.00 38.87  ? 700  HOH A O   1 
HETATM 7740 O  O   . HOH Q 6 .   ? -34.210 -15.264 24.453  1.00 57.96  ? 701  HOH A O   1 
HETATM 7741 O  O   . HOH Q 6 .   ? -17.974 -20.599 3.648   1.00 31.55  ? 702  HOH A O   1 
HETATM 7742 O  O   . HOH Q 6 .   ? -3.756  -11.777 -3.783  1.00 36.41  ? 703  HOH A O   1 
HETATM 7743 O  O   . HOH Q 6 .   ? -25.017 -30.754 24.408  1.00 51.83  ? 704  HOH A O   1 
HETATM 7744 O  O   . HOH Q 6 .   ? -12.816 2.446   30.214  1.00 46.57  ? 705  HOH A O   1 
HETATM 7745 O  O   . HOH Q 6 .   ? -25.994 -24.641 20.620  1.00 43.42  ? 706  HOH A O   1 
HETATM 7746 O  O   . HOH Q 6 .   ? 2.910   -14.075 31.786  1.00 39.50  ? 707  HOH A O   1 
HETATM 7747 O  O   . HOH Q 6 .   ? -23.416 -19.073 13.197  1.00 33.05  ? 708  HOH A O   1 
HETATM 7748 O  O   . HOH Q 6 .   ? -25.170 -0.292  20.685  1.00 56.69  ? 709  HOH A O   1 
HETATM 7749 O  O   . HOH Q 6 .   ? -35.235 -10.388 6.394   1.00 40.61  ? 710  HOH A O   1 
HETATM 7750 O  O   . HOH Q 6 .   ? -10.379 -16.211 39.363  1.00 50.60  ? 711  HOH A O   1 
HETATM 7751 O  O   . HOH Q 6 .   ? -21.822 1.912   25.888  1.00 57.38  ? 712  HOH A O   1 
HETATM 7752 O  O   . HOH Q 6 .   ? 3.268   -24.575 11.579  1.00 37.05  ? 713  HOH A O   1 
HETATM 7753 O  O   . HOH Q 6 .   ? -25.988 -19.699 0.998   1.00 34.52  ? 714  HOH A O   1 
HETATM 7754 O  O   . HOH Q 6 .   ? -17.477 4.237   24.919  1.00 40.14  ? 715  HOH A O   1 
HETATM 7755 O  O   . HOH Q 6 .   ? 11.508  -0.895  32.525  1.00 56.32  ? 716  HOH A O   1 
HETATM 7756 O  O   . HOH Q 6 .   ? -31.446 -18.018 30.411  1.00 50.63  ? 717  HOH A O   1 
HETATM 7757 O  O   . HOH Q 6 .   ? -17.916 -4.245  11.782  1.00 45.82  ? 718  HOH A O   1 
HETATM 7758 O  O   . HOH Q 6 .   ? 8.563   -12.264 6.709   1.00 55.18  ? 719  HOH A O   1 
HETATM 7759 O  O   . HOH Q 6 .   ? -14.056 -27.404 -14.205 1.00 45.02  ? 720  HOH A O   1 
HETATM 7760 O  O   . HOH Q 6 .   ? 8.288   -23.065 18.114  1.00 45.29  ? 721  HOH A O   1 
HETATM 7761 O  O   . HOH Q 6 .   ? -8.046  -2.623  -2.399  1.00 42.86  ? 722  HOH A O   1 
HETATM 7762 O  O   . HOH Q 6 .   ? -37.298 -20.219 19.603  1.00 49.40  ? 723  HOH A O   1 
HETATM 7763 O  O   . HOH Q 6 .   ? -31.902 -3.859  15.433  1.00 45.16  ? 724  HOH A O   1 
HETATM 7764 O  O   . HOH Q 6 .   ? -13.834 -4.592  -5.357  1.00 37.99  ? 725  HOH A O   1 
HETATM 7765 O  O   . HOH Q 6 .   ? -17.922 -14.378 3.012   1.00 31.58  ? 726  HOH A O   1 
HETATM 7766 O  O   . HOH Q 6 .   ? -2.378  -21.321 19.985  1.00 40.79  ? 727  HOH A O   1 
HETATM 7767 O  O   . HOH Q 6 .   ? -18.556 -2.599  33.730  1.00 55.99  ? 728  HOH A O   1 
HETATM 7768 O  O   . HOH Q 6 .   ? 5.216   -20.362 28.762  1.00 51.34  ? 729  HOH A O   1 
HETATM 7769 O  O   . HOH Q 6 .   ? -25.044 -29.105 10.146  1.00 47.29  ? 730  HOH A O   1 
HETATM 7770 O  O   . HOH Q 6 .   ? -26.390 -27.989 -14.303 1.00 52.60  ? 731  HOH A O   1 
HETATM 7771 O  O   . HOH Q 6 .   ? -7.400  -17.340 15.244  1.00 33.92  ? 732  HOH A O   1 
HETATM 7772 O  O   . HOH Q 6 .   ? 0.628   -31.153 1.685   1.00 40.05  ? 733  HOH A O   1 
HETATM 7773 O  O   . HOH Q 6 .   ? -22.385 -3.943  27.371  1.00 38.48  ? 734  HOH A O   1 
HETATM 7774 O  O   . HOH Q 6 .   ? 7.199   -0.462  21.452  1.00 43.16  ? 735  HOH A O   1 
HETATM 7775 O  O   . HOH Q 6 .   ? -16.091 -22.377 5.046   1.00 33.50  ? 736  HOH A O   1 
HETATM 7776 O  O   . HOH Q 6 .   ? -34.992 -17.173 0.808   1.00 48.75  ? 737  HOH A O   1 
HETATM 7777 O  O   . HOH Q 6 .   ? -34.396 -9.486  17.601  1.00 40.17  ? 738  HOH A O   1 
HETATM 7778 O  O   . HOH Q 6 .   ? -0.467  -28.588 -11.855 1.00 48.86  ? 739  HOH A O   1 
HETATM 7779 O  O   . HOH Q 6 .   ? -16.004 2.513   13.382  1.00 59.20  ? 740  HOH A O   1 
HETATM 7780 O  O   . HOH Q 6 .   ? -5.132  0.414   3.863   1.00 54.07  ? 741  HOH A O   1 
HETATM 7781 O  O   . HOH Q 6 .   ? -24.429 -12.694 -13.799 1.00 44.77  ? 742  HOH A O   1 
HETATM 7782 O  O   . HOH Q 6 .   ? -12.561 -12.566 16.445  1.00 31.17  ? 743  HOH A O   1 
HETATM 7783 O  O   . HOH Q 6 .   ? -33.223 -27.565 10.484  1.00 53.88  ? 744  HOH A O   1 
HETATM 7784 O  O   . HOH Q 6 .   ? -33.012 -20.913 15.201  1.00 40.04  ? 745  HOH A O   1 
HETATM 7785 O  O   . HOH Q 6 .   ? -25.227 -14.287 -4.102  1.00 37.52  ? 746  HOH A O   1 
HETATM 7786 O  O   . HOH Q 6 .   ? 9.800   -9.166  6.554   1.00 46.82  ? 747  HOH A O   1 
HETATM 7787 O  O   . HOH Q 6 .   ? -9.074  -31.501 21.692  1.00 56.05  ? 748  HOH A O   1 
HETATM 7788 O  O   . HOH Q 6 .   ? -18.058 -29.151 -15.031 1.00 52.88  ? 749  HOH A O   1 
HETATM 7789 O  O   . HOH Q 6 .   ? -4.430  -0.465  6.167   1.00 45.96  ? 750  HOH A O   1 
HETATM 7790 O  O   . HOH Q 6 .   ? 14.223  -10.689 12.761  1.00 51.68  ? 751  HOH A O   1 
HETATM 7791 O  O   . HOH Q 6 .   ? 3.493   4.848   6.007   1.00 57.67  ? 752  HOH A O   1 
HETATM 7792 O  O   . HOH Q 6 .   ? -9.423  -1.598  33.391  1.00 39.47  ? 753  HOH A O   1 
HETATM 7793 O  O   . HOH Q 6 .   ? -13.233 -8.020  33.859  1.00 34.41  ? 754  HOH A O   1 
HETATM 7794 O  O   . HOH Q 6 .   ? 2.586   -19.097 24.160  1.00 37.98  ? 755  HOH A O   1 
HETATM 7795 O  O   . HOH Q 6 .   ? 9.381   -9.592  32.126  1.00 54.96  ? 756  HOH A O   1 
HETATM 7796 O  O   . HOH Q 6 .   ? -15.402 -31.635 21.692  1.00 43.84  ? 757  HOH A O   1 
HETATM 7797 O  O   . HOH Q 6 .   ? -4.847  -21.931 18.903  1.00 41.17  ? 758  HOH A O   1 
HETATM 7798 O  O   . HOH Q 6 .   ? -26.512 -8.160  31.203  1.00 44.74  ? 759  HOH A O   1 
HETATM 7799 O  O   . HOH Q 6 .   ? -4.133  8.566   24.367  1.00 43.34  ? 760  HOH A O   1 
HETATM 7800 O  O   . HOH Q 6 .   ? -17.312 -12.437 -12.716 1.00 51.57  ? 761  HOH A O   1 
HETATM 7801 O  O   . HOH Q 6 .   ? -0.516  -16.691 30.483  1.00 43.50  ? 762  HOH A O   1 
HETATM 7802 O  O   . HOH Q 6 .   ? -18.627 -17.965 1.727   1.00 32.25  ? 763  HOH A O   1 
HETATM 7803 O  O   . HOH Q 6 .   ? -14.857 -17.459 -17.907 1.00 51.68  ? 764  HOH A O   1 
HETATM 7804 O  O   . HOH Q 6 .   ? 6.256   -2.283  35.143  1.00 44.14  ? 765  HOH A O   1 
HETATM 7805 O  O   . HOH Q 6 .   ? 10.684  -21.727 18.918  1.00 46.90  ? 766  HOH A O   1 
HETATM 7806 O  O   . HOH Q 6 .   ? 13.813  -9.057  20.118  1.00 46.52  ? 767  HOH A O   1 
HETATM 7807 O  O   . HOH Q 6 .   ? -17.456 -38.901 14.234  1.00 55.24  ? 768  HOH A O   1 
HETATM 7808 O  O   . HOH Q 6 .   ? -21.097 -30.294 30.026  1.00 51.65  ? 769  HOH A O   1 
HETATM 7809 O  O   . HOH Q 6 .   ? -9.972  -40.814 5.700   1.00 51.53  ? 770  HOH A O   1 
HETATM 7810 O  O   . HOH Q 6 .   ? -22.162 -13.106 -0.729  1.00 36.26  ? 771  HOH A O   1 
HETATM 7811 O  O   . HOH Q 6 .   ? -7.061  -7.889  35.635  1.00 32.71  ? 772  HOH A O   1 
HETATM 7812 O  O   . HOH Q 6 .   ? -37.468 -16.431 11.817  1.00 47.83  ? 773  HOH A O   1 
HETATM 7813 O  O   . HOH Q 6 .   ? -28.658 -15.781 11.213  1.00 32.91  ? 774  HOH A O   1 
HETATM 7814 O  O   . HOH Q 6 .   ? 8.847   -11.507 9.248   1.00 47.52  ? 775  HOH A O   1 
HETATM 7815 O  O   . HOH Q 6 .   ? -12.346 -9.686  2.922   1.00 33.03  ? 776  HOH A O   1 
HETATM 7816 O  O   . HOH Q 6 .   ? -7.625  -25.441 10.330  1.00 36.28  ? 777  HOH A O   1 
HETATM 7817 O  O   . HOH Q 6 .   ? -35.489 -12.898 6.037   1.00 42.83  ? 778  HOH A O   1 
HETATM 7818 O  O   . HOH Q 6 .   ? -27.342 -15.867 -3.877  1.00 42.15  ? 779  HOH A O   1 
HETATM 7819 O  O   . HOH Q 6 .   ? 6.593   9.455   18.441  1.00 52.75  ? 780  HOH A O   1 
HETATM 7820 O  O   . HOH Q 6 .   ? 2.366   -21.481 0.560   1.00 47.53  ? 781  HOH A O   1 
HETATM 7821 O  O   . HOH Q 6 .   ? 4.329   -17.076 -3.441  1.00 52.31  ? 782  HOH A O   1 
HETATM 7822 O  O   . HOH Q 6 .   ? -5.022  -27.035 -15.150 1.00 57.89  ? 783  HOH A O   1 
HETATM 7823 O  O   . HOH Q 6 .   ? 0.954   13.733  26.338  1.00 61.77  ? 784  HOH A O   1 
HETATM 7824 O  O   . HOH Q 6 .   ? -24.892 -2.468  19.873  1.00 45.83  ? 785  HOH A O   1 
HETATM 7825 O  O   . HOH Q 6 .   ? -16.082 -6.820  -7.672  1.00 42.00  ? 786  HOH A O   1 
HETATM 7826 O  O   . HOH Q 6 .   ? -5.806  -22.269 16.292  1.00 36.25  ? 787  HOH A O   1 
HETATM 7827 O  O   . HOH Q 6 .   ? -25.516 -10.371 30.411  1.00 42.11  ? 788  HOH A O   1 
HETATM 7828 O  O   . HOH Q 6 .   ? -3.600  12.554  19.327  1.00 43.33  ? 789  HOH A O   1 
HETATM 7829 O  O   . HOH Q 6 .   ? -19.258 -2.162  10.646  1.00 50.35  ? 790  HOH A O   1 
HETATM 7830 O  O   . HOH Q 6 .   ? -10.031 -4.546  24.153  1.00 33.82  ? 791  HOH A O   1 
HETATM 7831 O  O   . HOH Q 6 .   ? 1.658   -40.417 0.928   1.00 43.65  ? 792  HOH A O   1 
HETATM 7832 O  O   . HOH Q 6 .   ? -4.458  -37.668 -8.189  1.00 47.60  ? 793  HOH A O   1 
HETATM 7833 O  O   . HOH Q 6 .   ? 9.768   5.864   28.630  1.00 56.26  ? 794  HOH A O   1 
HETATM 7834 O  O   . HOH Q 6 .   ? -10.252 -10.129 33.232  1.00 31.23  ? 795  HOH A O   1 
HETATM 7835 O  O   . HOH Q 6 .   ? 5.191   6.353   12.530  1.00 48.79  ? 796  HOH A O   1 
HETATM 7836 O  O   . HOH Q 6 .   ? -26.381 -28.828 -11.767 1.00 50.21  ? 797  HOH A O   1 
HETATM 7837 O  O   . HOH Q 6 .   ? -0.439  -28.433 15.778  1.00 48.66  ? 798  HOH A O   1 
HETATM 7838 O  O   . HOH Q 6 .   ? -9.771  -42.215 -5.611  1.00 50.38  ? 799  HOH A O   1 
HETATM 7839 O  O   . HOH Q 6 .   ? -31.186 -2.883  29.490  1.00 71.92  ? 800  HOH A O   1 
HETATM 7840 O  O   . HOH Q 6 .   ? -22.600 -32.897 6.889   1.00 59.62  ? 801  HOH A O   1 
HETATM 7841 O  O   . HOH Q 6 .   ? -13.445 -7.630  -0.258  1.00 54.76  ? 802  HOH A O   1 
HETATM 7842 O  O   . HOH Q 6 .   ? 10.374  -20.442 21.607  1.00 46.69  ? 803  HOH A O   1 
HETATM 7843 O  O   . HOH Q 6 .   ? -39.737 -14.134 16.330  1.00 53.57  ? 804  HOH A O   1 
HETATM 7844 O  O   . HOH Q 6 .   ? -19.520 -14.801 -4.457  1.00 34.46  ? 805  HOH A O   1 
HETATM 7845 O  O   . HOH Q 6 .   ? -13.557 -43.122 9.937   1.00 61.34  ? 806  HOH A O   1 
HETATM 7846 O  O   . HOH Q 6 .   ? -20.374 -9.421  -6.985  1.00 41.45  ? 807  HOH A O   1 
HETATM 7847 O  O   . HOH Q 6 .   ? -24.332 -14.073 -1.543  1.00 36.13  ? 808  HOH A O   1 
HETATM 7848 O  O   . HOH Q 6 .   ? -30.731 -4.427  27.021  1.00 49.59  ? 809  HOH A O   1 
HETATM 7849 O  O   . HOH Q 6 .   ? -35.183 -19.854 14.879  1.00 44.68  ? 810  HOH A O   1 
HETATM 7850 O  O   . HOH Q 6 .   ? -39.006 -17.141 21.144  1.00 52.09  ? 811  HOH A O   1 
HETATM 7851 O  O   . HOH Q 6 .   ? 10.521  -3.022  21.332  1.00 47.42  ? 812  HOH A O   1 
HETATM 7852 O  O   . HOH Q 6 .   ? -11.500 -32.470 20.627  1.00 48.74  ? 813  HOH A O   1 
HETATM 7853 O  O   . HOH Q 6 .   ? 12.727  -7.564  18.152  1.00 49.34  ? 814  HOH A O   1 
HETATM 7854 O  O   . HOH Q 6 .   ? -0.681  -1.499  -8.760  1.00 58.36  ? 815  HOH A O   1 
HETATM 7855 O  O   . HOH Q 6 .   ? -1.340  -22.430 -11.442 1.00 45.67  ? 816  HOH A O   1 
HETATM 7856 O  O   . HOH Q 6 .   ? 11.964  -1.521  17.309  1.00 49.32  ? 817  HOH A O   1 
HETATM 7857 O  O   . HOH Q 6 .   ? -5.653  13.585  20.837  1.00 51.45  ? 818  HOH A O   1 
HETATM 7858 O  O   . HOH Q 6 .   ? -3.110  -11.454 -11.300 1.00 48.66  ? 819  HOH A O   1 
HETATM 7859 O  O   . HOH Q 6 .   ? -27.606 -7.856  1.568   1.00 50.38  ? 820  HOH A O   1 
HETATM 7860 O  O   . HOH Q 6 .   ? -23.618 -0.675  10.794  1.00 46.35  ? 821  HOH A O   1 
HETATM 7861 O  O   . HOH Q 6 .   ? -8.856  -4.850  -3.653  1.00 43.41  ? 822  HOH A O   1 
HETATM 7862 O  O   . HOH Q 6 .   ? 14.511  -12.059 16.957  1.00 51.84  ? 823  HOH A O   1 
HETATM 7863 O  O   . HOH Q 6 .   ? 3.038   -5.633  -2.610  1.00 42.60  ? 824  HOH A O   1 
HETATM 7864 O  O   . HOH Q 6 .   ? -18.933 -6.679  1.536   1.00 47.23  ? 825  HOH A O   1 
HETATM 7865 O  O   . HOH Q 6 .   ? 1.244   -14.529 29.843  1.00 35.63  ? 826  HOH A O   1 
HETATM 7866 O  O   . HOH Q 6 .   ? -19.825 -14.218 -1.733  1.00 33.86  ? 827  HOH A O   1 
HETATM 7867 O  O   . HOH Q 6 .   ? 0.050   9.245   28.427  1.00 56.90  ? 828  HOH A O   1 
HETATM 7868 O  O   . HOH Q 6 .   ? -3.129  -12.500 11.360  1.00 35.74  ? 829  HOH A O   1 
HETATM 7869 O  O   . HOH Q 6 .   ? -22.737 -28.051 0.585   1.00 53.05  ? 830  HOH A O   1 
HETATM 7870 O  O   . HOH Q 6 .   ? 0.753   -10.055 36.252  1.00 35.98  ? 831  HOH A O   1 
HETATM 7871 O  O   . HOH Q 6 .   ? -16.196 -37.697 -4.946  1.00 51.74  ? 832  HOH A O   1 
HETATM 7872 O  O   . HOH Q 6 .   ? -5.216  -19.135 23.071  1.00 45.71  ? 833  HOH A O   1 
HETATM 7873 O  O   . HOH Q 6 .   ? -7.676  -46.461 1.248   1.00 52.64  ? 834  HOH A O   1 
HETATM 7874 O  O   . HOH Q 6 .   ? -34.423 -19.444 8.930   1.00 43.40  ? 835  HOH A O   1 
HETATM 7875 O  O   . HOH Q 6 .   ? -22.309 -6.644  -1.664  1.00 49.29  ? 836  HOH A O   1 
HETATM 7876 O  O   . HOH Q 6 .   ? -23.507 5.413   13.341  1.00 51.91  ? 837  HOH A O   1 
HETATM 7877 O  O   . HOH Q 6 .   ? 7.728   -9.672  30.166  1.00 47.81  ? 838  HOH A O   1 
HETATM 7878 O  O   . HOH Q 6 .   ? -27.537 -4.663  4.445   1.00 55.45  ? 839  HOH A O   1 
HETATM 7879 O  O   . HOH Q 6 .   ? -22.609 0.507   21.566  1.00 42.05  ? 840  HOH A O   1 
HETATM 7880 O  O   . HOH Q 6 .   ? -15.521 -20.156 6.525   1.00 32.91  ? 841  HOH A O   1 
HETATM 7881 O  O   . HOH Q 6 .   ? -17.711 -8.981  -4.101  1.00 41.82  ? 842  HOH A O   1 
HETATM 7882 O  O   . HOH Q 6 .   ? -16.393 -14.907 35.089  1.00 44.03  ? 843  HOH A O   1 
HETATM 7883 O  O   . HOH Q 6 .   ? -26.606 1.781   16.029  1.00 58.35  ? 844  HOH A O   1 
HETATM 7884 O  O   . HOH Q 6 .   ? 9.255   -4.034  5.787   1.00 55.05  ? 845  HOH A O   1 
HETATM 7885 O  O   . HOH Q 6 .   ? -8.698  -22.111 19.097  1.00 39.04  ? 846  HOH A O   1 
HETATM 7886 O  O   . HOH Q 6 .   ? -16.358 -30.348 30.674  1.00 65.07  ? 847  HOH A O   1 
HETATM 7887 O  O   . HOH Q 6 .   ? -27.847 -27.302 15.117  1.00 52.47  ? 848  HOH A O   1 
HETATM 7888 O  O   . HOH Q 6 .   ? -16.536 -8.027  -0.526  1.00 47.27  ? 849  HOH A O   1 
HETATM 7889 O  O   . HOH Q 6 .   ? -1.034  -17.797 -5.090  1.00 46.53  ? 850  HOH A O   1 
HETATM 7890 O  O   . HOH Q 6 .   ? 8.643   -8.010  -7.762  1.00 62.71  ? 851  HOH A O   1 
HETATM 7891 O  O   . HOH Q 6 .   ? -13.663 7.966   23.201  1.00 43.40  ? 852  HOH A O   1 
HETATM 7892 O  O   . HOH Q 6 .   ? -29.448 -16.090 -3.977  1.00 56.91  ? 853  HOH A O   1 
HETATM 7893 O  O   . HOH Q 6 .   ? -33.557 -13.970 34.583  1.00 56.30  ? 854  HOH A O   1 
HETATM 7894 O  O   . HOH Q 6 .   ? 9.160   -13.416 -0.641  1.00 51.33  ? 855  HOH A O   1 
HETATM 7895 O  O   . HOH Q 6 .   ? -16.308 6.881   22.306  1.00 43.33  ? 856  HOH A O   1 
HETATM 7896 O  O   . HOH Q 6 .   ? -3.398  -18.795 -15.311 1.00 61.56  ? 857  HOH A O   1 
HETATM 7897 O  O   . HOH Q 6 .   ? 5.512   5.693   24.330  1.00 46.73  ? 858  HOH A O   1 
HETATM 7898 O  O   . HOH Q 6 .   ? -32.910 -6.032  26.743  1.00 55.08  ? 859  HOH A O   1 
HETATM 7899 O  O   . HOH Q 6 .   ? -19.409 -28.692 1.664   1.00 44.25  ? 860  HOH A O   1 
HETATM 7900 O  O   . HOH Q 6 .   ? -16.230 6.971   13.200  1.00 54.18  ? 861  HOH A O   1 
HETATM 7901 O  O   . HOH Q 6 .   ? 11.158  -18.094 28.363  1.00 52.55  ? 862  HOH A O   1 
HETATM 7902 O  O   . HOH Q 6 .   ? -28.398 -23.018 21.385  1.00 50.85  ? 863  HOH A O   1 
HETATM 7903 O  O   . HOH Q 6 .   ? -7.497  -8.071  -11.648 1.00 35.31  ? 864  HOH A O   1 
HETATM 7904 O  O   . HOH Q 6 .   ? -10.724 -20.793 34.881  1.00 51.83  ? 865  HOH A O   1 
HETATM 7905 O  O   . HOH Q 6 .   ? -6.176  -18.041 27.333  1.00 44.98  ? 866  HOH A O   1 
HETATM 7906 O  O   . HOH Q 6 .   ? -11.868 -5.922  -3.965  1.00 36.98  ? 867  HOH A O   1 
HETATM 7907 O  O   . HOH Q 6 .   ? -20.917 -1.960  25.162  1.00 46.58  ? 868  HOH A O   1 
HETATM 7908 O  O   . HOH Q 6 .   ? -16.784 -38.062 2.933   1.00 48.70  ? 869  HOH A O   1 
HETATM 7909 O  O   . HOH Q 6 .   ? -35.714 -15.666 14.399  1.00 45.01  ? 870  HOH A O   1 
HETATM 7910 O  O   . HOH Q 6 .   ? -29.304 -12.538 -2.004  1.00 53.74  ? 871  HOH A O   1 
HETATM 7911 O  O   . HOH Q 6 .   ? -3.269  -34.224 -11.132 1.00 49.10  ? 872  HOH A O   1 
HETATM 7912 O  O   . HOH Q 6 .   ? 2.795   -29.128 5.625   1.00 54.79  ? 873  HOH A O   1 
HETATM 7913 O  O   . HOH Q 6 .   ? 1.562   -35.879 2.269   1.00 54.99  ? 874  HOH A O   1 
HETATM 7914 O  O   . HOH Q 6 .   ? -9.372  -7.292  -2.162  1.00 36.33  ? 875  HOH A O   1 
HETATM 7915 O  O   . HOH Q 6 .   ? -1.108  -7.212  -10.578 1.00 55.16  ? 876  HOH A O   1 
HETATM 7916 O  O   . HOH Q 6 .   ? -27.860 -27.218 6.241   1.00 45.62  ? 877  HOH A O   1 
HETATM 7917 O  O   . HOH Q 6 .   ? -19.930 -32.171 -3.889  1.00 47.96  ? 878  HOH A O   1 
HETATM 7918 O  O   . HOH Q 6 .   ? -8.441  -5.538  -10.562 1.00 34.64  ? 879  HOH A O   1 
HETATM 7919 O  O   . HOH Q 6 .   ? -22.292 3.749   10.764  1.00 47.36  ? 880  HOH A O   1 
HETATM 7920 O  O   . HOH Q 6 .   ? -7.973  -17.396 31.257  1.00 41.91  ? 881  HOH A O   1 
HETATM 7921 O  O   . HOH Q 6 .   ? -5.667  4.136   31.254  1.00 53.16  ? 882  HOH A O   1 
HETATM 7922 O  O   . HOH Q 6 .   ? 14.035  -15.069 13.576  1.00 50.33  ? 883  HOH A O   1 
HETATM 7923 O  O   . HOH Q 6 .   ? -16.083 -10.424 -10.662 1.00 49.64  ? 884  HOH A O   1 
HETATM 7924 O  O   . HOH Q 6 .   ? -35.590 -2.244  16.152  1.00 52.11  ? 885  HOH A O   1 
HETATM 7925 O  O   . HOH Q 6 .   ? 6.635   -5.465  38.120  1.00 46.92  ? 886  HOH A O   1 
HETATM 7926 O  O   . HOH Q 6 .   ? -14.947 -34.425 21.070  1.00 49.05  ? 887  HOH A O   1 
HETATM 7927 O  O   . HOH Q 6 .   ? 7.409   -16.301 9.262   1.00 52.01  ? 888  HOH A O   1 
HETATM 7928 O  O   . HOH Q 6 .   ? 5.137   -16.636 7.999   1.00 48.29  ? 889  HOH A O   1 
HETATM 7929 O  O   . HOH Q 6 .   ? 4.732   -29.172 12.627  1.00 61.13  ? 890  HOH A O   1 
HETATM 7930 O  O   . HOH Q 6 .   ? -6.724  9.970   29.545  1.00 55.27  ? 891  HOH A O   1 
HETATM 7931 O  O   . HOH Q 6 .   ? -4.554  -28.921 16.961  1.00 54.22  ? 892  HOH A O   1 
HETATM 7932 O  O   . HOH Q 6 .   ? -18.488 -42.491 25.583  1.00 65.54  ? 893  HOH A O   1 
HETATM 7933 O  O   . HOH Q 6 .   ? -7.582  -30.644 16.515  1.00 58.37  ? 894  HOH A O   1 
HETATM 7934 O  O   . HOH Q 6 .   ? 0.861   -29.568 7.383   1.00 48.66  ? 895  HOH A O   1 
HETATM 7935 O  O   . HOH Q 6 .   ? -6.259  -9.892  37.670  1.00 34.10  ? 896  HOH A O   1 
HETATM 7936 O  O   . HOH Q 6 .   ? -8.135  2.632   13.193  1.00 55.75  ? 897  HOH A O   1 
HETATM 7937 O  O   . HOH Q 6 .   ? -30.652 -22.651 20.135  1.00 45.77  ? 898  HOH A O   1 
HETATM 7938 O  O   . HOH Q 6 .   ? 6.005   -26.098 -0.358  1.00 58.72  ? 899  HOH A O   1 
HETATM 7939 O  O   . HOH Q 6 .   ? 13.497  -18.965 14.746  1.00 50.02  ? 900  HOH A O   1 
HETATM 7940 O  O   . HOH Q 6 .   ? -0.295  -34.881 -3.800  1.00 43.94  ? 901  HOH A O   1 
HETATM 7941 O  O   . HOH Q 6 .   ? 4.382   -20.187 1.215   1.00 57.95  ? 902  HOH A O   1 
HETATM 7942 O  O   . HOH Q 6 .   ? -0.488  -21.713 -5.552  1.00 54.01  ? 903  HOH A O   1 
HETATM 7943 O  O   . HOH Q 6 .   ? 2.568   -23.264 29.075  1.00 70.81  ? 904  HOH A O   1 
HETATM 7944 O  O   . HOH Q 6 .   ? -22.583 -0.398  24.199  1.00 48.13  ? 905  HOH A O   1 
HETATM 7945 O  O   . HOH Q 6 .   ? 16.044  -12.248 18.923  1.00 53.74  ? 906  HOH A O   1 
HETATM 7946 O  O   . HOH Q 6 .   ? -4.048  -13.926 34.026  1.00 40.03  ? 907  HOH A O   1 
HETATM 7947 O  O   . HOH Q 6 .   ? -45.093 -13.476 11.884  1.00 53.27  ? 908  HOH A O   1 
HETATM 7948 O  O   . HOH Q 6 .   ? 10.694  4.997   11.731  1.00 61.97  ? 909  HOH A O   1 
HETATM 7949 O  O   . HOH Q 6 .   ? -11.361 -42.095 9.093   1.00 59.14  ? 910  HOH A O   1 
HETATM 7950 O  O   . HOH Q 6 .   ? 0.754   -3.184  -2.968  1.00 54.02  ? 911  HOH A O   1 
HETATM 7951 O  O   . HOH Q 6 .   ? -26.831 -27.097 19.995  1.00 52.23  ? 912  HOH A O   1 
HETATM 7952 O  O   . HOH Q 6 .   ? -8.950  -12.162 -16.126 1.00 55.66  ? 913  HOH A O   1 
HETATM 7953 O  O   . HOH Q 6 .   ? -7.279  -20.064 21.938  1.00 49.58  ? 914  HOH A O   1 
HETATM 7954 O  O   . HOH Q 6 .   ? -4.502  -41.784 12.173  1.00 63.10  ? 915  HOH A O   1 
HETATM 7955 O  O   . HOH Q 6 .   ? -4.979  6.232   -6.414  1.00 47.12  ? 916  HOH A O   1 
HETATM 7956 O  O   . HOH Q 6 .   ? -35.116 -23.221 10.149  1.00 56.85  ? 917  HOH A O   1 
HETATM 7957 O  O   . HOH Q 6 .   ? -4.188  -19.556 -18.275 1.00 66.89  ? 918  HOH A O   1 
HETATM 7958 O  O   . HOH Q 6 .   ? -0.487  -5.517  -8.783  1.00 56.37  ? 919  HOH A O   1 
HETATM 7959 O  O   . HOH Q 6 .   ? 11.195  -8.806  30.867  1.00 50.90  ? 920  HOH A O   1 
HETATM 7960 O  O   . HOH Q 6 .   ? -13.396 10.077  20.983  1.00 45.05  ? 921  HOH A O   1 
HETATM 7961 O  O   . HOH Q 6 .   ? -39.157 -16.279 14.478  1.00 54.22  ? 922  HOH A O   1 
HETATM 7962 O  O   . HOH Q 6 .   ? -30.105 -14.641 -8.038  1.00 64.42  ? 923  HOH A O   1 
HETATM 7963 O  O   . HOH Q 6 .   ? -28.906 -21.466 -6.970  1.00 51.82  ? 924  HOH A O   1 
HETATM 7964 O  O   . HOH Q 6 .   ? 12.399  -17.474 13.231  1.00 50.35  ? 925  HOH A O   1 
HETATM 7965 O  O   . HOH Q 6 .   ? 6.118   -23.993 19.823  1.00 59.41  ? 926  HOH A O   1 
HETATM 7966 O  O   . HOH Q 6 .   ? -19.500 4.088   26.656  1.00 53.74  ? 927  HOH A O   1 
HETATM 7967 O  O   . HOH Q 6 .   ? -2.114  -19.700 -7.015  1.00 54.69  ? 928  HOH A O   1 
HETATM 7968 O  O   . HOH Q 6 .   ? -11.045 -46.206 -5.621  1.00 58.53  ? 929  HOH A O   1 
HETATM 7969 O  O   . HOH Q 6 .   ? -19.986 -5.658  34.046  1.00 58.21  ? 930  HOH A O   1 
HETATM 7970 O  O   . HOH Q 6 .   ? -8.919  -17.620 29.005  1.00 48.16  ? 931  HOH A O   1 
HETATM 7971 O  O   . HOH Q 6 .   ? -38.914 -14.162 21.298  1.00 63.39  ? 932  HOH A O   1 
HETATM 7972 O  O   . HOH Q 6 .   ? 11.450  -13.590 38.770  1.00 51.67  ? 933  HOH A O   1 
HETATM 7973 O  O   . HOH Q 6 .   ? 15.012  -0.558  14.338  1.00 61.47  ? 934  HOH A O   1 
HETATM 7974 O  O   . HOH Q 6 .   ? -40.078 -18.612 22.707  1.00 65.70  ? 935  HOH A O   1 
HETATM 7975 O  O   . HOH Q 6 .   ? -3.165  -20.491 22.803  1.00 49.93  ? 936  HOH A O   1 
HETATM 7976 O  O   . HOH Q 6 .   ? -12.415 -15.539 37.777  1.00 50.93  ? 937  HOH A O   1 
HETATM 7977 O  O   . HOH Q 6 .   ? -7.732  12.174  17.574  1.00 49.39  ? 938  HOH A O   1 
HETATM 7978 O  O   . HOH Q 6 .   ? 11.773  -4.402  19.115  1.00 58.63  ? 939  HOH A O   1 
HETATM 7979 O  O   . HOH Q 6 .   ? 0.412   1.608   35.321  1.00 56.70  ? 940  HOH A O   1 
HETATM 7980 O  O   . HOH Q 6 .   ? -18.873 -15.445 0.510   1.00 33.35  ? 941  HOH A O   1 
HETATM 7981 O  O   . HOH Q 6 .   ? -12.918 -35.710 21.708  1.00 54.83  ? 942  HOH A O   1 
HETATM 7982 O  O   . HOH Q 6 .   ? -12.195 12.539  21.907  1.00 51.59  ? 943  HOH A O   1 
HETATM 7983 O  O   . HOH Q 6 .   ? -0.724  -36.585 -7.486  1.00 51.02  ? 944  HOH A O   1 
HETATM 7984 O  O   . HOH Q 6 .   ? -34.581 -11.607 1.895   1.00 59.15  ? 945  HOH A O   1 
HETATM 7985 O  O   . HOH Q 6 .   ? -28.722 -25.938 -14.481 1.00 53.93  ? 946  HOH A O   1 
HETATM 7986 O  O   . HOH Q 6 .   ? 14.774  -10.315 15.113  1.00 57.26  ? 947  HOH A O   1 
HETATM 7987 O  O   . HOH Q 6 .   ? -13.426 -13.469 39.056  1.00 43.11  ? 948  HOH A O   1 
HETATM 7988 O  O   . HOH Q 6 .   ? -6.069  -38.824 -8.923  1.00 58.87  ? 949  HOH A O   1 
HETATM 7989 O  O   . HOH Q 6 .   ? -14.865 7.458   10.429  1.00 60.55  ? 950  HOH A O   1 
HETATM 7990 O  O   . HOH Q 6 .   ? -3.219  -24.981 -13.338 1.00 46.70  ? 951  HOH A O   1 
HETATM 7991 O  O   . HOH Q 6 .   ? -2.237  -15.450 -12.049 1.00 48.64  ? 952  HOH A O   1 
HETATM 7992 O  O   . HOH Q 6 .   ? -6.722  -23.097 20.469  1.00 46.76  ? 953  HOH A O   1 
HETATM 7993 O  O   . HOH Q 6 .   ? -19.313 -39.084 6.453   1.00 64.55  ? 954  HOH A O   1 
HETATM 7994 O  O   . HOH Q 6 .   ? 3.552   -20.872 25.899  1.00 47.48  ? 955  HOH A O   1 
HETATM 7995 O  O   . HOH Q 6 .   ? 8.618   -25.062 16.404  1.00 54.61  ? 956  HOH A O   1 
HETATM 7996 O  O   . HOH Q 6 .   ? -9.053  -44.426 -7.001  1.00 48.73  ? 957  HOH A O   1 
HETATM 7997 O  O   . HOH Q 6 .   ? 6.164   11.588  19.805  1.00 60.59  ? 958  HOH A O   1 
HETATM 7998 O  O   . HOH Q 6 .   ? -26.093 1.843   18.766  1.00 59.12  ? 959  HOH A O   1 
HETATM 7999 O  O   . HOH Q 6 .   ? -2.106  14.561  18.876  1.00 51.92  ? 960  HOH A O   1 
HETATM 8000 O  O   . HOH Q 6 .   ? -28.551 -24.248 -3.250  1.00 53.59  ? 961  HOH A O   1 
HETATM 8001 O  O   . HOH Q 6 .   ? -23.134 -1.587  27.923  1.00 53.93  ? 962  HOH A O   1 
HETATM 8002 O  O   . HOH Q 6 .   ? -8.952  12.970  15.340  1.00 55.18  ? 963  HOH A O   1 
HETATM 8003 O  O   . HOH Q 6 .   ? 0.005   -34.303 -0.947  1.00 46.20  ? 964  HOH A O   1 
HETATM 8004 O  O   . HOH Q 6 .   ? 16.202  -10.111 19.936  1.00 60.05  ? 965  HOH A O   1 
HETATM 8005 O  O   . HOH Q 6 .   ? 1.849   -14.633 34.056  1.00 45.33  ? 966  HOH A O   1 
HETATM 8006 O  O   . HOH Q 6 .   ? -22.213 -32.855 29.920  1.00 53.49  ? 967  HOH A O   1 
HETATM 8007 O  O   . HOH Q 6 .   ? -34.555 -13.827 3.555   1.00 44.76  ? 968  HOH A O   1 
HETATM 8008 O  O   . HOH Q 6 .   ? 4.351   -20.821 3.978   1.00 59.73  ? 969  HOH A O   1 
HETATM 8009 O  O   . HOH Q 6 .   ? -4.106  12.753  15.019  1.00 53.85  ? 970  HOH A O   1 
HETATM 8010 O  O   . HOH Q 6 .   ? 2.182   -31.862 -0.529  1.00 49.25  ? 971  HOH A O   1 
HETATM 8011 O  O   . HOH Q 6 .   ? -15.674 -18.063 -20.510 1.00 57.56  ? 972  HOH A O   1 
HETATM 8012 O  O   . HOH Q 6 .   ? 18.149  -14.336 18.877  1.00 51.32  ? 973  HOH A O   1 
HETATM 8013 O  O   . HOH Q 6 .   ? -6.996  -1.858  2.698   1.00 58.74  ? 974  HOH A O   1 
HETATM 8014 O  O   . HOH Q 6 .   ? 0.547   -33.250 5.595   1.00 51.76  ? 975  HOH A O   1 
HETATM 8015 O  O   . HOH Q 6 .   ? -3.235  -8.656  -11.874 1.00 55.83  ? 976  HOH A O   1 
HETATM 8016 O  O   . HOH Q 6 .   ? -37.014 -19.818 9.573   1.00 54.59  ? 977  HOH A O   1 
HETATM 8017 O  O   . HOH Q 6 .   ? -19.544 2.006   28.592  1.00 53.56  ? 978  HOH A O   1 
HETATM 8018 O  O   . HOH Q 6 .   ? -27.205 -25.062 -5.333  1.00 58.68  ? 979  HOH A O   1 
HETATM 8019 O  O   . HOH Q 6 .   ? -8.112  13.712  19.859  1.00 47.12  ? 980  HOH A O   1 
HETATM 8020 O  O   . HOH Q 6 .   ? -5.946  -19.872 25.505  1.00 50.55  ? 981  HOH A O   1 
HETATM 8021 O  O   . HOH Q 6 .   ? 4.441   7.835   24.841  1.00 54.70  ? 982  HOH A O   1 
HETATM 8022 O  O   . HOH Q 6 .   ? -7.049  2.976   35.321  1.00 64.61  ? 983  HOH A O   1 
HETATM 8023 O  O   . HOH Q 6 .   ? -4.802  3.994   6.252   1.00 56.50  ? 984  HOH A O   1 
HETATM 8024 O  O   . HOH Q 6 .   ? -5.862  -27.675 23.666  1.00 66.28  ? 985  HOH A O   1 
HETATM 8025 O  O   . HOH Q 6 .   ? -18.865 -36.529 7.873   1.00 62.30  ? 986  HOH A O   1 
HETATM 8026 O  O   . HOH Q 6 .   ? -12.458 4.920   29.378  1.00 54.16  ? 987  HOH A O   1 
HETATM 8027 O  O   . HOH Q 6 .   ? -15.626 10.419  19.732  1.00 57.53  ? 988  HOH A O   1 
HETATM 8028 O  O   . HOH Q 6 .   ? -5.252  -7.546  -12.884 1.00 50.38  ? 989  HOH A O   1 
HETATM 8029 O  O   . HOH Q 6 .   ? -5.182  11.788  17.235  1.00 48.07  ? 990  HOH A O   1 
HETATM 8030 O  O   . HOH Q 6 .   ? -16.594 -35.464 3.404   1.00 55.60  ? 991  HOH A O   1 
HETATM 8031 O  O   . HOH Q 6 .   ? -15.903 -19.810 -22.223 1.00 62.19  ? 992  HOH A O   1 
HETATM 8032 O  O   . HOH Q 6 .   ? 2.118   -31.463 3.985   1.00 43.93  ? 993  HOH A O   1 
HETATM 8033 O  O   . HOH Q 6 .   ? 7.886   6.594   24.522  1.00 54.94  ? 994  HOH A O   1 
HETATM 8034 O  O   . HOH Q 6 .   ? -16.525 -26.813 32.181  1.00 58.79  ? 995  HOH A O   1 
HETATM 8035 O  O   . HOH Q 6 .   ? -27.285 -29.119 -6.095  1.00 58.36  ? 996  HOH A O   1 
HETATM 8036 O  O   . HOH Q 6 .   ? -17.511 9.088   21.398  1.00 60.60  ? 997  HOH A O   1 
HETATM 8037 O  O   . HOH Q 6 .   ? -0.415  -33.659 1.800   1.00 44.86  ? 998  HOH A O   1 
HETATM 8038 O  O   . HOH Q 6 .   ? 8.811   -21.187 26.082  1.00 62.04  ? 999  HOH A O   1 
HETATM 8039 O  O   . HOH Q 6 .   ? -7.559  -3.776  0.044   1.00 51.85  ? 1000 HOH A O   1 
HETATM 8040 O  O   . HOH Q 6 .   ? -13.653 -15.042 -21.304 1.00 63.37  ? 1001 HOH A O   1 
HETATM 8041 O  O   . HOH Q 6 .   ? -5.282  -23.357 22.965  1.00 58.13  ? 1002 HOH A O   1 
HETATM 8042 O  O   . HOH Q 6 .   ? 8.140   9.294   22.593  1.00 63.25  ? 1003 HOH A O   1 
HETATM 8043 O  O   . HOH Q 6 .   ? -15.698 -15.617 -21.737 1.00 60.88  ? 1004 HOH A O   1 
HETATM 8044 O  O   . HOH R 6 .   ? 0.610   -9.670  65.249  1.00 46.68  ? 601  HOH B O   1 
HETATM 8045 O  O   . HOH R 6 .   ? 2.851   7.182   62.380  1.00 59.52  ? 602  HOH B O   1 
HETATM 8046 O  O   . HOH R 6 .   ? 0.311   -46.559 61.416  1.00 63.91  ? 603  HOH B O   1 
HETATM 8047 O  O   . HOH R 6 .   ? 9.158   -31.497 60.602  1.00 45.27  ? 604  HOH B O   1 
HETATM 8048 O  O   . HOH R 6 .   ? -3.940  -10.798 87.906  1.00 58.99  ? 605  HOH B O   1 
HETATM 8049 O  O   . HOH R 6 .   ? -12.555 -40.652 74.255  1.00 47.05  ? 606  HOH B O   1 
HETATM 8050 O  O   . HOH R 6 .   ? 0.853   -33.434 88.564  1.00 65.11  ? 607  HOH B O   1 
HETATM 8051 O  O   . HOH R 6 .   ? -3.587  -46.292 74.157  1.00 53.70  ? 608  HOH B O   1 
HETATM 8052 O  O   . HOH R 6 .   ? -0.615  -20.105 39.342  1.00 52.26  ? 609  HOH B O   1 
HETATM 8053 O  O   . HOH R 6 .   ? -0.322  -14.856 89.573  1.00 46.54  ? 610  HOH B O   1 
HETATM 8054 O  O   . HOH R 6 .   ? 11.477  -18.027 90.870  1.00 50.82  ? 611  HOH B O   1 
HETATM 8055 O  O   . HOH R 6 .   ? 6.963   -35.061 57.706  1.00 53.72  ? 612  HOH B O   1 
HETATM 8056 O  O   . HOH R 6 .   ? -4.964  9.857   49.495  1.00 50.89  ? 613  HOH B O   1 
HETATM 8057 O  O   . HOH R 6 .   ? -5.594  -23.561 89.876  1.00 48.87  ? 614  HOH B O   1 
HETATM 8058 O  O   . HOH R 6 .   ? -5.112  -28.678 53.876  1.00 50.20  ? 615  HOH B O   1 
HETATM 8059 O  O   . HOH R 6 .   ? -20.078 5.103   40.397  1.00 57.86  ? 616  HOH B O   1 
HETATM 8060 O  O   . HOH R 6 .   ? -4.910  -1.730  75.518  1.00 56.92  ? 617  HOH B O   1 
HETATM 8061 O  O   . HOH R 6 .   ? 5.724   -27.191 75.931  1.00 42.81  ? 618  HOH B O   1 
HETATM 8062 O  O   . HOH R 6 .   ? 3.539   -27.959 89.022  1.00 43.64  ? 619  HOH B O   1 
HETATM 8063 O  O   . HOH R 6 .   ? -14.517 0.802   42.624  1.00 43.50  ? 620  HOH B O   1 
HETATM 8064 O  O   . HOH R 6 .   ? 5.278   1.444   49.005  1.00 45.63  ? 621  HOH B O   1 
HETATM 8065 O  O   . HOH R 6 .   ? 0.323   -4.129  68.194  1.00 56.05  ? 622  HOH B O   1 
HETATM 8066 O  O   . HOH R 6 .   ? 9.508   -15.006 39.152  1.00 50.74  ? 623  HOH B O   1 
HETATM 8067 O  O   . HOH R 6 .   ? -13.193 -32.144 63.882  1.00 54.36  ? 624  HOH B O   1 
HETATM 8068 O  O   . HOH R 6 .   ? -21.445 -15.896 36.140  1.00 46.88  ? 625  HOH B O   1 
HETATM 8069 O  O   . HOH R 6 .   ? -6.447  -12.183 86.777  1.00 49.87  ? 626  HOH B O   1 
HETATM 8070 O  O   . HOH R 6 .   ? 8.080   -2.343  42.350  1.00 50.78  ? 627  HOH B O   1 
HETATM 8071 O  O   . HOH R 6 .   ? -18.412 -7.572  79.792  1.00 49.99  ? 628  HOH B O   1 
HETATM 8072 O  O   . HOH R 6 .   ? -21.258 -8.533  34.600  1.00 48.20  ? 629  HOH B O   1 
HETATM 8073 O  O   . HOH R 6 .   ? -16.835 -21.202 46.371  1.00 49.60  ? 630  HOH B O   1 
HETATM 8074 O  O   . HOH R 6 .   ? -19.607 -22.652 52.534  1.00 47.41  ? 631  HOH B O   1 
HETATM 8075 O  O   . HOH R 6 .   ? 29.392  -4.388  70.081  1.00 45.15  ? 632  HOH B O   1 
HETATM 8076 O  O   . HOH R 6 .   ? -19.589 -23.305 64.111  1.00 49.64  ? 633  HOH B O   1 
HETATM 8077 O  O   . HOH R 6 .   ? 15.629  -30.912 90.205  1.00 62.65  ? 634  HOH B O   1 
HETATM 8078 O  O   . HOH R 6 .   ? 6.515   -13.040 87.965  1.00 41.54  ? 635  HOH B O   1 
HETATM 8079 O  O   . HOH R 6 .   ? -15.828 7.603   51.392  1.00 41.63  ? 636  HOH B O   1 
HETATM 8080 O  O   . HOH R 6 .   ? -2.577  -36.512 86.648  1.00 54.11  ? 637  HOH B O   1 
HETATM 8081 O  O   . HOH R 6 .   ? 18.588  -2.319  65.389  1.00 54.49  ? 638  HOH B O   1 
HETATM 8082 O  O   . HOH R 6 .   ? -2.924  -31.559 59.235  1.00 46.21  ? 639  HOH B O   1 
HETATM 8083 O  O   . HOH R 6 .   ? 1.482   0.805   42.621  1.00 52.21  ? 640  HOH B O   1 
HETATM 8084 O  O   . HOH R 6 .   ? -4.548  12.152  53.974  1.00 49.10  ? 641  HOH B O   1 
HETATM 8085 O  O   . HOH R 6 .   ? 18.506  -20.362 78.543  1.00 53.84  ? 642  HOH B O   1 
HETATM 8086 O  O   . HOH R 6 .   ? -19.179 -3.129  40.352  1.00 46.79  ? 643  HOH B O   1 
HETATM 8087 O  O   . HOH R 6 .   ? -1.851  1.611   61.291  1.00 47.78  ? 644  HOH B O   1 
HETATM 8088 O  O   . HOH R 6 .   ? 8.757   -15.267 68.715  1.00 31.30  ? 645  HOH B O   1 
HETATM 8089 O  O   . HOH R 6 .   ? 13.806  -14.199 79.020  1.00 38.56  ? 646  HOH B O   1 
HETATM 8090 O  O   . HOH R 6 .   ? -17.671 -16.472 70.273  1.00 41.66  ? 647  HOH B O   1 
HETATM 8091 O  O   . HOH R 6 .   ? 11.933  -9.721  66.728  1.00 38.76  ? 648  HOH B O   1 
HETATM 8092 O  O   . HOH R 6 .   ? -12.178 -27.029 58.839  1.00 43.38  ? 649  HOH B O   1 
HETATM 8093 O  O   . HOH R 6 .   ? 9.608   -36.782 45.701  1.00 59.25  ? 650  HOH B O   1 
HETATM 8094 O  O   . HOH R 6 .   ? 21.297  -20.329 59.326  1.00 38.91  ? 651  HOH B O   1 
HETATM 8095 O  O   . HOH R 6 .   ? 21.953  -23.449 67.217  1.00 37.12  ? 652  HOH B O   1 
HETATM 8096 O  O   . HOH R 6 .   ? 4.763   -10.543 84.376  1.00 48.49  ? 653  HOH B O   1 
HETATM 8097 O  O   . HOH R 6 .   ? 12.734  -27.558 78.236  1.00 49.55  ? 654  HOH B O   1 
HETATM 8098 O  O   . HOH R 6 .   ? -18.658 4.775   62.978  1.00 35.22  ? 655  HOH B O   1 
HETATM 8099 O  O   . HOH R 6 .   ? -9.285  -23.178 49.617  1.00 55.85  ? 656  HOH B O   1 
HETATM 8100 O  O   . HOH R 6 .   ? -21.435 9.425   58.406  1.00 50.03  ? 657  HOH B O   1 
HETATM 8101 O  O   . HOH R 6 .   ? 4.548   -44.156 77.584  1.00 58.11  ? 658  HOH B O   1 
HETATM 8102 O  O   . HOH R 6 .   ? -11.296 8.306   40.841  1.00 57.79  ? 659  HOH B O   1 
HETATM 8103 O  O   . HOH R 6 .   ? -8.766  -11.524 87.170  1.00 49.72  ? 660  HOH B O   1 
HETATM 8104 O  O   . HOH R 6 .   ? -21.892 -6.542  69.455  1.00 37.99  ? 661  HOH B O   1 
HETATM 8105 O  O   . HOH R 6 .   ? 6.889   -46.952 52.053  1.00 56.74  ? 662  HOH B O   1 
HETATM 8106 O  O   . HOH R 6 .   ? -9.709  -28.651 53.531  1.00 63.06  ? 663  HOH B O   1 
HETATM 8107 O  O   . HOH R 6 .   ? -13.326 8.048   47.302  1.00 45.82  ? 664  HOH B O   1 
HETATM 8108 O  O   . HOH R 6 .   ? -21.407 -19.489 62.745  1.00 38.86  ? 665  HOH B O   1 
HETATM 8109 O  O   . HOH R 6 .   ? 20.537  -14.246 70.447  1.00 34.92  ? 666  HOH B O   1 
HETATM 8110 O  O   . HOH R 6 .   ? -20.069 -9.371  83.439  1.00 55.80  ? 667  HOH B O   1 
HETATM 8111 O  O   . HOH R 6 .   ? -13.507 -22.085 74.848  1.00 41.07  ? 668  HOH B O   1 
HETATM 8112 O  O   . HOH R 6 .   ? -22.325 -1.200  54.601  1.00 45.56  ? 669  HOH B O   1 
HETATM 8113 O  O   . HOH R 6 .   ? -13.841 7.364   63.825  1.00 44.87  ? 670  HOH B O   1 
HETATM 8114 O  O   . HOH R 6 .   ? 19.499  -3.183  59.416  1.00 43.77  ? 671  HOH B O   1 
HETATM 8115 O  O   . HOH R 6 .   ? 0.257   -30.736 97.292  1.00 74.09  ? 672  HOH B O   1 
HETATM 8116 O  O   . HOH R 6 .   ? 8.556   -30.515 87.512  1.00 50.76  ? 673  HOH B O   1 
HETATM 8117 O  O   . HOH R 6 .   ? -7.093  -26.025 86.316  1.00 36.47  ? 674  HOH B O   1 
HETATM 8118 O  O   . HOH R 6 .   ? 13.639  -28.852 64.481  1.00 46.37  ? 675  HOH B O   1 
HETATM 8119 O  O   . HOH R 6 .   ? 7.452   -6.634  73.203  1.00 48.57  ? 676  HOH B O   1 
HETATM 8120 O  O   . HOH R 6 .   ? -15.344 -20.820 73.880  1.00 49.38  ? 677  HOH B O   1 
HETATM 8121 O  O   . HOH R 6 .   ? -11.837 -0.090  76.468  1.00 50.84  ? 678  HOH B O   1 
HETATM 8122 O  O   . HOH R 6 .   ? 11.076  -7.122  76.826  1.00 53.70  ? 679  HOH B O   1 
HETATM 8123 O  O   . HOH R 6 .   ? -1.618  -40.871 62.339  1.00 53.16  ? 680  HOH B O   1 
HETATM 8124 O  O   . HOH R 6 .   ? -8.328  1.255   67.180  1.00 41.94  ? 681  HOH B O   1 
HETATM 8125 O  O   . HOH R 6 .   ? 2.403   -14.606 61.876  1.00 31.45  ? 682  HOH B O   1 
HETATM 8126 O  O   . HOH R 6 .   ? -12.136 -22.576 52.286  1.00 37.79  ? 683  HOH B O   1 
HETATM 8127 O  O   . HOH R 6 .   ? 9.828   -3.285  48.067  1.00 40.12  ? 684  HOH B O   1 
HETATM 8128 O  O   . HOH R 6 .   ? -27.162 -0.066  64.545  1.00 49.51  ? 685  HOH B O   1 
HETATM 8129 O  O   . HOH R 6 .   ? -2.130  -27.457 49.943  1.00 42.06  ? 686  HOH B O   1 
HETATM 8130 O  O   . HOH R 6 .   ? -1.369  -24.509 43.347  1.00 52.62  ? 687  HOH B O   1 
HETATM 8131 O  O   . HOH R 6 .   ? -16.440 -18.954 76.772  1.00 48.22  ? 688  HOH B O   1 
HETATM 8132 O  O   . HOH R 6 .   ? 21.592  -20.909 64.974  1.00 39.07  ? 689  HOH B O   1 
HETATM 8133 O  O   . HOH R 6 .   ? 5.225   -37.190 66.500  1.00 51.80  ? 690  HOH B O   1 
HETATM 8134 O  O   . HOH R 6 .   ? -15.912 -19.404 70.771  1.00 38.45  ? 691  HOH B O   1 
HETATM 8135 O  O   . HOH R 6 .   ? 22.125  -8.437  57.042  1.00 38.47  ? 692  HOH B O   1 
HETATM 8136 O  O   . HOH R 6 .   ? -8.518  -28.493 60.327  1.00 36.45  ? 693  HOH B O   1 
HETATM 8137 O  O   . HOH R 6 .   ? -7.718  7.270   41.401  1.00 53.49  ? 694  HOH B O   1 
HETATM 8138 O  O   . HOH R 6 .   ? -10.315 11.581  56.458  1.00 44.26  ? 695  HOH B O   1 
HETATM 8139 O  O   . HOH R 6 .   ? 0.775   -9.551  54.443  1.00 30.30  ? 696  HOH B O   1 
HETATM 8140 O  O   . HOH R 6 .   ? -6.142  -4.665  39.048  1.00 37.82  ? 697  HOH B O   1 
HETATM 8141 O  O   . HOH R 6 .   ? 8.558   -31.475 83.644  1.00 52.60  ? 698  HOH B O   1 
HETATM 8142 O  O   . HOH R 6 .   ? -24.378 -1.590  47.783  1.00 44.28  ? 699  HOH B O   1 
HETATM 8143 O  O   . HOH R 6 .   ? -4.769  -6.716  35.070  1.00 32.78  ? 700  HOH B O   1 
HETATM 8144 O  O   . HOH R 6 .   ? -15.066 -14.494 43.558  1.00 44.51  ? 701  HOH B O   1 
HETATM 8145 O  O   . HOH R 6 .   ? 12.640  -13.133 88.741  1.00 54.32  ? 702  HOH B O   1 
HETATM 8146 O  O   . HOH R 6 .   ? 25.569  -15.327 62.928  1.00 46.95  ? 703  HOH B O   1 
HETATM 8147 O  O   . HOH R 6 .   ? 10.288  -9.141  68.886  1.00 38.25  ? 704  HOH B O   1 
HETATM 8148 O  O   . HOH R 6 .   ? -22.747 -17.788 43.807  1.00 46.79  ? 705  HOH B O   1 
HETATM 8149 O  O   . HOH R 6 .   ? -14.665 -24.251 67.839  1.00 46.59  ? 706  HOH B O   1 
HETATM 8150 O  O   . HOH R 6 .   ? -17.356 0.779   45.157  1.00 34.92  ? 707  HOH B O   1 
HETATM 8151 O  O   . HOH R 6 .   ? -22.572 -16.884 53.399  1.00 36.36  ? 708  HOH B O   1 
HETATM 8152 O  O   . HOH R 6 .   ? 31.201  -2.956  58.925  1.00 54.34  ? 709  HOH B O   1 
HETATM 8153 O  O   . HOH R 6 .   ? -2.504  -18.277 53.665  1.00 38.59  ? 710  HOH B O   1 
HETATM 8154 O  O   . HOH R 6 .   ? 6.259   -14.432 72.086  1.00 32.31  ? 711  HOH B O   1 
HETATM 8155 O  O   . HOH R 6 .   ? 17.040  -23.538 89.066  1.00 45.05  ? 712  HOH B O   1 
HETATM 8156 O  O   . HOH R 6 .   ? 11.489  -33.562 58.718  1.00 60.83  ? 713  HOH B O   1 
HETATM 8157 O  O   . HOH R 6 .   ? -19.626 -24.257 57.250  1.00 38.51  ? 714  HOH B O   1 
HETATM 8158 O  O   . HOH R 6 .   ? -19.198 2.389   53.879  1.00 40.09  ? 715  HOH B O   1 
HETATM 8159 O  O   . HOH R 6 .   ? 18.543  -18.276 84.515  1.00 52.03  ? 716  HOH B O   1 
HETATM 8160 O  O   . HOH R 6 .   ? -2.379  -41.357 65.334  1.00 49.65  ? 717  HOH B O   1 
HETATM 8161 O  O   . HOH R 6 .   ? 13.634  -7.843  44.316  1.00 48.57  ? 718  HOH B O   1 
HETATM 8162 O  O   . HOH R 6 .   ? 10.544  -12.967 75.692  1.00 33.36  ? 719  HOH B O   1 
HETATM 8163 O  O   . HOH R 6 .   ? 7.705   -43.005 57.856  1.00 46.19  ? 720  HOH B O   1 
HETATM 8164 O  O   . HOH R 6 .   ? -14.084 7.859   44.507  1.00 48.49  ? 721  HOH B O   1 
HETATM 8165 O  O   . HOH R 6 .   ? -20.015 -1.917  54.093  1.00 41.31  ? 722  HOH B O   1 
HETATM 8166 O  O   . HOH R 6 .   ? -1.819  -16.145 35.745  1.00 49.40  ? 723  HOH B O   1 
HETATM 8167 O  O   . HOH R 6 .   ? 2.748   -16.122 92.385  1.00 46.90  ? 724  HOH B O   1 
HETATM 8168 O  O   . HOH R 6 .   ? -5.868  -24.395 80.781  1.00 33.25  ? 725  HOH B O   1 
HETATM 8169 O  O   . HOH R 6 .   ? 15.805  -28.355 88.877  1.00 52.83  ? 726  HOH B O   1 
HETATM 8170 O  O   . HOH R 6 .   ? 0.745   -7.689  41.384  1.00 32.92  ? 727  HOH B O   1 
HETATM 8171 O  O   . HOH R 6 .   ? -9.461  -34.562 70.889  1.00 42.47  ? 728  HOH B O   1 
HETATM 8172 O  O   . HOH R 6 .   ? 9.546   -48.026 54.834  1.00 53.03  ? 729  HOH B O   1 
HETATM 8173 O  O   . HOH R 6 .   ? 0.495   -12.590 58.879  1.00 30.68  ? 730  HOH B O   1 
HETATM 8174 O  O   . HOH R 6 .   ? -7.390  -12.120 79.524  1.00 37.81  ? 731  HOH B O   1 
HETATM 8175 O  O   . HOH R 6 .   ? -16.224 -13.916 37.461  1.00 37.74  ? 732  HOH B O   1 
HETATM 8176 O  O   . HOH R 6 .   ? 20.772  -23.329 86.976  1.00 57.87  ? 733  HOH B O   1 
HETATM 8177 O  O   . HOH R 6 .   ? 11.661  -18.714 61.711  1.00 31.10  ? 734  HOH B O   1 
HETATM 8178 O  O   . HOH R 6 .   ? 9.849   -40.865 52.586  1.00 52.22  ? 735  HOH B O   1 
HETATM 8179 O  O   . HOH R 6 .   ? -2.115  -40.283 68.661  1.00 50.38  ? 736  HOH B O   1 
HETATM 8180 O  O   . HOH R 6 .   ? 11.335  -33.037 68.028  1.00 56.00  ? 737  HOH B O   1 
HETATM 8181 O  O   . HOH R 6 .   ? -11.517 -30.398 68.052  1.00 41.11  ? 738  HOH B O   1 
HETATM 8182 O  O   . HOH R 6 .   ? -7.153  -14.743 85.828  1.00 35.99  ? 739  HOH B O   1 
HETATM 8183 O  O   . HOH R 6 .   ? 7.478   -29.653 89.726  1.00 48.83  ? 740  HOH B O   1 
HETATM 8184 O  O   . HOH R 6 .   ? 2.236   -49.438 58.575  1.00 56.59  ? 741  HOH B O   1 
HETATM 8185 O  O   . HOH R 6 .   ? 23.616  -18.948 59.680  1.00 45.66  ? 742  HOH B O   1 
HETATM 8186 O  O   . HOH R 6 .   ? -18.848 4.150   51.370  1.00 40.82  ? 743  HOH B O   1 
HETATM 8187 O  O   . HOH R 6 .   ? -0.363  2.730   45.394  1.00 43.67  ? 744  HOH B O   1 
HETATM 8188 O  O   . HOH R 6 .   ? -7.768  -0.091  71.493  1.00 50.41  ? 745  HOH B O   1 
HETATM 8189 O  O   . HOH R 6 .   ? 6.467   -4.244  40.248  1.00 53.68  ? 746  HOH B O   1 
HETATM 8190 O  O   . HOH R 6 .   ? 13.878  2.103   58.738  1.00 57.89  ? 747  HOH B O   1 
HETATM 8191 O  O   . HOH R 6 .   ? 20.447  -4.958  48.227  1.00 52.66  ? 748  HOH B O   1 
HETATM 8192 O  O   . HOH R 6 .   ? 20.240  -12.655 39.623  1.00 59.64  ? 749  HOH B O   1 
HETATM 8193 O  O   . HOH R 6 .   ? 0.165   -34.413 56.029  1.00 45.50  ? 750  HOH B O   1 
HETATM 8194 O  O   . HOH R 6 .   ? -14.829 -6.729  78.042  1.00 36.26  ? 751  HOH B O   1 
HETATM 8195 O  O   . HOH R 6 .   ? -25.770 -9.152  47.984  1.00 49.62  ? 752  HOH B O   1 
HETATM 8196 O  O   . HOH R 6 .   ? -8.819  -13.358 64.116  1.00 34.63  ? 753  HOH B O   1 
HETATM 8197 O  O   . HOH R 6 .   ? 9.659   1.167   53.853  1.00 46.07  ? 754  HOH B O   1 
HETATM 8198 O  O   . HOH R 6 .   ? -4.405  -17.722 60.016  1.00 33.20  ? 755  HOH B O   1 
HETATM 8199 O  O   . HOH R 6 .   ? 13.317  -32.017 56.756  1.00 53.75  ? 756  HOH B O   1 
HETATM 8200 O  O   . HOH R 6 .   ? 3.138   -26.529 45.181  1.00 43.75  ? 757  HOH B O   1 
HETATM 8201 O  O   . HOH R 6 .   ? 13.479  -30.533 50.361  1.00 48.08  ? 758  HOH B O   1 
HETATM 8202 O  O   . HOH R 6 .   ? 4.085   4.717   50.590  1.00 41.29  ? 759  HOH B O   1 
HETATM 8203 O  O   . HOH R 6 .   ? 5.438   -1.605  41.935  1.00 54.86  ? 760  HOH B O   1 
HETATM 8204 O  O   . HOH R 6 .   ? -2.296  -14.962 67.664  1.00 31.91  ? 761  HOH B O   1 
HETATM 8205 O  O   . HOH R 6 .   ? 16.642  -22.802 53.245  1.00 51.83  ? 762  HOH B O   1 
HETATM 8206 O  O   . HOH R 6 .   ? 14.632  -19.419 73.692  1.00 33.04  ? 763  HOH B O   1 
HETATM 8207 O  O   . HOH R 6 .   ? -26.420 -22.449 57.073  1.00 52.19  ? 764  HOH B O   1 
HETATM 8208 O  O   . HOH R 6 .   ? 7.997   -29.829 80.696  1.00 39.14  ? 765  HOH B O   1 
HETATM 8209 O  O   . HOH R 6 .   ? 1.534   -9.364  43.448  1.00 33.62  ? 766  HOH B O   1 
HETATM 8210 O  O   . HOH R 6 .   ? -11.173 8.852   63.553  1.00 46.19  ? 767  HOH B O   1 
HETATM 8211 O  O   . HOH R 6 .   ? -3.779  10.067  61.107  1.00 43.47  ? 768  HOH B O   1 
HETATM 8212 O  O   . HOH R 6 .   ? 14.371  -4.819  43.139  1.00 57.41  ? 769  HOH B O   1 
HETATM 8213 O  O   . HOH R 6 .   ? 31.689  -10.166 65.500  1.00 49.77  ? 770  HOH B O   1 
HETATM 8214 O  O   . HOH R 6 .   ? 3.385   -9.636  45.493  1.00 33.42  ? 771  HOH B O   1 
HETATM 8215 O  O   . HOH R 6 .   ? -6.394  -41.984 63.411  1.00 56.77  ? 772  HOH B O   1 
HETATM 8216 O  O   . HOH R 6 .   ? -13.394 -25.456 71.230  1.00 42.71  ? 773  HOH B O   1 
HETATM 8217 O  O   . HOH R 6 .   ? -3.427  -1.518  42.070  1.00 36.48  ? 774  HOH B O   1 
HETATM 8218 O  O   . HOH R 6 .   ? 8.292   -14.951 79.400  1.00 33.87  ? 775  HOH B O   1 
HETATM 8219 O  O   . HOH R 6 .   ? 4.755   -22.437 70.036  1.00 30.71  ? 776  HOH B O   1 
HETATM 8220 O  O   . HOH R 6 .   ? -26.538 -14.040 58.568  1.00 46.89  ? 777  HOH B O   1 
HETATM 8221 O  O   . HOH R 6 .   ? -18.786 -5.563  76.920  1.00 53.53  ? 778  HOH B O   1 
HETATM 8222 O  O   . HOH R 6 .   ? 23.385  -9.625  68.310  1.00 34.82  ? 779  HOH B O   1 
HETATM 8223 O  O   . HOH R 6 .   ? -9.384  7.749   51.303  1.00 36.20  ? 780  HOH B O   1 
HETATM 8224 O  O   . HOH R 6 .   ? -13.285 -15.123 45.483  1.00 33.56  ? 781  HOH B O   1 
HETATM 8225 O  O   . HOH R 6 .   ? 23.734  -16.915 73.848  1.00 48.99  ? 782  HOH B O   1 
HETATM 8226 O  O   . HOH R 6 .   ? 6.590   -20.648 71.303  1.00 30.97  ? 783  HOH B O   1 
HETATM 8227 O  O   . HOH R 6 .   ? 21.233  -2.317  61.338  1.00 50.55  ? 784  HOH B O   1 
HETATM 8228 O  O   . HOH R 6 .   ? -14.980 -18.252 79.410  1.00 48.56  ? 785  HOH B O   1 
HETATM 8229 O  O   . HOH R 6 .   ? -20.137 7.748   56.958  1.00 44.88  ? 786  HOH B O   1 
HETATM 8230 O  O   . HOH R 6 .   ? -4.809  -44.701 80.742  1.00 34.43  ? 787  HOH B O   1 
HETATM 8231 O  O   . HOH R 6 .   ? 16.397  -26.693 59.730  1.00 48.24  ? 788  HOH B O   1 
HETATM 8232 O  O   . HOH R 6 .   ? -21.867 -10.956 69.082  1.00 37.10  ? 789  HOH B O   1 
HETATM 8233 O  O   . HOH R 6 .   ? -8.383  -1.175  69.162  1.00 40.87  ? 790  HOH B O   1 
HETATM 8234 O  O   . HOH R 6 .   ? 6.079   -38.880 60.812  1.00 46.11  ? 791  HOH B O   1 
HETATM 8235 O  O   . HOH R 6 .   ? 18.073  -18.772 81.500  1.00 54.15  ? 792  HOH B O   1 
HETATM 8236 O  O   . HOH R 6 .   ? -21.947 -21.986 53.810  1.00 41.08  ? 793  HOH B O   1 
HETATM 8237 O  O   . HOH R 6 .   ? 8.366   -4.359  65.518  1.00 47.90  ? 794  HOH B O   1 
HETATM 8238 O  O   . HOH R 6 .   ? 12.902  -14.032 76.404  1.00 35.07  ? 795  HOH B O   1 
HETATM 8239 O  O   . HOH R 6 .   ? -9.679  -18.430 80.993  1.00 41.42  ? 796  HOH B O   1 
HETATM 8240 O  O   . HOH R 6 .   ? -19.888 -14.097 68.811  1.00 48.41  ? 797  HOH B O   1 
HETATM 8241 O  O   . HOH R 6 .   ? -16.183 12.722  55.356  1.00 49.71  ? 798  HOH B O   1 
HETATM 8242 O  O   . HOH R 6 .   ? -4.021  -33.655 63.245  1.00 46.90  ? 799  HOH B O   1 
HETATM 8243 O  O   . HOH R 6 .   ? -9.268  -21.762 55.327  1.00 38.43  ? 800  HOH B O   1 
HETATM 8244 O  O   . HOH R 6 .   ? 4.473   -18.101 93.258  1.00 52.20  ? 801  HOH B O   1 
HETATM 8245 O  O   . HOH R 6 .   ? -14.648 -25.192 63.819  1.00 34.41  ? 802  HOH B O   1 
HETATM 8246 O  O   . HOH R 6 .   ? -13.205 -10.587 39.071  1.00 35.26  ? 803  HOH B O   1 
HETATM 8247 O  O   . HOH R 6 .   ? -19.120 -8.431  43.849  1.00 45.20  ? 804  HOH B O   1 
HETATM 8248 O  O   . HOH R 6 .   ? -1.893  -15.583 91.946  1.00 50.79  ? 805  HOH B O   1 
HETATM 8249 O  O   . HOH R 6 .   ? -19.911 -18.798 71.168  1.00 57.12  ? 806  HOH B O   1 
HETATM 8250 O  O   . HOH R 6 .   ? -18.248 -17.321 37.073  1.00 53.31  ? 807  HOH B O   1 
HETATM 8251 O  O   . HOH R 6 .   ? 5.464   -4.230  63.282  1.00 46.61  ? 808  HOH B O   1 
HETATM 8252 O  O   . HOH R 6 .   ? -11.500 -16.334 41.786  1.00 41.50  ? 809  HOH B O   1 
HETATM 8253 O  O   . HOH R 6 .   ? 12.186  -19.218 86.593  1.00 40.66  ? 810  HOH B O   1 
HETATM 8254 O  O   . HOH R 6 .   ? 12.442  -1.997  55.308  1.00 46.60  ? 811  HOH B O   1 
HETATM 8255 O  O   . HOH R 6 .   ? 16.904  -15.291 63.601  1.00 31.65  ? 812  HOH B O   1 
HETATM 8256 O  O   . HOH R 6 .   ? -11.654 -31.625 73.645  1.00 36.85  ? 813  HOH B O   1 
HETATM 8257 O  O   . HOH R 6 .   ? 15.370  -20.745 91.492  1.00 50.89  ? 814  HOH B O   1 
HETATM 8258 O  O   . HOH R 6 .   ? 3.917   -31.389 53.246  1.00 39.44  ? 815  HOH B O   1 
HETATM 8259 O  O   . HOH R 6 .   ? 18.980  -17.381 43.929  1.00 53.72  ? 816  HOH B O   1 
HETATM 8260 O  O   . HOH R 6 .   ? 27.651  -0.808  68.463  1.00 54.43  ? 817  HOH B O   1 
HETATM 8261 O  O   . HOH R 6 .   ? -12.517 -9.732  88.347  1.00 48.97  ? 818  HOH B O   1 
HETATM 8262 O  O   . HOH R 6 .   ? 9.217   -30.718 71.895  1.00 52.02  ? 819  HOH B O   1 
HETATM 8263 O  O   . HOH R 6 .   ? -11.017 -29.282 59.437  1.00 44.94  ? 820  HOH B O   1 
HETATM 8264 O  O   . HOH R 6 .   ? -19.311 -6.453  37.368  1.00 42.01  ? 821  HOH B O   1 
HETATM 8265 O  O   . HOH R 6 .   ? -25.071 -3.659  58.875  1.00 38.57  ? 822  HOH B O   1 
HETATM 8266 O  O   . HOH R 6 .   ? 5.568   -38.585 72.154  1.00 47.20  ? 823  HOH B O   1 
HETATM 8267 O  O   . HOH R 6 .   ? 15.599  -29.188 86.149  1.00 45.00  ? 824  HOH B O   1 
HETATM 8268 O  O   . HOH R 6 .   ? 3.341   -34.118 53.655  1.00 36.95  ? 825  HOH B O   1 
HETATM 8269 O  O   . HOH R 6 .   ? 32.567  -12.989 63.220  1.00 47.36  ? 826  HOH B O   1 
HETATM 8270 O  O   . HOH R 6 .   ? 4.573   -34.970 69.348  1.00 42.13  ? 827  HOH B O   1 
HETATM 8271 O  O   . HOH R 6 .   ? -7.561  3.797   44.026  1.00 44.55  ? 828  HOH B O   1 
HETATM 8272 O  O   . HOH R 6 .   ? 1.524   -46.140 64.013  1.00 58.76  ? 829  HOH B O   1 
HETATM 8273 O  O   . HOH R 6 .   ? -22.092 -23.072 56.376  1.00 40.94  ? 830  HOH B O   1 
HETATM 8274 O  O   . HOH R 6 .   ? 22.017  -6.346  70.962  1.00 42.73  ? 831  HOH B O   1 
HETATM 8275 O  O   . HOH R 6 .   ? 4.592   -14.289 40.053  1.00 43.56  ? 832  HOH B O   1 
HETATM 8276 O  O   . HOH R 6 .   ? -10.584 -29.056 87.231  1.00 47.86  ? 833  HOH B O   1 
HETATM 8277 O  O   . HOH R 6 .   ? -2.124  -10.048 42.117  1.00 30.72  ? 834  HOH B O   1 
HETATM 8278 O  O   . HOH R 6 .   ? 11.255  -7.575  38.906  1.00 53.14  ? 835  HOH B O   1 
HETATM 8279 O  O   . HOH R 6 .   ? 24.052  -10.006 54.198  1.00 44.52  ? 836  HOH B O   1 
HETATM 8280 O  O   . HOH R 6 .   ? 12.600  -29.714 83.387  1.00 46.75  ? 837  HOH B O   1 
HETATM 8281 O  O   . HOH R 6 .   ? -5.356  -7.896  39.653  1.00 32.67  ? 838  HOH B O   1 
HETATM 8282 O  O   . HOH R 6 .   ? 14.289  -24.127 54.089  1.00 42.40  ? 839  HOH B O   1 
HETATM 8283 O  O   . HOH R 6 .   ? -3.930  -33.618 60.940  1.00 50.61  ? 840  HOH B O   1 
HETATM 8284 O  O   . HOH R 6 .   ? -3.257  -4.889  68.991  1.00 42.07  ? 841  HOH B O   1 
HETATM 8285 O  O   . HOH R 6 .   ? -26.302 -11.492 60.305  1.00 48.64  ? 842  HOH B O   1 
HETATM 8286 O  O   . HOH R 6 .   ? 8.149   -28.751 73.321  1.00 49.43  ? 843  HOH B O   1 
HETATM 8287 O  O   . HOH R 6 .   ? -13.583 12.729  57.524  1.00 54.75  ? 844  HOH B O   1 
HETATM 8288 O  O   . HOH R 6 .   ? 8.894   -32.900 78.648  1.00 47.39  ? 845  HOH B O   1 
HETATM 8289 O  O   . HOH R 6 .   ? 8.333   -14.230 76.714  1.00 34.20  ? 846  HOH B O   1 
HETATM 8290 O  O   . HOH R 6 .   ? -10.928 3.874   48.098  1.00 38.88  ? 847  HOH B O   1 
HETATM 8291 O  O   . HOH R 6 .   ? 7.176   -17.910 73.247  1.00 28.82  ? 848  HOH B O   1 
HETATM 8292 O  O   . HOH R 6 .   ? -7.503  -34.580 86.471  1.00 46.97  ? 849  HOH B O   1 
HETATM 8293 O  O   . HOH R 6 .   ? 5.203   -16.032 41.561  1.00 44.72  ? 850  HOH B O   1 
HETATM 8294 O  O   . HOH R 6 .   ? 0.015   -32.476 54.578  1.00 48.50  ? 851  HOH B O   1 
HETATM 8295 O  O   . HOH R 6 .   ? -14.298 -20.035 51.218  1.00 35.95  ? 852  HOH B O   1 
HETATM 8296 O  O   . HOH R 6 .   ? -24.286 -8.956  76.906  1.00 59.91  ? 853  HOH B O   1 
HETATM 8297 O  O   . HOH R 6 .   ? 23.840  -12.187 68.605  1.00 35.20  ? 854  HOH B O   1 
HETATM 8298 O  O   . HOH R 6 .   ? -20.819 -3.573  72.920  1.00 42.02  ? 855  HOH B O   1 
HETATM 8299 O  O   . HOH R 6 .   ? 0.620   -9.696  72.281  1.00 35.00  ? 856  HOH B O   1 
HETATM 8300 O  O   . HOH R 6 .   ? 18.978  -21.780 54.512  1.00 43.69  ? 857  HOH B O   1 
HETATM 8301 O  O   . HOH R 6 .   ? -20.177 -10.919 45.296  1.00 43.44  ? 858  HOH B O   1 
HETATM 8302 O  O   . HOH R 6 .   ? -3.884  -17.400 43.810  1.00 39.68  ? 859  HOH B O   1 
HETATM 8303 O  O   . HOH R 6 .   ? -5.845  -22.666 58.997  1.00 34.02  ? 860  HOH B O   1 
HETATM 8304 O  O   . HOH R 6 .   ? -25.177 -20.708 60.507  1.00 48.44  ? 861  HOH B O   1 
HETATM 8305 O  O   . HOH R 6 .   ? 22.975  -18.683 65.553  1.00 36.86  ? 862  HOH B O   1 
HETATM 8306 O  O   . HOH R 6 .   ? -19.042 -17.178 42.293  1.00 42.54  ? 863  HOH B O   1 
HETATM 8307 O  O   . HOH R 6 .   ? 0.173   -37.792 85.299  1.00 58.96  ? 864  HOH B O   1 
HETATM 8308 O  O   . HOH R 6 .   ? -25.210 -10.663 66.822  1.00 50.20  ? 865  HOH B O   1 
HETATM 8309 O  O   . HOH R 6 .   ? -22.972 2.468   57.933  1.00 46.11  ? 866  HOH B O   1 
HETATM 8310 O  O   . HOH R 6 .   ? -26.620 -6.266  73.874  1.00 51.15  ? 867  HOH B O   1 
HETATM 8311 O  O   . HOH R 6 .   ? -20.145 -15.011 76.675  1.00 43.32  ? 868  HOH B O   1 
HETATM 8312 O  O   . HOH R 6 .   ? 5.232   -38.166 79.856  1.00 48.39  ? 869  HOH B O   1 
HETATM 8313 O  O   . HOH R 6 .   ? -10.882 -18.857 42.421  1.00 53.33  ? 870  HOH B O   1 
HETATM 8314 O  O   . HOH R 6 .   ? 6.277   -8.894  78.908  1.00 51.61  ? 871  HOH B O   1 
HETATM 8315 O  O   . HOH R 6 .   ? -10.529 -35.401 79.111  1.00 38.70  ? 872  HOH B O   1 
HETATM 8316 O  O   . HOH R 6 .   ? -13.037 2.946   39.487  1.00 49.32  ? 873  HOH B O   1 
HETATM 8317 O  O   . HOH R 6 .   ? 23.472  -1.435  58.864  1.00 48.18  ? 874  HOH B O   1 
HETATM 8318 O  O   . HOH R 6 .   ? 9.009   -9.461  81.824  1.00 49.32  ? 875  HOH B O   1 
HETATM 8319 O  O   . HOH R 6 .   ? 22.895  -10.398 72.502  1.00 53.08  ? 876  HOH B O   1 
HETATM 8320 O  O   . HOH R 6 .   ? -24.666 0.358   65.156  1.00 45.76  ? 877  HOH B O   1 
HETATM 8321 O  O   . HOH R 6 .   ? 25.649  -18.895 54.805  1.00 45.55  ? 878  HOH B O   1 
HETATM 8322 O  O   . HOH R 6 .   ? -4.461  -20.242 53.511  1.00 43.32  ? 879  HOH B O   1 
HETATM 8323 O  O   . HOH R 6 .   ? 3.954   -20.217 68.594  1.00 32.51  ? 880  HOH B O   1 
HETATM 8324 O  O   . HOH R 6 .   ? -22.448 -19.500 47.177  1.00 47.37  ? 881  HOH B O   1 
HETATM 8325 O  O   . HOH R 6 .   ? -1.515  -42.690 80.940  1.00 43.01  ? 882  HOH B O   1 
HETATM 8326 O  O   . HOH R 6 .   ? -5.203  -36.220 63.153  1.00 49.99  ? 883  HOH B O   1 
HETATM 8327 O  O   . HOH R 6 .   ? 10.066  -25.142 92.166  1.00 49.48  ? 884  HOH B O   1 
HETATM 8328 O  O   . HOH R 6 .   ? -8.271  13.083  54.829  1.00 45.06  ? 885  HOH B O   1 
HETATM 8329 O  O   . HOH R 6 .   ? 7.974   -44.637 64.877  1.00 52.52  ? 886  HOH B O   1 
HETATM 8330 O  O   . HOH R 6 .   ? 15.968  -7.571  73.379  1.00 50.49  ? 887  HOH B O   1 
HETATM 8331 O  O   . HOH R 6 .   ? 27.130  -16.044 53.666  1.00 49.68  ? 888  HOH B O   1 
HETATM 8332 O  O   . HOH R 6 .   ? -9.358  -22.835 87.101  1.00 40.04  ? 889  HOH B O   1 
HETATM 8333 O  O   . HOH R 6 .   ? -24.466 -2.645  43.100  1.00 55.39  ? 890  HOH B O   1 
HETATM 8334 O  O   . HOH R 6 .   ? -3.643  -25.699 64.800  1.00 33.47  ? 891  HOH B O   1 
HETATM 8335 O  O   . HOH R 6 .   ? -0.353  -0.443  62.574  1.00 41.89  ? 892  HOH B O   1 
HETATM 8336 O  O   . HOH R 6 .   ? -25.323 -6.771  65.475  1.00 42.64  ? 893  HOH B O   1 
HETATM 8337 O  O   . HOH R 6 .   ? 19.975  -24.473 54.957  1.00 61.59  ? 894  HOH B O   1 
HETATM 8338 O  O   . HOH R 6 .   ? -25.098 -9.494  57.309  1.00 50.69  ? 895  HOH B O   1 
HETATM 8339 O  O   . HOH R 6 .   ? 23.986  -14.794 60.127  1.00 39.69  ? 896  HOH B O   1 
HETATM 8340 O  O   . HOH R 6 .   ? 1.793   -43.235 64.781  1.00 50.02  ? 897  HOH B O   1 
HETATM 8341 O  O   . HOH R 6 .   ? -19.205 -17.748 66.152  1.00 54.43  ? 898  HOH B O   1 
HETATM 8342 O  O   . HOH R 6 .   ? -6.823  -22.305 56.405  1.00 35.98  ? 899  HOH B O   1 
HETATM 8343 O  O   . HOH R 6 .   ? 0.310   8.222   52.549  1.00 42.47  ? 900  HOH B O   1 
HETATM 8344 O  O   . HOH R 6 .   ? -2.596  -4.574  51.226  1.00 34.15  ? 901  HOH B O   1 
HETATM 8345 O  O   . HOH R 6 .   ? -7.594  14.719  51.112  1.00 60.91  ? 902  HOH B O   1 
HETATM 8346 O  O   . HOH R 6 .   ? 8.833   -18.868 93.021  1.00 49.38  ? 903  HOH B O   1 
HETATM 8347 O  O   . HOH R 6 .   ? -5.708  -18.367 47.785  1.00 41.76  ? 904  HOH B O   1 
HETATM 8348 O  O   . HOH R 6 .   ? -10.390 6.415   73.606  1.00 53.41  ? 905  HOH B O   1 
HETATM 8349 O  O   . HOH R 6 .   ? -0.619  10.233  54.826  1.00 42.17  ? 906  HOH B O   1 
HETATM 8350 O  O   . HOH R 6 .   ? -8.021  -14.143 41.298  1.00 36.89  ? 907  HOH B O   1 
HETATM 8351 O  O   . HOH R 6 .   ? -17.537 -11.633 85.269  1.00 53.26  ? 908  HOH B O   1 
HETATM 8352 O  O   . HOH R 6 .   ? -10.794 -17.452 84.837  1.00 50.86  ? 909  HOH B O   1 
HETATM 8353 O  O   . HOH R 6 .   ? -13.321 -17.549 82.660  1.00 40.67  ? 910  HOH B O   1 
HETATM 8354 O  O   . HOH R 6 .   ? 4.657   -8.108  75.471  1.00 43.84  ? 911  HOH B O   1 
HETATM 8355 O  O   . HOH R 6 .   ? -1.240  -48.908 76.987  1.00 47.75  ? 912  HOH B O   1 
HETATM 8356 O  O   . HOH R 6 .   ? -13.945 12.322  60.390  1.00 46.10  ? 913  HOH B O   1 
HETATM 8357 O  O   . HOH R 6 .   ? 25.122  -1.312  62.676  1.00 49.16  ? 914  HOH B O   1 
HETATM 8358 O  O   . HOH R 6 .   ? -2.896  -22.357 56.110  1.00 36.17  ? 915  HOH B O   1 
HETATM 8359 O  O   . HOH R 6 .   ? 24.683  -1.295  55.949  1.00 57.62  ? 916  HOH B O   1 
HETATM 8360 O  O   . HOH R 6 .   ? -6.673  9.590   45.853  1.00 47.27  ? 917  HOH B O   1 
HETATM 8361 O  O   . HOH R 6 .   ? 17.582  -12.302 77.012  1.00 54.75  ? 918  HOH B O   1 
HETATM 8362 O  O   . HOH R 6 .   ? -6.462  -38.401 83.470  1.00 46.80  ? 919  HOH B O   1 
HETATM 8363 O  O   . HOH R 6 .   ? 6.101   -33.636 71.703  1.00 51.62  ? 920  HOH B O   1 
HETATM 8364 O  O   . HOH R 6 .   ? 3.580   -44.139 52.947  1.00 52.58  ? 921  HOH B O   1 
HETATM 8365 O  O   . HOH R 6 .   ? -11.484 -17.300 44.811  1.00 45.80  ? 922  HOH B O   1 
HETATM 8366 O  O   . HOH R 6 .   ? 16.414  -26.908 68.307  1.00 45.23  ? 923  HOH B O   1 
HETATM 8367 O  O   . HOH R 6 .   ? -10.043 -29.027 56.395  1.00 55.48  ? 924  HOH B O   1 
HETATM 8368 O  O   . HOH R 6 .   ? -10.945 -33.141 80.515  1.00 47.32  ? 925  HOH B O   1 
HETATM 8369 O  O   . HOH R 6 .   ? -0.671  -30.434 44.417  1.00 63.27  ? 926  HOH B O   1 
HETATM 8370 O  O   . HOH R 6 .   ? -10.140 -22.308 81.161  1.00 48.39  ? 927  HOH B O   1 
HETATM 8371 O  O   . HOH R 6 .   ? 20.503  -16.104 50.750  1.00 47.73  ? 928  HOH B O   1 
HETATM 8372 O  O   . HOH R 6 .   ? -4.603  -1.455  67.642  1.00 52.94  ? 929  HOH B O   1 
HETATM 8373 O  O   . HOH R 6 .   ? -14.777 -35.968 82.451  1.00 50.44  ? 930  HOH B O   1 
HETATM 8374 O  O   . HOH R 6 .   ? -19.583 1.582   74.503  1.00 53.13  ? 931  HOH B O   1 
HETATM 8375 O  O   . HOH R 6 .   ? -1.697  -16.074 47.586  1.00 41.42  ? 932  HOH B O   1 
HETATM 8376 O  O   . HOH R 6 .   ? -16.739 -17.515 67.712  1.00 44.15  ? 933  HOH B O   1 
HETATM 8377 O  O   . HOH R 6 .   ? -13.834 -35.128 79.079  1.00 55.81  ? 934  HOH B O   1 
HETATM 8378 O  O   . HOH R 6 .   ? -26.187 -10.705 55.568  1.00 43.92  ? 935  HOH B O   1 
HETATM 8379 O  O   . HOH R 6 .   ? 8.460   -1.363  50.427  1.00 47.26  ? 936  HOH B O   1 
HETATM 8380 O  O   . HOH R 6 .   ? -2.809  -6.938  77.456  1.00 44.31  ? 937  HOH B O   1 
HETATM 8381 O  O   . HOH R 6 .   ? -0.278  -42.394 66.198  1.00 45.27  ? 938  HOH B O   1 
HETATM 8382 O  O   . HOH R 6 .   ? -5.974  -2.641  65.512  1.00 46.47  ? 939  HOH B O   1 
HETATM 8383 O  O   . HOH R 6 .   ? 26.103  -8.546  53.591  1.00 47.93  ? 940  HOH B O   1 
HETATM 8384 O  O   . HOH R 6 .   ? 2.890   7.250   53.268  1.00 47.10  ? 941  HOH B O   1 
HETATM 8385 O  O   . HOH R 6 .   ? 6.954   -42.477 49.422  1.00 56.22  ? 942  HOH B O   1 
HETATM 8386 O  O   . HOH R 6 .   ? -20.839 -13.308 66.542  1.00 39.23  ? 943  HOH B O   1 
HETATM 8387 O  O   . HOH R 6 .   ? -11.545 -35.090 64.689  1.00 53.15  ? 944  HOH B O   1 
HETATM 8388 O  O   . HOH R 6 .   ? 21.632  -13.852 50.279  1.00 54.92  ? 945  HOH B O   1 
HETATM 8389 O  O   . HOH R 6 .   ? 8.700   3.980   64.941  1.00 58.83  ? 946  HOH B O   1 
HETATM 8390 O  O   . HOH R 6 .   ? 0.636   -30.689 89.414  1.00 52.41  ? 947  HOH B O   1 
HETATM 8391 O  O   . HOH R 6 .   ? 25.823  -20.158 57.967  1.00 60.21  ? 948  HOH B O   1 
HETATM 8392 O  O   . HOH R 6 .   ? -16.289 -27.316 64.688  1.00 58.82  ? 949  HOH B O   1 
HETATM 8393 O  O   . HOH R 6 .   ? -12.451 -36.176 73.178  1.00 44.56  ? 950  HOH B O   1 
HETATM 8394 O  O   . HOH R 6 .   ? 15.241  -26.550 54.786  1.00 49.23  ? 951  HOH B O   1 
HETATM 8395 O  O   . HOH R 6 .   ? -23.217 -4.407  54.487  1.00 45.93  ? 952  HOH B O   1 
HETATM 8396 O  O   . HOH R 6 .   ? -21.152 -15.486 65.356  1.00 50.44  ? 953  HOH B O   1 
HETATM 8397 O  O   . HOH R 6 .   ? -16.967 -24.077 64.946  1.00 53.98  ? 954  HOH B O   1 
HETATM 8398 O  O   . HOH R 6 .   ? -6.697  -19.505 52.240  1.00 40.53  ? 955  HOH B O   1 
HETATM 8399 O  O   . HOH R 6 .   ? 1.122   -35.283 53.038  1.00 50.60  ? 956  HOH B O   1 
HETATM 8400 O  O   . HOH R 6 .   ? 17.733  -21.599 81.545  1.00 57.39  ? 957  HOH B O   1 
HETATM 8401 O  O   . HOH R 6 .   ? 6.165   -9.098  82.354  1.00 53.54  ? 958  HOH B O   1 
HETATM 8402 O  O   . HOH R 6 .   ? 7.948   -5.516  41.533  1.00 53.91  ? 959  HOH B O   1 
HETATM 8403 O  O   . HOH R 6 .   ? -3.432  -17.833 46.344  1.00 43.32  ? 960  HOH B O   1 
HETATM 8404 O  O   . HOH R 6 .   ? 2.142   -29.087 91.132  1.00 50.44  ? 961  HOH B O   1 
HETATM 8405 O  O   . HOH R 6 .   ? -23.012 -8.834  70.877  1.00 46.73  ? 962  HOH B O   1 
HETATM 8406 O  O   . HOH R 6 .   ? -17.411 -25.082 55.956  1.00 52.10  ? 963  HOH B O   1 
HETATM 8407 O  O   . HOH R 6 .   ? 2.909   -8.086  73.879  1.00 58.00  ? 964  HOH B O   1 
HETATM 8408 O  O   . HOH R 6 .   ? -13.153 5.727   70.256  1.00 50.72  ? 965  HOH B O   1 
HETATM 8409 O  O   . HOH R 6 .   ? 20.854  -18.369 48.995  1.00 54.04  ? 966  HOH B O   1 
HETATM 8410 O  O   . HOH R 6 .   ? 30.473  -6.573  58.491  1.00 48.94  ? 967  HOH B O   1 
HETATM 8411 O  O   . HOH R 6 .   ? 9.903   0.344   51.573  1.00 51.87  ? 968  HOH B O   1 
HETATM 8412 O  O   . HOH R 6 .   ? -23.230 -10.615 44.136  1.00 52.90  ? 969  HOH B O   1 
HETATM 8413 O  O   . HOH R 6 .   ? -3.759  -8.631  87.186  1.00 58.68  ? 970  HOH B O   1 
HETATM 8414 O  O   . HOH R 6 .   ? -13.584 -35.775 76.747  1.00 44.03  ? 971  HOH B O   1 
HETATM 8415 O  O   . HOH R 6 .   ? -7.224  0.428   36.662  1.00 55.98  ? 972  HOH B O   1 
HETATM 8416 O  O   . HOH R 6 .   ? -23.919 -19.008 62.316  1.00 47.16  ? 973  HOH B O   1 
HETATM 8417 O  O   . HOH R 6 .   ? 2.772   -6.961  71.826  1.00 56.44  ? 974  HOH B O   1 
HETATM 8418 O  O   . HOH R 6 .   ? 9.817   -20.790 42.223  1.00 48.39  ? 975  HOH B O   1 
HETATM 8419 O  O   . HOH R 6 .   ? 6.307   4.879   49.023  1.00 54.42  ? 976  HOH B O   1 
HETATM 8420 O  O   . HOH R 6 .   ? -4.552  -39.261 84.729  1.00 56.70  ? 977  HOH B O   1 
HETATM 8421 O  O   . HOH R 6 .   ? 0.341   -15.061 37.497  1.00 48.20  ? 978  HOH B O   1 
HETATM 8422 O  O   . HOH R 6 .   ? 6.297   -5.469  70.937  1.00 54.97  ? 979  HOH B O   1 
HETATM 8423 O  O   . HOH R 6 .   ? -8.434  -21.078 52.594  1.00 45.06  ? 980  HOH B O   1 
HETATM 8424 O  O   . HOH R 6 .   ? -6.895  4.998   70.781  1.00 56.26  ? 981  HOH B O   1 
HETATM 8425 O  O   . HOH R 6 .   ? 24.535  -15.574 71.520  1.00 52.74  ? 982  HOH B O   1 
HETATM 8426 O  O   . HOH R 6 .   ? -0.448  -46.826 80.979  1.00 52.18  ? 983  HOH B O   1 
HETATM 8427 O  O   . HOH R 6 .   ? 5.863   -19.147 41.380  1.00 59.13  ? 984  HOH B O   1 
HETATM 8428 O  O   . HOH R 6 .   ? 5.220   -48.049 52.978  1.00 58.06  ? 985  HOH B O   1 
HETATM 8429 O  O   . HOH R 6 .   ? -21.491 -9.355  42.561  1.00 56.16  ? 986  HOH B O   1 
HETATM 8430 O  O   . HOH R 6 .   ? -21.707 3.397   55.258  1.00 51.49  ? 987  HOH B O   1 
HETATM 8431 O  O   . HOH R 6 .   ? 24.068  -11.152 51.513  1.00 56.53  ? 988  HOH B O   1 
HETATM 8432 O  O   . HOH R 6 .   ? 6.976   -12.897 90.486  1.00 57.66  ? 989  HOH B O   1 
HETATM 8433 O  O   . HOH R 6 .   ? 7.352   -15.397 74.511  1.00 34.36  ? 990  HOH B O   1 
HETATM 8434 O  O   . HOH R 6 .   ? -23.905 -13.265 66.595  1.00 57.10  ? 991  HOH B O   1 
HETATM 8435 O  O   . HOH R 6 .   ? -24.811 2.847   65.004  1.00 48.93  ? 992  HOH B O   1 
HETATM 8436 O  O   . HOH R 6 .   ? -8.977  -20.409 82.602  1.00 47.95  ? 993  HOH B O   1 
HETATM 8437 O  O   . HOH R 6 .   ? -8.843  14.791  58.125  1.00 55.67  ? 994  HOH B O   1 
HETATM 8438 O  O   . HOH R 6 .   ? 2.031   10.930  58.752  1.00 58.49  ? 995  HOH B O   1 
HETATM 8439 O  O   . HOH R 6 .   ? 4.609   -11.794 87.141  1.00 53.49  ? 996  HOH B O   1 
HETATM 8440 O  O   . HOH R 6 .   ? -25.341 0.753   46.781  1.00 56.27  ? 997  HOH B O   1 
HETATM 8441 O  O   . HOH R 6 .   ? -12.785 -32.464 76.125  1.00 47.75  ? 998  HOH B O   1 
HETATM 8442 O  O   . HOH R 6 .   ? -19.882 -26.413 58.822  1.00 54.34  ? 999  HOH B O   1 
HETATM 8443 O  O   . HOH R 6 .   ? -5.077  -23.302 54.853  1.00 40.22  ? 1000 HOH B O   1 
HETATM 8444 O  O   . HOH R 6 .   ? -4.312  -3.556  84.916  1.00 53.35  ? 1001 HOH B O   1 
HETATM 8445 O  O   . HOH R 6 .   ? -2.190  -2.733  68.404  1.00 53.07  ? 1002 HOH B O   1 
HETATM 8446 O  O   . HOH R 6 .   ? 3.630   -0.447  44.657  1.00 47.73  ? 1003 HOH B O   1 
HETATM 8447 O  O   . HOH R 6 .   ? -7.367  -25.194 88.848  1.00 51.71  ? 1004 HOH B O   1 
HETATM 8448 O  O   . HOH R 6 .   ? -19.685 9.670   54.876  1.00 52.98  ? 1005 HOH B O   1 
HETATM 8449 O  O   . HOH R 6 .   ? 12.994  -17.809 88.618  1.00 50.03  ? 1006 HOH B O   1 
HETATM 8450 O  O   . HOH R 6 .   ? -13.551 -24.669 51.048  1.00 52.23  ? 1007 HOH B O   1 
HETATM 8451 O  O   . HOH R 6 .   ? 0.950   -12.950 36.098  1.00 43.93  ? 1008 HOH B O   1 
HETATM 8452 O  O   . HOH R 6 .   ? 7.691   -4.720  68.104  1.00 60.22  ? 1009 HOH B O   1 
HETATM 8453 O  O   . HOH R 6 .   ? -1.676  12.499  54.022  1.00 49.64  ? 1010 HOH B O   1 
HETATM 8454 O  O   . HOH R 6 .   ? -17.859 6.731   50.525  1.00 51.84  ? 1011 HOH B O   1 
HETATM 8455 O  O   . HOH R 6 .   ? 26.387  -12.300 69.582  1.00 47.51  ? 1012 HOH B O   1 
HETATM 8456 O  O   . HOH R 6 .   ? 30.029  -9.349  69.750  1.00 63.76  ? 1013 HOH B O   1 
HETATM 8457 O  O   . HOH R 6 .   ? 2.222   6.606   50.045  1.00 53.12  ? 1014 HOH B O   1 
HETATM 8458 O  O   . HOH R 6 .   ? 14.219  -31.856 48.012  1.00 66.31  ? 1015 HOH B O   1 
HETATM 8459 O  O   . HOH R 6 .   ? -24.417 5.035   61.225  1.00 45.90  ? 1016 HOH B O   1 
HETATM 8460 O  O   . HOH R 6 .   ? 10.011  -6.860  69.754  1.00 50.63  ? 1017 HOH B O   1 
HETATM 8461 O  O   . HOH R 6 .   ? 15.527  -13.322 88.321  1.00 67.61  ? 1018 HOH B O   1 
HETATM 8462 O  O   . HOH R 6 .   ? -11.527 -33.479 69.547  1.00 43.75  ? 1019 HOH B O   1 
HETATM 8463 O  O   . HOH R 6 .   ? -2.473  -45.136 82.178  1.00 44.60  ? 1020 HOH B O   1 
HETATM 8464 O  O   . HOH R 6 .   ? 6.422   -50.670 79.744  1.00 54.82  ? 1021 HOH B O   1 
HETATM 8465 O  O   . HOH R 6 .   ? -8.388  -16.358 87.621  1.00 46.81  ? 1022 HOH B O   1 
HETATM 8466 O  O   . HOH R 6 .   ? 18.482  -25.739 89.074  1.00 58.72  ? 1023 HOH B O   1 
HETATM 8467 O  O   . HOH R 6 .   ? 6.134   2.340   46.988  1.00 54.09  ? 1024 HOH B O   1 
HETATM 8468 O  O   . HOH R 6 .   ? 8.045   -39.561 68.676  1.00 56.74  ? 1025 HOH B O   1 
HETATM 8469 O  O   . HOH R 6 .   ? -15.213 -21.802 49.597  1.00 45.06  ? 1026 HOH B O   1 
HETATM 8470 O  O   . HOH R 6 .   ? -13.107 9.300   42.627  1.00 57.13  ? 1027 HOH B O   1 
HETATM 8471 O  O   . HOH R 6 .   ? -17.223 -19.849 68.213  1.00 54.05  ? 1028 HOH B O   1 
HETATM 8472 O  O   . HOH R 6 .   ? -3.967  -25.053 49.178  1.00 51.51  ? 1029 HOH B O   1 
HETATM 8473 O  O   . HOH R 6 .   ? -23.026 3.968   63.335  1.00 42.42  ? 1030 HOH B O   1 
HETATM 8474 O  O   . HOH R 6 .   ? -3.009  8.375   64.879  1.00 60.38  ? 1031 HOH B O   1 
HETATM 8475 O  O   . HOH R 6 .   ? 1.766   10.729  56.336  1.00 54.40  ? 1032 HOH B O   1 
HETATM 8476 O  O   . HOH R 6 .   ? 20.321  -0.684  63.392  1.00 54.25  ? 1033 HOH B O   1 
HETATM 8477 O  O   . HOH R 6 .   ? 22.959  -13.056 71.002  1.00 40.63  ? 1034 HOH B O   1 
HETATM 8478 O  O   . HOH R 6 .   ? -14.802 -2.037  37.576  1.00 55.18  ? 1035 HOH B O   1 
HETATM 8479 O  O   . HOH R 6 .   ? -20.478 -20.906 72.237  1.00 61.73  ? 1036 HOH B O   1 
HETATM 8480 O  O   . HOH R 6 .   ? -9.258  -14.575 89.706  1.00 57.06  ? 1037 HOH B O   1 
HETATM 8481 O  O   . HOH R 6 .   ? 5.199   -18.777 95.668  1.00 59.94  ? 1038 HOH B O   1 
HETATM 8482 O  O   . HOH R 6 .   ? -5.668  -20.040 49.831  1.00 42.90  ? 1039 HOH B O   1 
HETATM 8483 O  O   . HOH R 6 .   ? -20.200 8.670   52.211  1.00 61.84  ? 1040 HOH B O   1 
HETATM 8484 O  O   . HOH R 6 .   ? -2.785  -49.249 79.084  1.00 48.19  ? 1041 HOH B O   1 
HETATM 8485 O  O   . HOH R 6 .   ? -21.225 4.985   51.129  1.00 56.44  ? 1042 HOH B O   1 
HETATM 8486 O  O   . HOH R 6 .   ? 17.412  -22.441 91.626  1.00 54.68  ? 1043 HOH B O   1 
HETATM 8487 O  O   . HOH R 6 .   ? 25.502  -18.981 64.694  1.00 52.96  ? 1044 HOH B O   1 
HETATM 8488 O  O   . HOH R 6 .   ? -11.104 -34.664 76.303  1.00 45.16  ? 1045 HOH B O   1 
HETATM 8489 O  O   . HOH R 6 .   ? -18.874 -0.895  75.901  1.00 53.95  ? 1046 HOH B O   1 
HETATM 8490 O  O   . HOH R 6 .   ? -13.506 0.385   40.199  1.00 47.79  ? 1047 HOH B O   1 
HETATM 8491 O  O   . HOH R 6 .   ? -14.070 -15.081 41.174  1.00 41.96  ? 1048 HOH B O   1 
HETATM 8492 O  O   . HOH R 6 .   ? -19.187 -3.388  75.050  1.00 48.81  ? 1049 HOH B O   1 
HETATM 8493 O  O   . HOH R 6 .   ? -15.492 -21.755 71.511  1.00 54.93  ? 1050 HOH B O   1 
HETATM 8494 O  O   . HOH R 6 .   ? -13.906 -23.422 69.955  1.00 50.73  ? 1051 HOH B O   1 
HETATM 8495 O  O   . HOH R 6 .   ? -5.119  3.379   42.856  1.00 50.70  ? 1052 HOH B O   1 
HETATM 8496 O  O   . HOH R 6 .   ? -7.271  -22.778 48.286  1.00 52.22  ? 1053 HOH B O   1 
HETATM 8497 O  O   . HOH R 6 .   ? 30.935  -10.918 68.302  1.00 60.82  ? 1054 HOH B O   1 
HETATM 8498 O  O   . HOH R 6 .   ? -9.490  -25.523 50.242  1.00 56.79  ? 1055 HOH B O   1 
HETATM 8499 O  O   . HOH R 6 .   ? -22.109 5.922   55.764  1.00 52.41  ? 1056 HOH B O   1 
HETATM 8500 O  O   . HOH R 6 .   ? -24.359 4.680   58.479  1.00 57.75  ? 1057 HOH B O   1 
HETATM 8501 O  O   . HOH R 6 .   ? -13.150 -31.886 71.440  1.00 46.74  ? 1058 HOH B O   1 
HETATM 8502 O  O   . HOH R 6 .   ? -18.923 12.034  56.004  1.00 56.70  ? 1059 HOH B O   1 
HETATM 8503 O  O   . HOH R 6 .   ? -25.661 -5.998  57.727  1.00 50.52  ? 1060 HOH B O   1 
HETATM 8504 O  O   . HOH R 6 .   ? -16.671 -22.276 66.962  1.00 55.06  ? 1061 HOH B O   1 
HETATM 8505 O  O   . HOH R 6 .   ? -4.499  5.767   41.305  1.00 62.41  ? 1062 HOH B O   1 
HETATM 8506 O  O   . HOH R 6 .   ? -2.052  6.283   65.797  1.00 64.45  ? 1063 HOH B O   1 
HETATM 8507 O  O   . HOH R 6 .   ? 4.681   -26.268 42.672  1.00 51.92  ? 1064 HOH B O   1 
HETATM 8508 O  O   . HOH R 6 .   ? -10.663 -34.155 73.464  1.00 43.57  ? 1065 HOH B O   1 
HETATM 8509 O  O   . HOH R 6 .   ? 3.449   9.219   54.755  1.00 53.91  ? 1066 HOH B O   1 
HETATM 8510 O  O   . HOH R 6 .   ? 22.164  -12.428 47.616  1.00 54.41  ? 1067 HOH B O   1 
HETATM 8511 O  O   . HOH R 6 .   ? -5.257  -22.888 49.845  1.00 54.92  ? 1068 HOH B O   1 
HETATM 8512 O  O   . HOH R 6 .   ? 23.793  -10.640 47.445  1.00 64.15  ? 1069 HOH B O   1 
HETATM 8513 O  O   . HOH R 6 .   ? 2.539   -26.254 40.693  1.00 64.42  ? 1070 HOH B O   1 
HETATM 8514 O  O   . HOH R 6 .   ? -21.966 6.816   52.914  1.00 57.92  ? 1071 HOH B O   1 
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