data_8YB1
# 
_entry.id   8YB1 
# 
_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   8YB1         pdb_00008yb1 10.2210/pdb8yb1/pdb 
WWPDB D_1300044634 ?            ?                   
# 
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                        8YB1 
_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'                           52084.340 2   1.14.14.1,1.6.2.4 
F87A,F393H ? ? 
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    3   ?                 ? 
? ? 
6 water       nat water                                                                          18.015    783 ?                 ? 
? ? 
# 
_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
FAGDGLATSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPHGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRD
FAGDGLATSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
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  ALA 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 1458' 
_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  ALA 87  87  87  ALA ALA 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  ALA 87  87  87  ALA ALA 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 2 HEM 1   501  501 HEM HEM B . 
G 3 D0L 1   502  503 D0L 7PF B . 
H 4 SYN 1   503  601 SYN SYN B . 
I 5 GOL 1   504  602 GOL GOL B . 
J 5 GOL 1   505  603 GOL GOL B . 
K 5 GOL 1   506  604 GOL GOL B . 
L 6 HOH 1   601  773 HOH HOH A . 
L 6 HOH 2   602  487 HOH HOH A . 
L 6 HOH 3   603  396 HOH HOH A . 
L 6 HOH 4   604  758 HOH HOH A . 
L 6 HOH 5   605  211 HOH HOH A . 
L 6 HOH 6   606  692 HOH HOH A . 
L 6 HOH 7   607  356 HOH HOH A . 
L 6 HOH 8   608  378 HOH HOH A . 
L 6 HOH 9   609  517 HOH HOH A . 
L 6 HOH 10  610  525 HOH HOH A . 
L 6 HOH 11  611  504 HOH HOH A . 
L 6 HOH 12  612  288 HOH HOH A . 
L 6 HOH 13  613  774 HOH HOH A . 
L 6 HOH 14  614  777 HOH HOH A . 
L 6 HOH 15  615  548 HOH HOH A . 
L 6 HOH 16  616  261 HOH HOH A . 
L 6 HOH 17  617  8   HOH HOH A . 
L 6 HOH 18  618  509 HOH HOH A . 
L 6 HOH 19  619  666 HOH HOH A . 
L 6 HOH 20  620  502 HOH HOH A . 
L 6 HOH 21  621  731 HOH HOH A . 
L 6 HOH 22  622  246 HOH HOH A . 
L 6 HOH 23  623  37  HOH HOH A . 
L 6 HOH 24  624  296 HOH HOH A . 
L 6 HOH 25  625  719 HOH HOH A . 
L 6 HOH 26  626  168 HOH HOH A . 
L 6 HOH 27  627  223 HOH HOH A . 
L 6 HOH 28  628  674 HOH HOH A . 
L 6 HOH 29  629  520 HOH HOH A . 
L 6 HOH 30  630  241 HOH HOH A . 
L 6 HOH 31  631  442 HOH HOH A . 
L 6 HOH 32  632  177 HOH HOH A . 
L 6 HOH 33  633  52  HOH HOH A . 
L 6 HOH 34  634  640 HOH HOH A . 
L 6 HOH 35  635  160 HOH HOH A . 
L 6 HOH 36  636  123 HOH HOH A . 
L 6 HOH 37  637  155 HOH HOH A . 
L 6 HOH 38  638  668 HOH HOH A . 
L 6 HOH 39  639  765 HOH HOH A . 
L 6 HOH 40  640  409 HOH HOH A . 
L 6 HOH 41  641  51  HOH HOH A . 
L 6 HOH 42  642  341 HOH HOH A . 
L 6 HOH 43  643  201 HOH HOH A . 
L 6 HOH 44  644  653 HOH HOH A . 
L 6 HOH 45  645  538 HOH HOH A . 
L 6 HOH 46  646  62  HOH HOH A . 
L 6 HOH 47  647  161 HOH HOH A . 
L 6 HOH 48  648  76  HOH HOH A . 
L 6 HOH 49  649  611 HOH HOH A . 
L 6 HOH 50  650  390 HOH HOH A . 
L 6 HOH 51  651  65  HOH HOH A . 
L 6 HOH 52  652  18  HOH HOH A . 
L 6 HOH 53  653  660 HOH HOH A . 
L 6 HOH 54  654  75  HOH HOH A . 
L 6 HOH 55  655  475 HOH HOH A . 
L 6 HOH 56  656  95  HOH HOH A . 
L 6 HOH 57  657  19  HOH HOH A . 
L 6 HOH 58  658  360 HOH HOH A . 
L 6 HOH 59  659  374 HOH HOH A . 
L 6 HOH 60  660  1   HOH HOH A . 
L 6 HOH 61  661  139 HOH HOH A . 
L 6 HOH 62  662  209 HOH HOH A . 
L 6 HOH 63  663  543 HOH HOH A . 
L 6 HOH 64  664  291 HOH HOH A . 
L 6 HOH 65  665  82  HOH HOH A . 
L 6 HOH 66  666  508 HOH HOH A . 
L 6 HOH 67  667  376 HOH HOH A . 
L 6 HOH 68  668  94  HOH HOH A . 
L 6 HOH 69  669  34  HOH HOH A . 
L 6 HOH 70  670  71  HOH HOH A . 
L 6 HOH 71  671  511 HOH HOH A . 
L 6 HOH 72  672  476 HOH HOH A . 
L 6 HOH 73  673  523 HOH HOH A . 
L 6 HOH 74  674  292 HOH HOH A . 
L 6 HOH 75  675  193 HOH HOH A . 
L 6 HOH 76  676  339 HOH HOH A . 
L 6 HOH 77  677  580 HOH HOH A . 
L 6 HOH 78  678  713 HOH HOH A . 
L 6 HOH 79  679  570 HOH HOH A . 
L 6 HOH 80  680  83  HOH HOH A . 
L 6 HOH 81  681  686 HOH HOH A . 
L 6 HOH 82  682  449 HOH HOH A . 
L 6 HOH 83  683  657 HOH HOH A . 
L 6 HOH 84  684  528 HOH HOH A . 
L 6 HOH 85  685  315 HOH HOH A . 
L 6 HOH 86  686  154 HOH HOH A . 
L 6 HOH 87  687  696 HOH HOH A . 
L 6 HOH 88  688  532 HOH HOH A . 
L 6 HOH 89  689  752 HOH HOH A . 
L 6 HOH 90  690  103 HOH HOH A . 
L 6 HOH 91  691  250 HOH HOH A . 
L 6 HOH 92  692  620 HOH HOH A . 
L 6 HOH 93  693  432 HOH HOH A . 
L 6 HOH 94  694  274 HOH HOH A . 
L 6 HOH 95  695  179 HOH HOH A . 
L 6 HOH 96  696  277 HOH HOH A . 
L 6 HOH 97  697  272 HOH HOH A . 
L 6 HOH 98  698  22  HOH HOH A . 
L 6 HOH 99  699  546 HOH HOH A . 
L 6 HOH 100 700  48  HOH HOH A . 
L 6 HOH 101 701  38  HOH HOH A . 
L 6 HOH 102 702  115 HOH HOH A . 
L 6 HOH 103 703  630 HOH HOH A . 
L 6 HOH 104 704  654 HOH HOH A . 
L 6 HOH 105 705  750 HOH HOH A . 
L 6 HOH 106 706  80  HOH HOH A . 
L 6 HOH 107 707  238 HOH HOH A . 
L 6 HOH 108 708  188 HOH HOH A . 
L 6 HOH 109 709  326 HOH HOH A . 
L 6 HOH 110 710  98  HOH HOH A . 
L 6 HOH 111 711  273 HOH HOH A . 
L 6 HOH 112 712  92  HOH HOH A . 
L 6 HOH 113 713  658 HOH HOH A . 
L 6 HOH 114 714  333 HOH HOH A . 
L 6 HOH 115 715  15  HOH HOH A . 
L 6 HOH 116 716  761 HOH HOH A . 
L 6 HOH 117 717  382 HOH HOH A . 
L 6 HOH 118 718  63  HOH HOH A . 
L 6 HOH 119 719  610 HOH HOH A . 
L 6 HOH 120 720  126 HOH HOH A . 
L 6 HOH 121 721  96  HOH HOH A . 
L 6 HOH 122 722  309 HOH HOH A . 
L 6 HOH 123 723  6   HOH HOH A . 
L 6 HOH 124 724  470 HOH HOH A . 
L 6 HOH 125 725  498 HOH HOH A . 
L 6 HOH 126 726  664 HOH HOH A . 
L 6 HOH 127 727  50  HOH HOH A . 
L 6 HOH 128 728  633 HOH HOH A . 
L 6 HOH 129 729  345 HOH HOH A . 
L 6 HOH 130 730  757 HOH HOH A . 
L 6 HOH 131 731  202 HOH HOH A . 
L 6 HOH 132 732  99  HOH HOH A . 
L 6 HOH 133 733  12  HOH HOH A . 
L 6 HOH 134 734  67  HOH HOH A . 
L 6 HOH 135 735  200 HOH HOH A . 
L 6 HOH 136 736  234 HOH HOH A . 
L 6 HOH 137 737  85  HOH HOH A . 
L 6 HOH 138 738  225 HOH HOH A . 
L 6 HOH 139 739  699 HOH HOH A . 
L 6 HOH 140 740  16  HOH HOH A . 
L 6 HOH 141 741  120 HOH HOH A . 
L 6 HOH 142 742  199 HOH HOH A . 
L 6 HOH 143 743  499 HOH HOH A . 
L 6 HOH 144 744  102 HOH HOH A . 
L 6 HOH 145 745  55  HOH HOH A . 
L 6 HOH 146 746  204 HOH HOH A . 
L 6 HOH 147 747  670 HOH HOH A . 
L 6 HOH 148 748  190 HOH HOH A . 
L 6 HOH 149 749  181 HOH HOH A . 
L 6 HOH 150 750  165 HOH HOH A . 
L 6 HOH 151 751  659 HOH HOH A . 
L 6 HOH 152 752  167 HOH HOH A . 
L 6 HOH 153 753  496 HOH HOH A . 
L 6 HOH 154 754  457 HOH HOH A . 
L 6 HOH 155 755  9   HOH HOH A . 
L 6 HOH 156 756  285 HOH HOH A . 
L 6 HOH 157 757  321 HOH HOH A . 
L 6 HOH 158 758  293 HOH HOH A . 
L 6 HOH 159 759  93  HOH HOH A . 
L 6 HOH 160 760  466 HOH HOH A . 
L 6 HOH 161 761  746 HOH HOH A . 
L 6 HOH 162 762  212 HOH HOH A . 
L 6 HOH 163 763  638 HOH HOH A . 
L 6 HOH 164 764  227 HOH HOH A . 
L 6 HOH 165 765  313 HOH HOH A . 
L 6 HOH 166 766  352 HOH HOH A . 
L 6 HOH 167 767  744 HOH HOH A . 
L 6 HOH 168 768  576 HOH HOH A . 
L 6 HOH 169 769  17  HOH HOH A . 
L 6 HOH 170 770  678 HOH HOH A . 
L 6 HOH 171 771  141 HOH HOH A . 
L 6 HOH 172 772  279 HOH HOH A . 
L 6 HOH 173 773  661 HOH HOH A . 
L 6 HOH 174 774  363 HOH HOH A . 
L 6 HOH 175 775  183 HOH HOH A . 
L 6 HOH 176 776  203 HOH HOH A . 
L 6 HOH 177 777  655 HOH HOH A . 
L 6 HOH 178 778  503 HOH HOH A . 
L 6 HOH 179 779  198 HOH HOH A . 
L 6 HOH 180 780  258 HOH HOH A . 
L 6 HOH 181 781  140 HOH HOH A . 
L 6 HOH 182 782  389 HOH HOH A . 
L 6 HOH 183 783  656 HOH HOH A . 
L 6 HOH 184 784  545 HOH HOH A . 
L 6 HOH 185 785  522 HOH HOH A . 
L 6 HOH 186 786  207 HOH HOH A . 
L 6 HOH 187 787  681 HOH HOH A . 
L 6 HOH 188 788  506 HOH HOH A . 
L 6 HOH 189 789  255 HOH HOH A . 
L 6 HOH 190 790  195 HOH HOH A . 
L 6 HOH 191 791  459 HOH HOH A . 
L 6 HOH 192 792  569 HOH HOH A . 
L 6 HOH 193 793  763 HOH HOH A . 
L 6 HOH 194 794  53  HOH HOH A . 
L 6 HOH 195 795  399 HOH HOH A . 
L 6 HOH 196 796  27  HOH HOH A . 
L 6 HOH 197 797  105 HOH HOH A . 
L 6 HOH 198 798  26  HOH HOH A . 
L 6 HOH 199 799  524 HOH HOH A . 
L 6 HOH 200 800  215 HOH HOH A . 
L 6 HOH 201 801  153 HOH HOH A . 
L 6 HOH 202 802  584 HOH HOH A . 
L 6 HOH 203 803  68  HOH HOH A . 
L 6 HOH 204 804  247 HOH HOH A . 
L 6 HOH 205 805  747 HOH HOH A . 
L 6 HOH 206 806  749 HOH HOH A . 
L 6 HOH 207 807  304 HOH HOH A . 
L 6 HOH 208 808  281 HOH HOH A . 
L 6 HOH 209 809  560 HOH HOH A . 
L 6 HOH 210 810  484 HOH HOH A . 
L 6 HOH 211 811  300 HOH HOH A . 
L 6 HOH 212 812  310 HOH HOH A . 
L 6 HOH 213 813  600 HOH HOH A . 
L 6 HOH 214 814  673 HOH HOH A . 
L 6 HOH 215 815  471 HOH HOH A . 
L 6 HOH 216 816  163 HOH HOH A . 
L 6 HOH 217 817  45  HOH HOH A . 
L 6 HOH 218 818  59  HOH HOH A . 
L 6 HOH 219 819  47  HOH HOH A . 
L 6 HOH 220 820  232 HOH HOH A . 
L 6 HOH 221 821  391 HOH HOH A . 
L 6 HOH 222 822  695 HOH HOH A . 
L 6 HOH 223 823  468 HOH HOH A . 
L 6 HOH 224 824  283 HOH HOH A . 
L 6 HOH 225 825  469 HOH HOH A . 
L 6 HOH 226 826  507 HOH HOH A . 
L 6 HOH 227 827  317 HOH HOH A . 
L 6 HOH 228 828  118 HOH HOH A . 
L 6 HOH 229 829  706 HOH HOH A . 
L 6 HOH 230 830  74  HOH HOH A . 
L 6 HOH 231 831  687 HOH HOH A . 
L 6 HOH 232 832  336 HOH HOH A . 
L 6 HOH 233 833  735 HOH HOH A . 
L 6 HOH 234 834  755 HOH HOH A . 
L 6 HOH 235 835  531 HOH HOH A . 
L 6 HOH 236 836  20  HOH HOH A . 
L 6 HOH 237 837  783 HOH HOH A . 
L 6 HOH 238 838  490 HOH HOH A . 
L 6 HOH 239 839  704 HOH HOH A . 
L 6 HOH 240 840  460 HOH HOH A . 
L 6 HOH 241 841  607 HOH HOH A . 
L 6 HOH 242 842  547 HOH HOH A . 
L 6 HOH 243 843  107 HOH HOH A . 
L 6 HOH 244 844  137 HOH HOH A . 
L 6 HOH 245 845  766 HOH HOH A . 
L 6 HOH 246 846  728 HOH HOH A . 
L 6 HOH 247 847  555 HOH HOH A . 
L 6 HOH 248 848  756 HOH HOH A . 
L 6 HOH 249 849  388 HOH HOH A . 
L 6 HOH 250 850  147 HOH HOH A . 
L 6 HOH 251 851  741 HOH HOH A . 
L 6 HOH 252 852  301 HOH HOH A . 
L 6 HOH 253 853  644 HOH HOH A . 
L 6 HOH 254 854  582 HOH HOH A . 
L 6 HOH 255 855  458 HOH HOH A . 
L 6 HOH 256 856  541 HOH HOH A . 
L 6 HOH 257 857  565 HOH HOH A . 
L 6 HOH 258 858  421 HOH HOH A . 
L 6 HOH 259 859  474 HOH HOH A . 
L 6 HOH 260 860  242 HOH HOH A . 
L 6 HOH 261 861  748 HOH HOH A . 
L 6 HOH 262 862  554 HOH HOH A . 
L 6 HOH 263 863  414 HOH HOH A . 
L 6 HOH 264 864  707 HOH HOH A . 
L 6 HOH 265 865  627 HOH HOH A . 
L 6 HOH 266 866  705 HOH HOH A . 
L 6 HOH 267 867  456 HOH HOH A . 
L 6 HOH 268 868  635 HOH HOH A . 
L 6 HOH 269 869  108 HOH HOH A . 
L 6 HOH 270 870  632 HOH HOH A . 
L 6 HOH 271 871  488 HOH HOH A . 
L 6 HOH 272 872  662 HOH HOH A . 
L 6 HOH 273 873  730 HOH HOH A . 
L 6 HOH 274 874  205 HOH HOH A . 
L 6 HOH 275 875  542 HOH HOH A . 
L 6 HOH 276 876  377 HOH HOH A . 
L 6 HOH 277 877  100 HOH HOH A . 
L 6 HOH 278 878  220 HOH HOH A . 
L 6 HOH 279 879  709 HOH HOH A . 
L 6 HOH 280 880  586 HOH HOH A . 
L 6 HOH 281 881  702 HOH HOH A . 
L 6 HOH 282 882  753 HOH HOH A . 
L 6 HOH 283 883  688 HOH HOH A . 
L 6 HOH 284 884  252 HOH HOH A . 
L 6 HOH 285 885  415 HOH HOH A . 
L 6 HOH 286 886  683 HOH HOH A . 
L 6 HOH 287 887  585 HOH HOH A . 
L 6 HOH 288 888  501 HOH HOH A . 
L 6 HOH 289 889  495 HOH HOH A . 
L 6 HOH 290 890  769 HOH HOH A . 
L 6 HOH 291 891  481 HOH HOH A . 
L 6 HOH 292 892  297 HOH HOH A . 
L 6 HOH 293 893  516 HOH HOH A . 
L 6 HOH 294 894  448 HOH HOH A . 
L 6 HOH 295 895  400 HOH HOH A . 
L 6 HOH 296 896  13  HOH HOH A . 
L 6 HOH 297 897  386 HOH HOH A . 
L 6 HOH 298 898  482 HOH HOH A . 
L 6 HOH 299 899  617 HOH HOH A . 
L 6 HOH 300 900  467 HOH HOH A . 
L 6 HOH 301 901  299 HOH HOH A . 
L 6 HOH 302 902  771 HOH HOH A . 
L 6 HOH 303 903  510 HOH HOH A . 
L 6 HOH 304 904  513 HOH HOH A . 
L 6 HOH 305 905  612 HOH HOH A . 
L 6 HOH 306 906  631 HOH HOH A . 
L 6 HOH 307 907  652 HOH HOH A . 
L 6 HOH 308 908  477 HOH HOH A . 
L 6 HOH 309 909  782 HOH HOH A . 
L 6 HOH 310 910  493 HOH HOH A . 
L 6 HOH 311 911  169 HOH HOH A . 
L 6 HOH 312 912  465 HOH HOH A . 
L 6 HOH 313 913  700 HOH HOH A . 
L 6 HOH 314 914  596 HOH HOH A . 
L 6 HOH 315 915  740 HOH HOH A . 
L 6 HOH 316 916  651 HOH HOH A . 
L 6 HOH 317 917  625 HOH HOH A . 
L 6 HOH 318 918  597 HOH HOH A . 
L 6 HOH 319 919  671 HOH HOH A . 
L 6 HOH 320 920  438 HOH HOH A . 
L 6 HOH 321 921  636 HOH HOH A . 
L 6 HOH 322 922  714 HOH HOH A . 
L 6 HOH 323 923  492 HOH HOH A . 
L 6 HOH 324 924  485 HOH HOH A . 
L 6 HOH 325 925  723 HOH HOH A . 
L 6 HOH 326 926  214 HOH HOH A . 
L 6 HOH 327 927  641 HOH HOH A . 
L 6 HOH 328 928  727 HOH HOH A . 
L 6 HOH 329 929  500 HOH HOH A . 
L 6 HOH 330 930  649 HOH HOH A . 
L 6 HOH 331 931  691 HOH HOH A . 
L 6 HOH 332 932  276 HOH HOH A . 
L 6 HOH 333 933  619 HOH HOH A . 
L 6 HOH 334 934  539 HOH HOH A . 
L 6 HOH 335 935  578 HOH HOH A . 
L 6 HOH 336 936  305 HOH HOH A . 
L 6 HOH 337 937  634 HOH HOH A . 
L 6 HOH 338 938  308 HOH HOH A . 
L 6 HOH 339 939  431 HOH HOH A . 
L 6 HOH 340 940  768 HOH HOH A . 
L 6 HOH 341 941  682 HOH HOH A . 
L 6 HOH 342 942  133 HOH HOH A . 
L 6 HOH 343 943  564 HOH HOH A . 
L 6 HOH 344 944  394 HOH HOH A . 
L 6 HOH 345 945  303 HOH HOH A . 
L 6 HOH 346 946  642 HOH HOH A . 
L 6 HOH 347 947  416 HOH HOH A . 
L 6 HOH 348 948  406 HOH HOH A . 
L 6 HOH 349 949  236 HOH HOH A . 
L 6 HOH 350 950  426 HOH HOH A . 
L 6 HOH 351 951  650 HOH HOH A . 
L 6 HOH 352 952  689 HOH HOH A . 
L 6 HOH 353 953  228 HOH HOH A . 
L 6 HOH 354 954  533 HOH HOH A . 
L 6 HOH 355 955  711 HOH HOH A . 
L 6 HOH 356 956  344 HOH HOH A . 
M 6 HOH 1   601  776 HOH HOH B . 
M 6 HOH 2   602  598 HOH HOH B . 
M 6 HOH 3   603  703 HOH HOH B . 
M 6 HOH 4   604  185 HOH HOH B . 
M 6 HOH 5   605  772 HOH HOH B . 
M 6 HOH 6   606  759 HOH HOH B . 
M 6 HOH 7   607  573 HOH HOH B . 
M 6 HOH 8   608  589 HOH HOH B . 
M 6 HOH 9   609  592 HOH HOH B . 
M 6 HOH 10  610  672 HOH HOH B . 
M 6 HOH 11  611  319 HOH HOH B . 
M 6 HOH 12  612  445 HOH HOH B . 
M 6 HOH 13  613  779 HOH HOH B . 
M 6 HOH 14  614  497 HOH HOH B . 
M 6 HOH 15  615  556 HOH HOH B . 
M 6 HOH 16  616  624 HOH HOH B . 
M 6 HOH 17  617  365 HOH HOH B . 
M 6 HOH 18  618  327 HOH HOH B . 
M 6 HOH 19  619  384 HOH HOH B . 
M 6 HOH 20  620  328 HOH HOH B . 
M 6 HOH 21  621  561 HOH HOH B . 
M 6 HOH 22  622  608 HOH HOH B . 
M 6 HOH 23  623  253 HOH HOH B . 
M 6 HOH 24  624  537 HOH HOH B . 
M 6 HOH 25  625  694 HOH HOH B . 
M 6 HOH 26  626  156 HOH HOH B . 
M 6 HOH 27  627  483 HOH HOH B . 
M 6 HOH 28  628  605 HOH HOH B . 
M 6 HOH 29  629  618 HOH HOH B . 
M 6 HOH 30  630  174 HOH HOH B . 
M 6 HOH 31  631  122 HOH HOH B . 
M 6 HOH 32  632  31  HOH HOH B . 
M 6 HOH 33  633  216 HOH HOH B . 
M 6 HOH 34  634  521 HOH HOH B . 
M 6 HOH 35  635  446 HOH HOH B . 
M 6 HOH 36  636  751 HOH HOH B . 
M 6 HOH 37  637  81  HOH HOH B . 
M 6 HOH 38  638  371 HOH HOH B . 
M 6 HOH 39  639  110 HOH HOH B . 
M 6 HOH 40  640  451 HOH HOH B . 
M 6 HOH 41  641  629 HOH HOH B . 
M 6 HOH 42  642  254 HOH HOH B . 
M 6 HOH 43  643  444 HOH HOH B . 
M 6 HOH 44  644  263 HOH HOH B . 
M 6 HOH 45  645  455 HOH HOH B . 
M 6 HOH 46  646  366 HOH HOH B . 
M 6 HOH 47  647  536 HOH HOH B . 
M 6 HOH 48  648  453 HOH HOH B . 
M 6 HOH 49  649  280 HOH HOH B . 
M 6 HOH 50  650  86  HOH HOH B . 
M 6 HOH 51  651  412 HOH HOH B . 
M 6 HOH 52  652  269 HOH HOH B . 
M 6 HOH 53  653  24  HOH HOH B . 
M 6 HOH 54  654  732 HOH HOH B . 
M 6 HOH 55  655  626 HOH HOH B . 
M 6 HOH 56  656  425 HOH HOH B . 
M 6 HOH 57  657  337 HOH HOH B . 
M 6 HOH 58  658  28  HOH HOH B . 
M 6 HOH 59  659  57  HOH HOH B . 
M 6 HOH 60  660  175 HOH HOH B . 
M 6 HOH 61  661  302 HOH HOH B . 
M 6 HOH 62  662  90  HOH HOH B . 
M 6 HOH 63  663  325 HOH HOH B . 
M 6 HOH 64  664  113 HOH HOH B . 
M 6 HOH 65  665  176 HOH HOH B . 
M 6 HOH 66  666  270 HOH HOH B . 
M 6 HOH 67  667  260 HOH HOH B . 
M 6 HOH 68  668  151 HOH HOH B . 
M 6 HOH 69  669  134 HOH HOH B . 
M 6 HOH 70  670  375 HOH HOH B . 
M 6 HOH 71  671  408 HOH HOH B . 
M 6 HOH 72  672  439 HOH HOH B . 
M 6 HOH 73  673  130 HOH HOH B . 
M 6 HOH 74  674  230 HOH HOH B . 
M 6 HOH 75  675  84  HOH HOH B . 
M 6 HOH 76  676  287 HOH HOH B . 
M 6 HOH 77  677  229 HOH HOH B . 
M 6 HOH 78  678  132 HOH HOH B . 
M 6 HOH 79  679  49  HOH HOH B . 
M 6 HOH 80  680  243 HOH HOH B . 
M 6 HOH 81  681  284 HOH HOH B . 
M 6 HOH 82  682  648 HOH HOH B . 
M 6 HOH 83  683  217 HOH HOH B . 
M 6 HOH 84  684  362 HOH HOH B . 
M 6 HOH 85  685  387 HOH HOH B . 
M 6 HOH 86  686  124 HOH HOH B . 
M 6 HOH 87  687  69  HOH HOH B . 
M 6 HOH 88  688  129 HOH HOH B . 
M 6 HOH 89  689  443 HOH HOH B . 
M 6 HOH 90  690  21  HOH HOH B . 
M 6 HOH 91  691  318 HOH HOH B . 
M 6 HOH 92  692  33  HOH HOH B . 
M 6 HOH 93  693  267 HOH HOH B . 
M 6 HOH 94  694  571 HOH HOH B . 
M 6 HOH 95  695  101 HOH HOH B . 
M 6 HOH 96  696  39  HOH HOH B . 
M 6 HOH 97  697  5   HOH HOH B . 
M 6 HOH 98  698  259 HOH HOH B . 
M 6 HOH 99  699  114 HOH HOH B . 
M 6 HOH 100 700  294 HOH HOH B . 
M 6 HOH 101 701  572 HOH HOH B . 
M 6 HOH 102 702  725 HOH HOH B . 
M 6 HOH 103 703  117 HOH HOH B . 
M 6 HOH 104 704  61  HOH HOH B . 
M 6 HOH 105 705  148 HOH HOH B . 
M 6 HOH 106 706  423 HOH HOH B . 
M 6 HOH 107 707  329 HOH HOH B . 
M 6 HOH 108 708  72  HOH HOH B . 
M 6 HOH 109 709  7   HOH HOH B . 
M 6 HOH 110 710  245 HOH HOH B . 
M 6 HOH 111 711  322 HOH HOH B . 
M 6 HOH 112 712  66  HOH HOH B . 
M 6 HOH 113 713  184 HOH HOH B . 
M 6 HOH 114 714  70  HOH HOH B . 
M 6 HOH 115 715  320 HOH HOH B . 
M 6 HOH 116 716  403 HOH HOH B . 
M 6 HOH 117 717  251 HOH HOH B . 
M 6 HOH 118 718  157 HOH HOH B . 
M 6 HOH 119 719  127 HOH HOH B . 
M 6 HOH 120 720  550 HOH HOH B . 
M 6 HOH 121 721  616 HOH HOH B . 
M 6 HOH 122 722  128 HOH HOH B . 
M 6 HOH 123 723  116 HOH HOH B . 
M 6 HOH 124 724  486 HOH HOH B . 
M 6 HOH 125 725  192 HOH HOH B . 
M 6 HOH 126 726  350 HOH HOH B . 
M 6 HOH 127 727  3   HOH HOH B . 
M 6 HOH 128 728  736 HOH HOH B . 
M 6 HOH 129 729  77  HOH HOH B . 
M 6 HOH 130 730  312 HOH HOH B . 
M 6 HOH 131 731  354 HOH HOH B . 
M 6 HOH 132 732  109 HOH HOH B . 
M 6 HOH 133 733  266 HOH HOH B . 
M 6 HOH 134 734  330 HOH HOH B . 
M 6 HOH 135 735  23  HOH HOH B . 
M 6 HOH 136 736  159 HOH HOH B . 
M 6 HOH 137 737  637 HOH HOH B . 
M 6 HOH 138 738  131 HOH HOH B . 
M 6 HOH 139 739  182 HOH HOH B . 
M 6 HOH 140 740  136 HOH HOH B . 
M 6 HOH 141 741  54  HOH HOH B . 
M 6 HOH 142 742  461 HOH HOH B . 
M 6 HOH 143 743  42  HOH HOH B . 
M 6 HOH 144 744  395 HOH HOH B . 
M 6 HOH 145 745  385 HOH HOH B . 
M 6 HOH 146 746  427 HOH HOH B . 
M 6 HOH 147 747  278 HOH HOH B . 
M 6 HOH 148 748  79  HOH HOH B . 
M 6 HOH 149 749  290 HOH HOH B . 
M 6 HOH 150 750  91  HOH HOH B . 
M 6 HOH 151 751  25  HOH HOH B . 
M 6 HOH 152 752  112 HOH HOH B . 
M 6 HOH 153 753  239 HOH HOH B . 
M 6 HOH 154 754  677 HOH HOH B . 
M 6 HOH 155 755  745 HOH HOH B . 
M 6 HOH 156 756  58  HOH HOH B . 
M 6 HOH 157 757  56  HOH HOH B . 
M 6 HOH 158 758  311 HOH HOH B . 
M 6 HOH 159 759  602 HOH HOH B . 
M 6 HOH 160 760  718 HOH HOH B . 
M 6 HOH 161 761  359 HOH HOH B . 
M 6 HOH 162 762  256 HOH HOH B . 
M 6 HOH 163 763  4   HOH HOH B . 
M 6 HOH 164 764  224 HOH HOH B . 
M 6 HOH 165 765  685 HOH HOH B . 
M 6 HOH 166 766  577 HOH HOH B . 
M 6 HOH 167 767  10  HOH HOH B . 
M 6 HOH 168 768  164 HOH HOH B . 
M 6 HOH 169 769  14  HOH HOH B . 
M 6 HOH 170 770  210 HOH HOH B . 
M 6 HOH 171 771  383 HOH HOH B . 
M 6 HOH 172 772  342 HOH HOH B . 
M 6 HOH 173 773  40  HOH HOH B . 
M 6 HOH 174 774  268 HOH HOH B . 
M 6 HOH 175 775  237 HOH HOH B . 
M 6 HOH 176 776  621 HOH HOH B . 
M 6 HOH 177 777  733 HOH HOH B . 
M 6 HOH 178 778  11  HOH HOH B . 
M 6 HOH 179 779  149 HOH HOH B . 
M 6 HOH 180 780  479 HOH HOH B . 
M 6 HOH 181 781  73  HOH HOH B . 
M 6 HOH 182 782  235 HOH HOH B . 
M 6 HOH 183 783  158 HOH HOH B . 
M 6 HOH 184 784  338 HOH HOH B . 
M 6 HOH 185 785  381 HOH HOH B . 
M 6 HOH 186 786  358 HOH HOH B . 
M 6 HOH 187 787  464 HOH HOH B . 
M 6 HOH 188 788  491 HOH HOH B . 
M 6 HOH 189 789  298 HOH HOH B . 
M 6 HOH 190 790  265 HOH HOH B . 
M 6 HOH 191 791  314 HOH HOH B . 
M 6 HOH 192 792  143 HOH HOH B . 
M 6 HOH 193 793  144 HOH HOH B . 
M 6 HOH 194 794  171 HOH HOH B . 
M 6 HOH 195 795  593 HOH HOH B . 
M 6 HOH 196 796  189 HOH HOH B . 
M 6 HOH 197 797  36  HOH HOH B . 
M 6 HOH 198 798  505 HOH HOH B . 
M 6 HOH 199 799  180 HOH HOH B . 
M 6 HOH 200 800  574 HOH HOH B . 
M 6 HOH 201 801  353 HOH HOH B . 
M 6 HOH 202 802  87  HOH HOH B . 
M 6 HOH 203 803  97  HOH HOH B . 
M 6 HOH 204 804  173 HOH HOH B . 
M 6 HOH 205 805  307 HOH HOH B . 
M 6 HOH 206 806  197 HOH HOH B . 
M 6 HOH 207 807  590 HOH HOH B . 
M 6 HOH 208 808  262 HOH HOH B . 
M 6 HOH 209 809  340 HOH HOH B . 
M 6 HOH 210 810  398 HOH HOH B . 
M 6 HOH 211 811  187 HOH HOH B . 
M 6 HOH 212 812  60  HOH HOH B . 
M 6 HOH 213 813  78  HOH HOH B . 
M 6 HOH 214 814  41  HOH HOH B . 
M 6 HOH 215 815  257 HOH HOH B . 
M 6 HOH 216 816  32  HOH HOH B . 
M 6 HOH 217 817  29  HOH HOH B . 
M 6 HOH 218 818  44  HOH HOH B . 
M 6 HOH 219 819  30  HOH HOH B . 
M 6 HOH 220 820  780 HOH HOH B . 
M 6 HOH 221 821  742 HOH HOH B . 
M 6 HOH 222 822  343 HOH HOH B . 
M 6 HOH 223 823  332 HOH HOH B . 
M 6 HOH 224 824  553 HOH HOH B . 
M 6 HOH 225 825  2   HOH HOH B . 
M 6 HOH 226 826  186 HOH HOH B . 
M 6 HOH 227 827  166 HOH HOH B . 
M 6 HOH 228 828  737 HOH HOH B . 
M 6 HOH 229 829  708 HOH HOH B . 
M 6 HOH 230 830  249 HOH HOH B . 
M 6 HOH 231 831  473 HOH HOH B . 
M 6 HOH 232 832  669 HOH HOH B . 
M 6 HOH 233 833  435 HOH HOH B . 
M 6 HOH 234 834  335 HOH HOH B . 
M 6 HOH 235 835  717 HOH HOH B . 
M 6 HOH 236 836  43  HOH HOH B . 
M 6 HOH 237 837  530 HOH HOH B . 
M 6 HOH 238 838  433 HOH HOH B . 
M 6 HOH 239 839  162 HOH HOH B . 
M 6 HOH 240 840  710 HOH HOH B . 
M 6 HOH 241 841  646 HOH HOH B . 
M 6 HOH 242 842  422 HOH HOH B . 
M 6 HOH 243 843  286 HOH HOH B . 
M 6 HOH 244 844  231 HOH HOH B . 
M 6 HOH 245 845  420 HOH HOH B . 
M 6 HOH 246 846  111 HOH HOH B . 
M 6 HOH 247 847  370 HOH HOH B . 
M 6 HOH 248 848  450 HOH HOH B . 
M 6 HOH 249 849  558 HOH HOH B . 
M 6 HOH 250 850  401 HOH HOH B . 
M 6 HOH 251 851  684 HOH HOH B . 
M 6 HOH 252 852  46  HOH HOH B . 
M 6 HOH 253 853  402 HOH HOH B . 
M 6 HOH 254 854  264 HOH HOH B . 
M 6 HOH 255 855  441 HOH HOH B . 
M 6 HOH 256 856  437 HOH HOH B . 
M 6 HOH 257 857  665 HOH HOH B . 
M 6 HOH 258 858  218 HOH HOH B . 
M 6 HOH 259 859  106 HOH HOH B . 
M 6 HOH 260 860  739 HOH HOH B . 
M 6 HOH 261 861  221 HOH HOH B . 
M 6 HOH 262 862  178 HOH HOH B . 
M 6 HOH 263 863  566 HOH HOH B . 
M 6 HOH 264 864  463 HOH HOH B . 
M 6 HOH 265 865  226 HOH HOH B . 
M 6 HOH 266 866  172 HOH HOH B . 
M 6 HOH 267 867  357 HOH HOH B . 
M 6 HOH 268 868  150 HOH HOH B . 
M 6 HOH 269 869  64  HOH HOH B . 
M 6 HOH 270 870  88  HOH HOH B . 
M 6 HOH 271 871  222 HOH HOH B . 
M 6 HOH 272 872  125 HOH HOH B . 
M 6 HOH 273 873  551 HOH HOH B . 
M 6 HOH 274 874  430 HOH HOH B . 
M 6 HOH 275 875  594 HOH HOH B . 
M 6 HOH 276 876  152 HOH HOH B . 
M 6 HOH 277 877  557 HOH HOH B . 
M 6 HOH 278 878  191 HOH HOH B . 
M 6 HOH 279 879  440 HOH HOH B . 
M 6 HOH 280 880  138 HOH HOH B . 
M 6 HOH 281 881  219 HOH HOH B . 
M 6 HOH 282 882  405 HOH HOH B . 
M 6 HOH 283 883  275 HOH HOH B . 
M 6 HOH 284 884  323 HOH HOH B . 
M 6 HOH 285 885  208 HOH HOH B . 
M 6 HOH 286 886  697 HOH HOH B . 
M 6 HOH 287 887  295 HOH HOH B . 
M 6 HOH 288 888  712 HOH HOH B . 
M 6 HOH 289 889  213 HOH HOH B . 
M 6 HOH 290 890  494 HOH HOH B . 
M 6 HOH 291 891  316 HOH HOH B . 
M 6 HOH 292 892  347 HOH HOH B . 
M 6 HOH 293 893  588 HOH HOH B . 
M 6 HOH 294 894  369 HOH HOH B . 
M 6 HOH 295 895  526 HOH HOH B . 
M 6 HOH 296 896  248 HOH HOH B . 
M 6 HOH 297 897  760 HOH HOH B . 
M 6 HOH 298 898  89  HOH HOH B . 
M 6 HOH 299 899  434 HOH HOH B . 
M 6 HOH 300 900  514 HOH HOH B . 
M 6 HOH 301 901  121 HOH HOH B . 
M 6 HOH 302 902  535 HOH HOH B . 
M 6 HOH 303 903  512 HOH HOH B . 
M 6 HOH 304 904  145 HOH HOH B . 
M 6 HOH 305 905  591 HOH HOH B . 
M 6 HOH 306 906  424 HOH HOH B . 
M 6 HOH 307 907  119 HOH HOH B . 
M 6 HOH 308 908  534 HOH HOH B . 
M 6 HOH 309 909  346 HOH HOH B . 
M 6 HOH 310 910  601 HOH HOH B . 
M 6 HOH 311 911  334 HOH HOH B . 
M 6 HOH 312 912  549 HOH HOH B . 
M 6 HOH 313 913  781 HOH HOH B . 
M 6 HOH 314 914  701 HOH HOH B . 
M 6 HOH 315 915  170 HOH HOH B . 
M 6 HOH 316 916  404 HOH HOH B . 
M 6 HOH 317 917  575 HOH HOH B . 
M 6 HOH 318 918  146 HOH HOH B . 
M 6 HOH 319 919  480 HOH HOH B . 
M 6 HOH 320 920  418 HOH HOH B . 
M 6 HOH 321 921  447 HOH HOH B . 
M 6 HOH 322 922  562 HOH HOH B . 
M 6 HOH 323 923  764 HOH HOH B . 
M 6 HOH 324 924  372 HOH HOH B . 
M 6 HOH 325 925  676 HOH HOH B . 
M 6 HOH 326 926  194 HOH HOH B . 
M 6 HOH 327 927  623 HOH HOH B . 
M 6 HOH 328 928  324 HOH HOH B . 
M 6 HOH 329 929  675 HOH HOH B . 
M 6 HOH 330 930  518 HOH HOH B . 
M 6 HOH 331 931  667 HOH HOH B . 
M 6 HOH 332 932  306 HOH HOH B . 
M 6 HOH 333 933  380 HOH HOH B . 
M 6 HOH 334 934  355 HOH HOH B . 
M 6 HOH 335 935  680 HOH HOH B . 
M 6 HOH 336 936  373 HOH HOH B . 
M 6 HOH 337 937  743 HOH HOH B . 
M 6 HOH 338 938  595 HOH HOH B . 
M 6 HOH 339 939  519 HOH HOH B . 
M 6 HOH 340 940  599 HOH HOH B . 
M 6 HOH 341 941  407 HOH HOH B . 
M 6 HOH 342 942  428 HOH HOH B . 
M 6 HOH 343 943  289 HOH HOH B . 
M 6 HOH 344 944  643 HOH HOH B . 
M 6 HOH 345 945  271 HOH HOH B . 
M 6 HOH 346 946  436 HOH HOH B . 
M 6 HOH 347 947  716 HOH HOH B . 
M 6 HOH 348 948  544 HOH HOH B . 
M 6 HOH 349 949  419 HOH HOH B . 
M 6 HOH 350 950  734 HOH HOH B . 
M 6 HOH 351 951  397 HOH HOH B . 
M 6 HOH 352 952  379 HOH HOH B . 
M 6 HOH 353 953  639 HOH HOH B . 
M 6 HOH 354 954  454 HOH HOH B . 
M 6 HOH 355 955  724 HOH HOH B . 
M 6 HOH 356 956  720 HOH HOH B . 
M 6 HOH 357 957  622 HOH HOH B . 
M 6 HOH 358 958  361 HOH HOH B . 
M 6 HOH 359 959  35  HOH HOH B . 
M 6 HOH 360 960  775 HOH HOH B . 
M 6 HOH 361 961  478 HOH HOH B . 
M 6 HOH 362 962  579 HOH HOH B . 
M 6 HOH 363 963  767 HOH HOH B . 
M 6 HOH 364 964  615 HOH HOH B . 
M 6 HOH 365 965  645 HOH HOH B . 
M 6 HOH 366 966  206 HOH HOH B . 
M 6 HOH 367 967  368 HOH HOH B . 
M 6 HOH 368 968  462 HOH HOH B . 
M 6 HOH 369 969  770 HOH HOH B . 
M 6 HOH 370 970  698 HOH HOH B . 
M 6 HOH 371 971  540 HOH HOH B . 
M 6 HOH 372 972  410 HOH HOH B . 
M 6 HOH 373 973  392 HOH HOH B . 
M 6 HOH 374 974  472 HOH HOH B . 
M 6 HOH 375 975  351 HOH HOH B . 
M 6 HOH 376 976  604 HOH HOH B . 
M 6 HOH 377 977  762 HOH HOH B . 
M 6 HOH 378 978  367 HOH HOH B . 
M 6 HOH 379 979  754 HOH HOH B . 
M 6 HOH 380 980  583 HOH HOH B . 
M 6 HOH 381 981  529 HOH HOH B . 
M 6 HOH 382 982  233 HOH HOH B . 
M 6 HOH 383 983  244 HOH HOH B . 
M 6 HOH 384 984  413 HOH HOH B . 
M 6 HOH 385 985  135 HOH HOH B . 
M 6 HOH 386 986  563 HOH HOH B . 
M 6 HOH 387 987  663 HOH HOH B . 
M 6 HOH 388 988  552 HOH HOH B . 
M 6 HOH 389 989  609 HOH HOH B . 
M 6 HOH 390 990  452 HOH HOH B . 
M 6 HOH 391 991  349 HOH HOH B . 
M 6 HOH 392 992  364 HOH HOH B . 
M 6 HOH 393 993  142 HOH HOH B . 
M 6 HOH 394 994  282 HOH HOH B . 
M 6 HOH 395 995  515 HOH HOH B . 
M 6 HOH 396 996  559 HOH HOH B . 
M 6 HOH 397 997  613 HOH HOH B . 
M 6 HOH 398 998  679 HOH HOH B . 
M 6 HOH 399 999  568 HOH HOH B . 
M 6 HOH 400 1000 240 HOH HOH B . 
M 6 HOH 401 1001 348 HOH HOH B . 
M 6 HOH 402 1002 331 HOH HOH B . 
M 6 HOH 403 1003 738 HOH HOH B . 
M 6 HOH 404 1004 581 HOH HOH B . 
M 6 HOH 405 1005 567 HOH HOH B . 
M 6 HOH 406 1006 527 HOH HOH B . 
M 6 HOH 407 1007 690 HOH HOH B . 
M 6 HOH 408 1008 196 HOH HOH B . 
M 6 HOH 409 1009 778 HOH HOH B . 
M 6 HOH 410 1010 603 HOH HOH B . 
M 6 HOH 411 1011 606 HOH HOH B . 
M 6 HOH 412 1012 429 HOH HOH B . 
M 6 HOH 413 1013 614 HOH HOH B . 
M 6 HOH 414 1014 587 HOH HOH B . 
M 6 HOH 415 1015 647 HOH HOH B . 
M 6 HOH 416 1016 417 HOH HOH B . 
M 6 HOH 417 1017 393 HOH HOH B . 
M 6 HOH 418 1018 721 HOH HOH B . 
M 6 HOH 419 1019 411 HOH HOH B . 
M 6 HOH 420 1020 104 HOH HOH B . 
M 6 HOH 421 1021 715 HOH HOH B . 
M 6 HOH 422 1022 489 HOH HOH B . 
M 6 HOH 423 1023 729 HOH HOH B . 
M 6 HOH 424 1024 722 HOH HOH B . 
M 6 HOH 425 1025 693 HOH HOH B . 
M 6 HOH 426 1026 726 HOH HOH B . 
M 6 HOH 427 1027 628 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   ? ? ? '(1.20.1_4487: ???)' 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                     8YB1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.860 
_cell.length_a_esd                 ? 
_cell.length_b                     128.490 
_cell.length_b_esd                 ? 
_cell.length_c                     149.510 
_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                         8YB1 
_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                   8YB1 
_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          54.67 
_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                                       8YB1 
_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                                     149341 
_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                                93.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.88 
_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                                   0.956 
_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                           1.35 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3671 
_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                                  0.421 
_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                                 8YB1 
_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                             10.00 
_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                     149188 
_refine.ls_number_reflns_R_free                  7477 
_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                          0.1852 
_refine.ls_R_factor_R_free                       0.2138 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1838 
_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             1.10 
_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                 25.42 
_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                            0.25 
_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                        10.00 
_refine_hist.number_atoms_solvent             783 
_refine_hist.number_atoms_total               8283 
_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        7328 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         172 
_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 ? 7722  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.978 ? 10459 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.989 ? 1068  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053 ? 1109  ? 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  . . 241 4650 100.00 . . . . 0.3875 . . . . . . . . . . . 0.3891 
'X-RAY DIFFRACTION' 1.62 1.64  . . 240 4723 100.00 . . . . 0.3777 . . . . . . . . . . . 0.3538 
'X-RAY DIFFRACTION' 1.64 1.66  . . 243 4645 100.00 . . . . 0.3666 . . . . . . . . . . . 0.3944 
'X-RAY DIFFRACTION' 1.66 1.68  . . 268 4696 100.00 . . . . 0.3614 . . . . . . . . . . . 0.3646 
'X-RAY DIFFRACTION' 1.68 1.70  . . 240 4638 100.00 . . . . 0.3533 . . . . . . . . . . . 0.3554 
'X-RAY DIFFRACTION' 1.70 1.72  . . 262 4673 100.00 . . . . 0.3391 . . . . . . . . . . . 0.3568 
'X-RAY DIFFRACTION' 1.72 1.75  . . 266 4657 100.00 . . . . 0.3312 . . . . . . . . . . . 0.3534 
'X-RAY DIFFRACTION' 1.75 1.77  . . 233 4686 100.00 . . . . 0.3233 . . . . . . . . . . . 0.3576 
'X-RAY DIFFRACTION' 1.77 1.80  . . 257 4664 100.00 . . . . 0.3050 . . . . . . . . . . . 0.3302 
'X-RAY DIFFRACTION' 1.80 1.83  . . 240 4706 100.00 . . . . 0.2865 . . . . . . . . . . . 0.2799 
'X-RAY DIFFRACTION' 1.83 1.86  . . 257 4676 100.00 . . . . 0.2671 . . . . . . . . . . . 0.3235 
'X-RAY DIFFRACTION' 1.86 1.90  . . 267 4691 100.00 . . . . 0.2574 . . . . . . . . . . . 0.2959 
'X-RAY DIFFRACTION' 1.90 1.93  . . 258 4643 100.00 . . . . 0.2436 . . . . . . . . . . . 0.2959 
'X-RAY DIFFRACTION' 1.93 1.97  . . 234 4721 100.00 . . . . 0.2138 . . . . . . . . . . . 0.2632 
'X-RAY DIFFRACTION' 1.97 2.01  . . 240 4719 100.00 . . . . 0.2074 . . . . . . . . . . . 0.2244 
'X-RAY DIFFRACTION' 2.01 2.06  . . 260 4679 100.00 . . . . 0.1972 . . . . . . . . . . . 0.2461 
'X-RAY DIFFRACTION' 2.06 2.11  . . 267 4706 100.00 . . . . 0.1765 . . . . . . . . . . . 0.2190 
'X-RAY DIFFRACTION' 2.11 2.17  . . 246 4720 100.00 . . . . 0.1792 . . . . . . . . . . . 0.2160 
'X-RAY DIFFRACTION' 2.17 2.23  . . 261 4677 100.00 . . . . 0.1773 . . . . . . . . . . . 0.2209 
'X-RAY DIFFRACTION' 2.23 2.30  . . 226 4725 100.00 . . . . 0.1741 . . . . . . . . . . . 0.2141 
'X-RAY DIFFRACTION' 2.30 2.38  . . 221 4766 100.00 . . . . 0.1674 . . . . . . . . . . . 0.1908 
'X-RAY DIFFRACTION' 2.38 2.48  . . 264 4739 100.00 . . . . 0.1648 . . . . . . . . . . . 0.2029 
'X-RAY DIFFRACTION' 2.48 2.59  . . 250 4722 100.00 . . . . 0.1753 . . . . . . . . . . . 0.2010 
'X-RAY DIFFRACTION' 2.59 2.72  . . 222 4788 100.00 . . . . 0.1809 . . . . . . . . . . . 0.2205 
'X-RAY DIFFRACTION' 2.72 2.89  . . 275 4716 100.00 . . . . 0.1757 . . . . . . . . . . . 0.2096 
'X-RAY DIFFRACTION' 2.89 3.10  . . 236 4795 100.00 . . . . 0.1805 . . . . . . . . . . . 0.2124 
'X-RAY DIFFRACTION' 3.10 3.41  . . 250 4790 100.00 . . . . 0.1711 . . . . . . . . . . . 0.2145 
'X-RAY DIFFRACTION' 3.41 3.87  . . 241 4829 100.00 . . . . 0.1587 . . . . . . . . . . . 0.1824 
'X-RAY DIFFRACTION' 3.87 4.79  . . 230 4881 100.00 . . . . 0.1527 . . . . . . . . . . . 0.1726 
'X-RAY DIFFRACTION' 4.79 10.00 . . 282 4990 100.00 . . . . 0.1761 . . . . . . . . . . . 0.1909 
# 
_struct.entry_id                     8YB1 
_struct.title                        
'XFEL crystal structure of the reduced form of F87A/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        8YB1 
_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 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
K N N 5 ? 
L N N 6 ? 
M 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 8YB1 A 1 ? 455 ? P14779 2 ? 456 ? 1 455 
2 1 8YB1 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 8YB1 ALA A 87  ? UNP P14779 PHE 88  'engineered mutation' 87  1 
1 8YB1 HIS A 393 ? UNP P14779 PHE 394 'engineered mutation' 393 2 
2 8YB1 ALA B 87  ? UNP P14779 PHE 88  'engineered mutation' 87  3 
2 8YB1 HIS B 393 ? UNP P14779 PHE 394 'engineered mutation' 393 4 
# 
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)'  19110 ? 
2 'ABSA (A^2)' 1320  ? 
2 MORE         -20   ? 
2 'SSA (A^2)'  19010 ? 
# 
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,L       
2 1 B,F,G,H,I,J,K,M 
# 
_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 ? LYS A 309 ? SER A 304 LYS A 309 1 ? 6  
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 ? GLN B 189 ? HIS B 171 GLN B 189 1 ? 19 
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 ? ? ? ? ? ? ? 2.400 ? ? 
metalc2 metalc ? ? B CYS 400 SG ? ? ? 1_555 F HEM . FE ? ? B CYS 400 B HEM 501 1_555 ? ? ? ? ? ? ? 2.423 ? ? 
# 
_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_555 100.8 ? 
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 89.2  ? 
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 89.1  ? 
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 87.4  ? 
5  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 170.8 ? 
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 86.7  ? 
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 99.2  ? 
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 91.0  ? 
9  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 171.4 ? 
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 92.0  ? 
11 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NA ? F HEM . ? B HEM 501 ? 1_555 102.5 ? 
12 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NB ? F HEM . ? B HEM 501 ? 1_555 90.2  ? 
13 NA ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NB ? F HEM . ? B HEM 501 ? 1_555 88.9  ? 
14 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NC ? F HEM . ? B HEM 501 ? 1_555 86.2  ? 
15 NA ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NC ? F HEM . ? B HEM 501 ? 1_555 170.5 ? 
16 NB ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NC ? F HEM . ? B HEM 501 ? 1_555 87.4  ? 
17 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 ND ? F HEM . ? B HEM 501 ? 1_555 99.0  ? 
18 NA ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 ND ? F HEM . ? B HEM 501 ? 1_555 91.6  ? 
19 NB ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 ND ? F HEM . ? B HEM 501 ? 1_555 170.4 ? 
20 NC ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 ND ? F HEM . ? B HEM 501 ? 1_555 90.7  ? 
# 
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 PHE A 42  ? N PHE A 42  O THR A 49  ? O THR A 49  
AA1 2 3 N LEU A 52  ? N LEU A 52  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 ALA B 44  ? N ALA B 44  O ARG B 47  ? O ARG B 47  
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                   8YB1 
_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 ? ? 2.11 
2 1 NZ  B LYS 309 ? ? O1 B GOL 504 ? ? 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  ? ? 57.95   -123.76 
2  1 ASP A 84  ? ? -98.74  37.90   
3  1 HIS A 266 ? ? -142.14 -38.22  
4  1 ASP A 370 ? ? -79.64  32.55   
5  1 LEU A 437 ? ? 70.99   -61.63  
6  1 LYS B 15  ? ? 57.08   -127.34 
7  1 ASP B 84  ? ? -99.54  36.99   
8  1 ASP B 232 ? ? -123.85 -165.89 
9  1 HIS B 266 ? ? -141.20 -38.88  
10 1 GLU B 344 ? ? -142.38 -24.54  
11 1 ASP B 370 ? ? -91.97  39.67   
12 1 LEU B 437 ? ? 70.54   -61.90  
# 
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          21740 
_pdbx_serial_crystallography_data_reduction.droplet_hits          ? 
_pdbx_serial_crystallography_data_reduction.frames_failed_index   ? 
_pdbx_serial_crystallography_data_reduction.frames_indexed        14685 
_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        5.6 
# 
_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                    8YB1 
_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]   0.016989 
_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]   0.007783 
_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]   0.006689 
_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   ? -11.082 -23.089 -24.392 1.00 72.05  ? 1    THR A N   1 
ATOM   2    C  CA  . THR A 1 1   ? -9.820  -23.422 -23.734 1.00 72.17  ? 1    THR A CA  1 
ATOM   3    C  C   . THR A 1 1   ? -10.046 -24.198 -22.431 1.00 67.04  ? 1    THR A C   1 
ATOM   4    O  O   . THR A 1 1   ? -9.407  -23.920 -21.415 1.00 69.04  ? 1    THR A O   1 
ATOM   5    C  CB  . THR A 1 1   ? -8.988  -22.149 -23.440 1.00 74.11  ? 1    THR A CB  1 
ATOM   6    O  OG1 . THR A 1 1   ? -8.055  -22.403 -22.378 1.00 77.84  ? 1    THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 1   ? -9.894  -20.980 -23.064 1.00 68.03  ? 1    THR A CG2 1 
ATOM   8    N  N   . ILE A 1 2   ? -10.955 -25.174 -22.472 1.00 65.70  ? 2    ILE A N   1 
ATOM   9    C  CA  . ILE A 1 2   ? -11.274 -25.999 -21.308 1.00 65.18  ? 2    ILE A CA  1 
ATOM   10   C  C   . ILE A 1 2   ? -10.026 -26.746 -20.851 1.00 67.28  ? 2    ILE A C   1 
ATOM   11   O  O   . ILE A 1 2   ? -9.514  -27.619 -21.564 1.00 65.27  ? 2    ILE A O   1 
ATOM   12   C  CB  . ILE A 1 2   ? -12.416 -26.985 -21.623 1.00 63.05  ? 2    ILE A CB  1 
ATOM   13   C  CG1 . ILE A 1 2   ? -13.707 -26.224 -21.940 1.00 66.96  ? 2    ILE A CG1 1 
ATOM   14   C  CG2 . ILE A 1 2   ? -12.628 -27.952 -20.467 1.00 60.27  ? 2    ILE A CG2 1 
ATOM   15   C  CD1 . ILE A 1 2   ? -14.838 -27.115 -22.441 1.00 71.27  ? 2    ILE A CD1 1 
ATOM   16   N  N   . LYS A 1 3   ? -9.530  -26.411 -19.662 1.00 62.67  ? 3    LYS A N   1 
ATOM   17   C  CA  . LYS A 1 3   ? -8.360  -27.070 -19.098 1.00 59.58  ? 3    LYS A CA  1 
ATOM   18   C  C   . LYS A 1 3   ? -8.772  -28.210 -18.172 1.00 60.44  ? 3    LYS A C   1 
ATOM   19   O  O   . LYS A 1 3   ? -9.904  -28.274 -17.680 1.00 58.66  ? 3    LYS A O   1 
ATOM   20   C  CB  . LYS A 1 3   ? -7.491  -26.082 -18.322 1.00 56.30  ? 3    LYS A CB  1 
ATOM   21   C  CG  . LYS A 1 3   ? -6.532  -25.272 -19.157 1.00 61.68  ? 3    LYS A CG  1 
ATOM   22   C  CD  . LYS A 1 3   ? -5.357  -24.824 -18.302 1.00 60.90  ? 3    LYS A CD  1 
ATOM   23   C  CE  . LYS A 1 3   ? -4.299  -24.116 -19.136 1.00 66.50  ? 3    LYS A CE  1 
ATOM   24   N  NZ  . LYS A 1 3   ? -4.712  -22.749 -19.555 1.00 68.48  ? 3    LYS A NZ  1 
ATOM   25   N  N   . GLU A 1 4   ? -7.821  -29.109 -17.933 1.00 59.58  ? 4    GLU A N   1 
ATOM   26   C  CA  . GLU A 1 4   ? -7.975  -30.216 -17.000 1.00 59.89  ? 4    GLU A CA  1 
ATOM   27   C  C   . GLU A 1 4   ? -7.288  -29.841 -15.695 1.00 52.62  ? 4    GLU A C   1 
ATOM   28   O  O   . GLU A 1 4   ? -6.096  -29.525 -15.687 1.00 52.06  ? 4    GLU A O   1 
ATOM   29   C  CB  . GLU A 1 4   ? -7.366  -31.494 -17.577 1.00 63.06  ? 4    GLU A CB  1 
ATOM   30   C  CG  . GLU A 1 4   ? -7.541  -32.737 -16.718 1.00 64.01  ? 4    GLU A CG  1 
ATOM   31   C  CD  . GLU A 1 4   ? -8.979  -33.206 -16.658 1.00 75.03  ? 4    GLU A CD  1 
ATOM   32   O  OE1 . GLU A 1 4   ? -9.885  -32.346 -16.604 1.00 76.27  ? 4    GLU A OE1 1 
ATOM   33   O  OE2 . GLU A 1 4   ? -9.205  -34.437 -16.673 1.00 80.52  ? 4    GLU A OE2 1 
ATOM   34   N  N   . MET A 1 5   ? -8.031  -29.890 -14.595 1.00 54.80  ? 5    MET A N   1 
ATOM   35   C  CA  . MET A 1 5   ? -7.354  -29.314 -13.438 1.00 44.19  ? 5    MET A CA  1 
ATOM   36   C  C   . MET A 1 5   ? -6.616  -30.393 -12.641 1.00 41.82  ? 5    MET A C   1 
ATOM   37   O  O   . MET A 1 5   ? -7.084  -31.531 -12.556 1.00 41.44  ? 5    MET A O   1 
ATOM   38   C  CB  . MET A 1 5   ? -8.381  -28.573 -12.563 1.00 44.64  ? 5    MET A CB  1 
ATOM   39   C  CG  . MET A 1 5   ? -9.053  -29.374 -11.482 1.00 39.74  ? 5    MET A CG  1 
ATOM   40   S  SD  . MET A 1 5   ? -10.238 -28.425 -10.498 1.00 41.31  ? 5    MET A SD  1 
ATOM   41   C  CE  . MET A 1 5   ? -11.019 -27.427 -11.774 1.00 40.39  ? 5    MET A CE  1 
ATOM   42   N  N   . PRO A 1 6   ? -5.438  -30.081 -12.097 1.00 36.41  ? 6    PRO A N   1 
ATOM   43   C  CA  . PRO A 1 6   ? -4.687  -31.074 -11.319 1.00 37.27  ? 6    PRO A CA  1 
ATOM   44   C  C   . PRO A 1 6   ? -5.449  -31.503 -10.076 1.00 43.08  ? 6    PRO A C   1 
ATOM   45   O  O   . PRO A 1 6   ? -6.423  -30.875 -9.657  1.00 35.37  ? 6    PRO A O   1 
ATOM   46   C  CB  . PRO A 1 6   ? -3.398  -30.337 -10.943 1.00 41.78  ? 6    PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 6   ? -3.769  -28.897 -10.965 1.00 39.62  ? 6    PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 6   ? -4.776  -28.766 -12.092 1.00 38.09  ? 6    PRO A CD  1 
ATOM   49   N  N   . GLN A 1 7   ? -4.974  -32.596 -9.470  1.00 37.96  ? 7    GLN A N   1 
ATOM   50   C  CA  . GLN A 1 7   ? -5.566  -33.141 -8.256  1.00 39.74  ? 7    GLN A CA  1 
ATOM   51   C  C   . GLN A 1 7   ? -4.449  -33.780 -7.449  1.00 39.37  ? 7    GLN A C   1 
ATOM   52   O  O   . GLN A 1 7   ? -3.604  -34.476 -8.034  1.00 37.79  ? 7    GLN A O   1 
ATOM   53   C  CB  . GLN A 1 7   ? -6.647  -34.175 -8.568  1.00 37.45  ? 7    GLN A CB  1 
ATOM   54   C  CG  . GLN A 1 7   ? -7.271  -34.816 -7.335  1.00 40.97  ? 7    GLN A CG  1 
ATOM   55   C  CD  . GLN A 1 7   ? -8.371  -35.792 -7.693  1.00 43.55  ? 7    GLN A CD  1 
ATOM   56   O  OE1 . GLN A 1 7   ? -8.580  -36.117 -8.864  1.00 47.51  ? 7    GLN A OE1 1 
ATOM   57   N  NE2 . GLN A 1 7   ? -9.093  -36.254 -6.690  1.00 42.92  ? 7    GLN A NE2 1 
ATOM   58   N  N   . PRO A 1 8   ? -4.397  -33.562 -6.114  1.00 38.17  ? 8    PRO A N   1 
ATOM   59   C  CA  . PRO A 1 8   ? -3.357  -34.221 -5.317  1.00 34.61  ? 8    PRO A CA  1 
ATOM   60   C  C   . PRO A 1 8   ? -3.580  -35.721 -5.190  1.00 34.74  ? 8    PRO A C   1 
ATOM   61   O  O   . PRO A 1 8   ? -4.560  -36.277 -5.699  1.00 35.75  ? 8    PRO A O   1 
ATOM   62   C  CB  . PRO A 1 8   ? -3.443  -33.518 -3.949  1.00 32.36  ? 8    PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 8   ? -4.852  -33.039 -3.858  1.00 36.29  ? 8    PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 8   ? -5.244  -32.675 -5.288  1.00 37.54  ? 8    PRO A CD  1 
ATOM   65   N  N   . LYS A 1 9   ? -2.663  -36.382 -4.496  1.00 36.14  ? 9    LYS A N   1 
ATOM   66   C  CA  . LYS A 1 9   ? -2.652  -37.838 -4.468  1.00 34.72  ? 9    LYS A CA  1 
ATOM   67   C  C   . LYS A 1 9   ? -3.888  -38.395 -3.776  1.00 39.96  ? 9    LYS A C   1 
ATOM   68   O  O   . LYS A 1 9   ? -4.368  -37.848 -2.780  1.00 37.12  ? 9    LYS A O   1 
ATOM   69   C  CB  . LYS A 1 9   ? -1.383  -38.347 -3.766  1.00 34.46  ? 9    LYS A CB  1 
ATOM   70   C  CG  . LYS A 1 9   ? -1.230  -37.974 -2.298  1.00 35.75  ? 9    LYS A CG  1 
ATOM   71   C  CD  . LYS A 1 9   ? 0.215   -38.206 -1.841  1.00 37.32  ? 9    LYS A CD  1 
ATOM   72   C  CE  . LYS A 1 9   ? 0.404   -37.826 -0.382  1.00 41.50  ? 9    LYS A CE  1 
ATOM   73   N  NZ  . LYS A 1 9   ? 1.841   -37.685 0.023   1.00 42.78  ? 9    LYS A NZ  1 
ATOM   74   N  N   . THR A 1 10  ? -4.367  -39.520 -4.292  1.00 36.31  ? 10   THR A N   1 
ATOM   75   C  CA  . THR A 1 10  ? -5.570  -40.189 -3.829  1.00 38.61  ? 10   THR A CA  1 
ATOM   76   C  C   . THR A 1 10  ? -5.244  -41.481 -3.083  1.00 38.44  ? 10   THR A C   1 
ATOM   77   O  O   . THR A 1 10  ? -4.160  -42.067 -3.215  1.00 34.43  ? 10   THR A O   1 
ATOM   78   C  CB  . THR A 1 10  ? -6.501  -40.508 -5.003  1.00 40.03  ? 10   THR A CB  1 
ATOM   79   O  OG1 . THR A 1 10  ? -5.800  -41.315 -5.968  1.00 41.44  ? 10   THR A OG1 1 
ATOM   80   C  CG2 . THR A 1 10  ? -6.989  -39.221 -5.668  1.00 35.41  ? 10   THR A CG2 1 
ATOM   81   N  N   . PHE A 1 11  ? -6.238  -41.932 -2.317  1.00 36.87  ? 11   PHE A N   1 
ATOM   82   C  CA  . PHE A 1 11  ? -6.114  -43.058 -1.396  1.00 38.40  ? 11   PHE A CA  1 
ATOM   83   C  C   . PHE A 1 11  ? -7.270  -44.034 -1.645  1.00 40.39  ? 11   PHE A C   1 
ATOM   84   O  O   . PHE A 1 11  ? -8.037  -44.370 -0.742  1.00 40.76  ? 11   PHE A O   1 
ATOM   85   C  CB  . PHE A 1 11  ? -6.115  -42.577 0.061   1.00 34.08  ? 11   PHE A CB  1 
ATOM   86   C  CG  . PHE A 1 11  ? -4.919  -41.737 0.427   1.00 34.98  ? 11   PHE A CG  1 
ATOM   87   C  CD1 . PHE A 1 11  ? -4.814  -40.428 -0.015  1.00 36.06  ? 11   PHE A CD1 1 
ATOM   88   C  CD2 . PHE A 1 11  ? -3.924  -42.239 1.239   1.00 34.42  ? 11   PHE A CD2 1 
ATOM   89   C  CE1 . PHE A 1 11  ? -3.730  -39.649 0.320   1.00 35.93  ? 11   PHE A CE1 1 
ATOM   90   C  CE2 . PHE A 1 11  ? -2.830  -41.466 1.575   1.00 37.65  ? 11   PHE A CE2 1 
ATOM   91   C  CZ  . PHE A 1 11  ? -2.729  -40.169 1.112   1.00 36.69  ? 11   PHE A CZ  1 
ATOM   92   N  N   . GLY A 1 12  ? -7.389  -44.499 -2.887  1.00 37.09  ? 12   GLY A N   1 
ATOM   93   C  CA  . GLY A 1 12  ? -8.476  -45.408 -3.215  1.00 37.86  ? 12   GLY A CA  1 
ATOM   94   C  C   . GLY A 1 12  ? -9.828  -44.781 -2.930  1.00 44.56  ? 12   GLY A C   1 
ATOM   95   O  O   . GLY A 1 12  ? -10.069 -43.604 -3.228  1.00 43.07  ? 12   GLY A O   1 
ATOM   96   N  N   . GLU A 1 13  ? -10.716 -45.565 -2.312  1.00 41.83  ? 13   GLU A N   1 
ATOM   97   C  CA  . GLU A 1 13  ? -12.090 -45.109 -2.104  1.00 48.57  ? 13   GLU A CA  1 
ATOM   98   C  C   . GLU A 1 13  ? -12.172 -43.895 -1.178  1.00 47.39  ? 13   GLU A C   1 
ATOM   99   O  O   . GLU A 1 13  ? -13.183 -43.180 -1.197  1.00 44.15  ? 13   GLU A O   1 
ATOM   100  C  CB  . GLU A 1 13  ? -12.957 -46.245 -1.541  1.00 49.86  ? 13   GLU A CB  1 
ATOM   101  C  CG  . GLU A 1 13  ? -12.621 -46.654 -0.103  1.00 52.93  ? 13   GLU A CG  1 
ATOM   102  C  CD  . GLU A 1 13  ? -11.445 -47.624 0.026   1.00 63.70  ? 13   GLU A CD  1 
ATOM   103  O  OE1 . GLU A 1 13  ? -10.494 -47.574 -0.802  1.00 65.13  ? 13   GLU A OE1 1 
ATOM   104  O  OE2 . GLU A 1 13  ? -11.472 -48.434 0.984   1.00 69.55  ? 13   GLU A OE2 1 
ATOM   105  N  N   . LEU A 1 14  ? -11.151 -43.655 -0.355  1.00 41.47  ? 14   LEU A N   1 
ATOM   106  C  CA  . LEU A 1 14  ? -11.114 -42.456 0.476   1.00 41.22  ? 14   LEU A CA  1 
ATOM   107  C  C   . LEU A 1 14  ? -10.724 -41.202 -0.304  1.00 43.90  ? 14   LEU A C   1 
ATOM   108  O  O   . LEU A 1 14  ? -10.770 -40.103 0.264   1.00 42.21  ? 14   LEU A O   1 
ATOM   109  C  CB  . LEU A 1 14  ? -10.137 -42.654 1.634   1.00 41.29  ? 14   LEU A CB  1 
ATOM   110  C  CG  . LEU A 1 14  ? -10.449 -43.861 2.518   1.00 42.49  ? 14   LEU A CG  1 
ATOM   111  C  CD1 . LEU A 1 14  ? -9.426  -44.011 3.625   1.00 42.52  ? 14   LEU A CD1 1 
ATOM   112  C  CD2 . LEU A 1 14  ? -11.845 -43.720 3.098   1.00 47.08  ? 14   LEU A CD2 1 
ATOM   113  N  N   . LYS A 1 15  ? -10.298 -41.350 -1.562  1.00 39.13  ? 15   LYS A N   1 
ATOM   114  C  CA  . LYS A 1 15  ? -9.999  -40.232 -2.465  1.00 38.89  ? 15   LYS A CA  1 
ATOM   115  C  C   . LYS A 1 15  ? -8.928  -39.349 -1.829  1.00 42.13  ? 15   LYS A C   1 
ATOM   116  O  O   . LYS A 1 15  ? -7.844  -39.872 -1.514  1.00 39.15  ? 15   LYS A O   1 
ATOM   117  C  CB  . LYS A 1 15  ? -11.332 -39.575 -2.809  1.00 43.00  ? 15   LYS A CB  1 
ATOM   118  C  CG  . LYS A 1 15  ? -12.261 -40.558 -3.531  1.00 48.46  ? 15   LYS A CG  1 
ATOM   119  C  CD  . LYS A 1 15  ? -13.619 -39.977 -3.852  1.00 50.13  ? 15   LYS A CD  1 
ATOM   120  C  CE  . LYS A 1 15  ? -14.512 -41.025 -4.535  1.00 51.24  ? 15   LYS A CE  1 
ATOM   121  N  NZ  . LYS A 1 15  ? -15.938 -40.580 -4.549  1.00 55.15  ? 15   LYS A NZ  1 
ATOM   122  N  N   . ASN A 1 16  ? -9.150  -38.042 -1.632  1.00 38.54  ? 16   ASN A N   1 
ATOM   123  C  CA  . ASN A 1 16  ? -8.131  -37.175 -1.042  1.00 38.16  ? 16   ASN A CA  1 
ATOM   124  C  C   . ASN A 1 16  ? -8.285  -37.011 0.465   1.00 34.75  ? 16   ASN A C   1 
ATOM   125  O  O   . ASN A 1 16  ? -7.449  -36.351 1.092   1.00 39.21  ? 16   ASN A O   1 
ATOM   126  C  CB  . ASN A 1 16  ? -8.150  -35.781 -1.694  1.00 36.14  ? 16   ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 16  ? -7.800  -35.816 -3.182  1.00 35.41  ? 16   ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 16  ? -8.625  -35.476 -4.041  1.00 35.89  ? 16   ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 16  ? -6.571  -36.234 -3.493  1.00 35.84  ? 16   ASN A ND2 1 
ATOM   130  N  N   . LEU A 1 17  ? -9.329  -37.583 1.056   1.00 39.79  ? 17   LEU A N   1 
ATOM   131  C  CA  . LEU A 1 17  ? -9.608  -37.348 2.472   1.00 38.94  ? 17   LEU A CA  1 
ATOM   132  C  C   . LEU A 1 17  ? -8.402  -37.517 3.384   1.00 40.97  ? 17   LEU A C   1 
ATOM   133  O  O   . LEU A 1 17  ? -8.217  -36.673 4.279   1.00 40.30  ? 17   LEU A O   1 
ATOM   134  C  CB  . LEU A 1 17  ? -10.743 -38.278 2.915   1.00 40.03  ? 17   LEU A CB  1 
ATOM   135  C  CG  . LEU A 1 17  ? -11.578 -37.762 4.085   1.00 46.01  ? 17   LEU A CG  1 
ATOM   136  C  CD1 . LEU A 1 17  ? -12.098 -36.341 3.792   1.00 45.27  ? 17   LEU A CD1 1 
ATOM   137  C  CD2 . LEU A 1 17  ? -12.721 -38.719 4.335   1.00 46.35  ? 17   LEU A CD2 1 
ATOM   138  N  N   . PRO A 1 18  ? -7.562  -38.546 3.234   1.00 35.21  ? 18   PRO A N   1 
ATOM   139  C  CA  . PRO A 1 18  ? -6.440  -38.719 4.170   1.00 34.02  ? 18   PRO A CA  1 
ATOM   140  C  C   . PRO A 1 18  ? -5.415  -37.602 4.121   1.00 35.04  ? 18   PRO A C   1 
ATOM   141  O  O   . PRO A 1 18  ? -4.616  -37.476 5.061   1.00 36.02  ? 18   PRO A O   1 
ATOM   142  C  CB  . PRO A 1 18  ? -5.834  -40.064 3.746   1.00 38.47  ? 18   PRO A CB  1 
ATOM   143  C  CG  . PRO A 1 18  ? -6.998  -40.799 3.131   1.00 39.76  ? 18   PRO A CG  1 
ATOM   144  C  CD  . PRO A 1 18  ? -7.776  -39.733 2.387   1.00 32.40  ? 18   PRO A CD  1 
ATOM   145  N  N   . LEU A 1 19  ? -5.420  -36.769 3.079   1.00 33.59  ? 19   LEU A N   1 
ATOM   146  C  CA  . LEU A 1 19  ? -4.564  -35.585 3.097   1.00 33.49  ? 19   LEU A CA  1 
ATOM   147  C  C   . LEU A 1 19  ? -4.924  -34.638 4.236   1.00 36.02  ? 19   LEU A C   1 
ATOM   148  O  O   . LEU A 1 19  ? -4.096  -33.819 4.634   1.00 38.29  ? 19   LEU A O   1 
ATOM   149  C  CB  . LEU A 1 19  ? -4.650  -34.854 1.755   1.00 35.86  ? 19   LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 19  ? -4.154  -35.719 0.588   1.00 37.12  ? 19   LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 19  ? -4.299  -34.964 -0.724  1.00 37.81  ? 19   LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 19  ? -2.700  -36.122 0.833   1.00 38.26  ? 19   LEU A CD2 1 
ATOM   153  N  N   . LEU A 1 20  ? -6.138  -34.725 4.757   1.00 37.05  ? 20   LEU A N   1 
ATOM   154  C  CA  . LEU A 1 20  ? -6.540  -33.928 5.910   1.00 39.07  ? 20   LEU A CA  1 
ATOM   155  C  C   . LEU A 1 20  ? -6.197  -34.585 7.238   1.00 39.73  ? 20   LEU A C   1 
ATOM   156  O  O   . LEU A 1 20  ? -6.524  -34.023 8.295   1.00 39.51  ? 20   LEU A O   1 
ATOM   157  C  CB  . LEU A 1 20  ? -8.044  -33.655 5.856   1.00 35.59  ? 20   LEU A CB  1 
ATOM   158  C  CG  . LEU A 1 20  ? -8.467  -32.885 4.601   1.00 44.43  ? 20   LEU A CG  1 
ATOM   159  C  CD1 . LEU A 1 20  ? -9.978  -32.684 4.522   1.00 41.63  ? 20   LEU A CD1 1 
ATOM   160  C  CD2 . LEU A 1 20  ? -7.741  -31.557 4.558   1.00 39.30  ? 20   LEU A CD2 1 
ATOM   161  N  N   . ASN A 1 21  ? -5.543  -35.748 7.226   1.00 38.60  ? 21   ASN A N   1 
ATOM   162  C  CA  . ASN A 1 21  ? -5.246  -36.452 8.480   1.00 41.04  ? 21   ASN A CA  1 
ATOM   163  C  C   . ASN A 1 21  ? -3.926  -35.896 9.002   1.00 41.93  ? 21   ASN A C   1 
ATOM   164  O  O   . ASN A 1 21  ? -2.860  -36.516 8.906   1.00 45.75  ? 21   ASN A O   1 
ATOM   165  C  CB  . ASN A 1 21  ? -5.179  -37.961 8.263   1.00 40.15  ? 21   ASN A CB  1 
ATOM   166  C  CG  . ASN A 1 21  ? -4.850  -38.728 9.546   1.00 52.09  ? 21   ASN A CG  1 
ATOM   167  O  OD1 . ASN A 1 21  ? -4.723  -38.142 10.627  1.00 51.51  ? 21   ASN A OD1 1 
ATOM   168  N  ND2 . ASN A 1 21  ? -4.678  -40.039 9.419   1.00 52.52  ? 21   ASN A ND2 1 
ATOM   169  N  N   . THR A 1 22  ? -4.008  -34.685 9.550   1.00 37.48  ? 22   THR A N   1 
ATOM   170  C  CA  . THR A 1 22  ? -2.862  -33.936 10.044  1.00 39.21  ? 22   THR A CA  1 
ATOM   171  C  C   . THR A 1 22  ? -3.373  -32.863 10.995  1.00 39.59  ? 22   THR A C   1 
ATOM   172  O  O   . THR A 1 22  ? -4.508  -32.405 10.874  1.00 40.92  ? 22   THR A O   1 
ATOM   173  C  CB  . THR A 1 22  ? -2.073  -33.278 8.912   1.00 42.40  ? 22   THR A CB  1 
ATOM   174  O  OG1 . THR A 1 22  ? -1.159  -32.313 9.462   1.00 43.34  ? 22   THR A OG1 1 
ATOM   175  C  CG2 . THR A 1 22  ? -3.032  -32.571 7.932   1.00 40.85  ? 22   THR A CG2 1 
ATOM   176  N  N   . ASP A 1 23  ? -2.524  -32.457 11.937  1.00 39.62  ? 23   ASP A N   1 
ATOM   177  C  CA  . ASP A 1 23  ? -2.959  -31.373 12.807  1.00 44.18  ? 23   ASP A CA  1 
ATOM   178  C  C   . ASP A 1 23  ? -2.869  -30.013 12.127  1.00 40.13  ? 23   ASP A C   1 
ATOM   179  O  O   . ASP A 1 23  ? -3.368  -29.032 12.682  1.00 38.25  ? 23   ASP A O   1 
ATOM   180  C  CB  . ASP A 1 23  ? -2.155  -31.354 14.111  1.00 44.46  ? 23   ASP A CB  1 
ATOM   181  C  CG  . ASP A 1 23  ? -0.662  -31.336 13.876  1.00 53.50  ? 23   ASP A CG  1 
ATOM   182  O  OD1 . ASP A 1 23  ? -0.247  -31.339 12.692  1.00 53.63  ? 23   ASP A OD1 1 
ATOM   183  O  OD2 . ASP A 1 23  ? 0.097   -31.321 14.878  1.00 62.32  ? 23   ASP A OD2 1 
ATOM   184  N  N   . LYS A 1 24  ? -2.277  -29.927 10.934  1.00 37.13  ? 24   LYS A N   1 
ATOM   185  C  CA  . LYS A 1 24  ? -2.128  -28.654 10.227  1.00 35.78  ? 24   LYS A CA  1 
ATOM   186  C  C   . LYS A 1 24  ? -2.668  -28.761 8.803   1.00 35.65  ? 24   LYS A C   1 
ATOM   187  O  O   . LYS A 1 24  ? -1.923  -28.611 7.827   1.00 35.28  ? 24   LYS A O   1 
ATOM   188  C  CB  . LYS A 1 24  ? -0.666  -28.217 10.236  1.00 34.18  ? 24   LYS A CB  1 
ATOM   189  C  CG  . LYS A 1 24  ? -0.129  -27.976 11.642  1.00 39.21  ? 24   LYS A CG  1 
ATOM   190  C  CD  . LYS A 1 24  ? 1.303   -27.468 11.632  1.00 37.78  ? 24   LYS A CD  1 
ATOM   191  C  CE  . LYS A 1 24  ? 1.808   -27.266 13.060  1.00 39.36  ? 24   LYS A CE  1 
ATOM   192  N  NZ  . LYS A 1 24  ? 3.200   -26.742 13.089  1.00 39.68  ? 24   LYS A NZ  1 
ATOM   193  N  N   . PRO A 1 25  ? -3.978  -28.975 8.651   1.00 34.09  ? 25   PRO A N   1 
ATOM   194  C  CA  . PRO A 1 25  ? -4.522  -29.205 7.300   1.00 37.26  ? 25   PRO A CA  1 
ATOM   195  C  C   . PRO A 1 25  ? -4.472  -27.987 6.381   1.00 36.25  ? 25   PRO A C   1 
ATOM   196  O  O   . PRO A 1 25  ? -4.245  -28.155 5.174   1.00 34.63  ? 25   PRO A O   1 
ATOM   197  C  CB  . PRO A 1 25  ? -5.962  -29.664 7.578   1.00 35.88  ? 25   PRO A CB  1 
ATOM   198  C  CG  . PRO A 1 25  ? -6.285  -29.093 8.934   1.00 34.43  ? 25   PRO A CG  1 
ATOM   199  C  CD  . PRO A 1 25  ? -4.994  -29.154 9.703   1.00 36.18  ? 25   PRO A CD  1 
ATOM   200  N  N   . VAL A 1 26  ? -4.698  -26.771 6.886   1.00 35.65  ? 26   VAL A N   1 
ATOM   201  C  CA  . VAL A 1 26  ? -4.600  -25.612 5.996   1.00 33.83  ? 26   VAL A CA  1 
ATOM   202  C  C   . VAL A 1 26  ? -3.185  -25.467 5.464   1.00 34.39  ? 26   VAL A C   1 
ATOM   203  O  O   . VAL A 1 26  ? -2.972  -25.172 4.276   1.00 34.13  ? 26   VAL A O   1 
ATOM   204  C  CB  . VAL A 1 26  ? -5.053  -24.330 6.716   1.00 34.34  ? 26   VAL A CB  1 
ATOM   205  C  CG1 . VAL A 1 26  ? -4.673  -23.128 5.881   1.00 31.11  ? 26   VAL A CG1 1 
ATOM   206  C  CG2 . VAL A 1 26  ? -6.561  -24.363 6.940   1.00 35.77  ? 26   VAL A CG2 1 
ATOM   207  N  N   . GLN A 1 27  ? -2.191  -25.662 6.335   1.00 33.13  ? 27   GLN A N   1 
ATOM   208  C  CA  . GLN A 1 27  ? -0.809  -25.574 5.884   1.00 33.62  ? 27   GLN A CA  1 
ATOM   209  C  C   . GLN A 1 27  ? -0.457  -26.699 4.912   1.00 36.73  ? 27   GLN A C   1 
ATOM   210  O  O   . GLN A 1 27  ? 0.298   -26.476 3.953   1.00 37.99  ? 27   GLN A O   1 
ATOM   211  C  CB  . GLN A 1 27  ? 0.116   -25.543 7.103   1.00 33.15  ? 27   GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 27  ? -0.043  -24.245 7.911   1.00 33.60  ? 27   GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 27  ? 0.546   -24.315 9.301   1.00 33.94  ? 27   GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 27  ? 1.730   -24.059 9.496   1.00 35.26  ? 27   GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 27  ? -0.288  -24.635 10.288  1.00 33.64  ? 27   GLN A NE2 1 
ATOM   216  N  N   . ALA A 1 28  ? -1.028  -27.892 5.101   1.00 34.78  ? 28   ALA A N   1 
ATOM   217  C  CA  . ALA A 1 28  ? -0.845  -28.956 4.119   1.00 34.66  ? 28   ALA A CA  1 
ATOM   218  C  C   . ALA A 1 28  ? -1.460  -28.564 2.785   1.00 37.00  ? 28   ALA A C   1 
ATOM   219  O  O   . ALA A 1 28  ? -0.892  -28.845 1.717   1.00 36.58  ? 28   ALA A O   1 
ATOM   220  C  CB  . ALA A 1 28  ? -1.460  -30.261 4.633   1.00 35.61  ? 28   ALA A CB  1 
ATOM   221  N  N   . LEU A 1 29  ? -2.626  -27.905 2.827   1.00 34.99  ? 29   LEU A N   1 
ATOM   222  C  CA  . LEU A 1 29  ? -3.276  -27.480 1.594   1.00 35.31  ? 29   LEU A CA  1 
ATOM   223  C  C   . LEU A 1 29  ? -2.501  -26.365 0.911   1.00 31.54  ? 29   LEU A C   1 
ATOM   224  O  O   . LEU A 1 29  ? -2.451  -26.336 -0.327  1.00 33.89  ? 29   LEU A O   1 
ATOM   225  C  CB  . LEU A 1 29  ? -4.724  -27.050 1.869   1.00 34.93  ? 29   LEU A CB  1 
ATOM   226  C  CG  . LEU A 1 29  ? -5.694  -28.207 2.149   1.00 35.61  ? 29   LEU A CG  1 
ATOM   227  C  CD1 . LEU A 1 29  ? -6.930  -27.722 2.923   1.00 33.91  ? 29   LEU A CD1 1 
ATOM   228  C  CD2 . LEU A 1 29  ? -6.115  -28.884 0.838   1.00 32.30  ? 29   LEU A CD2 1 
ATOM   229  N  N   . MET A 1 30  ? -1.862  -25.470 1.681   1.00 36.15  ? 30   MET A N   1 
ATOM   230  C  CA  . MET A 1 30  ? -0.999  -24.477 1.058   1.00 34.53  ? 30   MET A CA  1 
ATOM   231  C  C   . MET A 1 30  ? 0.153   -25.146 0.320   1.00 34.18  ? 30   MET A C   1 
ATOM   232  O  O   . MET A 1 30  ? 0.568   -24.685 -0.751  1.00 37.40  ? 30   MET A O   1 
ATOM   233  C  CB  . MET A 1 30  ? -0.387  -23.500 2.062   1.00 34.33  ? 30   MET A CB  1 
ATOM   234  C  CG  . MET A 1 30  ? -1.204  -22.269 2.401   1.00 38.62  ? 30   MET A CG  1 
ATOM   235  S  SD  . MET A 1 30  ? -1.110  -21.749 4.120   1.00 36.02  ? 30   MET A SD  1 
ATOM   236  C  CE  . MET A 1 30  ? 0.247   -20.607 3.847   1.00 41.47  ? 30   MET A CE  1 
ATOM   237  N  N   . LYS A 1 31  ? 0.726   -26.196 0.912   1.00 36.46  ? 31   LYS A N   1 
ATOM   238  C  CA  . LYS A 1 31  ? 1.842   -26.886 0.267   1.00 36.98  ? 31   LYS A CA  1 
ATOM   239  C  C   . LYS A 1 31  ? 1.386   -27.572 -1.021  1.00 39.62  ? 31   LYS A C   1 
ATOM   240  O  O   . LYS A 1 31  ? 2.078   -27.530 -2.049  1.00 37.30  ? 31   LYS A O   1 
ATOM   241  C  CB  . LYS A 1 31  ? 2.454   -27.881 1.256   1.00 39.85  ? 31   LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 31  ? 3.745   -28.546 0.822   1.00 46.98  ? 31   LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 31  ? 4.740   -28.652 1.995   1.00 51.88  ? 31   LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 31  ? 5.807   -27.551 1.913   1.00 58.75  ? 31   LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 31  ? 6.368   -27.160 3.246   1.00 61.69  ? 31   LYS A NZ  1 
ATOM   246  N  N   . ILE A 1 32  ? 0.198   -28.175 -1.001  1.00 35.99  ? 32   ILE A N   1 
ATOM   247  C  CA  . ILE A 1 32  ? -0.360  -28.731 -2.228  1.00 35.00  ? 32   ILE A CA  1 
ATOM   248  C  C   . ILE A 1 32  ? -0.521  -27.641 -3.293  1.00 35.12  ? 32   ILE A C   1 
ATOM   249  O  O   . ILE A 1 32  ? -0.176  -27.834 -4.470  1.00 35.64  ? 32   ILE A O   1 
ATOM   250  C  CB  . ILE A 1 32  ? -1.695  -29.432 -1.923  1.00 36.92  ? 32   ILE A CB  1 
ATOM   251  C  CG1 . ILE A 1 32  ? -1.480  -30.647 -1.007  1.00 36.05  ? 32   ILE A CG1 1 
ATOM   252  C  CG2 . ILE A 1 32  ? -2.380  -29.834 -3.226  1.00 38.88  ? 32   ILE A CG2 1 
ATOM   253  C  CD1 . ILE A 1 32  ? -2.790  -31.294 -0.521  1.00 34.20  ? 32   ILE A CD1 1 
ATOM   254  N  N   . ALA A 1 33  ? -1.057  -26.478 -2.901  1.00 38.49  ? 33   ALA A N   1 
ATOM   255  C  CA  . ALA A 1 33  ? -1.190  -25.367 -3.845  1.00 37.57  ? 33   ALA A CA  1 
ATOM   256  C  C   . ALA A 1 33  ? 0.163   -24.945 -4.407  1.00 38.89  ? 33   ALA A C   1 
ATOM   257  O  O   . ALA A 1 33  ? 0.270   -24.625 -5.598  1.00 38.02  ? 33   ALA A O   1 
ATOM   258  C  CB  . ALA A 1 33  ? -1.885  -24.175 -3.173  1.00 36.33  ? 33   ALA A CB  1 
ATOM   259  N  N   . ASP A 1 34  ? 1.199   -24.896 -3.559  1.00 38.83  ? 34   ASP A N   1 
ATOM   260  C  CA  . ASP A 1 34  ? 2.542   -24.613 -4.060  1.00 38.65  ? 34   ASP A CA  1 
ATOM   261  C  C   . ASP A 1 34  ? 2.897   -25.548 -5.200  1.00 39.73  ? 34   ASP A C   1 
ATOM   262  O  O   . ASP A 1 34  ? 3.530   -25.140 -6.181  1.00 46.16  ? 34   ASP A O   1 
ATOM   263  C  CB  . ASP A 1 34  ? 3.596   -24.759 -2.960  1.00 40.49  ? 34   ASP A CB  1 
ATOM   264  C  CG  . ASP A 1 34  ? 3.616   -23.603 -2.001  1.00 45.31  ? 34   ASP A CG  1 
ATOM   265  O  OD1 . ASP A 1 34  ? 3.147   -22.508 -2.372  1.00 48.62  ? 34   ASP A OD1 1 
ATOM   266  O  OD2 . ASP A 1 34  ? 4.106   -23.794 -0.867  1.00 46.64  ? 34   ASP A OD2 1 
ATOM   267  N  N   . GLU A 1 35  ? 2.523   -26.816 -5.079  1.00 42.05  ? 35   GLU A N   1 
ATOM   268  C  CA  . GLU A 1 35  ? 2.938   -27.771 -6.091  1.00 41.09  ? 35   GLU A CA  1 
ATOM   269  C  C   . GLU A 1 35  ? 1.985   -27.811 -7.280  1.00 43.80  ? 35   GLU A C   1 
ATOM   270  O  O   . GLU A 1 35  ? 2.441   -27.934 -8.423  1.00 42.05  ? 35   GLU A O   1 
ATOM   271  C  CB  . GLU A 1 35  ? 3.102   -29.162 -5.469  1.00 46.37  ? 35   GLU A CB  1 
ATOM   272  C  CG  . GLU A 1 35  ? 3.141   -30.284 -6.493  1.00 52.33  ? 35   GLU A CG  1 
ATOM   273  C  CD  . GLU A 1 35  ? 3.149   -31.675 -5.873  1.00 60.02  ? 35   GLU A CD  1 
ATOM   274  O  OE1 . GLU A 1 35  ? 3.170   -31.783 -4.625  1.00 58.77  ? 35   GLU A OE1 1 
ATOM   275  O  OE2 . GLU A 1 35  ? 3.142   -32.664 -6.650  1.00 60.64  ? 35   GLU A OE2 1 
ATOM   276  N  N   . LEU A 1 36  ? 0.671   -27.673 -7.063  1.00 33.57  ? 36   LEU A N   1 
ATOM   277  C  CA  . LEU A 1 36  ? -0.279  -27.837 -8.153  1.00 37.14  ? 36   LEU A CA  1 
ATOM   278  C  C   . LEU A 1 36  ? -0.706  -26.533 -8.827  1.00 38.83  ? 36   LEU A C   1 
ATOM   279  O  O   . LEU A 1 36  ? -1.148  -26.575 -9.983  1.00 39.96  ? 36   LEU A O   1 
ATOM   280  C  CB  . LEU A 1 36  ? -1.525  -28.589 -7.666  1.00 38.56  ? 36   LEU A CB  1 
ATOM   281  C  CG  . LEU A 1 36  ? -1.320  -30.015 -7.142  1.00 39.56  ? 36   LEU A CG  1 
ATOM   282  C  CD1 . LEU A 1 36  ? -2.672  -30.750 -7.081  1.00 39.80  ? 36   LEU A CD1 1 
ATOM   283  C  CD2 . LEU A 1 36  ? -0.304  -30.782 -8.000  1.00 43.07  ? 36   LEU A CD2 1 
ATOM   284  N  N   . GLY A 1 37  ? -0.618  -25.396 -8.153  1.00 40.40  ? 37   GLY A N   1 
ATOM   285  C  CA  . GLY A 1 37  ? -0.927  -24.110 -8.759  1.00 34.95  ? 37   GLY A CA  1 
ATOM   286  C  C   . GLY A 1 37  ? -2.237  -23.510 -8.273  1.00 40.72  ? 37   GLY A C   1 
ATOM   287  O  O   . GLY A 1 37  ? -2.762  -23.839 -7.198  1.00 37.14  ? 37   GLY A O   1 
ATOM   288  N  N   . GLU A 1 38  ? -2.778  -22.612 -9.102  1.00 36.12  ? 38   GLU A N   1 
ATOM   289  C  CA  . GLU A 1 38  ? -3.892  -21.754 -8.710  1.00 37.60  ? 38   GLU A CA  1 
ATOM   290  C  C   . GLU A 1 38  ? -5.202  -22.506 -8.491  1.00 37.27  ? 38   GLU A C   1 
ATOM   291  O  O   . GLU A 1 38  ? -6.119  -21.950 -7.884  1.00 35.35  ? 38   GLU A O   1 
ATOM   292  C  CB  . GLU A 1 38  ? -4.111  -20.671 -9.773  1.00 36.13  ? 38   GLU A CB  1 
ATOM   293  C  CG  . GLU A 1 38  ? -4.590  -21.249 -11.096 1.00 36.45  ? 38   GLU A CG  1 
ATOM   294  C  CD  . GLU A 1 38  ? -4.770  -20.196 -12.182 1.00 40.78  ? 38   GLU A CD  1 
ATOM   295  O  OE1 . GLU A 1 38  ? -4.880  -18.988 -11.855 1.00 35.68  ? 38   GLU A OE1 1 
ATOM   296  O  OE2 . GLU A 1 38  ? -4.788  -20.585 -13.366 1.00 42.15  ? 38   GLU A OE2 1 
ATOM   297  N  N   . ILE A 1 39  ? -5.344  -23.728 -8.995  1.00 34.96  ? 39   ILE A N   1 
ATOM   298  C  CA  . ILE A 1 39  ? -6.595  -24.457 -8.808  1.00 35.26  ? 39   ILE A CA  1 
ATOM   299  C  C   . ILE A 1 39  ? -6.298  -25.947 -8.741  1.00 39.22  ? 39   ILE A C   1 
ATOM   300  O  O   . ILE A 1 39  ? -5.524  -26.468 -9.554  1.00 38.13  ? 39   ILE A O   1 
ATOM   301  C  CB  . ILE A 1 39  ? -7.616  -24.147 -9.926  1.00 37.11  ? 39   ILE A CB  1 
ATOM   302  C  CG1 . ILE A 1 39  ? -8.942  -24.847 -9.645  1.00 37.98  ? 39   ILE A CG1 1 
ATOM   303  C  CG2 . ILE A 1 39  ? -7.088  -24.536 -11.302 1.00 39.38  ? 39   ILE A CG2 1 
ATOM   304  C  CD1 . ILE A 1 39  ? -10.083 -24.338 -10.503 1.00 38.05  ? 39   ILE A CD1 1 
ATOM   305  N  N   . PHE A 1 40  ? -6.927  -26.645 -7.784  1.00 35.10  ? 40   PHE A N   1 
ATOM   306  C  CA  . PHE A 1 40  ? -6.875  -28.100 -7.823  1.00 32.74  ? 40   PHE A CA  1 
ATOM   307  C  C   . PHE A 1 40  ? -8.158  -28.713 -7.275  1.00 36.68  ? 40   PHE A C   1 
ATOM   308  O  O   . PHE A 1 40  ? -8.832  -28.146 -6.406  1.00 33.14  ? 40   PHE A O   1 
ATOM   309  C  CB  . PHE A 1 40  ? -5.635  -28.654 -7.090  1.00 32.70  ? 40   PHE A CB  1 
ATOM   310  C  CG  . PHE A 1 40  ? -5.581  -28.341 -5.613  1.00 35.56  ? 40   PHE A CG  1 
ATOM   311  C  CD1 . PHE A 1 40  ? -6.176  -29.185 -4.685  1.00 34.09  ? 40   PHE A CD1 1 
ATOM   312  C  CD2 . PHE A 1 40  ? -4.869  -27.247 -5.153  1.00 35.59  ? 40   PHE A CD2 1 
ATOM   313  C  CE1 . PHE A 1 40  ? -6.100  -28.909 -3.323  1.00 35.26  ? 40   PHE A CE1 1 
ATOM   314  C  CE2 . PHE A 1 40  ? -4.786  -26.962 -3.796  1.00 37.54  ? 40   PHE A CE2 1 
ATOM   315  C  CZ  . PHE A 1 40  ? -5.404  -27.794 -2.879  1.00 36.55  ? 40   PHE A CZ  1 
ATOM   316  N  N   . LYS A 1 41  ? -8.514  -29.858 -7.852  1.00 34.75  ? 41   LYS A N   1 
ATOM   317  C  CA  . LYS A 1 41  ? -9.664  -30.634 -7.414  1.00 37.29  ? 41   LYS A CA  1 
ATOM   318  C  C   . LYS A 1 41  ? -9.323  -31.420 -6.151  1.00 36.57  ? 41   LYS A C   1 
ATOM   319  O  O   . LYS A 1 41  ? -8.205  -31.919 -6.004  1.00 36.06  ? 41   LYS A O   1 
ATOM   320  C  CB  . LYS A 1 41  ? -10.084 -31.583 -8.535  1.00 35.19  ? 41   LYS A CB  1 
ATOM   321  C  CG  . LYS A 1 41  ? -11.209 -32.531 -8.193  1.00 38.42  ? 41   LYS A CG  1 
ATOM   322  C  CD  . LYS A 1 41  ? -11.602 -33.301 -9.448  1.00 45.55  ? 41   LYS A CD  1 
ATOM   323  C  CE  . LYS A 1 41  ? -12.738 -34.273 -9.183  1.00 54.08  ? 41   LYS A CE  1 
ATOM   324  N  NZ  . LYS A 1 41  ? -13.793 -34.224 -10.235 1.00 58.38  ? 41   LYS A NZ  1 
ATOM   325  N  N   . PHE A 1 42  ? -10.290 -31.517 -5.231  1.00 34.87  ? 42   PHE A N   1 
ATOM   326  C  CA  . PHE A 1 42  ? -10.114 -32.257 -3.981  1.00 33.30  ? 42   PHE A CA  1 
ATOM   327  C  C   . PHE A 1 42  ? -11.392 -33.035 -3.732  1.00 41.65  ? 42   PHE A C   1 
ATOM   328  O  O   . PHE A 1 42  ? -12.465 -32.432 -3.605  1.00 36.85  ? 42   PHE A O   1 
ATOM   329  C  CB  . PHE A 1 42  ? -9.823  -31.303 -2.813  1.00 36.51  ? 42   PHE A CB  1 
ATOM   330  C  CG  . PHE A 1 42  ? -9.431  -31.991 -1.520  1.00 39.05  ? 42   PHE A CG  1 
ATOM   331  C  CD1 . PHE A 1 42  ? -10.388 -32.596 -0.718  1.00 42.21  ? 42   PHE A CD1 1 
ATOM   332  C  CD2 . PHE A 1 42  ? -8.115  -31.985 -1.090  1.00 37.19  ? 42   PHE A CD2 1 
ATOM   333  C  CE1 . PHE A 1 42  ? -10.039 -33.204 0.488   1.00 40.16  ? 42   PHE A CE1 1 
ATOM   334  C  CE2 . PHE A 1 42  ? -7.754  -32.601 0.122   1.00 40.08  ? 42   PHE A CE2 1 
ATOM   335  C  CZ  . PHE A 1 42  ? -8.724  -33.205 0.905   1.00 36.44  ? 42   PHE A CZ  1 
ATOM   336  N  N   . GLU A 1 43  ? -11.287 -34.363 -3.663  1.00 40.32  ? 43   GLU A N   1 
ATOM   337  C  CA  . GLU A 1 43  ? -12.453 -35.210 -3.481  1.00 37.56  ? 43   GLU A CA  1 
ATOM   338  C  C   . GLU A 1 43  ? -12.400 -35.949 -2.150  1.00 40.66  ? 43   GLU A C   1 
ATOM   339  O  O   . GLU A 1 43  ? -11.328 -36.280 -1.631  1.00 39.46  ? 43   GLU A O   1 
ATOM   340  C  CB  . GLU A 1 43  ? -12.624 -36.248 -4.599  1.00 40.68  ? 43   GLU A CB  1 
ATOM   341  C  CG  . GLU A 1 43  ? -12.700 -35.697 -5.997  1.00 47.13  ? 43   GLU A CG  1 
ATOM   342  C  CD  . GLU A 1 43  ? -12.773 -36.804 -7.032  1.00 51.04  ? 43   GLU A CD  1 
ATOM   343  O  OE1 . GLU A 1 43  ? -11.836 -37.633 -7.090  1.00 50.82  ? 43   GLU A OE1 1 
ATOM   344  O  OE2 . GLU A 1 43  ? -13.778 -36.856 -7.771  1.00 56.66  ? 43   GLU A OE2 1 
ATOM   345  N  N   . ALA A 1 44  ? -13.582 -36.200 -1.611  1.00 40.92  ? 44   ALA A N   1 
ATOM   346  C  CA  . ALA A 1 44  ? -13.772 -37.131 -0.514  1.00 40.60  ? 44   ALA A CA  1 
ATOM   347  C  C   . ALA A 1 44  ? -14.984 -37.979 -0.869  1.00 43.80  ? 44   ALA A C   1 
ATOM   348  O  O   . ALA A 1 44  ? -15.691 -37.664 -1.831  1.00 43.19  ? 44   ALA A O   1 
ATOM   349  C  CB  . ALA A 1 44  ? -13.974 -36.391 0.813   1.00 45.51  ? 44   ALA A CB  1 
ATOM   350  N  N   . PRO A 1 45  ? -15.260 -39.059 -0.149  1.00 45.24  ? 45   PRO A N   1 
ATOM   351  C  CA  . PRO A 1 45  ? -16.465 -39.837 -0.463  1.00 47.94  ? 45   PRO A CA  1 
ATOM   352  C  C   . PRO A 1 45  ? -17.705 -38.955 -0.520  1.00 48.11  ? 45   PRO A C   1 
ATOM   353  O  O   . PRO A 1 45  ? -18.022 -38.254 0.447   1.00 45.79  ? 45   PRO A O   1 
ATOM   354  C  CB  . PRO A 1 45  ? -16.526 -40.852 0.681   1.00 42.68  ? 45   PRO A CB  1 
ATOM   355  C  CG  . PRO A 1 45  ? -15.072 -41.046 1.056   1.00 44.18  ? 45   PRO A CG  1 
ATOM   356  C  CD  . PRO A 1 45  ? -14.463 -39.675 0.927   1.00 43.26  ? 45   PRO A CD  1 
ATOM   357  N  N   . GLY A 1 46  ? -18.383 -38.951 -1.666  1.00 51.44  ? 46   GLY A N   1 
ATOM   358  C  CA  . GLY A 1 46  ? -19.607 -38.182 -1.819  1.00 53.68  ? 46   GLY A CA  1 
ATOM   359  C  C   . GLY A 1 46  ? -19.448 -36.675 -1.792  1.00 55.92  ? 46   GLY A C   1 
ATOM   360  O  O   . GLY A 1 46  ? -20.391 -35.970 -1.411  1.00 59.66  ? 46   GLY A O   1 
ATOM   361  N  N   . ARG A 1 47  ? -18.288 -36.151 -2.186  1.00 50.78  ? 47   ARG A N   1 
ATOM   362  C  CA  . ARG A 1 47  ? -18.141 -34.702 -2.228  1.00 48.57  ? 47   ARG A CA  1 
ATOM   363  C  C   . ARG A 1 47  ? -16.929 -34.320 -3.068  1.00 48.11  ? 47   ARG A C   1 
ATOM   364  O  O   . ARG A 1 47  ? -15.864 -34.943 -2.960  1.00 41.91  ? 47   ARG A O   1 
ATOM   365  C  CB  . ARG A 1 47  ? -17.991 -34.093 -0.828  1.00 44.51  ? 47   ARG A CB  1 
ATOM   366  C  CG  . ARG A 1 47  ? -17.320 -32.726 -0.903  1.00 51.42  ? 47   ARG A CG  1 
ATOM   367  C  CD  . ARG A 1 47  ? -17.833 -31.721 0.125   1.00 45.33  ? 47   ARG A CD  1 
ATOM   368  N  NE  . ARG A 1 47  ? -17.041 -30.492 0.115   1.00 47.31  ? 47   ARG A NE  1 
ATOM   369  C  CZ  . ARG A 1 47  ? -16.509 -29.919 1.189   1.00 46.15  ? 47   ARG A CZ  1 
ATOM   370  N  NH1 . ARG A 1 47  ? -16.570 -30.493 2.381   1.00 47.34  ? 47   ARG A NH1 1 
ATOM   371  N  NH2 . ARG A 1 47  ? -15.887 -28.746 1.061   1.00 39.33  ? 47   ARG A NH2 1 
ATOM   372  N  N   . VAL A 1 48  ? -17.095 -33.262 -3.864  1.00 42.94  ? 48   VAL A N   1 
ATOM   373  C  CA  . VAL A 1 48  ? -16.032 -32.666 -4.662  1.00 41.66  ? 48   VAL A CA  1 
ATOM   374  C  C   . VAL A 1 48  ? -15.964 -31.175 -4.327  1.00 37.50  ? 48   VAL A C   1 
ATOM   375  O  O   . VAL A 1 48  ? -16.997 -30.513 -4.178  1.00 37.59  ? 48   VAL A O   1 
ATOM   376  C  CB  . VAL A 1 48  ? -16.278 -32.855 -6.177  1.00 40.56  ? 48   VAL A CB  1 
ATOM   377  C  CG1 . VAL A 1 48  ? -15.267 -32.064 -6.995  1.00 42.06  ? 48   VAL A CG1 1 
ATOM   378  C  CG2 . VAL A 1 48  ? -16.287 -34.335 -6.569  1.00 47.03  ? 48   VAL A CG2 1 
ATOM   379  N  N   . THR A 1 49  ? -14.753 -30.643 -4.214  1.00 34.56  ? 49   THR A N   1 
ATOM   380  C  CA  . THR A 1 49  ? -14.562 -29.199 -4.186  1.00 36.46  ? 49   THR A CA  1 
ATOM   381  C  C   . THR A 1 49  ? -13.302 -28.867 -4.978  1.00 39.31  ? 49   THR A C   1 
ATOM   382  O  O   . THR A 1 49  ? -12.577 -29.755 -5.442  1.00 37.70  ? 49   THR A O   1 
ATOM   383  C  CB  . THR A 1 49  ? -14.517 -28.655 -2.739  1.00 34.78  ? 49   THR A CB  1 
ATOM   384  O  OG1 . THR A 1 49  ? -14.618 -27.224 -2.751  1.00 35.75  ? 49   THR A OG1 1 
ATOM   385  C  CG2 . THR A 1 49  ? -13.237 -29.070 -2.018  1.00 35.05  ? 49   THR A CG2 1 
ATOM   386  N  N   . ARG A 1 50  ? -13.074 -27.570 -5.178  1.00 38.00  ? 50   ARG A N   1 
ATOM   387  C  CA  . ARG A 1 50  ? -11.927 -27.070 -5.922  1.00 36.57  ? 50   ARG A CA  1 
ATOM   388  C  C   . ARG A 1 50  ? -11.292 -25.945 -5.125  1.00 38.60  ? 50   ARG A C   1 
ATOM   389  O  O   . ARG A 1 50  ? -11.960 -24.953 -4.815  1.00 34.59  ? 50   ARG A O   1 
ATOM   390  C  CB  . ARG A 1 50  ? -12.346 -26.580 -7.311  1.00 41.78  ? 50   ARG A CB  1 
ATOM   391  C  CG  . ARG A 1 50  ? -13.091 -27.645 -8.106  1.00 38.75  ? 50   ARG A CG  1 
ATOM   392  C  CD  . ARG A 1 50  ? -14.330 -27.087 -8.785  1.00 36.94  ? 50   ARG A CD  1 
ATOM   393  N  NE  . ARG A 1 50  ? -15.102 -28.148 -9.420  1.00 40.31  ? 50   ARG A NE  1 
ATOM   394  C  CZ  . ARG A 1 50  ? -16.086 -28.827 -8.842  1.00 40.84  ? 50   ARG A CZ  1 
ATOM   395  N  NH1 . ARG A 1 50  ? -16.535 -28.510 -7.637  1.00 39.39  ? 50   ARG A NH1 1 
ATOM   396  N  NH2 . ARG A 1 50  ? -16.644 -29.847 -9.497  1.00 37.91  ? 50   ARG A NH2 1 
ATOM   397  N  N   . TYR A 1 51  ? -10.003 -26.084 -4.816  1.00 32.58  ? 51   TYR A N   1 
ATOM   398  C  CA  . TYR A 1 51  ? -9.277  -25.084 -4.042  1.00 32.83  ? 51   TYR A CA  1 
ATOM   399  C  C   . TYR A 1 51  ? -8.687  -24.029 -4.975  1.00 37.48  ? 51   TYR A C   1 
ATOM   400  O  O   . TYR A 1 51  ? -7.896  -24.351 -5.871  1.00 37.26  ? 51   TYR A O   1 
ATOM   401  C  CB  . TYR A 1 51  ? -8.184  -25.746 -3.200  1.00 34.56  ? 51   TYR A CB  1 
ATOM   402  C  CG  . TYR A 1 51  ? -8.733  -26.463 -1.987  1.00 34.04  ? 51   TYR A CG  1 
ATOM   403  C  CD1 . TYR A 1 51  ? -9.256  -27.750 -2.090  1.00 36.86  ? 51   TYR A CD1 1 
ATOM   404  C  CD2 . TYR A 1 51  ? -8.763  -25.838 -0.750  1.00 32.86  ? 51   TYR A CD2 1 
ATOM   405  C  CE1 . TYR A 1 51  ? -9.780  -28.403 -0.982  1.00 34.70  ? 51   TYR A CE1 1 
ATOM   406  C  CE2 . TYR A 1 51  ? -9.281  -26.467 0.364   1.00 34.65  ? 51   TYR A CE2 1 
ATOM   407  C  CZ  . TYR A 1 51  ? -9.778  -27.750 0.249   1.00 34.13  ? 51   TYR A CZ  1 
ATOM   408  O  OH  . TYR A 1 51  ? -10.301 -28.360 1.362   1.00 34.87  ? 51   TYR A OH  1 
ATOM   409  N  N   . LEU A 1 52  ? -9.055  -22.770 -4.749  1.00 33.36  ? 52   LEU A N   1 
ATOM   410  C  CA  . LEU A 1 52  ? -8.565  -21.642 -5.535  1.00 33.42  ? 52   LEU A CA  1 
ATOM   411  C  C   . LEU A 1 52  ? -7.511  -20.887 -4.743  1.00 34.25  ? 52   LEU A C   1 
ATOM   412  O  O   . LEU A 1 52  ? -7.699  -20.602 -3.555  1.00 35.14  ? 52   LEU A O   1 
ATOM   413  C  CB  . LEU A 1 52  ? -9.699  -20.682 -5.896  1.00 35.17  ? 52   LEU A CB  1 
ATOM   414  C  CG  . LEU A 1 52  ? -10.877 -21.251 -6.670  1.00 35.09  ? 52   LEU A CG  1 
ATOM   415  C  CD1 . LEU A 1 52  ? -11.833 -20.110 -7.052  1.00 38.42  ? 52   LEU A CD1 1 
ATOM   416  C  CD2 . LEU A 1 52  ? -10.378 -22.001 -7.916  1.00 35.60  ? 52   LEU A CD2 1 
ATOM   417  N  N   . SER A 1 53  ? -6.412  -20.539 -5.417  1.00 33.07  ? 53   SER A N   1 
ATOM   418  C  CA  . SER A 1 53  ? -5.304  -19.837 -4.785  1.00 35.41  ? 53   SER A CA  1 
ATOM   419  C  C   . SER A 1 53  ? -4.879  -18.552 -5.486  1.00 32.98  ? 53   SER A C   1 
ATOM   420  O  O   . SER A 1 53  ? -4.028  -17.845 -4.944  1.00 34.85  ? 53   SER A O   1 
ATOM   421  C  CB  . SER A 1 53  ? -4.066  -20.756 -4.699  1.00 37.33  ? 53   SER A CB  1 
ATOM   422  O  OG  . SER A 1 53  ? -4.257  -21.775 -3.738  1.00 43.70  ? 53   SER A OG  1 
ATOM   423  N  N   . SER A 1 54  ? -5.375  -18.253 -6.688  1.00 34.66  ? 54   SER A N   1 
ATOM   424  C  CA  . SER A 1 54  ? -4.892  -17.085 -7.413  1.00 35.15  ? 54   SER A CA  1 
ATOM   425  C  C   . SER A 1 54  ? -5.938  -15.979 -7.395  1.00 32.95  ? 54   SER A C   1 
ATOM   426  O  O   . SER A 1 54  ? -7.145  -16.236 -7.409  1.00 32.30  ? 54   SER A O   1 
ATOM   427  C  CB  . SER A 1 54  ? -4.537  -17.419 -8.873  1.00 33.31  ? 54   SER A CB  1 
ATOM   428  O  OG  . SER A 1 54  ? -5.700  -17.796 -9.595  1.00 34.42  ? 54   SER A OG  1 
ATOM   429  N  N   . GLN A 1 55  ? -5.462  -14.738 -7.413  1.00 33.89  ? 55   GLN A N   1 
ATOM   430  C  CA  . GLN A 1 55  ? -6.401  -13.629 -7.538  1.00 33.47  ? 55   GLN A CA  1 
ATOM   431  C  C   . GLN A 1 55  ? -7.126  -13.675 -8.878  1.00 35.67  ? 55   GLN A C   1 
ATOM   432  O  O   . GLN A 1 55  ? -8.290  -13.260 -8.972  1.00 34.20  ? 55   GLN A O   1 
ATOM   433  C  CB  . GLN A 1 55  ? -5.670  -12.302 -7.342  1.00 35.84  ? 55   GLN A CB  1 
ATOM   434  C  CG  . GLN A 1 55  ? -6.564  -11.076 -7.423  1.00 32.04  ? 55   GLN A CG  1 
ATOM   435  C  CD  . GLN A 1 55  ? -6.671  -10.511 -8.846  1.00 36.28  ? 55   GLN A CD  1 
ATOM   436  O  OE1 . GLN A 1 55  ? -6.046  -11.008 -9.770  1.00 37.32  ? 55   GLN A OE1 1 
ATOM   437  N  NE2 . GLN A 1 55  ? -7.458  -9.457  -9.011  1.00 35.45  ? 55   GLN A NE2 1 
ATOM   438  N  N   . ARG A 1 56  ? -6.469  -14.209 -9.913  1.00 34.91  ? 56   ARG A N   1 
ATOM   439  C  CA  . ARG A 1 56  ? -7.099  -14.324 -11.225 1.00 36.56  ? 56   ARG A CA  1 
ATOM   440  C  C   . ARG A 1 56  ? -8.440  -15.037 -11.136 1.00 36.62  ? 56   ARG A C   1 
ATOM   441  O  O   . ARG A 1 56  ? -9.439  -14.583 -11.708 1.00 35.09  ? 56   ARG A O   1 
ATOM   442  C  CB  . ARG A 1 56  ? -6.153  -15.054 -12.190 1.00 35.60  ? 56   ARG A CB  1 
ATOM   443  C  CG  . ARG A 1 56  ? -6.677  -15.228 -13.602 1.00 45.65  ? 56   ARG A CG  1 
ATOM   444  C  CD  . ARG A 1 56  ? -5.686  -16.043 -14.455 1.00 44.96  ? 56   ARG A CD  1 
ATOM   445  N  NE  . ARG A 1 56  ? -5.934  -17.482 -14.396 1.00 46.40  ? 56   ARG A NE  1 
ATOM   446  C  CZ  . ARG A 1 56  ? -6.763  -18.139 -15.199 1.00 47.99  ? 56   ARG A CZ  1 
ATOM   447  N  NH1 . ARG A 1 56  ? -7.481  -17.511 -16.119 1.00 47.09  ? 56   ARG A NH1 1 
ATOM   448  N  NH2 . ARG A 1 56  ? -6.864  -19.462 -15.088 1.00 47.19  ? 56   ARG A NH2 1 
ATOM   449  N  N   . LEU A 1 57  ? -8.477  -16.173 -10.444 1.00 34.90  ? 57   LEU A N   1 
ATOM   450  C  CA  . LEU A 1 57  ? -9.708  -16.950 -10.350 1.00 34.60  ? 57   LEU A CA  1 
ATOM   451  C  C   . LEU A 1 57  ? -10.600 -16.494 -9.200  1.00 32.18  ? 57   LEU A C   1 
ATOM   452  O  O   . LEU A 1 57  ? -11.833 -16.504 -9.328  1.00 33.02  ? 57   LEU A O   1 
ATOM   453  C  CB  . LEU A 1 57  ? -9.380  -18.439 -10.197 1.00 36.10  ? 57   LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 57  ? -8.721  -19.091 -11.427 1.00 34.69  ? 57   LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 57  ? -8.393  -20.558 -11.155 1.00 39.39  ? 57   LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 57  ? -9.593  -18.960 -12.683 1.00 35.78  ? 57   LEU A CD2 1 
ATOM   457  N  N   . ILE A 1 58  ? -10.009 -16.060 -8.093  1.00 31.54  ? 58   ILE A N   1 
ATOM   458  C  CA  . ILE A 1 58  ? -10.823 -15.710 -6.938  1.00 31.99  ? 58   ILE A CA  1 
ATOM   459  C  C   . ILE A 1 58  ? -11.639 -14.436 -7.198  1.00 35.24  ? 58   ILE A C   1 
ATOM   460  O  O   . ILE A 1 58  ? -12.749 -14.286 -6.670  1.00 33.36  ? 58   ILE A O   1 
ATOM   461  C  CB  . ILE A 1 58  ? -9.901  -15.633 -5.703  1.00 31.52  ? 58   ILE A CB  1 
ATOM   462  C  CG1 . ILE A 1 58  ? -9.555  -17.068 -5.252  1.00 32.19  ? 58   ILE A CG1 1 
ATOM   463  C  CG2 . ILE A 1 58  ? -10.539 -14.841 -4.580  1.00 35.19  ? 58   ILE A CG2 1 
ATOM   464  C  CD1 . ILE A 1 58  ? -8.326  -17.161 -4.333  1.00 30.97  ? 58   ILE A CD1 1 
ATOM   465  N  N   . LYS A 1 59  ? -11.147 -13.521 -8.040  1.00 33.44  ? 59   LYS A N   1 
ATOM   466  C  CA  . LYS A 1 59  ? -11.947 -12.342 -8.358  1.00 35.69  ? 59   LYS A CA  1 
ATOM   467  C  C   . LYS A 1 59  ? -13.235 -12.724 -9.077  1.00 37.23  ? 59   LYS A C   1 
ATOM   468  O  O   . LYS A 1 59  ? -14.259 -12.052 -8.905  1.00 37.91  ? 59   LYS A O   1 
ATOM   469  C  CB  . LYS A 1 59  ? -11.127 -11.325 -9.167  1.00 32.45  ? 59   LYS A CB  1 
ATOM   470  C  CG  . LYS A 1 59  ? -10.835 -11.707 -10.617 1.00 31.96  ? 59   LYS A CG  1 
ATOM   471  C  CD  . LYS A 1 59  ? -9.819  -10.773 -11.286 1.00 34.05  ? 59   LYS A CD  1 
ATOM   472  C  CE  . LYS A 1 59  ? -9.449  -11.269 -12.691 1.00 37.35  ? 59   LYS A CE  1 
ATOM   473  N  NZ  . LYS A 1 59  ? -8.396  -10.398 -13.335 1.00 41.24  ? 59   LYS A NZ  1 
ATOM   474  N  N   . GLU A 1 60  ? -13.224 -13.811 -9.856  1.00 33.51  ? 60   GLU A N   1 
ATOM   475  C  CA  . GLU A 1 60  ? -14.478 -14.279 -10.444 1.00 35.25  ? 60   GLU A CA  1 
ATOM   476  C  C   . GLU A 1 60  ? -15.339 -14.998 -9.414  1.00 35.00  ? 60   GLU A C   1 
ATOM   477  O  O   . GLU A 1 60  ? -16.570 -14.868 -9.429  1.00 35.06  ? 60   GLU A O   1 
ATOM   478  C  CB  . GLU A 1 60  ? -14.201 -15.197 -11.639 1.00 33.65  ? 60   GLU A CB  1 
ATOM   479  C  CG  . GLU A 1 60  ? -13.467 -14.499 -12.764 1.00 37.56  ? 60   GLU A CG  1 
ATOM   480  C  CD  . GLU A 1 60  ? -13.384 -15.340 -14.026 1.00 41.83  ? 60   GLU A CD  1 
ATOM   481  O  OE1 . GLU A 1 60  ? -14.285 -16.162 -14.254 1.00 40.48  ? 60   GLU A OE1 1 
ATOM   482  O  OE2 . GLU A 1 60  ? -12.414 -15.169 -14.796 1.00 46.31  ? 60   GLU A OE2 1 
ATOM   483  N  N   . ALA A 1 61  ? -14.710 -15.750 -8.500  1.00 33.69  ? 61   ALA A N   1 
ATOM   484  C  CA  . ALA A 1 61  ? -15.466 -16.431 -7.460  1.00 34.05  ? 61   ALA A CA  1 
ATOM   485  C  C   . ALA A 1 61  ? -16.188 -15.441 -6.556  1.00 34.23  ? 61   ALA A C   1 
ATOM   486  O  O   . ALA A 1 61  ? -17.229 -15.778 -5.979  1.00 34.05  ? 61   ALA A O   1 
ATOM   487  C  CB  . ALA A 1 61  ? -14.539 -17.322 -6.625  1.00 32.65  ? 61   ALA A CB  1 
ATOM   488  N  N   . CYS A 1 62  ? -15.662 -14.220 -6.425  1.00 31.80  ? 62   CYS A N   1 
ATOM   489  C  CA  . CYS A 1 62  ? -16.293 -13.209 -5.581  1.00 32.05  ? 62   CYS A CA  1 
ATOM   490  C  C   . CYS A 1 62  ? -17.436 -12.467 -6.262  1.00 36.69  ? 62   CYS A C   1 
ATOM   491  O  O   . CYS A 1 62  ? -17.996 -11.553 -5.654  1.00 31.94  ? 62   CYS A O   1 
ATOM   492  C  CB  . CYS A 1 62  ? -15.227 -12.229 -5.090  1.00 32.23  ? 62   CYS A CB  1 
ATOM   493  S  SG  . CYS A 1 62  ? -14.123 -13.015 -3.893  1.00 33.48  ? 62   CYS A SG  1 
ATOM   494  N  N   . ASP A 1 63  ? -17.799 -12.836 -7.490  1.00 35.29  ? 63   ASP A N   1 
ATOM   495  C  CA  . ASP A 1 63  ? -18.982 -12.294 -8.161  1.00 34.75  ? 63   ASP A CA  1 
ATOM   496  C  C   . ASP A 1 63  ? -20.237 -12.904 -7.543  1.00 31.56  ? 63   ASP A C   1 
ATOM   497  O  O   . ASP A 1 63  ? -20.555 -14.073 -7.789  1.00 34.60  ? 63   ASP A O   1 
ATOM   498  C  CB  . ASP A 1 63  ? -18.893 -12.590 -9.656  1.00 35.81  ? 63   ASP A CB  1 
ATOM   499  C  CG  . ASP A 1 63  ? -20.085 -12.058 -10.451 1.00 37.91  ? 63   ASP A CG  1 
ATOM   500  O  OD1 . ASP A 1 63  ? -21.120 -11.672 -9.854  1.00 35.99  ? 63   ASP A OD1 1 
ATOM   501  O  OD2 . ASP A 1 63  ? -19.982 -12.055 -11.698 1.00 40.61  ? 63   ASP A OD2 1 
ATOM   502  N  N   . GLU A 1 64  ? -20.957 -12.114 -6.739  1.00 31.94  ? 64   GLU A N   1 
ATOM   503  C  CA  . GLU A 1 64  ? -22.119 -12.636 -6.020  1.00 32.78  ? 64   GLU A CA  1 
ATOM   504  C  C   . GLU A 1 64  ? -23.270 -13.005 -6.943  1.00 37.32  ? 64   GLU A C   1 
ATOM   505  O  O   . GLU A 1 64  ? -24.194 -13.706 -6.513  1.00 35.54  ? 64   GLU A O   1 
ATOM   506  C  CB  . GLU A 1 64  ? -22.624 -11.622 -4.991  1.00 33.36  ? 64   GLU A CB  1 
ATOM   507  C  CG  . GLU A 1 64  ? -21.603 -11.199 -3.958  1.00 33.78  ? 64   GLU A CG  1 
ATOM   508  C  CD  . GLU A 1 64  ? -22.196 -10.284 -2.910  1.00 37.30  ? 64   GLU A CD  1 
ATOM   509  O  OE1 . GLU A 1 64  ? -22.739 -10.805 -1.924  1.00 33.94  ? 64   GLU A OE1 1 
ATOM   510  O  OE2 . GLU A 1 64  ? -22.123 -9.044  -3.070  1.00 41.39  ? 64   GLU A OE2 1 
ATOM   511  N  N   . SER A 1 65  ? -23.276 -12.515 -8.180  1.00 35.58  ? 65   SER A N   1 
ATOM   512  C  CA  . SER A 1 65  ? -24.304 -12.975 -9.099  1.00 35.13  ? 65   SER A CA  1 
ATOM   513  C  C   . SER A 1 65  ? -24.035 -14.388 -9.588  1.00 36.79  ? 65   SER A C   1 
ATOM   514  O  O   . SER A 1 65  ? -24.948 -15.034 -10.106 1.00 37.84  ? 65   SER A O   1 
ATOM   515  C  CB  . SER A 1 65  ? -24.415 -12.014 -10.291 1.00 38.32  ? 65   SER A CB  1 
ATOM   516  O  OG  . SER A 1 65  ? -23.340 -12.212 -11.193 1.00 36.07  ? 65   SER A OG  1 
ATOM   517  N  N   . ARG A 1 66  ? -22.801 -14.874 -9.463  1.00 33.54  ? 66   ARG A N   1 
ATOM   518  C  CA  . ARG A 1 66  ? -22.447 -16.208 -9.933  1.00 36.08  ? 66   ARG A CA  1 
ATOM   519  C  C   . ARG A 1 66  ? -22.233 -17.213 -8.810  1.00 37.90  ? 66   ARG A C   1 
ATOM   520  O  O   . ARG A 1 66  ? -22.441 -18.411 -9.027  1.00 34.86  ? 66   ARG A O   1 
ATOM   521  C  CB  . ARG A 1 66  ? -21.177 -16.155 -10.802 1.00 35.78  ? 66   ARG A CB  1 
ATOM   522  C  CG  . ARG A 1 66  ? -21.318 -15.357 -12.099 1.00 40.29  ? 66   ARG A CG  1 
ATOM   523  C  CD  . ARG A 1 66  ? -19.950 -14.948 -12.667 1.00 40.74  ? 66   ARG A CD  1 
ATOM   524  N  NE  . ARG A 1 66  ? -19.208 -16.090 -13.179 1.00 41.27  ? 66   ARG A NE  1 
ATOM   525  C  CZ  . ARG A 1 66  ? -17.927 -16.069 -13.524 1.00 42.34  ? 66   ARG A CZ  1 
ATOM   526  N  NH1 . ARG A 1 66  ? -17.190 -14.977 -13.389 1.00 40.80  ? 66   ARG A NH1 1 
ATOM   527  N  NH2 . ARG A 1 66  ? -17.367 -17.175 -14.015 1.00 46.38  ? 66   ARG A NH2 1 
ATOM   528  N  N   . PHE A 1 67  ? -21.835 -16.755 -7.624  1.00 34.95  ? 67   PHE A N   1 
ATOM   529  C  CA  . PHE A 1 67  ? -21.472 -17.636 -6.526  1.00 32.04  ? 67   PHE A CA  1 
ATOM   530  C  C   . PHE A 1 67  ? -22.034 -17.098 -5.217  1.00 30.62  ? 67   PHE A C   1 
ATOM   531  O  O   . PHE A 1 67  ? -21.976 -15.897 -4.946  1.00 32.42  ? 67   PHE A O   1 
ATOM   532  C  CB  . PHE A 1 67  ? -19.945 -17.782 -6.401  1.00 31.78  ? 67   PHE A CB  1 
ATOM   533  C  CG  . PHE A 1 67  ? -19.292 -18.338 -7.628  1.00 34.66  ? 67   PHE A CG  1 
ATOM   534  C  CD1 . PHE A 1 67  ? -19.206 -19.713 -7.821  1.00 36.62  ? 67   PHE A CD1 1 
ATOM   535  C  CD2 . PHE A 1 67  ? -18.761 -17.491 -8.589  1.00 35.21  ? 67   PHE A CD2 1 
ATOM   536  C  CE1 . PHE A 1 67  ? -18.605 -20.233 -8.966  1.00 37.18  ? 67   PHE A CE1 1 
ATOM   537  C  CE2 . PHE A 1 67  ? -18.161 -17.998 -9.734  1.00 39.90  ? 67   PHE A CE2 1 
ATOM   538  C  CZ  . PHE A 1 67  ? -18.081 -19.374 -9.924  1.00 38.29  ? 67   PHE A CZ  1 
ATOM   539  N  N   . ASP A 1 68  ? -22.538 -18.005 -4.398  1.00 31.98  ? 68   ASP A N   1 
ATOM   540  C  CA  . ASP A 1 68  ? -23.081 -17.700 -3.085  1.00 32.76  ? 68   ASP A CA  1 
ATOM   541  C  C   . ASP A 1 68  ? -22.245 -18.438 -2.049  1.00 33.24  ? 68   ASP A C   1 
ATOM   542  O  O   . ASP A 1 68  ? -21.520 -19.384 -2.377  1.00 32.96  ? 68   ASP A O   1 
ATOM   543  C  CB  . ASP A 1 68  ? -24.548 -18.140 -3.014  1.00 31.97  ? 68   ASP A CB  1 
ATOM   544  C  CG  . ASP A 1 68  ? -25.228 -17.805 -1.689  1.00 34.32  ? 68   ASP A CG  1 
ATOM   545  O  OD1 . ASP A 1 68  ? -24.835 -16.846 -0.990  1.00 32.74  ? 68   ASP A OD1 1 
ATOM   546  O  OD2 . ASP A 1 68  ? -26.205 -18.506 -1.376  1.00 32.42  ? 68   ASP A OD2 1 
ATOM   547  N  N   . LYS A 1 69  ? -22.364 -18.017 -0.788  1.00 31.98  ? 69   LYS A N   1 
ATOM   548  C  CA  . LYS A 1 69  ? -21.657 -18.708 0.283   1.00 32.60  ? 69   LYS A CA  1 
ATOM   549  C  C   . LYS A 1 69  ? -22.117 -20.160 0.411   1.00 31.56  ? 69   LYS A C   1 
ATOM   550  O  O   . LYS A 1 69  ? -23.315 -20.446 0.446   1.00 32.59  ? 69   LYS A O   1 
ATOM   551  C  CB  . LYS A 1 69  ? -21.869 -17.989 1.617   1.00 32.32  ? 69   LYS A CB  1 
ATOM   552  C  CG  . LYS A 1 69  ? -21.527 -18.867 2.828   1.00 29.11  ? 69   LYS A CG  1 
ATOM   553  C  CD  . LYS A 1 69  ? -21.210 -18.036 4.079   1.00 30.65  ? 69   LYS A CD  1 
ATOM   554  C  CE  . LYS A 1 69  ? -21.016 -18.950 5.280   1.00 30.91  ? 69   LYS A CE  1 
ATOM   555  N  NZ  . LYS A 1 69  ? -20.311 -18.312 6.438   1.00 29.21  ? 69   LYS A NZ  1 
ATOM   556  N  N   . ASN A 1 70  ? -21.155 -21.069 0.539   1.00 28.52  ? 70   ASN A N   1 
ATOM   557  C  CA  . ASN A 1 70  ? -21.403 -22.475 0.810   1.00 31.73  ? 70   ASN A CA  1 
ATOM   558  C  C   . ASN A 1 70  ? -20.979 -22.817 2.236   1.00 31.75  ? 70   ASN A C   1 
ATOM   559  O  O   . ASN A 1 70  ? -20.067 -22.197 2.791   1.00 32.79  ? 70   ASN A O   1 
ATOM   560  C  CB  . ASN A 1 70  ? -20.645 -23.346 -0.202  1.00 30.08  ? 70   ASN A CB  1 
ATOM   561  C  CG  . ASN A 1 70  ? -20.842 -24.818 0.040   1.00 34.64  ? 70   ASN A CG  1 
ATOM   562  O  OD1 . ASN A 1 70  ? -21.971 -25.294 0.052   1.00 33.42  ? 70   ASN A OD1 1 
ATOM   563  N  ND2 . ASN A 1 70  ? -19.743 -25.547 0.246   1.00 35.67  ? 70   ASN A ND2 1 
ATOM   564  N  N   . LEU A 1 71  ? -21.674 -23.774 2.859   1.00 31.25  ? 71   LEU A N   1 
ATOM   565  C  CA  . LEU A 1 71  ? -21.215 -24.302 4.146   1.00 29.99  ? 71   LEU A CA  1 
ATOM   566  C  C   . LEU A 1 71  ? -20.203 -25.400 3.868   1.00 32.38  ? 71   LEU A C   1 
ATOM   567  O  O   . LEU A 1 71  ? -20.550 -26.464 3.346   1.00 35.02  ? 71   LEU A O   1 
ATOM   568  C  CB  . LEU A 1 71  ? -22.362 -24.821 5.011   1.00 31.45  ? 71   LEU A CB  1 
ATOM   569  C  CG  . LEU A 1 71  ? -23.466 -23.829 5.402   1.00 28.87  ? 71   LEU A CG  1 
ATOM   570  C  CD1 . LEU A 1 71  ? -24.392 -24.423 6.446   1.00 31.58  ? 71   LEU A CD1 1 
ATOM   571  C  CD2 . LEU A 1 71  ? -22.893 -22.488 5.914   1.00 31.00  ? 71   LEU A CD2 1 
ATOM   572  N  N   . SER A 1 72  ? -18.942 -25.108 4.162   1.00 30.97  ? 72   SER A N   1 
ATOM   573  C  CA  . SER A 1 72  ? -17.906 -26.121 4.157   1.00 33.55  ? 72   SER A CA  1 
ATOM   574  C  C   . SER A 1 72  ? -18.250 -27.208 5.170   1.00 34.65  ? 72   SER A C   1 
ATOM   575  O  O   . SER A 1 72  ? -19.086 -27.022 6.068   1.00 34.35  ? 72   SER A O   1 
ATOM   576  C  CB  . SER A 1 72  ? -16.557 -25.491 4.508   1.00 31.94  ? 72   SER A CB  1 
ATOM   577  O  OG  . SER A 1 72  ? -16.643 -24.854 5.772   1.00 33.51  ? 72   SER A OG  1 
ATOM   578  N  N   . GLN A 1 73  ? -17.605 -28.364 5.026   1.00 35.89  ? 73   GLN A N   1 
ATOM   579  C  CA  . GLN A 1 73  ? -17.811 -29.398 6.034   1.00 36.99  ? 73   GLN A CA  1 
ATOM   580  C  C   . GLN A 1 73  ? -17.503 -28.853 7.425   1.00 35.68  ? 73   GLN A C   1 
ATOM   581  O  O   . GLN A 1 73  ? -18.218 -29.138 8.395   1.00 35.14  ? 73   GLN A O   1 
ATOM   582  C  CB  . GLN A 1 73  ? -16.945 -30.623 5.737   1.00 37.32  ? 73   GLN A CB  1 
ATOM   583  C  CG  . GLN A 1 73  ? -17.398 -31.847 6.515   1.00 43.82  ? 73   GLN A CG  1 
ATOM   584  C  CD  . GLN A 1 73  ? -18.861 -32.151 6.260   1.00 44.27  ? 73   GLN A CD  1 
ATOM   585  O  OE1 . GLN A 1 73  ? -19.267 -32.339 5.112   1.00 43.97  ? 73   GLN A OE1 1 
ATOM   586  N  NE2 . GLN A 1 73  ? -19.666 -32.179 7.322   1.00 47.21  ? 73   GLN A NE2 1 
ATOM   587  N  N   . ALA A 1 74  ? -16.436 -28.063 7.537   1.00 34.72  ? 74   ALA A N   1 
ATOM   588  C  CA  . ALA A 1 74  ? -16.090 -27.461 8.818   1.00 33.67  ? 74   ALA A CA  1 
ATOM   589  C  C   . ALA A 1 74  ? -17.260 -26.658 9.387   1.00 34.03  ? 74   ALA A C   1 
ATOM   590  O  O   . ALA A 1 74  ? -17.642 -26.835 10.551  1.00 35.67  ? 74   ALA A O   1 
ATOM   591  C  CB  . ALA A 1 74  ? -14.857 -26.576 8.650   1.00 35.05  ? 74   ALA A CB  1 
ATOM   592  N  N   . LEU A 1 75  ? -17.842 -25.764 8.575   1.00 36.14  ? 75   LEU A N   1 
ATOM   593  C  CA  . LEU A 1 75  ? -18.978 -24.973 9.049   1.00 31.08  ? 75   LEU A CA  1 
ATOM   594  C  C   . LEU A 1 75  ? -20.191 -25.841 9.335   1.00 31.87  ? 75   LEU A C   1 
ATOM   595  O  O   . LEU A 1 75  ? -20.961 -25.533 10.256  1.00 34.90  ? 75   LEU A O   1 
ATOM   596  C  CB  . LEU A 1 75  ? -19.346 -23.876 8.034   1.00 33.01  ? 75   LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 75  ? -18.359 -22.692 7.892   1.00 31.82  ? 75   LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 75  ? -18.891 -21.606 6.929   1.00 30.92  ? 75   LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 75  ? -18.016 -22.067 9.244   1.00 33.44  ? 75   LEU A CD2 1 
ATOM   600  N  N   . LYS A 1 76  ? -20.399 -26.914 8.561   1.00 33.32  ? 76   LYS A N   1 
ATOM   601  C  CA  . LYS A 1 76  ? -21.498 -27.828 8.874   1.00 34.88  ? 76   LYS A CA  1 
ATOM   602  C  C   . LYS A 1 76  ? -21.317 -28.468 10.245  1.00 35.39  ? 76   LYS A C   1 
ATOM   603  O  O   . LYS A 1 76  ? -22.293 -28.666 10.980  1.00 35.80  ? 76   LYS A O   1 
ATOM   604  C  CB  . LYS A 1 76  ? -21.607 -28.897 7.798   1.00 33.69  ? 76   LYS A CB  1 
ATOM   605  C  CG  . LYS A 1 76  ? -22.225 -28.355 6.531   1.00 33.66  ? 76   LYS A CG  1 
ATOM   606  C  CD  . LYS A 1 76  ? -22.397 -29.439 5.501   1.00 40.37  ? 76   LYS A CD  1 
ATOM   607  C  CE  . LYS A 1 76  ? -22.903 -28.851 4.199   1.00 45.17  ? 76   LYS A CE  1 
ATOM   608  N  NZ  . LYS A 1 76  ? -22.882 -29.869 3.123   1.00 53.05  ? 76   LYS A NZ  1 
ATOM   609  N  N   . PHE A 1 77  ? -20.080 -28.812 10.603  1.00 33.56  ? 77   PHE A N   1 
ATOM   610  C  CA  . PHE A 1 77  ? -19.846 -29.394 11.919  1.00 37.65  ? 77   PHE A CA  1 
ATOM   611  C  C   . PHE A 1 77  ? -20.001 -28.340 13.008  1.00 37.40  ? 77   PHE A C   1 
ATOM   612  O  O   . PHE A 1 77  ? -20.594 -28.607 14.060  1.00 38.46  ? 77   PHE A O   1 
ATOM   613  C  CB  . PHE A 1 77  ? -18.461 -30.043 11.962  1.00 41.62  ? 77   PHE A CB  1 
ATOM   614  C  CG  . PHE A 1 77  ? -18.362 -31.321 11.163  1.00 45.17  ? 77   PHE A CG  1 
ATOM   615  C  CD1 . PHE A 1 77  ? -19.483 -32.101 10.947  1.00 45.61  ? 77   PHE A CD1 1 
ATOM   616  C  CD2 . PHE A 1 77  ? -17.144 -31.748 10.645  1.00 44.42  ? 77   PHE A CD2 1 
ATOM   617  C  CE1 . PHE A 1 77  ? -19.400 -33.278 10.215  1.00 51.21  ? 77   PHE A CE1 1 
ATOM   618  C  CE2 . PHE A 1 77  ? -17.055 -32.926 9.909   1.00 49.06  ? 77   PHE A CE2 1 
ATOM   619  C  CZ  . PHE A 1 77  ? -18.184 -33.689 9.699   1.00 46.50  ? 77   PHE A CZ  1 
ATOM   620  N  N   . VAL A 1 78  ? -19.502 -27.126 12.763  1.00 34.21  ? 78   VAL A N   1 
ATOM   621  C  CA  . VAL A 1 78  ? -19.699 -26.051 13.731  1.00 33.74  ? 78   VAL A CA  1 
ATOM   622  C  C   . VAL A 1 78  ? -21.179 -25.739 13.870  1.00 32.88  ? 78   VAL A C   1 
ATOM   623  O  O   . VAL A 1 78  ? -21.638 -25.305 14.940  1.00 35.99  ? 78   VAL A O   1 
ATOM   624  C  CB  . VAL A 1 78  ? -18.893 -24.806 13.322  1.00 34.71  ? 78   VAL A CB  1 
ATOM   625  C  CG1 . VAL A 1 78  ? -19.302 -23.594 14.180  1.00 39.85  ? 78   VAL A CG1 1 
ATOM   626  C  CG2 . VAL A 1 78  ? -17.388 -25.106 13.435  1.00 35.16  ? 78   VAL A CG2 1 
ATOM   627  N  N   . ARG A 1 79  ? -21.955 -25.962 12.805  1.00 32.63  ? 79   ARG A N   1 
ATOM   628  C  CA  . ARG A 1 79  ? -23.389 -25.721 12.901  1.00 32.08  ? 79   ARG A CA  1 
ATOM   629  C  C   . ARG A 1 79  ? -24.045 -26.590 13.968  1.00 36.09  ? 79   ARG A C   1 
ATOM   630  O  O   . ARG A 1 79  ? -25.124 -26.241 14.456  1.00 34.69  ? 79   ARG A O   1 
ATOM   631  C  CB  . ARG A 1 79  ? -24.063 -25.955 11.549  1.00 37.11  ? 79   ARG A CB  1 
ATOM   632  C  CG  . ARG A 1 79  ? -25.577 -25.757 11.586  1.00 37.35  ? 79   ARG A CG  1 
ATOM   633  C  CD  . ARG A 1 79  ? -26.137 -25.408 10.200  1.00 33.32  ? 79   ARG A CD  1 
ATOM   634  N  NE  . ARG A 1 79  ? -27.601 -25.342 10.192  1.00 40.43  ? 79   ARG A NE  1 
ATOM   635  C  CZ  . ARG A 1 79  ? -28.325 -24.484 9.482   1.00 42.53  ? 79   ARG A CZ  1 
ATOM   636  N  NH1 . ARG A 1 79  ? -27.755 -23.558 8.723   1.00 34.47  ? 79   ARG A NH1 1 
ATOM   637  N  NH2 . ARG A 1 79  ? -29.655 -24.541 9.555   1.00 40.42  ? 79   ARG A NH2 1 
ATOM   638  N  N   . ASP A 1 80  ? -23.418 -27.699 14.356  1.00 36.31  ? 80   ASP A N   1 
ATOM   639  C  CA  . ASP A 1 80  ? -23.995 -28.518 15.415  1.00 38.42  ? 80   ASP A CA  1 
ATOM   640  C  C   . ASP A 1 80  ? -24.126 -27.768 16.733  1.00 38.54  ? 80   ASP A C   1 
ATOM   641  O  O   . ASP A 1 80  ? -24.982 -28.128 17.549  1.00 41.01  ? 80   ASP A O   1 
ATOM   642  C  CB  . ASP A 1 80  ? -23.176 -29.790 15.607  1.00 38.97  ? 80   ASP A CB  1 
ATOM   643  C  CG  . ASP A 1 80  ? -23.445 -30.801 14.510  1.00 44.80  ? 80   ASP A CG  1 
ATOM   644  O  OD1 . ASP A 1 80  ? -24.530 -30.731 13.905  1.00 45.74  ? 80   ASP A OD1 1 
ATOM   645  O  OD2 . ASP A 1 80  ? -22.571 -31.645 14.245  1.00 52.83  ? 80   ASP A OD2 1 
ATOM   646  N  N   . PHE A 1 81  ? -23.321 -26.732 16.977  1.00 36.93  ? 81   PHE A N   1 
ATOM   647  C  CA  . PHE A 1 81  ? -23.588 -25.895 18.137  1.00 39.10  ? 81   PHE A CA  1 
ATOM   648  C  C   . PHE A 1 81  ? -23.888 -24.438 17.811  1.00 36.26  ? 81   PHE A C   1 
ATOM   649  O  O   . PHE A 1 81  ? -24.431 -23.742 18.673  1.00 35.84  ? 81   PHE A O   1 
ATOM   650  C  CB  . PHE A 1 81  ? -22.431 -25.971 19.154  1.00 41.75  ? 81   PHE A CB  1 
ATOM   651  C  CG  . PHE A 1 81  ? -21.060 -25.823 18.553  1.00 40.81  ? 81   PHE A CG  1 
ATOM   652  C  CD1 . PHE A 1 81  ? -20.373 -26.927 18.068  1.00 40.35  ? 81   PHE A CD1 1 
ATOM   653  C  CD2 . PHE A 1 81  ? -20.429 -24.587 18.525  1.00 41.46  ? 81   PHE A CD2 1 
ATOM   654  C  CE1 . PHE A 1 81  ? -19.087 -26.779 17.526  1.00 40.50  ? 81   PHE A CE1 1 
ATOM   655  C  CE2 . PHE A 1 81  ? -19.157 -24.437 17.986  1.00 36.94  ? 81   PHE A CE2 1 
ATOM   656  C  CZ  . PHE A 1 81  ? -18.484 -25.536 17.495  1.00 39.94  ? 81   PHE A CZ  1 
ATOM   657  N  N   . ALA A 1 82  ? -23.588 -23.960 16.599  1.00 34.77  ? 82   ALA A N   1 
ATOM   658  C  CA  . ALA A 1 82  ? -23.904 -22.584 16.224  1.00 34.66  ? 82   ALA A CA  1 
ATOM   659  C  C   . ALA A 1 82  ? -25.203 -22.468 15.434  1.00 37.00  ? 82   ALA A C   1 
ATOM   660  O  O   . ALA A 1 82  ? -25.629 -21.348 15.117  1.00 34.15  ? 82   ALA A O   1 
ATOM   661  C  CB  . ALA A 1 82  ? -22.750 -21.973 15.426  1.00 32.20  ? 82   ALA A CB  1 
ATOM   662  N  N   . GLY A 1 83  ? -25.840 -23.594 15.114  1.00 34.68  ? 83   GLY A N   1 
ATOM   663  C  CA  . GLY A 1 83  ? -27.172 -23.558 14.533  1.00 34.18  ? 83   GLY A CA  1 
ATOM   664  C  C   . GLY A 1 83  ? -27.254 -22.686 13.300  1.00 35.26  ? 83   GLY A C   1 
ATOM   665  O  O   . GLY A 1 83  ? -26.346 -22.661 12.455  1.00 33.75  ? 83   GLY A O   1 
ATOM   666  N  N   . ASP A 1 84  ? -28.362 -21.958 13.177  1.00 31.96  ? 84   ASP A N   1 
ATOM   667  C  CA  . ASP A 1 84  ? -28.518 -21.004 12.080  1.00 35.30  ? 84   ASP A CA  1 
ATOM   668  C  C   . ASP A 1 84  ? -28.199 -19.586 12.536  1.00 35.39  ? 84   ASP A C   1 
ATOM   669  O  O   . ASP A 1 84  ? -28.843 -18.628 12.125  1.00 32.64  ? 84   ASP A O   1 
ATOM   670  C  CB  . ASP A 1 84  ? -29.911 -21.095 11.447  1.00 37.86  ? 84   ASP A CB  1 
ATOM   671  C  CG  . ASP A 1 84  ? -31.050 -20.801 12.427  1.00 40.09  ? 84   ASP A CG  1 
ATOM   672  O  OD1 . ASP A 1 84  ? -30.810 -20.676 13.640  1.00 36.96  ? 84   ASP A OD1 1 
ATOM   673  O  OD2 . ASP A 1 84  ? -32.204 -20.698 11.963  1.00 37.59  ? 84   ASP A OD2 1 
ATOM   674  N  N   . GLY A 1 85  ? -27.189 -19.438 13.396  1.00 31.99  ? 85   GLY A N   1 
ATOM   675  C  CA  . GLY A 1 85  ? -26.581 -18.142 13.606  1.00 32.60  ? 85   GLY A CA  1 
ATOM   676  C  C   . GLY A 1 85  ? -25.987 -17.617 12.310  1.00 32.83  ? 85   GLY A C   1 
ATOM   677  O  O   . GLY A 1 85  ? -25.941 -18.295 11.282  1.00 31.56  ? 85   GLY A O   1 
ATOM   678  N  N   . LEU A 1 86  ? -25.524 -16.365 12.368  1.00 28.13  ? 86   LEU A N   1 
ATOM   679  C  CA  . LEU A 1 86  ? -25.150 -15.669 11.136  1.00 30.16  ? 86   LEU A CA  1 
ATOM   680  C  C   . LEU A 1 86  ? -24.082 -16.420 10.348  1.00 31.97  ? 86   LEU A C   1 
ATOM   681  O  O   . LEU A 1 86  ? -24.112 -16.424 9.113   1.00 30.82  ? 86   LEU A O   1 
ATOM   682  C  CB  . LEU A 1 86  ? -24.658 -14.255 11.454  1.00 31.44  ? 86   LEU A CB  1 
ATOM   683  C  CG  . LEU A 1 86  ? -25.777 -13.219 11.632  1.00 35.49  ? 86   LEU A CG  1 
ATOM   684  C  CD1 . LEU A 1 86  ? -25.152 -11.924 12.140  1.00 36.99  ? 86   LEU A CD1 1 
ATOM   685  C  CD2 . LEU A 1 86  ? -26.534 -12.991 10.329  1.00 30.58  ? 86   LEU A CD2 1 
ATOM   686  N  N   . ALA A 1 87  ? -23.095 -17.017 11.029  1.00 31.12  ? 87   ALA A N   1 
ATOM   687  C  CA  . ALA A 1 87  ? -21.952 -17.538 10.285  1.00 30.34  ? 87   ALA A CA  1 
ATOM   688  C  C   . ALA A 1 87  ? -22.205 -18.917 9.695   1.00 32.34  ? 87   ALA A C   1 
ATOM   689  O  O   . ALA A 1 87  ? -21.505 -19.323 8.764   1.00 29.73  ? 87   ALA A O   1 
ATOM   690  C  CB  . ALA A 1 87  ? -20.700 -17.590 11.171  1.00 27.70  ? 87   ALA A CB  1 
ATOM   691  N  N   . THR A 1 88  ? -23.186 -19.647 10.202  1.00 30.38  ? 88   THR A N   1 
ATOM   692  C  CA  . THR A 1 88  ? -23.406 -21.013 9.763   1.00 30.79  ? 88   THR A CA  1 
ATOM   693  C  C   . THR A 1 88  ? -24.769 -21.185 9.104   1.00 34.89  ? 88   THR A C   1 
ATOM   694  O  O   . THR A 1 88  ? -25.207 -22.318 8.900   1.00 33.33  ? 88   THR A O   1 
ATOM   695  C  CB  . THR A 1 88  ? -23.235 -21.984 10.942  1.00 33.78  ? 88   THR A CB  1 
ATOM   696  O  OG1 . THR A 1 88  ? -23.995 -21.523 12.060  1.00 32.22  ? 88   THR A OG1 1 
ATOM   697  C  CG2 . THR A 1 88  ? -21.775 -22.075 11.347  1.00 33.12  ? 88   THR A CG2 1 
ATOM   698  N  N   . SER A 1 89  ? -25.434 -20.099 8.744   1.00 33.44  ? 89   SER A N   1 
ATOM   699  C  CA  . SER A 1 89  ? -26.676 -20.176 7.993   1.00 36.12  ? 89   SER A CA  1 
ATOM   700  C  C   . SER A 1 89  ? -26.419 -20.034 6.492   1.00 32.61  ? 89   SER A C   1 
ATOM   701  O  O   . SER A 1 89  ? -25.460 -19.389 6.063   1.00 30.96  ? 89   SER A O   1 
ATOM   702  C  CB  . SER A 1 89  ? -27.651 -19.098 8.466   1.00 36.75  ? 89   SER A CB  1 
ATOM   703  O  OG  . SER A 1 89  ? -27.004 -17.836 8.520   1.00 40.54  ? 89   SER A OG  1 
ATOM   704  N  N   . TRP A 1 90  ? -27.281 -20.663 5.694   1.00 33.50  ? 90   TRP A N   1 
ATOM   705  C  CA  . TRP A 1 90  ? -27.286 -20.398 4.261   1.00 33.75  ? 90   TRP A CA  1 
ATOM   706  C  C   . TRP A 1 90  ? -27.916 -19.036 3.977   1.00 31.31  ? 90   TRP A C   1 
ATOM   707  O  O   . TRP A 1 90  ? -28.824 -18.585 4.684   1.00 32.74  ? 90   TRP A O   1 
ATOM   708  C  CB  . TRP A 1 90  ? -28.070 -21.480 3.508   1.00 31.56  ? 90   TRP A CB  1 
ATOM   709  C  CG  . TRP A 1 90  ? -27.564 -22.870 3.737   1.00 32.87  ? 90   TRP A CG  1 
ATOM   710  C  CD1 . TRP A 1 90  ? -27.957 -23.739 4.709   1.00 31.49  ? 90   TRP A CD1 1 
ATOM   711  C  CD2 . TRP A 1 90  ? -26.567 -23.545 2.968   1.00 32.73  ? 90   TRP A CD2 1 
ATOM   712  N  NE1 . TRP A 1 90  ? -27.264 -24.923 4.593   1.00 32.70  ? 90   TRP A NE1 1 
ATOM   713  C  CE2 . TRP A 1 90  ? -26.409 -24.829 3.525   1.00 31.81  ? 90   TRP A CE2 1 
ATOM   714  C  CE3 . TRP A 1 90  ? -25.800 -23.192 1.852   1.00 31.01  ? 90   TRP A CE3 1 
ATOM   715  C  CZ2 . TRP A 1 90  ? -25.505 -25.762 3.009   1.00 32.77  ? 90   TRP A CZ2 1 
ATOM   716  C  CZ3 . TRP A 1 90  ? -24.894 -24.121 1.341   1.00 35.62  ? 90   TRP A CZ3 1 
ATOM   717  C  CH2 . TRP A 1 90  ? -24.759 -25.391 1.921   1.00 35.62  ? 90   TRP A CH2 1 
ATOM   718  N  N   . THR A 1 91  ? -27.452 -18.390 2.905   1.00 30.32  ? 91   THR A N   1 
ATOM   719  C  CA  . THR A 1 91  ? -27.962 -17.061 2.581   1.00 30.78  ? 91   THR A CA  1 
ATOM   720  C  C   . THR A 1 91  ? -29.476 -17.070 2.390   1.00 32.67  ? 91   THR A C   1 
ATOM   721  O  O   . THR A 1 91  ? -30.138 -16.059 2.639   1.00 31.84  ? 91   THR A O   1 
ATOM   722  C  CB  . THR A 1 91  ? -27.284 -16.526 1.317   1.00 29.24  ? 91   THR A CB  1 
ATOM   723  O  OG1 . THR A 1 91  ? -25.854 -16.585 1.459   1.00 32.02  ? 91   THR A OG1 1 
ATOM   724  C  CG2 . THR A 1 91  ? -27.712 -15.102 1.027   1.00 32.89  ? 91   THR A CG2 1 
ATOM   725  N  N   . HIS A 1 92  ? -30.030 -18.187 1.928   1.00 31.37  ? 92   HIS A N   1 
ATOM   726  C  CA  . HIS A 1 92  ? -31.452 -18.287 1.619   1.00 30.97  ? 92   HIS A CA  1 
ATOM   727  C  C   . HIS A 1 92  ? -32.302 -18.706 2.813   1.00 35.73  ? 92   HIS A C   1 
ATOM   728  O  O   . HIS A 1 92  ? -33.536 -18.743 2.696   1.00 36.36  ? 92   HIS A O   1 
ATOM   729  C  CB  . HIS A 1 92  ? -31.657 -19.264 0.458   1.00 34.40  ? 92   HIS A CB  1 
ATOM   730  C  CG  . HIS A 1 92  ? -30.957 -20.576 0.637   1.00 35.20  ? 92   HIS A CG  1 
ATOM   731  N  ND1 . HIS A 1 92  ? -31.404 -21.548 1.509   1.00 33.81  ? 92   HIS A ND1 1 
ATOM   732  C  CD2 . HIS A 1 92  ? -29.829 -21.069 0.070   1.00 31.84  ? 92   HIS A CD2 1 
ATOM   733  C  CE1 . HIS A 1 92  ? -30.589 -22.587 1.461   1.00 32.81  ? 92   HIS A CE1 1 
ATOM   734  N  NE2 . HIS A 1 92  ? -29.628 -22.323 0.594   1.00 34.13  ? 92   HIS A NE2 1 
ATOM   735  N  N   . GLU A 1 93  ? -31.689 -19.020 3.954   1.00 34.39  ? 93   GLU A N   1 
ATOM   736  C  CA  . GLU A 1 93  ? -32.482 -19.294 5.144   1.00 32.14  ? 93   GLU A CA  1 
ATOM   737  C  C   . GLU A 1 93  ? -33.044 -17.992 5.683   1.00 35.56  ? 93   GLU A C   1 
ATOM   738  O  O   . GLU A 1 93  ? -32.343 -16.976 5.756   1.00 33.25  ? 93   GLU A O   1 
ATOM   739  C  CB  . GLU A 1 93  ? -31.650 -19.982 6.228   1.00 35.65  ? 93   GLU A CB  1 
ATOM   740  C  CG  . GLU A 1 93  ? -31.317 -21.453 5.936   1.00 34.29  ? 93   GLU A CG  1 
ATOM   741  C  CD  . GLU A 1 93  ? -30.479 -22.086 7.050   1.00 38.17  ? 93   GLU A CD  1 
ATOM   742  O  OE1 . GLU A 1 93  ? -29.250 -21.886 7.058   1.00 35.79  ? 93   GLU A OE1 1 
ATOM   743  O  OE2 . GLU A 1 93  ? -31.054 -22.779 7.926   1.00 37.85  ? 93   GLU A OE2 1 
ATOM   744  N  N   . LYS A 1 94  ? -34.324 -18.019 6.054   1.00 37.82  ? 94   LYS A N   1 
ATOM   745  C  CA  . LYS A 1 94  ? -34.963 -16.805 6.548   1.00 35.00  ? 94   LYS A CA  1 
ATOM   746  C  C   . LYS A 1 94  ? -34.114 -16.127 7.620   1.00 35.25  ? 94   LYS A C   1 
ATOM   747  O  O   . LYS A 1 94  ? -33.940 -14.903 7.602   1.00 36.40  ? 94   LYS A O   1 
ATOM   748  C  CB  . LYS A 1 94  ? -36.350 -17.137 7.095   1.00 39.85  ? 94   LYS A CB  1 
ATOM   749  C  CG  . LYS A 1 94  ? -37.072 -15.961 7.748   1.00 38.42  ? 94   LYS A CG  1 
ATOM   750  C  CD  . LYS A 1 94  ? -38.446 -16.397 8.223   1.00 43.73  ? 94   LYS A CD  1 
ATOM   751  C  CE  . LYS A 1 94  ? -39.070 -15.373 9.136   1.00 42.67  ? 94   LYS A CE  1 
ATOM   752  N  NZ  . LYS A 1 94  ? -40.376 -15.861 9.653   1.00 48.27  ? 94   LYS A NZ  1 
ATOM   753  N  N   . ASN A 1 95  ? -33.565 -16.909 8.551   1.00 36.45  ? 95   ASN A N   1 
ATOM   754  C  CA  . ASN A 1 95  ? -32.889 -16.324 9.696   1.00 34.70  ? 95   ASN A CA  1 
ATOM   755  C  C   . ASN A 1 95  ? -31.573 -15.640 9.334   1.00 33.42  ? 95   ASN A C   1 
ATOM   756  O  O   . ASN A 1 95  ? -31.072 -14.861 10.155  1.00 32.91  ? 95   ASN A O   1 
ATOM   757  C  CB  . ASN A 1 95  ? -32.666 -17.388 10.777  1.00 35.33  ? 95   ASN A CB  1 
ATOM   758  C  CG  . ASN A 1 95  ? -33.858 -17.507 11.699  1.00 40.68  ? 95   ASN A CG  1 
ATOM   759  O  OD1 . ASN A 1 95  ? -34.659 -16.574 11.796  1.00 39.31  ? 95   ASN A OD1 1 
ATOM   760  N  ND2 . ASN A 1 95  ? -33.999 -18.650 12.365  1.00 36.46  ? 95   ASN A ND2 1 
ATOM   761  N  N   . TRP A 1 96  ? -31.023 -15.858 8.132   1.00 32.67  ? 96   TRP A N   1 
ATOM   762  C  CA  . TRP A 1 96  ? -29.794 -15.142 7.798   1.00 33.41  ? 96   TRP A CA  1 
ATOM   763  C  C   . TRP A 1 96  ? -30.073 -13.654 7.589   1.00 34.00  ? 96   TRP A C   1 
ATOM   764  O  O   . TRP A 1 96  ? -29.552 -12.808 8.319   1.00 33.27  ? 96   TRP A O   1 
ATOM   765  C  CB  . TRP A 1 96  ? -29.071 -15.721 6.573   1.00 31.94  ? 96   TRP A CB  1 
ATOM   766  C  CG  . TRP A 1 96  ? -27.888 -14.798 6.368   1.00 33.15  ? 96   TRP A CG  1 
ATOM   767  C  CD1 . TRP A 1 96  ? -26.785 -14.698 7.182   1.00 33.47  ? 96   TRP A CD1 1 
ATOM   768  C  CD2 . TRP A 1 96  ? -27.781 -13.730 5.422   1.00 34.10  ? 96   TRP A CD2 1 
ATOM   769  N  NE1 . TRP A 1 96  ? -25.972 -13.677 6.755   1.00 32.97  ? 96   TRP A NE1 1 
ATOM   770  C  CE2 . TRP A 1 96  ? -26.566 -13.055 5.686   1.00 33.73  ? 96   TRP A CE2 1 
ATOM   771  C  CE3 . TRP A 1 96  ? -28.587 -13.280 4.366   1.00 35.03  ? 96   TRP A CE3 1 
ATOM   772  C  CZ2 . TRP A 1 96  ? -26.123 -11.973 4.916   1.00 37.24  ? 96   TRP A CZ2 1 
ATOM   773  C  CZ3 . TRP A 1 96  ? -28.140 -12.190 3.598   1.00 35.34  ? 96   TRP A CZ3 1 
ATOM   774  C  CH2 . TRP A 1 96  ? -26.920 -11.551 3.889   1.00 36.07  ? 96   TRP A CH2 1 
ATOM   775  N  N   . LYS A 1 97  ? -30.904 -13.308 6.595   1.00 32.85  ? 97   LYS A N   1 
ATOM   776  C  CA  . LYS A 1 97  ? -31.129 -11.889 6.329   1.00 31.22  ? 97   LYS A CA  1 
ATOM   777  C  C   . LYS A 1 97  ? -31.831 -11.203 7.498   1.00 35.19  ? 97   LYS A C   1 
ATOM   778  O  O   . LYS A 1 97  ? -31.585 -10.017 7.767   1.00 33.43  ? 97   LYS A O   1 
ATOM   779  C  CB  . LYS A 1 97  ? -31.925 -11.710 5.033   1.00 34.01  ? 97   LYS A CB  1 
ATOM   780  C  CG  . LYS A 1 97  ? -32.147 -10.241 4.641   1.00 39.06  ? 97   LYS A CG  1 
ATOM   781  C  CD  . LYS A 1 97  ? -30.832 -9.498  4.437   1.00 41.98  ? 97   LYS A CD  1 
ATOM   782  C  CE  . LYS A 1 97  ? -31.083 -8.171  3.755   1.00 50.71  ? 97   LYS A CE  1 
ATOM   783  N  NZ  . LYS A 1 97  ? -29.811 -7.480  3.449   1.00 53.85  ? 97   LYS A NZ  1 
ATOM   784  N  N   . LYS A 1 98  ? -32.691 -11.928 8.217   1.00 32.74  ? 98   LYS A N   1 
ATOM   785  C  CA  . LYS A 1 98  ? -33.395 -11.329 9.341   1.00 36.37  ? 98   LYS A CA  1 
ATOM   786  C  C   . LYS A 1 98  ? -32.422 -10.942 10.453  1.00 36.60  ? 98   LYS A C   1 
ATOM   787  O  O   . LYS A 1 98  ? -32.467 -9.819  10.970  1.00 33.60  ? 98   LYS A O   1 
ATOM   788  C  CB  . LYS A 1 98  ? -34.468 -12.295 9.844   1.00 39.32  ? 98   LYS A CB  1 
ATOM   789  C  CG  . LYS A 1 98  ? -35.189 -11.888 11.113  1.00 39.60  ? 98   LYS A CG  1 
ATOM   790  C  CD  . LYS A 1 98  ? -36.278 -12.940 11.426  1.00 38.81  ? 98   LYS A CD  1 
ATOM   791  C  CE  . LYS A 1 98  ? -36.818 -12.827 12.846  1.00 37.02  ? 98   LYS A CE  1 
ATOM   792  N  NZ  . LYS A 1 98  ? -37.859 -13.876 13.066  1.00 39.54  ? 98   LYS A NZ  1 
ATOM   793  N  N   . ALA A 1 99  ? -31.522 -11.858 10.827  1.00 33.96  ? 99   ALA A N   1 
ATOM   794  C  CA  . ALA A 1 99  ? -30.542 -11.513 11.853  1.00 32.23  ? 99   ALA A CA  1 
ATOM   795  C  C   . ALA A 1 99  ? -29.541 -10.490 11.338  1.00 35.89  ? 99   ALA A C   1 
ATOM   796  O  O   . ALA A 1 99  ? -29.081 -9.639  12.102  1.00 33.77  ? 99   ALA A O   1 
ATOM   797  C  CB  . ALA A 1 99  ? -29.813 -12.760 12.351  1.00 29.27  ? 99   ALA A CB  1 
ATOM   798  N  N   . HIS A 1 100 ? -29.192 -10.560 10.051  1.00 32.96  ? 100  HIS A N   1 
ATOM   799  C  CA  . HIS A 1 100 ? -28.290 -9.569  9.477   1.00 33.49  ? 100  HIS A CA  1 
ATOM   800  C  C   . HIS A 1 100 ? -28.868 -8.168  9.607   1.00 36.99  ? 100  HIS A C   1 
ATOM   801  O  O   . HIS A 1 100 ? -28.204 -7.245  10.099  1.00 33.70  ? 100  HIS A O   1 
ATOM   802  C  CB  . HIS A 1 100 ? -28.028 -9.908  8.011   1.00 32.93  ? 100  HIS A CB  1 
ATOM   803  C  CG  . HIS A 1 100 ? -27.203 -8.887  7.297   1.00 36.25  ? 100  HIS A CG  1 
ATOM   804  N  ND1 . HIS A 1 100 ? -25.826 -8.909  7.309   1.00 43.27  ? 100  HIS A ND1 1 
ATOM   805  C  CD2 . HIS A 1 100 ? -27.558 -7.826  6.531   1.00 45.46  ? 100  HIS A CD2 1 
ATOM   806  C  CE1 . HIS A 1 100 ? -25.366 -7.903  6.587   1.00 44.92  ? 100  HIS A CE1 1 
ATOM   807  N  NE2 . HIS A 1 100 ? -26.396 -7.228  6.105   1.00 50.04  ? 100  HIS A NE2 1 
ATOM   808  N  N   . ASN A 1 101 ? -30.126 -7.998  9.185   1.00 33.56  ? 101  ASN A N   1 
ATOM   809  C  CA  . ASN A 1 101 ? -30.776 -6.695  9.286   1.00 34.75  ? 101  ASN A CA  1 
ATOM   810  C  C   . ASN A 1 101 ? -30.815 -6.217  10.724  1.00 36.14  ? 101  ASN A C   1 
ATOM   811  O  O   . ASN A 1 101 ? -30.620 -5.027  10.998  1.00 37.84  ? 101  ASN A O   1 
ATOM   812  C  CB  . ASN A 1 101 ? -32.197 -6.774  8.722   1.00 34.53  ? 101  ASN A CB  1 
ATOM   813  C  CG  . ASN A 1 101 ? -32.209 -6.831  7.198   1.00 35.65  ? 101  ASN A CG  1 
ATOM   814  O  OD1 . ASN A 1 101 ? -31.203 -6.544  6.562   1.00 36.63  ? 101  ASN A OD1 1 
ATOM   815  N  ND2 . ASN A 1 101 ? -33.339 -7.231  6.617   1.00 37.25  ? 101  ASN A ND2 1 
ATOM   816  N  N   . ILE A 1 102 ? -31.084 -7.136  11.653  1.00 34.53  ? 102  ILE A N   1 
ATOM   817  C  CA  . ILE A 1 102 ? -31.270 -6.771  13.051  1.00 33.42  ? 102  ILE A CA  1 
ATOM   818  C  C   . ILE A 1 102 ? -29.938 -6.415  13.694  1.00 36.86  ? 102  ILE A C   1 
ATOM   819  O  O   . ILE A 1 102 ? -29.860 -5.494  14.507  1.00 33.34  ? 102  ILE A O   1 
ATOM   820  C  CB  . ILE A 1 102 ? -31.971 -7.916  13.811  1.00 34.42  ? 102  ILE A CB  1 
ATOM   821  C  CG1 . ILE A 1 102 ? -33.449 -8.006  13.412  1.00 36.68  ? 102  ILE A CG1 1 
ATOM   822  C  CG2 . ILE A 1 102 ? -31.837 -7.733  15.299  1.00 37.20  ? 102  ILE A CG2 1 
ATOM   823  C  CD1 . ILE A 1 102 ? -34.156 -9.303  13.886  1.00 36.39  ? 102  ILE A CD1 1 
ATOM   824  N  N   . LEU A 1 103 ? -28.868 -7.117  13.325  1.00 31.40  ? 103  LEU A N   1 
ATOM   825  C  CA  . LEU A 1 103 ? -27.596 -6.968  14.035  1.00 33.37  ? 103  LEU A CA  1 
ATOM   826  C  C   . LEU A 1 103 ? -26.611 -6.027  13.350  1.00 34.68  ? 103  LEU A C   1 
ATOM   827  O  O   . LEU A 1 103 ? -25.645 -5.597  13.991  1.00 34.36  ? 103  LEU A O   1 
ATOM   828  C  CB  . LEU A 1 103 ? -26.943 -8.347  14.229  1.00 32.21  ? 103  LEU A CB  1 
ATOM   829  C  CG  . LEU A 1 103 ? -27.744 -9.306  15.119  1.00 34.91  ? 103  LEU A CG  1 
ATOM   830  C  CD1 . LEU A 1 103 ? -27.112 -10.695 15.148  1.00 33.13  ? 103  LEU A CD1 1 
ATOM   831  C  CD2 . LEU A 1 103 ? -27.886 -8.746  16.526  1.00 40.77  ? 103  LEU A CD2 1 
ATOM   832  N  N   . LEU A 1 104 ? -26.821 -5.682  12.087  1.00 34.50  ? 104  LEU A N   1 
ATOM   833  C  CA  . LEU A 1 104 ? -25.931 -4.726  11.427  1.00 36.98  ? 104  LEU A CA  1 
ATOM   834  C  C   . LEU A 1 104 ? -25.772 -3.421  12.207  1.00 34.85  ? 104  LEU A C   1 
ATOM   835  O  O   . LEU A 1 104 ? -24.626 -2.961  12.361  1.00 36.12  ? 104  LEU A O   1 
ATOM   836  C  CB  . LEU A 1 104 ? -26.430 -4.452  9.999   1.00 34.86  ? 104  LEU A CB  1 
ATOM   837  C  CG  . LEU A 1 104 ? -25.451 -3.781  9.028   1.00 42.22  ? 104  LEU A CG  1 
ATOM   838  C  CD1 . LEU A 1 104 ? -24.189 -4.623  8.889   1.00 41.65  ? 104  LEU A CD1 1 
ATOM   839  C  CD2 . LEU A 1 104 ? -26.097 -3.594  7.668   1.00 39.24  ? 104  LEU A CD2 1 
ATOM   840  N  N   . PRO A 1 105 ? -26.826 -2.799  12.739  1.00 34.92  ? 105  PRO A N   1 
ATOM   841  C  CA  . PRO A 1 105 ? -26.631 -1.548  13.495  1.00 36.90  ? 105  PRO A CA  1 
ATOM   842  C  C   . PRO A 1 105 ? -25.764 -1.717  14.735  1.00 36.10  ? 105  PRO A C   1 
ATOM   843  O  O   . PRO A 1 105 ? -25.182 -0.732  15.203  1.00 38.59  ? 105  PRO A O   1 
ATOM   844  C  CB  . PRO A 1 105 ? -28.063 -1.129  13.868  1.00 37.77  ? 105  PRO A CB  1 
ATOM   845  C  CG  . PRO A 1 105 ? -28.923 -1.808  12.845  1.00 40.60  ? 105  PRO A CG  1 
ATOM   846  C  CD  . PRO A 1 105 ? -28.251 -3.135  12.591  1.00 33.62  ? 105  PRO A CD  1 
ATOM   847  N  N   . SER A 1 106 ? -25.637 -2.931  15.274  1.00 32.35  ? 106  SER A N   1 
ATOM   848  C  CA  . SER A 1 106 ? -24.726 -3.131  16.397  1.00 35.22  ? 106  SER A CA  1 
ATOM   849  C  C   . SER A 1 106 ? -23.256 -2.986  16.011  1.00 37.03  ? 106  SER A C   1 
ATOM   850  O  O   . SER A 1 106 ? -22.402 -3.057  16.900  1.00 35.83  ? 106  SER A O   1 
ATOM   851  C  CB  . SER A 1 106 ? -24.943 -4.511  17.024  1.00 39.65  ? 106  SER A CB  1 
ATOM   852  O  OG  . SER A 1 106 ? -26.255 -4.617  17.538  1.00 44.37  ? 106  SER A OG  1 
ATOM   853  N  N   . PHE A 1 107 ? -22.944 -2.788  14.725  1.00 35.98  ? 107  PHE A N   1 
ATOM   854  C  CA  . PHE A 1 107 ? -21.579 -2.507  14.279  1.00 40.16  ? 107  PHE A CA  1 
ATOM   855  C  C   . PHE A 1 107 ? -21.468 -1.183  13.513  1.00 41.06  ? 107  PHE A C   1 
ATOM   856  O  O   . PHE A 1 107 ? -20.482 -0.953  12.809  1.00 44.87  ? 107  PHE A O   1 
ATOM   857  C  CB  . PHE A 1 107 ? -21.051 -3.693  13.469  1.00 37.11  ? 107  PHE A CB  1 
ATOM   858  C  CG  . PHE A 1 107 ? -21.081 -4.986  14.247  1.00 37.88  ? 107  PHE A CG  1 
ATOM   859  C  CD1 . PHE A 1 107 ? -20.056 -5.295  15.135  1.00 39.18  ? 107  PHE A CD1 1 
ATOM   860  C  CD2 . PHE A 1 107 ? -22.164 -5.836  14.174  1.00 37.11  ? 107  PHE A CD2 1 
ATOM   861  C  CE1 . PHE A 1 107 ? -20.097 -6.468  15.900  1.00 39.12  ? 107  PHE A CE1 1 
ATOM   862  C  CE2 . PHE A 1 107 ? -22.226 -6.999  14.930  1.00 37.26  ? 107  PHE A CE2 1 
ATOM   863  C  CZ  . PHE A 1 107 ? -21.178 -7.319  15.806  1.00 39.39  ? 107  PHE A CZ  1 
ATOM   864  N  N   . SER A 1 108 ? -22.434 -0.285  13.679  1.00 46.29  ? 108  SER A N   1 
ATOM   865  C  CA  . SER A 1 108 ? -22.322 1.071   13.156  1.00 39.82  ? 108  SER A CA  1 
ATOM   866  C  C   . SER A 1 108 ? -21.216 1.849   13.877  1.00 52.30  ? 108  SER A C   1 
ATOM   867  O  O   . SER A 1 108 ? -20.754 1.469   14.961  1.00 44.70  ? 108  SER A O   1 
ATOM   868  C  CB  . SER A 1 108 ? -23.644 1.806   13.322  1.00 45.17  ? 108  SER A CB  1 
ATOM   869  O  OG  . SER A 1 108 ? -23.838 2.158   14.686  1.00 51.21  ? 108  SER A OG  1 
ATOM   870  N  N   . GLN A 1 109 ? -20.791 2.965   13.266  1.00 44.47  ? 109  GLN A N   1 
ATOM   871  C  CA  . GLN A 1 109 ? -19.851 3.846   13.955  1.00 44.75  ? 109  GLN A CA  1 
ATOM   872  C  C   . GLN A 1 109 ? -20.359 4.185   15.350  1.00 47.75  ? 109  GLN A C   1 
ATOM   873  O  O   . GLN A 1 109 ? -19.615 4.114   16.338  1.00 49.54  ? 109  GLN A O   1 
ATOM   874  C  CB  . GLN A 1 109 ? -19.592 5.145   13.166  1.00 47.01  ? 109  GLN A CB  1 
ATOM   875  C  CG  . GLN A 1 109 ? -18.861 5.001   11.816  1.00 53.51  ? 109  GLN A CG  1 
ATOM   876  C  CD  . GLN A 1 109 ? -19.240 6.085   10.789  1.00 54.78  ? 109  GLN A CD  1 
ATOM   877  O  OE1 . GLN A 1 109 ? -19.885 7.080   11.125  1.00 51.77  ? 109  GLN A OE1 1 
ATOM   878  N  NE2 . GLN A 1 109 ? -18.802 5.903   9.540   1.00 52.01  ? 109  GLN A NE2 1 
ATOM   879  N  N   . GLN A 1 110 ? -21.633 4.556   15.455  1.00 46.86  ? 110  GLN A N   1 
ATOM   880  C  CA  . GLN A 1 110 ? -22.141 4.953   16.758  1.00 51.53  ? 110  GLN A CA  1 
ATOM   881  C  C   . GLN A 1 110 ? -22.105 3.789   17.744  1.00 48.38  ? 110  GLN A C   1 
ATOM   882  O  O   . GLN A 1 110 ? -21.908 4.000   18.952  1.00 45.90  ? 110  GLN A O   1 
ATOM   883  C  CB  . GLN A 1 110 ? -23.554 5.517   16.618  1.00 55.94  ? 110  GLN A CB  1 
ATOM   884  C  CG  . GLN A 1 110 ? -24.303 5.550   17.920  1.00 59.61  ? 110  GLN A CG  1 
ATOM   885  C  CD  . GLN A 1 110 ? -23.904 6.757   18.751  1.00 69.64  ? 110  GLN A CD  1 
ATOM   886  O  OE1 . GLN A 1 110 ? -23.887 6.701   19.986  1.00 79.20  ? 110  GLN A OE1 1 
ATOM   887  N  NE2 . GLN A 1 110 ? -23.543 7.849   18.075  1.00 66.88  ? 110  GLN A NE2 1 
ATOM   888  N  N   . ALA A 1 111 ? -22.288 2.557   17.251  1.00 49.00  ? 111  ALA A N   1 
ATOM   889  C  CA  . ALA A 1 111 ? -22.116 1.383   18.102  1.00 44.01  ? 111  ALA A CA  1 
ATOM   890  C  C   . ALA A 1 111 ? -20.668 1.247   18.563  1.00 37.70  ? 111  ALA A C   1 
ATOM   891  O  O   . ALA A 1 111 ? -20.414 1.029   19.750  1.00 42.23  ? 111  ALA A O   1 
ATOM   892  C  CB  . ALA A 1 111 ? -22.581 0.116   17.370  1.00 39.60  ? 111  ALA A CB  1 
ATOM   893  N  N   . MET A 1 112 ? -19.708 1.357   17.633  1.00 36.97  ? 112  MET A N   1 
ATOM   894  C  CA  . MET A 1 112 ? -18.289 1.301   17.991  1.00 39.93  ? 112  MET A CA  1 
ATOM   895  C  C   . MET A 1 112 ? -17.927 2.325   19.066  1.00 38.46  ? 112  MET A C   1 
ATOM   896  O  O   . MET A 1 112 ? -17.210 2.011   20.023  1.00 37.47  ? 112  MET A O   1 
ATOM   897  C  CB  . MET A 1 112 ? -17.433 1.496   16.738  1.00 46.34  ? 112  MET A CB  1 
ATOM   898  C  CG  . MET A 1 112 ? -17.055 0.244   15.912  1.00 49.26  ? 112  MET A CG  1 
ATOM   899  S  SD  . MET A 1 112 ? -17.193 -1.379  16.693  1.00 41.64  ? 112  MET A SD  1 
ATOM   900  C  CE  . MET A 1 112 ? -15.653 -1.371  17.588  1.00 47.89  ? 112  MET A CE  1 
ATOM   901  N  N   . LYS A 1 113 ? -18.389 3.565   18.911  1.00 36.80  ? 113  LYS A N   1 
ATOM   902  C  CA  . LYS A 1 113 ? -18.133 4.559   19.941  1.00 35.23  ? 113  LYS A CA  1 
ATOM   903  C  C   . LYS A 1 113 ? -18.670 4.095   21.284  1.00 37.03  ? 113  LYS A C   1 
ATOM   904  O  O   . LYS A 1 113 ? -18.060 4.367   22.328  1.00 39.90  ? 113  LYS A O   1 
ATOM   905  C  CB  . LYS A 1 113 ? -18.757 5.898   19.531  1.00 33.35  ? 113  LYS A CB  1 
ATOM   906  C  CG  . LYS A 1 113 ? -18.232 6.420   18.200  1.00 40.21  ? 113  LYS A CG  1 
ATOM   907  C  CD  . LYS A 1 113 ? -18.871 7.749   17.803  1.00 43.51  ? 113  LYS A CD  1 
ATOM   908  C  CE  . LYS A 1 113 ? -18.231 8.311   16.530  1.00 47.56  ? 113  LYS A CE  1 
ATOM   909  N  NZ  . LYS A 1 113 ? -19.136 9.288   15.839  1.00 47.81  ? 113  LYS A NZ  1 
ATOM   910  N  N   . GLY A 1 114 ? -19.785 3.361   21.272  1.00 34.07  ? 114  GLY A N   1 
ATOM   911  C  CA  . GLY A 1 114 ? -20.373 2.879   22.514  1.00 37.96  ? 114  GLY A CA  1 
ATOM   912  C  C   . GLY A 1 114 ? -19.626 1.722   23.145  1.00 40.94  ? 114  GLY A C   1 
ATOM   913  O  O   . GLY A 1 114 ? -19.666 1.560   24.368  1.00 37.60  ? 114  GLY A O   1 
ATOM   914  N  N   . TYR A 1 115 ? -18.965 0.885   22.329  1.00 36.47  ? 115  TYR A N   1 
ATOM   915  C  CA  . TYR A 1 115 ? -18.170 -0.228  22.843  1.00 36.53  ? 115  TYR A CA  1 
ATOM   916  C  C   . TYR A 1 115 ? -16.828 0.212   23.401  1.00 36.72  ? 115  TYR A C   1 
ATOM   917  O  O   . TYR A 1 115 ? -16.230 -0.529  24.193  1.00 33.64  ? 115  TYR A O   1 
ATOM   918  C  CB  . TYR A 1 115 ? -17.884 -1.254  21.741  1.00 32.15  ? 115  TYR A CB  1 
ATOM   919  C  CG  . TYR A 1 115 ? -19.114 -1.897  21.188  1.00 31.55  ? 115  TYR A CG  1 
ATOM   920  C  CD1 . TYR A 1 115 ? -20.113 -2.364  22.027  1.00 33.74  ? 115  TYR A CD1 1 
ATOM   921  C  CD2 . TYR A 1 115 ? -19.273 -2.045  19.811  1.00 34.60  ? 115  TYR A CD2 1 
ATOM   922  C  CE1 . TYR A 1 115 ? -21.237 -2.963  21.502  1.00 38.57  ? 115  TYR A CE1 1 
ATOM   923  C  CE2 . TYR A 1 115 ? -20.375 -2.623  19.289  1.00 35.03  ? 115  TYR A CE2 1 
ATOM   924  C  CZ  . TYR A 1 115 ? -21.362 -3.079  20.125  1.00 35.77  ? 115  TYR A CZ  1 
ATOM   925  O  OH  . TYR A 1 115 ? -22.472 -3.672  19.567  1.00 38.29  ? 115  TYR A OH  1 
ATOM   926  N  N   . HIS A 1 116 ? -16.346 1.385   22.988  1.00 35.95  ? 116  HIS A N   1 
ATOM   927  C  CA  . HIS A 1 116 ? -14.949 1.759   23.189  1.00 33.27  ? 116  HIS A CA  1 
ATOM   928  C  C   . HIS A 1 116 ? -14.529 1.700   24.657  1.00 35.94  ? 116  HIS A C   1 
ATOM   929  O  O   . HIS A 1 116 ? -13.452 1.190   24.986  1.00 35.08  ? 116  HIS A O   1 
ATOM   930  C  CB  . HIS A 1 116 ? -14.709 3.163   22.629  1.00 36.43  ? 116  HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 116 ? -13.302 3.627   22.802  1.00 35.63  ? 116  HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 116 ? -12.304 3.320   21.903  1.00 37.30  ? 116  HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 116 ? -12.712 4.326   23.803  1.00 35.28  ? 116  HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 116 ? -11.163 3.835   22.329  1.00 37.36  ? 116  HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 116 ? -11.388 4.462   23.472  1.00 35.18  ? 116  HIS A NE2 1 
ATOM   936  N  N   . ALA A 1 117 ? -15.344 2.261   25.556  1.00 36.36  ? 117  ALA A N   1 
ATOM   937  C  CA  . ALA A 1 117 ? -14.945 2.339   26.964  1.00 37.45  ? 117  ALA A CA  1 
ATOM   938  C  C   . ALA A 1 117 ? -14.710 0.957   27.558  1.00 35.46  ? 117  ALA A C   1 
ATOM   939  O  O   . ALA A 1 117 ? -13.761 0.753   28.327  1.00 34.89  ? 117  ALA A O   1 
ATOM   940  C  CB  . ALA A 1 117 ? -16.005 3.089   27.775  1.00 33.42  ? 117  ALA A CB  1 
ATOM   941  N  N   A MET A 1 118 ? -15.577 -0.001  27.226  0.59 33.15  ? 118  MET A N   1 
ATOM   942  N  N   B MET A 1 118 ? -15.566 -0.009  27.232  0.41 33.19  ? 118  MET A N   1 
ATOM   943  C  CA  A MET A 1 118 ? -15.407 -1.358  27.734  0.59 34.07  ? 118  MET A CA  1 
ATOM   944  C  CA  B MET A 1 118 ? -15.379 -1.349  27.772  0.41 34.08  ? 118  MET A CA  1 
ATOM   945  C  C   A MET A 1 118 ? -14.221 -2.050  27.073  0.59 32.83  ? 118  MET A C   1 
ATOM   946  C  C   B MET A 1 118 ? -14.258 -2.098  27.053  0.41 32.85  ? 118  MET A C   1 
ATOM   947  O  O   A MET A 1 118 ? -13.583 -2.915  27.683  0.59 30.99  ? 118  MET A O   1 
ATOM   948  O  O   B MET A 1 118 ? -13.696 -3.045  27.612  0.41 31.04  ? 118  MET A O   1 
ATOM   949  C  CB  A MET A 1 118 ? -16.681 -2.163  27.516  0.59 36.13  ? 118  MET A CB  1 
ATOM   950  C  CB  B MET A 1 118 ? -16.692 -2.125  27.703  0.41 36.19  ? 118  MET A CB  1 
ATOM   951  C  CG  A MET A 1 118 ? -17.786 -1.796  28.487  0.59 38.11  ? 118  MET A CG  1 
ATOM   952  C  CG  B MET A 1 118 ? -17.695 -1.744  28.816  0.41 37.59  ? 118  MET A CG  1 
ATOM   953  S  SD  A MET A 1 118 ? -19.362 -2.511  27.999  0.59 38.18  ? 118  MET A SD  1 
ATOM   954  S  SD  B MET A 1 118 ? -17.001 -1.562  30.478  0.41 41.70  ? 118  MET A SD  1 
ATOM   955  C  CE  A MET A 1 118 ? -20.235 -2.445  29.568  0.59 41.80  ? 118  MET A CE  1 
ATOM   956  C  CE  B MET A 1 118 ? -16.822 0.215   30.622  0.41 40.58  ? 118  MET A CE  1 
ATOM   957  N  N   . MET A 1 119 ? -13.932 -1.700  25.820  1.00 32.21  ? 119  MET A N   1 
ATOM   958  C  CA  . MET A 1 119 ? -12.739 -2.202  25.163  1.00 30.79  ? 119  MET A CA  1 
ATOM   959  C  C   . MET A 1 119 ? -11.512 -1.779  25.965  1.00 34.34  ? 119  MET A C   1 
ATOM   960  O  O   . MET A 1 119 ? -10.594 -2.573  26.213  1.00 32.50  ? 119  MET A O   1 
ATOM   961  C  CB  . MET A 1 119 ? -12.725 -1.569  23.774  1.00 34.44  ? 119  MET A CB  1 
ATOM   962  C  CG  . MET A 1 119 ? -13.668 -2.198  22.745  1.00 34.02  ? 119  MET A CG  1 
ATOM   963  S  SD  . MET A 1 119 ? -13.003 -2.293  21.092  1.00 35.57  ? 119  MET A SD  1 
ATOM   964  C  CE  . MET A 1 119 ? -14.396 -3.078  20.261  1.00 35.48  ? 119  MET A CE  1 
ATOM   965  N  N   . VAL A 1 120 ? -11.501 -0.514  26.390  1.00 33.40  ? 120  VAL A N   1 
ATOM   966  C  CA  . VAL A 1 120 ? -10.394 0.032   27.163  1.00 32.10  ? 120  VAL A CA  1 
ATOM   967  C  C   . VAL A 1 120 ? -10.291 -0.670  28.510  1.00 33.32  ? 120  VAL A C   1 
ATOM   968  O  O   . VAL A 1 120 ? -9.194  -0.997  28.969  1.00 33.96  ? 120  VAL A O   1 
ATOM   969  C  CB  . VAL A 1 120 ? -10.560 1.557   27.331  1.00 35.54  ? 120  VAL A CB  1 
ATOM   970  C  CG1 . VAL A 1 120 ? -9.546  2.096   28.341  1.00 37.39  ? 120  VAL A CG1 1 
ATOM   971  C  CG2 . VAL A 1 120 ? -10.417 2.281   25.967  1.00 32.56  ? 120  VAL A CG2 1 
ATOM   972  N  N   . ASP A 1 121 ? -11.432 -0.909  29.162  1.00 33.08  ? 121  ASP A N   1 
ATOM   973  C  CA  . ASP A 1 121 ? -11.443 -1.648  30.416  1.00 32.35  ? 121  ASP A CA  1 
ATOM   974  C  C   . ASP A 1 121 ? -10.589 -2.909  30.319  1.00 36.66  ? 121  ASP A C   1 
ATOM   975  O  O   . ASP A 1 121 ? -9.720  -3.143  31.165  1.00 35.25  ? 121  ASP A O   1 
ATOM   976  C  CB  . ASP A 1 121 ? -12.892 -1.989  30.792  1.00 32.64  ? 121  ASP A CB  1 
ATOM   977  C  CG  . ASP A 1 121 ? -13.018 -2.669  32.145  1.00 37.56  ? 121  ASP A CG  1 
ATOM   978  O  OD1 . ASP A 1 121 ? -12.462 -3.774  32.339  1.00 33.15  ? 121  ASP A OD1 1 
ATOM   979  O  OD2 . ASP A 1 121 ? -13.719 -2.108  33.008  1.00 37.96  ? 121  ASP A OD2 1 
ATOM   980  N  N   . ILE A 1 122 ? -10.810 -3.727  29.279  1.00 33.15  ? 122  ILE A N   1 
ATOM   981  C  CA  . ILE A 1 122 ? -10.078 -4.991  29.158  1.00 32.28  ? 122  ILE A CA  1 
ATOM   982  C  C   . ILE A 1 122 ? -8.626  -4.748  28.746  1.00 30.89  ? 122  ILE A C   1 
ATOM   983  O  O   . ILE A 1 122 ? -7.703  -5.423  29.231  1.00 32.53  ? 122  ILE A O   1 
ATOM   984  C  CB  . ILE A 1 122 ? -10.783 -5.935  28.163  1.00 29.98  ? 122  ILE A CB  1 
ATOM   985  C  CG1 . ILE A 1 122 ? -12.259 -6.102  28.537  1.00 29.55  ? 122  ILE A CG1 1 
ATOM   986  C  CG2 . ILE A 1 122 ? -10.079 -7.295  28.146  1.00 31.79  ? 122  ILE A CG2 1 
ATOM   987  C  CD1 . ILE A 1 122 ? -12.477 -6.562  29.990  1.00 32.43  ? 122  ILE A CD1 1 
ATOM   988  N  N   . ALA A 1 123 ? -8.403  -3.806  27.827  1.00 32.76  ? 123  ALA A N   1 
ATOM   989  C  CA  . ALA A 1 123 ? -7.046  -3.479  27.397  1.00 32.88  ? 123  ALA A CA  1 
ATOM   990  C  C   . ALA A 1 123 ? -6.192  -3.029  28.574  1.00 33.84  ? 123  ALA A C   1 
ATOM   991  O  O   . ALA A 1 123 ? -5.000  -3.361  28.660  1.00 35.20  ? 123  ALA A O   1 
ATOM   992  C  CB  . ALA A 1 123 ? -7.086  -2.375  26.336  1.00 31.32  ? 123  ALA A CB  1 
ATOM   993  N  N   . VAL A 1 124 ? -6.775  -2.237  29.469  1.00 33.20  ? 124  VAL A N   1 
ATOM   994  C  CA  . VAL A 1 124 ? -6.022  -1.781  30.633  1.00 32.64  ? 124  VAL A CA  1 
ATOM   995  C  C   . VAL A 1 124 ? -5.665  -2.969  31.520  1.00 32.72  ? 124  VAL A C   1 
ATOM   996  O  O   . VAL A 1 124 ? -4.568  -3.037  32.071  1.00 35.32  ? 124  VAL A O   1 
ATOM   997  C  CB  . VAL A 1 124 ? -6.819  -0.705  31.391  1.00 35.21  ? 124  VAL A CB  1 
ATOM   998  C  CG1 . VAL A 1 124 ? -6.252  -0.513  32.804  1.00 31.80  ? 124  VAL A CG1 1 
ATOM   999  C  CG2 . VAL A 1 124 ? -6.787  0.609   30.619  1.00 34.43  ? 124  VAL A CG2 1 
ATOM   1000 N  N   . GLN A 1 125 ? -6.578  -3.932  31.659  1.00 32.59  ? 125  GLN A N   1 
ATOM   1001 C  CA  . GLN A 1 125 ? -6.250  -5.134  32.418  1.00 30.90  ? 125  GLN A CA  1 
ATOM   1002 C  C   . GLN A 1 125 ? -5.056  -5.858  31.807  1.00 32.97  ? 125  GLN A C   1 
ATOM   1003 O  O   . GLN A 1 125 ? -4.191  -6.374  32.529  1.00 30.97  ? 125  GLN A O   1 
ATOM   1004 C  CB  . GLN A 1 125 ? -7.459  -6.062  32.481  1.00 32.55  ? 125  GLN A CB  1 
ATOM   1005 C  CG  . GLN A 1 125 ? -8.603  -5.523  33.349  1.00 31.63  ? 125  GLN A CG  1 
ATOM   1006 C  CD  . GLN A 1 125 ? -9.641  -6.588  33.616  1.00 33.15  ? 125  GLN A CD  1 
ATOM   1007 O  OE1 . GLN A 1 125 ? -9.306  -7.701  34.024  1.00 31.71  ? 125  GLN A OE1 1 
ATOM   1008 N  NE2 . GLN A 1 125 ? -10.909 -6.264  33.370  1.00 32.09  ? 125  GLN A NE2 1 
ATOM   1009 N  N   . LEU A 1 126 ? -5.000  -5.931  30.474  1.00 30.74  ? 126  LEU A N   1 
ATOM   1010 C  CA  . LEU A 1 126 ? -3.853  -6.548  29.818  1.00 29.35  ? 126  LEU A CA  1 
ATOM   1011 C  C   . LEU A 1 126 ? -2.563  -5.801  30.147  1.00 32.17  ? 126  LEU A C   1 
ATOM   1012 O  O   . LEU A 1 126 ? -1.562  -6.412  30.552  1.00 34.20  ? 126  LEU A O   1 
ATOM   1013 C  CB  . LEU A 1 126 ? -4.085  -6.602  28.306  1.00 31.59  ? 126  LEU A CB  1 
ATOM   1014 C  CG  . LEU A 1 126 ? -2.848  -7.071  27.530  1.00 32.71  ? 126  LEU A CG  1 
ATOM   1015 C  CD1 . LEU A 1 126 ? -2.692  -8.553  27.714  1.00 32.10  ? 126  LEU A CD1 1 
ATOM   1016 C  CD2 . LEU A 1 126 ? -3.014  -6.757  26.046  1.00 39.96  ? 126  LEU A CD2 1 
ATOM   1017 N  N   . VAL A 1 127 ? -2.570  -4.475  29.974  1.00 32.02  ? 127  VAL A N   1 
ATOM   1018 C  CA  . VAL A 1 127 ? -1.365  -3.678  30.227  1.00 34.24  ? 127  VAL A CA  1 
ATOM   1019 C  C   . VAL A 1 127 ? -0.933  -3.822  31.679  1.00 35.71  ? 127  VAL A C   1 
ATOM   1020 O  O   . VAL A 1 127 ? 0.256   -3.983  31.979  1.00 34.01  ? 127  VAL A O   1 
ATOM   1021 C  CB  . VAL A 1 127 ? -1.604  -2.202  29.858  1.00 33.63  ? 127  VAL A CB  1 
ATOM   1022 C  CG1 . VAL A 1 127 ? -0.409  -1.362  30.287  1.00 37.21  ? 127  VAL A CG1 1 
ATOM   1023 C  CG2 . VAL A 1 127 ? -1.886  -2.051  28.346  1.00 33.89  ? 127  VAL A CG2 1 
ATOM   1024 N  N   . GLN A 1 128 ? -1.893  -3.779  32.599  1.00 33.60  ? 128  GLN A N   1 
ATOM   1025 C  CA  . GLN A 1 128 ? -1.569  -3.912  34.014  1.00 34.38  ? 128  GLN A CA  1 
ATOM   1026 C  C   . GLN A 1 128 ? -0.971  -5.285  34.318  1.00 37.41  ? 128  GLN A C   1 
ATOM   1027 O  O   . GLN A 1 128 ? 0.001   -5.390  35.079  1.00 33.86  ? 128  GLN A O   1 
ATOM   1028 C  CB  . GLN A 1 128 ? -2.828  -3.655  34.829  1.00 35.30  ? 128  GLN A CB  1 
ATOM   1029 C  CG  . GLN A 1 128 ? -3.034  -2.170  35.066  1.00 33.86  ? 128  GLN A CG  1 
ATOM   1030 C  CD  . GLN A 1 128 ? -4.290  -1.886  35.858  1.00 46.47  ? 128  GLN A CD  1 
ATOM   1031 O  OE1 . GLN A 1 128 ? -5.220  -2.699  35.872  1.00 47.18  ? 128  GLN A OE1 1 
ATOM   1032 N  NE2 . GLN A 1 128 ? -4.334  -0.726  36.518  1.00 49.08  ? 128  GLN A NE2 1 
ATOM   1033 N  N   . LYS A 1 129 ? -1.524  -6.356  33.732  1.00 33.12  ? 129  LYS A N   1 
ATOM   1034 C  CA  . LYS A 1 129 ? -0.914  -7.671  33.933  1.00 30.35  ? 129  LYS A CA  1 
ATOM   1035 C  C   . LYS A 1 129 ? 0.564   -7.659  33.546  1.00 33.43  ? 129  LYS A C   1 
ATOM   1036 O  O   . LYS A 1 129 ? 1.409   -8.207  34.261  1.00 32.70  ? 129  LYS A O   1 
ATOM   1037 C  CB  . LYS A 1 129 ? -1.633  -8.756  33.132  1.00 33.24  ? 129  LYS A CB  1 
ATOM   1038 C  CG  . LYS A 1 129 ? -0.901  -10.109 33.211  1.00 36.36  ? 129  LYS A CG  1 
ATOM   1039 C  CD  . LYS A 1 129 ? -1.677  -11.246 32.561  1.00 36.75  ? 129  LYS A CD  1 
ATOM   1040 C  CE  . LYS A 1 129 ? -0.857  -12.552 32.609  1.00 37.70  ? 129  LYS A CE  1 
ATOM   1041 N  NZ  . LYS A 1 129 ? -1.545  -13.743 32.023  1.00 40.64  ? 129  LYS A NZ  1 
ATOM   1042 N  N   . TRP A 1 130 ? 0.889   -7.054  32.401  1.00 30.91  ? 130  TRP A N   1 
ATOM   1043 C  CA  . TRP A 1 130 ? 2.271   -7.073  31.920  1.00 31.30  ? 130  TRP A CA  1 
ATOM   1044 C  C   . TRP A 1 130 ? 3.168   -6.155  32.746  1.00 35.54  ? 130  TRP A C   1 
ATOM   1045 O  O   . TRP A 1 130 ? 4.333   -6.492  33.004  1.00 32.72  ? 130  TRP A O   1 
ATOM   1046 C  CB  . TRP A 1 130 ? 2.308   -6.690  30.430  1.00 31.40  ? 130  TRP A CB  1 
ATOM   1047 C  CG  . TRP A 1 130 ? 1.715   -7.759  29.545  1.00 32.47  ? 130  TRP A CG  1 
ATOM   1048 C  CD1 . TRP A 1 130 ? 1.189   -8.962  29.944  1.00 33.42  ? 130  TRP A CD1 1 
ATOM   1049 C  CD2 . TRP A 1 130 ? 1.578   -7.714  28.120  1.00 30.00  ? 130  TRP A CD2 1 
ATOM   1050 N  NE1 . TRP A 1 130 ? 0.742   -9.671  28.852  1.00 31.73  ? 130  TRP A NE1 1 
ATOM   1051 C  CE2 . TRP A 1 130 ? 0.976   -8.928  27.719  1.00 32.14  ? 130  TRP A CE2 1 
ATOM   1052 C  CE3 . TRP A 1 130 ? 1.933   -6.779  27.145  1.00 29.82  ? 130  TRP A CE3 1 
ATOM   1053 C  CZ2 . TRP A 1 130 ? 0.702   -9.220  26.390  1.00 33.53  ? 130  TRP A CZ2 1 
ATOM   1054 C  CZ3 . TRP A 1 130 ? 1.660   -7.080  25.803  1.00 31.50  ? 130  TRP A CZ3 1 
ATOM   1055 C  CH2 . TRP A 1 130 ? 1.047   -8.287  25.449  1.00 33.27  ? 130  TRP A CH2 1 
ATOM   1056 N  N   . GLU A 1 131 ? 2.656   -4.981  33.146  1.00 32.54  ? 131  GLU A N   1 
ATOM   1057 C  CA  . GLU A 1 131 ? 3.395   -4.119  34.073  1.00 37.35  ? 131  GLU A CA  1 
ATOM   1058 C  C   . GLU A 1 131 ? 3.755   -4.847  35.363  1.00 36.74  ? 131  GLU A C   1 
ATOM   1059 O  O   . GLU A 1 131 ? 4.759   -4.514  36.010  1.00 32.65  ? 131  GLU A O   1 
ATOM   1060 C  CB  . GLU A 1 131 ? 2.579   -2.868  34.412  1.00 38.02  ? 131  GLU A CB  1 
ATOM   1061 C  CG  . GLU A 1 131 ? 2.276   -1.944  33.232  1.00 38.21  ? 131  GLU A CG  1 
ATOM   1062 C  CD  . GLU A 1 131 ? 3.421   -1.016  32.875  1.00 41.97  ? 131  GLU A CD  1 
ATOM   1063 O  OE1 . GLU A 1 131 ? 4.601   -1.368  33.140  1.00 42.61  ? 131  GLU A OE1 1 
ATOM   1064 O  OE2 . GLU A 1 131 ? 3.142   0.069   32.320  1.00 42.13  ? 131  GLU A OE2 1 
ATOM   1065 N  N   . ARG A 1 132 ? 2.956   -5.833  35.756  1.00 32.43  ? 132  ARG A N   1 
ATOM   1066 C  CA  . ARG A 1 132 ? 3.118   -6.525  37.029  1.00 33.43  ? 132  ARG A CA  1 
ATOM   1067 C  C   . ARG A 1 132 ? 3.969   -7.786  36.954  1.00 37.24  ? 132  ARG A C   1 
ATOM   1068 O  O   . ARG A 1 132 ? 4.161   -8.443  37.984  1.00 34.67  ? 132  ARG A O   1 
ATOM   1069 C  CB  . ARG A 1 132 ? 1.740   -6.863  37.604  1.00 33.72  ? 132  ARG A CB  1 
ATOM   1070 C  CG  . ARG A 1 132 ? 1.084   -5.653  38.205  1.00 33.53  ? 132  ARG A CG  1 
ATOM   1071 C  CD  . ARG A 1 132 ? -0.414  -5.834  38.416  1.00 32.50  ? 132  ARG A CD  1 
ATOM   1072 N  NE  . ARG A 1 132 ? -0.987  -4.568  38.852  1.00 33.41  ? 132  ARG A NE  1 
ATOM   1073 C  CZ  . ARG A 1 132 ? -2.286  -4.319  38.977  1.00 35.35  ? 132  ARG A CZ  1 
ATOM   1074 N  NH1 . ARG A 1 132 ? -3.200  -5.218  38.656  1.00 35.07  ? 132  ARG A NH1 1 
ATOM   1075 N  NH2 . ARG A 1 132 ? -2.674  -3.141  39.452  1.00 37.67  ? 132  ARG A NH2 1 
ATOM   1076 N  N   . LEU A 1 133 ? 4.481   -8.143  35.778  1.00 38.07  ? 133  LEU A N   1 
ATOM   1077 C  CA  . LEU A 1 133 ? 5.372   -9.289  35.680  1.00 32.67  ? 133  LEU A CA  1 
ATOM   1078 C  C   . LEU A 1 133 ? 6.707   -9.000  36.360  1.00 35.59  ? 133  LEU A C   1 
ATOM   1079 O  O   . LEU A 1 133 ? 7.176   -7.858  36.390  1.00 36.96  ? 133  LEU A O   1 
ATOM   1080 C  CB  . LEU A 1 133 ? 5.610   -9.647  34.218  1.00 39.11  ? 133  LEU A CB  1 
ATOM   1081 C  CG  . LEU A 1 133 ? 4.366   -10.195 33.526  1.00 35.67  ? 133  LEU A CG  1 
ATOM   1082 C  CD1 . LEU A 1 133 ? 4.676   -10.616 32.057  1.00 37.21  ? 133  LEU A CD1 1 
ATOM   1083 C  CD2 . LEU A 1 133 ? 3.816   -11.358 34.321  1.00 37.57  ? 133  LEU A CD2 1 
ATOM   1084 N  N   . ASN A 1 134 ? 7.327   -10.048 36.903  1.00 34.54  ? 134  ASN A N   1 
ATOM   1085 C  CA  . ASN A 1 134 ? 8.644   -9.850  37.488  1.00 39.90  ? 134  ASN A CA  1 
ATOM   1086 C  C   . ASN A 1 134 ? 9.715   -9.906  36.404  1.00 42.08  ? 134  ASN A C   1 
ATOM   1087 O  O   . ASN A 1 134 ? 9.467   -10.320 35.272  1.00 41.11  ? 134  ASN A O   1 
ATOM   1088 C  CB  . ASN A 1 134 ? 8.936   -10.898 38.557  1.00 37.78  ? 134  ASN A CB  1 
ATOM   1089 C  CG  . ASN A 1 134 ? 7.898   -10.902 39.648  1.00 38.56  ? 134  ASN A CG  1 
ATOM   1090 O  OD1 . ASN A 1 134 ? 7.803   -9.949  40.423  1.00 36.24  ? 134  ASN A OD1 1 
ATOM   1091 N  ND2 . ASN A 1 134 ? 7.101   -11.971 39.709  1.00 36.24  ? 134  ASN A ND2 1 
ATOM   1092 N  N   . ALA A 1 135 ? 10.925  -9.486  36.780  1.00 43.58  ? 135  ALA A N   1 
ATOM   1093 C  CA  . ALA A 1 135 ? 12.067  -9.511  35.872  1.00 49.78  ? 135  ALA A CA  1 
ATOM   1094 C  C   . ALA A 1 135 ? 12.243  -10.888 35.250  1.00 44.36  ? 135  ALA A C   1 
ATOM   1095 O  O   . ALA A 1 135 ? 12.207  -11.911 35.937  1.00 44.64  ? 135  ALA A O   1 
ATOM   1096 C  CB  . ALA A 1 135 ? 13.340  -9.113  36.625  1.00 50.11  ? 135  ALA A CB  1 
ATOM   1097 N  N   . ASP A 1 136 ? 12.437  -10.922 33.937  1.00 48.06  ? 136  ASP A N   1 
ATOM   1098 C  CA  . ASP A 1 136 ? 12.761  -12.162 33.240  1.00 53.68  ? 136  ASP A CA  1 
ATOM   1099 C  C   . ASP A 1 136 ? 11.636  -13.202 33.291  1.00 55.36  ? 136  ASP A C   1 
ATOM   1100 O  O   . ASP A 1 136 ? 11.844  -14.337 32.830  1.00 56.93  ? 136  ASP A O   1 
ATOM   1101 C  CB  . ASP A 1 136 ? 14.058  -12.794 33.777  1.00 60.31  ? 136  ASP A CB  1 
ATOM   1102 C  CG  . ASP A 1 136 ? 15.307  -11.988 33.405  1.00 66.25  ? 136  ASP A CG  1 
ATOM   1103 O  OD1 . ASP A 1 136 ? 15.244  -11.157 32.466  1.00 65.47  ? 136  ASP A OD1 1 
ATOM   1104 O  OD2 . ASP A 1 136 ? 16.346  -12.162 34.081  1.00 72.15  ? 136  ASP A OD2 1 
ATOM   1105 N  N   . GLU A 1 137 ? 10.462  -12.875 33.839  1.00 47.64  ? 137  GLU A N   1 
ATOM   1106 C  CA  . GLU A 1 137 ? 9.277   -13.619 33.441  1.00 41.59  ? 137  GLU A CA  1 
ATOM   1107 C  C   . GLU A 1 137 ? 8.922   -13.223 32.011  1.00 38.27  ? 137  GLU A C   1 
ATOM   1108 O  O   . GLU A 1 137 ? 9.390   -12.212 31.495  1.00 41.48  ? 137  GLU A O   1 
ATOM   1109 C  CB  . GLU A 1 137 ? 8.102   -13.346 34.387  1.00 39.19  ? 137  GLU A CB  1 
ATOM   1110 C  CG  . GLU A 1 137 ? 8.295   -13.971 35.772  1.00 43.13  ? 137  GLU A CG  1 
ATOM   1111 C  CD  . GLU A 1 137 ? 7.184   -13.633 36.756  1.00 45.90  ? 137  GLU A CD  1 
ATOM   1112 O  OE1 . GLU A 1 137 ? 6.314   -12.783 36.450  1.00 37.66  ? 137  GLU A OE1 1 
ATOM   1113 O  OE2 . GLU A 1 137 ? 7.182   -14.235 37.853  1.00 49.36  ? 137  GLU A OE2 1 
ATOM   1114 N  N   . HIS A 1 138 ? 8.087   -14.022 31.364  1.00 38.59  ? 138  HIS A N   1 
ATOM   1115 C  CA  . HIS A 1 138 ? 7.746   -13.733 29.981  1.00 38.19  ? 138  HIS A CA  1 
ATOM   1116 C  C   . HIS A 1 138 ? 6.235   -13.722 29.809  1.00 35.08  ? 138  HIS A C   1 
ATOM   1117 O  O   . HIS A 1 138 ? 5.474   -14.082 30.707  1.00 35.40  ? 138  HIS A O   1 
ATOM   1118 C  CB  . HIS A 1 138 ? 8.385   -14.741 29.013  1.00 38.28  ? 138  HIS A CB  1 
ATOM   1119 C  CG  . HIS A 1 138 ? 7.947   -16.154 29.237  1.00 38.89  ? 138  HIS A CG  1 
ATOM   1120 N  ND1 . HIS A 1 138 ? 8.674   -17.046 29.995  1.00 45.24  ? 138  HIS A ND1 1 
ATOM   1121 C  CD2 . HIS A 1 138 ? 6.848   -16.824 28.819  1.00 37.66  ? 138  HIS A CD2 1 
ATOM   1122 C  CE1 . HIS A 1 138 ? 8.048   -18.209 30.025  1.00 46.18  ? 138  HIS A CE1 1 
ATOM   1123 N  NE2 . HIS A 1 138 ? 6.936   -18.102 29.319  1.00 42.28  ? 138  HIS A NE2 1 
ATOM   1124 N  N   . ILE A 1 139 ? 5.829   -13.300 28.616  1.00 33.01  ? 139  ILE A N   1 
ATOM   1125 C  CA  . ILE A 1 139 ? 4.431   -13.216 28.221  1.00 35.17  ? 139  ILE A CA  1 
ATOM   1126 C  C   . ILE A 1 139 ? 4.122   -14.402 27.319  1.00 34.20  ? 139  ILE A C   1 
ATOM   1127 O  O   . ILE A 1 139 ? 4.847   -14.657 26.345  1.00 34.45  ? 139  ILE A O   1 
ATOM   1128 C  CB  . ILE A 1 139 ? 4.148   -11.893 27.494  1.00 32.48  ? 139  ILE A CB  1 
ATOM   1129 C  CG1 . ILE A 1 139 ? 4.198   -10.711 28.465  1.00 35.35  ? 139  ILE A CG1 1 
ATOM   1130 C  CG2 . ILE A 1 139 ? 2.819   -11.958 26.726  1.00 33.59  ? 139  ILE A CG2 1 
ATOM   1131 C  CD1 . ILE A 1 139 ? 4.531   -9.407  27.789  1.00 33.31  ? 139  ILE A CD1 1 
ATOM   1132 N  N   . GLU A 1 140 ? 3.048   -15.128 27.641  1.00 32.99  ? 140  GLU A N   1 
ATOM   1133 C  CA  . GLU A 1 140 ? 2.487   -16.144 26.753  1.00 32.55  ? 140  GLU A CA  1 
ATOM   1134 C  C   . GLU A 1 140 ? 1.491   -15.434 25.842  1.00 35.08  ? 140  GLU A C   1 
ATOM   1135 O  O   . GLU A 1 140 ? 0.373   -15.114 26.257  1.00 33.17  ? 140  GLU A O   1 
ATOM   1136 C  CB  . GLU A 1 140 ? 1.827   -17.260 27.557  1.00 34.74  ? 140  GLU A CB  1 
ATOM   1137 C  CG  . GLU A 1 140 ? 2.814   -18.021 28.421  1.00 37.83  ? 140  GLU A CG  1 
ATOM   1138 C  CD  . GLU A 1 140 ? 2.161   -19.130 29.236  1.00 46.15  ? 140  GLU A CD  1 
ATOM   1139 O  OE1 . GLU A 1 140 ? 0.974   -18.997 29.610  1.00 42.12  ? 140  GLU A OE1 1 
ATOM   1140 O  OE2 . GLU A 1 140 ? 2.845   -20.139 29.502  1.00 51.49  ? 140  GLU A OE2 1 
ATOM   1141 N  N   . VAL A 1 141 ? 1.904   -15.161 24.608  1.00 32.22  ? 141  VAL A N   1 
ATOM   1142 C  CA  . VAL A 1 141 ? 1.215   -14.175 23.763  1.00 30.78  ? 141  VAL A CA  1 
ATOM   1143 C  C   . VAL A 1 141 ? -0.179  -14.655 23.357  1.00 32.28  ? 141  VAL A C   1 
ATOM   1144 O  O   . VAL A 1 141 ? -1.167  -13.996 23.700  1.00 33.16  ? 141  VAL A O   1 
ATOM   1145 C  CB  . VAL A 1 141 ? 2.060   -13.817 22.528  1.00 32.85  ? 141  VAL A CB  1 
ATOM   1146 C  CG1 . VAL A 1 141 ? 1.248   -12.949 21.561  1.00 32.61  ? 141  VAL A CG1 1 
ATOM   1147 C  CG2 . VAL A 1 141 ? 3.327   -13.088 22.962  1.00 31.36  ? 141  VAL A CG2 1 
ATOM   1148 N  N   . PRO A 1 142 ? -0.330  -15.765 22.625  1.00 32.10  ? 142  PRO A N   1 
ATOM   1149 C  CA  . PRO A 1 142 ? -1.695  -16.161 22.230  1.00 33.50  ? 142  PRO A CA  1 
ATOM   1150 C  C   . PRO A 1 142 ? -2.620  -16.361 23.417  1.00 32.60  ? 142  PRO A C   1 
ATOM   1151 O  O   . PRO A 1 142 ? -3.832  -16.091 23.326  1.00 30.07  ? 142  PRO A O   1 
ATOM   1152 C  CB  . PRO A 1 142 ? -1.477  -17.463 21.450  1.00 30.77  ? 142  PRO A CB  1 
ATOM   1153 C  CG  . PRO A 1 142 ? -0.076  -17.916 21.818  1.00 34.93  ? 142  PRO A CG  1 
ATOM   1154 C  CD  . PRO A 1 142 ? 0.682   -16.655 22.034  1.00 32.57  ? 142  PRO A CD  1 
ATOM   1155 N  N   . GLU A 1 143 ? -2.077  -16.862 24.522  1.00 31.47  ? 143  GLU A N   1 
ATOM   1156 C  CA  . GLU A 1 143 ? -2.874  -17.078 25.724  1.00 30.78  ? 143  GLU A CA  1 
ATOM   1157 C  C   . GLU A 1 143 ? -3.439  -15.762 26.241  1.00 33.35  ? 143  GLU A C   1 
ATOM   1158 O  O   . GLU A 1 143 ? -4.642  -15.651 26.510  1.00 32.38  ? 143  GLU A O   1 
ATOM   1159 C  CB  . GLU A 1 143 ? -2.014  -17.758 26.796  1.00 32.22  ? 143  GLU A CB  1 
ATOM   1160 C  CG  . GLU A 1 143 ? -1.654  -19.228 26.517  1.00 33.89  ? 143  GLU A CG  1 
ATOM   1161 C  CD  . GLU A 1 143 ? -0.538  -19.436 25.471  1.00 39.55  ? 143  GLU A CD  1 
ATOM   1162 O  OE1 . GLU A 1 143 ? 0.119   -18.472 25.002  1.00 34.97  ? 143  GLU A OE1 1 
ATOM   1163 O  OE2 . GLU A 1 143 ? -0.319  -20.605 25.109  1.00 43.42  ? 143  GLU A OE2 1 
ATOM   1164 N  N   . ASP A 1 144 ? -2.583  -14.742 26.365  1.00 30.09  ? 144  ASP A N   1 
ATOM   1165 C  CA  . ASP A 1 144 ? -3.049  -13.442 26.836  1.00 30.75  ? 144  ASP A CA  1 
ATOM   1166 C  C   . ASP A 1 144 ? -3.905  -12.734 25.793  1.00 31.45  ? 144  ASP A C   1 
ATOM   1167 O  O   . ASP A 1 144 ? -4.831  -11.992 26.153  1.00 31.54  ? 144  ASP A O   1 
ATOM   1168 C  CB  . ASP A 1 144 ? -1.856  -12.558 27.226  1.00 34.78  ? 144  ASP A CB  1 
ATOM   1169 C  CG  . ASP A 1 144 ? -1.392  -12.799 28.666  1.00 38.55  ? 144  ASP A CG  1 
ATOM   1170 O  OD1 . ASP A 1 144 ? -2.142  -13.441 29.433  1.00 33.01  ? 144  ASP A OD1 1 
ATOM   1171 O  OD2 . ASP A 1 144 ? -0.288  -12.328 29.036  1.00 33.75  ? 144  ASP A OD2 1 
ATOM   1172 N  N   . MET A 1 145 ? -3.613  -12.922 24.502  1.00 30.69  ? 145  MET A N   1 
ATOM   1173 C  CA  . MET A 1 145 ? -4.459  -12.287 23.498  1.00 31.53  ? 145  MET A CA  1 
ATOM   1174 C  C   . MET A 1 145 ? -5.860  -12.900 23.547  1.00 31.04  ? 145  MET A C   1 
ATOM   1175 O  O   . MET A 1 145 ? -6.864  -12.212 23.319  1.00 30.56  ? 145  MET A O   1 
ATOM   1176 C  CB  . MET A 1 145 ? -3.806  -12.459 22.116  1.00 28.22  ? 145  MET A CB  1 
ATOM   1177 C  CG  . MET A 1 145 ? -2.540  -11.568 21.959  1.00 29.15  ? 145  MET A CG  1 
ATOM   1178 S  SD  . MET A 1 145 ? -2.705  -9.833  22.357  1.00 34.98  ? 145  MET A SD  1 
ATOM   1179 C  CE  . MET A 1 145 ? -1.970  -9.709  23.991  1.00 38.32  ? 145  MET A CE  1 
ATOM   1180 N  N   . THR A 1 146 ? -5.945  -14.195 23.863  1.00 28.10  ? 146  THR A N   1 
ATOM   1181 C  CA  . THR A 1 146 ? -7.248  -14.856 23.936  1.00 32.52  ? 146  THR A CA  1 
ATOM   1182 C  C   . THR A 1 146 ? -8.007  -14.418 25.178  1.00 33.16  ? 146  THR A C   1 
ATOM   1183 O  O   . THR A 1 146 ? -9.228  -14.213 25.126  1.00 30.43  ? 146  THR A O   1 
ATOM   1184 C  CB  . THR A 1 146 ? -7.055  -16.373 23.904  1.00 34.62  ? 146  THR A CB  1 
ATOM   1185 O  OG1 . THR A 1 146 ? -6.523  -16.751 22.627  1.00 37.92  ? 146  THR A OG1 1 
ATOM   1186 C  CG2 . THR A 1 146 ? -8.387  -17.119 24.132  1.00 34.60  ? 146  THR A CG2 1 
ATOM   1187 N  N   . ARG A 1 147 ? -7.299  -14.247 26.304  1.00 32.37  ? 147  ARG A N   1 
ATOM   1188 C  CA  . ARG A 1 147 ? -7.918  -13.631 27.475  1.00 32.04  ? 147  ARG A CA  1 
ATOM   1189 C  C   . ARG A 1 147 ? -8.538  -12.292 27.114  1.00 30.70  ? 147  ARG A C   1 
ATOM   1190 O  O   . ARG A 1 147 ? -9.703  -12.028 27.427  1.00 33.10  ? 147  ARG A O   1 
ATOM   1191 C  CB  . ARG A 1 147 ? -6.891  -13.449 28.592  1.00 32.38  ? 147  ARG A CB  1 
ATOM   1192 C  CG  . ARG A 1 147 ? -6.411  -14.722 29.213  1.00 34.14  ? 147  ARG A CG  1 
ATOM   1193 C  CD  . ARG A 1 147 ? -5.439  -14.368 30.347  1.00 35.61  ? 147  ARG A CD  1 
ATOM   1194 N  NE  . ARG A 1 147 ? -5.163  -15.516 31.199  1.00 37.31  ? 147  ARG A NE  1 
ATOM   1195 C  CZ  . ARG A 1 147 ? -4.143  -16.346 31.029  1.00 42.27  ? 147  ARG A CZ  1 
ATOM   1196 N  NH1 . ARG A 1 147 ? -3.275  -16.190 30.033  1.00 36.83  ? 147  ARG A NH1 1 
ATOM   1197 N  NH2 . ARG A 1 147 ? -3.983  -17.355 31.881  1.00 45.21  ? 147  ARG A NH2 1 
ATOM   1198 N  N   . LEU A 1 148 ? -7.775  -11.441 26.422  1.00 33.30  ? 148  LEU A N   1 
ATOM   1199 C  CA  . LEU A 1 148 ? -8.265  -10.107 26.088  1.00 32.41  ? 148  LEU A CA  1 
ATOM   1200 C  C   . LEU A 1 148 ? -9.479  -10.168 25.165  1.00 32.59  ? 148  LEU A C   1 
ATOM   1201 O  O   . LEU A 1 148 ? -10.509 -9.535  25.435  1.00 33.26  ? 148  LEU A O   1 
ATOM   1202 C  CB  . LEU A 1 148 ? -7.148  -9.280  25.447  1.00 36.34  ? 148  LEU A CB  1 
ATOM   1203 C  CG  . LEU A 1 148 ? -7.659  -7.900  25.010  1.00 34.55  ? 148  LEU A CG  1 
ATOM   1204 C  CD1 . LEU A 1 148 ? -6.824  -6.785  25.593  1.00 36.10  ? 148  LEU A CD1 1 
ATOM   1205 C  CD2 . LEU A 1 148 ? -7.720  -7.807  23.490  1.00 39.52  ? 148  LEU A CD2 1 
ATOM   1206 N  N   . THR A 1 149 ? -9.381  -10.906 24.054  1.00 28.58  ? 149  THR A N   1 
ATOM   1207 C  CA  . THR A 1 149 ? -10.463 -10.814 23.066  1.00 29.15  ? 149  THR A CA  1 
ATOM   1208 C  C   . THR A 1 149 ? -11.748 -11.474 23.563  1.00 30.01  ? 149  THR A C   1 
ATOM   1209 O  O   . THR A 1 149 ? -12.850 -10.980 23.284  1.00 31.90  ? 149  THR A O   1 
ATOM   1210 C  CB  . THR A 1 149 ? -10.038 -11.401 21.719  1.00 33.26  ? 149  THR A CB  1 
ATOM   1211 O  OG1 . THR A 1 149 ? -9.683  -12.781 21.874  1.00 30.82  ? 149  THR A OG1 1 
ATOM   1212 C  CG2 . THR A 1 149 ? -8.873  -10.610 21.142  1.00 27.78  ? 149  THR A CG2 1 
ATOM   1213 N  N   . LEU A 1 150 ? -11.640 -12.594 24.279  1.00 30.94  ? 150  LEU A N   1 
ATOM   1214 C  CA  . LEU A 1 150 ? -12.827 -13.206 24.878  1.00 31.85  ? 150  LEU A CA  1 
ATOM   1215 C  C   . LEU A 1 150 ? -13.492 -12.241 25.854  1.00 33.72  ? 150  LEU A C   1 
ATOM   1216 O  O   . LEU A 1 150 ? -14.713 -12.037 25.823  1.00 31.46  ? 150  LEU A O   1 
ATOM   1217 C  CB  . LEU A 1 150 ? -12.455 -14.519 25.586  1.00 32.52  ? 150  LEU A CB  1 
ATOM   1218 C  CG  . LEU A 1 150 ? -13.622 -15.134 26.368  1.00 32.35  ? 150  LEU A CG  1 
ATOM   1219 C  CD1 . LEU A 1 150 ? -14.653 -15.648 25.355  1.00 35.27  ? 150  LEU A CD1 1 
ATOM   1220 C  CD2 . LEU A 1 150 ? -13.186 -16.248 27.361  1.00 34.85  ? 150  LEU A CD2 1 
ATOM   1221 N  N   . ASP A 1 151 ? -12.698 -11.624 26.729  1.00 30.15  ? 151  ASP A N   1 
ATOM   1222 C  CA  . ASP A 1 151 ? -13.270 -10.704 27.704  1.00 32.11  ? 151  ASP A CA  1 
ATOM   1223 C  C   . ASP A 1 151 ? -13.881 -9.500  27.011  1.00 31.21  ? 151  ASP A C   1 
ATOM   1224 O  O   . ASP A 1 151 ? -14.926 -9.001  27.436  1.00 34.29  ? 151  ASP A O   1 
ATOM   1225 C  CB  . ASP A 1 151 ? -12.208 -10.271 28.715  1.00 28.52  ? 151  ASP A CB  1 
ATOM   1226 C  CG  . ASP A 1 151 ? -12.051 -11.285 29.850  1.00 29.74  ? 151  ASP A CG  1 
ATOM   1227 O  OD1 . ASP A 1 151 ? -12.295 -12.484 29.611  1.00 34.02  ? 151  ASP A OD1 1 
ATOM   1228 O  OD2 . ASP A 1 151 ? -11.712 -10.874 30.972  1.00 34.71  ? 151  ASP A OD2 1 
ATOM   1229 N  N   . THR A 1 152 ? -13.275 -9.050  25.915  1.00 30.92  ? 152  THR A N   1 
ATOM   1230 C  CA  . THR A 1 152 ? -13.815 -7.887  25.226  1.00 33.43  ? 152  THR A CA  1 
ATOM   1231 C  C   . THR A 1 152 ? -15.179 -8.194  24.602  1.00 33.67  ? 152  THR A C   1 
ATOM   1232 O  O   . THR A 1 152 ? -16.128 -7.414  24.754  1.00 32.81  ? 152  THR A O   1 
ATOM   1233 C  CB  . THR A 1 152 ? -12.806 -7.374  24.190  1.00 30.00  ? 152  THR A CB  1 
ATOM   1234 O  OG1 . THR A 1 152 ? -11.614 -6.958  24.872  1.00 33.05  ? 152  THR A OG1 1 
ATOM   1235 C  CG2 . THR A 1 152 ? -13.370 -6.181  23.420  1.00 35.06  ? 152  THR A CG2 1 
ATOM   1236 N  N   . ILE A 1 153 ? -15.323 -9.331  23.914  1.00 32.66  ? 153  ILE A N   1 
ATOM   1237 C  CA  . ILE A 1 153 ? -16.641 -9.589  23.331  1.00 32.14  ? 153  ILE A CA  1 
ATOM   1238 C  C   . ILE A 1 153 ? -17.661 -9.867  24.430  1.00 34.22  ? 153  ILE A C   1 
ATOM   1239 O  O   . ILE A 1 153 ? -18.831 -9.456  24.325  1.00 31.26  ? 153  ILE A O   1 
ATOM   1240 C  CB  . ILE A 1 153 ? -16.591 -10.726 22.283  1.00 32.90  ? 153  ILE A CB  1 
ATOM   1241 C  CG1 . ILE A 1 153 ? -17.951 -10.861 21.560  1.00 33.01  ? 153  ILE A CG1 1 
ATOM   1242 C  CG2 . ILE A 1 153 ? -16.203 -12.046 22.929  1.00 34.09  ? 153  ILE A CG2 1 
ATOM   1243 C  CD1 . ILE A 1 153 ? -18.368 -9.640  20.781  1.00 35.86  ? 153  ILE A CD1 1 
ATOM   1244 N  N   . GLY A 1 154 ? -17.242 -10.518 25.516  1.00 31.27  ? 154  GLY A N   1 
ATOM   1245 C  CA  . GLY A 1 154 ? -18.165 -10.745 26.628  1.00 33.60  ? 154  GLY A CA  1 
ATOM   1246 C  C   . GLY A 1 154 ? -18.691 -9.447  27.219  1.00 33.02  ? 154  GLY A C   1 
ATOM   1247 O  O   . GLY A 1 154 ? -19.897 -9.287  27.440  1.00 34.92  ? 154  GLY A O   1 
ATOM   1248 N  N   . LEU A 1 155 ? -17.789 -8.506  27.495  1.00 32.38  ? 155  LEU A N   1 
ATOM   1249 C  CA  . LEU A 1 155 ? -18.181 -7.257  28.152  1.00 32.11  ? 155  LEU A CA  1 
ATOM   1250 C  C   . LEU A 1 155 ? -18.900 -6.326  27.181  1.00 35.32  ? 155  LEU A C   1 
ATOM   1251 O  O   . LEU A 1 155 ? -20.020 -5.877  27.450  1.00 37.21  ? 155  LEU A O   1 
ATOM   1252 C  CB  . LEU A 1 155 ? -16.945 -6.573  28.744  1.00 31.27  ? 155  LEU A CB  1 
ATOM   1253 C  CG  . LEU A 1 155 ? -17.203 -5.318  29.587  1.00 31.95  ? 155  LEU A CG  1 
ATOM   1254 C  CD1 . LEU A 1 155 ? -18.160 -5.659  30.735  1.00 33.91  ? 155  LEU A CD1 1 
ATOM   1255 C  CD2 . LEU A 1 155 ? -15.884 -4.743  30.119  1.00 33.85  ? 155  LEU A CD2 1 
ATOM   1256 N  N   . CYS A 1 156 ? -18.282 -6.040  26.033  1.00 34.66  ? 156  CYS A N   1 
ATOM   1257 C  CA  . CYS A 1 156 ? -18.886 -5.116  25.072  1.00 37.87  ? 156  CYS A CA  1 
ATOM   1258 C  C   . CYS A 1 156 ? -20.202 -5.652  24.544  1.00 37.47  ? 156  CYS A C   1 
ATOM   1259 O  O   . CYS A 1 156 ? -21.166 -4.897  24.378  1.00 35.22  ? 156  CYS A O   1 
ATOM   1260 C  CB  . CYS A 1 156 ? -17.943 -4.875  23.898  1.00 32.21  ? 156  CYS A CB  1 
ATOM   1261 S  SG  . CYS A 1 156 ? -16.451 -4.019  24.396  1.00 37.99  ? 156  CYS A SG  1 
ATOM   1262 N  N   . GLY A 1 157 ? -20.251 -6.952  24.250  1.00 33.93  ? 157  GLY A N   1 
ATOM   1263 C  CA  . GLY A 1 157 ? -21.411 -7.503  23.575  1.00 37.64  ? 157  GLY A CA  1 
ATOM   1264 C  C   . GLY A 1 157 ? -22.539 -7.876  24.506  1.00 37.16  ? 157  GLY A C   1 
ATOM   1265 O  O   . GLY A 1 157 ? -23.709 -7.704  24.156  1.00 38.29  ? 157  GLY A O   1 
ATOM   1266 N  N   . PHE A 1 158 ? -22.215 -8.347  25.718  1.00 36.88  ? 158  PHE A N   1 
ATOM   1267 C  CA  . PHE A 1 158 ? -23.202 -8.970  26.597  1.00 35.12  ? 158  PHE A CA  1 
ATOM   1268 C  C   . PHE A 1 158 ? -23.157 -8.491  28.043  1.00 37.21  ? 158  PHE A C   1 
ATOM   1269 O  O   . PHE A 1 158 ? -23.899 -9.026  28.882  1.00 37.27  ? 158  PHE A O   1 
ATOM   1270 C  CB  . PHE A 1 158 ? -23.031 -10.497 26.555  1.00 36.21  ? 158  PHE A CB  1 
ATOM   1271 C  CG  . PHE A 1 158 ? -23.014 -11.029 25.152  1.00 37.19  ? 158  PHE A CG  1 
ATOM   1272 C  CD1 . PHE A 1 158 ? -24.207 -11.250 24.479  1.00 34.46  ? 158  PHE A CD1 1 
ATOM   1273 C  CD2 . PHE A 1 158 ? -21.822 -11.195 24.474  1.00 37.11  ? 158  PHE A CD2 1 
ATOM   1274 C  CE1 . PHE A 1 158 ? -24.215 -11.682 23.167  1.00 34.97  ? 158  PHE A CE1 1 
ATOM   1275 C  CE2 . PHE A 1 158 ? -21.811 -11.636 23.146  1.00 39.00  ? 158  PHE A CE2 1 
ATOM   1276 C  CZ  . PHE A 1 158 ? -23.013 -11.872 22.495  1.00 36.72  ? 158  PHE A CZ  1 
ATOM   1277 N  N   . ASN A 1 159 ? -22.309 -7.520  28.361  1.00 35.29  ? 159  ASN A N   1 
ATOM   1278 C  CA  . ASN A 1 159 ? -22.165 -7.050  29.734  1.00 34.14  ? 159  ASN A CA  1 
ATOM   1279 C  C   . ASN A 1 159 ? -21.865 -8.193  30.694  1.00 39.80  ? 159  ASN A C   1 
ATOM   1280 O  O   . ASN A 1 159 ? -22.374 -8.231  31.814  1.00 36.99  ? 159  ASN A O   1 
ATOM   1281 C  CB  . ASN A 1 159 ? -23.412 -6.289  30.192  1.00 41.16  ? 159  ASN A CB  1 
ATOM   1282 C  CG  . ASN A 1 159 ? -23.097 -5.298  31.285  1.00 50.04  ? 159  ASN A CG  1 
ATOM   1283 O  OD1 . ASN A 1 159 ? -21.960 -4.836  31.388  1.00 41.15  ? 159  ASN A OD1 1 
ATOM   1284 N  ND2 . ASN A 1 159 ? -24.079 -5.003  32.143  1.00 47.28  ? 159  ASN A ND2 1 
ATOM   1285 N  N   . TYR A 1 160 ? -21.026 -9.133  30.260  1.00 36.40  ? 160  TYR A N   1 
ATOM   1286 C  CA  . TYR A 1 160 ? -20.636 -10.274 31.072  1.00 33.08  ? 160  TYR A CA  1 
ATOM   1287 C  C   . TYR A 1 160 ? -19.118 -10.269 31.205  1.00 34.83  ? 160  TYR A C   1 
ATOM   1288 O  O   . TYR A 1 160 ? -18.411 -10.069 30.209  1.00 32.36  ? 160  TYR A O   1 
ATOM   1289 C  CB  . TYR A 1 160 ? -21.122 -11.590 30.451  1.00 37.61  ? 160  TYR A CB  1 
ATOM   1290 C  CG  . TYR A 1 160 ? -20.869 -12.784 31.329  1.00 35.76  ? 160  TYR A CG  1 
ATOM   1291 C  CD1 . TYR A 1 160 ? -21.729 -13.097 32.374  1.00 40.21  ? 160  TYR A CD1 1 
ATOM   1292 C  CD2 . TYR A 1 160 ? -19.766 -13.607 31.112  1.00 36.87  ? 160  TYR A CD2 1 
ATOM   1293 C  CE1 . TYR A 1 160 ? -21.497 -14.185 33.190  1.00 43.62  ? 160  TYR A CE1 1 
ATOM   1294 C  CE2 . TYR A 1 160 ? -19.521 -14.703 31.928  1.00 39.71  ? 160  TYR A CE2 1 
ATOM   1295 C  CZ  . TYR A 1 160 ? -20.395 -14.982 32.969  1.00 43.58  ? 160  TYR A CZ  1 
ATOM   1296 O  OH  . TYR A 1 160 ? -20.172 -16.061 33.787  1.00 43.06  ? 160  TYR A OH  1 
ATOM   1297 N  N   . ARG A 1 161 ? -18.618 -10.460 32.430  1.00 36.37  ? 161  ARG A N   1 
ATOM   1298 C  CA  . ARG A 1 161 ? -17.174 -10.478 32.679  1.00 32.63  ? 161  ARG A CA  1 
ATOM   1299 C  C   . ARG A 1 161 ? -16.709 -11.925 32.799  1.00 31.77  ? 161  ARG A C   1 
ATOM   1300 O  O   . ARG A 1 161 ? -17.018 -12.614 33.775  1.00 33.91  ? 161  ARG A O   1 
ATOM   1301 C  CB  . ARG A 1 161 ? -16.824 -9.656  33.916  1.00 34.10  ? 161  ARG A CB  1 
ATOM   1302 C  CG  . ARG A 1 161 ? -17.032 -8.169  33.659  1.00 34.33  ? 161  ARG A CG  1 
ATOM   1303 C  CD  . ARG A 1 161 ? -16.522 -7.265  34.756  1.00 33.40  ? 161  ARG A CD  1 
ATOM   1304 N  NE  . ARG A 1 161 ? -16.711 -5.859  34.408  1.00 33.62  ? 161  ARG A NE  1 
ATOM   1305 C  CZ  . ARG A 1 161 ? -15.773 -5.070  33.901  1.00 33.04  ? 161  ARG A CZ  1 
ATOM   1306 N  NH1 . ARG A 1 161 ? -14.557 -5.512  33.653  1.00 32.23  ? 161  ARG A NH1 1 
ATOM   1307 N  NH2 . ARG A 1 161 ? -16.058 -3.795  33.657  1.00 33.41  ? 161  ARG A NH2 1 
ATOM   1308 N  N   . PHE A 1 162 ? -15.986 -12.397 31.779  1.00 31.51  ? 162  PHE A N   1 
ATOM   1309 C  CA  . PHE A 1 162 ? -15.327 -13.689 31.864  1.00 33.07  ? 162  PHE A CA  1 
ATOM   1310 C  C   . PHE A 1 162 ? -14.151 -13.656 32.827  1.00 33.27  ? 162  PHE A C   1 
ATOM   1311 O  O   . PHE A 1 162 ? -13.710 -14.716 33.285  1.00 34.28  ? 162  PHE A O   1 
ATOM   1312 C  CB  . PHE A 1 162 ? -14.825 -14.120 30.487  1.00 34.26  ? 162  PHE A CB  1 
ATOM   1313 C  CG  . PHE A 1 162 ? -15.913 -14.552 29.545  1.00 33.34  ? 162  PHE A CG  1 
ATOM   1314 C  CD1 . PHE A 1 162 ? -16.464 -15.814 29.641  1.00 39.11  ? 162  PHE A CD1 1 
ATOM   1315 C  CD2 . PHE A 1 162 ? -16.356 -13.704 28.541  1.00 33.21  ? 162  PHE A CD2 1 
ATOM   1316 C  CE1 . PHE A 1 162 ? -17.460 -16.221 28.765  1.00 44.45  ? 162  PHE A CE1 1 
ATOM   1317 C  CE2 . PHE A 1 162 ? -17.354 -14.106 27.654  1.00 36.42  ? 162  PHE A CE2 1 
ATOM   1318 C  CZ  . PHE A 1 162 ? -17.898 -15.374 27.770  1.00 40.18  ? 162  PHE A CZ  1 
ATOM   1319 N  N   . ASN A 1 163 ? -13.632 -12.466 33.125  1.00 32.70  ? 163  ASN A N   1 
ATOM   1320 C  CA  . ASN A 1 163 ? -12.568 -12.313 34.121  1.00 31.51  ? 163  ASN A CA  1 
ATOM   1321 C  C   . ASN A 1 163 ? -11.391 -13.229 33.804  1.00 34.79  ? 163  ASN A C   1 
ATOM   1322 O  O   . ASN A 1 163 ? -10.804 -13.872 34.682  1.00 33.31  ? 163  ASN A O   1 
ATOM   1323 C  CB  . ASN A 1 163 ? -13.115 -12.536 35.527  1.00 32.01  ? 163  ASN A CB  1 
ATOM   1324 C  CG  . ASN A 1 163 ? -13.926 -11.351 36.000  1.00 30.77  ? 163  ASN A CG  1 
ATOM   1325 O  OD1 . ASN A 1 163 ? -13.498 -10.208 35.833  1.00 33.01  ? 163  ASN A OD1 1 
ATOM   1326 N  ND2 . ASN A 1 163 ? -15.125 -11.603 36.548  1.00 30.42  ? 163  ASN A ND2 1 
ATOM   1327 N  N   . SER A 1 164 ? -11.025 -13.260 32.518  1.00 34.75  ? 164  SER A N   1 
ATOM   1328 C  CA  . SER A 1 164 ? -9.992  -14.179 32.068  1.00 35.37  ? 164  SER A CA  1 
ATOM   1329 C  C   . SER A 1 164 ? -8.641  -13.858 32.682  1.00 37.05  ? 164  SER A C   1 
ATOM   1330 O  O   . SER A 1 164 ? -7.812  -14.764 32.840  1.00 31.67  ? 164  SER A O   1 
ATOM   1331 C  CB  . SER A 1 164 ? -9.891  -14.161 30.536  1.00 34.84  ? 164  SER A CB  1 
ATOM   1332 O  OG  . SER A 1 164 ? -11.060 -14.699 29.944  1.00 33.27  ? 164  SER A OG  1 
ATOM   1333 N  N   . PHE A 1 165 ? -8.383  -12.592 33.007  1.00 32.69  ? 165  PHE A N   1 
ATOM   1334 C  CA  . PHE A 1 165 ? -7.100  -12.244 33.613  1.00 34.49  ? 165  PHE A CA  1 
ATOM   1335 C  C   . PHE A 1 165 ? -7.040  -12.573 35.094  1.00 36.04  ? 165  PHE A C   1 
ATOM   1336 O  O   . PHE A 1 165 ? -5.993  -12.359 35.718  1.00 37.69  ? 165  PHE A O   1 
ATOM   1337 C  CB  . PHE A 1 165 ? -6.791  -10.761 33.399  1.00 32.33  ? 165  PHE A CB  1 
ATOM   1338 C  CG  . PHE A 1 165 ? -6.478  -10.431 31.973  1.00 33.26  ? 165  PHE A CG  1 
ATOM   1339 C  CD1 . PHE A 1 165 ? -5.301  -10.896 31.382  1.00 35.99  ? 165  PHE A CD1 1 
ATOM   1340 C  CD2 . PHE A 1 165 ? -7.368  -9.708  31.208  1.00 32.96  ? 165  PHE A CD2 1 
ATOM   1341 C  CE1 . PHE A 1 165 ? -5.010  -10.614 30.050  1.00 35.08  ? 165  PHE A CE1 1 
ATOM   1342 C  CE2 . PHE A 1 165 ? -7.089  -9.421  29.868  1.00 34.04  ? 165  PHE A CE2 1 
ATOM   1343 C  CZ  . PHE A 1 165 ? -5.897  -9.874  29.294  1.00 32.47  ? 165  PHE A CZ  1 
ATOM   1344 N  N   . TYR A 1 166 ? -8.131  -13.074 35.670  1.00 34.25  ? 166  TYR A N   1 
ATOM   1345 C  CA  . TYR A 1 166 ? -8.123  -13.612 37.027  1.00 38.05  ? 166  TYR A CA  1 
ATOM   1346 C  C   . TYR A 1 166 ? -7.965  -15.121 37.027  1.00 40.21  ? 166  TYR A C   1 
ATOM   1347 O  O   . TYR A 1 166 ? -8.149  -15.755 38.066  1.00 39.95  ? 166  TYR A O   1 
ATOM   1348 C  CB  . TYR A 1 166 ? -9.398  -13.199 37.771  1.00 33.99  ? 166  TYR A CB  1 
ATOM   1349 C  CG  . TYR A 1 166 ? -9.474  -11.712 37.979  1.00 33.71  ? 166  TYR A CG  1 
ATOM   1350 C  CD1 . TYR A 1 166 ? -10.008 -10.874 36.997  1.00 31.43  ? 166  TYR A CD1 1 
ATOM   1351 C  CD2 . TYR A 1 166 ? -8.964  -11.133 39.143  1.00 32.88  ? 166  TYR A CD2 1 
ATOM   1352 C  CE1 . TYR A 1 166 ? -10.059 -9.497  37.179  1.00 31.90  ? 166  TYR A CE1 1 
ATOM   1353 C  CE2 . TYR A 1 166 ? -8.998  -9.779  39.334  1.00 30.29  ? 166  TYR A CE2 1 
ATOM   1354 C  CZ  . TYR A 1 166 ? -9.552  -8.956  38.350  1.00 30.65  ? 166  TYR A CZ  1 
ATOM   1355 O  OH  . TYR A 1 166 ? -9.576  -7.602  38.545  1.00 31.06  ? 166  TYR A OH  1 
ATOM   1356 N  N   . ARG A 1 167 ? -7.597  -15.702 35.881  1.00 36.38  ? 167  ARG A N   1 
ATOM   1357 C  CA  . ARG A 1 167 ? -7.459  -17.139 35.711  1.00 42.52  ? 167  ARG A CA  1 
ATOM   1358 C  C   . ARG A 1 167 ? -6.085  -17.450 35.136  1.00 46.70  ? 167  ARG A C   1 
ATOM   1359 O  O   . ARG A 1 167 ? -5.665  -16.829 34.153  1.00 46.81  ? 167  ARG A O   1 
ATOM   1360 C  CB  . ARG A 1 167 ? -8.538  -17.682 34.780  1.00 43.07  ? 167  ARG A CB  1 
ATOM   1361 C  CG  . ARG A 1 167 ? -9.944  -17.485 35.299  1.00 42.16  ? 167  ARG A CG  1 
ATOM   1362 C  CD  . ARG A 1 167 ? -10.957 -17.795 34.213  1.00 44.37  ? 167  ARG A CD  1 
ATOM   1363 N  NE  . ARG A 1 167 ? -12.250 -17.196 34.509  1.00 48.42  ? 167  ARG A NE  1 
ATOM   1364 C  CZ  . ARG A 1 167 ? -13.202 -17.798 35.205  1.00 52.26  ? 167  ARG A CZ  1 
ATOM   1365 N  NH1 . ARG A 1 167 ? -13.072 -19.055 35.608  1.00 54.35  ? 167  ARG A NH1 1 
ATOM   1366 N  NH2 . ARG A 1 167 ? -14.314 -17.127 35.501  1.00 50.24  ? 167  ARG A NH2 1 
ATOM   1367 N  N   . ASP A 1 168 ? -5.391  -18.405 35.754  1.00 51.65  ? 168  ASP A N   1 
ATOM   1368 C  CA  . ASP A 1 168 ? -4.139  -18.907 35.200  1.00 51.14  ? 168  ASP A CA  1 
ATOM   1369 C  C   . ASP A 1 168 ? -4.372  -19.985 34.154  1.00 53.53  ? 168  ASP A C   1 
ATOM   1370 O  O   . ASP A 1 168 ? -3.502  -20.206 33.304  1.00 56.05  ? 168  ASP A O   1 
ATOM   1371 C  CB  . ASP A 1 168 ? -3.239  -19.422 36.335  1.00 52.74  ? 168  ASP A CB  1 
ATOM   1372 C  CG  . ASP A 1 168 ? -3.900  -20.522 37.152  1.00 61.24  ? 168  ASP A CG  1 
ATOM   1373 O  OD1 . ASP A 1 168 ? -3.967  -21.669 36.663  1.00 70.09  ? 168  ASP A OD1 1 
ATOM   1374 O  OD2 . ASP A 1 168 ? -4.367  -20.239 38.283  1.00 58.46  ? 168  ASP A OD2 1 
ATOM   1375 N  N   . GLN A 1 169 ? -5.532  -20.631 34.188  1.00 55.06  ? 169  GLN A N   1 
ATOM   1376 C  CA  . GLN A 1 169 ? -5.994  -21.596 33.211  1.00 59.06  ? 169  GLN A CA  1 
ATOM   1377 C  C   . GLN A 1 169 ? -7.125  -20.998 32.382  1.00 58.68  ? 169  GLN A C   1 
ATOM   1378 O  O   . GLN A 1 169 ? -7.823  -20.084 32.836  1.00 58.43  ? 169  GLN A O   1 
ATOM   1379 C  CB  . GLN A 1 169 ? -6.482  -22.869 33.917  1.00 65.10  ? 169  GLN A CB  1 
ATOM   1380 C  CG  . GLN A 1 169 ? -5.368  -23.858 34.256  1.00 72.25  ? 169  GLN A CG  1 
ATOM   1381 C  CD  . GLN A 1 169 ? -5.901  -25.211 34.691  1.00 81.15  ? 169  GLN A CD  1 
ATOM   1382 O  OE1 . GLN A 1 169 ? -5.908  -26.169 33.915  1.00 84.18  ? 169  GLN A OE1 1 
ATOM   1383 N  NE2 . GLN A 1 169 ? -6.348  -25.297 35.943  1.00 79.00  ? 169  GLN A NE2 1 
ATOM   1384 N  N   . PRO A 1 170 ? -7.343  -21.494 31.163  1.00 59.92  ? 170  PRO A N   1 
ATOM   1385 C  CA  . PRO A 1 170 ? -8.391  -20.914 30.308  1.00 56.61  ? 170  PRO A CA  1 
ATOM   1386 C  C   . PRO A 1 170 ? -9.775  -21.014 30.940  1.00 56.51  ? 170  PRO A C   1 
ATOM   1387 O  O   . PRO A 1 170 ? -10.071 -21.929 31.714  1.00 52.59  ? 170  PRO A O   1 
ATOM   1388 C  CB  . PRO A 1 170 ? -8.303  -21.747 29.021  1.00 62.47  ? 170  PRO A CB  1 
ATOM   1389 C  CG  . PRO A 1 170 ? -6.930  -22.363 29.049  1.00 59.40  ? 170  PRO A CG  1 
ATOM   1390 C  CD  . PRO A 1 170 ? -6.615  -22.587 30.494  1.00 58.47  ? 170  PRO A CD  1 
ATOM   1391 N  N   . HIS A 1 171 ? -10.634 -20.042 30.603  1.00 54.22  ? 171  HIS A N   1 
ATOM   1392 C  CA  . HIS A 1 171 ? -12.012 -20.070 31.079  1.00 55.85  ? 171  HIS A CA  1 
ATOM   1393 C  C   . HIS A 1 171 ? -12.622 -21.408 30.679  1.00 57.54  ? 171  HIS A C   1 
ATOM   1394 O  O   . HIS A 1 171 ? -12.199 -21.999 29.675  1.00 54.21  ? 171  HIS A O   1 
ATOM   1395 C  CB  . HIS A 1 171 ? -12.821 -18.901 30.498  1.00 47.21  ? 171  HIS A CB  1 
ATOM   1396 C  CG  . HIS A 1 171 ? -14.168 -18.716 31.132  1.00 50.98  ? 171  HIS A CG  1 
ATOM   1397 N  ND1 . HIS A 1 171 ? -15.247 -19.523 30.841  1.00 53.29  ? 171  HIS A ND1 1 
ATOM   1398 C  CD2 . HIS A 1 171 ? -14.609 -17.815 32.042  1.00 45.86  ? 171  HIS A CD2 1 
ATOM   1399 C  CE1 . HIS A 1 171 ? -16.293 -19.135 31.551  1.00 52.11  ? 171  HIS A CE1 1 
ATOM   1400 N  NE2 . HIS A 1 171 ? -15.933 -18.098 32.285  1.00 51.70  ? 171  HIS A NE2 1 
ATOM   1401 N  N   . PRO A 1 172 ? -13.585 -21.930 31.447  1.00 56.76  ? 172  PRO A N   1 
ATOM   1402 C  CA  . PRO A 1 172 ? -14.314 -23.133 30.997  1.00 52.32  ? 172  PRO A CA  1 
ATOM   1403 C  C   . PRO A 1 172 ? -14.773 -23.053 29.549  1.00 59.47  ? 172  PRO A C   1 
ATOM   1404 O  O   . PRO A 1 172 ? -14.608 -24.011 28.772  1.00 49.81  ? 172  PRO A O   1 
ATOM   1405 C  CB  . PRO A 1 172 ? -15.503 -23.183 31.964  1.00 55.31  ? 172  PRO A CB  1 
ATOM   1406 C  CG  . PRO A 1 172 ? -14.978 -22.583 33.213  1.00 56.53  ? 172  PRO A CG  1 
ATOM   1407 C  CD  . PRO A 1 172 ? -13.970 -21.527 32.811  1.00 53.08  ? 172  PRO A CD  1 
ATOM   1408 N  N   . PHE A 1 173 ? -15.363 -21.919 29.168  1.00 53.41  ? 173  PHE A N   1 
ATOM   1409 C  CA  . PHE A 1 173 ? -15.850 -21.759 27.806  1.00 49.23  ? 173  PHE A CA  1 
ATOM   1410 C  C   . PHE A 1 173 ? -14.725 -22.018 26.810  1.00 51.04  ? 173  PHE A C   1 
ATOM   1411 O  O   . PHE A 1 173 ? -14.847 -22.870 25.923  1.00 53.23  ? 173  PHE A O   1 
ATOM   1412 C  CB  . PHE A 1 173 ? -16.438 -20.355 27.642  1.00 53.26  ? 173  PHE A CB  1 
ATOM   1413 C  CG  . PHE A 1 173 ? -17.220 -20.164 26.375  1.00 51.89  ? 173  PHE A CG  1 
ATOM   1414 C  CD1 . PHE A 1 173 ? -16.591 -19.768 25.201  1.00 55.94  ? 173  PHE A CD1 1 
ATOM   1415 C  CD2 . PHE A 1 173 ? -18.592 -20.391 26.357  1.00 44.52  ? 173  PHE A CD2 1 
ATOM   1416 C  CE1 . PHE A 1 173 ? -17.320 -19.597 24.022  1.00 51.02  ? 173  PHE A CE1 1 
ATOM   1417 C  CE2 . PHE A 1 173 ? -19.324 -20.221 25.191  1.00 49.28  ? 173  PHE A CE2 1 
ATOM   1418 C  CZ  . PHE A 1 173 ? -18.687 -19.824 24.023  1.00 50.41  ? 173  PHE A CZ  1 
ATOM   1419 N  N   . ILE A 1 174 ? -13.595 -21.327 26.981  1.00 48.84  ? 174  ILE A N   1 
ATOM   1420 C  CA  . ILE A 1 174 ? -12.471 -21.465 26.052  1.00 51.58  ? 174  ILE A CA  1 
ATOM   1421 C  C   . ILE A 1 174 ? -12.045 -22.927 25.907  1.00 57.28  ? 174  ILE A C   1 
ATOM   1422 O  O   . ILE A 1 174 ? -11.720 -23.395 24.802  1.00 54.45  ? 174  ILE A O   1 
ATOM   1423 C  CB  . ILE A 1 174 ? -11.292 -20.580 26.510  1.00 54.02  ? 174  ILE A CB  1 
ATOM   1424 C  CG1 . ILE A 1 174 ? -11.590 -19.093 26.269  1.00 48.71  ? 174  ILE A CG1 1 
ATOM   1425 C  CG2 . ILE A 1 174 ? -9.987  -21.008 25.811  1.00 52.40  ? 174  ILE A CG2 1 
ATOM   1426 C  CD1 . ILE A 1 174 ? -11.789 -18.714 24.777  1.00 38.72  ? 174  ILE A CD1 1 
ATOM   1427 N  N   . THR A 1 175 ? -12.017 -23.666 27.022  1.00 56.57  ? 175  THR A N   1 
ATOM   1428 C  CA  . THR A 1 175 ? -11.559 -25.054 26.985  1.00 58.31  ? 175  THR A CA  1 
ATOM   1429 C  C   . THR A 1 175 ? -12.518 -25.928 26.185  1.00 56.33  ? 175  THR A C   1 
ATOM   1430 O  O   . THR A 1 175 ? -12.090 -26.721 25.337  1.00 53.91  ? 175  THR A O   1 
ATOM   1431 C  CB  . THR A 1 175 ? -11.397 -25.598 28.403  1.00 56.97  ? 175  THR A CB  1 
ATOM   1432 O  OG1 . THR A 1 175 ? -10.368 -24.868 29.086  1.00 57.16  ? 175  THR A OG1 1 
ATOM   1433 C  CG2 . THR A 1 175 ? -11.028 -27.075 28.362  1.00 61.29  ? 175  THR A CG2 1 
ATOM   1434 N  N   . SER A 1 176 ? -13.820 -25.807 26.456  1.00 50.95  ? 176  SER A N   1 
ATOM   1435 C  CA  . SER A 1 176 ? -14.811 -26.515 25.655  1.00 57.48  ? 176  SER A CA  1 
ATOM   1436 C  C   . SER A 1 176 ? -14.737 -26.086 24.189  1.00 56.09  ? 176  SER A C   1 
ATOM   1437 O  O   . SER A 1 176 ? -14.611 -26.928 23.295  1.00 52.95  ? 176  SER A O   1 
ATOM   1438 C  CB  . SER A 1 176 ? -16.207 -26.276 26.229  1.00 58.95  ? 176  SER A CB  1 
ATOM   1439 O  OG  . SER A 1 176 ? -16.311 -26.834 27.521  1.00 53.45  ? 176  SER A OG  1 
ATOM   1440 N  N   . MET A 1 177 ? -14.797 -24.772 23.931  1.00 47.54  ? 177  MET A N   1 
ATOM   1441 C  CA  . MET A 1 177 ? -14.737 -24.263 22.564  1.00 51.34  ? 177  MET A CA  1 
ATOM   1442 C  C   . MET A 1 177 ? -13.572 -24.854 21.787  1.00 53.61  ? 177  MET A C   1 
ATOM   1443 O  O   . MET A 1 177 ? -13.737 -25.328 20.653  1.00 52.01  ? 177  MET A O   1 
ATOM   1444 C  CB  . MET A 1 177 ? -14.595 -22.742 22.555  1.00 52.20  ? 177  MET A CB  1 
ATOM   1445 C  CG  . MET A 1 177 ? -14.582 -22.197 21.122  1.00 52.67  ? 177  MET A CG  1 
ATOM   1446 S  SD  . MET A 1 177 ? -14.065 -20.477 20.983  1.00 51.26  ? 177  MET A SD  1 
ATOM   1447 C  CE  . MET A 1 177 ? -12.282 -20.653 21.155  1.00 50.07  ? 177  MET A CE  1 
ATOM   1448 N  N   . VAL A 1 178 ? -12.367 -24.782 22.358  1.00 46.40  ? 178  VAL A N   1 
ATOM   1449 C  CA  . VAL A 1 178 ? -11.206 -25.273 21.626  1.00 55.29  ? 178  VAL A CA  1 
ATOM   1450 C  C   . VAL A 1 178 ? -11.379 -26.756 21.336  1.00 57.60  ? 178  VAL A C   1 
ATOM   1451 O  O   . VAL A 1 178 ? -10.937 -27.254 20.292  1.00 56.98  ? 178  VAL A O   1 
ATOM   1452 C  CB  . VAL A 1 178 ? -9.908  -24.986 22.409  1.00 53.05  ? 178  VAL A CB  1 
ATOM   1453 C  CG1 . VAL A 1 178 ? -8.755  -25.865 21.891  1.00 53.64  ? 178  VAL A CG1 1 
ATOM   1454 C  CG2 . VAL A 1 178 ? -9.559  -23.500 22.346  1.00 53.78  ? 178  VAL A CG2 1 
ATOM   1455 N  N   . ARG A 1 179 ? -12.063 -27.474 22.235  1.00 56.25  ? 179  ARG A N   1 
ATOM   1456 C  CA  . ARG A 1 179 ? -12.278 -28.910 22.076  1.00 57.45  ? 179  ARG A CA  1 
ATOM   1457 C  C   . ARG A 1 179 ? -13.341 -29.208 21.024  1.00 56.69  ? 179  ARG A C   1 
ATOM   1458 O  O   . ARG A 1 179 ? -13.170 -30.124 20.210  1.00 55.51  ? 179  ARG A O   1 
ATOM   1459 C  CB  . ARG A 1 179 ? -12.666 -29.527 23.417  1.00 57.54  ? 179  ARG A CB  1 
ATOM   1460 C  CG  . ARG A 1 179 ? -11.858 -30.757 23.782  1.00 64.18  ? 179  ARG A CG  1 
ATOM   1461 C  CD  . ARG A 1 179 ? -11.588 -30.814 25.282  1.00 67.19  ? 179  ARG A CD  1 
ATOM   1462 N  NE  . ARG A 1 179 ? -12.807 -30.792 26.085  1.00 63.97  ? 179  ARG A NE  1 
ATOM   1463 C  CZ  . ARG A 1 179 ? -12.819 -30.804 27.411  1.00 70.53  ? 179  ARG A CZ  1 
ATOM   1464 N  NH1 . ARG A 1 179 ? -11.693 -30.805 28.111  1.00 69.35  ? 179  ARG A NH1 1 
ATOM   1465 N  NH2 . ARG A 1 179 ? -13.986 -30.810 28.052  1.00 64.40  ? 179  ARG A NH2 1 
ATOM   1466 N  N   . ALA A 1 180 ? -14.448 -28.459 21.036  1.00 55.54  ? 180  ALA A N   1 
ATOM   1467 C  CA  . ALA A 1 180 ? -15.437 -28.590 19.971  1.00 51.28  ? 180  ALA A CA  1 
ATOM   1468 C  C   . ALA A 1 180 ? -14.815 -28.305 18.610  1.00 54.76  ? 180  ALA A C   1 
ATOM   1469 O  O   . ALA A 1 180 ? -15.093 -29.010 17.631  1.00 51.80  ? 180  ALA A O   1 
ATOM   1470 C  CB  . ALA A 1 180 ? -16.612 -27.655 20.231  1.00 53.58  ? 180  ALA A CB  1 
ATOM   1471 N  N   . LEU A 1 181 ? -13.962 -27.276 18.533  1.00 49.51  ? 181  LEU A N   1 
ATOM   1472 C  CA  . LEU A 1 181 ? -13.314 -26.929 17.271  1.00 52.42  ? 181  LEU A CA  1 
ATOM   1473 C  C   . LEU A 1 181 ? -12.285 -27.980 16.878  1.00 52.34  ? 181  LEU A C   1 
ATOM   1474 O  O   . LEU A 1 181 ? -12.179 -28.341 15.697  1.00 51.19  ? 181  LEU A O   1 
ATOM   1475 C  CB  . LEU A 1 181 ? -12.659 -25.548 17.368  1.00 50.37  ? 181  LEU A CB  1 
ATOM   1476 C  CG  . LEU A 1 181 ? -13.576 -24.342 17.588  1.00 51.44  ? 181  LEU A CG  1 
ATOM   1477 C  CD1 . LEU A 1 181 ? -12.745 -23.089 17.843  1.00 50.02  ? 181  LEU A CD1 1 
ATOM   1478 C  CD2 . LEU A 1 181 ? -14.508 -24.144 16.386  1.00 52.53  ? 181  LEU A CD2 1 
ATOM   1479 N  N   A ASP A 1 182 ? -11.504 -28.467 17.849  0.50 53.91  ? 182  ASP A N   1 
ATOM   1480 N  N   B ASP A 1 182 ? -11.507 -28.474 17.847  0.50 53.91  ? 182  ASP A N   1 
ATOM   1481 C  CA  A ASP A 1 182 ? -10.611 -29.593 17.590  0.50 56.42  ? 182  ASP A CA  1 
ATOM   1482 C  CA  B ASP A 1 182 ? -10.608 -29.591 17.570  0.50 56.42  ? 182  ASP A CA  1 
ATOM   1483 C  C   A ASP A 1 182 ? -11.388 -30.776 17.031  0.50 53.52  ? 182  ASP A C   1 
ATOM   1484 C  C   B ASP A 1 182 ? -11.381 -30.788 17.036  0.50 53.52  ? 182  ASP A C   1 
ATOM   1485 O  O   A ASP A 1 182 ? -10.989 -31.386 16.033  0.50 55.37  ? 182  ASP A O   1 
ATOM   1486 O  O   B ASP A 1 182 ? -10.972 -31.422 16.056  0.50 55.37  ? 182  ASP A O   1 
ATOM   1487 C  CB  A ASP A 1 182 ? -9.879  -30.002 18.872  0.50 56.62  ? 182  ASP A CB  1 
ATOM   1488 C  CB  B ASP A 1 182 ? -9.829  -29.977 18.830  0.50 56.62  ? 182  ASP A CB  1 
ATOM   1489 C  CG  A ASP A 1 182 ? -8.767  -29.042 19.246  0.50 60.06  ? 182  ASP A CG  1 
ATOM   1490 C  CG  B ASP A 1 182 ? -8.687  -29.024 19.126  0.50 60.06  ? 182  ASP A CG  1 
ATOM   1491 O  OD1 A ASP A 1 182 ? -8.197  -28.398 18.340  0.50 62.23  ? 182  ASP A OD1 1 
ATOM   1492 O  OD1 B ASP A 1 182 ? -8.150  -28.423 18.171  0.50 62.29  ? 182  ASP A OD1 1 
ATOM   1493 O  OD2 A ASP A 1 182 ? -8.461  -28.932 20.454  0.50 62.79  ? 182  ASP A OD2 1 
ATOM   1494 O  OD2 B ASP A 1 182 ? -8.326  -28.875 20.314  0.50 62.76  ? 182  ASP A OD2 1 
ATOM   1495 N  N   . GLU A 1 183 ? -12.506 -31.115 17.675  1.00 49.50  ? 183  GLU A N   1 
ATOM   1496 C  CA  . GLU A 1 183 ? -13.313 -32.238 17.217  1.00 55.43  ? 183  GLU A CA  1 
ATOM   1497 C  C   . GLU A 1 183 ? -13.829 -31.992 15.803  1.00 54.66  ? 183  GLU A C   1 
ATOM   1498 O  O   . GLU A 1 183 ? -13.803 -32.897 14.958  1.00 50.56  ? 183  GLU A O   1 
ATOM   1499 C  CB  . GLU A 1 183 ? -14.457 -32.479 18.207  1.00 51.95  ? 183  GLU A CB  1 
ATOM   1500 C  CG  . GLU A 1 183 ? -15.606 -33.341 17.699  1.00 59.88  ? 183  GLU A CG  1 
ATOM   1501 C  CD  . GLU A 1 183 ? -15.259 -34.819 17.565  1.00 59.00  ? 183  GLU A CD  1 
ATOM   1502 O  OE1 . GLU A 1 183 ? -14.093 -35.191 17.804  1.00 51.49  ? 183  GLU A OE1 1 
ATOM   1503 O  OE2 . GLU A 1 183 ? -16.161 -35.604 17.199  1.00 52.49  ? 183  GLU A OE2 1 
ATOM   1504 N  N   . ALA A 1 184 ? -14.259 -30.757 15.517  1.00 54.57  ? 184  ALA A N   1 
ATOM   1505 C  CA  . ALA A 1 184 ? -14.764 -30.438 14.187  1.00 47.67  ? 184  ALA A CA  1 
ATOM   1506 C  C   . ALA A 1 184 ? -13.669 -30.551 13.133  1.00 53.01  ? 184  ALA A C   1 
ATOM   1507 O  O   . ALA A 1 184 ? -13.914 -31.062 12.032  1.00 48.98  ? 184  ALA A O   1 
ATOM   1508 C  CB  . ALA A 1 184 ? -15.374 -29.038 14.178  1.00 51.86  ? 184  ALA A CB  1 
ATOM   1509 N  N   . MET A 1 185 ? -12.459 -30.068 13.437  1.00 47.64  ? 185  MET A N   1 
ATOM   1510 C  CA  . MET A 1 185 ? -11.380 -30.166 12.459  1.00 50.77  ? 185  MET A CA  1 
ATOM   1511 C  C   . MET A 1 185 ? -10.943 -31.618 12.284  1.00 50.77  ? 185  MET A C   1 
ATOM   1512 O  O   . MET A 1 185 ? -10.703 -32.073 11.156  1.00 48.46  ? 185  MET A O   1 
ATOM   1513 C  CB  . MET A 1 185 ? -10.190 -29.293 12.878  1.00 49.10  ? 185  MET A CB  1 
ATOM   1514 C  CG  . MET A 1 185 ? -9.007  -29.328 11.885  1.00 41.45  ? 185  MET A CG  1 
ATOM   1515 S  SD  . MET A 1 185 ? -7.625  -28.240 12.339  1.00 48.59  ? 185  MET A SD  1 
ATOM   1516 C  CE  . MET A 1 185 ? -6.722  -29.273 13.495  1.00 48.21  ? 185  MET A CE  1 
ATOM   1517 N  N   . ASN A 1 186 ? -10.850 -32.370 13.390  1.00 51.49  ? 186  ASN A N   1 
ATOM   1518 C  CA  . ASN A 1 186 ? -10.463 -33.774 13.287  1.00 50.96  ? 186  ASN A CA  1 
ATOM   1519 C  C   . ASN A 1 186 ? -11.543 -34.608 12.614  1.00 48.75  ? 186  ASN A C   1 
ATOM   1520 O  O   . ASN A 1 186 ? -11.226 -35.560 11.897  1.00 52.39  ? 186  ASN A O   1 
ATOM   1521 C  CB  . ASN A 1 186 ? -10.137 -34.350 14.667  1.00 51.44  ? 186  ASN A CB  1 
ATOM   1522 C  CG  . ASN A 1 186 ? -9.602  -35.782 14.588  1.00 58.05  ? 186  ASN A CG  1 
ATOM   1523 O  OD1 . ASN A 1 186 ? -10.359 -36.754 14.714  1.00 56.65  ? 186  ASN A OD1 1 
ATOM   1524 N  ND2 . ASN A 1 186 ? -8.298  -35.916 14.359  1.00 52.83  ? 186  ASN A ND2 1 
ATOM   1525 N  N   . LYS A 1 187 ? -12.817 -34.267 12.816  1.00 49.16  ? 187  LYS A N   1 
ATOM   1526 C  CA  . LYS A 1 187 ? -13.890 -34.995 12.149  1.00 51.08  ? 187  LYS A CA  1 
ATOM   1527 C  C   . LYS A 1 187 ? -13.889 -34.800 10.633  1.00 48.95  ? 187  LYS A C   1 
ATOM   1528 O  O   . LYS A 1 187 ? -14.542 -35.575 9.925   1.00 49.11  ? 187  LYS A O   1 
ATOM   1529 C  CB  . LYS A 1 187 ? -15.240 -34.574 12.737  1.00 51.26  ? 187  LYS A CB  1 
ATOM   1530 C  CG  . LYS A 1 187 ? -16.328 -35.629 12.596  1.00 54.91  ? 187  LYS A CG  1 
ATOM   1531 C  CD  . LYS A 1 187 ? -17.705 -35.068 12.923  1.00 57.95  ? 187  LYS A CD  1 
ATOM   1532 C  CE  . LYS A 1 187 ? -17.785 -34.581 14.363  1.00 55.00  ? 187  LYS A CE  1 
ATOM   1533 N  NZ  . LYS A 1 187 ? -19.153 -34.059 14.701  1.00 58.36  ? 187  LYS A NZ  1 
ATOM   1534 N  N   . LEU A 1 188 ? -13.166 -33.801 10.122  1.00 49.45  ? 188  LEU A N   1 
ATOM   1535 C  CA  . LEU A 1 188 ? -13.124 -33.565 8.682   1.00 49.10  ? 188  LEU A CA  1 
ATOM   1536 C  C   . LEU A 1 188 ? -12.587 -34.778 7.929   1.00 50.51  ? 188  LEU A C   1 
ATOM   1537 O  O   . LEU A 1 188 ? -13.055 -35.087 6.827   1.00 50.45  ? 188  LEU A O   1 
ATOM   1538 C  CB  . LEU A 1 188 ? -12.263 -32.338 8.375   1.00 45.43  ? 188  LEU A CB  1 
ATOM   1539 C  CG  . LEU A 1 188 ? -12.836 -31.005 8.853   1.00 49.07  ? 188  LEU A CG  1 
ATOM   1540 C  CD1 . LEU A 1 188 ? -11.810 -29.890 8.641   1.00 48.86  ? 188  LEU A CD1 1 
ATOM   1541 C  CD2 . LEU A 1 188 ? -14.151 -30.701 8.130   1.00 44.52  ? 188  LEU A CD2 1 
ATOM   1542 N  N   . GLN A 1 189 ? -11.594 -35.464 8.491   1.00 54.69  ? 189  GLN A N   1 
ATOM   1543 C  CA  . GLN A 1 189 ? -10.964 -36.577 7.788   1.00 54.94  ? 189  GLN A CA  1 
ATOM   1544 C  C   . GLN A 1 189 ? -11.575 -37.932 8.124   1.00 60.18  ? 189  GLN A C   1 
ATOM   1545 O  O   . GLN A 1 189 ? -11.201 -38.929 7.495   1.00 61.96  ? 189  GLN A O   1 
ATOM   1546 C  CB  . GLN A 1 189 ? -9.456  -36.617 8.084   1.00 54.15  ? 189  GLN A CB  1 
ATOM   1547 C  CG  . GLN A 1 189 ? -9.104  -36.488 9.554   1.00 51.82  ? 189  GLN A CG  1 
ATOM   1548 C  CD  . GLN A 1 189 ? -9.114  -37.821 10.283  1.00 61.63  ? 189  GLN A CD  1 
ATOM   1549 O  OE1 . GLN A 1 189 ? -8.486  -38.787 9.846   1.00 67.47  ? 189  GLN A OE1 1 
ATOM   1550 N  NE2 . GLN A 1 189 ? -9.818  -37.875 11.406  1.00 61.36  ? 189  GLN A NE2 1 
ATOM   1551 N  N   . ARG A 1 190 ? -12.501 -38.002 9.083   1.00 59.28  ? 190  ARG A N   1 
ATOM   1552 C  CA  . ARG A 1 190 ? -13.064 -39.286 9.487   1.00 59.48  ? 190  ARG A CA  1 
ATOM   1553 C  C   . ARG A 1 190 ? -13.941 -39.845 8.379   1.00 63.69  ? 190  ARG A C   1 
ATOM   1554 O  O   . ARG A 1 190 ? -14.930 -39.217 7.985   1.00 65.67  ? 190  ARG A O   1 
ATOM   1555 C  CB  . ARG A 1 190 ? -13.873 -39.142 10.772  1.00 61.75  ? 190  ARG A CB  1 
ATOM   1556 C  CG  . ARG A 1 190 ? -13.040 -39.137 12.024  1.00 61.67  ? 190  ARG A CG  1 
ATOM   1557 C  CD  . ARG A 1 190 ? -13.919 -38.964 13.238  1.00 56.98  ? 190  ARG A CD  1 
ATOM   1558 N  NE  . ARG A 1 190 ? -13.239 -38.216 14.284  1.00 54.25  ? 190  ARG A NE  1 
ATOM   1559 C  CZ  . ARG A 1 190 ? -13.855 -37.663 15.317  1.00 54.53  ? 190  ARG A CZ  1 
ATOM   1560 N  NH1 . ARG A 1 190 ? -15.167 -37.765 15.475  1.00 51.41  ? 190  ARG A NH1 1 
ATOM   1561 N  NH2 . ARG A 1 190 ? -13.140 -36.995 16.215  1.00 55.51  ? 190  ARG A NH2 1 
ATOM   1562 N  N   . ALA A 1 191 ? -13.585 -41.033 7.882   1.00 67.43  ? 191  ALA A N   1 
ATOM   1563 C  CA  . ALA A 1 191 ? -14.354 -41.642 6.802   1.00 70.56  ? 191  ALA A CA  1 
ATOM   1564 C  C   . ALA A 1 191 ? -15.601 -42.354 7.319   1.00 73.03  ? 191  ALA A C   1 
ATOM   1565 O  O   . ALA A 1 191 ? -16.585 -42.487 6.579   1.00 72.57  ? 191  ALA A O   1 
ATOM   1566 C  CB  . ALA A 1 191 ? -13.468 -42.609 6.011   1.00 70.00  ? 191  ALA A CB  1 
ATOM   1567 N  N   . ASN A 1 192 ? -15.584 -42.812 8.573   1.00 71.09  ? 192  ASN A N   1 
ATOM   1568 C  CA  . ASN A 1 192 ? -16.740 -43.449 9.208   1.00 75.25  ? 192  ASN A CA  1 
ATOM   1569 C  C   . ASN A 1 192 ? -16.941 -42.842 10.590  1.00 71.44  ? 192  ASN A C   1 
ATOM   1570 O  O   . ASN A 1 192 ? -16.558 -43.439 11.606  1.00 71.77  ? 192  ASN A O   1 
ATOM   1571 C  CB  . ASN A 1 192 ? -16.564 -44.966 9.289   1.00 76.68  ? 192  ASN A CB  1 
ATOM   1572 C  CG  . ASN A 1 192 ? -16.161 -45.575 7.963   1.00 81.29  ? 192  ASN A CG  1 
ATOM   1573 O  OD1 . ASN A 1 192 ? -15.098 -46.187 7.846   1.00 82.83  ? 192  ASN A OD1 1 
ATOM   1574 N  ND2 . ASN A 1 192 ? -17.006 -45.399 6.947   1.00 78.03  ? 192  ASN A ND2 1 
ATOM   1575 N  N   . PRO A 1 193 ? -17.565 -41.663 10.669  1.00 71.76  ? 193  PRO A N   1 
ATOM   1576 C  CA  . PRO A 1 193 ? -17.787 -41.051 11.987  1.00 71.75  ? 193  PRO A CA  1 
ATOM   1577 C  C   . PRO A 1 193 ? -18.741 -41.840 12.863  1.00 72.45  ? 193  PRO A C   1 
ATOM   1578 O  O   . PRO A 1 193 ? -18.745 -41.626 14.081  1.00 71.50  ? 193  PRO A O   1 
ATOM   1579 C  CB  . PRO A 1 193 ? -18.350 -39.665 11.648  1.00 66.49  ? 193  PRO A CB  1 
ATOM   1580 C  CG  . PRO A 1 193 ? -18.861 -39.770 10.231  1.00 70.45  ? 193  PRO A CG  1 
ATOM   1581 C  CD  . PRO A 1 193 ? -18.451 -41.092 9.643   1.00 68.55  ? 193  PRO A CD  1 
ATOM   1582 N  N   . ASP A 1 194 ? -19.544 -42.741 12.286  1.00 72.73  ? 194  ASP A N   1 
ATOM   1583 C  CA  . ASP A 1 194 ? -20.423 -43.605 13.065  1.00 73.57  ? 194  ASP A CA  1 
ATOM   1584 C  C   . ASP A 1 194 ? -19.708 -44.815 13.647  1.00 73.86  ? 194  ASP A C   1 
ATOM   1585 O  O   . ASP A 1 194 ? -20.316 -45.550 14.433  1.00 76.07  ? 194  ASP A O   1 
ATOM   1586 C  CB  . ASP A 1 194 ? -21.603 -44.090 12.214  1.00 75.95  ? 194  ASP A CB  1 
ATOM   1587 C  CG  . ASP A 1 194 ? -22.630 -43.005 11.963  1.00 79.40  ? 194  ASP A CG  1 
ATOM   1588 O  OD1 . ASP A 1 194 ? -22.671 -42.026 12.740  1.00 77.72  ? 194  ASP A OD1 1 
ATOM   1589 O  OD2 . ASP A 1 194 ? -23.404 -43.141 10.991  1.00 81.95  ? 194  ASP A OD2 1 
ATOM   1590 N  N   . ASP A 1 195 ? -18.455 -45.048 13.286  1.00 71.45  ? 195  ASP A N   1 
ATOM   1591 C  CA  . ASP A 1 195 ? -17.704 -46.151 13.870  1.00 74.49  ? 195  ASP A CA  1 
ATOM   1592 C  C   . ASP A 1 195 ? -17.660 -46.008 15.388  1.00 76.29  ? 195  ASP A C   1 
ATOM   1593 O  O   . ASP A 1 195 ? -17.175 -44.983 15.892  1.00 72.04  ? 195  ASP A O   1 
ATOM   1594 C  CB  . ASP A 1 195 ? -16.290 -46.191 13.303  1.00 73.91  ? 195  ASP A CB  1 
ATOM   1595 C  CG  . ASP A 1 195 ? -15.474 -47.335 13.860  1.00 77.47  ? 195  ASP A CG  1 
ATOM   1596 O  OD1 . ASP A 1 195 ? -15.878 -48.498 13.661  1.00 82.33  ? 195  ASP A OD1 1 
ATOM   1597 O  OD2 . ASP A 1 195 ? -14.431 -47.074 14.494  1.00 79.10  ? 195  ASP A OD2 1 
ATOM   1598 N  N   . PRO A 1 196 ? -18.126 -47.002 16.151  1.00 79.63  ? 196  PRO A N   1 
ATOM   1599 C  CA  . PRO A 1 196 ? -18.167 -46.854 17.619  1.00 76.40  ? 196  PRO A CA  1 
ATOM   1600 C  C   . PRO A 1 196 ? -16.834 -46.466 18.254  1.00 71.78  ? 196  PRO A C   1 
ATOM   1601 O  O   . PRO A 1 196 ? -16.819 -46.114 19.441  1.00 69.96  ? 196  PRO A O   1 
ATOM   1602 C  CB  . PRO A 1 196 ? -18.636 -48.236 18.099  1.00 77.84  ? 196  PRO A CB  1 
ATOM   1603 C  CG  . PRO A 1 196 ? -19.384 -48.799 16.936  1.00 78.11  ? 196  PRO A CG  1 
ATOM   1604 C  CD  . PRO A 1 196 ? -18.662 -48.300 15.710  1.00 77.79  ? 196  PRO A CD  1 
ATOM   1605 N  N   . ALA A 1 197 ? -15.721 -46.505 17.516  1.00 72.88  ? 197  ALA A N   1 
ATOM   1606 C  CA  . ALA A 1 197 ? -14.466 -45.978 18.045  1.00 72.82  ? 197  ALA A CA  1 
ATOM   1607 C  C   . ALA A 1 197 ? -14.577 -44.506 18.426  1.00 68.42  ? 197  ALA A C   1 
ATOM   1608 O  O   . ALA A 1 197 ? -13.747 -44.005 19.193  1.00 67.38  ? 197  ALA A O   1 
ATOM   1609 C  CB  . ALA A 1 197 ? -13.342 -46.158 17.023  1.00 70.48  ? 197  ALA A CB  1 
ATOM   1610 N  N   . TYR A 1 198 ? -15.584 -43.804 17.910  1.00 68.79  ? 198  TYR A N   1 
ATOM   1611 C  CA  . TYR A 1 198 ? -15.753 -42.377 18.145  1.00 66.58  ? 198  TYR A CA  1 
ATOM   1612 C  C   . TYR A 1 198 ? -16.899 -42.087 19.106  1.00 62.60  ? 198  TYR A C   1 
ATOM   1613 O  O   . TYR A 1 198 ? -17.439 -40.977 19.107  1.00 59.35  ? 198  TYR A O   1 
ATOM   1614 C  CB  . TYR A 1 198 ? -15.969 -41.662 16.813  1.00 63.83  ? 198  TYR A CB  1 
ATOM   1615 C  CG  . TYR A 1 198 ? -14.775 -41.783 15.906  1.00 62.67  ? 198  TYR A CG  1 
ATOM   1616 C  CD1 . TYR A 1 198 ? -13.514 -41.392 16.341  1.00 62.83  ? 198  TYR A CD1 1 
ATOM   1617 C  CD2 . TYR A 1 198 ? -14.894 -42.330 14.634  1.00 66.42  ? 198  TYR A CD2 1 
ATOM   1618 C  CE1 . TYR A 1 198 ? -12.407 -41.512 15.525  1.00 66.28  ? 198  TYR A CE1 1 
ATOM   1619 C  CE2 . TYR A 1 198 ? -13.787 -42.459 13.806  1.00 63.94  ? 198  TYR A CE2 1 
ATOM   1620 C  CZ  . TYR A 1 198 ? -12.544 -42.048 14.260  1.00 63.77  ? 198  TYR A CZ  1 
ATOM   1621 O  OH  . TYR A 1 198 ? -11.432 -42.162 13.451  1.00 74.01  ? 198  TYR A OH  1 
ATOM   1622 N  N   . ASP A 1 199 ? -17.291 -43.073 19.914  1.00 63.52  ? 199  ASP A N   1 
ATOM   1623 C  CA  . ASP A 1 199 ? -18.397 -42.860 20.840  1.00 63.81  ? 199  ASP A CA  1 
ATOM   1624 C  C   . ASP A 1 199 ? -18.009 -41.865 21.925  1.00 61.23  ? 199  ASP A C   1 
ATOM   1625 O  O   . ASP A 1 199 ? -18.819 -41.018 22.316  1.00 63.59  ? 199  ASP A O   1 
ATOM   1626 C  CB  . ASP A 1 199 ? -18.836 -44.189 21.454  1.00 66.35  ? 199  ASP A CB  1 
ATOM   1627 C  CG  . ASP A 1 199 ? -19.602 -45.062 20.475  1.00 71.10  ? 199  ASP A CG  1 
ATOM   1628 O  OD1 . ASP A 1 199 ? -20.171 -44.522 19.504  1.00 71.78  ? 199  ASP A OD1 1 
ATOM   1629 O  OD2 . ASP A 1 199 ? -19.641 -46.292 20.681  1.00 75.95  ? 199  ASP A OD2 1 
ATOM   1630 N  N   . GLU A 1 200 ? -16.769 -41.943 22.412  1.00 62.26  ? 200  GLU A N   1 
ATOM   1631 C  CA  . GLU A 1 200 ? -16.309 -40.990 23.417  1.00 64.56  ? 200  GLU A CA  1 
ATOM   1632 C  C   . GLU A 1 200 ? -16.204 -39.583 22.838  1.00 61.61  ? 200  GLU A C   1 
ATOM   1633 O  O   . GLU A 1 200 ? -16.584 -38.609 23.498  1.00 60.16  ? 200  GLU A O   1 
ATOM   1634 C  CB  . GLU A 1 200 ? -14.967 -41.442 23.997  1.00 61.71  ? 200  GLU A CB  1 
ATOM   1635 C  CG  . GLU A 1 200 ? -14.272 -40.396 24.854  1.00 62.11  ? 200  GLU A CG  1 
ATOM   1636 C  CD  . GLU A 1 200 ? -15.022 -40.080 26.140  1.00 69.75  ? 200  GLU A CD  1 
ATOM   1637 O  OE1 . GLU A 1 200 ? -16.042 -40.746 26.436  1.00 69.18  ? 200  GLU A OE1 1 
ATOM   1638 O  OE2 . GLU A 1 200 ? -14.594 -39.146 26.849  1.00 72.83  ? 200  GLU A OE2 1 
ATOM   1639 N  N   . ASN A 1 201 ? -15.683 -39.453 21.614  1.00 61.70  ? 201  ASN A N   1 
ATOM   1640 C  CA  . ASN A 1 201 ? -15.689 -38.152 20.950  1.00 59.44  ? 201  ASN A CA  1 
ATOM   1641 C  C   . ASN A 1 201 ? -17.099 -37.573 20.932  1.00 60.66  ? 201  ASN A C   1 
ATOM   1642 O  O   . ASN A 1 201 ? -17.319 -36.415 21.306  1.00 60.94  ? 201  ASN A O   1 
ATOM   1643 C  CB  . ASN A 1 201 ? -15.148 -38.275 19.522  1.00 61.61  ? 201  ASN A CB  1 
ATOM   1644 C  CG  . ASN A 1 201 ? -13.743 -38.840 19.469  1.00 63.61  ? 201  ASN A CG  1 
ATOM   1645 O  OD1 . ASN A 1 201 ? -13.539 -40.046 19.597  1.00 67.77  ? 201  ASN A OD1 1 
ATOM   1646 N  ND2 . ASN A 1 201 ? -12.763 -37.966 19.275  1.00 64.69  ? 201  ASN A ND2 1 
ATOM   1647 N  N   . LYS A 1 202 ? -18.073 -38.389 20.521  1.00 55.50  ? 202  LYS A N   1 
ATOM   1648 C  CA  . LYS A 1 202 ? -19.458 -37.940 20.443  1.00 59.86  ? 202  LYS A CA  1 
ATOM   1649 C  C   . LYS A 1 202 ? -19.982 -37.515 21.812  1.00 60.23  ? 202  LYS A C   1 
ATOM   1650 O  O   . LYS A 1 202 ? -20.633 -36.472 21.947  1.00 57.51  ? 202  LYS A O   1 
ATOM   1651 C  CB  . LYS A 1 202 ? -20.312 -39.060 19.855  1.00 59.67  ? 202  LYS A CB  1 
ATOM   1652 C  CG  . LYS A 1 202 ? -20.485 -38.994 18.347  1.00 65.19  ? 202  LYS A CG  1 
ATOM   1653 C  CD  . LYS A 1 202 ? -21.867 -39.494 17.946  1.00 69.44  ? 202  LYS A CD  1 
ATOM   1654 C  CE  . LYS A 1 202 ? -22.931 -38.417 18.097  1.00 69.34  ? 202  LYS A CE  1 
ATOM   1655 N  NZ  . LYS A 1 202 ? -24.237 -38.872 17.541  1.00 75.19  ? 202  LYS A NZ  1 
ATOM   1656 N  N   . ARG A 1 203 ? -19.715 -38.319 22.841  1.00 56.90  ? 203  ARG A N   1 
ATOM   1657 C  CA  . ARG A 1 203 ? -20.122 -37.951 24.192  1.00 59.92  ? 203  ARG A CA  1 
ATOM   1658 C  C   . ARG A 1 203 ? -19.435 -36.661 24.640  1.00 62.61  ? 203  ARG A C   1 
ATOM   1659 O  O   . ARG A 1 203 ? -20.089 -35.728 25.123  1.00 64.49  ? 203  ARG A O   1 
ATOM   1660 C  CB  . ARG A 1 203 ? -19.809 -39.097 25.152  1.00 62.54  ? 203  ARG A CB  1 
ATOM   1661 C  CG  . ARG A 1 203 ? -20.184 -38.813 26.594  1.00 64.63  ? 203  ARG A CG  1 
ATOM   1662 C  CD  . ARG A 1 203 ? -19.404 -39.698 27.541  1.00 65.45  ? 203  ARG A CD  1 
ATOM   1663 N  NE  . ARG A 1 203 ? -18.019 -39.254 27.624  1.00 68.04  ? 203  ARG A NE  1 
ATOM   1664 C  CZ  . ARG A 1 203 ? -17.628 -38.132 28.215  1.00 71.74  ? 203  ARG A CZ  1 
ATOM   1665 N  NH1 . ARG A 1 203 ? -18.494 -37.326 28.812  1.00 71.25  ? 203  ARG A NH1 1 
ATOM   1666 N  NH2 . ARG A 1 203 ? -16.338 -37.806 28.204  1.00 72.85  ? 203  ARG A NH2 1 
ATOM   1667 N  N   . GLN A 1 204 ? -18.107 -36.594 24.492  1.00 60.41  ? 204  GLN A N   1 
ATOM   1668 C  CA  . GLN A 1 204 ? -17.368 -35.386 24.857  1.00 62.05  ? 204  GLN A CA  1 
ATOM   1669 C  C   . GLN A 1 204 ? -17.848 -34.177 24.058  1.00 67.48  ? 204  GLN A C   1 
ATOM   1670 O  O   . GLN A 1 204 ? -17.969 -33.070 24.600  1.00 63.24  ? 204  GLN A O   1 
ATOM   1671 C  CB  . GLN A 1 204 ? -15.871 -35.614 24.644  1.00 68.25  ? 204  GLN A CB  1 
ATOM   1672 C  CG  . GLN A 1 204 ? -14.985 -34.403 24.901  1.00 69.31  ? 204  GLN A CG  1 
ATOM   1673 C  CD  . GLN A 1 204 ? -14.893 -34.037 26.370  1.00 72.90  ? 204  GLN A CD  1 
ATOM   1674 O  OE1 . GLN A 1 204 ? -15.555 -33.104 26.835  1.00 72.08  ? 204  GLN A OE1 1 
ATOM   1675 N  NE2 . GLN A 1 204 ? -14.075 -34.776 27.113  1.00 71.58  ? 204  GLN A NE2 1 
ATOM   1676 N  N   . PHE A 1 205 ? -18.117 -34.369 22.763  1.00 61.23  ? 205  PHE A N   1 
ATOM   1677 C  CA  . PHE A 1 205 ? -18.677 -33.297 21.947  1.00 61.54  ? 205  PHE A CA  1 
ATOM   1678 C  C   . PHE A 1 205 ? -19.962 -32.743 22.555  1.00 62.99  ? 205  PHE A C   1 
ATOM   1679 O  O   . PHE A 1 205 ? -20.184 -31.527 22.557  1.00 63.19  ? 205  PHE A O   1 
ATOM   1680 C  CB  . PHE A 1 205 ? -18.921 -33.811 20.527  1.00 58.67  ? 205  PHE A CB  1 
ATOM   1681 C  CG  . PHE A 1 205 ? -19.188 -32.727 19.518  1.00 60.23  ? 205  PHE A CG  1 
ATOM   1682 C  CD1 . PHE A 1 205 ? -18.243 -31.743 19.267  1.00 55.69  ? 205  PHE A CD1 1 
ATOM   1683 C  CD2 . PHE A 1 205 ? -20.371 -32.720 18.790  1.00 55.22  ? 205  PHE A CD2 1 
ATOM   1684 C  CE1 . PHE A 1 205 ? -18.488 -30.752 18.322  1.00 56.18  ? 205  PHE A CE1 1 
ATOM   1685 C  CE2 . PHE A 1 205 ? -20.622 -31.737 17.842  1.00 56.23  ? 205  PHE A CE2 1 
ATOM   1686 C  CZ  . PHE A 1 205 ? -19.683 -30.755 17.607  1.00 52.72  ? 205  PHE A CZ  1 
ATOM   1687 N  N   . GLN A 1 206 ? -20.820 -33.615 23.085  1.00 62.79  ? 206  GLN A N   1 
ATOM   1688 C  CA  . GLN A 1 206 ? -22.045 -33.133 23.713  1.00 66.12  ? 206  GLN A CA  1 
ATOM   1689 C  C   . GLN A 1 206 ? -21.737 -32.407 25.018  1.00 67.67  ? 206  GLN A C   1 
ATOM   1690 O  O   . GLN A 1 206 ? -22.312 -31.349 25.306  1.00 63.39  ? 206  GLN A O   1 
ATOM   1691 C  CB  . GLN A 1 206 ? -22.998 -34.298 23.959  1.00 64.82  ? 206  GLN A CB  1 
ATOM   1692 C  CG  . GLN A 1 206 ? -23.497 -34.929 22.683  1.00 70.55  ? 206  GLN A CG  1 
ATOM   1693 C  CD  . GLN A 1 206 ? -24.124 -33.915 21.748  1.00 74.06  ? 206  GLN A CD  1 
ATOM   1694 O  OE1 . GLN A 1 206 ? -24.736 -32.937 22.190  1.00 72.70  ? 206  GLN A OE1 1 
ATOM   1695 N  NE2 . GLN A 1 206 ? -23.960 -34.134 20.443  1.00 71.51  ? 206  GLN A NE2 1 
ATOM   1696 N  N   . GLU A 1 207 ? -20.817 -32.960 25.810  1.00 69.59  ? 207  GLU A N   1 
ATOM   1697 C  CA  . GLU A 1 207 ? -20.419 -32.331 27.066  1.00 70.17  ? 207  GLU A CA  1 
ATOM   1698 C  C   . GLU A 1 207 ? -19.911 -30.911 26.829  1.00 67.62  ? 207  GLU A C   1 
ATOM   1699 O  O   . GLU A 1 207 ? -20.355 -29.961 27.486  1.00 64.94  ? 207  GLU A O   1 
ATOM   1700 C  CB  . GLU A 1 207 ? -19.358 -33.207 27.743  1.00 73.21  ? 207  GLU A CB  1 
ATOM   1701 C  CG  . GLU A 1 207 ? -18.785 -32.697 29.054  1.00 77.83  ? 207  GLU A CG  1 
ATOM   1702 C  CD  . GLU A 1 207 ? -17.775 -33.676 29.646  1.00 80.44  ? 207  GLU A CD  1 
ATOM   1703 O  OE1 . GLU A 1 207 ? -18.097 -34.884 29.734  1.00 79.20  ? 207  GLU A OE1 1 
ATOM   1704 O  OE2 . GLU A 1 207 ? -16.662 -33.240 30.018  1.00 83.10  ? 207  GLU A OE2 1 
ATOM   1705 N  N   . ASP A 1 208 ? -18.988 -30.743 25.878  1.00 64.62  ? 208  ASP A N   1 
ATOM   1706 C  CA  . ASP A 1 208 ? -18.498 -29.406 25.565  1.00 63.77  ? 208  ASP A CA  1 
ATOM   1707 C  C   . ASP A 1 208 ? -19.611 -28.505 25.043  1.00 62.35  ? 208  ASP A C   1 
ATOM   1708 O  O   . ASP A 1 208 ? -19.566 -27.286 25.248  1.00 59.34  ? 208  ASP A O   1 
ATOM   1709 C  CB  . ASP A 1 208 ? -17.351 -29.492 24.556  1.00 66.31  ? 208  ASP A CB  1 
ATOM   1710 C  CG  . ASP A 1 208 ? -16.169 -30.274 25.088  1.00 66.10  ? 208  ASP A CG  1 
ATOM   1711 O  OD1 . ASP A 1 208 ? -16.132 -30.533 26.311  1.00 71.23  ? 208  ASP A OD1 1 
ATOM   1712 O  OD2 . ASP A 1 208 ? -15.288 -30.650 24.287  1.00 61.87  ? 208  ASP A OD2 1 
ATOM   1713 N  N   . ILE A 1 209 ? -20.623 -29.080 24.386  1.00 63.98  ? 209  ILE A N   1 
ATOM   1714 C  CA  . ILE A 1 209 ? -21.709 -28.261 23.859  1.00 62.49  ? 209  ILE A CA  1 
ATOM   1715 C  C   . ILE A 1 209 ? -22.587 -27.735 24.983  1.00 60.67  ? 209  ILE A C   1 
ATOM   1716 O  O   . ILE A 1 209 ? -23.090 -26.606 24.910  1.00 57.86  ? 209  ILE A O   1 
ATOM   1717 C  CB  . ILE A 1 209 ? -22.527 -29.052 22.822  1.00 64.43  ? 209  ILE A CB  1 
ATOM   1718 C  CG1 . ILE A 1 209 ? -21.922 -28.853 21.426  1.00 56.50  ? 209  ILE A CG1 1 
ATOM   1719 C  CG2 . ILE A 1 209 ? -23.988 -28.630 22.857  1.00 62.13  ? 209  ILE A CG2 1 
ATOM   1720 C  CD1 . ILE A 1 209 ? -22.373 -29.869 20.405  1.00 57.32  ? 209  ILE A CD1 1 
ATOM   1721 N  N   . LYS A 1 210 ? -22.777 -28.519 26.046  1.00 64.94  ? 210  LYS A N   1 
ATOM   1722 C  CA  . LYS A 1 210 ? -23.611 -28.046 27.145  1.00 59.40  ? 210  LYS A CA  1 
ATOM   1723 C  C   . LYS A 1 210 ? -22.886 -26.982 27.961  1.00 59.24  ? 210  LYS A C   1 
ATOM   1724 O  O   . LYS A 1 210 ? -23.499 -25.996 28.387  1.00 56.58  ? 210  LYS A O   1 
ATOM   1725 C  CB  . LYS A 1 210 ? -24.039 -29.217 28.025  1.00 63.89  ? 210  LYS A CB  1 
ATOM   1726 C  CG  . LYS A 1 210 ? -23.897 -28.957 29.515  1.00 64.60  ? 210  LYS A CG  1 
ATOM   1727 C  CD  . LYS A 1 210 ? -24.467 -30.104 30.337  1.00 70.30  ? 210  LYS A CD  1 
ATOM   1728 C  CE  . LYS A 1 210 ? -24.346 -29.823 31.834  1.00 71.30  ? 210  LYS A CE  1 
ATOM   1729 N  NZ  . LYS A 1 210 ? -25.467 -28.965 32.317  1.00 67.78  ? 210  LYS A NZ  1 
ATOM   1730 N  N   . VAL A 1 211 ? -21.580 -27.161 28.182  1.00 58.54  ? 211  VAL A N   1 
ATOM   1731 C  CA  . VAL A 1 211 ? -20.783 -26.140 28.862  1.00 60.41  ? 211  VAL A CA  1 
ATOM   1732 C  C   . VAL A 1 211 ? -20.987 -24.785 28.192  1.00 58.55  ? 211  VAL A C   1 
ATOM   1733 O  O   . VAL A 1 211 ? -21.271 -23.777 28.849  1.00 56.04  ? 211  VAL A O   1 
ATOM   1734 C  CB  . VAL A 1 211 ? -19.294 -26.546 28.881  1.00 60.82  ? 211  VAL A CB  1 
ATOM   1735 C  CG1 . VAL A 1 211 ? -18.413 -25.381 29.328  1.00 58.89  ? 211  VAL A CG1 1 
ATOM   1736 C  CG2 . VAL A 1 211 ? -19.078 -27.751 29.782  1.00 56.58  ? 211  VAL A CG2 1 
ATOM   1737 N  N   . MET A 1 212 ? -20.866 -24.755 26.861  1.00 59.24  ? 212  MET A N   1 
ATOM   1738 C  CA  . MET A 1 212 ? -20.990 -23.510 26.110  1.00 57.78  ? 212  MET A CA  1 
ATOM   1739 C  C   . MET A 1 212 ? -22.408 -22.951 26.199  1.00 55.26  ? 212  MET A C   1 
ATOM   1740 O  O   . MET A 1 212 ? -22.595 -21.728 26.280  1.00 54.85  ? 212  MET A O   1 
ATOM   1741 C  CB  . MET A 1 212 ? -20.568 -23.757 24.655  1.00 58.24  ? 212  MET A CB  1 
ATOM   1742 C  CG  . MET A 1 212 ? -19.043 -23.769 24.471  1.00 54.20  ? 212  MET A CG  1 
ATOM   1743 S  SD  . MET A 1 212 ? -18.493 -23.769 22.749  1.00 62.99  ? 212  MET A SD  1 
ATOM   1744 C  CE  . MET A 1 212 ? -19.922 -24.573 22.024  1.00 58.35  ? 212  MET A CE  1 
ATOM   1745 N  N   . ASN A 1 213 ? -23.414 -23.835 26.215  1.00 52.69  ? 213  ASN A N   1 
ATOM   1746 C  CA  . ASN A 1 213 ? -24.811 -23.408 26.295  1.00 52.07  ? 213  ASN A CA  1 
ATOM   1747 C  C   . ASN A 1 213 ? -25.192 -22.936 27.696  1.00 60.23  ? 213  ASN A C   1 
ATOM   1748 O  O   . ASN A 1 213 ? -26.086 -22.091 27.845  1.00 58.51  ? 213  ASN A O   1 
ATOM   1749 C  CB  . ASN A 1 213 ? -25.729 -24.554 25.865  1.00 51.03  ? 213  ASN A CB  1 
ATOM   1750 C  CG  . ASN A 1 213 ? -26.097 -24.488 24.400  1.00 60.89  ? 213  ASN A CG  1 
ATOM   1751 O  OD1 . ASN A 1 213 ? -27.229 -24.161 24.054  1.00 64.53  ? 213  ASN A OD1 1 
ATOM   1752 N  ND2 . ASN A 1 213 ? -25.142 -24.792 23.530  1.00 55.90  ? 213  ASN A ND2 1 
ATOM   1753 N  N   . ASP A 1 214 ? -24.544 -23.479 28.731  1.00 58.33  ? 214  ASP A N   1 
ATOM   1754 C  CA  . ASP A 1 214 ? -24.829 -23.050 30.098  1.00 59.12  ? 214  ASP A CA  1 
ATOM   1755 C  C   . ASP A 1 214 ? -24.474 -21.581 30.296  1.00 53.11  ? 214  ASP A C   1 
ATOM   1756 O  O   . ASP A 1 214 ? -25.264 -20.805 30.846  1.00 57.24  ? 214  ASP A O   1 
ATOM   1757 C  CB  . ASP A 1 214 ? -24.065 -23.933 31.085  1.00 57.65  ? 214  ASP A CB  1 
ATOM   1758 C  CG  . ASP A 1 214 ? -24.630 -25.343 31.165  1.00 60.76  ? 214  ASP A CG  1 
ATOM   1759 O  OD1 . ASP A 1 214 ? -25.691 -25.594 30.555  1.00 58.05  ? 214  ASP A OD1 1 
ATOM   1760 O  OD2 . ASP A 1 214 ? -24.011 -26.203 31.830  1.00 65.42  ? 214  ASP A OD2 1 
ATOM   1761 N  N   . LEU A 1 215 ? -23.283 -21.180 29.846  1.00 57.78  ? 215  LEU A N   1 
ATOM   1762 C  CA  . LEU A 1 215 ? -22.905 -19.771 29.906  1.00 56.88  ? 215  LEU A CA  1 
ATOM   1763 C  C   . LEU A 1 215 ? -23.904 -18.903 29.155  1.00 56.20  ? 215  LEU A C   1 
ATOM   1764 O  O   . LEU A 1 215 ? -24.271 -17.818 29.626  1.00 55.25  ? 215  LEU A O   1 
ATOM   1765 C  CB  . LEU A 1 215 ? -21.506 -19.565 29.331  1.00 56.36  ? 215  LEU A CB  1 
ATOM   1766 C  CG  . LEU A 1 215 ? -21.152 -18.078 29.266  1.00 54.41  ? 215  LEU A CG  1 
ATOM   1767 C  CD1 . LEU A 1 215 ? -20.467 -17.668 30.557  1.00 54.26  ? 215  LEU A CD1 1 
ATOM   1768 C  CD2 . LEU A 1 215 ? -20.295 -17.752 28.061  1.00 54.63  ? 215  LEU A CD2 1 
ATOM   1769 N  N   . VAL A 1 216 ? -24.346 -19.362 27.977  1.00 55.22  ? 216  VAL A N   1 
ATOM   1770 C  CA  . VAL A 1 216 ? -25.344 -18.621 27.209  1.00 54.32  ? 216  VAL A CA  1 
ATOM   1771 C  C   . VAL A 1 216 ? -26.614 -18.435 28.029  1.00 57.36  ? 216  VAL A C   1 
ATOM   1772 O  O   . VAL A 1 216 ? -27.242 -17.365 28.003  1.00 54.29  ? 216  VAL A O   1 
ATOM   1773 C  CB  . VAL A 1 216 ? -25.622 -19.337 25.874  1.00 50.03  ? 216  VAL A CB  1 
ATOM   1774 C  CG1 . VAL A 1 216 ? -26.835 -18.738 25.186  1.00 49.44  ? 216  VAL A CG1 1 
ATOM   1775 C  CG2 . VAL A 1 216 ? -24.398 -19.256 24.991  1.00 46.81  ? 216  VAL A CG2 1 
ATOM   1776 N  N   . ASP A 1 217 ? -27.007 -19.464 28.783  1.00 61.16  ? 217  ASP A N   1 
ATOM   1777 C  CA  . ASP A 1 217 ? -28.155 -19.317 29.671  1.00 60.46  ? 217  ASP A CA  1 
ATOM   1778 C  C   . ASP A 1 217 ? -27.901 -18.224 30.705  1.00 59.53  ? 217  ASP A C   1 
ATOM   1779 O  O   . ASP A 1 217 ? -28.742 -17.340 30.921  1.00 48.96  ? 217  ASP A O   1 
ATOM   1780 C  CB  . ASP A 1 217 ? -28.462 -20.650 30.359  1.00 63.38  ? 217  ASP A CB  1 
ATOM   1781 C  CG  . ASP A 1 217 ? -28.759 -21.767 29.375  1.00 65.60  ? 217  ASP A CG  1 
ATOM   1782 O  OD1 . ASP A 1 217 ? -29.458 -21.511 28.369  1.00 67.56  ? 217  ASP A OD1 1 
ATOM   1783 O  OD2 . ASP A 1 217 ? -28.297 -22.905 29.623  1.00 68.43  ? 217  ASP A OD2 1 
ATOM   1784 N  N   . LYS A 1 218 ? -26.732 -18.273 31.351  1.00 57.82  ? 218  LYS A N   1 
ATOM   1785 C  CA  . LYS A 1 218 ? -26.411 -17.292 32.384  1.00 58.97  ? 218  LYS A CA  1 
ATOM   1786 C  C   . LYS A 1 218 ? -26.334 -15.887 31.800  1.00 56.78  ? 218  LYS A C   1 
ATOM   1787 O  O   . LYS A 1 218 ? -26.841 -14.930 32.395  1.00 57.50  ? 218  LYS A O   1 
ATOM   1788 C  CB  . LYS A 1 218 ? -25.099 -17.669 33.079  1.00 55.62  ? 218  LYS A CB  1 
ATOM   1789 C  CG  . LYS A 1 218 ? -24.564 -16.604 34.047  1.00 59.44  ? 218  LYS A CG  1 
ATOM   1790 C  CD  . LYS A 1 218 ? -25.456 -16.464 35.278  1.00 65.89  ? 218  LYS A CD  1 
ATOM   1791 C  CE  . LYS A 1 218 ? -24.657 -16.043 36.514  1.00 66.07  ? 218  LYS A CE  1 
ATOM   1792 N  NZ  . LYS A 1 218 ? -23.883 -14.774 36.316  1.00 55.63  ? 218  LYS A NZ  1 
ATOM   1793 N  N   . ILE A 1 219 ? -25.711 -15.739 30.630  1.00 52.24  ? 219  ILE A N   1 
ATOM   1794 C  CA  . ILE A 1 219 ? -25.695 -14.427 29.996  1.00 52.10  ? 219  ILE A CA  1 
ATOM   1795 C  C   . ILE A 1 219 ? -27.118 -13.935 29.765  1.00 51.70  ? 219  ILE A C   1 
ATOM   1796 O  O   . ILE A 1 219 ? -27.429 -12.761 30.009  1.00 51.40  ? 219  ILE A O   1 
ATOM   1797 C  CB  . ILE A 1 219 ? -24.880 -14.464 28.690  1.00 52.51  ? 219  ILE A CB  1 
ATOM   1798 C  CG1 . ILE A 1 219 ? -23.385 -14.601 29.003  1.00 45.14  ? 219  ILE A CG1 1 
ATOM   1799 C  CG2 . ILE A 1 219 ? -25.167 -13.221 27.865  1.00 49.98  ? 219  ILE A CG2 1 
ATOM   1800 C  CD1 . ILE A 1 219 ? -22.525 -14.990 27.818  1.00 44.65  ? 219  ILE A CD1 1 
ATOM   1801 N  N   . ILE A 1 220 ? -28.013 -14.820 29.313  1.00 54.16  ? 220  ILE A N   1 
ATOM   1802 C  CA  . ILE A 1 220 ? -29.385 -14.389 29.053  1.00 53.33  ? 220  ILE A CA  1 
ATOM   1803 C  C   . ILE A 1 220 ? -30.135 -14.156 30.356  1.00 55.78  ? 220  ILE A C   1 
ATOM   1804 O  O   . ILE A 1 220 ? -30.923 -13.208 30.467  1.00 56.89  ? 220  ILE A O   1 
ATOM   1805 C  CB  . ILE A 1 220 ? -30.127 -15.394 28.154  1.00 54.70  ? 220  ILE A CB  1 
ATOM   1806 C  CG1 . ILE A 1 220 ? -29.650 -15.264 26.703  1.00 52.62  ? 220  ILE A CG1 1 
ATOM   1807 C  CG2 . ILE A 1 220 ? -31.633 -15.158 28.241  1.00 58.27  ? 220  ILE A CG2 1 
ATOM   1808 C  CD1 . ILE A 1 220 ? -30.250 -16.276 25.754  1.00 54.62  ? 220  ILE A CD1 1 
ATOM   1809 N  N   . ALA A 1 221 ? -29.919 -15.016 31.356  1.00 59.60  ? 221  ALA A N   1 
ATOM   1810 C  CA  . ALA A 1 221 ? -30.592 -14.835 32.643  1.00 64.12  ? 221  ALA A CA  1 
ATOM   1811 C  C   . ALA A 1 221 ? -30.222 -13.497 33.278  1.00 63.67  ? 221  ALA A C   1 
ATOM   1812 O  O   . ALA A 1 221 ? -31.099 -12.739 33.711  1.00 64.64  ? 221  ALA A O   1 
ATOM   1813 C  CB  . ALA A 1 221 ? -30.251 -15.988 33.589  1.00 62.92  ? 221  ALA A CB  1 
ATOM   1814 N  N   . ASP A 1 222 ? -28.921 -13.183 33.331  1.00 59.55  ? 222  ASP A N   1 
ATOM   1815 C  CA  . ASP A 1 222 ? -28.477 -11.960 33.997  1.00 59.56  ? 222  ASP A CA  1 
ATOM   1816 C  C   . ASP A 1 222 ? -29.033 -10.710 33.324  1.00 62.92  ? 222  ASP A C   1 
ATOM   1817 O  O   . ASP A 1 222 ? -29.407 -9.746  34.004  1.00 58.91  ? 222  ASP A O   1 
ATOM   1818 C  CB  . ASP A 1 222 ? -26.950 -11.904 34.041  1.00 60.70  ? 222  ASP A CB  1 
ATOM   1819 C  CG  . ASP A 1 222 ? -26.347 -13.059 34.819  1.00 63.81  ? 222  ASP A CG  1 
ATOM   1820 O  OD1 . ASP A 1 222 ? -25.114 -13.253 34.736  1.00 60.08  ? 222  ASP A OD1 1 
ATOM   1821 O  OD2 . ASP A 1 222 ? -27.109 -13.770 35.511  1.00 62.18  ? 222  ASP A OD2 1 
ATOM   1822 N  N   . ARG A 1 223 ? -29.088 -10.695 31.991  1.00 57.23  ? 223  ARG A N   1 
ATOM   1823 C  CA  . ARG A 1 223 ? -29.620 -9.516  31.319  1.00 57.99  ? 223  ARG A CA  1 
ATOM   1824 C  C   . ARG A 1 223 ? -31.116 -9.352  31.576  1.00 62.14  ? 223  ARG A C   1 
ATOM   1825 O  O   . ARG A 1 223 ? -31.576 -8.242  31.866  1.00 65.30  ? 223  ARG A O   1 
ATOM   1826 C  CB  . ARG A 1 223 ? -29.352 -9.580  29.820  1.00 54.14  ? 223  ARG A CB  1 
ATOM   1827 C  CG  . ARG A 1 223 ? -30.162 -8.568  29.062  1.00 52.80  ? 223  ARG A CG  1 
ATOM   1828 C  CD  . ARG A 1 223 ? -29.543 -7.209  29.268  1.00 54.63  ? 223  ARG A CD  1 
ATOM   1829 N  NE  . ARG A 1 223 ? -28.093 -7.243  29.109  1.00 47.25  ? 223  ARG A NE  1 
ATOM   1830 C  CZ  . ARG A 1 223 ? -27.447 -6.689  28.088  1.00 51.38  ? 223  ARG A CZ  1 
ATOM   1831 N  NH1 . ARG A 1 223 ? -28.096 -6.057  27.121  1.00 45.87  ? 223  ARG A NH1 1 
ATOM   1832 N  NH2 . ARG A 1 223 ? -26.116 -6.757  28.044  1.00 46.14  ? 223  ARG A NH2 1 
ATOM   1833 N  N   . LYS A 1 224 ? -31.892 -10.440 31.480  1.00 52.25  ? 224  LYS A N   1 
ATOM   1834 C  CA  . LYS A 1 224 ? -33.346 -10.309 31.593  1.00 68.49  ? 224  LYS A CA  1 
ATOM   1835 C  C   . LYS A 1 224 ? -33.775 -9.842  32.982  1.00 69.07  ? 224  LYS A C   1 
ATOM   1836 O  O   . LYS A 1 224 ? -34.790 -9.146  33.116  1.00 70.06  ? 224  LYS A O   1 
ATOM   1837 C  CB  . LYS A 1 224 ? -34.031 -11.634 31.246  1.00 65.65  ? 224  LYS A CB  1 
ATOM   1838 C  CG  . LYS A 1 224 ? -34.014 -11.958 29.761  1.00 65.21  ? 224  LYS A CG  1 
ATOM   1839 C  CD  . LYS A 1 224 ? -35.414 -12.000 29.169  1.00 71.87  ? 224  LYS A CD  1 
ATOM   1840 C  CE  . LYS A 1 224 ? -35.355 -12.040 27.645  1.00 72.13  ? 224  LYS A CE  1 
ATOM   1841 N  NZ  . LYS A 1 224 ? -35.984 -13.264 27.068  1.00 71.77  ? 224  LYS A NZ  1 
ATOM   1842 N  N   . ALA A 1 225 ? -33.032 -10.211 34.019  1.00 68.98  ? 225  ALA A N   1 
ATOM   1843 C  CA  . ALA A 1 225 ? -33.362 -9.789  35.374  1.00 73.82  ? 225  ALA A CA  1 
ATOM   1844 C  C   . ALA A 1 225 ? -32.649 -8.507  35.784  1.00 78.86  ? 225  ALA A C   1 
ATOM   1845 O  O   . ALA A 1 225 ? -32.977 -7.943  36.833  1.00 84.53  ? 225  ALA A O   1 
ATOM   1846 C  CB  . ALA A 1 225 ? -33.028 -10.905 36.371  1.00 70.10  ? 225  ALA A CB  1 
ATOM   1847 N  N   . SER A 1 226 ? -31.694 -8.037  34.984  1.00 78.56  ? 226  SER A N   1 
ATOM   1848 C  CA  . SER A 1 226 ? -30.897 -6.873  35.348  1.00 83.87  ? 226  SER A CA  1 
ATOM   1849 C  C   . SER A 1 226 ? -31.773 -5.640  35.530  1.00 90.88  ? 226  SER A C   1 
ATOM   1850 O  O   . SER A 1 226 ? -32.866 -5.533  34.964  1.00 88.86  ? 226  SER A O   1 
ATOM   1851 C  CB  . SER A 1 226 ? -29.836 -6.600  34.277  1.00 84.89  ? 226  SER A CB  1 
ATOM   1852 O  OG  . SER A 1 226 ? -29.196 -5.351  34.489  1.00 86.50  ? 226  SER A OG  1 
ATOM   1853 N  N   . GLY A 1 227 ? -31.273 -4.701  36.332  1.00 95.26  ? 227  GLY A N   1 
ATOM   1854 C  CA  . GLY A 1 227 ? -31.909 -3.412  36.513  1.00 97.48  ? 227  GLY A CA  1 
ATOM   1855 C  C   . GLY A 1 227 ? -31.157 -2.311  35.794  1.00 101.60 ? 227  GLY A C   1 
ATOM   1856 O  O   . GLY A 1 227 ? -31.597 -1.156  35.771  1.00 103.56 ? 227  GLY A O   1 
ATOM   1857 N  N   . GLU A 1 228 ? -30.011 -2.659  35.212  1.00 102.51 ? 228  GLU A N   1 
ATOM   1858 C  CA  . GLU A 1 228 ? -29.247 -1.724  34.401  1.00 101.92 ? 228  GLU A CA  1 
ATOM   1859 C  C   . GLU A 1 228 ? -29.804 -1.679  32.983  1.00 99.52  ? 228  GLU A C   1 
ATOM   1860 O  O   . GLU A 1 228 ? -30.323 -2.672  32.461  1.00 99.03  ? 228  GLU A O   1 
ATOM   1861 C  CB  . GLU A 1 228 ? -27.764 -2.112  34.365  1.00 101.54 ? 228  GLU A CB  1 
ATOM   1862 C  CG  . GLU A 1 228 ? -27.133 -2.430  35.724  1.00 104.96 ? 228  GLU A CG  1 
ATOM   1863 C  CD  . GLU A 1 228 ? -27.056 -1.224  36.653  1.00 106.18 ? 228  GLU A CD  1 
ATOM   1864 O  OE1 . GLU A 1 228 ? -26.812 -0.101  36.163  1.00 102.20 ? 228  GLU A OE1 1 
ATOM   1865 O  OE2 . GLU A 1 228 ? -27.229 -1.404  37.879  1.00 109.72 ? 228  GLU A OE2 1 
ATOM   1866 N  N   . GLN A 1 229 ? -29.693 -0.512  32.359  1.00 99.08  ? 229  GLN A N   1 
ATOM   1867 C  CA  . GLN A 1 229 ? -30.221 -0.287  31.018  1.00 93.40  ? 229  GLN A CA  1 
ATOM   1868 C  C   . GLN A 1 229 ? -29.063 -0.364  30.030  1.00 89.09  ? 229  GLN A C   1 
ATOM   1869 O  O   . GLN A 1 229 ? -28.240 0.554   29.954  1.00 87.33  ? 229  GLN A O   1 
ATOM   1870 C  CB  . GLN A 1 229 ? -30.934 1.060   30.937  1.00 94.62  ? 229  GLN A CB  1 
ATOM   1871 C  CG  . GLN A 1 229 ? -32.145 1.150   31.849  1.00 98.28  ? 229  GLN A CG  1 
ATOM   1872 C  CD  . GLN A 1 229 ? -33.371 0.486   31.257  1.00 99.07  ? 229  GLN A CD  1 
ATOM   1873 O  OE1 . GLN A 1 229 ? -33.771 -0.594  31.688  1.00 100.91 ? 229  GLN A OE1 1 
ATOM   1874 N  NE2 . GLN A 1 229 ? -33.976 1.130   30.267  1.00 100.38 ? 229  GLN A NE2 1 
ATOM   1875 N  N   . SER A 1 230 ? -28.999 -1.459  29.279  1.00 80.11  ? 230  SER A N   1 
ATOM   1876 C  CA  . SER A 1 230 ? -27.911 -1.691  28.342  1.00 71.14  ? 230  SER A CA  1 
ATOM   1877 C  C   . SER A 1 230 ? -28.325 -1.307  26.926  1.00 69.55  ? 230  SER A C   1 
ATOM   1878 O  O   . SER A 1 230 ? -29.510 -1.273  26.581  1.00 66.31  ? 230  SER A O   1 
ATOM   1879 C  CB  . SER A 1 230 ? -27.468 -3.156  28.378  1.00 66.61  ? 230  SER A CB  1 
ATOM   1880 O  OG  . SER A 1 230 ? -26.700 -3.436  29.538  1.00 65.05  ? 230  SER A OG  1 
ATOM   1881 N  N   . ASP A 1 231 ? -27.313 -0.994  26.103  1.00 59.81  ? 231  ASP A N   1 
ATOM   1882 C  CA  . ASP A 1 231 ? -27.493 -0.786  24.677  1.00 59.75  ? 231  ASP A CA  1 
ATOM   1883 C  C   . ASP A 1 231 ? -26.294 -1.426  23.975  1.00 62.27  ? 231  ASP A C   1 
ATOM   1884 O  O   . ASP A 1 231 ? -25.372 -0.758  23.504  1.00 68.82  ? 231  ASP A O   1 
ATOM   1885 C  CB  . ASP A 1 231 ? -27.626 0.694   24.320  1.00 62.70  ? 231  ASP A CB  1 
ATOM   1886 C  CG  . ASP A 1 231 ? -27.983 0.905   22.859  1.00 71.04  ? 231  ASP A CG  1 
ATOM   1887 O  OD1 . ASP A 1 231 ? -28.431 -0.070  22.215  1.00 65.84  ? 231  ASP A OD1 1 
ATOM   1888 O  OD2 . ASP A 1 231 ? -27.825 2.038   22.353  1.00 75.88  ? 231  ASP A OD2 1 
ATOM   1889 N  N   . ASP A 1 232 ? -26.296 -2.753  23.911  1.00 54.74  ? 232  ASP A N   1 
ATOM   1890 C  CA  . ASP A 1 232 ? -25.183 -3.493  23.332  1.00 46.53  ? 232  ASP A CA  1 
ATOM   1891 C  C   . ASP A 1 232 ? -25.728 -4.524  22.347  1.00 52.08  ? 232  ASP A C   1 
ATOM   1892 O  O   . ASP A 1 232 ? -26.879 -4.463  21.892  1.00 48.41  ? 232  ASP A O   1 
ATOM   1893 C  CB  . ASP A 1 232 ? -24.327 -4.119  24.442  1.00 46.69  ? 232  ASP A CB  1 
ATOM   1894 C  CG  . ASP A 1 232 ? -25.108 -5.086  25.323  1.00 47.89  ? 232  ASP A CG  1 
ATOM   1895 O  OD1 . ASP A 1 232 ? -26.250 -5.459  24.974  1.00 47.81  ? 232  ASP A OD1 1 
ATOM   1896 O  OD2 . ASP A 1 232 ? -24.560 -5.493  26.370  1.00 46.02  ? 232  ASP A OD2 1 
ATOM   1897 N  N   . LEU A 1 233 ? -24.884 -5.495  21.997  1.00 47.81  ? 233  LEU A N   1 
ATOM   1898 C  CA  . LEU A 1 233 ? -25.279 -6.505  21.020  1.00 45.05  ? 233  LEU A CA  1 
ATOM   1899 C  C   . LEU A 1 233 ? -26.461 -7.324  21.532  1.00 41.86  ? 233  LEU A C   1 
ATOM   1900 O  O   . LEU A 1 233 ? -27.434 -7.554  20.806  1.00 39.43  ? 233  LEU A O   1 
ATOM   1901 C  CB  . LEU A 1 233 ? -24.062 -7.384  20.706  1.00 41.05  ? 233  LEU A CB  1 
ATOM   1902 C  CG  . LEU A 1 233 ? -24.016 -8.500  19.676  1.00 44.77  ? 233  LEU A CG  1 
ATOM   1903 C  CD1 . LEU A 1 233 ? -24.428 -8.054  18.257  1.00 42.45  ? 233  LEU A CD1 1 
ATOM   1904 C  CD2 . LEU A 1 233 ? -22.588 -9.039  19.659  1.00 42.66  ? 233  LEU A CD2 1 
ATOM   1905 N  N   . LEU A 1 234 ? -26.413 -7.740  22.798  1.00 40.71  ? 234  LEU A N   1 
ATOM   1906 C  CA  . LEU A 1 234 ? -27.529 -8.485  23.375  1.00 37.03  ? 234  LEU A CA  1 
ATOM   1907 C  C   . LEU A 1 234 ? -28.826 -7.685  23.335  1.00 47.62  ? 234  LEU A C   1 
ATOM   1908 O  O   . LEU A 1 234 ? -29.905 -8.246  23.091  1.00 43.78  ? 234  LEU A O   1 
ATOM   1909 C  CB  . LEU A 1 234 ? -27.212 -8.867  24.816  1.00 40.13  ? 234  LEU A CB  1 
ATOM   1910 C  CG  . LEU A 1 234 ? -28.169 -9.882  25.436  1.00 43.40  ? 234  LEU A CG  1 
ATOM   1911 C  CD1 . LEU A 1 234 ? -28.338 -11.088 24.553  1.00 41.34  ? 234  LEU A CD1 1 
ATOM   1912 C  CD2 . LEU A 1 234 ? -27.689 -10.285 26.838  1.00 45.80  ? 234  LEU A CD2 1 
ATOM   1913 N  N   . THR A 1 235 ? -28.748 -6.381  23.625  1.00 45.44  ? 235  THR A N   1 
ATOM   1914 C  CA  . THR A 1 235 ? -29.936 -5.529  23.560  1.00 46.31  ? 235  THR A CA  1 
ATOM   1915 C  C   . THR A 1 235 ? -30.606 -5.641  22.204  1.00 42.84  ? 235  THR A C   1 
ATOM   1916 O  O   . THR A 1 235 ? -31.832 -5.766  22.108  1.00 46.46  ? 235  THR A O   1 
ATOM   1917 C  CB  . THR A 1 235 ? -29.564 -4.069  23.825  1.00 48.16  ? 235  THR A CB  1 
ATOM   1918 O  OG1 . THR A 1 235 ? -28.898 -3.955  25.086  1.00 47.78  ? 235  THR A OG1 1 
ATOM   1919 C  CG2 . THR A 1 235 ? -30.824 -3.184  23.817  1.00 46.66  ? 235  THR A CG2 1 
ATOM   1920 N  N   . HIS A 1 236 ? -29.806 -5.569  21.140  1.00 42.21  ? 236  HIS A N   1 
ATOM   1921 C  CA  . HIS A 1 236 ? -30.341 -5.645  19.789  1.00 44.82  ? 236  HIS A CA  1 
ATOM   1922 C  C   . HIS A 1 236 ? -30.924 -7.026  19.519  1.00 47.36  ? 236  HIS A C   1 
ATOM   1923 O  O   . HIS A 1 236 ? -31.991 -7.152  18.907  1.00 44.00  ? 236  HIS A O   1 
ATOM   1924 C  CB  . HIS A 1 236 ? -29.232 -5.325  18.790  1.00 41.57  ? 236  HIS A CB  1 
ATOM   1925 C  CG  . HIS A 1 236 ? -29.032 -3.862  18.560  1.00 49.37  ? 236  HIS A CG  1 
ATOM   1926 N  ND1 . HIS A 1 236 ? -28.245 -3.086  19.387  1.00 52.88  ? 236  HIS A ND1 1 
ATOM   1927 C  CD2 . HIS A 1 236 ? -29.497 -3.034  17.593  1.00 54.04  ? 236  HIS A CD2 1 
ATOM   1928 C  CE1 . HIS A 1 236 ? -28.244 -1.839  18.945  1.00 49.11  ? 236  HIS A CE1 1 
ATOM   1929 N  NE2 . HIS A 1 236 ? -28.989 -1.782  17.854  1.00 50.00  ? 236  HIS A NE2 1 
ATOM   1930 N  N   . MET A 1 237 ? -30.230 -8.072  19.972  1.00 41.04  ? 237  MET A N   1 
ATOM   1931 C  CA  . MET A 1 237 ? -30.717 -9.436  19.798  1.00 42.45  ? 237  MET A CA  1 
ATOM   1932 C  C   . MET A 1 237 ? -32.107 -9.603  20.413  1.00 49.13  ? 237  MET A C   1 
ATOM   1933 O  O   . MET A 1 237 ? -32.994 -10.223 19.810  1.00 47.60  ? 237  MET A O   1 
ATOM   1934 C  CB  . MET A 1 237 ? -29.717 -10.420 20.416  1.00 40.93  ? 237  MET A CB  1 
ATOM   1935 C  CG  . MET A 1 237 ? -28.626 -11.016 19.475  1.00 39.15  ? 237  MET A CG  1 
ATOM   1936 S  SD  . MET A 1 237 ? -27.383 -11.917 20.461  1.00 42.78  ? 237  MET A SD  1 
ATOM   1937 C  CE  . MET A 1 237 ? -25.844 -11.596 19.576  1.00 39.18  ? 237  MET A CE  1 
ATOM   1938 N  N   . LEU A 1 238 ? -32.328 -9.018  21.594  1.00 42.88  ? 238  LEU A N   1 
ATOM   1939 C  CA  . LEU A 1 238 ? -33.567 -9.212  22.335  1.00 43.81  ? 238  LEU A CA  1 
ATOM   1940 C  C   . LEU A 1 238 ? -34.674 -8.247  21.931  1.00 44.64  ? 238  LEU A C   1 
ATOM   1941 O  O   . LEU A 1 238 ? -35.849 -8.566  22.125  1.00 46.95  ? 238  LEU A O   1 
ATOM   1942 C  CB  . LEU A 1 238 ? -33.309 -9.085  23.848  1.00 46.45  ? 238  LEU A CB  1 
ATOM   1943 C  CG  . LEU A 1 238 ? -32.291 -10.068 24.451  1.00 47.37  ? 238  LEU A CG  1 
ATOM   1944 C  CD1 . LEU A 1 238 ? -31.868 -9.683  25.871  1.00 42.83  ? 238  LEU A CD1 1 
ATOM   1945 C  CD2 . LEU A 1 238 ? -32.856 -11.478 24.442  1.00 49.77  ? 238  LEU A CD2 1 
ATOM   1946 N  N   . ASN A 1 239 ? -34.337 -7.096  21.354  1.00 45.97  ? 239  ASN A N   1 
ATOM   1947 C  CA  . ASN A 1 239 ? -35.317 -6.057  21.073  1.00 45.50  ? 239  ASN A CA  1 
ATOM   1948 C  C   . ASN A 1 239 ? -35.408 -5.645  19.613  1.00 49.12  ? 239  ASN A C   1 
ATOM   1949 O  O   . ASN A 1 239 ? -36.443 -5.098  19.213  1.00 47.40  ? 239  ASN A O   1 
ATOM   1950 C  CB  . ASN A 1 239 ? -35.021 -4.806  21.914  1.00 47.62  ? 239  ASN A CB  1 
ATOM   1951 C  CG  . ASN A 1 239 ? -35.078 -5.090  23.395  1.00 52.60  ? 239  ASN A CG  1 
ATOM   1952 O  OD1 . ASN A 1 239 ? -36.154 -5.310  23.945  1.00 55.48  ? 239  ASN A OD1 1 
ATOM   1953 N  ND2 . ASN A 1 239 ? -33.915 -5.134  24.045  1.00 55.59  ? 239  ASN A ND2 1 
ATOM   1954 N  N   . GLY A 1 240 ? -34.375 -5.888  18.809  1.00 45.67  ? 240  GLY A N   1 
ATOM   1955 C  CA  . GLY A 1 240 ? -34.401 -5.430  17.436  1.00 41.99  ? 240  GLY A CA  1 
ATOM   1956 C  C   . GLY A 1 240 ? -35.479 -6.118  16.620  1.00 43.57  ? 240  GLY A C   1 
ATOM   1957 O  O   . GLY A 1 240 ? -35.794 -7.297  16.808  1.00 41.06  ? 240  GLY A O   1 
ATOM   1958 N  N   . LYS A 1 241 ? -36.053 -5.366  15.688  1.00 41.91  ? 241  LYS A N   1 
ATOM   1959 C  CA  . LYS A 1 241 ? -37.035 -5.901  14.757  1.00 43.60  ? 241  LYS A CA  1 
ATOM   1960 C  C   . LYS A 1 241 ? -36.486 -5.763  13.348  1.00 38.99  ? 241  LYS A C   1 
ATOM   1961 O  O   . LYS A 1 241 ? -35.936 -4.711  13.001  1.00 41.19  ? 241  LYS A O   1 
ATOM   1962 C  CB  . LYS A 1 241 ? -38.379 -5.179  14.889  1.00 45.97  ? 241  LYS A CB  1 
ATOM   1963 C  CG  . LYS A 1 241 ? -38.881 -5.045  16.320  1.00 51.82  ? 241  LYS A CG  1 
ATOM   1964 C  CD  . LYS A 1 241 ? -39.398 -6.362  16.870  1.00 49.81  ? 241  LYS A CD  1 
ATOM   1965 C  CE  . LYS A 1 241 ? -40.123 -6.163  18.200  1.00 57.41  ? 241  LYS A CE  1 
ATOM   1966 N  NZ  . LYS A 1 241 ? -39.253 -6.443  19.389  1.00 57.54  ? 241  LYS A NZ  1 
ATOM   1967 N  N   . ASP A 1 242 ? -36.615 -6.826  12.557  1.00 39.20  ? 242  ASP A N   1 
ATOM   1968 C  CA  . ASP A 1 242 ? -36.133 -6.837  11.170  1.00 39.22  ? 242  ASP A CA  1 
ATOM   1969 C  C   . ASP A 1 242 ? -37.067 -6.013  10.298  1.00 46.15  ? 242  ASP A C   1 
ATOM   1970 O  O   . ASP A 1 242 ? -38.253 -6.347  10.196  1.00 51.13  ? 242  ASP A O   1 
ATOM   1971 C  CB  . ASP A 1 242 ? -36.046 -8.274  10.639  1.00 38.82  ? 242  ASP A CB  1 
ATOM   1972 C  CG  . ASP A 1 242 ? -35.895 -8.347  9.114   1.00 41.87  ? 242  ASP A CG  1 
ATOM   1973 O  OD1 . ASP A 1 242 ? -35.378 -7.386  8.511   1.00 43.60  ? 242  ASP A OD1 1 
ATOM   1974 O  OD2 . ASP A 1 242 ? -36.271 -9.383  8.512   1.00 40.71  ? 242  ASP A OD2 1 
ATOM   1975 N  N   . PRO A 1 243 ? -36.591 -4.944  9.654   1.00 46.59  ? 243  PRO A N   1 
ATOM   1976 C  CA  . PRO A 1 243 ? -37.486 -4.162  8.776   1.00 48.94  ? 243  PRO A CA  1 
ATOM   1977 C  C   . PRO A 1 243 ? -38.195 -4.991  7.712   1.00 48.80  ? 243  PRO A C   1 
ATOM   1978 O  O   . PRO A 1 243 ? -39.341 -4.685  7.368   1.00 58.74  ? 243  PRO A O   1 
ATOM   1979 C  CB  . PRO A 1 243 ? -36.537 -3.121  8.160   1.00 49.73  ? 243  PRO A CB  1 
ATOM   1980 C  CG  . PRO A 1 243 ? -35.425 -2.982  9.176   1.00 48.88  ? 243  PRO A CG  1 
ATOM   1981 C  CD  . PRO A 1 243 ? -35.238 -4.364  9.741   1.00 44.19  ? 243  PRO A CD  1 
ATOM   1982 N  N   . GLU A 1 244 ? -37.563 -6.038  7.184   1.00 50.41  ? 244  GLU A N   1 
ATOM   1983 C  CA  . GLU A 1 244 ? -38.174 -6.802  6.100   1.00 47.47  ? 244  GLU A CA  1 
ATOM   1984 C  C   . GLU A 1 244 ? -39.321 -7.676  6.601   1.00 54.91  ? 244  GLU A C   1 
ATOM   1985 O  O   . GLU A 1 244 ? -40.482 -7.450  6.239   1.00 57.34  ? 244  GLU A O   1 
ATOM   1986 C  CB  . GLU A 1 244 ? -37.125 -7.659  5.383   1.00 45.65  ? 244  GLU A CB  1 
ATOM   1987 C  CG  . GLU A 1 244 ? -37.669 -8.410  4.170   1.00 53.80  ? 244  GLU A CG  1 
ATOM   1988 C  CD  . GLU A 1 244 ? -36.627 -9.287  3.494   1.00 58.08  ? 244  GLU A CD  1 
ATOM   1989 O  OE1 . GLU A 1 244 ? -35.459 -9.300  3.946   1.00 50.98  ? 244  GLU A OE1 1 
ATOM   1990 O  OE2 . GLU A 1 244 ? -36.979 -9.979  2.512   1.00 63.70  ? 244  GLU A OE2 1 
ATOM   1991 N  N   . THR A 1 245 ? -39.014 -8.680  7.429   1.00 53.04  ? 245  THR A N   1 
ATOM   1992 C  CA  . THR A 1 245 ? -40.044 -9.575  7.948   1.00 48.74  ? 245  THR A CA  1 
ATOM   1993 C  C   . THR A 1 245 ? -40.878 -8.949  9.057   1.00 48.35  ? 245  THR A C   1 
ATOM   1994 O  O   . THR A 1 245 ? -41.942 -9.483  9.383   1.00 52.87  ? 245  THR A O   1 
ATOM   1995 C  CB  . THR A 1 245 ? -39.415 -10.866 8.486   1.00 48.90  ? 245  THR A CB  1 
ATOM   1996 O  OG1 . THR A 1 245 ? -38.571 -10.550 9.603   1.00 46.28  ? 245  THR A OG1 1 
ATOM   1997 C  CG2 . THR A 1 245 ? -38.598 -11.588 7.398   1.00 45.78  ? 245  THR A CG2 1 
ATOM   1998 N  N   . GLY A 1 246 ? -40.413 -7.856  9.664   1.00 45.39  ? 246  GLY A N   1 
ATOM   1999 C  CA  . GLY A 1 246 ? -41.107 -7.217  10.768  1.00 46.55  ? 246  GLY A CA  1 
ATOM   2000 C  C   . GLY A 1 246 ? -40.913 -7.870  12.121  1.00 53.64  ? 246  GLY A C   1 
ATOM   2001 O  O   . GLY A 1 246 ? -41.293 -7.273  13.143  1.00 49.82  ? 246  GLY A O   1 
ATOM   2002 N  N   . GLU A 1 247 ? -40.299 -9.094  12.171  1.00 46.75  ? 247  GLU A N   1 
ATOM   2003 C  CA  . GLU A 1 247 ? -40.160 -9.978  13.317  1.00 38.73  ? 247  GLU A CA  1 
ATOM   2004 C  C   . GLU A 1 247 ? -38.846 -9.737  14.057  1.00 43.92  ? 247  GLU A C   1 
ATOM   2005 O  O   . GLU A 1 247 ? -37.831 -9.397  13.446  1.00 38.21  ? 247  GLU A O   1 
ATOM   2006 C  CB  . GLU A 1 247 ? -40.208 -11.437 12.870  1.00 44.81  ? 247  GLU A CB  1 
ATOM   2007 C  CG  . GLU A 1 247 ? -41.297 -11.765 11.856  1.00 47.25  ? 247  GLU A CG  1 
ATOM   2008 C  CD  . GLU A 1 247 ? -41.204 -13.198 11.352  1.00 51.76  ? 247  GLU A CD  1 
ATOM   2009 O  OE1 . GLU A 1 247 ? -40.152 -13.841 11.565  1.00 46.39  ? 247  GLU A OE1 1 
ATOM   2010 O  OE2 . GLU A 1 247 ? -42.192 -13.686 10.759  1.00 49.37  ? 247  GLU A OE2 1 
ATOM   2011 N  N   . PRO A 1 248 ? -38.844 -9.932  15.368  1.00 40.41  ? 248  PRO A N   1 
ATOM   2012 C  CA  . PRO A 1 248 ? -37.579 -10.053 16.099  1.00 39.61  ? 248  PRO A CA  1 
ATOM   2013 C  C   . PRO A 1 248 ? -37.057 -11.482 16.003  1.00 39.32  ? 248  PRO A C   1 
ATOM   2014 O  O   . PRO A 1 248 ? -37.739 -12.393 15.533  1.00 39.30  ? 248  PRO A O   1 
ATOM   2015 C  CB  . PRO A 1 248 ? -37.978 -9.685  17.531  1.00 43.07  ? 248  PRO A CB  1 
ATOM   2016 C  CG  . PRO A 1 248 ? -39.389 -10.216 17.645  1.00 44.55  ? 248  PRO A CG  1 
ATOM   2017 C  CD  . PRO A 1 248 ? -40.014 -10.076 16.254  1.00 42.58  ? 248  PRO A CD  1 
ATOM   2018 N  N   . LEU A 1 249 ? -35.798 -11.657 16.403  1.00 35.53  ? 249  LEU A N   1 
ATOM   2019 C  CA  . LEU A 1 249 ? -35.245 -12.997 16.550  1.00 37.12  ? 249  LEU A CA  1 
ATOM   2020 C  C   . LEU A 1 249 ? -35.993 -13.752 17.635  1.00 37.67  ? 249  LEU A C   1 
ATOM   2021 O  O   . LEU A 1 249 ? -36.361 -13.179 18.664  1.00 37.28  ? 249  LEU A O   1 
ATOM   2022 C  CB  . LEU A 1 249 ? -33.759 -12.931 16.918  1.00 34.66  ? 249  LEU A CB  1 
ATOM   2023 C  CG  . LEU A 1 249 ? -32.916 -12.120 15.948  1.00 34.45  ? 249  LEU A CG  1 
ATOM   2024 C  CD1 . LEU A 1 249 ? -31.454 -12.244 16.364  1.00 35.95  ? 249  LEU A CD1 1 
ATOM   2025 C  CD2 . LEU A 1 249 ? -33.113 -12.638 14.544  1.00 36.83  ? 249  LEU A CD2 1 
ATOM   2026 N  N   . ASP A 1 250 ? -36.198 -15.050 17.418  1.00 36.31  ? 250  ASP A N   1 
ATOM   2027 C  CA  . ASP A 1 250 ? -36.782 -15.864 18.476  1.00 43.07  ? 250  ASP A CA  1 
ATOM   2028 C  C   . ASP A 1 250 ? -35.686 -16.433 19.383  1.00 43.25  ? 250  ASP A C   1 
ATOM   2029 O  O   . ASP A 1 250 ? -34.486 -16.323 19.112  1.00 41.80  ? 250  ASP A O   1 
ATOM   2030 C  CB  . ASP A 1 250 ? -37.684 -16.957 17.880  1.00 46.74  ? 250  ASP A CB  1 
ATOM   2031 C  CG  . ASP A 1 250 ? -36.937 -17.967 17.031  1.00 49.12  ? 250  ASP A CG  1 
ATOM   2032 O  OD1 . ASP A 1 250 ? -35.727 -18.204 17.231  1.00 46.01  ? 250  ASP A OD1 1 
ATOM   2033 O  OD2 . ASP A 1 250 ? -37.565 -18.487 16.092  1.00 59.77  ? 250  ASP A OD2 1 
ATOM   2034 N  N   . ASP A 1 251 ? -36.119 -17.038 20.489  1.00 41.35  ? 251  ASP A N   1 
ATOM   2035 C  CA  . ASP A 1 251 ? -35.181 -17.401 21.545  1.00 46.85  ? 251  ASP A CA  1 
ATOM   2036 C  C   . ASP A 1 251 ? -34.160 -18.420 21.058  1.00 38.90  ? 251  ASP A C   1 
ATOM   2037 O  O   . ASP A 1 251 ? -32.981 -18.340 21.411  1.00 43.81  ? 251  ASP A O   1 
ATOM   2038 C  CB  . ASP A 1 251 ? -35.942 -17.942 22.753  1.00 48.02  ? 251  ASP A CB  1 
ATOM   2039 C  CG  . ASP A 1 251 ? -36.528 -16.832 23.620  1.00 52.46  ? 251  ASP A CG  1 
ATOM   2040 O  OD1 . ASP A 1 251 ? -36.216 -15.644 23.392  1.00 51.46  ? 251  ASP A OD1 1 
ATOM   2041 O  OD2 . ASP A 1 251 ? -37.310 -17.156 24.533  1.00 54.47  ? 251  ASP A OD2 1 
ATOM   2042 N  N   . GLU A 1 252 ? -34.584 -19.378 20.231  1.00 44.17  ? 252  GLU A N   1 
ATOM   2043 C  CA  . GLU A 1 252 ? -33.633 -20.391 19.786  1.00 42.91  ? 252  GLU A CA  1 
ATOM   2044 C  C   . GLU A 1 252 ? -32.527 -19.763 18.940  1.00 39.94  ? 252  GLU A C   1 
ATOM   2045 O  O   . GLU A 1 252 ? -31.341 -20.086 19.116  1.00 38.24  ? 252  GLU A O   1 
ATOM   2046 C  CB  . GLU A 1 252 ? -34.347 -21.497 19.006  1.00 44.61  ? 252  GLU A CB  1 
ATOM   2047 C  CG  . GLU A 1 252 ? -33.381 -22.547 18.487  1.00 43.57  ? 252  GLU A CG  1 
ATOM   2048 C  CD  . GLU A 1 252 ? -34.043 -23.619 17.641  1.00 54.35  ? 252  GLU A CD  1 
ATOM   2049 O  OE1 . GLU A 1 252 ? -34.260 -23.380 16.437  1.00 59.03  ? 252  GLU A OE1 1 
ATOM   2050 O  OE2 . GLU A 1 252 ? -34.342 -24.708 18.181  1.00 65.42  ? 252  GLU A OE2 1 
ATOM   2051 N  N   . ASN A 1 253 ? -32.892 -18.845 18.038  1.00 36.78  ? 253  ASN A N   1 
ATOM   2052 C  CA  . ASN A 1 253 ? -31.886 -18.211 17.191  1.00 37.01  ? 253  ASN A CA  1 
ATOM   2053 C  C   . ASN A 1 253 ? -31.012 -17.242 17.983  1.00 37.20  ? 253  ASN A C   1 
ATOM   2054 O  O   . ASN A 1 253 ? -29.798 -17.166 17.748  1.00 33.83  ? 253  ASN A O   1 
ATOM   2055 C  CB  . ASN A 1 253 ? -32.538 -17.496 16.019  1.00 37.04  ? 253  ASN A CB  1 
ATOM   2056 C  CG  . ASN A 1 253 ? -31.504 -16.952 15.028  1.00 35.30  ? 253  ASN A CG  1 
ATOM   2057 O  OD1 . ASN A 1 253 ? -31.229 -15.751 15.007  1.00 35.26  ? 253  ASN A OD1 1 
ATOM   2058 N  ND2 . ASN A 1 253 ? -30.940 -17.833 14.202  1.00 32.13  ? 253  ASN A ND2 1 
ATOM   2059 N  N   . ILE A 1 254 ? -31.600 -16.496 18.923  1.00 34.10  ? 254  ILE A N   1 
ATOM   2060 C  CA  . ILE A 1 254 ? -30.787 -15.648 19.801  1.00 33.46  ? 254  ILE A CA  1 
ATOM   2061 C  C   . ILE A 1 254 ? -29.671 -16.462 20.453  1.00 35.53  ? 254  ILE A C   1 
ATOM   2062 O  O   . ILE A 1 254 ? -28.506 -16.045 20.494  1.00 34.25  ? 254  ILE A O   1 
ATOM   2063 C  CB  . ILE A 1 254 ? -31.666 -14.962 20.865  1.00 38.42  ? 254  ILE A CB  1 
ATOM   2064 C  CG1 . ILE A 1 254 ? -32.552 -13.897 20.229  1.00 36.48  ? 254  ILE A CG1 1 
ATOM   2065 C  CG2 . ILE A 1 254 ? -30.778 -14.351 21.971  1.00 36.92  ? 254  ILE A CG2 1 
ATOM   2066 C  CD1 . ILE A 1 254 ? -33.717 -13.455 21.109  1.00 43.68  ? 254  ILE A CD1 1 
ATOM   2067 N  N   . ARG A 1 255 ? -30.017 -17.631 20.992  1.00 33.16  ? 255  ARG A N   1 
ATOM   2068 C  CA  . ARG A 1 255 ? -29.004 -18.479 21.616  1.00 35.69  ? 255  ARG A CA  1 
ATOM   2069 C  C   . ARG A 1 255 ? -27.898 -18.828 20.625  1.00 35.42  ? 255  ARG A C   1 
ATOM   2070 O  O   . ARG A 1 255 ? -26.709 -18.818 20.970  1.00 34.63  ? 255  ARG A O   1 
ATOM   2071 C  CB  . ARG A 1 255 ? -29.645 -19.753 22.153  1.00 40.31  ? 255  ARG A CB  1 
ATOM   2072 C  CG  . ARG A 1 255 ? -28.661 -20.712 22.799  1.00 47.28  ? 255  ARG A CG  1 
ATOM   2073 C  CD  . ARG A 1 255 ? -28.492 -21.972 21.955  1.00 55.03  ? 255  ARG A CD  1 
ATOM   2074 N  NE  . ARG A 1 255 ? -29.679 -22.822 21.974  1.00 68.28  ? 255  ARG A NE  1 
ATOM   2075 C  CZ  . ARG A 1 255 ? -29.675 -24.114 21.670  1.00 66.49  ? 255  ARG A CZ  1 
ATOM   2076 N  NH1 . ARG A 1 255 ? -28.553 -24.745 21.360  1.00 65.01  ? 255  ARG A NH1 1 
ATOM   2077 N  NH2 . ARG A 1 255 ? -30.823 -24.787 21.675  1.00 69.98  ? 255  ARG A NH2 1 
ATOM   2078 N  N   . TYR A 1 256 ? -28.276 -19.159 19.391  1.00 34.94  ? 256  TYR A N   1 
ATOM   2079 C  CA  . TYR A 1 256 ? -27.271 -19.460 18.378  1.00 31.79  ? 256  TYR A CA  1 
ATOM   2080 C  C   . TYR A 1 256 ? -26.401 -18.249 18.092  1.00 33.22  ? 256  TYR A C   1 
ATOM   2081 O  O   . TYR A 1 256 ? -25.195 -18.392 17.858  1.00 32.10  ? 256  TYR A O   1 
ATOM   2082 C  CB  . TYR A 1 256 ? -27.941 -19.942 17.094  1.00 34.13  ? 256  TYR A CB  1 
ATOM   2083 C  CG  . TYR A 1 256 ? -28.458 -21.356 17.189  1.00 36.92  ? 256  TYR A CG  1 
ATOM   2084 C  CD1 . TYR A 1 256 ? -27.692 -22.360 17.761  1.00 40.40  ? 256  TYR A CD1 1 
ATOM   2085 C  CD2 . TYR A 1 256 ? -29.723 -21.684 16.712  1.00 38.75  ? 256  TYR A CD2 1 
ATOM   2086 C  CE1 . TYR A 1 256 ? -28.161 -23.654 17.855  1.00 44.06  ? 256  TYR A CE1 1 
ATOM   2087 C  CE2 . TYR A 1 256 ? -30.200 -22.982 16.799  1.00 43.63  ? 256  TYR A CE2 1 
ATOM   2088 C  CZ  . TYR A 1 256 ? -29.417 -23.957 17.374  1.00 42.35  ? 256  TYR A CZ  1 
ATOM   2089 O  OH  . TYR A 1 256 ? -29.885 -25.246 17.459  1.00 50.54  ? 256  TYR A OH  1 
ATOM   2090 N  N   . GLN A 1 257 ? -26.999 -17.051 18.047  1.00 31.49  ? 257  GLN A N   1 
ATOM   2091 C  CA  . GLN A 1 257 ? -26.210 -15.850 17.773  1.00 31.57  ? 257  GLN A CA  1 
ATOM   2092 C  C   . GLN A 1 257 ? -25.206 -15.587 18.891  1.00 34.08  ? 257  GLN A C   1 
ATOM   2093 O  O   . GLN A 1 257 ? -24.066 -15.205 18.621  1.00 30.26  ? 257  GLN A O   1 
ATOM   2094 C  CB  . GLN A 1 257 ? -27.111 -14.620 17.582  1.00 34.24  ? 257  GLN A CB  1 
ATOM   2095 C  CG  . GLN A 1 257 ? -28.156 -14.683 16.448  1.00 31.36  ? 257  GLN A CG  1 
ATOM   2096 C  CD  . GLN A 1 257 ? -27.596 -14.961 15.044  1.00 32.69  ? 257  GLN A CD  1 
ATOM   2097 O  OE1 . GLN A 1 257 ? -26.391 -14.839 14.790  1.00 30.66  ? 257  GLN A OE1 1 
ATOM   2098 N  NE2 . GLN A 1 257 ? -28.496 -15.261 14.108  1.00 30.35  ? 257  GLN A NE2 1 
ATOM   2099 N  N   . ILE A 1 258 ? -25.600 -15.806 20.153  1.00 33.65  ? 258  ILE A N   1 
ATOM   2100 C  CA  . ILE A 1 258 ? -24.671 -15.588 21.262  1.00 31.27  ? 258  ILE A CA  1 
ATOM   2101 C  C   . ILE A 1 258 ? -23.476 -16.528 21.155  1.00 31.35  ? 258  ILE A C   1 
ATOM   2102 O  O   . ILE A 1 258 ? -22.327 -16.107 21.292  1.00 31.66  ? 258  ILE A O   1 
ATOM   2103 C  CB  . ILE A 1 258 ? -25.387 -15.744 22.620  1.00 34.65  ? 258  ILE A CB  1 
ATOM   2104 C  CG1 . ILE A 1 258 ? -26.412 -14.625 22.800  1.00 36.43  ? 258  ILE A CG1 1 
ATOM   2105 C  CG2 . ILE A 1 258 ? -24.358 -15.684 23.761  1.00 34.16  ? 258  ILE A CG2 1 
ATOM   2106 C  CD1 . ILE A 1 258 ? -27.272 -14.752 24.089  1.00 34.86  ? 258  ILE A CD1 1 
ATOM   2107 N  N   . ILE A 1 259 ? -23.733 -17.818 20.923  1.00 31.42  ? 259  ILE A N   1 
ATOM   2108 C  CA  . ILE A 1 259 ? -22.650 -18.776 20.727  1.00 33.28  ? 259  ILE A CA  1 
ATOM   2109 C  C   . ILE A 1 259 ? -21.748 -18.324 19.585  1.00 32.30  ? 259  ILE A C   1 
ATOM   2110 O  O   . ILE A 1 259 ? -20.511 -18.318 19.698  1.00 31.74  ? 259  ILE A O   1 
ATOM   2111 C  CB  . ILE A 1 259 ? -23.224 -20.179 20.455  1.00 37.83  ? 259  ILE A CB  1 
ATOM   2112 C  CG1 . ILE A 1 259 ? -23.859 -20.754 21.728  1.00 37.79  ? 259  ILE A CG1 1 
ATOM   2113 C  CG2 . ILE A 1 259 ? -22.142 -21.094 19.880  1.00 37.28  ? 259  ILE A CG2 1 
ATOM   2114 C  CD1 . ILE A 1 259 ? -24.610 -22.049 21.499  1.00 44.43  ? 259  ILE A CD1 1 
ATOM   2115 N  N   . THR A 1 260 ? -22.364 -17.959 18.459  1.00 30.39  ? 260  THR A N   1 
ATOM   2116 C  CA  . THR A 1 260 ? -21.618 -17.523 17.277  1.00 31.87  ? 260  THR A CA  1 
ATOM   2117 C  C   . THR A 1 260 ? -20.725 -16.334 17.602  1.00 34.37  ? 260  THR A C   1 
ATOM   2118 O  O   . THR A 1 260 ? -19.524 -16.328 17.282  1.00 33.50  ? 260  THR A O   1 
ATOM   2119 C  CB  . THR A 1 260 ? -22.607 -17.161 16.160  1.00 29.74  ? 260  THR A CB  1 
ATOM   2120 O  OG1 . THR A 1 260 ? -23.315 -18.342 15.753  1.00 34.17  ? 260  THR A OG1 1 
ATOM   2121 C  CG2 . THR A 1 260 ? -21.892 -16.558 14.955  1.00 31.73  ? 260  THR A CG2 1 
ATOM   2122 N  N   . PHE A 1 261 ? -21.297 -15.310 18.231  1.00 30.21  ? 261  PHE A N   1 
ATOM   2123 C  CA  . PHE A 1 261 ? -20.514 -14.101 18.455  1.00 32.53  ? 261  PHE A CA  1 
ATOM   2124 C  C   . PHE A 1 261 ? -19.461 -14.314 19.532  1.00 36.63  ? 261  PHE A C   1 
ATOM   2125 O  O   . PHE A 1 261 ? -18.385 -13.717 19.456  1.00 36.03  ? 261  PHE A O   1 
ATOM   2126 C  CB  . PHE A 1 261 ? -21.443 -12.914 18.769  1.00 35.14  ? 261  PHE A CB  1 
ATOM   2127 C  CG  . PHE A 1 261 ? -22.037 -12.284 17.529  1.00 33.44  ? 261  PHE A CG  1 
ATOM   2128 C  CD1 . PHE A 1 261 ? -21.372 -11.266 16.856  1.00 36.86  ? 261  PHE A CD1 1 
ATOM   2129 C  CD2 . PHE A 1 261 ? -23.257 -12.706 17.029  1.00 37.90  ? 261  PHE A CD2 1 
ATOM   2130 C  CE1 . PHE A 1 261 ? -21.902 -10.692 15.719  1.00 34.27  ? 261  PHE A CE1 1 
ATOM   2131 C  CE2 . PHE A 1 261 ? -23.789 -12.129 15.896  1.00 35.83  ? 261  PHE A CE2 1 
ATOM   2132 C  CZ  . PHE A 1 261 ? -23.112 -11.123 15.234  1.00 37.23  ? 261  PHE A CZ  1 
ATOM   2133 N  N   . LEU A 1 262 ? -19.717 -15.187 20.515  1.00 35.05  ? 262  LEU A N   1 
ATOM   2134 C  CA  . LEU A 1 262 ? -18.686 -15.452 21.517  1.00 35.96  ? 262  LEU A CA  1 
ATOM   2135 C  C   . LEU A 1 262 ? -17.486 -16.143 20.888  1.00 38.44  ? 262  LEU A C   1 
ATOM   2136 O  O   . LEU A 1 262 ? -16.338 -15.888 21.277  1.00 37.16  ? 262  LEU A O   1 
ATOM   2137 C  CB  . LEU A 1 262 ? -19.244 -16.299 22.660  1.00 35.94  ? 262  LEU A CB  1 
ATOM   2138 C  CG  . LEU A 1 262 ? -20.147 -15.535 23.633  1.00 36.14  ? 262  LEU A CG  1 
ATOM   2139 C  CD1 . LEU A 1 262 ? -20.698 -16.504 24.661  1.00 36.44  ? 262  LEU A CD1 1 
ATOM   2140 C  CD2 . LEU A 1 262 ? -19.401 -14.390 24.313  1.00 36.60  ? 262  LEU A CD2 1 
ATOM   2141 N  N   . ILE A 1 263 ? -17.732 -17.016 19.915  1.00 36.11  ? 263  ILE A N   1 
ATOM   2142 C  CA  . ILE A 1 263 ? -16.644 -17.708 19.235  1.00 33.33  ? 263  ILE A CA  1 
ATOM   2143 C  C   . ILE A 1 263 ? -16.039 -16.822 18.156  1.00 34.63  ? 263  ILE A C   1 
ATOM   2144 O  O   . ILE A 1 263 ? -14.840 -16.524 18.172  1.00 39.31  ? 263  ILE A O   1 
ATOM   2145 C  CB  . ILE A 1 263 ? -17.144 -19.043 18.661  1.00 37.01  ? 263  ILE A CB  1 
ATOM   2146 C  CG1 . ILE A 1 263 ? -17.532 -19.975 19.807  1.00 41.94  ? 263  ILE A CG1 1 
ATOM   2147 C  CG2 . ILE A 1 263 ? -16.100 -19.671 17.748  1.00 36.98  ? 263  ILE A CG2 1 
ATOM   2148 C  CD1 . ILE A 1 263 ? -18.333 -21.176 19.364  1.00 39.72  ? 263  ILE A CD1 1 
ATOM   2149 N  N   . ALA A 1 264 ? -16.869 -16.388 17.207  1.00 35.25  ? 264  ALA A N   1 
ATOM   2150 C  CA  . ALA A 1 264 ? -16.389 -15.593 16.082  1.00 37.15  ? 264  ALA A CA  1 
ATOM   2151 C  C   . ALA A 1 264 ? -15.925 -14.217 16.525  1.00 36.30  ? 264  ALA A C   1 
ATOM   2152 O  O   . ALA A 1 264 ? -15.019 -13.639 15.908  1.00 35.66  ? 264  ALA A O   1 
ATOM   2153 C  CB  . ALA A 1 264 ? -17.495 -15.460 15.031  1.00 36.33  ? 264  ALA A CB  1 
ATOM   2154 N  N   . GLY A 1 265 ? -16.527 -13.686 17.587  1.00 37.33  ? 265  GLY A N   1 
ATOM   2155 C  CA  . GLY A 1 265 ? -16.189 -12.377 18.097  1.00 38.90  ? 265  GLY A CA  1 
ATOM   2156 C  C   . GLY A 1 265 ? -14.895 -12.289 18.873  1.00 40.30  ? 265  GLY A C   1 
ATOM   2157 O  O   . GLY A 1 265 ? -14.564 -11.194 19.337  1.00 37.39  ? 265  GLY A O   1 
ATOM   2158 N  N   . HIS A 1 266 ? -14.151 -13.387 19.031  1.00 38.54  ? 266  HIS A N   1 
ATOM   2159 C  CA  . HIS A 1 266 ? -12.888 -13.306 19.765  1.00 36.62  ? 266  HIS A CA  1 
ATOM   2160 C  C   . HIS A 1 266 ? -11.774 -14.170 19.187  1.00 39.83  ? 266  HIS A C   1 
ATOM   2161 O  O   . HIS A 1 266 ? -10.608 -13.763 19.202  1.00 36.17  ? 266  HIS A O   1 
ATOM   2162 C  CB  . HIS A 1 266 ? -13.085 -13.695 21.236  1.00 37.44  ? 266  HIS A CB  1 
ATOM   2163 C  CG  . HIS A 1 266 ? -12.769 -15.132 21.536  1.00 34.43  ? 266  HIS A CG  1 
ATOM   2164 N  ND1 . HIS A 1 266 ? -13.686 -16.144 21.373  1.00 38.77  ? 266  HIS A ND1 1 
ATOM   2165 C  CD2 . HIS A 1 266 ? -11.640 -15.723 22.000  1.00 36.96  ? 266  HIS A CD2 1 
ATOM   2166 C  CE1 . HIS A 1 266 ? -13.139 -17.300 21.714  1.00 36.53  ? 266  HIS A CE1 1 
ATOM   2167 N  NE2 . HIS A 1 266 ? -11.896 -17.071 22.098  1.00 36.47  ? 266  HIS A NE2 1 
ATOM   2168 N  N   . GLU A 1 267 ? -12.093 -15.372 18.705  1.00 38.56  ? 267  GLU A N   1 
ATOM   2169 C  CA  . GLU A 1 267 ? -11.013 -16.323 18.452  1.00 38.00  ? 267  GLU A CA  1 
ATOM   2170 C  C   . GLU A 1 267 ? -10.081 -15.815 17.355  1.00 36.11  ? 267  GLU A C   1 
ATOM   2171 O  O   . GLU A 1 267 ? -8.852  -15.873 17.490  1.00 38.31  ? 267  GLU A O   1 
ATOM   2172 C  CB  . GLU A 1 267 ? -11.569 -17.698 18.101  1.00 36.85  ? 267  GLU A CB  1 
ATOM   2173 C  CG  . GLU A 1 267 ? -10.622 -18.444 17.201  1.00 36.70  ? 267  GLU A CG  1 
ATOM   2174 C  CD  . GLU A 1 267 ? -9.425  -19.004 17.952  1.00 44.09  ? 267  GLU A CD  1 
ATOM   2175 O  OE1 . GLU A 1 267 ? -8.457  -19.459 17.285  1.00 46.05  ? 267  GLU A OE1 1 
ATOM   2176 O  OE2 . GLU A 1 267 ? -9.467  -19.025 19.200  1.00 43.11  ? 267  GLU A OE2 1 
ATOM   2177 N  N   . THR A 1 268 ? -10.638 -15.259 16.293  1.00 33.10  ? 268  THR A N   1 
ATOM   2178 C  CA  . THR A 1 268 ? -9.791  -14.796 15.207  1.00 35.77  ? 268  THR A CA  1 
ATOM   2179 C  C   . THR A 1 268 ? -9.056  -13.505 15.548  1.00 32.97  ? 268  THR A C   1 
ATOM   2180 O  O   . THR A 1 268 ? -7.957  -13.281 15.019  1.00 35.94  ? 268  THR A O   1 
ATOM   2181 C  CB  . THR A 1 268 ? -10.626 -14.631 13.944  1.00 38.99  ? 268  THR A CB  1 
ATOM   2182 O  OG1 . THR A 1 268 ? -11.862 -13.980 14.274  1.00 35.36  ? 268  THR A OG1 1 
ATOM   2183 C  CG2 . THR A 1 268 ? -10.917 -16.016 13.341  1.00 33.38  ? 268  THR A CG2 1 
ATOM   2184 N  N   . THR A 1 269 ? -9.623  -12.648 16.408  1.00 30.58  ? 269  THR A N   1 
ATOM   2185 C  CA  . THR A 1 269 ? -8.926  -11.411 16.772  1.00 27.38  ? 269  THR A CA  1 
ATOM   2186 C  C   . THR A 1 269 ? -7.727  -11.714 17.665  1.00 30.04  ? 269  THR A C   1 
ATOM   2187 O  O   . THR A 1 269 ? -6.701  -11.020 17.594  1.00 31.97  ? 269  THR A O   1 
ATOM   2188 C  CB  . THR A 1 269 ? -9.891  -10.441 17.463  1.00 29.80  ? 269  THR A CB  1 
ATOM   2189 O  OG1 . THR A 1 269 ? -11.032 -10.240 16.614  1.00 29.07  ? 269  THR A OG1 1 
ATOM   2190 C  CG2 . THR A 1 269 ? -9.223  -9.087  17.747  1.00 30.81  ? 269  THR A CG2 1 
ATOM   2191 N  N   A SER A 1 270 ? -7.829  -12.746 18.501  0.61 30.32  ? 270  SER A N   1 
ATOM   2192 N  N   B SER A 1 270 ? -7.838  -12.735 18.516  0.39 30.35  ? 270  SER A N   1 
ATOM   2193 C  CA  A SER A 1 270 ? -6.670  -13.146 19.295  0.61 29.66  ? 270  SER A CA  1 
ATOM   2194 C  CA  B SER A 1 270 ? -6.680  -13.164 19.295  0.39 29.71  ? 270  SER A CA  1 
ATOM   2195 C  C   A SER A 1 270 ? -5.559  -13.695 18.404  0.61 31.72  ? 270  SER A C   1 
ATOM   2196 C  C   B SER A 1 270 ? -5.566  -13.665 18.384  0.39 31.71  ? 270  SER A C   1 
ATOM   2197 O  O   A SER A 1 270 ? -4.371  -13.456 18.663  0.61 32.83  ? 270  SER A O   1 
ATOM   2198 O  O   B SER A 1 270 ? -4.386  -13.364 18.607  0.39 32.79  ? 270  SER A O   1 
ATOM   2199 C  CB  A SER A 1 270 ? -7.083  -14.178 20.350  0.61 32.43  ? 270  SER A CB  1 
ATOM   2200 C  CB  B SER A 1 270 ? -7.088  -14.250 20.294  0.39 32.43  ? 270  SER A CB  1 
ATOM   2201 O  OG  A SER A 1 270 ? -7.536  -15.377 19.745  0.61 31.86  ? 270  SER A OG  1 
ATOM   2202 O  OG  B SER A 1 270 ? -5.953  -14.960 20.770  0.39 31.90  ? 270  SER A OG  1 
ATOM   2203 N  N   . GLY A 1 271 ? -5.921  -14.437 17.354  1.00 31.06  ? 271  GLY A N   1 
ATOM   2204 C  CA  . GLY A 1 271 ? -4.918  -14.861 16.391  1.00 30.79  ? 271  GLY A CA  1 
ATOM   2205 C  C   . GLY A 1 271 ? -4.286  -13.676 15.690  1.00 32.67  ? 271  GLY A C   1 
ATOM   2206 O  O   . GLY A 1 271 ? -3.060  -13.592 15.554  1.00 31.95  ? 271  GLY A O   1 
ATOM   2207 N  N   . LEU A 1 272 ? -5.114  -12.729 15.245  1.00 31.20  ? 272  LEU A N   1 
ATOM   2208 C  CA  . LEU A 1 272 ? -4.574  -11.537 14.586  1.00 32.74  ? 272  LEU A CA  1 
ATOM   2209 C  C   . LEU A 1 272 ? -3.558  -10.817 15.466  1.00 32.67  ? 272  LEU A C   1 
ATOM   2210 O  O   . LEU A 1 272 ? -2.442  -10.491 15.029  1.00 29.73  ? 272  LEU A O   1 
ATOM   2211 C  CB  . LEU A 1 272 ? -5.712  -10.592 14.211  1.00 31.12  ? 272  LEU A CB  1 
ATOM   2212 C  CG  . LEU A 1 272 ? -5.257  -9.209  13.733  1.00 29.96  ? 272  LEU A CG  1 
ATOM   2213 C  CD1 . LEU A 1 272 ? -4.298  -9.328  12.491  1.00 28.76  ? 272  LEU A CD1 1 
ATOM   2214 C  CD2 . LEU A 1 272 ? -6.470  -8.354  13.409  1.00 30.11  ? 272  LEU A CD2 1 
ATOM   2215 N  N   . LEU A 1 273 ? -3.941  -10.509 16.698  1.00 30.78  ? 273  LEU A N   1 
ATOM   2216 C  CA  . LEU A 1 273 ? -3.015  -9.811  17.581  1.00 30.44  ? 273  LEU A CA  1 
ATOM   2217 C  C   . LEU A 1 273 ? -1.733  -10.614 17.784  1.00 31.75  ? 273  LEU A C   1 
ATOM   2218 O  O   . LEU A 1 273 ? -0.632  -10.048 17.800  1.00 32.93  ? 273  LEU A O   1 
ATOM   2219 C  CB  . LEU A 1 273 ? -3.708  -9.510  18.905  1.00 29.26  ? 273  LEU A CB  1 
ATOM   2220 C  CG  . LEU A 1 273 ? -4.666  -8.327  18.848  1.00 29.21  ? 273  LEU A CG  1 
ATOM   2221 C  CD1 . LEU A 1 273 ? -5.579  -8.352  20.062  1.00 32.35  ? 273  LEU A CD1 1 
ATOM   2222 C  CD2 . LEU A 1 273 ? -3.877  -7.015  18.821  1.00 33.47  ? 273  LEU A CD2 1 
ATOM   2223 N  N   . SER A 1 274 ? -1.852  -11.933 17.916  1.00 29.15  ? 274  SER A N   1 
ATOM   2224 C  CA  . SER A 1 274 ? -0.670  -12.770 18.114  1.00 34.15  ? 274  SER A CA  1 
ATOM   2225 C  C   . SER A 1 274 ? 0.248   -12.703 16.902  1.00 34.93  ? 274  SER A C   1 
ATOM   2226 O  O   . SER A 1 274 ? 1.464   -12.519 17.040  1.00 31.55  ? 274  SER A O   1 
ATOM   2227 C  CB  . SER A 1 274 ? -1.085  -14.215 18.406  1.00 32.02  ? 274  SER A CB  1 
ATOM   2228 O  OG  . SER A 1 274 ? -1.908  -14.281 19.576  1.00 31.68  ? 274  SER A OG  1 
ATOM   2229 N  N   . PHE A 1 275 ? -0.319  -12.847 15.699  1.00 32.77  ? 275  PHE A N   1 
ATOM   2230 C  CA  . PHE A 1 275 ? 0.494   -12.725 14.487  1.00 32.85  ? 275  PHE A CA  1 
ATOM   2231 C  C   . PHE A 1 275 ? 1.096   -11.328 14.352  1.00 33.81  ? 275  PHE A C   1 
ATOM   2232 O  O   . PHE A 1 275 ? 2.257   -11.182 13.936  1.00 34.47  ? 275  PHE A O   1 
ATOM   2233 C  CB  . PHE A 1 275 ? -0.353  -13.073 13.253  1.00 29.90  ? 275  PHE A CB  1 
ATOM   2234 C  CG  . PHE A 1 275 ? -0.494  -14.547 13.013  1.00 33.33  ? 275  PHE A CG  1 
ATOM   2235 C  CD1 . PHE A 1 275 ? 0.624   -15.334 12.767  1.00 32.70  ? 275  PHE A CD1 1 
ATOM   2236 C  CD2 . PHE A 1 275 ? -1.748  -15.149 13.038  1.00 29.03  ? 275  PHE A CD2 1 
ATOM   2237 C  CE1 . PHE A 1 275 ? 0.498   -16.705 12.519  1.00 30.42  ? 275  PHE A CE1 1 
ATOM   2238 C  CE2 . PHE A 1 275 ? -1.890  -16.494 12.813  1.00 34.65  ? 275  PHE A CE2 1 
ATOM   2239 C  CZ  . PHE A 1 275 ? -0.760  -17.290 12.550  1.00 36.74  ? 275  PHE A CZ  1 
ATOM   2240 N  N   . ALA A 1 276 ? 0.340   -10.280 14.708  1.00 31.12  ? 276  ALA A N   1 
ATOM   2241 C  CA  . ALA A 1 276 ? 0.853   -8.925  14.518  1.00 30.21  ? 276  ALA A CA  1 
ATOM   2242 C  C   . ALA A 1 276 ? 2.048   -8.667  15.429  1.00 33.55  ? 276  ALA A C   1 
ATOM   2243 O  O   . ALA A 1 276 ? 3.065   -8.118  14.990  1.00 33.65  ? 276  ALA A O   1 
ATOM   2244 C  CB  . ALA A 1 276 ? -0.247  -7.881  14.755  1.00 33.07  ? 276  ALA A CB  1 
ATOM   2245 N  N   . LEU A 1 277 ? 1.963   -9.095  16.686  1.00 36.01  ? 277  LEU A N   1 
ATOM   2246 C  CA  . LEU A 1 277 ? 3.108   -8.938  17.580  1.00 30.52  ? 277  LEU A CA  1 
ATOM   2247 C  C   . LEU A 1 277 ? 4.287   -9.781  17.110  1.00 34.81  ? 277  LEU A C   1 
ATOM   2248 O  O   . LEU A 1 277 ? 5.437   -9.330  17.172  1.00 33.48  ? 277  LEU A O   1 
ATOM   2249 C  CB  . LEU A 1 277 ? 2.715   -9.308  19.009  1.00 34.08  ? 277  LEU A CB  1 
ATOM   2250 C  CG  . LEU A 1 277 ? 3.827   -9.074  20.036  1.00 34.90  ? 277  LEU A CG  1 
ATOM   2251 C  CD1 . LEU A 1 277 ? 4.260   -7.610  19.997  1.00 36.87  ? 277  LEU A CD1 1 
ATOM   2252 C  CD2 . LEU A 1 277 ? 3.400   -9.484  21.461  1.00 36.96  ? 277  LEU A CD2 1 
ATOM   2253 N  N   . TYR A 1 278 ? 4.026   -11.006 16.640  1.00 30.37  ? 278  TYR A N   1 
ATOM   2254 C  CA  . TYR A 1 278 ? 5.091   -11.833 16.070  1.00 33.62  ? 278  TYR A CA  1 
ATOM   2255 C  C   . TYR A 1 278 ? 5.816   -11.090 14.953  1.00 36.48  ? 278  TYR A C   1 
ATOM   2256 O  O   . TYR A 1 278 ? 7.051   -11.007 14.934  1.00 34.40  ? 278  TYR A O   1 
ATOM   2257 C  CB  . TYR A 1 278 ? 4.521   -13.155 15.537  1.00 31.75  ? 278  TYR A CB  1 
ATOM   2258 C  CG  . TYR A 1 278 ? 5.487   -13.888 14.627  1.00 35.49  ? 278  TYR A CG  1 
ATOM   2259 C  CD1 . TYR A 1 278 ? 6.429   -14.766 15.157  1.00 35.88  ? 278  TYR A CD1 1 
ATOM   2260 C  CD2 . TYR A 1 278 ? 5.479   -13.677 13.242  1.00 35.13  ? 278  TYR A CD2 1 
ATOM   2261 C  CE1 . TYR A 1 278 ? 7.322   -15.434 14.344  1.00 35.78  ? 278  TYR A CE1 1 
ATOM   2262 C  CE2 . TYR A 1 278 ? 6.382   -14.342 12.413  1.00 37.09  ? 278  TYR A CE2 1 
ATOM   2263 C  CZ  . TYR A 1 278 ? 7.298   -15.217 12.971  1.00 38.15  ? 278  TYR A CZ  1 
ATOM   2264 O  OH  . TYR A 1 278 ? 8.197   -15.886 12.170  1.00 38.50  ? 278  TYR A OH  1 
ATOM   2265 N  N   . PHE A 1 279 ? 5.067   -10.544 14.001  1.00 33.78  ? 279  PHE A N   1 
ATOM   2266 C  CA  . PHE A 1 279 ? 5.745   -9.873  12.896  1.00 33.16  ? 279  PHE A CA  1 
ATOM   2267 C  C   . PHE A 1 279 ? 6.441   -8.609  13.365  1.00 33.05  ? 279  PHE A C   1 
ATOM   2268 O  O   . PHE A 1 279 ? 7.461   -8.220  12.787  1.00 36.74  ? 279  PHE A O   1 
ATOM   2269 C  CB  . PHE A 1 279 ? 4.770   -9.558  11.754  1.00 32.45  ? 279  PHE A CB  1 
ATOM   2270 C  CG  . PHE A 1 279 ? 4.438   -10.747 10.911  1.00 33.61  ? 279  PHE A CG  1 
ATOM   2271 C  CD1 . PHE A 1 279 ? 5.421   -11.376 10.163  1.00 35.37  ? 279  PHE A CD1 1 
ATOM   2272 C  CD2 . PHE A 1 279 ? 3.142   -11.238 10.852  1.00 35.41  ? 279  PHE A CD2 1 
ATOM   2273 C  CE1 . PHE A 1 279 ? 5.125   -12.472 9.392   1.00 36.09  ? 279  PHE A CE1 1 
ATOM   2274 C  CE2 . PHE A 1 279 ? 2.842   -12.349 10.079  1.00 32.93  ? 279  PHE A CE2 1 
ATOM   2275 C  CZ  . PHE A 1 279 ? 3.828   -12.958 9.343   1.00 40.24  ? 279  PHE A CZ  1 
ATOM   2276 N  N   . LEU A 1 280 ? 5.917   -7.953  14.394  1.00 33.28  ? 280  LEU A N   1 
ATOM   2277 C  CA  . LEU A 1 280 ? 6.542   -6.720  14.850  1.00 33.73  ? 280  LEU A CA  1 
ATOM   2278 C  C   . LEU A 1 280 ? 7.891   -7.005  15.513  1.00 36.00  ? 280  LEU A C   1 
ATOM   2279 O  O   . LEU A 1 280 ? 8.873   -6.296  15.250  1.00 35.64  ? 280  LEU A O   1 
ATOM   2280 C  CB  . LEU A 1 280 ? 5.612   -5.969  15.799  1.00 34.31  ? 280  LEU A CB  1 
ATOM   2281 C  CG  . LEU A 1 280 ? 4.416   -5.244  15.152  1.00 35.28  ? 280  LEU A CG  1 
ATOM   2282 C  CD1 . LEU A 1 280 ? 3.644   -4.454  16.199  1.00 36.05  ? 280  LEU A CD1 1 
ATOM   2283 C  CD2 . LEU A 1 280 ? 4.872   -4.329  14.027  1.00 36.09  ? 280  LEU A CD2 1 
ATOM   2284 N  N   . VAL A 1 281 ? 7.969   -8.038  16.365  1.00 35.72  ? 281  VAL A N   1 
ATOM   2285 C  CA  . VAL A 1 281 ? 9.267   -8.334  16.992  1.00 33.67  ? 281  VAL A CA  1 
ATOM   2286 C  C   . VAL A 1 281 ? 10.247  -8.908  15.980  1.00 40.59  ? 281  VAL A C   1 
ATOM   2287 O  O   . VAL A 1 281 ? 11.463  -8.743  16.133  1.00 39.53  ? 281  VAL A O   1 
ATOM   2288 C  CB  . VAL A 1 281 ? 9.133   -9.266  18.213  1.00 36.44  ? 281  VAL A CB  1 
ATOM   2289 C  CG1 . VAL A 1 281 ? 8.290   -8.612  19.284  1.00 39.84  ? 281  VAL A CG1 1 
ATOM   2290 C  CG2 . VAL A 1 281 ? 8.612   -10.691 17.820  1.00 33.81  ? 281  VAL A CG2 1 
ATOM   2291 N  N   . LYS A 1 282 ? 9.759   -9.570  14.928  1.00 35.10  ? 282  LYS A N   1 
ATOM   2292 C  CA  . LYS A 1 282 ? 10.662  -10.031 13.876  1.00 38.10  ? 282  LYS A CA  1 
ATOM   2293 C  C   . LYS A 1 282 ? 11.075  -8.915  12.918  1.00 39.99  ? 282  LYS A C   1 
ATOM   2294 O  O   . LYS A 1 282 ? 11.990  -9.119  12.102  1.00 41.68  ? 282  LYS A O   1 
ATOM   2295 C  CB  . LYS A 1 282 ? 10.023  -11.167 13.081  1.00 39.88  ? 282  LYS A CB  1 
ATOM   2296 C  CG  . LYS A 1 282 ? 9.770   -12.473 13.866  1.00 37.79  ? 282  LYS A CG  1 
ATOM   2297 C  CD  . LYS A 1 282 ? 11.044  -13.062 14.508  1.00 36.51  ? 282  LYS A CD  1 
ATOM   2298 C  CE  . LYS A 1 282 ? 10.814  -14.502 14.969  1.00 36.42  ? 282  LYS A CE  1 
ATOM   2299 N  NZ  . LYS A 1 282 ? 11.992  -15.092 15.698  1.00 39.58  ? 282  LYS A NZ  1 
ATOM   2300 N  N   . ASN A 1 283 ? 10.438  -7.745  13.004  1.00 37.37  ? 283  ASN A N   1 
ATOM   2301 C  CA  . ASN A 1 283 ? 10.692  -6.625  12.092  1.00 38.38  ? 283  ASN A CA  1 
ATOM   2302 C  C   . ASN A 1 283 ? 10.791  -5.342  12.900  1.00 39.70  ? 283  ASN A C   1 
ATOM   2303 O  O   . ASN A 1 283 ? 9.904   -4.479  12.857  1.00 38.73  ? 283  ASN A O   1 
ATOM   2304 C  CB  . ASN A 1 283 ? 9.601   -6.535  11.022  1.00 37.91  ? 283  ASN A CB  1 
ATOM   2305 C  CG  . ASN A 1 283 ? 9.636   -7.709  10.067  1.00 34.62  ? 283  ASN A CG  1 
ATOM   2306 O  OD1 . ASN A 1 283 ? 10.413  -7.713  9.109   1.00 41.11  ? 283  ASN A OD1 1 
ATOM   2307 N  ND2 . ASN A 1 283 ? 8.788   -8.698  10.301  1.00 35.16  ? 283  ASN A ND2 1 
ATOM   2308 N  N   . PRO A 1 284 ? 11.892  -5.173  13.634  1.00 39.49  ? 284  PRO A N   1 
ATOM   2309 C  CA  . PRO A 1 284 ? 11.986  -4.054  14.590  1.00 42.71  ? 284  PRO A CA  1 
ATOM   2310 C  C   . PRO A 1 284 ? 11.801  -2.680  13.972  1.00 38.78  ? 284  PRO A C   1 
ATOM   2311 O  O   . PRO A 1 284 ? 11.328  -1.766  14.668  1.00 40.35  ? 284  PRO A O   1 
ATOM   2312 C  CB  . PRO A 1 284 ? 13.400  -4.207  15.172  1.00 43.67  ? 284  PRO A CB  1 
ATOM   2313 C  CG  . PRO A 1 284 ? 13.786  -5.627  14.906  1.00 46.01  ? 284  PRO A CG  1 
ATOM   2314 C  CD  . PRO A 1 284 ? 13.086  -6.035  13.645  1.00 42.70  ? 284  PRO A CD  1 
ATOM   2315 N  N   . HIS A 1 285 ? 12.208  -2.491  12.709  1.00 40.15  ? 285  HIS A N   1 
ATOM   2316 C  CA  . HIS A 1 285 ? 12.003  -1.206  12.042  1.00 41.81  ? 285  HIS A CA  1 
ATOM   2317 C  C   . HIS A 1 285 ? 10.520  -0.896  11.914  1.00 37.88  ? 285  HIS A C   1 
ATOM   2318 O  O   . HIS A 1 285 ? 10.090  0.247   12.120  1.00 35.60  ? 285  HIS A O   1 
ATOM   2319 C  CB  . HIS A 1 285 ? 12.662  -1.199  10.660  1.00 43.41  ? 285  HIS A CB  1 
ATOM   2320 C  CG  . HIS A 1 285 ? 14.142  -1.435  10.682  1.00 56.66  ? 285  HIS A CG  1 
ATOM   2321 N  ND1 . HIS A 1 285 ? 14.991  -0.785  11.554  1.00 61.61  ? 285  HIS A ND1 1 
ATOM   2322 C  CD2 . HIS A 1 285 ? 14.927  -2.242  9.925   1.00 61.81  ? 285  HIS A CD2 1 
ATOM   2323 C  CE1 . HIS A 1 285 ? 16.232  -1.188  11.339  1.00 63.14  ? 285  HIS A CE1 1 
ATOM   2324 N  NE2 . HIS A 1 285 ? 16.221  -2.069  10.353  1.00 62.27  ? 285  HIS A NE2 1 
ATOM   2325 N  N   . VAL A 1 286 ? 9.720   -1.916  11.600  1.00 40.88  ? 286  VAL A N   1 
ATOM   2326 C  CA  . VAL A 1 286 ? 8.271   -1.734  11.569  1.00 37.50  ? 286  VAL A CA  1 
ATOM   2327 C  C   . VAL A 1 286 ? 7.730   -1.462  12.969  1.00 37.42  ? 286  VAL A C   1 
ATOM   2328 O  O   . VAL A 1 286 ? 6.908   -0.551  13.166  1.00 36.80  ? 286  VAL A O   1 
ATOM   2329 C  CB  . VAL A 1 286 ? 7.599   -2.954  10.909  1.00 35.52  ? 286  VAL A CB  1 
ATOM   2330 C  CG1 . VAL A 1 286 ? 6.069   -2.750  10.863  1.00 34.11  ? 286  VAL A CG1 1 
ATOM   2331 C  CG2 . VAL A 1 286 ? 8.161   -3.180  9.490   1.00 35.13  ? 286  VAL A CG2 1 
ATOM   2332 N  N   . LEU A 1 287 ? 8.187   -2.225  13.970  1.00 41.33  ? 287  LEU A N   1 
ATOM   2333 C  CA  . LEU A 1 287 ? 7.778   -1.951  15.346  1.00 35.37  ? 287  LEU A CA  1 
ATOM   2334 C  C   . LEU A 1 287 ? 8.047   -0.498  15.729  1.00 35.20  ? 287  LEU A C   1 
ATOM   2335 O  O   . LEU A 1 287 ? 7.181   0.191   16.293  1.00 36.10  ? 287  LEU A O   1 
ATOM   2336 C  CB  . LEU A 1 287 ? 8.494   -2.907  16.313  1.00 37.28  ? 287  LEU A CB  1 
ATOM   2337 C  CG  . LEU A 1 287 ? 7.877   -3.003  17.722  1.00 38.08  ? 287  LEU A CG  1 
ATOM   2338 C  CD1 . LEU A 1 287 ? 8.352   -4.245  18.457  1.00 43.72  ? 287  LEU A CD1 1 
ATOM   2339 C  CD2 . LEU A 1 287 ? 8.189   -1.748  18.533  1.00 39.35  ? 287  LEU A CD2 1 
ATOM   2340 N  N   . GLN A 1 288 ? 9.258   -0.014  15.437  1.00 38.87  ? 288  GLN A N   1 
ATOM   2341 C  CA  . GLN A 1 288 ? 9.584   1.365   15.777  1.00 38.48  ? 288  GLN A CA  1 
ATOM   2342 C  C   . GLN A 1 288 ? 8.605   2.341   15.137  1.00 38.59  ? 288  GLN A C   1 
ATOM   2343 O  O   . GLN A 1 288 ? 8.119   3.269   15.797  1.00 40.25  ? 288  GLN A O   1 
ATOM   2344 C  CB  . GLN A 1 288 ? 11.011  1.698   15.347  1.00 44.39  ? 288  GLN A CB  1 
ATOM   2345 C  CG  . GLN A 1 288 ? 11.367  3.148   15.615  1.00 44.24  ? 288  GLN A CG  1 
ATOM   2346 C  CD  . GLN A 1 288 ? 12.848  3.406   15.538  1.00 54.03  ? 288  GLN A CD  1 
ATOM   2347 O  OE1 . GLN A 1 288 ? 13.594  2.640   14.925  1.00 63.09  ? 288  GLN A OE1 1 
ATOM   2348 N  NE2 . GLN A 1 288 ? 13.288  4.491   16.161  1.00 63.67  ? 288  GLN A NE2 1 
ATOM   2349 N  N   . LYS A 1 289 ? 8.322   2.163   13.838  1.00 38.03  ? 289  LYS A N   1 
ATOM   2350 C  CA  . LYS A 1 289 ? 7.424   3.094   13.163  1.00 33.74  ? 289  LYS A CA  1 
ATOM   2351 C  C   . LYS A 1 289 ? 6.050   3.098   13.823  1.00 34.64  ? 289  LYS A C   1 
ATOM   2352 O  O   . LYS A 1 289 ? 5.460   4.163   14.045  1.00 35.38  ? 289  LYS A O   1 
ATOM   2353 C  CB  . LYS A 1 289 ? 7.321   2.742   11.674  1.00 36.72  ? 289  LYS A CB  1 
ATOM   2354 C  CG  . LYS A 1 289 ? 6.691   3.826   10.810  1.00 40.10  ? 289  LYS A CG  1 
ATOM   2355 C  CD  . LYS A 1 289 ? 6.889   3.537   9.302   1.00 39.98  ? 289  LYS A CD  1 
ATOM   2356 C  CE  . LYS A 1 289 ? 5.937   4.351   8.445   1.00 45.13  ? 289  LYS A CE  1 
ATOM   2357 N  NZ  . LYS A 1 289 ? 6.176   4.113   6.989   1.00 47.21  ? 289  LYS A NZ  1 
ATOM   2358 N  N   . ALA A 1 290 ? 5.532   1.915   14.161  1.00 39.46  ? 290  ALA A N   1 
ATOM   2359 C  CA  . ALA A 1 290 ? 4.211   1.855   14.784  1.00 37.85  ? 290  ALA A CA  1 
ATOM   2360 C  C   . ALA A 1 290 ? 4.255   2.384   16.212  1.00 30.53  ? 290  ALA A C   1 
ATOM   2361 O  O   . ALA A 1 290 ? 3.290   3.004   16.687  1.00 36.88  ? 290  ALA A O   1 
ATOM   2362 C  CB  . ALA A 1 290 ? 3.685   0.420   14.740  1.00 37.53  ? 290  ALA A CB  1 
ATOM   2363 N  N   . ALA A 1 291 ? 5.371   2.156   16.916  1.00 33.35  ? 291  ALA A N   1 
ATOM   2364 C  CA  . ALA A 1 291 ? 5.527   2.712   18.255  1.00 36.76  ? 291  ALA A CA  1 
ATOM   2365 C  C   . ALA A 1 291 ? 5.594   4.238   18.220  1.00 37.16  ? 291  ALA A C   1 
ATOM   2366 O  O   . ALA A 1 291 ? 5.028   4.916   19.087  1.00 37.30  ? 291  ALA A O   1 
ATOM   2367 C  CB  . ALA A 1 291 ? 6.780   2.130   18.913  1.00 37.71  ? 291  ALA A CB  1 
ATOM   2368 N  N   . GLU A 1 292 ? 6.281   4.799   17.221  1.00 38.31  ? 292  GLU A N   1 
ATOM   2369 C  CA  . GLU A 1 292 ? 6.310   6.254   17.096  1.00 37.82  ? 292  GLU A CA  1 
ATOM   2370 C  C   . GLU A 1 292 ? 4.907   6.810   16.903  1.00 38.52  ? 292  GLU A C   1 
ATOM   2371 O  O   . GLU A 1 292 ? 4.533   7.804   17.532  1.00 41.31  ? 292  GLU A O   1 
ATOM   2372 C  CB  . GLU A 1 292 ? 7.226   6.656   15.945  1.00 40.85  ? 292  GLU A CB  1 
ATOM   2373 C  CG  . GLU A 1 292 ? 8.688   6.672   16.372  1.00 46.23  ? 292  GLU A CG  1 
ATOM   2374 C  CD  . GLU A 1 292 ? 9.662   6.561   15.215  1.00 52.73  ? 292  GLU A CD  1 
ATOM   2375 O  OE1 . GLU A 1 292 ? 9.230   6.672   14.051  1.00 55.29  ? 292  GLU A OE1 1 
ATOM   2376 O  OE2 . GLU A 1 292 ? 10.865  6.341   15.477  1.00 52.91  ? 292  GLU A OE2 1 
ATOM   2377 N  N   . GLU A 1 293 ? 4.103   6.157   16.060  1.00 39.51  ? 293  GLU A N   1 
ATOM   2378 C  CA  . GLU A 1 293 ? 2.716   6.579   15.897  1.00 39.56  ? 293  GLU A CA  1 
ATOM   2379 C  C   . GLU A 1 293 ? 1.971   6.505   17.222  1.00 37.25  ? 293  GLU A C   1 
ATOM   2380 O  O   . GLU A 1 293 ? 1.287   7.452   17.625  1.00 37.83  ? 293  GLU A O   1 
ATOM   2381 C  CB  . GLU A 1 293 ? 2.021   5.711   14.848  1.00 36.93  ? 293  GLU A CB  1 
ATOM   2382 C  CG  . GLU A 1 293 ? 0.574   6.160   14.589  1.00 37.85  ? 293  GLU A CG  1 
ATOM   2383 C  CD  . GLU A 1 293 ? -0.089  5.322   13.531  1.00 39.34  ? 293  GLU A CD  1 
ATOM   2384 O  OE1 . GLU A 1 293 ? -0.464  4.166   13.839  1.00 35.90  ? 293  GLU A OE1 1 
ATOM   2385 O  OE2 . GLU A 1 293 ? -0.226  5.812   12.395  1.00 37.50  ? 293  GLU A OE2 1 
ATOM   2386 N  N   . ALA A 1 294 ? 2.096   5.374   17.915  1.00 37.52  ? 294  ALA A N   1 
ATOM   2387 C  CA  . ALA A 1 294 ? 1.410   5.199   19.185  1.00 37.08  ? 294  ALA A CA  1 
ATOM   2388 C  C   . ALA A 1 294 ? 1.760   6.320   20.157  1.00 33.65  ? 294  ALA A C   1 
ATOM   2389 O  O   . ALA A 1 294 ? 0.875   6.908   20.792  1.00 37.48  ? 294  ALA A O   1 
ATOM   2390 C  CB  . ALA A 1 294 ? 1.769   3.831   19.762  1.00 34.91  ? 294  ALA A CB  1 
ATOM   2391 N  N   . ALA A 1 295 ? 3.053   6.645   20.265  1.00 43.83  ? 295  ALA A N   1 
ATOM   2392 C  CA  . ALA A 1 295 ? 3.478   7.709   21.173  1.00 41.64  ? 295  ALA A CA  1 
ATOM   2393 C  C   . ALA A 1 295 ? 2.883   9.054   20.771  1.00 42.98  ? 295  ALA A C   1 
ATOM   2394 O  O   . ALA A 1 295 ? 2.450   9.837   21.629  1.00 40.81  ? 295  ALA A O   1 
ATOM   2395 C  CB  . ALA A 1 295 ? 5.006   7.788   21.207  1.00 41.55  ? 295  ALA A CB  1 
ATOM   2396 N  N   . ARG A 1 296 ? 2.847   9.340   19.471  1.00 44.00  ? 296  ARG A N   1 
ATOM   2397 C  CA  . ARG A 1 296 ? 2.370   10.643  19.024  1.00 40.97  ? 296  ARG A CA  1 
ATOM   2398 C  C   . ARG A 1 296 ? 0.860   10.768  19.171  1.00 40.51  ? 296  ARG A C   1 
ATOM   2399 O  O   . ARG A 1 296 ? 0.357   11.853  19.493  1.00 39.65  ? 296  ARG A O   1 
ATOM   2400 C  CB  . ARG A 1 296 ? 2.790   10.887  17.575  1.00 45.39  ? 296  ARG A CB  1 
ATOM   2401 C  CG  . ARG A 1 296 ? 1.941   11.917  16.876  1.00 44.60  ? 296  ARG A CG  1 
ATOM   2402 C  CD  . ARG A 1 296 ? 2.535   12.314  15.551  1.00 50.25  ? 296  ARG A CD  1 
ATOM   2403 N  NE  . ARG A 1 296 ? 3.137   11.164  14.893  1.00 52.91  ? 296  ARG A NE  1 
ATOM   2404 C  CZ  . ARG A 1 296 ? 2.479   10.357  14.075  1.00 54.65  ? 296  ARG A CZ  1 
ATOM   2405 N  NH1 . ARG A 1 296 ? 1.172   10.495  13.878  1.00 47.95  ? 296  ARG A NH1 1 
ATOM   2406 N  NH2 . ARG A 1 296 ? 3.145   9.390   13.439  1.00 53.46  ? 296  ARG A NH2 1 
ATOM   2407 N  N   . VAL A 1 297 ? 0.124   9.676   18.982  1.00 39.98  ? 297  VAL A N   1 
ATOM   2408 C  CA  . VAL A 1 297 ? -1.336  9.751   18.972  1.00 38.58  ? 297  VAL A CA  1 
ATOM   2409 C  C   . VAL A 1 297 ? -1.933  9.552   20.361  1.00 40.39  ? 297  VAL A C   1 
ATOM   2410 O  O   . VAL A 1 297 ? -2.875  10.252  20.744  1.00 40.02  ? 297  VAL A O   1 
ATOM   2411 C  CB  . VAL A 1 297 ? -1.904  8.728   17.967  1.00 35.77  ? 297  VAL A CB  1 
ATOM   2412 C  CG1 . VAL A 1 297 ? -3.411  8.594   18.138  1.00 36.19  ? 297  VAL A CG1 1 
ATOM   2413 C  CG2 . VAL A 1 297 ? -1.551  9.123   16.529  1.00 39.16  ? 297  VAL A CG2 1 
ATOM   2414 N  N   . LEU A 1 298 ? -1.433  8.588   21.134  1.00 40.19  ? 298  LEU A N   1 
ATOM   2415 C  CA  . LEU A 1 298 ? -2.084  8.215   22.386  1.00 41.63  ? 298  LEU A CA  1 
ATOM   2416 C  C   . LEU A 1 298 ? -1.526  9.077   23.524  1.00 43.50  ? 298  LEU A C   1 
ATOM   2417 O  O   . LEU A 1 298 ? -0.772  8.633   24.393  1.00 43.61  ? 298  LEU A O   1 
ATOM   2418 C  CB  . LEU A 1 298 ? -1.916  6.721   22.643  1.00 36.77  ? 298  LEU A CB  1 
ATOM   2419 C  CG  . LEU A 1 298 ? -2.460  5.832   21.515  1.00 36.97  ? 298  LEU A CG  1 
ATOM   2420 C  CD1 . LEU A 1 298 ? -2.160  4.363   21.800  1.00 37.47  ? 298  LEU A CD1 1 
ATOM   2421 C  CD2 . LEU A 1 298 ? -3.960  6.070   21.348  1.00 40.33  ? 298  LEU A CD2 1 
ATOM   2422 N  N   . VAL A 1 299 ? -1.933  10.354  23.503  1.00 43.55  ? 299  VAL A N   1 
ATOM   2423 C  CA  . VAL A 1 299 ? -1.366  11.354  24.411  1.00 46.21  ? 299  VAL A CA  1 
ATOM   2424 C  C   . VAL A 1 299 ? -2.071  11.412  25.757  1.00 47.84  ? 299  VAL A C   1 
ATOM   2425 O  O   . VAL A 1 299 ? -1.664  12.199  26.623  1.00 47.47  ? 299  VAL A O   1 
ATOM   2426 C  CB  . VAL A 1 299 ? -1.381  12.761  23.770  1.00 43.23  ? 299  VAL A CB  1 
ATOM   2427 C  CG1 . VAL A 1 299 ? -0.628  12.746  22.449  1.00 46.36  ? 299  VAL A CG1 1 
ATOM   2428 C  CG2 . VAL A 1 299 ? -2.816  13.239  23.566  1.00 42.22  ? 299  VAL A CG2 1 
ATOM   2429 N  N   . ASP A 1 300 ? -3.113  10.620  25.967  1.00 44.51  ? 300  ASP A N   1 
ATOM   2430 C  CA  . ASP A 1 300 ? -3.815  10.574  27.237  1.00 42.98  ? 300  ASP A CA  1 
ATOM   2431 C  C   . ASP A 1 300 ? -3.606  9.221   27.908  1.00 45.27  ? 300  ASP A C   1 
ATOM   2432 O  O   . ASP A 1 300 ? -3.256  8.237   27.248  1.00 42.21  ? 300  ASP A O   1 
ATOM   2433 C  CB  . ASP A 1 300 ? -5.315  10.828  27.034  1.00 44.11  ? 300  ASP A CB  1 
ATOM   2434 C  CG  . ASP A 1 300 ? -5.600  12.191  26.421  1.00 48.14  ? 300  ASP A CG  1 
ATOM   2435 O  OD1 . ASP A 1 300 ? -4.949  13.174  26.832  1.00 45.12  ? 300  ASP A OD1 1 
ATOM   2436 O  OD2 . ASP A 1 300 ? -6.457  12.278  25.511  1.00 50.85  ? 300  ASP A OD2 1 
ATOM   2437 N  N   . PRO A 1 301 ? -3.807  9.133   29.226  1.00 46.80  ? 301  PRO A N   1 
ATOM   2438 C  CA  . PRO A 1 301 ? -3.661  7.828   29.897  1.00 49.49  ? 301  PRO A CA  1 
ATOM   2439 C  C   . PRO A 1 301 ? -4.624  6.778   29.370  1.00 45.17  ? 301  PRO A C   1 
ATOM   2440 O  O   . PRO A 1 301 ? -4.272  5.593   29.326  1.00 46.65  ? 301  PRO A O   1 
ATOM   2441 C  CB  . PRO A 1 301 ? -3.939  8.154   31.374  1.00 49.36  ? 301  PRO A CB  1 
ATOM   2442 C  CG  . PRO A 1 301 ? -3.766  9.647   31.492  1.00 52.20  ? 301  PRO A CG  1 
ATOM   2443 C  CD  . PRO A 1 301 ? -4.175  10.208  30.160  1.00 50.69  ? 301  PRO A CD  1 
ATOM   2444 N  N   . VAL A 1 302 ? -5.823  7.186   28.976  1.00 43.78  ? 302  VAL A N   1 
ATOM   2445 C  CA  . VAL A 1 302 ? -6.866  6.335   28.407  1.00 45.97  ? 302  VAL A CA  1 
ATOM   2446 C  C   . VAL A 1 302 ? -7.009  6.701   26.931  1.00 44.24  ? 302  VAL A C   1 
ATOM   2447 O  O   . VAL A 1 302 ? -7.267  7.871   26.619  1.00 44.60  ? 302  VAL A O   1 
ATOM   2448 C  CB  . VAL A 1 302 ? -8.204  6.527   29.147  1.00 46.12  ? 302  VAL A CB  1 
ATOM   2449 C  CG1 . VAL A 1 302 ? -9.259  5.579   28.619  1.00 53.54  ? 302  VAL A CG1 1 
ATOM   2450 C  CG2 . VAL A 1 302 ? -8.027  6.357   30.667  1.00 53.07  ? 302  VAL A CG2 1 
ATOM   2451 N  N   . PRO A 1 303 ? -6.860  5.761   25.998  1.00 43.62  ? 303  PRO A N   1 
ATOM   2452 C  CA  . PRO A 1 303 ? -7.120  6.091   24.586  1.00 42.13  ? 303  PRO A CA  1 
ATOM   2453 C  C   . PRO A 1 303 ? -8.588  6.420   24.340  1.00 40.79  ? 303  PRO A C   1 
ATOM   2454 O  O   . PRO A 1 303 ? -9.490  5.824   24.931  1.00 34.68  ? 303  PRO A O   1 
ATOM   2455 C  CB  . PRO A 1 303 ? -6.696  4.822   23.838  1.00 44.58  ? 303  PRO A CB  1 
ATOM   2456 C  CG  . PRO A 1 303 ? -5.758  4.111   24.793  1.00 41.69  ? 303  PRO A CG  1 
ATOM   2457 C  CD  . PRO A 1 303 ? -6.283  4.415   26.156  1.00 42.18  ? 303  PRO A CD  1 
ATOM   2458 N  N   . SER A 1 304 ? -8.829  7.389   23.458  1.00 39.06  ? 304  SER A N   1 
ATOM   2459 C  CA  . SER A 1 304 ? -10.194 7.709   23.063  1.00 40.18  ? 304  SER A CA  1 
ATOM   2460 C  C   . SER A 1 304 ? -10.537 7.054   21.724  1.00 36.47  ? 304  SER A C   1 
ATOM   2461 O  O   . SER A 1 304 ? -9.662  6.622   20.970  1.00 35.58  ? 304  SER A O   1 
ATOM   2462 C  CB  . SER A 1 304 ? -10.389 9.222   22.961  1.00 40.59  ? 304  SER A CB  1 
ATOM   2463 O  OG  . SER A 1 304 ? -9.759  9.713   21.793  1.00 37.64  ? 304  SER A OG  1 
ATOM   2464 N  N   . TYR A 1 305 ? -11.841 6.983   21.432  1.00 36.03  ? 305  TYR A N   1 
ATOM   2465 C  CA  . TYR A 1 305 ? -12.267 6.449   20.139  1.00 37.33  ? 305  TYR A CA  1 
ATOM   2466 C  C   . TYR A 1 305 ? -11.631 7.226   18.994  1.00 39.57  ? 305  TYR A C   1 
ATOM   2467 O  O   . TYR A 1 305 ? -11.141 6.634   18.025  1.00 37.84  ? 305  TYR A O   1 
ATOM   2468 C  CB  . TYR A 1 305 ? -13.791 6.491   20.031  1.00 40.38  ? 305  TYR A CB  1 
ATOM   2469 C  CG  . TYR A 1 305 ? -14.312 6.121   18.667  1.00 41.47  ? 305  TYR A CG  1 
ATOM   2470 C  CD1 . TYR A 1 305 ? -14.558 4.794   18.332  1.00 40.17  ? 305  TYR A CD1 1 
ATOM   2471 C  CD2 . TYR A 1 305 ? -14.529 7.100   17.693  1.00 41.01  ? 305  TYR A CD2 1 
ATOM   2472 C  CE1 . TYR A 1 305 ? -15.024 4.451   17.066  1.00 41.94  ? 305  TYR A CE1 1 
ATOM   2473 C  CE2 . TYR A 1 305 ? -14.991 6.765   16.432  1.00 42.01  ? 305  TYR A CE2 1 
ATOM   2474 C  CZ  . TYR A 1 305 ? -15.228 5.440   16.124  1.00 40.70  ? 305  TYR A CZ  1 
ATOM   2475 O  OH  . TYR A 1 305 ? -15.696 5.100   14.875  1.00 50.49  ? 305  TYR A OH  1 
ATOM   2476 N  N   . LYS A 1 306 ? -11.639 8.565   19.087  1.00 40.73  ? 306  LYS A N   1 
ATOM   2477 C  CA  . LYS A 1 306 ? -11.071 9.390   18.025  1.00 39.28  ? 306  LYS A CA  1 
ATOM   2478 C  C   . LYS A 1 306 ? -9.585  9.122   17.842  1.00 37.07  ? 306  LYS A C   1 
ATOM   2479 O  O   . LYS A 1 306 ? -9.073  9.167   16.719  1.00 40.10  ? 306  LYS A O   1 
ATOM   2480 C  CB  . LYS A 1 306 ? -11.294 10.873  18.326  1.00 46.24  ? 306  LYS A CB  1 
ATOM   2481 C  CG  . LYS A 1 306 ? -12.748 11.283  18.367  1.00 46.96  ? 306  LYS A CG  1 
ATOM   2482 C  CD  . LYS A 1 306 ? -12.933 12.689  17.850  1.00 54.89  ? 306  LYS A CD  1 
ATOM   2483 C  CE  . LYS A 1 306 ? -13.826 13.480  18.788  1.00 64.55  ? 306  LYS A CE  1 
ATOM   2484 N  NZ  . LYS A 1 306 ? -15.244 13.492  18.333  1.00 65.33  ? 306  LYS A NZ  1 
ATOM   2485 N  N   . GLN A 1 307 ? -8.866  8.860   18.938  1.00 37.31  ? 307  GLN A N   1 
ATOM   2486 C  CA  . GLN A 1 307 ? -7.432  8.610   18.826  1.00 37.13  ? 307  GLN A CA  1 
ATOM   2487 C  C   . GLN A 1 307 ? -7.152  7.265   18.163  1.00 32.51  ? 307  GLN A C   1 
ATOM   2488 O  O   . GLN A 1 307 ? -6.218  7.147   17.367  1.00 37.13  ? 307  GLN A O   1 
ATOM   2489 C  CB  . GLN A 1 307 ? -6.768  8.678   20.208  1.00 37.73  ? 307  GLN A CB  1 
ATOM   2490 C  CG  . GLN A 1 307 ? -6.690  10.096  20.777  1.00 39.75  ? 307  GLN A CG  1 
ATOM   2491 C  CD  . GLN A 1 307 ? -6.417  10.121  22.282  1.00 44.32  ? 307  GLN A CD  1 
ATOM   2492 O  OE1 . GLN A 1 307 ? -6.486  9.094   22.947  1.00 40.44  ? 307  GLN A OE1 1 
ATOM   2493 N  NE2 . GLN A 1 307 ? -6.102  11.302  22.816  1.00 44.09  ? 307  GLN A NE2 1 
ATOM   2494 N  N   . VAL A 1 308 ? -7.928  6.230   18.503  1.00 38.22  ? 308  VAL A N   1 
ATOM   2495 C  CA  . VAL A 1 308 ? -7.738  4.937   17.853  1.00 35.92  ? 308  VAL A CA  1 
ATOM   2496 C  C   . VAL A 1 308 ? -7.914  5.077   16.345  1.00 39.02  ? 308  VAL A C   1 
ATOM   2497 O  O   . VAL A 1 308 ? -7.184  4.464   15.559  1.00 36.18  ? 308  VAL A O   1 
ATOM   2498 C  CB  . VAL A 1 308 ? -8.698  3.891   18.449  1.00 38.37  ? 308  VAL A CB  1 
ATOM   2499 C  CG1 . VAL A 1 308 ? -8.622  2.577   17.638  1.00 34.70  ? 308  VAL A CG1 1 
ATOM   2500 C  CG2 . VAL A 1 308 ? -8.367  3.654   19.925  1.00 34.61  ? 308  VAL A CG2 1 
ATOM   2501 N  N   . LYS A 1 309 ? -8.861  5.913   15.916  1.00 38.41  ? 309  LYS A N   1 
ATOM   2502 C  CA  . LYS A 1 309 ? -9.077  6.115   14.489  1.00 37.45  ? 309  LYS A CA  1 
ATOM   2503 C  C   . LYS A 1 309 ? -7.869  6.732   13.800  1.00 41.13  ? 309  LYS A C   1 
ATOM   2504 O  O   . LYS A 1 309 ? -7.753  6.631   12.575  1.00 39.39  ? 309  LYS A O   1 
ATOM   2505 C  CB  . LYS A 1 309 ? -10.296 6.995   14.265  1.00 39.99  ? 309  LYS A CB  1 
ATOM   2506 C  CG  . LYS A 1 309 ? -11.599 6.314   14.582  1.00 39.18  ? 309  LYS A CG  1 
ATOM   2507 C  CD  . LYS A 1 309 ? -11.620 4.926   13.959  1.00 42.58  ? 309  LYS A CD  1 
ATOM   2508 C  CE  . LYS A 1 309 ? -13.033 4.386   13.857  1.00 48.59  ? 309  LYS A CE  1 
ATOM   2509 N  NZ  . LYS A 1 309 ? -13.064 2.996   13.294  1.00 57.23  ? 309  LYS A NZ  1 
ATOM   2510 N  N   . GLN A 1 310 ? -6.975  7.378   14.549  1.00 37.65  ? 310  GLN A N   1 
ATOM   2511 C  CA  . GLN A 1 310 ? -5.803  8.009   13.951  1.00 39.47  ? 310  GLN A CA  1 
ATOM   2512 C  C   . GLN A 1 310 ? -4.569  7.122   13.978  1.00 38.66  ? 310  GLN A C   1 
ATOM   2513 O  O   . GLN A 1 310 ? -3.501  7.550   13.509  1.00 37.64  ? 310  GLN A O   1 
ATOM   2514 C  CB  . GLN A 1 310 ? -5.514  9.352   14.645  1.00 40.24  ? 310  GLN A CB  1 
ATOM   2515 C  CG  . GLN A 1 310 ? -6.556  10.440  14.335  1.00 44.00  ? 310  GLN A CG  1 
ATOM   2516 C  CD  . GLN A 1 310 ? -6.805  10.607  12.833  1.00 48.92  ? 310  GLN A CD  1 
ATOM   2517 O  OE1 . GLN A 1 310 ? -5.860  10.732  12.056  1.00 51.71  ? 310  GLN A OE1 1 
ATOM   2518 N  NE2 . GLN A 1 310 ? -8.074  10.589  12.421  1.00 48.81  ? 310  GLN A NE2 1 
ATOM   2519 N  N   . LEU A 1 311 ? -4.684  5.893   14.492  1.00 34.45  ? 311  LEU A N   1 
ATOM   2520 C  CA  . LEU A 1 311 ? -3.566  4.944   14.488  1.00 34.18  ? 311  LEU A CA  1 
ATOM   2521 C  C   . LEU A 1 311 ? -3.530  4.223   13.135  1.00 37.89  ? 311  LEU A C   1 
ATOM   2522 O  O   . LEU A 1 311 ? -3.739  3.011   13.008  1.00 35.50  ? 311  LEU A O   1 
ATOM   2523 C  CB  . LEU A 1 311 ? -3.691  3.973   15.657  1.00 35.32  ? 311  LEU A CB  1 
ATOM   2524 C  CG  . LEU A 1 311 ? -3.560  4.578   17.064  1.00 33.31  ? 311  LEU A CG  1 
ATOM   2525 C  CD1 . LEU A 1 311 ? -3.936  3.543   18.111  1.00 35.41  ? 311  LEU A CD1 1 
ATOM   2526 C  CD2 . LEU A 1 311 ? -2.120  5.083   17.288  1.00 36.06  ? 311  LEU A CD2 1 
ATOM   2527 N  N   . LYS A 1 312 ? -3.230  5.009   12.101  1.00 37.16  ? 312  LYS A N   1 
ATOM   2528 C  CA  . LYS A 1 312 ? -3.382  4.538   10.730  1.00 36.91  ? 312  LYS A CA  1 
ATOM   2529 C  C   . LYS A 1 312 ? -2.309  3.518   10.366  1.00 38.41  ? 312  LYS A C   1 
ATOM   2530 O  O   . LYS A 1 312 ? -2.594  2.529   9.682   1.00 33.22  ? 312  LYS A O   1 
ATOM   2531 C  CB  . LYS A 1 312 ? -3.374  5.742   9.782   1.00 38.29  ? 312  LYS A CB  1 
ATOM   2532 C  CG  . LYS A 1 312 ? -4.770  6.359   9.650   1.00 46.58  ? 312  LYS A CG  1 
ATOM   2533 C  CD  . LYS A 1 312 ? -4.773  7.794   9.152   1.00 50.38  ? 312  LYS A CD  1 
ATOM   2534 C  CE  . LYS A 1 312 ? -6.210  8.334   9.150   1.00 58.70  ? 312  LYS A CE  1 
ATOM   2535 N  NZ  . LYS A 1 312 ? -6.267  9.826   9.153   1.00 64.09  ? 312  LYS A NZ  1 
ATOM   2536 N  N   . TYR A 1 313 ? -1.073  3.733   10.828  1.00 36.72  ? 313  TYR A N   1 
ATOM   2537 C  CA  . TYR A 1 313 ? -0.019  2.771   10.539  1.00 36.82  ? 313  TYR A CA  1 
ATOM   2538 C  C   . TYR A 1 313 ? -0.237  1.466   11.299  1.00 35.12  ? 313  TYR A C   1 
ATOM   2539 O  O   . TYR A 1 313 ? -0.004  0.381   10.753  1.00 35.15  ? 313  TYR A O   1 
ATOM   2540 C  CB  . TYR A 1 313 ? 1.354   3.359   10.879  1.00 36.31  ? 313  TYR A CB  1 
ATOM   2541 C  CG  . TYR A 1 313 ? 2.472   2.480   10.371  1.00 35.82  ? 313  TYR A CG  1 
ATOM   2542 C  CD1 . TYR A 1 313 ? 2.748   2.407   9.006   1.00 40.45  ? 313  TYR A CD1 1 
ATOM   2543 C  CD2 . TYR A 1 313 ? 3.227   1.698   11.236  1.00 35.31  ? 313  TYR A CD2 1 
ATOM   2544 C  CE1 . TYR A 1 313 ? 3.748   1.600   8.521   1.00 37.95  ? 313  TYR A CE1 1 
ATOM   2545 C  CE2 . TYR A 1 313 ? 4.224   0.870   10.759  1.00 36.02  ? 313  TYR A CE2 1 
ATOM   2546 C  CZ  . TYR A 1 313 ? 4.486   0.835   9.397   1.00 38.95  ? 313  TYR A CZ  1 
ATOM   2547 O  OH  . TYR A 1 313 ? 5.473   0.041   8.898   1.00 37.49  ? 313  TYR A OH  1 
ATOM   2548 N  N   . VAL A 1 314 ? -0.647  1.550   12.571  1.00 34.09  ? 314  VAL A N   1 
ATOM   2549 C  CA  . VAL A 1 314 ? -1.044  0.341   13.287  1.00 33.56  ? 314  VAL A CA  1 
ATOM   2550 C  C   . VAL A 1 314 ? -2.098  -0.406  12.478  1.00 35.16  ? 314  VAL A C   1 
ATOM   2551 O  O   . VAL A 1 314 ? -2.072  -1.637  12.373  1.00 32.73  ? 314  VAL A O   1 
ATOM   2552 C  CB  . VAL A 1 314 ? -1.551  0.697   14.697  1.00 34.57  ? 314  VAL A CB  1 
ATOM   2553 C  CG1 . VAL A 1 314 ? -2.056  -0.558  15.428  1.00 36.72  ? 314  VAL A CG1 1 
ATOM   2554 C  CG2 . VAL A 1 314 ? -0.448  1.367   15.499  1.00 35.31  ? 314  VAL A CG2 1 
ATOM   2555 N  N   . GLY A 1 315 ? -3.023  0.331   11.867  1.00 35.18  ? 315  GLY A N   1 
ATOM   2556 C  CA  . GLY A 1 315 ? -4.021  -0.322  11.028  1.00 37.95  ? 315  GLY A CA  1 
ATOM   2557 C  C   . GLY A 1 315 ? -3.412  -1.078  9.855   1.00 35.92  ? 315  GLY A C   1 
ATOM   2558 O  O   . GLY A 1 315 ? -3.873  -2.172  9.497   1.00 34.72  ? 315  GLY A O   1 
ATOM   2559 N  N   . MET A 1 316 ? -2.390  -0.493  9.213   1.00 32.35  ? 316  MET A N   1 
ATOM   2560 C  CA  . MET A 1 316 ? -1.732  -1.188  8.111   1.00 32.90  ? 316  MET A CA  1 
ATOM   2561 C  C   . MET A 1 316 ? -0.937  -2.383  8.607   1.00 32.77  ? 316  MET A C   1 
ATOM   2562 O  O   . MET A 1 316 ? -0.849  -3.398  7.906   1.00 31.76  ? 316  MET A O   1 
ATOM   2563 C  CB  . MET A 1 316 ? -0.830  -0.223  7.310   1.00 36.83  ? 316  MET A CB  1 
ATOM   2564 C  CG  . MET A 1 316 ? -1.567  1.013   6.773   1.00 40.58  ? 316  MET A CG  1 
ATOM   2565 S  SD  . MET A 1 316 ? -0.481  2.251   5.992   1.00 47.32  ? 316  MET A SD  1 
ATOM   2566 C  CE  . MET A 1 316 ? 0.983   1.314   5.617   1.00 43.92  ? 316  MET A CE  1 
ATOM   2567 N  N   . VAL A 1 317 ? -0.368  -2.286  9.817   1.00 32.98  ? 317  VAL A N   1 
ATOM   2568 C  CA  . VAL A 1 317 ? 0.326   -3.426  10.418  1.00 34.90  ? 317  VAL A CA  1 
ATOM   2569 C  C   . VAL A 1 317 ? -0.628  -4.604  10.576  1.00 32.98  ? 317  VAL A C   1 
ATOM   2570 O  O   . VAL A 1 317 ? -0.299  -5.748  10.238  1.00 31.82  ? 317  VAL A O   1 
ATOM   2571 C  CB  . VAL A 1 317 ? 0.946   -3.028  11.773  1.00 34.29  ? 317  VAL A CB  1 
ATOM   2572 C  CG1 . VAL A 1 317 ? 1.285   -4.284  12.580  1.00 31.24  ? 317  VAL A CG1 1 
ATOM   2573 C  CG2 . VAL A 1 317 ? 2.191   -2.182  11.555  1.00 31.94  ? 317  VAL A CG2 1 
ATOM   2574 N  N   . LEU A 1 318 ? -1.836  -4.334  11.072  1.00 33.13  ? 318  LEU A N   1 
ATOM   2575 C  CA  . LEU A 1 318 ? -2.819  -5.403  11.229  1.00 31.75  ? 318  LEU A CA  1 
ATOM   2576 C  C   . LEU A 1 318 ? -3.248  -5.980  9.886   1.00 31.04  ? 318  LEU A C   1 
ATOM   2577 O  O   . LEU A 1 318 ? -3.419  -7.199  9.757   1.00 31.43  ? 318  LEU A O   1 
ATOM   2578 C  CB  . LEU A 1 318 ? -4.032  -4.883  12.001  1.00 32.65  ? 318  LEU A CB  1 
ATOM   2579 C  CG  . LEU A 1 318 ? -3.722  -4.528  13.457  1.00 30.27  ? 318  LEU A CG  1 
ATOM   2580 C  CD1 . LEU A 1 318 ? -4.867  -3.696  14.028  1.00 31.36  ? 318  LEU A CD1 1 
ATOM   2581 C  CD2 . LEU A 1 318 ? -3.498  -5.807  14.265  1.00 28.60  ? 318  LEU A CD2 1 
ATOM   2582 N  N   . ASN A 1 319 ? -3.460  -5.129  8.877   1.00 30.43  ? 319  ASN A N   1 
ATOM   2583 C  CA  . ASN A 1 319 ? -3.821  -5.656  7.566   1.00 32.72  ? 319  ASN A CA  1 
ATOM   2584 C  C   . ASN A 1 319 ? -2.717  -6.531  6.999   1.00 32.68  ? 319  ASN A C   1 
ATOM   2585 O  O   . ASN A 1 319 ? -2.987  -7.574  6.390   1.00 30.34  ? 319  ASN A O   1 
ATOM   2586 C  CB  . ASN A 1 319 ? -4.144  -4.510  6.613   1.00 33.69  ? 319  ASN A CB  1 
ATOM   2587 C  CG  . ASN A 1 319 ? -5.558  -4.027  6.774   1.00 38.24  ? 319  ASN A CG  1 
ATOM   2588 O  OD1 . ASN A 1 319 ? -6.470  -4.817  7.032   1.00 37.38  ? 319  ASN A OD1 1 
ATOM   2589 N  ND2 . ASN A 1 319 ? -5.754  -2.728  6.637   1.00 41.06  ? 319  ASN A ND2 1 
ATOM   2590 N  N   . GLU A 1 320 ? -1.460  -6.125  7.185   1.00 32.00  ? 320  GLU A N   1 
ATOM   2591 C  CA  . GLU A 1 320 ? -0.363  -6.913  6.642   1.00 29.03  ? 320  GLU A CA  1 
ATOM   2592 C  C   . GLU A 1 320 ? -0.232  -8.241  7.381   1.00 30.71  ? 320  GLU A C   1 
ATOM   2593 O  O   . GLU A 1 320 ? 0.115   -9.253  6.770   1.00 32.63  ? 320  GLU A O   1 
ATOM   2594 C  CB  . GLU A 1 320 ? 0.935   -6.097  6.707   1.00 31.50  ? 320  GLU A CB  1 
ATOM   2595 C  CG  . GLU A 1 320 ? 2.188   -6.825  6.206   1.00 35.37  ? 320  GLU A CG  1 
ATOM   2596 C  CD  . GLU A 1 320 ? 2.244   -7.001  4.702   1.00 37.98  ? 320  GLU A CD  1 
ATOM   2597 O  OE1 . GLU A 1 320 ? 1.189   -6.917  4.011   1.00 33.79  ? 320  GLU A OE1 1 
ATOM   2598 O  OE2 . GLU A 1 320 ? 3.359   -7.266  4.196   1.00 34.15  ? 320  GLU A OE2 1 
ATOM   2599 N  N   . ALA A 1 321 ? -0.531  -8.261  8.690   1.00 30.25  ? 321  ALA A N   1 
ATOM   2600 C  CA  . ALA A 1 321 ? -0.579  -9.531  9.413   1.00 31.35  ? 321  ALA A CA  1 
ATOM   2601 C  C   . ALA A 1 321 ? -1.736  -10.403 8.922   1.00 31.42  ? 321  ALA A C   1 
ATOM   2602 O  O   . ALA A 1 321 ? -1.587  -11.622 8.803   1.00 32.02  ? 321  ALA A O   1 
ATOM   2603 C  CB  . ALA A 1 321 ? -0.692  -9.283  10.923  1.00 29.06  ? 321  ALA A CB  1 
ATOM   2604 N  N   . LEU A 1 322 ? -2.895  -9.804  8.609   1.00 30.07  ? 322  LEU A N   1 
ATOM   2605 C  CA  . LEU A 1 322 ? -3.968  -10.605 8.011   1.00 30.32  ? 322  LEU A CA  1 
ATOM   2606 C  C   . LEU A 1 322 ? -3.620  -11.070 6.597   1.00 32.73  ? 322  LEU A C   1 
ATOM   2607 O  O   . LEU A 1 322 ? -4.183  -12.061 6.105   1.00 32.15  ? 322  LEU A O   1 
ATOM   2608 C  CB  . LEU A 1 322 ? -5.280  -9.817  7.962   1.00 31.55  ? 322  LEU A CB  1 
ATOM   2609 C  CG  . LEU A 1 322 ? -6.005  -9.577  9.288   1.00 31.49  ? 322  LEU A CG  1 
ATOM   2610 C  CD1 . LEU A 1 322 ? -7.163  -8.612  9.060   1.00 34.36  ? 322  LEU A CD1 1 
ATOM   2611 C  CD2 . LEU A 1 322 ? -6.512  -10.887 9.859   1.00 31.59  ? 322  LEU A CD2 1 
ATOM   2612 N  N   . ARG A 1 323 ? -2.752  -10.349 5.894   1.00 31.01  ? 323  ARG A N   1 
ATOM   2613 C  CA  . ARG A 1 323 ? -2.373  -10.831 4.574   1.00 30.64  ? 323  ARG A CA  1 
ATOM   2614 C  C   . ARG A 1 323 ? -1.576  -12.119 4.692   1.00 29.76  ? 323  ARG A C   1 
ATOM   2615 O  O   . ARG A 1 323 ? -1.910  -13.126 4.065   1.00 33.14  ? 323  ARG A O   1 
ATOM   2616 C  CB  . ARG A 1 323 ? -1.572  -9.768  3.808   1.00 31.74  ? 323  ARG A CB  1 
ATOM   2617 C  CG  . ARG A 1 323 ? -1.138  -10.258 2.419   1.00 31.80  ? 323  ARG A CG  1 
ATOM   2618 C  CD  . ARG A 1 323 ? -0.269  -9.241  1.675   1.00 33.74  ? 323  ARG A CD  1 
ATOM   2619 N  NE  . ARG A 1 323 ? 1.065   -9.147  2.259   1.00 33.79  ? 323  ARG A NE  1 
ATOM   2620 C  CZ  . ARG A 1 323 ? 2.054   -9.997  2.005   1.00 36.47  ? 323  ARG A CZ  1 
ATOM   2621 N  NH1 . ARG A 1 323 ? 1.888   -11.029 1.197   1.00 35.21  ? 323  ARG A NH1 1 
ATOM   2622 N  NH2 . ARG A 1 323 ? 3.232   -9.822  2.603   1.00 33.40  ? 323  ARG A NH2 1 
ATOM   2623 N  N   . LEU A 1 324 ? -0.528  -12.120 5.526   1.00 33.25  ? 324  LEU A N   1 
ATOM   2624 C  CA  . LEU A 1 324 ? 0.336   -13.297 5.589   1.00 32.74  ? 324  LEU A CA  1 
ATOM   2625 C  C   . LEU A 1 324 ? -0.344  -14.463 6.296   1.00 33.50  ? 324  LEU A C   1 
ATOM   2626 O  O   . LEU A 1 324 ? -0.171  -15.620 5.902   1.00 35.50  ? 324  LEU A O   1 
ATOM   2627 C  CB  . LEU A 1 324 ? 1.654   -12.928 6.269   1.00 35.68  ? 324  LEU A CB  1 
ATOM   2628 C  CG  . LEU A 1 324 ? 2.543   -12.172 5.280   1.00 37.24  ? 324  LEU A CG  1 
ATOM   2629 C  CD1 . LEU A 1 324 ? 3.717   -11.496 5.992   1.00 36.82  ? 324  LEU A CD1 1 
ATOM   2630 C  CD2 . LEU A 1 324 ? 3.026   -13.123 4.187   1.00 37.98  ? 324  LEU A CD2 1 
ATOM   2631 N  N   . TRP A 1 325 ? -1.117  -14.193 7.348   1.00 34.03  ? 325  TRP A N   1 
ATOM   2632 C  CA  . TRP A 1 325 ? -1.763  -15.254 8.124   1.00 30.69  ? 325  TRP A CA  1 
ATOM   2633 C  C   . TRP A 1 325 ? -3.187  -14.839 8.462   1.00 32.65  ? 325  TRP A C   1 
ATOM   2634 O  O   . TRP A 1 325 ? -3.490  -14.465 9.600   1.00 32.13  ? 325  TRP A O   1 
ATOM   2635 C  CB  . TRP A 1 325 ? -0.945  -15.582 9.378   1.00 29.89  ? 325  TRP A CB  1 
ATOM   2636 C  CG  . TRP A 1 325 ? 0.279   -16.310 8.960   1.00 31.58  ? 325  TRP A CG  1 
ATOM   2637 C  CD1 . TRP A 1 325 ? 1.567   -15.876 9.058   1.00 33.74  ? 325  TRP A CD1 1 
ATOM   2638 C  CD2 . TRP A 1 325 ? 0.324   -17.575 8.300   1.00 31.61  ? 325  TRP A CD2 1 
ATOM   2639 N  NE1 . TRP A 1 325 ? 2.420   -16.813 8.513   1.00 34.20  ? 325  TRP A NE1 1 
ATOM   2640 C  CE2 . TRP A 1 325 ? 1.678   -17.866 8.042   1.00 34.75  ? 325  TRP A CE2 1 
ATOM   2641 C  CE3 . TRP A 1 325 ? -0.653  -18.496 7.898   1.00 32.27  ? 325  TRP A CE3 1 
ATOM   2642 C  CZ2 . TRP A 1 325 ? 2.083   -19.044 7.406   1.00 37.82  ? 325  TRP A CZ2 1 
ATOM   2643 C  CZ3 . TRP A 1 325 ? -0.246  -19.671 7.265   1.00 37.21  ? 325  TRP A CZ3 1 
ATOM   2644 C  CH2 . TRP A 1 325 ? 1.112   -19.927 7.029   1.00 37.95  ? 325  TRP A CH2 1 
ATOM   2645 N  N   . PRO A 1 326 ? -4.097  -14.908 7.487   1.00 30.84  ? 326  PRO A N   1 
ATOM   2646 C  CA  . PRO A 1 326 ? -5.524  -14.654 7.767   1.00 31.32  ? 326  PRO A CA  1 
ATOM   2647 C  C   . PRO A 1 326 ? -6.071  -15.735 8.691   1.00 32.72  ? 326  PRO A C   1 
ATOM   2648 O  O   . PRO A 1 326 ? -6.065  -16.918 8.344   1.00 31.88  ? 326  PRO A O   1 
ATOM   2649 C  CB  . PRO A 1 326 ? -6.170  -14.704 6.378   1.00 32.86  ? 326  PRO A CB  1 
ATOM   2650 C  CG  . PRO A 1 326 ? -5.245  -15.643 5.579   1.00 33.46  ? 326  PRO A CG  1 
ATOM   2651 C  CD  . PRO A 1 326 ? -3.863  -15.315 6.086   1.00 31.76  ? 326  PRO A CD  1 
ATOM   2652 N  N   . THR A 1 327 ? -6.570  -15.317 9.872   1.00 32.92  ? 327  THR A N   1 
ATOM   2653 C  CA  . THR A 1 327 ? -6.818  -16.258 10.967  1.00 31.19  ? 327  THR A CA  1 
ATOM   2654 C  C   . THR A 1 327 ? -8.081  -17.080 10.759  1.00 33.61  ? 327  THR A C   1 
ATOM   2655 O  O   . THR A 1 327 ? -8.198  -18.169 11.340  1.00 33.94  ? 327  THR A O   1 
ATOM   2656 C  CB  . THR A 1 327 ? -6.881  -15.503 12.305  1.00 34.94  ? 327  THR A CB  1 
ATOM   2657 O  OG1 . THR A 1 327 ? -7.731  -14.355 12.164  1.00 31.01  ? 327  THR A OG1 1 
ATOM   2658 C  CG2 . THR A 1 327 ? -5.489  -14.990 12.675  1.00 34.14  ? 327  THR A CG2 1 
ATOM   2659 N  N   . ALA A 1 328 ? -9.028  -16.609 9.922   1.00 32.13  ? 328  ALA A N   1 
ATOM   2660 C  CA  . ALA A 1 328 ? -10.029 -17.528 9.395   1.00 30.50  ? 328  ALA A CA  1 
ATOM   2661 C  C   . ALA A 1 328 ? -9.648  -17.883 7.964   1.00 34.69  ? 328  ALA A C   1 
ATOM   2662 O  O   . ALA A 1 328 ? -10.001 -17.147 7.036   1.00 35.30  ? 328  ALA A O   1 
ATOM   2663 C  CB  . ALA A 1 328 ? -11.425 -16.907 9.440   1.00 37.44  ? 328  ALA A CB  1 
ATOM   2664 N  N   . PRO A 1 329 ? -8.958  -19.001 7.739   1.00 32.07  ? 329  PRO A N   1 
ATOM   2665 C  CA  . PRO A 1 329 ? -8.116  -19.136 6.541   1.00 31.57  ? 329  PRO A CA  1 
ATOM   2666 C  C   . PRO A 1 329 ? -8.813  -19.591 5.269   1.00 32.44  ? 329  PRO A C   1 
ATOM   2667 O  O   . PRO A 1 329 ? -8.142  -19.745 4.245   1.00 31.06  ? 329  PRO A O   1 
ATOM   2668 C  CB  . PRO A 1 329 ? -7.076  -20.180 6.984   1.00 32.83  ? 329  PRO A CB  1 
ATOM   2669 C  CG  . PRO A 1 329 ? -7.851  -21.071 7.946   1.00 33.03  ? 329  PRO A CG  1 
ATOM   2670 C  CD  . PRO A 1 329 ? -8.759  -20.109 8.702   1.00 33.39  ? 329  PRO A CD  1 
ATOM   2671 N  N   . ALA A 1 330 ? -10.121 -19.788 5.276   1.00 29.89  ? 330  ALA A N   1 
ATOM   2672 C  CA  . ALA A 1 330 ? -10.781 -20.231 4.063   1.00 29.63  ? 330  ALA A CA  1 
ATOM   2673 C  C   . ALA A 1 330 ? -12.243 -19.857 4.166   1.00 29.81  ? 330  ALA A C   1 
ATOM   2674 O  O   . ALA A 1 330 ? -12.785 -19.671 5.260   1.00 32.31  ? 330  ALA A O   1 
ATOM   2675 C  CB  . ALA A 1 330 ? -10.651 -21.742 3.853   1.00 30.37  ? 330  ALA A CB  1 
ATOM   2676 N  N   . PHE A 1 331 ? -12.864 -19.743 3.008   1.00 29.55  ? 331  PHE A N   1 
ATOM   2677 C  CA  . PHE A 1 331 ? -14.310 -19.757 2.934   1.00 33.13  ? 331  PHE A CA  1 
ATOM   2678 C  C   . PHE A 1 331 ? -14.684 -20.488 1.653   1.00 33.27  ? 331  PHE A C   1 
ATOM   2679 O  O   . PHE A 1 331 ? -13.848 -20.712 0.769   1.00 31.33  ? 331  PHE A O   1 
ATOM   2680 C  CB  . PHE A 1 331 ? -14.922 -18.339 3.014   1.00 30.50  ? 331  PHE A CB  1 
ATOM   2681 C  CG  . PHE A 1 331 ? -14.444 -17.383 1.948   1.00 33.31  ? 331  PHE A CG  1 
ATOM   2682 C  CD1 . PHE A 1 331 ? -13.345 -16.569 2.176   1.00 32.26  ? 331  PHE A CD1 1 
ATOM   2683 C  CD2 . PHE A 1 331 ? -15.126 -17.257 0.747   1.00 33.30  ? 331  PHE A CD2 1 
ATOM   2684 C  CE1 . PHE A 1 331 ? -12.913 -15.667 1.215   1.00 35.34  ? 331  PHE A CE1 1 
ATOM   2685 C  CE2 . PHE A 1 331 ? -14.700 -16.346 -0.230  1.00 34.11  ? 331  PHE A CE2 1 
ATOM   2686 C  CZ  . PHE A 1 331 ? -13.590 -15.554 0.007   1.00 34.80  ? 331  PHE A CZ  1 
ATOM   2687 N  N   . SER A 1 332 ? -15.949 -20.880 1.578   1.00 33.13  ? 332  SER A N   1 
ATOM   2688 C  CA  . SER A 1 332 ? -16.447 -21.798 0.572   1.00 31.26  ? 332  SER A CA  1 
ATOM   2689 C  C   . SER A 1 332 ? -17.595 -21.141 -0.194  1.00 31.91  ? 332  SER A C   1 
ATOM   2690 O  O   . SER A 1 332 ? -18.367 -20.363 0.374   1.00 33.49  ? 332  SER A O   1 
ATOM   2691 C  CB  . SER A 1 332 ? -16.916 -23.096 1.253   1.00 32.64  ? 332  SER A CB  1 
ATOM   2692 O  OG  . SER A 1 332 ? -17.261 -24.089 0.326   1.00 34.09  ? 332  SER A OG  1 
ATOM   2693 N  N   . LEU A 1 333 ? -17.704 -21.472 -1.482  1.00 32.50  ? 333  LEU A N   1 
ATOM   2694 C  CA  . LEU A 1 333 ? -18.726 -20.928 -2.370  1.00 33.34  ? 333  LEU A CA  1 
ATOM   2695 C  C   . LEU A 1 333 ? -19.323 -22.052 -3.212  1.00 33.03  ? 333  LEU A C   1 
ATOM   2696 O  O   . LEU A 1 333 ? -18.707 -23.107 -3.401  1.00 35.61  ? 333  LEU A O   1 
ATOM   2697 C  CB  . LEU A 1 333 ? -18.142 -19.839 -3.289  1.00 30.86  ? 333  LEU A CB  1 
ATOM   2698 C  CG  . LEU A 1 333 ? -17.441 -18.702 -2.544  1.00 32.18  ? 333  LEU A CG  1 
ATOM   2699 C  CD1 . LEU A 1 333 ? -16.372 -18.068 -3.424  1.00 35.19  ? 333  LEU A CD1 1 
ATOM   2700 C  CD2 . LEU A 1 333 ? -18.462 -17.666 -2.051  1.00 30.86  ? 333  LEU A CD2 1 
ATOM   2701 N  N   . TYR A 1 334 ? -20.543 -21.839 -3.704  1.00 32.51  ? 334  TYR A N   1 
ATOM   2702 C  CA  . TYR A 1 334 ? -21.108 -22.744 -4.698  1.00 31.77  ? 334  TYR A CA  1 
ATOM   2703 C  C   . TYR A 1 334 ? -21.630 -21.949 -5.887  1.00 33.72  ? 334  TYR A C   1 
ATOM   2704 O  O   . TYR A 1 334 ? -22.072 -20.805 -5.754  1.00 32.35  ? 334  TYR A O   1 
ATOM   2705 C  CB  . TYR A 1 334 ? -22.232 -23.627 -4.119  1.00 33.12  ? 334  TYR A CB  1 
ATOM   2706 C  CG  . TYR A 1 334 ? -23.492 -22.857 -3.778  1.00 30.82  ? 334  TYR A CG  1 
ATOM   2707 C  CD1 . TYR A 1 334 ? -23.647 -22.249 -2.530  1.00 30.43  ? 334  TYR A CD1 1 
ATOM   2708 C  CD2 . TYR A 1 334 ? -24.534 -22.737 -4.704  1.00 33.67  ? 334  TYR A CD2 1 
ATOM   2709 C  CE1 . TYR A 1 334 ? -24.804 -21.534 -2.214  1.00 30.21  ? 334  TYR A CE1 1 
ATOM   2710 C  CE2 . TYR A 1 334 ? -25.685 -22.017 -4.399  1.00 33.82  ? 334  TYR A CE2 1 
ATOM   2711 C  CZ  . TYR A 1 334 ? -25.812 -21.425 -3.154  1.00 35.09  ? 334  TYR A CZ  1 
ATOM   2712 O  OH  . TYR A 1 334 ? -26.945 -20.723 -2.847  1.00 38.42  ? 334  TYR A OH  1 
ATOM   2713 N  N   . ALA A 1 335 ? -21.571 -22.571 -7.062  1.00 34.66  ? 335  ALA A N   1 
ATOM   2714 C  CA  . ALA A 1 335 ? -22.047 -21.926 -8.282  1.00 38.30  ? 335  ALA A CA  1 
ATOM   2715 C  C   . ALA A 1 335 ? -23.569 -21.800 -8.274  1.00 35.22  ? 335  ALA A C   1 
ATOM   2716 O  O   . ALA A 1 335 ? -24.287 -22.799 -8.129  1.00 37.07  ? 335  ALA A O   1 
ATOM   2717 C  CB  . ALA A 1 335 ? -21.587 -22.717 -9.506  1.00 38.17  ? 335  ALA A CB  1 
ATOM   2718 N  N   . LYS A 1 336 ? -24.062 -20.570 -8.439  1.00 33.44  ? 336  LYS A N   1 
ATOM   2719 C  CA  . LYS A 1 336 ? -25.506 -20.354 -8.503  1.00 37.68  ? 336  LYS A CA  1 
ATOM   2720 C  C   . LYS A 1 336 ? -26.100 -20.889 -9.804  1.00 41.37  ? 336  LYS A C   1 
ATOM   2721 O  O   . LYS A 1 336 ? -27.276 -21.275 -9.838  1.00 43.53  ? 336  LYS A O   1 
ATOM   2722 C  CB  . LYS A 1 336 ? -25.827 -18.865 -8.360  1.00 39.39  ? 336  LYS A CB  1 
ATOM   2723 C  CG  . LYS A 1 336 ? -25.603 -18.299 -6.943  1.00 39.12  ? 336  LYS A CG  1 
ATOM   2724 C  CD  . LYS A 1 336 ? -25.532 -16.767 -6.947  1.00 39.65  ? 336  LYS A CD  1 
ATOM   2725 C  CE  . LYS A 1 336 ? -26.847 -16.144 -7.408  1.00 42.73  ? 336  LYS A CE  1 
ATOM   2726 N  NZ  . LYS A 1 336 ? -27.959 -16.487 -6.485  1.00 38.51  ? 336  LYS A NZ  1 
ATOM   2727 N  N   . GLU A 1 337 ? -25.306 -20.915 -10.872 1.00 38.91  ? 337  GLU A N   1 
ATOM   2728 C  CA  . GLU A 1 337 ? -25.714 -21.408 -12.182 1.00 44.35  ? 337  GLU A CA  1 
ATOM   2729 C  C   . GLU A 1 337 ? -24.485 -21.991 -12.860 1.00 42.20  ? 337  GLU A C   1 
ATOM   2730 O  O   . GLU A 1 337 ? -23.353 -21.719 -12.453 1.00 39.05  ? 337  GLU A O   1 
ATOM   2731 C  CB  . GLU A 1 337 ? -26.290 -20.289 -13.063 1.00 40.70  ? 337  GLU A CB  1 
ATOM   2732 C  CG  . GLU A 1 337 ? -27.573 -19.643 -12.560 1.00 50.24  ? 337  GLU A CG  1 
ATOM   2733 C  CD  . GLU A 1 337 ? -28.740 -20.616 -12.489 1.00 53.43  ? 337  GLU A CD  1 
ATOM   2734 O  OE1 . GLU A 1 337 ? -28.691 -21.670 -13.160 1.00 54.42  ? 337  GLU A OE1 1 
ATOM   2735 O  OE2 . GLU A 1 337 ? -29.706 -20.329 -11.746 1.00 59.77  ? 337  GLU A OE2 1 
ATOM   2736 N  N   . ASP A 1 338 ? -24.704 -22.760 -13.930 1.00 43.34  ? 338  ASP A N   1 
ATOM   2737 C  CA  . ASP A 1 338 ? -23.578 -23.140 -14.772 1.00 39.51  ? 338  ASP A CA  1 
ATOM   2738 C  C   . ASP A 1 338 ? -22.782 -21.895 -15.127 1.00 41.88  ? 338  ASP A C   1 
ATOM   2739 O  O   . ASP A 1 338 ? -23.346 -20.842 -15.432 1.00 43.81  ? 338  ASP A O   1 
ATOM   2740 C  CB  . ASP A 1 338 ? -24.040 -23.829 -16.062 1.00 41.91  ? 338  ASP A CB  1 
ATOM   2741 C  CG  . ASP A 1 338 ? -24.823 -25.099 -15.808 1.00 44.14  ? 338  ASP A CG  1 
ATOM   2742 O  OD1 . ASP A 1 338 ? -24.803 -25.630 -14.674 1.00 45.95  ? 338  ASP A OD1 1 
ATOM   2743 O  OD2 . ASP A 1 338 ? -25.463 -25.588 -16.766 1.00 49.55  ? 338  ASP A OD2 1 
ATOM   2744 N  N   . THR A 1 339 ? -21.464 -22.017 -15.099 1.00 41.83  ? 339  THR A N   1 
ATOM   2745 C  CA  . THR A 1 339 ? -20.611 -20.887 -15.428 1.00 43.53  ? 339  THR A CA  1 
ATOM   2746 C  C   . THR A 1 339 ? -19.205 -21.416 -15.672 1.00 42.59  ? 339  THR A C   1 
ATOM   2747 O  O   . THR A 1 339 ? -18.874 -22.542 -15.289 1.00 45.60  ? 339  THR A O   1 
ATOM   2748 C  CB  . THR A 1 339 ? -20.640 -19.828 -14.307 1.00 44.92  ? 339  THR A CB  1 
ATOM   2749 O  OG1 . THR A 1 339 ? -20.194 -18.566 -14.814 1.00 43.20  ? 339  THR A OG1 1 
ATOM   2750 C  CG2 . THR A 1 339 ? -19.766 -20.255 -13.116 1.00 40.30  ? 339  THR A CG2 1 
ATOM   2751 N  N   . VAL A 1 340 ? -18.386 -20.597 -16.324 1.00 38.90  ? 340  VAL A N   1 
ATOM   2752 C  CA  . VAL A 1 340 ? -17.014 -20.965 -16.653 1.00 42.68  ? 340  VAL A CA  1 
ATOM   2753 C  C   . VAL A 1 340 ? -16.067 -20.073 -15.866 1.00 43.35  ? 340  VAL A C   1 
ATOM   2754 O  O   . VAL A 1 340 ? -16.115 -18.839 -15.980 1.00 40.99  ? 340  VAL A O   1 
ATOM   2755 C  CB  . VAL A 1 340 ? -16.745 -20.862 -18.161 1.00 40.81  ? 340  VAL A CB  1 
ATOM   2756 C  CG1 . VAL A 1 340 ? -15.269 -21.102 -18.448 1.00 43.83  ? 340  VAL A CG1 1 
ATOM   2757 C  CG2 . VAL A 1 340 ? -17.612 -21.865 -18.898 1.00 39.38  ? 340  VAL A CG2 1 
ATOM   2758 N  N   . LEU A 1 341 ? -15.195 -20.700 -15.083 1.00 41.19  ? 341  LEU A N   1 
ATOM   2759 C  CA  . LEU A 1 341 ? -14.202 -19.990 -14.293 1.00 44.46  ? 341  LEU A CA  1 
ATOM   2760 C  C   . LEU A 1 341 ? -12.949 -19.754 -15.125 1.00 45.23  ? 341  LEU A C   1 
ATOM   2761 O  O   . LEU A 1 341 ? -12.382 -20.701 -15.675 1.00 43.22  ? 341  LEU A O   1 
ATOM   2762 C  CB  . LEU A 1 341 ? -13.856 -20.798 -13.044 1.00 43.99  ? 341  LEU A CB  1 
ATOM   2763 C  CG  . LEU A 1 341 ? -13.353 -20.033 -11.841 1.00 48.28  ? 341  LEU A CG  1 
ATOM   2764 C  CD1 . LEU A 1 341 ? -14.446 -19.073 -11.396 1.00 42.70  ? 341  LEU A CD1 1 
ATOM   2765 C  CD2 . LEU A 1 341 ? -12.992 -21.030 -10.739 1.00 41.49  ? 341  LEU A CD2 1 
ATOM   2766 N  N   . GLY A 1 342 ? -12.526 -18.496 -15.219 1.00 42.83  ? 342  GLY A N   1 
ATOM   2767 C  CA  . GLY A 1 342 ? -11.266 -18.171 -15.866 1.00 43.09  ? 342  GLY A CA  1 
ATOM   2768 C  C   . GLY A 1 342 ? -11.195 -18.503 -17.344 1.00 49.81  ? 342  GLY A C   1 
ATOM   2769 O  O   . GLY A 1 342 ? -10.093 -18.596 -17.899 1.00 45.74  ? 342  GLY A O   1 
ATOM   2770 N  N   . GLY A 1 343 ? -12.337 -18.691 -18.000 1.00 45.34  ? 343  GLY A N   1 
ATOM   2771 C  CA  . GLY A 1 343 ? -12.345 -19.022 -19.415 1.00 49.31  ? 343  GLY A CA  1 
ATOM   2772 C  C   . GLY A 1 343 ? -11.821 -20.421 -19.671 1.00 51.96  ? 343  GLY A C   1 
ATOM   2773 O  O   . GLY A 1 343 ? -11.545 -20.805 -20.810 1.00 49.47  ? 343  GLY A O   1 
ATOM   2774 N  N   . GLU A 1 344 ? -11.688 -21.198 -18.604 1.00 46.67  ? 344  GLU A N   1 
ATOM   2775 C  CA  . GLU A 1 344 ? -10.970 -22.463 -18.695 1.00 51.87  ? 344  GLU A CA  1 
ATOM   2776 C  C   . GLU A 1 344 ? -11.605 -23.608 -17.922 1.00 50.22  ? 344  GLU A C   1 
ATOM   2777 O  O   . GLU A 1 344 ? -11.418 -24.765 -18.310 1.00 47.50  ? 344  GLU A O   1 
ATOM   2778 C  CB  . GLU A 1 344 ? -9.525  -22.272 -18.206 1.00 53.17  ? 344  GLU A CB  1 
ATOM   2779 C  CG  . GLU A 1 344 ? -8.568  -21.802 -19.291 1.00 58.90  ? 344  GLU A CG  1 
ATOM   2780 C  CD  . GLU A 1 344 ? -7.233  -21.325 -18.744 1.00 58.81  ? 344  GLU A CD  1 
ATOM   2781 O  OE1 . GLU A 1 344 ? -7.048  -21.306 -17.507 1.00 56.19  ? 344  GLU A OE1 1 
ATOM   2782 O  OE2 . GLU A 1 344 ? -6.350  -20.991 -19.564 1.00 67.22  ? 344  GLU A OE2 1 
ATOM   2783 N  N   . TYR A 1 345 ? -12.354 -23.346 -16.859 1.00 45.09  ? 345  TYR A N   1 
ATOM   2784 C  CA  . TYR A 1 345 ? -12.848 -24.407 -15.985 1.00 43.69  ? 345  TYR A CA  1 
ATOM   2785 C  C   . TYR A 1 345 ? -14.358 -24.322 -15.879 1.00 43.93  ? 345  TYR A C   1 
ATOM   2786 O  O   . TYR A 1 345 ? -14.888 -23.559 -15.050 1.00 43.00  ? 345  TYR A O   1 
ATOM   2787 C  CB  . TYR A 1 345 ? -12.193 -24.321 -14.607 1.00 41.28  ? 345  TYR A CB  1 
ATOM   2788 C  CG  . TYR A 1 345 ? -10.684 -24.368 -14.671 1.00 42.35  ? 345  TYR A CG  1 
ATOM   2789 C  CD1 . TYR A 1 345 ? -10.016 -25.568 -14.886 1.00 44.94  ? 345  TYR A CD1 1 
ATOM   2790 C  CD2 . TYR A 1 345 ? -9.925  -23.216 -14.532 1.00 40.41  ? 345  TYR A CD2 1 
ATOM   2791 C  CE1 . TYR A 1 345 ? -8.633  -25.619 -14.957 1.00 45.48  ? 345  TYR A CE1 1 
ATOM   2792 C  CE2 . TYR A 1 345 ? -8.543  -23.257 -14.597 1.00 44.24  ? 345  TYR A CE2 1 
ATOM   2793 C  CZ  . TYR A 1 345 ? -7.901  -24.463 -14.816 1.00 46.88  ? 345  TYR A CZ  1 
ATOM   2794 O  OH  . TYR A 1 345 ? -6.527  -24.519 -14.882 1.00 48.17  ? 345  TYR A OH  1 
ATOM   2795 N  N   . PRO A 1 346 ? -15.091 -25.084 -16.687 1.00 44.04  ? 346  PRO A N   1 
ATOM   2796 C  CA  . PRO A 1 346 ? -16.551 -25.034 -16.610 1.00 41.37  ? 346  PRO A CA  1 
ATOM   2797 C  C   . PRO A 1 346 ? -17.047 -25.654 -15.312 1.00 46.22  ? 346  PRO A C   1 
ATOM   2798 O  O   . PRO A 1 346 ? -16.531 -26.677 -14.849 1.00 39.59  ? 346  PRO A O   1 
ATOM   2799 C  CB  . PRO A 1 346 ? -16.998 -25.843 -17.833 1.00 45.98  ? 346  PRO A CB  1 
ATOM   2800 C  CG  . PRO A 1 346 ? -15.869 -26.789 -18.069 1.00 50.56  ? 346  PRO A CG  1 
ATOM   2801 C  CD  . PRO A 1 346 ? -14.623 -26.025 -17.719 1.00 46.98  ? 346  PRO A CD  1 
ATOM   2802 N  N   . LEU A 1 347 ? -18.054 -25.010 -14.726 1.00 39.91  ? 347  LEU A N   1 
ATOM   2803 C  CA  . LEU A 1 347 ? -18.703 -25.460 -13.506 1.00 39.76  ? 347  LEU A CA  1 
ATOM   2804 C  C   . LEU A 1 347 ? -20.196 -25.603 -13.751 1.00 39.66  ? 347  LEU A C   1 
ATOM   2805 O  O   . LEU A 1 347 ? -20.796 -24.829 -14.503 1.00 43.53  ? 347  LEU A O   1 
ATOM   2806 C  CB  . LEU A 1 347 ? -18.480 -24.477 -12.355 1.00 38.92  ? 347  LEU A CB  1 
ATOM   2807 C  CG  . LEU A 1 347 ? -17.022 -24.153 -12.037 1.00 42.52  ? 347  LEU A CG  1 
ATOM   2808 C  CD1 . LEU A 1 347 ? -16.908 -22.943 -11.107 1.00 43.49  ? 347  LEU A CD1 1 
ATOM   2809 C  CD2 . LEU A 1 347 ? -16.383 -25.379 -11.411 1.00 40.75  ? 347  LEU A CD2 1 
ATOM   2810 N  N   . GLU A 1 348 ? -20.786 -26.593 -13.097 1.00 38.93  ? 348  GLU A N   1 
ATOM   2811 C  CA  . GLU A 1 348 ? -22.225 -26.791 -13.103 1.00 40.93  ? 348  GLU A CA  1 
ATOM   2812 C  C   . GLU A 1 348 ? -22.843 -26.161 -11.859 1.00 42.85  ? 348  GLU A C   1 
ATOM   2813 O  O   . GLU A 1 348 ? -22.221 -26.108 -10.793 1.00 41.93  ? 348  GLU A O   1 
ATOM   2814 C  CB  . GLU A 1 348 ? -22.579 -28.280 -13.161 1.00 42.77  ? 348  GLU A CB  1 
ATOM   2815 C  CG  . GLU A 1 348 ? -21.958 -29.010 -14.338 1.00 43.10  ? 348  GLU A CG  1 
ATOM   2816 C  CD  . GLU A 1 348 ? -22.515 -30.412 -14.535 1.00 54.44  ? 348  GLU A CD  1 
ATOM   2817 O  OE1 . GLU A 1 348 ? -23.100 -30.978 -13.593 1.00 60.58  ? 348  GLU A OE1 1 
ATOM   2818 O  OE2 . GLU A 1 348 ? -22.374 -30.947 -15.653 1.00 68.38  ? 348  GLU A OE2 1 
ATOM   2819 N  N   . LYS A 1 349 ? -24.078 -25.684 -12.009 1.00 38.68  ? 349  LYS A N   1 
ATOM   2820 C  CA  . LYS A 1 349 ? -24.852 -25.203 -10.874 1.00 39.78  ? 349  LYS A CA  1 
ATOM   2821 C  C   . LYS A 1 349 ? -24.651 -26.123 -9.676  1.00 42.07  ? 349  LYS A C   1 
ATOM   2822 O  O   . LYS A 1 349 ? -24.735 -27.350 -9.794  1.00 41.81  ? 349  LYS A O   1 
ATOM   2823 C  CB  . LYS A 1 349 ? -26.339 -25.135 -11.250 1.00 43.28  ? 349  LYS A CB  1 
ATOM   2824 C  CG  . LYS A 1 349 ? -27.305 -24.980 -10.076 1.00 45.46  ? 349  LYS A CG  1 
ATOM   2825 C  CD  . LYS A 1 349 ? -28.706 -24.588 -10.555 1.00 45.29  ? 349  LYS A CD  1 
ATOM   2826 C  CE  . LYS A 1 349 ? -29.493 -23.815 -9.494  1.00 55.91  ? 349  LYS A CE  1 
ATOM   2827 N  NZ  . LYS A 1 349 ? -30.735 -23.199 -10.069 1.00 58.71  ? 349  LYS A NZ  1 
ATOM   2828 N  N   . GLY A 1 350 ? -24.345 -25.531 -8.524  1.00 36.72  ? 350  GLY A N   1 
ATOM   2829 C  CA  . GLY A 1 350 ? -24.160 -26.292 -7.307  1.00 41.11  ? 350  GLY A CA  1 
ATOM   2830 C  C   . GLY A 1 350 ? -22.732 -26.704 -7.020  1.00 40.63  ? 350  GLY A C   1 
ATOM   2831 O  O   . GLY A 1 350 ? -22.424 -27.064 -5.874  1.00 39.53  ? 350  GLY A O   1 
ATOM   2832 N  N   . ASP A 1 351 ? -21.861 -26.666 -8.027  1.00 37.73  ? 351  ASP A N   1 
ATOM   2833 C  CA  . ASP A 1 351 ? -20.451 -26.987 -7.841  1.00 38.13  ? 351  ASP A CA  1 
ATOM   2834 C  C   . ASP A 1 351 ? -19.827 -26.061 -6.806  1.00 38.25  ? 351  ASP A C   1 
ATOM   2835 O  O   . ASP A 1 351 ? -20.118 -24.863 -6.780  1.00 37.01  ? 351  ASP A O   1 
ATOM   2836 C  CB  . ASP A 1 351 ? -19.702 -26.853 -9.171  1.00 37.70  ? 351  ASP A CB  1 
ATOM   2837 C  CG  . ASP A 1 351 ? -19.868 -28.082 -10.077 1.00 41.35  ? 351  ASP A CG  1 
ATOM   2838 O  OD1 . ASP A 1 351 ? -20.612 -29.021 -9.694  1.00 40.46  ? 351  ASP A OD1 1 
ATOM   2839 O  OD2 . ASP A 1 351 ? -19.247 -28.091 -11.165 1.00 37.31  ? 351  ASP A OD2 1 
ATOM   2840 N  N   . GLU A 1 352 ? -18.931 -26.621 -5.983  1.00 37.11  ? 352  GLU A N   1 
ATOM   2841 C  CA  . GLU A 1 352 ? -18.339 -25.955 -4.828  1.00 37.94  ? 352  GLU A CA  1 
ATOM   2842 C  C   . GLU A 1 352 ? -16.915 -25.494 -5.107  1.00 36.97  ? 352  GLU A C   1 
ATOM   2843 O  O   . GLU A 1 352 ? -16.188 -26.090 -5.907  1.00 38.02  ? 352  GLU A O   1 
ATOM   2844 C  CB  . GLU A 1 352 ? -18.315 -26.900 -3.622  1.00 38.53  ? 352  GLU A CB  1 
ATOM   2845 C  CG  . GLU A 1 352 ? -19.684 -27.363 -3.195  1.00 44.92  ? 352  GLU A CG  1 
ATOM   2846 C  CD  . GLU A 1 352 ? -19.648 -28.150 -1.904  1.00 48.45  ? 352  GLU A CD  1 
ATOM   2847 O  OE1 . GLU A 1 352 ? -18.581 -28.163 -1.233  1.00 40.81  ? 352  GLU A OE1 1 
ATOM   2848 O  OE2 . GLU A 1 352 ? -20.692 -28.757 -1.582  1.00 49.79  ? 352  GLU A OE2 1 
ATOM   2849 N  N   . LEU A 1 353 ? -16.517 -24.444 -4.391  1.00 34.36  ? 353  LEU A N   1 
ATOM   2850 C  CA  . LEU A 1 353 ? -15.175 -23.884 -4.421  1.00 35.15  ? 353  LEU A CA  1 
ATOM   2851 C  C   . LEU A 1 353 ? -14.705 -23.633 -2.998  1.00 36.52  ? 353  LEU A C   1 
ATOM   2852 O  O   . LEU A 1 353 ? -15.512 -23.352 -2.111  1.00 35.21  ? 353  LEU A O   1 
ATOM   2853 C  CB  . LEU A 1 353 ? -15.118 -22.558 -5.174  1.00 29.57  ? 353  LEU A CB  1 
ATOM   2854 C  CG  . LEU A 1 353 ? -15.647 -22.528 -6.598  1.00 40.71  ? 353  LEU A CG  1 
ATOM   2855 C  CD1 . LEU A 1 353 ? -15.741 -21.082 -7.056  1.00 33.52  ? 353  LEU A CD1 1 
ATOM   2856 C  CD2 . LEU A 1 353 ? -14.723 -23.352 -7.486  1.00 39.14  ? 353  LEU A CD2 1 
ATOM   2857 N  N   . MET A 1 354 ? -13.388 -23.689 -2.805  1.00 33.17  ? 354  MET A N   1 
ATOM   2858 C  CA  . MET A 1 354 ? -12.753 -23.394 -1.532  1.00 35.75  ? 354  MET A CA  1 
ATOM   2859 C  C   . MET A 1 354 ? -11.768 -22.266 -1.825  1.00 36.31  ? 354  MET A C   1 
ATOM   2860 O  O   . MET A 1 354 ? -10.920 -22.405 -2.710  1.00 34.20  ? 354  MET A O   1 
ATOM   2861 C  CB  . MET A 1 354 ? -12.023 -24.642 -1.044  1.00 37.55  ? 354  MET A CB  1 
ATOM   2862 C  CG  . MET A 1 354 ? -12.732 -25.560 -0.067  1.00 34.70  ? 354  MET A CG  1 
ATOM   2863 S  SD  . MET A 1 354 ? -14.062 -25.025 1.020   1.00 36.02  ? 354  MET A SD  1 
ATOM   2864 C  CE  . MET A 1 354 ? -13.090 -24.298 2.313   1.00 35.87  ? 354  MET A CE  1 
ATOM   2865 N  N   . VAL A 1 355 ? -11.888 -21.140 -1.132  1.00 32.75  ? 355  VAL A N   1 
ATOM   2866 C  CA  . VAL A 1 355 ? -10.940 -20.042 -1.302  1.00 31.99  ? 355  VAL A CA  1 
ATOM   2867 C  C   . VAL A 1 355 ? -9.855  -20.190 -0.243  1.00 29.14  ? 355  VAL A C   1 
ATOM   2868 O  O   . VAL A 1 355 ? -10.106 -19.997 0.947   1.00 30.12  ? 355  VAL A O   1 
ATOM   2869 C  CB  . VAL A 1 355 ? -11.624 -18.674 -1.200  1.00 34.30  ? 355  VAL A CB  1 
ATOM   2870 C  CG1 . VAL A 1 355 ? -10.577 -17.565 -1.267  1.00 32.13  ? 355  VAL A CG1 1 
ATOM   2871 C  CG2 . VAL A 1 355 ? -12.693 -18.516 -2.298  1.00 32.14  ? 355  VAL A CG2 1 
ATOM   2872 N  N   . LEU A 1 356 ? -8.633  -20.480 -0.681  1.00 29.19  ? 356  LEU A N   1 
ATOM   2873 C  CA  . LEU A 1 356 ? -7.531  -20.729 0.253   1.00 32.42  ? 356  LEU A CA  1 
ATOM   2874 C  C   . LEU A 1 356 ? -6.817  -19.407 0.487   1.00 32.28  ? 356  LEU A C   1 
ATOM   2875 O  O   . LEU A 1 356 ? -5.920  -19.022 -0.264  1.00 32.65  ? 356  LEU A O   1 
ATOM   2876 C  CB  . LEU A 1 356 ? -6.614  -21.800 -0.311  1.00 32.76  ? 356  LEU A CB  1 
ATOM   2877 C  CG  . LEU A 1 356 ? -5.492  -22.336 0.582   1.00 37.36  ? 356  LEU A CG  1 
ATOM   2878 C  CD1 . LEU A 1 356 ? -6.066  -23.016 1.806   1.00 37.25  ? 356  LEU A CD1 1 
ATOM   2879 C  CD2 . LEU A 1 356 ? -4.654  -23.320 -0.214  1.00 34.78  ? 356  LEU A CD2 1 
ATOM   2880 N  N   . ILE A 1 357 ? -7.223  -18.700 1.541   1.00 32.37  ? 357  ILE A N   1 
ATOM   2881 C  CA  . ILE A 1 357 ? -6.886  -17.284 1.675   1.00 29.72  ? 357  ILE A CA  1 
ATOM   2882 C  C   . ILE A 1 357 ? -5.386  -17.055 1.868   1.00 30.11  ? 357  ILE A C   1 
ATOM   2883 O  O   . ILE A 1 357 ? -4.837  -16.120 1.264   1.00 30.67  ? 357  ILE A O   1 
ATOM   2884 C  CB  . ILE A 1 357 ? -7.684  -16.623 2.811   1.00 31.32  ? 357  ILE A CB  1 
ATOM   2885 C  CG1 . ILE A 1 357 ? -9.185  -16.868 2.618   1.00 30.00  ? 357  ILE A CG1 1 
ATOM   2886 C  CG2 . ILE A 1 357 ? -7.440  -15.124 2.798   1.00 31.69  ? 357  ILE A CG2 1 
ATOM   2887 C  CD1 . ILE A 1 357 ? -10.021 -16.344 3.792   1.00 28.86  ? 357  ILE A CD1 1 
ATOM   2888 N  N   . PRO A 1 358 ? -4.678  -17.837 2.694   1.00 35.11  ? 358  PRO A N   1 
ATOM   2889 C  CA  . PRO A 1 358 ? -3.239  -17.556 2.873   1.00 33.38  ? 358  PRO A CA  1 
ATOM   2890 C  C   . PRO A 1 358 ? -2.463  -17.702 1.571   1.00 32.14  ? 358  PRO A C   1 
ATOM   2891 O  O   . PRO A 1 358 ? -1.467  -16.998 1.357   1.00 32.24  ? 358  PRO A O   1 
ATOM   2892 C  CB  . PRO A 1 358 ? -2.802  -18.579 3.937   1.00 37.44  ? 358  PRO A CB  1 
ATOM   2893 C  CG  . PRO A 1 358 ? -4.092  -18.970 4.643   1.00 32.79  ? 358  PRO A CG  1 
ATOM   2894 C  CD  . PRO A 1 358 ? -5.130  -18.952 3.544   1.00 31.33  ? 358  PRO A CD  1 
ATOM   2895 N  N   . GLN A 1 359 ? -2.935  -18.552 0.670   1.00 31.26  ? 359  GLN A N   1 
ATOM   2896 C  CA  . GLN A 1 359 ? -2.278  -18.741 -0.619  1.00 34.18  ? 359  GLN A CA  1 
ATOM   2897 C  C   . GLN A 1 359 ? -2.621  -17.608 -1.588  1.00 35.23  ? 359  GLN A C   1 
ATOM   2898 O  O   . GLN A 1 359 ? -1.739  -17.091 -2.290  1.00 34.12  ? 359  GLN A O   1 
ATOM   2899 C  CB  . GLN A 1 359 ? -2.673  -20.108 -1.182  1.00 36.15  ? 359  GLN A CB  1 
ATOM   2900 C  CG  . GLN A 1 359 ? -1.701  -20.678 -2.197  1.00 39.99  ? 359  GLN A CG  1 
ATOM   2901 C  CD  . GLN A 1 359 ? -0.332  -20.989 -1.608  1.00 41.29  ? 359  GLN A CD  1 
ATOM   2902 O  OE1 . GLN A 1 359 ? -0.140  -21.023 -0.378  1.00 39.06  ? 359  GLN A OE1 1 
ATOM   2903 N  NE2 . GLN A 1 359 ? 0.637   -21.221 -2.495  1.00 45.34  ? 359  GLN A NE2 1 
ATOM   2904 N  N   . LEU A 1 360 ? -3.890  -17.193 -1.625  1.00 33.39  ? 360  LEU A N   1 
ATOM   2905 C  CA  . LEU A 1 360 ? -4.254  -15.991 -2.367  1.00 32.78  ? 360  LEU A CA  1 
ATOM   2906 C  C   . LEU A 1 360 ? -3.362  -14.815 -1.994  1.00 31.98  ? 360  LEU A C   1 
ATOM   2907 O  O   . LEU A 1 360 ? -2.888  -14.074 -2.864  1.00 33.32  ? 360  LEU A O   1 
ATOM   2908 C  CB  . LEU A 1 360 ? -5.727  -15.633 -2.113  1.00 30.77  ? 360  LEU A CB  1 
ATOM   2909 C  CG  . LEU A 1 360 ? -6.149  -14.208 -2.554  1.00 34.15  ? 360  LEU A CG  1 
ATOM   2910 C  CD1 . LEU A 1 360 ? -6.283  -14.099 -4.072  1.00 31.39  ? 360  LEU A CD1 1 
ATOM   2911 C  CD2 . LEU A 1 360 ? -7.462  -13.776 -1.890  1.00 32.16  ? 360  LEU A CD2 1 
ATOM   2912 N  N   . HIS A 1 361 ? -3.155  -14.603 -0.699  1.00 30.39  ? 361  HIS A N   1 
ATOM   2913 C  CA  . HIS A 1 361 ? -2.381  -13.478 -0.207  1.00 31.39  ? 361  HIS A CA  1 
ATOM   2914 C  C   . HIS A 1 361 ? -0.892  -13.615 -0.498  1.00 31.03  ? 361  HIS A C   1 
ATOM   2915 O  O   . HIS A 1 361 ? -0.116  -12.733 -0.108  1.00 34.01  ? 361  HIS A O   1 
ATOM   2916 C  CB  . HIS A 1 361 ? -2.615  -13.323 1.297   1.00 33.17  ? 361  HIS A CB  1 
ATOM   2917 C  CG  . HIS A 1 361 ? -4.003  -12.865 1.638   1.00 28.56  ? 361  HIS A CG  1 
ATOM   2918 N  ND1 . HIS A 1 361 ? -4.474  -12.803 2.930   1.00 33.95  ? 361  HIS A ND1 1 
ATOM   2919 C  CD2 . HIS A 1 361 ? -5.014  -12.439 0.842   1.00 33.23  ? 361  HIS A CD2 1 
ATOM   2920 C  CE1 . HIS A 1 361 ? -5.717  -12.345 2.920   1.00 32.10  ? 361  HIS A CE1 1 
ATOM   2921 N  NE2 . HIS A 1 361 ? -6.070  -12.120 1.665   1.00 29.62  ? 361  HIS A NE2 1 
ATOM   2922 N  N   . ARG A 1 362 ? -0.487  -14.711 -1.134  1.00 33.48  ? 362  ARG A N   1 
ATOM   2923 C  CA  . ARG A 1 362 ? 0.890   -14.924 -1.559  1.00 32.84  ? 362  ARG A CA  1 
ATOM   2924 C  C   . ARG A 1 362 ? 1.025   -14.943 -3.080  1.00 38.15  ? 362  ARG A C   1 
ATOM   2925 O  O   . ARG A 1 362 ? 2.073   -15.330 -3.606  1.00 34.89  ? 362  ARG A O   1 
ATOM   2926 C  CB  . ARG A 1 362 ? 1.438   -16.216 -0.946  1.00 30.02  ? 362  ARG A CB  1 
ATOM   2927 C  CG  . ARG A 1 362 ? 1.810   -16.074 0.546   1.00 35.12  ? 362  ARG A CG  1 
ATOM   2928 C  CD  . ARG A 1 362 ? 1.982   -17.441 1.211   1.00 40.67  ? 362  ARG A CD  1 
ATOM   2929 N  NE  . ARG A 1 362 ? 2.484   -17.311 2.574   1.00 35.57  ? 362  ARG A NE  1 
ATOM   2930 C  CZ  . ARG A 1 362 ? 1.743   -16.935 3.605   1.00 37.25  ? 362  ARG A CZ  1 
ATOM   2931 N  NH1 . ARG A 1 362 ? 0.457   -16.655 3.464   1.00 32.71  ? 362  ARG A NH1 1 
ATOM   2932 N  NH2 . ARG A 1 362 ? 2.307   -16.827 4.804   1.00 34.74  ? 362  ARG A NH2 1 
ATOM   2933 N  N   . ASP A 1 363 ? -0.015  -14.535 -3.798  1.00 33.66  ? 363  ASP A N   1 
ATOM   2934 C  CA  . ASP A 1 363 ? 0.033   -14.418 -5.251  1.00 35.11  ? 363  ASP A CA  1 
ATOM   2935 C  C   . ASP A 1 363 ? 1.082   -13.395 -5.682  1.00 38.40  ? 363  ASP A C   1 
ATOM   2936 O  O   . ASP A 1 363 ? 0.887   -12.188 -5.511  1.00 35.04  ? 363  ASP A O   1 
ATOM   2937 C  CB  . ASP A 1 363 ? -1.364  -14.029 -5.753  1.00 38.39  ? 363  ASP A CB  1 
ATOM   2938 C  CG  . ASP A 1 363 ? -1.511  -14.127 -7.260  1.00 38.38  ? 363  ASP A CG  1 
ATOM   2939 O  OD1 . ASP A 1 363 ? -0.483  -14.033 -7.976  1.00 36.74  ? 363  ASP A OD1 1 
ATOM   2940 O  OD2 . ASP A 1 363 ? -2.669  -14.283 -7.731  1.00 36.39  ? 363  ASP A OD2 1 
ATOM   2941 N  N   . LYS A 1 364 ? 2.204   -13.856 -6.254  1.00 41.61  ? 364  LYS A N   1 
ATOM   2942 C  CA  . LYS A 1 364 ? 3.259   -12.913 -6.619  1.00 42.34  ? 364  LYS A CA  1 
ATOM   2943 C  C   . LYS A 1 364 ? 2.847   -11.966 -7.739  1.00 37.55  ? 364  LYS A C   1 
ATOM   2944 O  O   . LYS A 1 364 ? 3.429   -10.879 -7.856  1.00 39.99  ? 364  LYS A O   1 
ATOM   2945 C  CB  . LYS A 1 364 ? 4.538   -13.634 -7.048  1.00 43.19  ? 364  LYS A CB  1 
ATOM   2946 C  CG  . LYS A 1 364 ? 5.395   -14.158 -5.905  1.00 44.37  ? 364  LYS A CG  1 
ATOM   2947 C  CD  . LYS A 1 364 ? 6.457   -15.129 -6.460  1.00 52.21  ? 364  LYS A CD  1 
ATOM   2948 C  CE  . LYS A 1 364 ? 6.276   -16.549 -5.944  1.00 60.19  ? 364  LYS A CE  1 
ATOM   2949 N  NZ  . LYS A 1 364 ? 7.455   -16.982 -5.137  1.00 60.47  ? 364  LYS A NZ  1 
ATOM   2950 N  N   . THR A 1 365 ? 1.889   -12.354 -8.573  1.00 35.17  ? 365  THR A N   1 
ATOM   2951 C  CA  . THR A 1 365 ? 1.465   -11.449 -9.628  1.00 39.60  ? 365  THR A CA  1 
ATOM   2952 C  C   . THR A 1 365 ? 0.795   -10.213 -9.054  1.00 42.79  ? 365  THR A C   1 
ATOM   2953 O  O   . THR A 1 365 ? 0.744   -9.177  -9.725  1.00 38.13  ? 365  THR A O   1 
ATOM   2954 C  CB  . THR A 1 365 ? 0.552   -12.178 -10.630 1.00 42.08  ? 365  THR A CB  1 
ATOM   2955 O  OG1 . THR A 1 365 ? -0.774  -12.337 -10.093 1.00 42.22  ? 365  THR A OG1 1 
ATOM   2956 C  CG2 . THR A 1 365 ? 1.137   -13.544 -10.972 1.00 39.79  ? 365  THR A CG2 1 
ATOM   2957 N  N   . ILE A 1 366 ? 0.320   -10.294 -7.815  1.00 36.51  ? 366  ILE A N   1 
ATOM   2958 C  CA  . ILE A 1 366 ? -0.313  -9.159  -7.147  1.00 34.69  ? 366  ILE A CA  1 
ATOM   2959 C  C   . ILE A 1 366 ? 0.685   -8.397  -6.288  1.00 38.15  ? 366  ILE A C   1 
ATOM   2960 O  O   . ILE A 1 366 ? 0.839   -7.179  -6.412  1.00 38.77  ? 366  ILE A O   1 
ATOM   2961 C  CB  . ILE A 1 366 ? -1.498  -9.657  -6.291  1.00 35.58  ? 366  ILE A CB  1 
ATOM   2962 C  CG1 . ILE A 1 366 ? -2.588  -10.267 -7.180  1.00 35.22  ? 366  ILE A CG1 1 
ATOM   2963 C  CG2 . ILE A 1 366 ? -2.018  -8.526  -5.423  1.00 36.49  ? 366  ILE A CG2 1 
ATOM   2964 C  CD1 . ILE A 1 366 ? -3.269  -9.293  -8.142  1.00 37.60  ? 366  ILE A CD1 1 
ATOM   2965 N  N   . TRP A 1 367 ? 1.369   -9.104  -5.392  1.00 35.73  ? 367  TRP A N   1 
ATOM   2966 C  CA  . TRP A 1 367 ? 2.125   -8.453  -4.337  1.00 38.06  ? 367  TRP A CA  1 
ATOM   2967 C  C   . TRP A 1 367 ? 3.585   -8.233  -4.706  1.00 41.17  ? 367  TRP A C   1 
ATOM   2968 O  O   . TRP A 1 367 ? 4.245   -7.384  -4.093  1.00 48.32  ? 367  TRP A O   1 
ATOM   2969 C  CB  . TRP A 1 367 ? 2.000   -9.273  -3.040  1.00 38.11  ? 367  TRP A CB  1 
ATOM   2970 C  CG  . TRP A 1 367 ? 0.538   -9.470  -2.656  1.00 35.68  ? 367  TRP A CG  1 
ATOM   2971 C  CD1 . TRP A 1 367 ? -0.216  -10.586 -2.856  1.00 34.93  ? 367  TRP A CD1 1 
ATOM   2972 C  CD2 . TRP A 1 367 ? -0.338  -8.494  -2.058  1.00 36.76  ? 367  TRP A CD2 1 
ATOM   2973 N  NE1 . TRP A 1 367 ? -1.509  -10.370 -2.420  1.00 33.31  ? 367  TRP A NE1 1 
ATOM   2974 C  CE2 . TRP A 1 367 ? -1.604  -9.095  -1.925  1.00 34.18  ? 367  TRP A CE2 1 
ATOM   2975 C  CE3 . TRP A 1 367 ? -0.173  -7.166  -1.643  1.00 33.54  ? 367  TRP A CE3 1 
ATOM   2976 C  CZ2 . TRP A 1 367 ? -2.696  -8.422  -1.373  1.00 33.62  ? 367  TRP A CZ2 1 
ATOM   2977 C  CZ3 . TRP A 1 367 ? -1.253  -6.499  -1.095  1.00 37.97  ? 367  TRP A CZ3 1 
ATOM   2978 C  CH2 . TRP A 1 367 ? -2.499  -7.129  -0.959  1.00 31.93  ? 367  TRP A CH2 1 
ATOM   2979 N  N   . GLY A 1 368 ? 4.097   -8.954  -5.693  1.00 39.43  ? 368  GLY A N   1 
ATOM   2980 C  CA  . GLY A 1 368 ? 5.475   -8.788  -6.114  1.00 42.87  ? 368  GLY A CA  1 
ATOM   2981 C  C   . GLY A 1 368 ? 6.378   -9.845  -5.512  1.00 50.62  ? 368  GLY A C   1 
ATOM   2982 O  O   . GLY A 1 368 ? 5.951   -10.752 -4.791  1.00 47.25  ? 368  GLY A O   1 
ATOM   2983 N  N   . ASP A 1 369 ? 7.669   -9.713  -5.826  1.00 46.98  ? 369  ASP A N   1 
ATOM   2984 C  CA  . ASP A 1 369 ? 8.635   -10.718 -5.395  1.00 54.43  ? 369  ASP A CA  1 
ATOM   2985 C  C   . ASP A 1 369 ? 8.776   -10.759 -3.874  1.00 48.00  ? 369  ASP A C   1 
ATOM   2986 O  O   . ASP A 1 369 ? 8.987   -11.831 -3.301  1.00 54.91  ? 369  ASP A O   1 
ATOM   2987 C  CB  . ASP A 1 369 ? 9.987   -10.450 -6.055  1.00 54.66  ? 369  ASP A CB  1 
ATOM   2988 C  CG  . ASP A 1 369 ? 9.991   -10.781 -7.546  1.00 65.15  ? 369  ASP A CG  1 
ATOM   2989 O  OD1 . ASP A 1 369 ? 9.081   -11.511 -8.015  1.00 58.11  ? 369  ASP A OD1 1 
ATOM   2990 O  OD2 . ASP A 1 369 ? 10.903  -10.294 -8.251  1.00 70.12  ? 369  ASP A OD2 1 
ATOM   2991 N  N   . ASP A 1 370 ? 8.656   -9.617  -3.205  1.00 50.15  ? 370  ASP A N   1 
ATOM   2992 C  CA  . ASP A 1 370 ? 8.861   -9.556  -1.761  1.00 49.60  ? 370  ASP A CA  1 
ATOM   2993 C  C   . ASP A 1 370 ? 7.638   -10.043 -0.982  1.00 47.29  ? 370  ASP A C   1 
ATOM   2994 O  O   . ASP A 1 370 ? 7.398   -9.584  0.138   1.00 46.20  ? 370  ASP A O   1 
ATOM   2995 C  CB  . ASP A 1 370 ? 9.218   -8.124  -1.346  1.00 43.86  ? 370  ASP A CB  1 
ATOM   2996 C  CG  . ASP A 1 370 ? 8.040   -7.168  -1.464  1.00 50.86  ? 370  ASP A CG  1 
ATOM   2997 O  OD1 . ASP A 1 370 ? 7.012   -7.565  -2.052  1.00 53.19  ? 370  ASP A OD1 1 
ATOM   2998 O  OD2 . ASP A 1 370 ? 8.139   -6.021  -0.979  1.00 53.07  ? 370  ASP A OD2 1 
ATOM   2999 N  N   . VAL A 1 371 ? 6.897   -11.009 -1.534  1.00 45.11  ? 371  VAL A N   1 
ATOM   3000 C  CA  . VAL A 1 371 ? 5.568   -11.317 -0.997  1.00 45.46  ? 371  VAL A CA  1 
ATOM   3001 C  C   . VAL A 1 371 ? 5.632   -11.905 0.416   1.00 43.61  ? 371  VAL A C   1 
ATOM   3002 O  O   . VAL A 1 371 ? 4.666   -11.787 1.192   1.00 42.02  ? 371  VAL A O   1 
ATOM   3003 C  CB  . VAL A 1 371 ? 4.816   -12.248 -1.964  1.00 46.71  ? 371  VAL A CB  1 
ATOM   3004 C  CG1 . VAL A 1 371 ? 5.474   -13.620 -2.010  1.00 44.91  ? 371  VAL A CG1 1 
ATOM   3005 C  CG2 . VAL A 1 371 ? 3.354   -12.354 -1.547  1.00 42.81  ? 371  VAL A CG2 1 
ATOM   3006 N  N   . GLU A 1 372 ? 6.744   -12.541 0.786   1.00 43.50  ? 372  GLU A N   1 
ATOM   3007 C  CA  . GLU A 1 372 ? 6.860   -13.084 2.132   1.00 41.52  ? 372  GLU A CA  1 
ATOM   3008 C  C   . GLU A 1 372 ? 7.326   -12.050 3.153   1.00 38.33  ? 372  GLU A C   1 
ATOM   3009 O  O   . GLU A 1 372 ? 7.317   -12.347 4.351   1.00 40.84  ? 372  GLU A O   1 
ATOM   3010 C  CB  . GLU A 1 372 ? 7.808   -14.288 2.139   1.00 44.74  ? 372  GLU A CB  1 
ATOM   3011 C  CG  . GLU A 1 372 ? 7.228   -15.521 1.467   1.00 43.10  ? 372  GLU A CG  1 
ATOM   3012 C  CD  . GLU A 1 372 ? 6.220   -16.260 2.355   1.00 47.51  ? 372  GLU A CD  1 
ATOM   3013 O  OE1 . GLU A 1 372 ? 6.351   -16.195 3.602   1.00 51.83  ? 372  GLU A OE1 1 
ATOM   3014 O  OE2 . GLU A 1 372 ? 5.291   -16.897 1.812   1.00 48.05  ? 372  GLU A OE2 1 
ATOM   3015 N  N   . GLU A 1 373 ? 7.712   -10.854 2.718   1.00 41.85  ? 373  GLU A N   1 
ATOM   3016 C  CA  . GLU A 1 373 ? 8.164   -9.799  3.615   1.00 41.21  ? 373  GLU A CA  1 
ATOM   3017 C  C   . GLU A 1 373 ? 6.986   -9.125  4.308   1.00 43.85  ? 373  GLU A C   1 
ATOM   3018 O  O   . GLU A 1 373 ? 5.883   -9.039  3.763   1.00 36.89  ? 373  GLU A O   1 
ATOM   3019 C  CB  . GLU A 1 373 ? 8.954   -8.741  2.843   1.00 42.76  ? 373  GLU A CB  1 
ATOM   3020 C  CG  . GLU A 1 373 ? 10.375  -9.144  2.522   1.00 48.20  ? 373  GLU A CG  1 
ATOM   3021 C  CD  . GLU A 1 373 ? 11.147  -8.017  1.869   1.00 57.44  ? 373  GLU A CD  1 
ATOM   3022 O  OE1 . GLU A 1 373 ? 11.054  -6.868  2.353   1.00 64.76  ? 373  GLU A OE1 1 
ATOM   3023 O  OE2 . GLU A 1 373 ? 11.841  -8.278  0.866   1.00 61.05  ? 373  GLU A OE2 1 
ATOM   3024 N  N   . PHE A 1 374 ? 7.242   -8.612  5.504   1.00 37.63  ? 374  PHE A N   1 
ATOM   3025 C  CA  . PHE A 1 374 ? 6.236   -7.902  6.284   1.00 35.47  ? 374  PHE A CA  1 
ATOM   3026 C  C   . PHE A 1 374 ? 6.414   -6.409  6.038   1.00 36.94  ? 374  PHE A C   1 
ATOM   3027 O  O   . PHE A 1 374 ? 7.251   -5.748  6.669   1.00 36.70  ? 374  PHE A O   1 
ATOM   3028 C  CB  . PHE A 1 374 ? 6.349   -8.246  7.766   1.00 33.48  ? 374  PHE A CB  1 
ATOM   3029 C  CG  . PHE A 1 374 ? 5.195   -7.759  8.575   1.00 35.51  ? 374  PHE A CG  1 
ATOM   3030 C  CD1 . PHE A 1 374 ? 4.000   -8.470  8.590   1.00 34.47  ? 374  PHE A CD1 1 
ATOM   3031 C  CD2 . PHE A 1 374 ? 5.286   -6.586  9.300   1.00 35.66  ? 374  PHE A CD2 1 
ATOM   3032 C  CE1 . PHE A 1 374 ? 2.920   -8.027  9.335   1.00 27.26  ? 374  PHE A CE1 1 
ATOM   3033 C  CE2 . PHE A 1 374 ? 4.199   -6.127  10.046  1.00 37.85  ? 374  PHE A CE2 1 
ATOM   3034 C  CZ  . PHE A 1 374 ? 3.014   -6.849  10.057  1.00 34.57  ? 374  PHE A CZ  1 
ATOM   3035 N  N   . ARG A 1 375 ? 5.605   -5.866  5.131   1.00 35.18  ? 375  ARG A N   1 
ATOM   3036 C  CA  . ARG A 1 375 ? 5.713   -4.467  4.728   1.00 36.02  ? 375  ARG A CA  1 
ATOM   3037 C  C   . ARG A 1 375 ? 4.334   -3.831  4.795   1.00 34.83  ? 375  ARG A C   1 
ATOM   3038 O  O   . ARG A 1 375 ? 3.610   -3.797  3.792   1.00 37.07  ? 375  ARG A O   1 
ATOM   3039 C  CB  . ARG A 1 375 ? 6.291   -4.336  3.318   1.00 41.62  ? 375  ARG A CB  1 
ATOM   3040 C  CG  . ARG A 1 375 ? 6.551   -2.889  2.937   1.00 47.22  ? 375  ARG A CG  1 
ATOM   3041 C  CD  . ARG A 1 375 ? 7.509   -2.760  1.747   1.00 53.64  ? 375  ARG A CD  1 
ATOM   3042 N  NE  . ARG A 1 375 ? 7.013   -3.512  0.599   1.00 46.93  ? 375  ARG A NE  1 
ATOM   3043 C  CZ  . ARG A 1 375 ? 6.193   -3.008  -0.313  1.00 51.76  ? 375  ARG A CZ  1 
ATOM   3044 N  NH1 . ARG A 1 375 ? 5.692   -1.787  -0.188  1.00 53.27  ? 375  ARG A NH1 1 
ATOM   3045 N  NH2 . ARG A 1 375 ? 5.847   -3.753  -1.363  1.00 53.27  ? 375  ARG A NH2 1 
ATOM   3046 N  N   . PRO A 1 376 ? 3.943   -3.300  5.952   1.00 36.83  ? 376  PRO A N   1 
ATOM   3047 C  CA  . PRO A 1 376 ? 2.612   -2.680  6.058   1.00 35.58  ? 376  PRO A CA  1 
ATOM   3048 C  C   . PRO A 1 376 ? 2.358   -1.618  5.003   1.00 37.85  ? 376  PRO A C   1 
ATOM   3049 O  O   . PRO A 1 376 ? 1.198   -1.367  4.648   1.00 36.24  ? 376  PRO A O   1 
ATOM   3050 C  CB  . PRO A 1 376 ? 2.635   -2.063  7.461   1.00 35.34  ? 376  PRO A CB  1 
ATOM   3051 C  CG  . PRO A 1 376 ? 3.643   -2.889  8.227   1.00 38.93  ? 376  PRO A CG  1 
ATOM   3052 C  CD  . PRO A 1 376 ? 4.702   -3.209  7.213   1.00 38.51  ? 376  PRO A CD  1 
ATOM   3053 N  N   . GLU A 1 377 ? 3.414   -0.954  4.519   1.00 34.31  ? 377  GLU A N   1 
ATOM   3054 C  CA  . GLU A 1 377 ? 3.246   0.085   3.505   1.00 40.20  ? 377  GLU A CA  1 
ATOM   3055 C  C   . GLU A 1 377 ? 2.553   -0.430  2.239   1.00 37.26  ? 377  GLU A C   1 
ATOM   3056 O  O   . GLU A 1 377 ? 2.070   0.383   1.441   1.00 38.47  ? 377  GLU A O   1 
ATOM   3057 C  CB  . GLU A 1 377 ? 4.619   0.692   3.177   1.00 42.58  ? 377  GLU A CB  1 
ATOM   3058 C  CG  . GLU A 1 377 ? 5.239   1.515   4.339   1.00 44.36  ? 377  GLU A CG  1 
ATOM   3059 C  CD  . GLU A 1 377 ? 5.907   0.653   5.428   1.00 41.70  ? 377  GLU A CD  1 
ATOM   3060 O  OE1 . GLU A 1 377 ? 6.116   -0.562  5.209   1.00 39.65  ? 377  GLU A OE1 1 
ATOM   3061 O  OE2 . GLU A 1 377 ? 6.226   1.203   6.507   1.00 42.83  ? 377  GLU A OE2 1 
ATOM   3062 N  N   . ARG A 1 378 ? 2.519   -1.753  2.022   1.00 35.20  ? 378  ARG A N   1 
ATOM   3063 C  CA  . ARG A 1 378 ? 1.729   -2.322  0.927   1.00 40.08  ? 378  ARG A CA  1 
ATOM   3064 C  C   . ARG A 1 378 ? 0.312   -1.793  0.896   1.00 35.75  ? 378  ARG A C   1 
ATOM   3065 O  O   . ARG A 1 378 ? -0.334  -1.822  -0.159  1.00 40.31  ? 378  ARG A O   1 
ATOM   3066 C  CB  . ARG A 1 378 ? 1.613   -3.842  1.043   1.00 41.75  ? 378  ARG A CB  1 
ATOM   3067 C  CG  . ARG A 1 378 ? 2.817   -4.622  0.745   1.00 45.61  ? 378  ARG A CG  1 
ATOM   3068 C  CD  . ARG A 1 378 ? 2.549   -6.040  1.142   1.00 38.24  ? 378  ARG A CD  1 
ATOM   3069 N  NE  . ARG A 1 378 ? 3.787   -6.710  1.496   1.00 40.92  ? 378  ARG A NE  1 
ATOM   3070 C  CZ  . ARG A 1 378 ? 4.663   -7.154  0.609   1.00 44.24  ? 378  ARG A CZ  1 
ATOM   3071 N  NH1 . ARG A 1 378 ? 4.470   -6.994  -0.692  1.00 43.28  ? 378  ARG A NH1 1 
ATOM   3072 N  NH2 . ARG A 1 378 ? 5.755   -7.777  1.036   1.00 48.47  ? 378  ARG A NH2 1 
ATOM   3073 N  N   . PHE A 1 379 ? -0.215  -1.375  2.045   1.00 34.96  ? 379  PHE A N   1 
ATOM   3074 C  CA  . PHE A 1 379 ? -1.615  -0.985  2.166   1.00 38.10  ? 379  PHE A CA  1 
ATOM   3075 C  C   . PHE A 1 379 ? -1.808  0.525   2.151   1.00 37.92  ? 379  PHE A C   1 
ATOM   3076 O  O   . PHE A 1 379 ? -2.898  1.013   2.463   1.00 38.66  ? 379  PHE A O   1 
ATOM   3077 C  CB  . PHE A 1 379 ? -2.219  -1.623  3.424   1.00 36.23  ? 379  PHE A CB  1 
ATOM   3078 C  CG  . PHE A 1 379 ? -2.428  -3.110  3.275   1.00 35.20  ? 379  PHE A CG  1 
ATOM   3079 C  CD1 . PHE A 1 379 ? -3.592  -3.604  2.679   1.00 35.58  ? 379  PHE A CD1 1 
ATOM   3080 C  CD2 . PHE A 1 379 ? -1.449  -4.011  3.654   1.00 35.05  ? 379  PHE A CD2 1 
ATOM   3081 C  CE1 . PHE A 1 379 ? -3.782  -4.971  2.487   1.00 37.57  ? 379  PHE A CE1 1 
ATOM   3082 C  CE2 . PHE A 1 379 ? -1.630  -5.390  3.470   1.00 34.24  ? 379  PHE A CE2 1 
ATOM   3083 C  CZ  . PHE A 1 379 ? -2.798  -5.871  2.885   1.00 37.64  ? 379  PHE A CZ  1 
ATOM   3084 N  N   . GLU A 1 380 ? -0.793  1.273   1.720   1.00 33.89  ? 380  GLU A N   1 
ATOM   3085 C  CA  . GLU A 1 380 ? -0.896  2.721   1.755   1.00 39.63  ? 380  GLU A CA  1 
ATOM   3086 C  C   . GLU A 1 380 ? -2.007  3.219   0.838   1.00 37.95  ? 380  GLU A C   1 
ATOM   3087 O  O   . GLU A 1 380 ? -2.664  4.217   1.144   1.00 39.18  ? 380  GLU A O   1 
ATOM   3088 C  CB  . GLU A 1 380 ? 0.453   3.326   1.376   1.00 40.38  ? 380  GLU A CB  1 
ATOM   3089 C  CG  . GLU A 1 380 ? 1.067   4.102   2.547   1.00 54.56  ? 380  GLU A CG  1 
ATOM   3090 C  CD  . GLU A 1 380 ? 2.561   4.302   2.384   1.00 59.23  ? 380  GLU A CD  1 
ATOM   3091 O  OE1 . GLU A 1 380 ? 3.029   4.364   1.225   1.00 59.15  ? 380  GLU A OE1 1 
ATOM   3092 O  OE2 . GLU A 1 380 ? 3.270   4.326   3.412   1.00 57.64  ? 380  GLU A OE2 1 
ATOM   3093 N  N   . ASN A 1 381 ? -2.259  2.521   -0.264  1.00 36.79  ? 381  ASN A N   1 
ATOM   3094 C  CA  . ASN A 1 381 ? -3.244  2.957   -1.249  1.00 36.94  ? 381  ASN A CA  1 
ATOM   3095 C  C   . ASN A 1 381 ? -4.126  1.800   -1.705  1.00 35.16  ? 381  ASN A C   1 
ATOM   3096 O  O   . ASN A 1 381 ? -3.765  1.059   -2.635  1.00 33.47  ? 381  ASN A O   1 
ATOM   3097 C  CB  . ASN A 1 381 ? -2.548  3.606   -2.438  1.00 38.73  ? 381  ASN A CB  1 
ATOM   3098 C  CG  . ASN A 1 381 ? -3.529  4.172   -3.427  1.00 40.11  ? 381  ASN A CG  1 
ATOM   3099 O  OD1 . ASN A 1 381 ? -4.745  4.153   -3.195  1.00 37.50  ? 381  ASN A OD1 1 
ATOM   3100 N  ND2 . ASN A 1 381 ? -3.018  4.684   -4.534  1.00 37.02  ? 381  ASN A ND2 1 
ATOM   3101 N  N   . PRO A 1 382 ? -5.308  1.627   -1.093  1.00 34.02  ? 382  PRO A N   1 
ATOM   3102 C  CA  . PRO A 1 382 ? -6.219  0.557   -1.522  1.00 35.43  ? 382  PRO A CA  1 
ATOM   3103 C  C   . PRO A 1 382 ? -6.553  0.605   -3.007  1.00 34.47  ? 382  PRO A C   1 
ATOM   3104 O  O   . PRO A 1 382 ? -6.927  -0.417  -3.593  1.00 34.94  ? 382  PRO A O   1 
ATOM   3105 C  CB  . PRO A 1 382 ? -7.472  0.807   -0.670  1.00 34.46  ? 382  PRO A CB  1 
ATOM   3106 C  CG  . PRO A 1 382 ? -6.957  1.550   0.542   1.00 41.47  ? 382  PRO A CG  1 
ATOM   3107 C  CD  . PRO A 1 382 ? -5.867  2.436   0.001   1.00 35.71  ? 382  PRO A CD  1 
ATOM   3108 N  N   . SER A 1 383 ? -6.459  1.786   -3.629  1.00 31.62  ? 383  SER A N   1 
ATOM   3109 C  CA  . SER A 1 383 ? -6.776  1.866   -5.048  1.00 33.21  ? 383  SER A CA  1 
ATOM   3110 C  C   . SER A 1 383 ? -5.710  1.205   -5.911  1.00 34.13  ? 383  SER A C   1 
ATOM   3111 O  O   . SER A 1 383 ? -5.978  0.891   -7.072  1.00 34.75  ? 383  SER A O   1 
ATOM   3112 C  CB  . SER A 1 383 ? -6.962  3.329   -5.481  1.00 34.03  ? 383  SER A CB  1 
ATOM   3113 O  OG  . SER A 1 383 ? -7.995  3.968   -4.735  1.00 36.77  ? 383  SER A OG  1 
ATOM   3114 N  N   . ALA A 1 384 ? -4.508  1.001   -5.376  1.00 35.29  ? 384  ALA A N   1 
ATOM   3115 C  CA  . ALA A 1 384 ? -3.448  0.349   -6.129  1.00 36.93  ? 384  ALA A CA  1 
ATOM   3116 C  C   . ALA A 1 384 ? -3.467  -1.168  -5.980  1.00 36.39  ? 384  ALA A C   1 
ATOM   3117 O  O   . ALA A 1 384 ? -2.635  -1.841  -6.590  1.00 38.02  ? 384  ALA A O   1 
ATOM   3118 C  CB  . ALA A 1 384 ? -2.078  0.900   -5.701  1.00 37.78  ? 384  ALA A CB  1 
ATOM   3119 N  N   . ILE A 1 385 ? -4.377  -1.716  -5.184  1.00 34.31  ? 385  ILE A N   1 
ATOM   3120 C  CA  . ILE A 1 385 ? -4.494  -3.160  -4.986  1.00 32.38  ? 385  ILE A CA  1 
ATOM   3121 C  C   . ILE A 1 385 ? -5.614  -3.673  -5.889  1.00 32.98  ? 385  ILE A C   1 
ATOM   3122 O  O   . ILE A 1 385 ? -6.753  -3.208  -5.756  1.00 35.85  ? 385  ILE A O   1 
ATOM   3123 C  CB  . ILE A 1 385 ? -4.786  -3.506  -3.520  1.00 37.02  ? 385  ILE A CB  1 
ATOM   3124 C  CG1 . ILE A 1 385 ? -3.699  -2.910  -2.602  1.00 38.09  ? 385  ILE A CG1 1 
ATOM   3125 C  CG2 . ILE A 1 385 ? -4.926  -5.036  -3.347  1.00 37.81  ? 385  ILE A CG2 1 
ATOM   3126 C  CD1 . ILE A 1 385 ? -4.005  -3.045  -1.118  1.00 38.30  ? 385  ILE A CD1 1 
ATOM   3127 N  N   . PRO A 1 386 ? -5.350  -4.639  -6.770  1.00 33.01  ? 386  PRO A N   1 
ATOM   3128 C  CA  . PRO A 1 386 ? -6.408  -5.177  -7.639  1.00 33.28  ? 386  PRO A CA  1 
ATOM   3129 C  C   . PRO A 1 386 ? -7.595  -5.729  -6.847  1.00 30.91  ? 386  PRO A C   1 
ATOM   3130 O  O   . PRO A 1 386 ? -7.497  -6.082  -5.672  1.00 31.41  ? 386  PRO A O   1 
ATOM   3131 C  CB  . PRO A 1 386 ? -5.692  -6.300  -8.408  1.00 34.74  ? 386  PRO A CB  1 
ATOM   3132 C  CG  . PRO A 1 386 ? -4.255  -5.886  -8.403  1.00 36.46  ? 386  PRO A CG  1 
ATOM   3133 C  CD  . PRO A 1 386 ? -4.025  -5.201  -7.086  1.00 32.90  ? 386  PRO A CD  1 
ATOM   3134 N  N   . GLN A 1 387 ? -8.735  -5.839  -7.535  1.00 34.09  ? 387  GLN A N   1 
ATOM   3135 C  CA  . GLN A 1 387 ? -9.950  -6.299  -6.880  1.00 32.26  ? 387  GLN A CA  1 
ATOM   3136 C  C   . GLN A 1 387 ? -9.778  -7.715  -6.338  1.00 34.29  ? 387  GLN A C   1 
ATOM   3137 O  O   . GLN A 1 387 ? -9.187  -8.579  -6.993  1.00 33.14  ? 387  GLN A O   1 
ATOM   3138 C  CB  . GLN A 1 387 ? -11.121 -6.272  -7.868  1.00 31.35  ? 387  GLN A CB  1 
ATOM   3139 C  CG  . GLN A 1 387 ? -11.609 -4.899  -8.226  1.00 32.96  ? 387  GLN A CG  1 
ATOM   3140 C  CD  . GLN A 1 387 ? -13.023 -4.939  -8.752  1.00 32.75  ? 387  GLN A CD  1 
ATOM   3141 O  OE1 . GLN A 1 387 ? -13.984 -4.973  -7.977  1.00 32.87  ? 387  GLN A OE1 1 
ATOM   3142 N  NE2 . GLN A 1 387 ? -13.161 -4.975  -10.070 1.00 34.35  ? 387  GLN A NE2 1 
ATOM   3143 N  N   . HIS A 1 388 ? -10.311 -7.942  -5.136  1.00 31.79  ? 388  HIS A N   1 
ATOM   3144 C  CA  . HIS A 1 388 ? -10.384 -9.258  -4.494  1.00 31.23  ? 388  HIS A CA  1 
ATOM   3145 C  C   . HIS A 1 388 ? -9.017  -9.904  -4.308  1.00 32.67  ? 388  HIS A C   1 
ATOM   3146 O  O   . HIS A 1 388 ? -8.908  -11.132 -4.170  1.00 32.15  ? 388  HIS A O   1 
ATOM   3147 C  CB  . HIS A 1 388 ? -11.333 -10.171 -5.266  1.00 34.27  ? 388  HIS A CB  1 
ATOM   3148 C  CG  . HIS A 1 388 ? -12.681 -9.553  -5.455  1.00 33.70  ? 388  HIS A CG  1 
ATOM   3149 N  ND1 . HIS A 1 388 ? -13.504 -9.249  -4.392  1.00 33.31  ? 388  HIS A ND1 1 
ATOM   3150 C  CD2 . HIS A 1 388 ? -13.319 -9.115  -6.565  1.00 34.67  ? 388  HIS A CD2 1 
ATOM   3151 C  CE1 . HIS A 1 388 ? -14.608 -8.676  -4.842  1.00 34.80  ? 388  HIS A CE1 1 
ATOM   3152 N  NE2 . HIS A 1 388 ? -14.523 -8.587  -6.159  1.00 34.97  ? 388  HIS A NE2 1 
ATOM   3153 N  N   . ALA A 1 389 ? -7.971  -9.088  -4.261  1.00 31.87  ? 389  ALA A N   1 
ATOM   3154 C  CA  . ALA A 1 389 ? -6.652  -9.592  -3.910  1.00 32.28  ? 389  ALA A CA  1 
ATOM   3155 C  C   . ALA A 1 389 ? -6.522  -9.918  -2.422  1.00 33.10  ? 389  ALA A C   1 
ATOM   3156 O  O   . ALA A 1 389 ? -5.673  -10.737 -2.055  1.00 32.50  ? 389  ALA A O   1 
ATOM   3157 C  CB  . ALA A 1 389 ? -5.590  -8.566  -4.283  1.00 30.92  ? 389  ALA A CB  1 
ATOM   3158 N  N   . PHE A 1 390 ? -7.336  -9.302  -1.566  1.00 30.15  ? 390  PHE A N   1 
ATOM   3159 C  CA  . PHE A 1 390 ? -7.129  -9.305  -0.118  1.00 30.73  ? 390  PHE A CA  1 
ATOM   3160 C  C   . PHE A 1 390 ? -8.475  -9.613  0.531   1.00 33.78  ? 390  PHE A C   1 
ATOM   3161 O  O   . PHE A 1 390 ? -9.369  -8.764  0.529   1.00 32.21  ? 390  PHE A O   1 
ATOM   3162 C  CB  . PHE A 1 390 ? -6.560  -7.944  0.317   1.00 30.07  ? 390  PHE A CB  1 
ATOM   3163 C  CG  . PHE A 1 390 ? -6.357  -7.770  1.818   1.00 35.30  ? 390  PHE A CG  1 
ATOM   3164 C  CD1 . PHE A 1 390 ? -5.393  -8.495  2.515   1.00 30.60  ? 390  PHE A CD1 1 
ATOM   3165 C  CD2 . PHE A 1 390 ? -7.111  -6.825  2.515   1.00 31.66  ? 390  PHE A CD2 1 
ATOM   3166 C  CE1 . PHE A 1 390 ? -5.205  -8.291  3.874   1.00 32.44  ? 390  PHE A CE1 1 
ATOM   3167 C  CE2 . PHE A 1 390 ? -6.924  -6.629  3.874   1.00 32.60  ? 390  PHE A CE2 1 
ATOM   3168 C  CZ  . PHE A 1 390 ? -5.966  -7.360  4.550   1.00 32.73  ? 390  PHE A CZ  1 
ATOM   3169 N  N   . LYS A 1 391 ? -8.641  -10.837 1.061   1.00 31.70  ? 391  LYS A N   1 
ATOM   3170 C  CA  . LYS A 1 391 ? -9.981  -11.283 1.455   1.00 30.52  ? 391  LYS A CA  1 
ATOM   3171 C  C   . LYS A 1 391 ? -10.028 -11.875 2.862   1.00 30.50  ? 391  LYS A C   1 
ATOM   3172 O  O   . LYS A 1 391 ? -10.696 -12.895 3.067   1.00 30.32  ? 391  LYS A O   1 
ATOM   3173 C  CB  . LYS A 1 391 ? -10.519 -12.331 0.479   1.00 30.99  ? 391  LYS A CB  1 
ATOM   3174 C  CG  . LYS A 1 391 ? -10.484 -11.964 -1.009  1.00 32.90  ? 391  LYS A CG  1 
ATOM   3175 C  CD  . LYS A 1 391 ? -11.354 -10.757 -1.331  1.00 32.05  ? 391  LYS A CD  1 
ATOM   3176 C  CE  . LYS A 1 391 ? -12.832 -11.034 -1.006  1.00 34.56  ? 391  LYS A CE  1 
ATOM   3177 N  NZ  . LYS A 1 391 ? -13.719 -10.002 -1.597  1.00 34.11  ? 391  LYS A NZ  1 
ATOM   3178 N  N   . PRO A 1 392 ? -9.353  -11.284 3.850   1.00 30.81  ? 392  PRO A N   1 
ATOM   3179 C  CA  . PRO A 1 392 ? -9.357  -11.877 5.201   1.00 29.03  ? 392  PRO A CA  1 
ATOM   3180 C  C   . PRO A 1 392 ? -10.706 -11.825 5.895   1.00 34.40  ? 392  PRO A C   1 
ATOM   3181 O  O   . PRO A 1 392 ? -10.869 -12.495 6.921   1.00 32.14  ? 392  PRO A O   1 
ATOM   3182 C  CB  . PRO A 1 392 ? -8.339  -11.023 5.956   1.00 31.66  ? 392  PRO A CB  1 
ATOM   3183 C  CG  . PRO A 1 392 ? -8.446  -9.692  5.301   1.00 32.15  ? 392  PRO A CG  1 
ATOM   3184 C  CD  . PRO A 1 392 ? -8.626  -9.998  3.824   1.00 30.79  ? 392  PRO A CD  1 
ATOM   3185 N  N   . HIS A 1 393 ? -11.656 -11.044 5.380   1.00 29.93  ? 393  HIS A N   1 
ATOM   3186 C  CA  . HIS A 1 393 ? -12.978 -10.891 5.977   1.00 31.14  ? 393  HIS A CA  1 
ATOM   3187 C  C   . HIS A 1 393 ? -14.065 -11.543 5.135   1.00 29.63  ? 393  HIS A C   1 
ATOM   3188 O  O   . HIS A 1 393 ? -15.252 -11.231 5.306   1.00 32.84  ? 393  HIS A O   1 
ATOM   3189 C  CB  . HIS A 1 393 ? -13.324 -9.413  6.162   1.00 35.93  ? 393  HIS A CB  1 
ATOM   3190 C  CG  . HIS A 1 393 ? -12.225 -8.594  6.752   1.00 38.95  ? 393  HIS A CG  1 
ATOM   3191 N  ND1 . HIS A 1 393 ? -11.819 -8.727  8.058   1.00 37.60  ? 393  HIS A ND1 1 
ATOM   3192 C  CD2 . HIS A 1 393 ? -11.474 -7.601  6.219   1.00 43.09  ? 393  HIS A CD2 1 
ATOM   3193 C  CE1 . HIS A 1 393 ? -10.858 -7.859  8.310   1.00 36.94  ? 393  HIS A CE1 1 
ATOM   3194 N  NE2 . HIS A 1 393 ? -10.628 -7.163  7.209   1.00 38.62  ? 393  HIS A NE2 1 
ATOM   3195 N  N   . GLY A 1 394 ? -13.692 -12.405 4.190   1.00 32.42  ? 394  GLY A N   1 
ATOM   3196 C  CA  . GLY A 1 394 ? -14.700 -13.010 3.344   1.00 30.72  ? 394  GLY A CA  1 
ATOM   3197 C  C   . GLY A 1 394 ? -15.161 -12.070 2.238   1.00 31.38  ? 394  GLY A C   1 
ATOM   3198 O  O   . GLY A 1 394 ? -14.435 -11.165 1.825   1.00 31.76  ? 394  GLY A O   1 
ATOM   3199 N  N   . ASN A 1 395 ? -16.397 -12.279 1.757   1.00 29.22  ? 395  ASN A N   1 
ATOM   3200 C  CA  . ASN A 1 395 ? -16.826 -11.618 0.530   1.00 31.49  ? 395  ASN A CA  1 
ATOM   3201 C  C   . ASN A 1 395 ? -18.298 -11.212 0.548   1.00 32.43  ? 395  ASN A C   1 
ATOM   3202 O  O   . ASN A 1 395 ? -19.159 -11.967 1.010   1.00 29.35  ? 395  ASN A O   1 
ATOM   3203 C  CB  . ASN A 1 395 ? -16.625 -12.516 -0.687  1.00 28.88  ? 395  ASN A CB  1 
ATOM   3204 C  CG  . ASN A 1 395 ? -16.914 -11.785 -1.998  1.00 33.72  ? 395  ASN A CG  1 
ATOM   3205 O  OD1 . ASN A 1 395 ? -16.210 -10.837 -2.346  1.00 33.24  ? 395  ASN A OD1 1 
ATOM   3206 N  ND2 . ASN A 1 395 ? -17.952 -12.206 -2.708  1.00 31.65  ? 395  ASN A ND2 1 
ATOM   3207 N  N   . GLY A 1 396 ? -18.572 -10.017 0.011   1.00 31.59  ? 396  GLY A N   1 
ATOM   3208 C  CA  . GLY A 1 396 ? -19.941 -9.625  -0.314  1.00 32.87  ? 396  GLY A CA  1 
ATOM   3209 C  C   . GLY A 1 396 ? -20.846 -9.486  0.900   1.00 32.42  ? 396  GLY A C   1 
ATOM   3210 O  O   . GLY A 1 396 ? -20.418 -9.121  1.995   1.00 31.92  ? 396  GLY A O   1 
ATOM   3211 N  N   . GLN A 1 397 ? -22.140 -9.766  0.687   1.00 30.37  ? 397  GLN A N   1 
ATOM   3212 C  CA  . GLN A 1 397 ? -23.095 -9.659  1.781   1.00 34.16  ? 397  GLN A CA  1 
ATOM   3213 C  C   . GLN A 1 397 ? -22.836 -10.688 2.875   1.00 31.75  ? 397  GLN A C   1 
ATOM   3214 O  O   . GLN A 1 397 ? -23.334 -10.520 3.997   1.00 32.61  ? 397  GLN A O   1 
ATOM   3215 C  CB  . GLN A 1 397 ? -24.532 -9.797  1.249   1.00 33.08  ? 397  GLN A CB  1 
ATOM   3216 C  CG  . GLN A 1 397 ? -24.874 -11.176 0.681   1.00 34.47  ? 397  GLN A CG  1 
ATOM   3217 C  CD  . GLN A 1 397 ? -26.302 -11.221 0.146   1.00 34.21  ? 397  GLN A CD  1 
ATOM   3218 O  OE1 . GLN A 1 397 ? -27.094 -10.328 0.427   1.00 36.24  ? 397  GLN A OE1 1 
ATOM   3219 N  NE2 . GLN A 1 397 ? -26.622 -12.242 -0.634  1.00 35.11  ? 397  GLN A NE2 1 
ATOM   3220 N  N   . ARG A 1 398 ? -22.061 -11.735 2.587   1.00 33.08  ? 398  ARG A N   1 
ATOM   3221 C  CA  . ARG A 1 398 ? -21.666 -12.706 3.605   1.00 32.10  ? 398  ARG A CA  1 
ATOM   3222 C  C   . ARG A 1 398 ? -20.273 -12.433 4.163   1.00 29.68  ? 398  ARG A C   1 
ATOM   3223 O  O   . ARG A 1 398 ? -19.686 -13.312 4.805   1.00 27.79  ? 398  ARG A O   1 
ATOM   3224 C  CB  . ARG A 1 398 ? -21.730 -14.133 3.047   1.00 32.57  ? 398  ARG A CB  1 
ATOM   3225 C  CG  . ARG A 1 398 ? -23.115 -14.580 2.580   1.00 29.18  ? 398  ARG A CG  1 
ATOM   3226 C  CD  . ARG A 1 398 ? -24.216 -14.372 3.618   1.00 30.40  ? 398  ARG A CD  1 
ATOM   3227 N  NE  . ARG A 1 398 ? -23.947 -15.074 4.868   1.00 28.56  ? 398  ARG A NE  1 
ATOM   3228 C  CZ  . ARG A 1 398 ? -24.271 -16.335 5.123   1.00 32.65  ? 398  ARG A CZ  1 
ATOM   3229 N  NH1 . ARG A 1 398 ? -24.914 -17.083 4.241   1.00 31.90  ? 398  ARG A NH1 1 
ATOM   3230 N  NH2 . ARG A 1 398 ? -23.940 -16.858 6.295   1.00 30.75  ? 398  ARG A NH2 1 
ATOM   3231 N  N   . ALA A 1 399 ? -19.738 -11.233 3.936   1.00 29.59  ? 399  ALA A N   1 
ATOM   3232 C  CA  . ALA A 1 399 ? -18.484 -10.856 4.567   1.00 32.91  ? 399  ALA A CA  1 
ATOM   3233 C  C   . ALA A 1 399 ? -18.678 -10.693 6.073   1.00 33.51  ? 399  ALA A C   1 
ATOM   3234 O  O   . ALA A 1 399 ? -19.798 -10.618 6.591   1.00 30.08  ? 399  ALA A O   1 
ATOM   3235 C  CB  . ALA A 1 399 ? -17.935 -9.558  3.964   1.00 33.92  ? 399  ALA A CB  1 
ATOM   3236 N  N   . CYS A 1 400 ? -17.553 -10.617 6.777   1.00 28.83  ? 400  CYS A N   1 
ATOM   3237 C  CA  . CYS A 1 400 ? -17.542 -10.512 8.233   1.00 32.61  ? 400  CYS A CA  1 
ATOM   3238 C  C   . CYS A 1 400 ? -18.366 -9.322  8.724   1.00 35.66  ? 400  CYS A C   1 
ATOM   3239 O  O   . CYS A 1 400 ? -18.089 -8.174  8.371   1.00 34.36  ? 400  CYS A O   1 
ATOM   3240 C  CB  . CYS A 1 400 ? -16.092 -10.388 8.696   1.00 30.22  ? 400  CYS A CB  1 
ATOM   3241 S  SG  . CYS A 1 400 ? -15.942 -10.234 10.479  1.00 31.89  ? 400  CYS A SG  1 
ATOM   3242 N  N   . ILE A 1 401 ? -19.383 -9.588  9.550   1.00 33.31  ? 401  ILE A N   1 
ATOM   3243 C  CA  . ILE A 1 401 ? -20.134 -8.484  10.138  1.00 31.13  ? 401  ILE A CA  1 
ATOM   3244 C  C   . ILE A 1 401 ? -19.371 -7.795  11.270  1.00 33.45  ? 401  ILE A C   1 
ATOM   3245 O  O   . ILE A 1 401 ? -19.643 -6.624  11.567  1.00 33.79  ? 401  ILE A O   1 
ATOM   3246 C  CB  . ILE A 1 401 ? -21.496 -8.972  10.647  1.00 30.56  ? 401  ILE A CB  1 
ATOM   3247 C  CG1 . ILE A 1 401 ? -22.421 -7.786  10.911  1.00 34.43  ? 401  ILE A CG1 1 
ATOM   3248 C  CG2 . ILE A 1 401 ? -21.342 -9.798  11.913  1.00 29.08  ? 401  ILE A CG2 1 
ATOM   3249 C  CD1 . ILE A 1 401 ? -23.822 -8.219  11.366  1.00 31.82  ? 401  ILE A CD1 1 
ATOM   3250 N  N   . GLY A 1 402 ? -18.402 -8.470  11.877  1.00 29.23  ? 402  GLY A N   1 
ATOM   3251 C  CA  . GLY A 1 402 ? -17.622 -7.977  13.001  1.00 33.24  ? 402  GLY A CA  1 
ATOM   3252 C  C   . GLY A 1 402 ? -16.329 -7.271  12.645  1.00 33.84  ? 402  GLY A C   1 
ATOM   3253 O  O   . GLY A 1 402 ? -15.541 -6.946  13.543  1.00 33.61  ? 402  GLY A O   1 
ATOM   3254 N  N   . GLN A 1 403 ? -16.117 -6.967  11.367  1.00 31.61  ? 403  GLN A N   1 
ATOM   3255 C  CA  . GLN A 1 403 ? -14.814 -6.481  10.906  1.00 34.37  ? 403  GLN A CA  1 
ATOM   3256 C  C   . GLN A 1 403 ? -14.396 -5.194  11.616  1.00 33.05  ? 403  GLN A C   1 
ATOM   3257 O  O   . GLN A 1 403 ? -13.233 -5.050  12.020  1.00 34.00  ? 403  GLN A O   1 
ATOM   3258 C  CB  . GLN A 1 403 ? -14.846 -6.269  9.390   1.00 35.78  ? 403  GLN A CB  1 
ATOM   3259 C  CG  . GLN A 1 403 ? -13.671 -5.455  8.888   1.00 43.21  ? 403  GLN A CG  1 
ATOM   3260 C  CD  . GLN A 1 403 ? -13.797 -5.081  7.428   1.00 48.16  ? 403  GLN A CD  1 
ATOM   3261 O  OE1 . GLN A 1 403 ? -14.562 -5.694  6.677   1.00 40.85  ? 403  GLN A OE1 1 
ATOM   3262 N  NE2 . GLN A 1 403 ? -13.051 -4.054  7.018   1.00 53.09  ? 403  GLN A NE2 1 
ATOM   3263 N  N   . GLN A 1 404 ? -15.312 -4.236  11.741  1.00 36.01  ? 404  GLN A N   1 
ATOM   3264 C  CA  . GLN A 1 404 ? -14.979 -2.978  12.401  1.00 36.08  ? 404  GLN A CA  1 
ATOM   3265 C  C   . GLN A 1 404 ? -14.697 -3.193  13.880  1.00 33.55  ? 404  GLN A C   1 
ATOM   3266 O  O   . GLN A 1 404 ? -13.817 -2.540  14.448  1.00 37.48  ? 404  GLN A O   1 
ATOM   3267 C  CB  . GLN A 1 404 ? -16.116 -1.964  12.233  1.00 40.92  ? 404  GLN A CB  1 
ATOM   3268 C  CG  . GLN A 1 404 ? -16.444 -1.601  10.798  1.00 46.22  ? 404  GLN A CG  1 
ATOM   3269 C  CD  . GLN A 1 404 ? -15.263 -1.000  10.079  1.00 51.68  ? 404  GLN A CD  1 
ATOM   3270 O  OE1 . GLN A 1 404 ? -14.878 -1.463  9.003   1.00 58.31  ? 404  GLN A OE1 1 
ATOM   3271 N  NE2 . GLN A 1 404 ? -14.660 0.023   10.677  1.00 57.20  ? 404  GLN A NE2 1 
ATOM   3272 N  N   . PHE A 1 405 ? -15.457 -4.080  14.521  1.00 31.24  ? 405  PHE A N   1 
ATOM   3273 C  CA  . PHE A 1 405 ? -15.224 -4.405  15.932  1.00 30.48  ? 405  PHE A CA  1 
ATOM   3274 C  C   . PHE A 1 405 ? -13.821 -4.976  16.131  1.00 35.40  ? 405  PHE A C   1 
ATOM   3275 O  O   . PHE A 1 405 ? -13.060 -4.528  17.007  1.00 31.60  ? 405  PHE A O   1 
ATOM   3276 C  CB  . PHE A 1 405 ? -16.296 -5.398  16.396  1.00 31.42  ? 405  PHE A CB  1 
ATOM   3277 C  CG  . PHE A 1 405 ? -16.311 -5.660  17.879  1.00 33.07  ? 405  PHE A CG  1 
ATOM   3278 C  CD1 . PHE A 1 405 ? -15.432 -6.574  18.446  1.00 31.64  ? 405  PHE A CD1 1 
ATOM   3279 C  CD2 . PHE A 1 405 ? -17.222 -5.015  18.711  1.00 31.65  ? 405  PHE A CD2 1 
ATOM   3280 C  CE1 . PHE A 1 405 ? -15.442 -6.830  19.815  1.00 34.45  ? 405  PHE A CE1 1 
ATOM   3281 C  CE2 . PHE A 1 405 ? -17.241 -5.274  20.087  1.00 35.67  ? 405  PHE A CE2 1 
ATOM   3282 C  CZ  . PHE A 1 405 ? -16.345 -6.186  20.627  1.00 33.77  ? 405  PHE A CZ  1 
ATOM   3283 N  N   . ALA A 1 406 ? -13.482 -6.000  15.339  1.00 33.41  ? 406  ALA A N   1 
ATOM   3284 C  CA  . ALA A 1 406 ? -12.170 -6.636  15.410  1.00 33.21  ? 406  ALA A CA  1 
ATOM   3285 C  C   . ALA A 1 406 ? -11.055 -5.626  15.203  1.00 31.99  ? 406  ALA A C   1 
ATOM   3286 O  O   . ALA A 1 406 ? -10.078 -5.600  15.961  1.00 30.69  ? 406  ALA A O   1 
ATOM   3287 C  CB  . ALA A 1 406 ? -12.063 -7.751  14.358  1.00 31.69  ? 406  ALA A CB  1 
ATOM   3288 N  N   . LEU A 1 407 ? -11.164 -4.808  14.159  1.00 33.40  ? 407  LEU A N   1 
ATOM   3289 C  CA  . LEU A 1 407 ? -10.061 -3.910  13.847  1.00 36.52  ? 407  LEU A CA  1 
ATOM   3290 C  C   . LEU A 1 407 ? -9.962  -2.776  14.857  1.00 34.26  ? 407  LEU A C   1 
ATOM   3291 O  O   . LEU A 1 407 ? -8.858  -2.331  15.176  1.00 33.75  ? 407  LEU A O   1 
ATOM   3292 C  CB  . LEU A 1 407 ? -10.209 -3.378  12.426  1.00 36.32  ? 407  LEU A CB  1 
ATOM   3293 C  CG  . LEU A 1 407 ? -9.954  -4.448  11.354  1.00 39.72  ? 407  LEU A CG  1 
ATOM   3294 C  CD1 . LEU A 1 407 ? -10.155 -3.885  9.925   1.00 39.57  ? 407  LEU A CD1 1 
ATOM   3295 C  CD2 . LEU A 1 407 ? -8.588  -5.086  11.502  1.00 40.46  ? 407  LEU A CD2 1 
ATOM   3296 N  N   . HIS A 1 408 ? -11.084 -2.312  15.399  1.00 34.83  ? 408  HIS A N   1 
ATOM   3297 C  CA  . HIS A 1 408 ? -11.000 -1.284  16.425  1.00 35.87  ? 408  HIS A CA  1 
ATOM   3298 C  C   . HIS A 1 408 ? -10.359 -1.840  17.694  1.00 35.60  ? 408  HIS A C   1 
ATOM   3299 O  O   . HIS A 1 408 ? -9.486  -1.204  18.295  1.00 33.97  ? 408  HIS A O   1 
ATOM   3300 C  CB  . HIS A 1 408 ? -12.382 -0.707  16.732  1.00 36.31  ? 408  HIS A CB  1 
ATOM   3301 C  CG  . HIS A 1 408 ? -12.333 0.523   17.590  1.00 37.15  ? 408  HIS A CG  1 
ATOM   3302 N  ND1 . HIS A 1 408 ? -12.082 1.777   17.075  1.00 36.20  ? 408  HIS A ND1 1 
ATOM   3303 C  CD2 . HIS A 1 408 ? -12.486 0.688   18.928  1.00 36.37  ? 408  HIS A CD2 1 
ATOM   3304 C  CE1 . HIS A 1 408 ? -12.096 2.664   18.056  1.00 37.76  ? 408  HIS A CE1 1 
ATOM   3305 N  NE2 . HIS A 1 408 ? -12.332 2.029   19.191  1.00 39.28  ? 408  HIS A NE2 1 
ATOM   3306 N  N   . GLU A 1 409 ? -10.785 -3.029  18.119  1.00 31.88  ? 409  GLU A N   1 
ATOM   3307 C  CA  . GLU A 1 409 ? -10.187 -3.637  19.303  1.00 33.80  ? 409  GLU A CA  1 
ATOM   3308 C  C   . GLU A 1 409 ? -8.697  -3.883  19.100  1.00 35.24  ? 409  GLU A C   1 
ATOM   3309 O  O   . GLU A 1 409 ? -7.870  -3.571  19.972  1.00 33.69  ? 409  GLU A O   1 
ATOM   3310 C  CB  . GLU A 1 409 ? -10.898 -4.945  19.626  1.00 34.47  ? 409  GLU A CB  1 
ATOM   3311 C  CG  . GLU A 1 409 ? -10.159 -5.785  20.660  1.00 32.00  ? 409  GLU A CG  1 
ATOM   3312 C  CD  . GLU A 1 409 ? -10.903 -7.051  21.001  1.00 34.83  ? 409  GLU A CD  1 
ATOM   3313 O  OE1 . GLU A 1 409 ? -11.844 -7.416  20.261  1.00 32.86  ? 409  GLU A OE1 1 
ATOM   3314 O  OE2 . GLU A 1 409 ? -10.572 -7.659  22.026  1.00 33.99  ? 409  GLU A OE2 1 
ATOM   3315 N  N   . ALA A 1 410 ? -8.334  -4.449  17.952  1.00 32.29  ? 410  ALA A N   1 
ATOM   3316 C  CA  . ALA A 1 410 ? -6.931  -4.788  17.722  1.00 29.46  ? 410  ALA A CA  1 
ATOM   3317 C  C   . ALA A 1 410 ? -6.071  -3.534  17.601  1.00 35.86  ? 410  ALA A C   1 
ATOM   3318 O  O   . ALA A 1 410 ? -4.928  -3.511  18.077  1.00 35.52  ? 410  ALA A O   1 
ATOM   3319 C  CB  . ALA A 1 410 ? -6.805  -5.668  16.473  1.00 32.34  ? 410  ALA A CB  1 
ATOM   3320 N  N   . THR A 1 411 ? -6.594  -2.477  16.969  1.00 32.02  ? 411  THR A N   1 
ATOM   3321 C  CA  . THR A 1 411 ? -5.802  -1.252  16.843  1.00 33.61  ? 411  THR A CA  1 
ATOM   3322 C  C   . THR A 1 411 ? -5.601  -0.594  18.206  1.00 35.94  ? 411  THR A C   1 
ATOM   3323 O  O   . THR A 1 411 ? -4.488  -0.157  18.542  1.00 32.42  ? 411  THR A O   1 
ATOM   3324 C  CB  . THR A 1 411 ? -6.468  -0.287  15.857  1.00 35.86  ? 411  THR A CB  1 
ATOM   3325 O  OG1 . THR A 1 411 ? -6.655  -0.946  14.587  1.00 33.93  ? 411  THR A OG1 1 
ATOM   3326 C  CG2 . THR A 1 411 ? -5.594  0.968   15.655  1.00 32.69  ? 411  THR A CG2 1 
ATOM   3327 N  N   . LEU A 1 412 ? -6.663  -0.531  19.009  1.00 32.39  ? 412  LEU A N   1 
ATOM   3328 C  CA  . LEU A 1 412 ? -6.562  0.023   20.354  1.00 32.77  ? 412  LEU A CA  1 
ATOM   3329 C  C   . LEU A 1 412 ? -5.517  -0.727  21.168  1.00 33.01  ? 412  LEU A C   1 
ATOM   3330 O  O   . LEU A 1 412 ? -4.621  -0.119  21.768  1.00 33.60  ? 412  LEU A O   1 
ATOM   3331 C  CB  . LEU A 1 412 ? -7.926  -0.041  21.041  1.00 35.10  ? 412  LEU A CB  1 
ATOM   3332 C  CG  . LEU A 1 412 ? -7.937  0.080   22.569  1.00 38.32  ? 412  LEU A CG  1 
ATOM   3333 C  CD1 . LEU A 1 412 ? -7.605  1.514   22.973  1.00 39.35  ? 412  LEU A CD1 1 
ATOM   3334 C  CD2 . LEU A 1 412 ? -9.286  -0.334  23.142  1.00 35.86  ? 412  LEU A CD2 1 
ATOM   3335 N  N   . VAL A 1 413 ? -5.617  -2.059  21.188  1.00 31.85  ? 413  VAL A N   1 
ATOM   3336 C  CA  . VAL A 1 413 ? -4.786  -2.871  22.075  1.00 35.46  ? 413  VAL A CA  1 
ATOM   3337 C  C   . VAL A 1 413 ? -3.339  -2.854  21.613  1.00 34.71  ? 413  VAL A C   1 
ATOM   3338 O  O   . VAL A 1 413 ? -2.410  -2.716  22.422  1.00 32.73  ? 413  VAL A O   1 
ATOM   3339 C  CB  . VAL A 1 413 ? -5.337  -4.306  22.142  1.00 35.26  ? 413  VAL A CB  1 
ATOM   3340 C  CG1 . VAL A 1 413 ? -4.386  -5.197  22.890  1.00 39.99  ? 413  VAL A CG1 1 
ATOM   3341 C  CG2 . VAL A 1 413 ? -6.698  -4.297  22.831  1.00 35.17  ? 413  VAL A CG2 1 
ATOM   3342 N  N   . LEU A 1 414 ? -3.116  -3.007  20.305  1.00 32.10  ? 414  LEU A N   1 
ATOM   3343 C  CA  . LEU A 1 414 ? -1.738  -2.956  19.824  1.00 33.63  ? 414  LEU A CA  1 
ATOM   3344 C  C   . LEU A 1 414 ? -1.143  -1.565  20.037  1.00 36.36  ? 414  LEU A C   1 
ATOM   3345 O  O   . LEU A 1 414 ? 0.030   -1.435  20.420  1.00 35.94  ? 414  LEU A O   1 
ATOM   3346 C  CB  . LEU A 1 414 ? -1.678  -3.359  18.349  1.00 36.76  ? 414  LEU A CB  1 
ATOM   3347 C  CG  . LEU A 1 414 ? -0.324  -3.609  17.684  1.00 36.05  ? 414  LEU A CG  1 
ATOM   3348 C  CD1 . LEU A 1 414 ? 0.555   -4.589  18.481  1.00 35.38  ? 414  LEU A CD1 1 
ATOM   3349 C  CD2 . LEU A 1 414 ? -0.528  -4.116  16.265  1.00 36.12  ? 414  LEU A CD2 1 
ATOM   3350 N  N   . GLY A 1 415 ? -1.938  -0.513  19.798  1.00 33.54  ? 415  GLY A N   1 
ATOM   3351 C  CA  . GLY A 1 415 ? -1.470  0.834   20.092  1.00 33.73  ? 415  GLY A CA  1 
ATOM   3352 C  C   . GLY A 1 415 ? -1.044  0.989   21.540  1.00 39.36  ? 415  GLY A C   1 
ATOM   3353 O  O   . GLY A 1 415 ? 0.009   1.562   21.837  1.00 36.72  ? 415  GLY A O   1 
ATOM   3354 N  N   . MET A 1 416 ? -1.846  0.462   22.465  1.00 32.83  ? 416  MET A N   1 
ATOM   3355 C  CA  . MET A 1 416 ? -1.475  0.573   23.872  1.00 33.61  ? 416  MET A CA  1 
ATOM   3356 C  C   . MET A 1 416 ? -0.245  -0.276  24.190  1.00 34.09  ? 416  MET A C   1 
ATOM   3357 O  O   . MET A 1 416 ? 0.634   0.158   24.952  1.00 36.99  ? 416  MET A O   1 
ATOM   3358 C  CB  . MET A 1 416 ? -2.655  0.181   24.744  1.00 35.60  ? 416  MET A CB  1 
ATOM   3359 C  CG  . MET A 1 416 ? -3.771  1.194   24.726  1.00 36.34  ? 416  MET A CG  1 
ATOM   3360 S  SD  . MET A 1 416 ? -5.077  0.762   25.884  1.00 40.66  ? 416  MET A SD  1 
ATOM   3361 C  CE  . MET A 1 416 ? -4.296  1.145   27.440  1.00 41.85  ? 416  MET A CE  1 
ATOM   3362 N  N   . MET A 1 417 ? -0.153  -1.489  23.635  1.00 35.60  ? 417  MET A N   1 
ATOM   3363 C  CA  . MET A 1 417 ? 1.061   -2.264  23.874  1.00 34.90  ? 417  MET A CA  1 
ATOM   3364 C  C   . MET A 1 417 ? 2.300   -1.537  23.404  1.00 37.89  ? 417  MET A C   1 
ATOM   3365 O  O   . MET A 1 417 ? 3.312   -1.524  24.115  1.00 35.06  ? 417  MET A O   1 
ATOM   3366 C  CB  . MET A 1 417 ? 0.994   -3.681  23.284  1.00 35.16  ? 417  MET A CB  1 
ATOM   3367 C  CG  . MET A 1 417 ? -0.298  -4.470  23.534  1.00 37.46  ? 417  MET A CG  1 
ATOM   3368 S  SD  . MET A 1 417 ? -0.638  -5.836  22.409  1.00 36.84  ? 417  MET A SD  1 
ATOM   3369 C  CE  . MET A 1 417 ? 0.922   -6.680  22.225  1.00 33.71  ? 417  MET A CE  1 
ATOM   3370 N  N   . LEU A 1 418 ? 2.242   -0.915  22.228  1.00 33.54  ? 418  LEU A N   1 
ATOM   3371 C  CA  . LEU A 1 418 ? 3.416   -0.218  21.720  1.00 36.41  ? 418  LEU A CA  1 
ATOM   3372 C  C   . LEU A 1 418 ? 3.661   1.101   22.441  1.00 35.15  ? 418  LEU A C   1 
ATOM   3373 O  O   . LEU A 1 418 ? 4.791   1.600   22.445  1.00 37.19  ? 418  LEU A O   1 
ATOM   3374 C  CB  . LEU A 1 418 ? 3.254   -0.003  20.219  1.00 34.17  ? 418  LEU A CB  1 
ATOM   3375 C  CG  . LEU A 1 418 ? 3.189   -1.312  19.418  1.00 36.42  ? 418  LEU A CG  1 
ATOM   3376 C  CD1 . LEU A 1 418 ? 2.848   -1.047  17.948  1.00 38.77  ? 418  LEU A CD1 1 
ATOM   3377 C  CD2 . LEU A 1 418 ? 4.463   -2.131  19.525  1.00 41.27  ? 418  LEU A CD2 1 
ATOM   3378 N  N   . LYS A 1 419 ? 2.633   1.678   23.051  1.00 34.57  ? 419  LYS A N   1 
ATOM   3379 C  CA  . LYS A 1 419 ? 2.852   2.876   23.849  1.00 35.03  ? 419  LYS A CA  1 
ATOM   3380 C  C   . LYS A 1 419 ? 3.568   2.543   25.151  1.00 41.15  ? 419  LYS A C   1 
ATOM   3381 O  O   . LYS A 1 419 ? 4.457   3.288   25.585  1.00 40.46  ? 419  LYS A O   1 
ATOM   3382 C  CB  . LYS A 1 419 ? 1.520   3.571   24.137  1.00 35.73  ? 419  LYS A CB  1 
ATOM   3383 C  CG  . LYS A 1 419 ? 1.652   4.673   25.210  1.00 42.04  ? 419  LYS A CG  1 
ATOM   3384 C  CD  . LYS A 1 419 ? 0.331   5.392   25.431  1.00 41.10  ? 419  LYS A CD  1 
ATOM   3385 C  CE  . LYS A 1 419 ? 0.434   6.444   26.532  1.00 40.77  ? 419  LYS A CE  1 
ATOM   3386 N  NZ  . LYS A 1 419 ? -0.856  7.127   26.737  1.00 41.79  ? 419  LYS A NZ  1 
ATOM   3387 N  N   . HIS A 1 420 ? 3.225   1.415   25.770  1.00 36.87  ? 420  HIS A N   1 
ATOM   3388 C  CA  . HIS A 1 420 ? 3.635   1.180   27.147  1.00 36.14  ? 420  HIS A CA  1 
ATOM   3389 C  C   . HIS A 1 420 ? 4.843   0.263   27.301  1.00 37.78  ? 420  HIS A C   1 
ATOM   3390 O  O   . HIS A 1 420 ? 5.427   0.246   28.388  1.00 38.93  ? 420  HIS A O   1 
ATOM   3391 C  CB  . HIS A 1 420 ? 2.452   0.634   27.958  1.00 37.63  ? 420  HIS A CB  1 
ATOM   3392 C  CG  . HIS A 1 420 ? 1.437   1.685   28.290  1.00 40.23  ? 420  HIS A CG  1 
ATOM   3393 N  ND1 . HIS A 1 420 ? 1.549   2.509   29.390  1.00 38.84  ? 420  HIS A ND1 1 
ATOM   3394 C  CD2 . HIS A 1 420 ? 0.309   2.069   27.649  1.00 38.53  ? 420  HIS A CD2 1 
ATOM   3395 C  CE1 . HIS A 1 420 ? 0.525   3.341   29.422  1.00 40.34  ? 420  HIS A CE1 1 
ATOM   3396 N  NE2 . HIS A 1 420 ? -0.241  3.098   28.374  1.00 42.86  ? 420  HIS A NE2 1 
ATOM   3397 N  N   . PHE A 1 421 ? 5.256   -0.466  26.264  1.00 36.18  ? 421  PHE A N   1 
ATOM   3398 C  CA  . PHE A 1 421 ? 6.308   -1.469  26.410  1.00 38.06  ? 421  PHE A CA  1 
ATOM   3399 C  C   . PHE A 1 421 ? 7.220   -1.532  25.195  1.00 40.86  ? 421  PHE A C   1 
ATOM   3400 O  O   . PHE A 1 421 ? 6.785   -1.342  24.055  1.00 38.76  ? 421  PHE A O   1 
ATOM   3401 C  CB  . PHE A 1 421 ? 5.750   -2.898  26.601  1.00 38.84  ? 421  PHE A CB  1 
ATOM   3402 C  CG  . PHE A 1 421 ? 4.760   -3.023  27.716  1.00 37.67  ? 421  PHE A CG  1 
ATOM   3403 C  CD1 . PHE A 1 421 ? 5.184   -3.224  29.017  1.00 36.26  ? 421  PHE A CD1 1 
ATOM   3404 C  CD2 . PHE A 1 421 ? 3.400   -2.955  27.459  1.00 39.52  ? 421  PHE A CD2 1 
ATOM   3405 C  CE1 . PHE A 1 421 ? 4.272   -3.344  30.051  1.00 36.74  ? 421  PHE A CE1 1 
ATOM   3406 C  CE2 . PHE A 1 421 ? 2.480   -3.083  28.487  1.00 35.13  ? 421  PHE A CE2 1 
ATOM   3407 C  CZ  . PHE A 1 421 ? 2.918   -3.279  29.791  1.00 37.19  ? 421  PHE A CZ  1 
ATOM   3408 N  N   . ASP A 1 422 ? 8.492   -1.840  25.455  1.00 39.73  ? 422  ASP A N   1 
ATOM   3409 C  CA  . ASP A 1 422 ? 9.373   -2.432  24.460  1.00 42.28  ? 422  ASP A CA  1 
ATOM   3410 C  C   . ASP A 1 422 ? 9.264   -3.947  24.555  1.00 41.08  ? 422  ASP A C   1 
ATOM   3411 O  O   . ASP A 1 422 ? 9.016   -4.493  25.631  1.00 41.50  ? 422  ASP A O   1 
ATOM   3412 C  CB  . ASP A 1 422 ? 10.827  -2.012  24.686  1.00 42.63  ? 422  ASP A CB  1 
ATOM   3413 C  CG  . ASP A 1 422 ? 11.045  -0.546  24.446  1.00 47.14  ? 422  ASP A CG  1 
ATOM   3414 O  OD1 . ASP A 1 422 ? 10.701  -0.061  23.344  1.00 49.28  ? 422  ASP A OD1 1 
ATOM   3415 O  OD2 . ASP A 1 422 ? 11.547  0.122   25.367  1.00 47.22  ? 422  ASP A OD2 1 
ATOM   3416 N  N   . PHE A 1 423 ? 9.468   -4.629  23.430  1.00 35.99  ? 423  PHE A N   1 
ATOM   3417 C  CA  . PHE A 1 423 ? 9.315   -6.074  23.373  1.00 39.07  ? 423  PHE A CA  1 
ATOM   3418 C  C   . PHE A 1 423 ? 10.584  -6.741  22.874  1.00 41.31  ? 423  PHE A C   1 
ATOM   3419 O  O   . PHE A 1 423 ? 11.297  -6.204  22.021  1.00 41.72  ? 423  PHE A O   1 
ATOM   3420 C  CB  . PHE A 1 423 ? 8.149   -6.479  22.469  1.00 37.09  ? 423  PHE A CB  1 
ATOM   3421 C  CG  . PHE A 1 423 ? 6.822   -6.021  22.984  1.00 38.00  ? 423  PHE A CG  1 
ATOM   3422 C  CD1 . PHE A 1 423 ? 6.087   -6.825  23.836  1.00 37.99  ? 423  PHE A CD1 1 
ATOM   3423 C  CD2 . PHE A 1 423 ? 6.328   -4.775  22.642  1.00 37.37  ? 423  PHE A CD2 1 
ATOM   3424 C  CE1 . PHE A 1 423 ? 4.861   -6.402  24.326  1.00 39.07  ? 423  PHE A CE1 1 
ATOM   3425 C  CE2 . PHE A 1 423 ? 5.119   -4.345  23.129  1.00 36.33  ? 423  PHE A CE2 1 
ATOM   3426 C  CZ  . PHE A 1 423 ? 4.379   -5.160  23.967  1.00 39.41  ? 423  PHE A CZ  1 
ATOM   3427 N  N   . GLU A 1 424 ? 10.841  -7.935  23.398  1.00 37.01  ? 424  GLU A N   1 
ATOM   3428 C  CA  . GLU A 1 424 ? 12.046  -8.678  23.067  1.00 38.16  ? 424  GLU A CA  1 
ATOM   3429 C  C   . GLU A 1 424 ? 11.677  -10.104 22.694  1.00 37.58  ? 424  GLU A C   1 
ATOM   3430 O  O   . GLU A 1 424 ? 11.016  -10.804 23.467  1.00 38.05  ? 424  GLU A O   1 
ATOM   3431 C  CB  . GLU A 1 424 ? 13.032  -8.681  24.240  1.00 37.93  ? 424  GLU A CB  1 
ATOM   3432 C  CG  . GLU A 1 424 ? 14.257  -9.515  23.996  1.00 43.43  ? 424  GLU A CG  1 
ATOM   3433 C  CD  . GLU A 1 424 ? 15.071  -9.712  25.261  1.00 49.77  ? 424  GLU A CD  1 
ATOM   3434 O  OE1 . GLU A 1 424 ? 14.612  -9.277  26.339  1.00 48.07  ? 424  GLU A OE1 1 
ATOM   3435 O  OE2 . GLU A 1 424 ? 16.175  -10.283 25.169  1.00 52.17  ? 424  GLU A OE2 1 
ATOM   3436 N  N   . ASP A 1 425 ? 12.117  -10.533 21.513  1.00 37.10  ? 425  ASP A N   1 
ATOM   3437 C  CA  . ASP A 1 425 ? 11.973  -11.921 21.078  1.00 36.39  ? 425  ASP A CA  1 
ATOM   3438 C  C   . ASP A 1 425 ? 13.148  -12.672 21.697  1.00 36.71  ? 425  ASP A C   1 
ATOM   3439 O  O   . ASP A 1 425 ? 14.131  -13.018 21.036  1.00 38.03  ? 425  ASP A O   1 
ATOM   3440 C  CB  . ASP A 1 425 ? 11.939  -11.986 19.552  1.00 36.35  ? 425  ASP A CB  1 
ATOM   3441 C  CG  . ASP A 1 425 ? 11.909  -13.405 18.990  1.00 36.00  ? 425  ASP A CG  1 
ATOM   3442 O  OD1 . ASP A 1 425 ? 11.467  -14.366 19.666  1.00 37.53  ? 425  ASP A OD1 1 
ATOM   3443 O  OD2 . ASP A 1 425 ? 12.341  -13.546 17.821  1.00 38.24  ? 425  ASP A OD2 1 
ATOM   3444 N  N   . HIS A 1 426 ? 13.042  -12.912 23.009  1.00 38.99  ? 426  HIS A N   1 
ATOM   3445 C  CA  . HIS A 1 426 ? 14.190  -13.397 23.777  1.00 40.79  ? 426  HIS A CA  1 
ATOM   3446 C  C   . HIS A 1 426 ? 14.536  -14.850 23.474  1.00 41.89  ? 426  HIS A C   1 
ATOM   3447 O  O   . HIS A 1 426 ? 15.660  -15.272 23.763  1.00 42.15  ? 426  HIS A O   1 
ATOM   3448 C  CB  . HIS A 1 426 ? 13.943  -13.223 25.283  1.00 39.18  ? 426  HIS A CB  1 
ATOM   3449 C  CG  . HIS A 1 426 ? 12.811  -14.047 25.811  1.00 41.10  ? 426  HIS A CG  1 
ATOM   3450 N  ND1 . HIS A 1 426 ? 11.503  -13.848 25.419  1.00 38.88  ? 426  HIS A ND1 1 
ATOM   3451 C  CD2 . HIS A 1 426 ? 12.786  -15.070 26.700  1.00 43.66  ? 426  HIS A CD2 1 
ATOM   3452 C  CE1 . HIS A 1 426 ? 10.721  -14.717 26.039  1.00 41.41  ? 426  HIS A CE1 1 
ATOM   3453 N  NE2 . HIS A 1 426 ? 11.473  -15.465 26.829  1.00 46.00  ? 426  HIS A NE2 1 
ATOM   3454 N  N   . THR A 1 427 ? 13.610  -15.626 22.905  1.00 37.94  ? 427  THR A N   1 
ATOM   3455 C  CA  . THR A 1 427 ? 13.873  -17.018 22.549  1.00 37.24  ? 427  THR A CA  1 
ATOM   3456 C  C   . THR A 1 427 ? 14.167  -17.220 21.067  1.00 37.80  ? 427  THR A C   1 
ATOM   3457 O  O   . THR A 1 427 ? 14.377  -18.362 20.638  1.00 39.33  ? 427  THR A O   1 
ATOM   3458 C  CB  . THR A 1 427 ? 12.688  -17.906 22.957  1.00 41.37  ? 427  THR A CB  1 
ATOM   3459 O  OG1 . THR A 1 427 ? 11.617  -17.763 22.002  1.00 38.10  ? 427  THR A OG1 1 
ATOM   3460 C  CG2 . THR A 1 427 ? 12.186  -17.506 24.335  1.00 39.35  ? 427  THR A CG2 1 
ATOM   3461 N  N   . ASN A 1 428 ? 14.193  -16.150 20.277  1.00 36.82  ? 428  ASN A N   1 
ATOM   3462 C  CA  . ASN A 1 428 ? 14.252  -16.269 18.827  1.00 39.58  ? 428  ASN A CA  1 
ATOM   3463 C  C   . ASN A 1 428 ? 13.198  -17.261 18.340  1.00 39.63  ? 428  ASN A C   1 
ATOM   3464 O  O   . ASN A 1 428 ? 13.486  -18.278 17.709  1.00 38.94  ? 428  ASN A O   1 
ATOM   3465 C  CB  . ASN A 1 428 ? 15.650  -16.669 18.348  1.00 39.11  ? 428  ASN A CB  1 
ATOM   3466 C  CG  . ASN A 1 428 ? 15.833  -16.404 16.862  1.00 44.55  ? 428  ASN A CG  1 
ATOM   3467 O  OD1 . ASN A 1 428 ? 15.171  -15.529 16.300  1.00 43.97  ? 428  ASN A OD1 1 
ATOM   3468 N  ND2 . ASN A 1 428 ? 16.722  -17.156 16.220  1.00 43.90  ? 428  ASN A ND2 1 
ATOM   3469 N  N   . TYR A 1 429 ? 11.949  -16.932 18.648  1.00 35.95  ? 429  TYR A N   1 
ATOM   3470 C  CA  . TYR A 1 429 ? 10.862  -17.882 18.476  1.00 36.35  ? 429  TYR A CA  1 
ATOM   3471 C  C   . TYR A 1 429 ? 10.700  -18.307 17.021  1.00 35.83  ? 429  TYR A C   1 
ATOM   3472 O  O   . TYR A 1 429 ? 10.742  -17.487 16.103  1.00 36.21  ? 429  TYR A O   1 
ATOM   3473 C  CB  . TYR A 1 429 ? 9.575   -17.250 19.003  1.00 36.77  ? 429  TYR A CB  1 
ATOM   3474 C  CG  . TYR A 1 429 ? 8.323   -17.945 18.573  1.00 36.02  ? 429  TYR A CG  1 
ATOM   3475 C  CD1 . TYR A 1 429 ? 7.983   -19.195 19.085  1.00 35.35  ? 429  TYR A CD1 1 
ATOM   3476 C  CD2 . TYR A 1 429 ? 7.461   -17.347 17.646  1.00 37.93  ? 429  TYR A CD2 1 
ATOM   3477 C  CE1 . TYR A 1 429 ? 6.801   -19.834 18.686  1.00 36.70  ? 429  TYR A CE1 1 
ATOM   3478 C  CE2 . TYR A 1 429 ? 6.293   -17.970 17.251  1.00 34.95  ? 429  TYR A CE2 1 
ATOM   3479 C  CZ  . TYR A 1 429 ? 5.970   -19.203 17.762  1.00 36.43  ? 429  TYR A CZ  1 
ATOM   3480 O  OH  . TYR A 1 429 ? 4.809   -19.819 17.349  1.00 33.92  ? 429  TYR A OH  1 
ATOM   3481 N  N   . GLU A 1 430 ? 10.505  -19.609 16.820  1.00 35.36  ? 430  GLU A N   1 
ATOM   3482 C  CA  . GLU A 1 430 ? 10.256  -20.188 15.510  1.00 41.77  ? 430  GLU A CA  1 
ATOM   3483 C  C   . GLU A 1 430 ? 8.748   -20.329 15.331  1.00 36.49  ? 430  GLU A C   1 
ATOM   3484 O  O   . GLU A 1 430 ? 8.102   -21.079 16.072  1.00 37.15  ? 430  GLU A O   1 
ATOM   3485 C  CB  . GLU A 1 430 ? 10.934  -21.550 15.370  1.00 40.34  ? 430  GLU A CB  1 
ATOM   3486 C  CG  . GLU A 1 430 ? 10.765  -22.179 13.997  1.00 47.18  ? 430  GLU A CG  1 
ATOM   3487 C  CD  . GLU A 1 430 ? 11.469  -23.530 13.876  1.00 62.07  ? 430  GLU A CD  1 
ATOM   3488 O  OE1 . GLU A 1 430 ? 12.283  -23.868 14.763  1.00 67.93  ? 430  GLU A OE1 1 
ATOM   3489 O  OE2 . GLU A 1 430 ? 11.214  -24.251 12.887  1.00 67.84  ? 430  GLU A OE2 1 
ATOM   3490 N  N   . LEU A 1 431 ? 8.195   -19.604 14.360  1.00 36.24  ? 431  LEU A N   1 
ATOM   3491 C  CA  . LEU A 1 431 ? 6.746   -19.577 14.186  1.00 34.04  ? 431  LEU A CA  1 
ATOM   3492 C  C   . LEU A 1 431 ? 6.193   -20.991 14.029  1.00 35.84  ? 431  LEU A C   1 
ATOM   3493 O  O   . LEU A 1 431 ? 6.652   -21.775 13.196  1.00 36.71  ? 431  LEU A O   1 
ATOM   3494 C  CB  . LEU A 1 431 ? 6.379   -18.713 12.980  1.00 35.48  ? 431  LEU A CB  1 
ATOM   3495 C  CG  . LEU A 1 431 ? 4.884   -18.701 12.678  1.00 34.76  ? 431  LEU A CG  1 
ATOM   3496 C  CD1 . LEU A 1 431 ? 4.172   -18.033 13.833  1.00 33.29  ? 431  LEU A CD1 1 
ATOM   3497 C  CD2 . LEU A 1 431 ? 4.638   -17.966 11.357  1.00 36.64  ? 431  LEU A CD2 1 
ATOM   3498 N  N   . ASP A 1 432 ? 5.195   -21.315 14.839  1.00 34.36  ? 432  ASP A N   1 
ATOM   3499 C  CA  . ASP A 1 432 ? 4.564   -22.625 14.831  1.00 33.47  ? 432  ASP A CA  1 
ATOM   3500 C  C   . ASP A 1 432 ? 3.069   -22.357 14.882  1.00 32.25  ? 432  ASP A C   1 
ATOM   3501 O  O   . ASP A 1 432 ? 2.594   -21.769 15.859  1.00 35.48  ? 432  ASP A O   1 
ATOM   3502 C  CB  . ASP A 1 432 ? 5.023   -23.444 16.046  1.00 38.14  ? 432  ASP A CB  1 
ATOM   3503 C  CG  . ASP A 1 432 ? 4.368   -24.813 16.135  1.00 44.01  ? 432  ASP A CG  1 
ATOM   3504 O  OD1 . ASP A 1 432 ? 3.617   -25.198 15.221  1.00 42.38  ? 432  ASP A OD1 1 
ATOM   3505 O  OD2 . ASP A 1 432 ? 4.596   -25.508 17.149  1.00 48.80  ? 432  ASP A OD2 1 
ATOM   3506 N  N   . ILE A 1 433 ? 2.340   -22.735 13.840  1.00 33.56  ? 433  ILE A N   1 
ATOM   3507 C  CA  . ILE A 1 433 ? 0.948   -22.302 13.693  1.00 35.11  ? 433  ILE A CA  1 
ATOM   3508 C  C   . ILE A 1 433 ? 0.026   -23.464 14.020  1.00 32.63  ? 433  ILE A C   1 
ATOM   3509 O  O   . ILE A 1 433 ? -0.037  -24.462 13.293  1.00 34.47  ? 433  ILE A O   1 
ATOM   3510 C  CB  . ILE A 1 433 ? 0.668   -21.737 12.296  1.00 34.46  ? 433  ILE A CB  1 
ATOM   3511 C  CG1 . ILE A 1 433 ? 1.496   -20.462 12.114  1.00 35.51  ? 433  ILE A CG1 1 
ATOM   3512 C  CG2 . ILE A 1 433 ? -0.839  -21.430 12.151  1.00 33.14  ? 433  ILE A CG2 1 
ATOM   3513 C  CD1 . ILE A 1 433 ? 1.668   -20.023 10.682  1.00 35.44  ? 433  ILE A CD1 1 
ATOM   3514 N  N   . LYS A 1 434 ? -0.721  -23.317 15.110  1.00 33.31  ? 434  LYS A N   1 
ATOM   3515 C  CA  . LYS A 1 434 ? -1.699  -24.310 15.498  1.00 32.44  ? 434  LYS A CA  1 
ATOM   3516 C  C   . LYS A 1 434 ? -3.000  -24.063 14.757  1.00 36.24  ? 434  LYS A C   1 
ATOM   3517 O  O   . LYS A 1 434 ? -3.408  -22.914 14.560  1.00 35.99  ? 434  LYS A O   1 
ATOM   3518 C  CB  . LYS A 1 434 ? -1.939  -24.244 17.008  1.00 35.13  ? 434  LYS A CB  1 
ATOM   3519 C  CG  . LYS A 1 434 ? -2.933  -25.238 17.545  1.00 33.87  ? 434  LYS A CG  1 
ATOM   3520 C  CD  . LYS A 1 434 ? -2.973  -25.079 19.063  1.00 38.06  ? 434  LYS A CD  1 
ATOM   3521 C  CE  . LYS A 1 434 ? -4.072  -25.905 19.700  1.00 44.65  ? 434  LYS A CE  1 
ATOM   3522 N  NZ  . LYS A 1 434 ? -3.818  -27.354 19.514  1.00 48.18  ? 434  LYS A NZ  1 
ATOM   3523 N  N   . GLU A 1 435 ? -3.668  -25.146 14.382  1.00 31.69  ? 435  GLU A N   1 
ATOM   3524 C  CA  . GLU A 1 435 ? -4.911  -25.064 13.629  1.00 35.63  ? 435  GLU A CA  1 
ATOM   3525 C  C   . GLU A 1 435 ? -6.059  -25.592 14.479  1.00 35.79  ? 435  GLU A C   1 
ATOM   3526 O  O   . GLU A 1 435 ? -6.029  -26.737 14.949  1.00 35.36  ? 435  GLU A O   1 
ATOM   3527 C  CB  . GLU A 1 435 ? -4.796  -25.836 12.319  1.00 31.32  ? 435  GLU A CB  1 
ATOM   3528 C  CG  . GLU A 1 435 ? -3.722  -25.243 11.414  1.00 31.62  ? 435  GLU A CG  1 
ATOM   3529 C  CD  . GLU A 1 435 ? -3.872  -25.637 9.955   1.00 33.83  ? 435  GLU A CD  1 
ATOM   3530 O  OE1 . GLU A 1 435 ? -4.963  -26.084 9.551   1.00 34.59  ? 435  GLU A OE1 1 
ATOM   3531 O  OE2 . GLU A 1 435 ? -2.869  -25.534 9.215   1.00 35.00  ? 435  GLU A OE2 1 
ATOM   3532 N  N   . THR A 1 436 ? -7.059  -24.749 14.678  1.00 34.89  ? 436  THR A N   1 
ATOM   3533 C  CA  . THR A 1 436 ? -8.336  -25.152 15.256  1.00 36.18  ? 436  THR A CA  1 
ATOM   3534 C  C   . THR A 1 436 ? -9.445  -24.686 14.317  1.00 36.00  ? 436  THR A C   1 
ATOM   3535 O  O   . THR A 1 436 ? -10.380 -23.991 14.709  1.00 37.25  ? 436  THR A O   1 
ATOM   3536 C  CB  . THR A 1 436 ? -8.506  -24.575 16.656  1.00 38.21  ? 436  THR A CB  1 
ATOM   3537 O  OG1 . THR A 1 436 ? -8.328  -23.153 16.606  1.00 38.19  ? 436  THR A OG1 1 
ATOM   3538 C  CG2 . THR A 1 436 ? -7.489  -25.183 17.604  1.00 39.46  ? 436  THR A CG2 1 
ATOM   3539 N  N   . LEU A 1 437 ? -9.322  -25.082 13.054  1.00 34.11  ? 437  LEU A N   1 
ATOM   3540 C  CA  . LEU A 1 437 ? -10.052 -24.459 11.953  1.00 36.60  ? 437  LEU A CA  1 
ATOM   3541 C  C   . LEU A 1 437 ? -9.449  -23.067 11.736  1.00 40.87  ? 437  LEU A C   1 
ATOM   3542 O  O   . LEU A 1 437 ? -8.877  -22.818 10.669  1.00 36.78  ? 437  LEU A O   1 
ATOM   3543 C  CB  . LEU A 1 437 ? -11.574 -24.425 12.208  1.00 40.29  ? 437  LEU A CB  1 
ATOM   3544 C  CG  . LEU A 1 437 ? -12.313 -25.773 12.467  1.00 41.61  ? 437  LEU A CG  1 
ATOM   3545 C  CD1 . LEU A 1 437 ? -13.822 -25.615 12.575  1.00 40.24  ? 437  LEU A CD1 1 
ATOM   3546 C  CD2 . LEU A 1 437 ? -12.006 -26.793 11.405  1.00 38.34  ? 437  LEU A CD2 1 
ATOM   3547 N  N   . THR A 1 438 ? -9.517  -22.183 12.743  1.00 36.68  ? 438  THR A N   1 
ATOM   3548 C  CA  . THR A 1 438 ? -8.760  -20.928 12.760  1.00 37.77  ? 438  THR A CA  1 
ATOM   3549 C  C   . THR A 1 438 ? -7.264  -21.184 13.006  1.00 36.58  ? 438  THR A C   1 
ATOM   3550 O  O   . THR A 1 438 ? -6.850  -22.292 13.361  1.00 35.43  ? 438  THR A O   1 
ATOM   3551 C  CB  . THR A 1 438 ? -9.300  -20.006 13.840  1.00 39.92  ? 438  THR A CB  1 
ATOM   3552 O  OG1 . THR A 1 438 ? -9.270  -20.717 15.083  1.00 39.04  ? 438  THR A OG1 1 
ATOM   3553 C  CG2 . THR A 1 438 ? -10.748 -19.602 13.528  1.00 35.23  ? 438  THR A CG2 1 
ATOM   3554 N  N   . LEU A 1 439 ? -6.451  -20.136 12.809  1.00 32.32  ? 439  LEU A N   1 
ATOM   3555 C  CA  . LEU A 1 439 ? -4.989  -20.202 12.872  1.00 32.42  ? 439  LEU A CA  1 
ATOM   3556 C  C   . LEU A 1 439 ? -4.452  -19.285 13.969  1.00 32.84  ? 439  LEU A C   1 
ATOM   3557 O  O   . LEU A 1 439 ? -4.893  -18.142 14.106  1.00 31.41  ? 439  LEU A O   1 
ATOM   3558 C  CB  . LEU A 1 439 ? -4.362  -19.776 11.538  1.00 31.76  ? 439  LEU A CB  1 
ATOM   3559 C  CG  . LEU A 1 439 ? -4.782  -20.450 10.223  1.00 30.54  ? 439  LEU A CG  1 
ATOM   3560 C  CD1 . LEU A 1 439 ? -3.876  -19.962 9.077   1.00 30.39  ? 439  LEU A CD1 1 
ATOM   3561 C  CD2 . LEU A 1 439 ? -4.753  -21.972 10.349  1.00 30.68  ? 439  LEU A CD2 1 
ATOM   3562 N  N   . LYS A 1 440 ? -3.457  -19.765 14.726  1.00 32.01  ? 440  LYS A N   1 
ATOM   3563 C  CA  . LYS A 1 440 ? -2.882  -18.954 15.788  1.00 31.75  ? 440  LYS A CA  1 
ATOM   3564 C  C   . LYS A 1 440 ? -1.467  -19.440 16.051  1.00 32.61  ? 440  LYS A C   1 
ATOM   3565 O  O   . LYS A 1 440 ? -1.234  -20.651 15.974  1.00 36.01  ? 440  LYS A O   1 
ATOM   3566 C  CB  . LYS A 1 440 ? -3.734  -19.061 17.066  1.00 37.72  ? 440  LYS A CB  1 
ATOM   3567 C  CG  . LYS A 1 440 ? -3.472  -17.997 18.104  1.00 39.48  ? 440  LYS A CG  1 
ATOM   3568 C  CD  . LYS A 1 440 ? -4.363  -18.198 19.342  1.00 38.11  ? 440  LYS A CD  1 
ATOM   3569 C  CE  . LYS A 1 440 ? -5.814  -18.504 18.990  1.00 40.29  ? 440  LYS A CE  1 
ATOM   3570 N  NZ  . LYS A 1 440 ? -6.673  -18.337 20.218  1.00 39.67  ? 440  LYS A NZ  1 
ATOM   3571 N  N   . PRO A 1 441 ? -0.510  -18.555 16.347  1.00 34.11  ? 441  PRO A N   1 
ATOM   3572 C  CA  . PRO A 1 441 ? 0.807   -19.025 16.793  1.00 35.16  ? 441  PRO A CA  1 
ATOM   3573 C  C   . PRO A 1 441 ? 0.648   -19.868 18.051  1.00 38.01  ? 441  PRO A C   1 
ATOM   3574 O  O   . PRO A 1 441 ? -0.254  -19.643 18.860  1.00 36.04  ? 441  PRO A O   1 
ATOM   3575 C  CB  . PRO A 1 441 ? 1.580   -17.727 17.081  1.00 35.12  ? 441  PRO A CB  1 
ATOM   3576 C  CG  . PRO A 1 441 ? 0.861   -16.670 16.367  1.00 35.94  ? 441  PRO A CG  1 
ATOM   3577 C  CD  . PRO A 1 441 ? -0.586  -17.087 16.327  1.00 31.50  ? 441  PRO A CD  1 
ATOM   3578 N  N   . GLU A 1 442 ? 1.499   -20.881 18.186  1.00 34.34  ? 442  GLU A N   1 
ATOM   3579 C  CA  . GLU A 1 442 ? 1.549   -21.676 19.403  1.00 40.13  ? 442  GLU A CA  1 
ATOM   3580 C  C   . GLU A 1 442 ? 2.933   -21.539 20.011  1.00 40.82  ? 442  GLU A C   1 
ATOM   3581 O  O   . GLU A 1 442 ? 3.938   -21.610 19.297  1.00 37.48  ? 442  GLU A O   1 
ATOM   3582 C  CB  . GLU A 1 442 ? 1.232   -23.153 19.152  1.00 40.78  ? 442  GLU A CB  1 
ATOM   3583 C  CG  . GLU A 1 442 ? 1.399   -23.990 20.422  1.00 45.57  ? 442  GLU A CG  1 
ATOM   3584 C  CD  . GLU A 1 442 ? 0.882   -25.417 20.316  1.00 48.91  ? 442  GLU A CD  1 
ATOM   3585 O  OE1 . GLU A 1 442 ? 0.881   -25.999 19.209  1.00 45.26  ? 442  GLU A OE1 1 
ATOM   3586 O  OE2 . GLU A 1 442 ? 0.463   -25.960 21.364  1.00 53.80  ? 442  GLU A OE2 1 
ATOM   3587 N  N   . GLY A 1 443 ? 2.976   -21.330 21.326  1.00 35.84  ? 443  GLY A N   1 
ATOM   3588 C  CA  . GLY A 1 443 ? 4.242   -21.249 22.031  1.00 38.40  ? 443  GLY A CA  1 
ATOM   3589 C  C   . GLY A 1 443 ? 4.990   -19.957 21.825  1.00 34.48  ? 443  GLY A C   1 
ATOM   3590 O  O   . GLY A 1 443 ? 6.166   -19.874 22.188  1.00 37.37  ? 443  GLY A O   1 
ATOM   3591 N  N   . PHE A 1 444 ? 4.349   -18.947 21.242  1.00 36.70  ? 444  PHE A N   1 
ATOM   3592 C  CA  . PHE A 1 444 ? 4.985   -17.650 21.037  1.00 35.33  ? 444  PHE A CA  1 
ATOM   3593 C  C   . PHE A 1 444 ? 5.083   -16.923 22.369  1.00 37.22  ? 444  PHE A C   1 
ATOM   3594 O  O   . PHE A 1 444 ? 4.066   -16.654 23.018  1.00 33.94  ? 444  PHE A O   1 
ATOM   3595 C  CB  . PHE A 1 444 ? 4.182   -16.840 20.010  1.00 34.35  ? 444  PHE A CB  1 
ATOM   3596 C  CG  . PHE A 1 444 ? 4.689   -15.437 19.769  1.00 37.86  ? 444  PHE A CG  1 
ATOM   3597 C  CD1 . PHE A 1 444 ? 6.042   -15.136 19.805  1.00 34.78  ? 444  PHE A CD1 1 
ATOM   3598 C  CD2 . PHE A 1 444 ? 3.798   -14.416 19.453  1.00 33.80  ? 444  PHE A CD2 1 
ATOM   3599 C  CE1 . PHE A 1 444 ? 6.492   -13.835 19.570  1.00 35.38  ? 444  PHE A CE1 1 
ATOM   3600 C  CE2 . PHE A 1 444 ? 4.240   -13.111 19.209  1.00 34.43  ? 444  PHE A CE2 1 
ATOM   3601 C  CZ  . PHE A 1 444 ? 5.589   -12.819 19.270  1.00 35.56  ? 444  PHE A CZ  1 
ATOM   3602 N  N   . VAL A 1 445 ? 6.314   -16.628 22.792  1.00 33.09  ? 445  VAL A N   1 
ATOM   3603 C  CA  . VAL A 1 445 ? 6.571   -15.915 24.030  1.00 35.19  ? 445  VAL A CA  1 
ATOM   3604 C  C   . VAL A 1 445 ? 7.500   -14.746 23.729  1.00 33.10  ? 445  VAL A C   1 
ATOM   3605 O  O   . VAL A 1 445 ? 8.309   -14.796 22.797  1.00 36.33  ? 445  VAL A O   1 
ATOM   3606 C  CB  . VAL A 1 445 ? 7.183   -16.849 25.096  1.00 34.35  ? 445  VAL A CB  1 
ATOM   3607 C  CG1 . VAL A 1 445 ? 6.221   -17.985 25.402  1.00 33.92  ? 445  VAL A CG1 1 
ATOM   3608 C  CG2 . VAL A 1 445 ? 8.525   -17.395 24.618  1.00 36.61  ? 445  VAL A CG2 1 
ATOM   3609 N  N   . VAL A 1 446 ? 7.362   -13.679 24.510  1.00 34.45  ? 446  VAL A N   1 
ATOM   3610 C  CA  . VAL A 1 446 ? 8.237   -12.512 24.434  1.00 35.73  ? 446  VAL A CA  1 
ATOM   3611 C  C   . VAL A 1 446 ? 8.435   -11.970 25.846  1.00 36.53  ? 446  VAL A C   1 
ATOM   3612 O  O   . VAL A 1 446 ? 7.742   -12.358 26.788  1.00 35.07  ? 446  VAL A O   1 
ATOM   3613 C  CB  . VAL A 1 446 ? 7.668   -11.401 23.527  1.00 38.17  ? 446  VAL A CB  1 
ATOM   3614 C  CG1 . VAL A 1 446 ? 7.394   -11.932 22.112  1.00 35.67  ? 446  VAL A CG1 1 
ATOM   3615 C  CG2 . VAL A 1 446 ? 6.405   -10.799 24.158  1.00 35.21  ? 446  VAL A CG2 1 
ATOM   3616 N  N   . LYS A 1 447 ? 9.390   -11.051 25.978  1.00 37.77  ? 447  LYS A N   1 
ATOM   3617 C  CA  . LYS A 1 447 ? 9.569   -10.268 27.187  1.00 36.25  ? 447  LYS A CA  1 
ATOM   3618 C  C   . LYS A 1 447 ? 9.215   -8.819  26.896  1.00 40.52  ? 447  LYS A C   1 
ATOM   3619 O  O   . LYS A 1 447 ? 9.561   -8.283  25.840  1.00 41.52  ? 447  LYS A O   1 
ATOM   3620 C  CB  . LYS A 1 447 ? 11.008  -10.345 27.711  1.00 40.14  ? 447  LYS A CB  1 
ATOM   3621 C  CG  . LYS A 1 447 ? 11.322  -11.634 28.439  1.00 41.67  ? 447  LYS A CG  1 
ATOM   3622 C  CD  . LYS A 1 447 ? 12.805  -11.703 28.795  1.00 48.09  ? 447  LYS A CD  1 
ATOM   3623 C  CE  . LYS A 1 447 ? 13.030  -12.455 30.080  1.00 54.73  ? 447  LYS A CE  1 
ATOM   3624 N  NZ  . LYS A 1 447 ? 13.287  -13.895 29.785  1.00 60.24  ? 447  LYS A NZ  1 
ATOM   3625 N  N   . ALA A 1 448 ? 8.513   -8.192  27.823  1.00 37.17  ? 448  ALA A N   1 
ATOM   3626 C  CA  . ALA A 1 448 ? 8.179   -6.786  27.693  1.00 36.76  ? 448  ALA A CA  1 
ATOM   3627 C  C   . ALA A 1 448 ? 9.039   -5.997  28.665  1.00 42.79  ? 448  ALA A C   1 
ATOM   3628 O  O   . ALA A 1 448 ? 9.298   -6.447  29.788  1.00 48.61  ? 448  ALA A O   1 
ATOM   3629 C  CB  . ALA A 1 448 ? 6.684   -6.542  27.939  1.00 38.14  ? 448  ALA A CB  1 
ATOM   3630 N  N   . LYS A 1 449 ? 9.523   -4.850  28.213  1.00 39.91  ? 449  LYS A N   1 
ATOM   3631 C  CA  . LYS A 1 449 ? 10.229  -3.911  29.071  1.00 42.51  ? 449  LYS A CA  1 
ATOM   3632 C  C   . LYS A 1 449 ? 9.360   -2.671  29.196  1.00 41.70  ? 449  LYS A C   1 
ATOM   3633 O  O   . LYS A 1 449 ? 9.085   -2.003  28.196  1.00 40.82  ? 449  LYS A O   1 
ATOM   3634 C  CB  . LYS A 1 449 ? 11.607  -3.569  28.499  1.00 47.71  ? 449  LYS A CB  1 
ATOM   3635 C  CG  . LYS A 1 449 ? 12.610  -3.108  29.546  1.00 55.67  ? 449  LYS A CG  1 
ATOM   3636 C  CD  . LYS A 1 449 ? 13.334  -4.296  30.179  1.00 61.34  ? 449  LYS A CD  1 
ATOM   3637 C  CE  . LYS A 1 449 ? 14.502  -4.780  29.323  1.00 67.84  ? 449  LYS A CE  1 
ATOM   3638 N  NZ  . LYS A 1 449 ? 15.758  -3.985  29.542  1.00 71.53  ? 449  LYS A NZ  1 
ATOM   3639 N  N   . SER A 1 450 ? 8.911   -2.377  30.410  1.00 40.60  ? 450  SER A N   1 
ATOM   3640 C  CA  . SER A 1 450 ? 7.985   -1.273  30.598  1.00 40.26  ? 450  SER A CA  1 
ATOM   3641 C  C   . SER A 1 450 ? 8.651   0.061   30.288  1.00 41.87  ? 450  SER A C   1 
ATOM   3642 O  O   . SER A 1 450 ? 9.779   0.321   30.704  1.00 42.85  ? 450  SER A O   1 
ATOM   3643 C  CB  . SER A 1 450 ? 7.445   -1.257  32.028  1.00 39.74  ? 450  SER A CB  1 
ATOM   3644 O  OG  . SER A 1 450 ? 6.600   -0.127  32.208  1.00 43.21  ? 450  SER A OG  1 
ATOM   3645 N  N   . LYS A 1 451 ? 7.938   0.908   29.551  1.00 39.89  ? 451  LYS A N   1 
ATOM   3646 C  CA  . LYS A 1 451 ? 8.325   2.303   29.390  1.00 42.85  ? 451  LYS A CA  1 
ATOM   3647 C  C   . LYS A 1 451 ? 7.931   3.151   30.590  1.00 45.19  ? 451  LYS A C   1 
ATOM   3648 O  O   . LYS A 1 451 ? 8.229   4.350   30.609  1.00 45.57  ? 451  LYS A O   1 
ATOM   3649 C  CB  . LYS A 1 451 ? 7.722   2.867   28.093  1.00 42.65  ? 451  LYS A CB  1 
ATOM   3650 C  CG  . LYS A 1 451 ? 8.325   2.220   26.842  1.00 44.89  ? 451  LYS A CG  1 
ATOM   3651 C  CD  . LYS A 1 451 ? 7.781   2.822   25.544  1.00 44.40  ? 451  LYS A CD  1 
ATOM   3652 C  CE  . LYS A 1 451 ? 8.407   2.208   24.311  1.00 45.65  ? 451  LYS A CE  1 
ATOM   3653 N  NZ  . LYS A 1 451 ? 9.745   2.765   24.010  1.00 55.84  ? 451  LYS A NZ  1 
ATOM   3654 N  N   . LYS A 1 452 ? 7.282   2.548   31.587  1.00 40.47  ? 452  LYS A N   1 
ATOM   3655 C  CA  . LYS A 1 452 ? 6.918   3.211   32.837  1.00 45.06  ? 452  LYS A CA  1 
ATOM   3656 C  C   . LYS A 1 452 ? 6.063   4.455   32.593  1.00 50.25  ? 452  LYS A C   1 
ATOM   3657 O  O   . LYS A 1 452 ? 6.278   5.516   33.183  1.00 48.19  ? 452  LYS A O   1 
ATOM   3658 C  CB  . LYS A 1 452 ? 8.167   3.548   33.662  1.00 45.65  ? 452  LYS A CB  1 
ATOM   3659 C  CG  . LYS A 1 452 ? 8.757   2.346   34.400  1.00 53.18  ? 452  LYS A CG  1 
ATOM   3660 C  CD  . LYS A 1 452 ? 10.208  2.586   34.818  1.00 60.51  ? 452  LYS A CD  1 
ATOM   3661 C  CE  . LYS A 1 452 ? 11.003  1.282   34.893  1.00 62.44  ? 452  LYS A CE  1 
ATOM   3662 N  NZ  . LYS A 1 452 ? 11.107  0.750   36.282  1.00 70.47  ? 452  LYS A NZ  1 
ATOM   3663 N  N   . ILE A 1 453 ? 5.050   4.305   31.750  1.00 42.28  ? 453  ILE A N   1 
ATOM   3664 C  CA  . ILE A 1 453 ? 4.135   5.389   31.406  1.00 43.26  ? 453  ILE A CA  1 
ATOM   3665 C  C   . ILE A 1 453 ? 2.818   5.153   32.137  1.00 47.99  ? 453  ILE A C   1 
ATOM   3666 O  O   . ILE A 1 453 ? 2.167   4.123   31.909  1.00 44.03  ? 453  ILE A O   1 
ATOM   3667 C  CB  . ILE A 1 453 ? 3.918   5.487   29.891  1.00 44.23  ? 453  ILE A CB  1 
ATOM   3668 C  CG1 . ILE A 1 453 ? 5.249   5.814   29.211  1.00 45.63  ? 453  ILE A CG1 1 
ATOM   3669 C  CG2 . ILE A 1 453 ? 2.868   6.528   29.593  1.00 43.46  ? 453  ILE A CG2 1 
ATOM   3670 C  CD1 . ILE A 1 453 ? 5.204   5.722   27.715  1.00 42.89  ? 453  ILE A CD1 1 
ATOM   3671 N  N   . PRO A 1 454 ? 2.401   6.063   33.022  1.00 50.08  ? 454  PRO A N   1 
ATOM   3672 C  CA  . PRO A 1 454 ? 1.232   5.803   33.871  1.00 52.61  ? 454  PRO A CA  1 
ATOM   3673 C  C   . PRO A 1 454 ? -0.048  5.607   33.075  1.00 50.32  ? 454  PRO A C   1 
ATOM   3674 O  O   . PRO A 1 454 ? -0.277  6.248   32.044  1.00 50.20  ? 454  PRO A O   1 
ATOM   3675 C  CB  . PRO A 1 454 ? 1.130   7.073   34.728  1.00 51.66  ? 454  PRO A CB  1 
ATOM   3676 C  CG  . PRO A 1 454 ? 2.470   7.798   34.565  1.00 55.19  ? 454  PRO A CG  1 
ATOM   3677 C  CD  . PRO A 1 454 ? 3.359   6.933   33.718  1.00 50.48  ? 454  PRO A CD  1 
ATOM   3678 N  N   . LEU A 1 455 ? -0.916  4.742   33.600  1.00 47.64  ? 455  LEU A N   1 
ATOM   3679 C  CA  . LEU A 1 455 ? -2.271  4.614   33.077  1.00 49.82  ? 455  LEU A CA  1 
ATOM   3680 C  C   . LEU A 1 455 ? -3.244  5.550   33.800  1.00 56.27  ? 455  LEU A C   1 
ATOM   3681 O  O   . LEU A 1 455 ? -2.870  6.300   34.710  1.00 59.08  ? 455  LEU A O   1 
ATOM   3682 C  CB  . LEU A 1 455 ? -2.771  3.173   33.189  1.00 46.41  ? 455  LEU A CB  1 
ATOM   3683 C  CG  . LEU A 1 455 ? -2.083  2.154   32.290  1.00 42.73  ? 455  LEU A CG  1 
ATOM   3684 C  CD1 . LEU A 1 455 ? -2.364  0.755   32.797  1.00 44.72  ? 455  LEU A CD1 1 
ATOM   3685 C  CD2 . LEU A 1 455 ? -2.546  2.326   30.860  1.00 42.54  ? 455  LEU A CD2 1 
ATOM   3686 O  OXT . LEU A 1 455 ? -4.435  5.571   33.481  1.00 54.03  ? 455  LEU A OXT 1 
ATOM   3687 N  N   . THR B 1 1   ? -1.420  -25.542 100.062 1.00 73.76  ? 1    THR B N   1 
ATOM   3688 C  CA  . THR B 1 1   ? -0.621  -24.557 99.340  1.00 74.38  ? 1    THR B CA  1 
ATOM   3689 C  C   . THR B 1 1   ? -0.250  -25.068 97.943  1.00 67.75  ? 1    THR B C   1 
ATOM   3690 O  O   . THR B 1 1   ? -0.771  -24.575 96.934  1.00 62.49  ? 1    THR B O   1 
ATOM   3691 C  CB  . THR B 1 1   ? 0.659   -24.186 100.131 1.00 77.99  ? 1    THR B CB  1 
ATOM   3692 O  OG1 . THR B 1 1   ? 1.532   -23.398 99.308  1.00 73.52  ? 1    THR B OG1 1 
ATOM   3693 C  CG2 . THR B 1 1   ? 1.384   -25.441 100.626 1.00 72.45  ? 1    THR B CG2 1 
ATOM   3694 N  N   . ILE B 1 2   ? 0.642   -26.057 97.891  1.00 69.14  ? 2    ILE B N   1 
ATOM   3695 C  CA  . ILE B 1 2   ? 0.988   -26.713 96.633  1.00 64.96  ? 2    ILE B CA  1 
ATOM   3696 C  C   . ILE B 1 2   ? -0.210  -27.535 96.169  1.00 66.03  ? 2    ILE B C   1 
ATOM   3697 O  O   . ILE B 1 2   ? -0.670  -28.439 96.877  1.00 67.02  ? 2    ILE B O   1 
ATOM   3698 C  CB  . ILE B 1 2   ? 2.236   -27.590 96.801  1.00 64.17  ? 2    ILE B CB  1 
ATOM   3699 C  CG1 . ILE B 1 2   ? 3.398   -26.770 97.373  1.00 65.50  ? 2    ILE B CG1 1 
ATOM   3700 C  CG2 . ILE B 1 2   ? 2.618   -28.247 95.476  1.00 61.35  ? 2    ILE B CG2 1 
ATOM   3701 C  CD1 . ILE B 1 2   ? 3.747   -25.527 96.572  1.00 64.27  ? 2    ILE B CD1 1 
ATOM   3702 N  N   . LYS B 1 3   ? -0.731  -27.216 94.984  1.00 61.16  ? 3    LYS B N   1 
ATOM   3703 C  CA  . LYS B 1 3   ? -1.903  -27.886 94.439  1.00 61.27  ? 3    LYS B CA  1 
ATOM   3704 C  C   . LYS B 1 3   ? -1.485  -28.912 93.392  1.00 58.47  ? 3    LYS B C   1 
ATOM   3705 O  O   . LYS B 1 3   ? -0.479  -28.747 92.695  1.00 58.36  ? 3    LYS B O   1 
ATOM   3706 C  CB  . LYS B 1 3   ? -2.884  -26.887 93.807  1.00 57.58  ? 3    LYS B CB  1 
ATOM   3707 C  CG  . LYS B 1 3   ? -3.143  -25.628 94.632  1.00 60.33  ? 3    LYS B CG  1 
ATOM   3708 C  CD  . LYS B 1 3   ? -4.634  -25.325 94.788  1.00 63.70  ? 3    LYS B CD  1 
ATOM   3709 C  CE  . LYS B 1 3   ? -5.353  -25.148 93.455  1.00 64.80  ? 3    LYS B CE  1 
ATOM   3710 N  NZ  . LYS B 1 3   ? -6.775  -24.759 93.684  1.00 64.41  ? 3    LYS B NZ  1 
ATOM   3711 N  N   . GLU B 1 4   ? -2.277  -29.971 93.279  1.00 57.56  ? 4    GLU B N   1 
ATOM   3712 C  CA  . GLU B 1 4   ? -2.075  -30.962 92.236  1.00 59.00  ? 4    GLU B CA  1 
ATOM   3713 C  C   . GLU B 1 4   ? -2.859  -30.537 90.995  1.00 52.39  ? 4    GLU B C   1 
ATOM   3714 O  O   . GLU B 1 4   ? -4.030  -30.164 91.085  1.00 51.04  ? 4    GLU B O   1 
ATOM   3715 C  CB  . GLU B 1 4   ? -2.507  -32.347 92.722  1.00 64.12  ? 4    GLU B CB  1 
ATOM   3716 C  CG  . GLU B 1 4   ? -1.797  -33.499 92.023  1.00 66.35  ? 4    GLU B CG  1 
ATOM   3717 C  CD  . GLU B 1 4   ? -2.728  -34.657 91.699  1.00 75.97  ? 4    GLU B CD  1 
ATOM   3718 O  OE1 . GLU B 1 4   ? -3.946  -34.528 91.949  1.00 81.10  ? 4    GLU B OE1 1 
ATOM   3719 O  OE2 . GLU B 1 4   ? -2.242  -35.696 91.200  1.00 76.89  ? 4    GLU B OE2 1 
ATOM   3720 N  N   . MET B 1 5   ? -2.202  -30.561 89.867  1.00 50.91  ? 5    MET B N   1 
ATOM   3721 C  CA  . MET B 1 5   ? -2.680  -30.117 88.567  1.00 46.62  ? 5    MET B CA  1 
ATOM   3722 C  C   . MET B 1 5   ? -3.591  -31.167 87.932  1.00 39.96  ? 5    MET B C   1 
ATOM   3723 O  O   . MET B 1 5   ? -3.243  -32.349 87.906  1.00 43.96  ? 5    MET B O   1 
ATOM   3724 C  CB  . MET B 1 5   ? -1.486  -29.879 87.661  1.00 48.33  ? 5    MET B CB  1 
ATOM   3725 C  CG  . MET B 1 5   ? -1.709  -28.972 86.536  1.00 47.04  ? 5    MET B CG  1 
ATOM   3726 S  SD  . MET B 1 5   ? -0.137  -28.969 85.680  1.00 42.41  ? 5    MET B SD  1 
ATOM   3727 C  CE  . MET B 1 5   ? 0.901   -28.111 86.855  1.00 41.10  ? 5    MET B CE  1 
ATOM   3728 N  N   . PRO B 1 6   ? -4.749  -30.780 87.392  1.00 40.60  ? 6    PRO B N   1 
ATOM   3729 C  CA  . PRO B 1 6   ? -5.573  -31.760 86.677  1.00 38.56  ? 6    PRO B CA  1 
ATOM   3730 C  C   . PRO B 1 6   ? -4.934  -32.165 85.353  1.00 39.54  ? 6    PRO B C   1 
ATOM   3731 O  O   . PRO B 1 6   ? -4.021  -31.517 84.842  1.00 36.78  ? 6    PRO B O   1 
ATOM   3732 C  CB  . PRO B 1 6   ? -6.908  -31.037 86.457  1.00 37.78  ? 6    PRO B CB  1 
ATOM   3733 C  CG  . PRO B 1 6   ? -6.593  -29.603 86.592  1.00 39.32  ? 6    PRO B CG  1 
ATOM   3734 C  CD  . PRO B 1 6   ? -5.446  -29.494 87.557  1.00 39.78  ? 6    PRO B CD  1 
ATOM   3735 N  N   . GLN B 1 7   ? -5.425  -33.276 84.814  1.00 35.50  ? 7    GLN B N   1 
ATOM   3736 C  CA  . GLN B 1 7   ? -4.940  -33.850 83.580  1.00 35.58  ? 7    GLN B CA  1 
ATOM   3737 C  C   . GLN B 1 7   ? -6.121  -34.452 82.836  1.00 38.04  ? 7    GLN B C   1 
ATOM   3738 O  O   . GLN B 1 7   ? -6.997  -35.071 83.470  1.00 37.96  ? 7    GLN B O   1 
ATOM   3739 C  CB  . GLN B 1 7   ? -3.881  -34.923 83.852  1.00 37.96  ? 7    GLN B CB  1 
ATOM   3740 C  CG  . GLN B 1 7   ? -3.235  -35.518 82.609  1.00 37.73  ? 7    GLN B CG  1 
ATOM   3741 C  CD  . GLN B 1 7   ? -2.134  -36.501 82.966  1.00 43.75  ? 7    GLN B CD  1 
ATOM   3742 O  OE1 . GLN B 1 7   ? -1.900  -36.782 84.146  1.00 45.50  ? 7    GLN B OE1 1 
ATOM   3743 N  NE2 . GLN B 1 7   ? -1.448  -37.025 81.953  1.00 37.67  ? 7    GLN B NE2 1 
ATOM   3744 N  N   . PRO B 1 8   ? -6.181  -34.273 81.515  1.00 35.85  ? 8    PRO B N   1 
ATOM   3745 C  CA  . PRO B 1 8   ? -7.266  -34.865 80.722  1.00 34.88  ? 8    PRO B CA  1 
ATOM   3746 C  C   . PRO B 1 8   ? -7.072  -36.369 80.552  1.00 35.14  ? 8    PRO B C   1 
ATOM   3747 O  O   . PRO B 1 8   ? -6.076  -36.949 80.977  1.00 35.20  ? 8    PRO B O   1 
ATOM   3748 C  CB  . PRO B 1 8   ? -7.178  -34.124 79.382  1.00 34.94  ? 8    PRO B CB  1 
ATOM   3749 C  CG  . PRO B 1 8   ? -5.703  -33.737 79.267  1.00 33.21  ? 8    PRO B CG  1 
ATOM   3750 C  CD  . PRO B 1 8   ? -5.285  -33.423 80.701  1.00 35.66  ? 8    PRO B CD  1 
ATOM   3751 N  N   . LYS B 1 9   ? -8.066  -37.003 79.925  1.00 36.34  ? 9    LYS B N   1 
ATOM   3752 C  CA  . LYS B 1 9   ? -8.115  -38.461 79.858  1.00 31.24  ? 9    LYS B CA  1 
ATOM   3753 C  C   . LYS B 1 9   ? -6.899  -39.044 79.136  1.00 36.20  ? 9    LYS B C   1 
ATOM   3754 O  O   . LYS B 1 9   ? -6.320  -38.424 78.239  1.00 35.93  ? 9    LYS B O   1 
ATOM   3755 C  CB  . LYS B 1 9   ? -9.404  -38.915 79.161  1.00 35.44  ? 9    LYS B CB  1 
ATOM   3756 C  CG  . LYS B 1 9   ? -9.479  -38.570 77.673  1.00 31.36  ? 9    LYS B CG  1 
ATOM   3757 C  CD  . LYS B 1 9   ? -10.902 -38.810 77.161  1.00 35.36  ? 9    LYS B CD  1 
ATOM   3758 C  CE  . LYS B 1 9   ? -11.084 -38.310 75.740  1.00 41.48  ? 9    LYS B CE  1 
ATOM   3759 N  NZ  . LYS B 1 9   ? -12.480 -38.525 75.280  1.00 43.37  ? 9    LYS B NZ  1 
ATOM   3760 N  N   . THR B 1 10  ? -6.520  -40.263 79.533  1.00 36.17  ? 10   THR B N   1 
ATOM   3761 C  CA  . THR B 1 10  ? -5.316  -40.926 79.054  1.00 34.28  ? 10   THR B CA  1 
ATOM   3762 C  C   . THR B 1 10  ? -5.651  -42.193 78.279  1.00 35.53  ? 10   THR B C   1 
ATOM   3763 O  O   . THR B 1 10  ? -6.750  -42.742 78.372  1.00 33.50  ? 10   THR B O   1 
ATOM   3764 C  CB  . THR B 1 10  ? -4.380  -41.279 80.214  1.00 39.39  ? 10   THR B CB  1 
ATOM   3765 O  OG1 . THR B 1 10  ? -5.092  -42.091 81.163  1.00 34.16  ? 10   THR B OG1 1 
ATOM   3766 C  CG2 . THR B 1 10  ? -3.890  -40.027 80.897  1.00 37.54  ? 10   THR B CG2 1 
ATOM   3767 N  N   . PHE B 1 11  ? -4.647  -42.660 77.535  1.00 32.34  ? 11   PHE B N   1 
ATOM   3768 C  CA  . PHE B 1 11  ? -4.743  -43.765 76.591  1.00 35.15  ? 11   PHE B CA  1 
ATOM   3769 C  C   . PHE B 1 11  ? -3.587  -44.739 76.843  1.00 38.18  ? 11   PHE B C   1 
ATOM   3770 O  O   . PHE B 1 11  ? -2.786  -45.030 75.956  1.00 35.28  ? 11   PHE B O   1 
ATOM   3771 C  CB  . PHE B 1 11  ? -4.689  -43.257 75.145  1.00 34.54  ? 11   PHE B CB  1 
ATOM   3772 C  CG  . PHE B 1 11  ? -5.824  -42.337 74.772  1.00 33.49  ? 11   PHE B CG  1 
ATOM   3773 C  CD1 . PHE B 1 11  ? -5.851  -41.020 75.221  1.00 35.61  ? 11   PHE B CD1 1 
ATOM   3774 C  CD2 . PHE B 1 11  ? -6.859  -42.786 73.962  1.00 30.82  ? 11   PHE B CD2 1 
ATOM   3775 C  CE1 . PHE B 1 11  ? -6.898  -40.172 74.881  1.00 34.81  ? 11   PHE B CE1 1 
ATOM   3776 C  CE2 . PHE B 1 11  ? -7.912  -41.942 73.618  1.00 33.18  ? 11   PHE B CE2 1 
ATOM   3777 C  CZ  . PHE B 1 11  ? -7.928  -40.628 74.075  1.00 33.82  ? 11   PHE B CZ  1 
ATOM   3778 N  N   . GLY B 1 12  ? -3.489  -45.232 78.074  1.00 35.42  ? 12   GLY B N   1 
ATOM   3779 C  CA  . GLY B 1 12  ? -2.424  -46.180 78.377  1.00 37.03  ? 12   GLY B CA  1 
ATOM   3780 C  C   . GLY B 1 12  ? -1.058  -45.545 78.185  1.00 40.57  ? 12   GLY B C   1 
ATOM   3781 O  O   . GLY B 1 12  ? -0.821  -44.388 78.550  1.00 39.35  ? 12   GLY B O   1 
ATOM   3782 N  N   . GLU B 1 13  ? -0.144  -46.301 77.573  1.00 40.22  ? 13   GLU B N   1 
ATOM   3783 C  CA  . GLU B 1 13  ? 1.216   -45.795 77.417  1.00 41.63  ? 13   GLU B CA  1 
ATOM   3784 C  C   . GLU B 1 13  ? 1.307   -44.617 76.450  1.00 42.18  ? 13   GLU B C   1 
ATOM   3785 O  O   . GLU B 1 13  ? 2.336   -43.928 76.437  1.00 42.98  ? 13   GLU B O   1 
ATOM   3786 C  CB  . GLU B 1 13  ? 2.149   -46.922 76.978  1.00 45.99  ? 13   GLU B CB  1 
ATOM   3787 C  CG  . GLU B 1 13  ? 2.127   -48.116 77.924  1.00 53.30  ? 13   GLU B CG  1 
ATOM   3788 C  CD  . GLU B 1 13  ? 2.845   -47.850 79.240  1.00 62.31  ? 13   GLU B CD  1 
ATOM   3789 O  OE1 . GLU B 1 13  ? 3.485   -46.781 79.380  1.00 64.37  ? 13   GLU B OE1 1 
ATOM   3790 O  OE2 . GLU B 1 13  ? 2.780   -48.720 80.138  1.00 68.04  ? 13   GLU B OE2 1 
ATOM   3791 N  N   . LEU B 1 14  ? 0.269   -44.357 75.651  1.00 38.72  ? 14   LEU B N   1 
ATOM   3792 C  CA  . LEU B 1 14  ? 0.271   -43.159 74.818  1.00 37.59  ? 14   LEU B CA  1 
ATOM   3793 C  C   . LEU B 1 14  ? -0.088  -41.898 75.601  1.00 38.91  ? 14   LEU B C   1 
ATOM   3794 O  O   . LEU B 1 14  ? 0.014   -40.792 75.050  1.00 38.74  ? 14   LEU B O   1 
ATOM   3795 C  CB  . LEU B 1 14  ? -0.672  -43.337 73.627  1.00 37.13  ? 14   LEU B CB  1 
ATOM   3796 C  CG  . LEU B 1 14  ? -0.256  -44.408 72.609  1.00 42.54  ? 14   LEU B CG  1 
ATOM   3797 C  CD1 . LEU B 1 14  ? -1.292  -44.592 71.506  1.00 42.91  ? 14   LEU B CD1 1 
ATOM   3798 C  CD2 . LEU B 1 14  ? 1.122   -44.096 72.030  1.00 43.68  ? 14   LEU B CD2 1 
ATOM   3799 N  N   . LYS B 1 15  ? -0.475  -42.038 76.868  1.00 34.08  ? 15   LYS B N   1 
ATOM   3800 C  CA  . LYS B 1 15  ? -0.724  -40.918 77.788  1.00 36.72  ? 15   LYS B CA  1 
ATOM   3801 C  C   . LYS B 1 15  ? -1.786  -40.018 77.154  1.00 35.36  ? 15   LYS B C   1 
ATOM   3802 O  O   . LYS B 1 15  ? -2.858  -40.530 76.792  1.00 34.89  ? 15   LYS B O   1 
ATOM   3803 C  CB  . LYS B 1 15  ? 0.613   -40.278 78.129  1.00 40.06  ? 15   LYS B CB  1 
ATOM   3804 C  CG  . LYS B 1 15  ? 1.500   -41.265 78.897  1.00 41.59  ? 15   LYS B CG  1 
ATOM   3805 C  CD  . LYS B 1 15  ? 2.906   -40.747 79.116  1.00 46.86  ? 15   LYS B CD  1 
ATOM   3806 C  CE  . LYS B 1 15  ? 3.667   -41.649 80.072  1.00 51.51  ? 15   LYS B CE  1 
ATOM   3807 N  NZ  . LYS B 1 15  ? 4.976   -41.060 80.461  1.00 55.67  ? 15   LYS B NZ  1 
ATOM   3808 N  N   . ASN B 1 16  ? -1.566  -38.707 77.013  1.00 33.30  ? 16   ASN B N   1 
ATOM   3809 C  CA  . ASN B 1 16  ? -2.582  -37.843 76.408  1.00 33.10  ? 16   ASN B CA  1 
ATOM   3810 C  C   . ASN B 1 16  ? -2.450  -37.690 74.896  1.00 36.21  ? 16   ASN B C   1 
ATOM   3811 O  O   . ASN B 1 16  ? -3.270  -36.992 74.294  1.00 36.07  ? 16   ASN B O   1 
ATOM   3812 C  CB  . ASN B 1 16  ? -2.550  -36.446 77.041  1.00 33.64  ? 16   ASN B CB  1 
ATOM   3813 C  CG  . ASN B 1 16  ? -2.862  -36.480 78.510  1.00 37.59  ? 16   ASN B CG  1 
ATOM   3814 O  OD1 . ASN B 1 16  ? -2.052  -36.059 79.330  1.00 35.58  ? 16   ASN B OD1 1 
ATOM   3815 N  ND2 . ASN B 1 16  ? -4.043  -37.004 78.860  1.00 34.21  ? 16   ASN B ND2 1 
ATOM   3816 N  N   . LEU B 1 17  ? -1.455  -38.309 74.266  1.00 35.35  ? 17   LEU B N   1 
ATOM   3817 C  CA  . LEU B 1 17  ? -1.163  -37.970 72.874  1.00 35.62  ? 17   LEU B CA  1 
ATOM   3818 C  C   . LEU B 1 17  ? -2.358  -38.151 71.944  1.00 34.72  ? 17   LEU B C   1 
ATOM   3819 O  O   . LEU B 1 17  ? -2.544  -37.307 71.053  1.00 36.09  ? 17   LEU B O   1 
ATOM   3820 C  CB  . LEU B 1 17  ? 0.032   -38.792 72.378  1.00 35.53  ? 17   LEU B CB  1 
ATOM   3821 C  CG  . LEU B 1 17  ? 0.531   -38.382 70.986  1.00 38.19  ? 17   LEU B CG  1 
ATOM   3822 C  CD1 . LEU B 1 17  ? 1.068   -36.949 71.022  1.00 39.08  ? 17   LEU B CD1 1 
ATOM   3823 C  CD2 . LEU B 1 17  ? 1.595   -39.349 70.495  1.00 43.84  ? 17   LEU B CD2 1 
ATOM   3824 N  N   . PRO B 1 18  ? -3.175  -39.195 72.062  1.00 35.10  ? 18   PRO B N   1 
ATOM   3825 C  CA  . PRO B 1 18  ? -4.306  -39.335 71.134  1.00 33.80  ? 18   PRO B CA  1 
ATOM   3826 C  C   . PRO B 1 18  ? -5.315  -38.197 71.205  1.00 34.54  ? 18   PRO B C   1 
ATOM   3827 O  O   . PRO B 1 18  ? -6.154  -38.091 70.305  1.00 34.91  ? 18   PRO B O   1 
ATOM   3828 C  CB  . PRO B 1 18  ? -4.930  -40.674 71.548  1.00 36.59  ? 18   PRO B CB  1 
ATOM   3829 C  CG  . PRO B 1 18  ? -3.769  -41.436 72.156  1.00 37.77  ? 18   PRO B CG  1 
ATOM   3830 C  CD  . PRO B 1 18  ? -3.025  -40.379 72.926  1.00 35.98  ? 18   PRO B CD  1 
ATOM   3831 N  N   . LEU B 1 19  ? -5.285  -37.361 72.244  1.00 34.49  ? 19   LEU B N   1 
ATOM   3832 C  CA  . LEU B 1 19  ? -6.155  -36.189 72.250  1.00 35.37  ? 19   LEU B CA  1 
ATOM   3833 C  C   . LEU B 1 19  ? -5.829  -35.246 71.101  1.00 36.22  ? 19   LEU B C   1 
ATOM   3834 O  O   . LEU B 1 19  ? -6.691  -34.458 70.699  1.00 34.96  ? 19   LEU B O   1 
ATOM   3835 C  CB  . LEU B 1 19  ? -6.043  -35.447 73.583  1.00 32.59  ? 19   LEU B CB  1 
ATOM   3836 C  CG  . LEU B 1 19  ? -6.530  -36.267 74.773  1.00 30.28  ? 19   LEU B CG  1 
ATOM   3837 C  CD1 . LEU B 1 19  ? -6.322  -35.499 76.055  1.00 31.45  ? 19   LEU B CD1 1 
ATOM   3838 C  CD2 . LEU B 1 19  ? -7.995  -36.636 74.597  1.00 35.99  ? 19   LEU B CD2 1 
ATOM   3839 N  N   . LEU B 1 20  ? -4.613  -35.311 70.559  1.00 34.48  ? 20   LEU B N   1 
ATOM   3840 C  CA  . LEU B 1 20  ? -4.240  -34.495 69.406  1.00 35.55  ? 20   LEU B CA  1 
ATOM   3841 C  C   . LEU B 1 20  ? -4.531  -35.175 68.079  1.00 35.56  ? 20   LEU B C   1 
ATOM   3842 O  O   . LEU B 1 20  ? -4.241  -34.602 67.023  1.00 35.56  ? 20   LEU B O   1 
ATOM   3843 C  CB  . LEU B 1 20  ? -2.752  -34.140 69.471  1.00 33.19  ? 20   LEU B CB  1 
ATOM   3844 C  CG  . LEU B 1 20  ? -2.305  -33.402 70.732  1.00 33.53  ? 20   LEU B CG  1 
ATOM   3845 C  CD1 . LEU B 1 20  ? -0.819  -33.123 70.676  1.00 37.62  ? 20   LEU B CD1 1 
ATOM   3846 C  CD2 . LEU B 1 20  ? -3.098  -32.110 70.974  1.00 40.55  ? 20   LEU B CD2 1 
ATOM   3847 N  N   . ASN B 1 21  ? -5.079  -36.389 68.100  1.00 32.76  ? 21   ASN B N   1 
ATOM   3848 C  CA  . ASN B 1 21  ? -5.415  -37.094 66.867  1.00 34.24  ? 21   ASN B CA  1 
ATOM   3849 C  C   . ASN B 1 21  ? -6.770  -36.582 66.372  1.00 40.86  ? 21   ASN B C   1 
ATOM   3850 O  O   . ASN B 1 21  ? -7.811  -37.235 66.492  1.00 37.36  ? 21   ASN B O   1 
ATOM   3851 C  CB  . ASN B 1 21  ? -5.423  -38.603 67.082  1.00 37.32  ? 21   ASN B CB  1 
ATOM   3852 C  CG  . ASN B 1 21  ? -5.592  -39.374 65.772  1.00 46.92  ? 21   ASN B CG  1 
ATOM   3853 O  OD1 . ASN B 1 21  ? -5.637  -38.785 64.684  1.00 45.03  ? 21   ASN B OD1 1 
ATOM   3854 N  ND2 . ASN B 1 21  ? -5.687  -40.691 65.871  1.00 47.27  ? 21   ASN B ND2 1 
ATOM   3855 N  N   . THR B 1 22  ? -6.733  -35.362 65.838  1.00 35.46  ? 22   THR B N   1 
ATOM   3856 C  CA  . THR B 1 22  ? -7.908  -34.655 65.350  1.00 34.44  ? 22   THR B CA  1 
ATOM   3857 C  C   . THR B 1 22  ? -7.444  -33.578 64.379  1.00 36.03  ? 22   THR B C   1 
ATOM   3858 O  O   . THR B 1 22  ? -6.304  -33.117 64.441  1.00 37.48  ? 22   THR B O   1 
ATOM   3859 C  CB  . THR B 1 22  ? -8.728  -34.020 66.482  1.00 39.59  ? 22   THR B CB  1 
ATOM   3860 O  OG1 . THR B 1 22  ? -9.697  -33.134 65.906  1.00 41.86  ? 22   THR B OG1 1 
ATOM   3861 C  CG2 . THR B 1 22  ? -7.834  -33.209 67.454  1.00 35.48  ? 22   THR B CG2 1 
ATOM   3862 N  N   . ASP B 1 23  ? -8.344  -33.172 63.480  1.00 37.13  ? 23   ASP B N   1 
ATOM   3863 C  CA  . ASP B 1 23  ? -7.972  -32.091 62.578  1.00 38.97  ? 23   ASP B CA  1 
ATOM   3864 C  C   . ASP B 1 23  ? -8.058  -30.730 63.254  1.00 35.41  ? 23   ASP B C   1 
ATOM   3865 O  O   . ASP B 1 23  ? -7.666  -29.733 62.646  1.00 32.79  ? 23   ASP B O   1 
ATOM   3866 C  CB  . ASP B 1 23  ? -8.859  -32.074 61.323  1.00 41.57  ? 23   ASP B CB  1 
ATOM   3867 C  CG  . ASP B 1 23  ? -10.340 -32.083 61.642  1.00 45.86  ? 23   ASP B CG  1 
ATOM   3868 O  OD1 . ASP B 1 23  ? -11.128 -31.666 60.767  1.00 58.39  ? 23   ASP B OD1 1 
ATOM   3869 O  OD2 . ASP B 1 23  ? -10.726 -32.424 62.779  1.00 48.68  ? 23   ASP B OD2 1 
ATOM   3870 N  N   . LYS B 1 24  ? -8.572  -30.660 64.481  1.00 32.87  ? 24   LYS B N   1 
ATOM   3871 C  CA  . LYS B 1 24  ? -8.793  -29.388 65.175  1.00 32.56  ? 24   LYS B CA  1 
ATOM   3872 C  C   . LYS B 1 24  ? -8.223  -29.492 66.579  1.00 29.57  ? 24   LYS B C   1 
ATOM   3873 O  O   . LYS B 1 24  ? -8.954  -29.425 67.583  1.00 31.36  ? 24   LYS B O   1 
ATOM   3874 C  CB  . LYS B 1 24  ? -10.274 -29.015 65.185  1.00 34.63  ? 24   LYS B CB  1 
ATOM   3875 C  CG  . LYS B 1 24  ? -10.786 -28.754 63.773  1.00 35.55  ? 24   LYS B CG  1 
ATOM   3876 C  CD  . LYS B 1 24  ? -12.284 -28.509 63.756  1.00 39.01  ? 24   LYS B CD  1 
ATOM   3877 C  CE  . LYS B 1 24  ? -12.734 -28.153 62.343  1.00 34.76  ? 24   LYS B CE  1 
ATOM   3878 N  NZ  . LYS B 1 24  ? -14.173 -27.788 62.309  1.00 39.55  ? 24   LYS B NZ  1 
ATOM   3879 N  N   . PRO B 1 25  ? -6.896  -29.605 66.686  1.00 29.89  ? 25   PRO B N   1 
ATOM   3880 C  CA  . PRO B 1 25  ? -6.300  -29.863 68.005  1.00 31.26  ? 25   PRO B CA  1 
ATOM   3881 C  C   . PRO B 1 25  ? -6.352  -28.674 68.952  1.00 31.76  ? 25   PRO B C   1 
ATOM   3882 O  O   . PRO B 1 25  ? -6.561  -28.874 70.153  1.00 30.14  ? 25   PRO B O   1 
ATOM   3883 C  CB  . PRO B 1 25  ? -4.856  -30.270 67.660  1.00 29.45  ? 25   PRO B CB  1 
ATOM   3884 C  CG  . PRO B 1 25  ? -4.600  -29.668 66.289  1.00 31.43  ? 25   PRO B CG  1 
ATOM   3885 C  CD  . PRO B 1 25  ? -5.919  -29.716 65.585  1.00 32.55  ? 25   PRO B CD  1 
ATOM   3886 N  N   . VAL B 1 26  ? -6.152  -27.448 68.465  1.00 31.65  ? 26   VAL B N   1 
ATOM   3887 C  CA  . VAL B 1 26  ? -6.251  -26.299 69.362  1.00 33.06  ? 26   VAL B CA  1 
ATOM   3888 C  C   . VAL B 1 26  ? -7.661  -26.184 69.916  1.00 31.55  ? 26   VAL B C   1 
ATOM   3889 O  O   . VAL B 1 26  ? -7.857  -25.872 71.097  1.00 32.31  ? 26   VAL B O   1 
ATOM   3890 C  CB  . VAL B 1 26  ? -5.833  -25.004 68.638  1.00 32.08  ? 26   VAL B CB  1 
ATOM   3891 C  CG1 . VAL B 1 26  ? -6.172  -23.785 69.507  1.00 31.76  ? 26   VAL B CG1 1 
ATOM   3892 C  CG2 . VAL B 1 26  ? -4.330  -25.066 68.260  1.00 32.77  ? 26   VAL B CG2 1 
ATOM   3893 N  N   . GLN B 1 27  ? -8.667  -26.407 69.066  1.00 34.30  ? 27   GLN B N   1 
ATOM   3894 C  CA  . GLN B 1 27  ? -10.045 -26.332 69.540  1.00 33.97  ? 27   GLN B CA  1 
ATOM   3895 C  C   . GLN B 1 27  ? -10.348 -27.445 70.542  1.00 33.72  ? 27   GLN B C   1 
ATOM   3896 O  O   . GLN B 1 27  ? -11.075 -27.222 71.520  1.00 30.70  ? 27   GLN B O   1 
ATOM   3897 C  CB  . GLN B 1 27  ? -10.997 -26.364 68.349  1.00 33.98  ? 27   GLN B CB  1 
ATOM   3898 C  CG  . GLN B 1 27  ? -10.978 -25.041 67.568  1.00 35.69  ? 27   GLN B CG  1 
ATOM   3899 C  CD  . GLN B 1 27  ? -11.560 -25.156 66.171  1.00 32.79  ? 27   GLN B CD  1 
ATOM   3900 O  OE1 . GLN B 1 27  ? -12.762 -24.978 65.969  1.00 34.60  ? 27   GLN B OE1 1 
ATOM   3901 N  NE2 . GLN B 1 27  ? -10.702 -25.454 65.192  1.00 32.28  ? 27   GLN B NE2 1 
ATOM   3902 N  N   . ALA B 1 28  ? -9.758  -28.633 70.341  1.00 34.82  ? 28   ALA B N   1 
ATOM   3903 C  CA  . ALA B 1 28  ? -9.861  -29.696 71.340  1.00 35.02  ? 28   ALA B CA  1 
ATOM   3904 C  C   . ALA B 1 28  ? -9.264  -29.249 72.664  1.00 38.89  ? 28   ALA B C   1 
ATOM   3905 O  O   . ALA B 1 28  ? -9.848  -29.476 73.735  1.00 33.16  ? 28   ALA B O   1 
ATOM   3906 C  CB  . ALA B 1 28  ? -9.157  -30.963 70.842  1.00 34.05  ? 28   ALA B CB  1 
ATOM   3907 N  N   . LEU B 1 29  ? -8.079  -28.624 72.607  1.00 32.29  ? 29   LEU B N   1 
ATOM   3908 C  CA  . LEU B 1 29  ? -7.439  -28.163 73.830  1.00 33.08  ? 29   LEU B CA  1 
ATOM   3909 C  C   . LEU B 1 29  ? -8.235  -27.043 74.494  1.00 34.50  ? 29   LEU B C   1 
ATOM   3910 O  O   . LEU B 1 29  ? -8.237  -26.946 75.727  1.00 33.10  ? 29   LEU B O   1 
ATOM   3911 C  CB  . LEU B 1 29  ? -6.006  -27.710 73.537  1.00 32.39  ? 29   LEU B CB  1 
ATOM   3912 C  CG  . LEU B 1 29  ? -5.041  -28.823 73.137  1.00 31.54  ? 29   LEU B CG  1 
ATOM   3913 C  CD1 . LEU B 1 29  ? -3.816  -28.274 72.390  1.00 35.19  ? 29   LEU B CD1 1 
ATOM   3914 C  CD2 . LEU B 1 29  ? -4.610  -29.556 74.425  1.00 33.09  ? 29   LEU B CD2 1 
ATOM   3915 N  N   . MET B 1 30  ? -8.904  -26.187 73.712  1.00 31.32  ? 30   MET B N   1 
ATOM   3916 C  CA  . MET B 1 30  ? -9.768  -25.210 74.347  1.00 32.18  ? 30   MET B CA  1 
ATOM   3917 C  C   . MET B 1 30  ? -10.864 -25.894 75.148  1.00 34.48  ? 30   MET B C   1 
ATOM   3918 O  O   . MET B 1 30  ? -11.163 -25.481 76.273  1.00 33.23  ? 30   MET B O   1 
ATOM   3919 C  CB  . MET B 1 30  ? -10.388 -24.246 73.351  1.00 33.45  ? 30   MET B CB  1 
ATOM   3920 C  CG  . MET B 1 30  ? -9.472  -23.119 72.881  1.00 33.49  ? 30   MET B CG  1 
ATOM   3921 S  SD  . MET B 1 30  ? -9.886  -22.523 71.253  1.00 34.90  ? 30   MET B SD  1 
ATOM   3922 C  CE  . MET B 1 30  ? -11.113 -21.397 71.948  1.00 35.01  ? 30   MET B CE  1 
ATOM   3923 N  N   . LYS B 1 31  ? -11.492 -26.928 74.579  1.00 35.24  ? 31   LYS B N   1 
ATOM   3924 C  CA  . LYS B 1 31  ? -12.568 -27.608 75.308  1.00 36.29  ? 31   LYS B CA  1 
ATOM   3925 C  C   . LYS B 1 31  ? -12.039 -28.278 76.570  1.00 35.75  ? 31   LYS B C   1 
ATOM   3926 O  O   . LYS B 1 31  ? -12.706 -28.291 77.613  1.00 35.28  ? 31   LYS B O   1 
ATOM   3927 C  CB  . LYS B 1 31  ? -13.249 -28.629 74.399  1.00 34.55  ? 31   LYS B CB  1 
ATOM   3928 C  CG  . LYS B 1 31  ? -14.348 -28.010 73.544  1.00 48.06  ? 31   LYS B CG  1 
ATOM   3929 C  CD  . LYS B 1 31  ? -14.506 -28.744 72.222  1.00 54.76  ? 31   LYS B CD  1 
ATOM   3930 C  CE  . LYS B 1 31  ? -15.242 -27.884 71.187  1.00 51.40  ? 31   LYS B CE  1 
ATOM   3931 N  NZ  . LYS B 1 31  ? -14.869 -28.244 69.785  1.00 57.16  ? 31   LYS B NZ  1 
ATOM   3932 N  N   . ILE B 1 32  ? -10.833 -28.836 76.502  1.00 36.32  ? 32   ILE B N   1 
ATOM   3933 C  CA  . ILE B 1 32  ? -10.238 -29.416 77.701  1.00 32.81  ? 32   ILE B CA  1 
ATOM   3934 C  C   . ILE B 1 32  ? -10.031 -28.338 78.756  1.00 32.63  ? 32   ILE B C   1 
ATOM   3935 O  O   . ILE B 1 32  ? -10.336 -28.537 79.939  1.00 35.08  ? 32   ILE B O   1 
ATOM   3936 C  CB  . ILE B 1 32  ? -8.925  -30.136 77.353  1.00 33.68  ? 32   ILE B CB  1 
ATOM   3937 C  CG1 . ILE B 1 32  ? -9.217  -31.354 76.472  1.00 37.37  ? 32   ILE B CG1 1 
ATOM   3938 C  CG2 . ILE B 1 32  ? -8.193  -30.516 78.645  1.00 32.30  ? 32   ILE B CG2 1 
ATOM   3939 C  CD1 . ILE B 1 32  ? -8.026  -31.827 75.660  1.00 36.75  ? 32   ILE B CD1 1 
ATOM   3940 N  N   . ALA B 1 33  ? -9.538  -27.170 78.338  1.00 32.42  ? 33   ALA B N   1 
ATOM   3941 C  CA  . ALA B 1 33  ? -9.338  -26.058 79.260  1.00 33.75  ? 33   ALA B CA  1 
ATOM   3942 C  C   . ALA B 1 33  ? -10.655 -25.623 79.897  1.00 35.86  ? 33   ALA B C   1 
ATOM   3943 O  O   . ALA B 1 33  ? -10.709 -25.323 81.096  1.00 33.08  ? 33   ALA B O   1 
ATOM   3944 C  CB  . ALA B 1 33  ? -8.685  -24.889 78.519  1.00 34.06  ? 33   ALA B CB  1 
ATOM   3945 N  N   . ASP B 1 34  ? -11.727 -25.577 79.112  1.00 35.64  ? 34   ASP B N   1 
ATOM   3946 C  CA  . ASP B 1 34  ? -13.022 -25.217 79.685  1.00 37.32  ? 34   ASP B CA  1 
ATOM   3947 C  C   . ASP B 1 34  ? -13.422 -26.180 80.791  1.00 39.49  ? 34   ASP B C   1 
ATOM   3948 O  O   . ASP B 1 34  ? -14.031 -25.776 81.787  1.00 43.02  ? 34   ASP B O   1 
ATOM   3949 C  CB  . ASP B 1 34  ? -14.086 -25.187 78.595  1.00 39.45  ? 34   ASP B CB  1 
ATOM   3950 C  CG  . ASP B 1 34  ? -14.047 -23.914 77.795  1.00 43.07  ? 34   ASP B CG  1 
ATOM   3951 O  OD1 . ASP B 1 34  ? -13.445 -22.935 78.280  1.00 45.81  ? 34   ASP B OD1 1 
ATOM   3952 O  OD2 . ASP B 1 34  ? -14.616 -23.887 76.688  1.00 45.20  ? 34   ASP B OD2 1 
ATOM   3953 N  N   . GLU B 1 35  ? -13.095 -27.460 80.630  1.00 36.17  ? 35   GLU B N   1 
ATOM   3954 C  CA  . GLU B 1 35  ? -13.465 -28.471 81.612  1.00 35.03  ? 35   GLU B CA  1 
ATOM   3955 C  C   . GLU B 1 35  ? -12.526 -28.476 82.815  1.00 38.89  ? 35   GLU B C   1 
ATOM   3956 O  O   . GLU B 1 35  ? -12.972 -28.649 83.955  1.00 39.36  ? 35   GLU B O   1 
ATOM   3957 C  CB  . GLU B 1 35  ? -13.483 -29.848 80.936  1.00 40.21  ? 35   GLU B CB  1 
ATOM   3958 C  CG  . GLU B 1 35  ? -13.742 -30.994 81.878  1.00 50.53  ? 35   GLU B CG  1 
ATOM   3959 C  CD  . GLU B 1 35  ? -13.742 -32.346 81.174  1.00 59.71  ? 35   GLU B CD  1 
ATOM   3960 O  OE1 . GLU B 1 35  ? -13.731 -33.370 81.893  1.00 64.05  ? 35   GLU B OE1 1 
ATOM   3961 O  OE2 . GLU B 1 35  ? -13.758 -32.385 79.919  1.00 56.00  ? 35   GLU B OE2 1 
ATOM   3962 N  N   . LEU B 1 36  ? -11.227 -28.280 82.589  1.00 35.77  ? 36   LEU B N   1 
ATOM   3963 C  CA  . LEU B 1 36  ? -10.254 -28.472 83.650  1.00 33.94  ? 36   LEU B CA  1 
ATOM   3964 C  C   . LEU B 1 36  ? -9.811  -27.185 84.325  1.00 33.50  ? 36   LEU B C   1 
ATOM   3965 O  O   . LEU B 1 36  ? -9.353  -27.239 85.473  1.00 35.65  ? 36   LEU B O   1 
ATOM   3966 C  CB  . LEU B 1 36  ? -9.025  -29.205 83.104  1.00 35.51  ? 36   LEU B CB  1 
ATOM   3967 C  CG  . LEU B 1 36  ? -9.301  -30.622 82.607  1.00 33.74  ? 36   LEU B CG  1 
ATOM   3968 C  CD1 . LEU B 1 36  ? -7.986  -31.332 82.259  1.00 36.12  ? 36   LEU B CD1 1 
ATOM   3969 C  CD2 . LEU B 1 36  ? -10.077 -31.425 83.651  1.00 37.40  ? 36   LEU B CD2 1 
ATOM   3970 N  N   . GLY B 1 37  ? -9.938  -26.046 83.671  1.00 31.58  ? 37   GLY B N   1 
ATOM   3971 C  CA  . GLY B 1 37  ? -9.622  -24.774 84.292  1.00 34.32  ? 37   GLY B CA  1 
ATOM   3972 C  C   . GLY B 1 37  ? -8.312  -24.179 83.799  1.00 36.69  ? 37   GLY B C   1 
ATOM   3973 O  O   . GLY B 1 37  ? -7.837  -24.446 82.687  1.00 36.18  ? 37   GLY B O   1 
ATOM   3974 N  N   . GLU B 1 38  ? -7.710  -23.362 84.665  1.00 34.66  ? 38   GLU B N   1 
ATOM   3975 C  CA  . GLU B 1 38  ? -6.647  -22.450 84.261  1.00 37.75  ? 38   GLU B CA  1 
ATOM   3976 C  C   . GLU B 1 38  ? -5.325  -23.149 83.990  1.00 35.92  ? 38   GLU B C   1 
ATOM   3977 O  O   . GLU B 1 38  ? -4.434  -22.518 83.406  1.00 32.77  ? 38   GLU B O   1 
ATOM   3978 C  CB  . GLU B 1 38  ? -6.442  -21.375 85.336  1.00 37.25  ? 38   GLU B CB  1 
ATOM   3979 C  CG  . GLU B 1 38  ? -5.849  -21.924 86.631  1.00 37.37  ? 38   GLU B CG  1 
ATOM   3980 C  CD  . GLU B 1 38  ? -5.643  -20.858 87.703  1.00 41.40  ? 38   GLU B CD  1 
ATOM   3981 O  OE1 . GLU B 1 38  ? -5.559  -19.649 87.372  1.00 38.39  ? 38   GLU B OE1 1 
ATOM   3982 O  OE2 . GLU B 1 38  ? -5.571  -21.244 88.889  1.00 43.50  ? 38   GLU B OE2 1 
ATOM   3983 N  N   . ILE B 1 39  ? -5.171  -24.415 84.383  1.00 35.30  ? 39   ILE B N   1 
ATOM   3984 C  CA  . ILE B 1 39  ? -3.923  -25.142 84.147  1.00 34.20  ? 39   ILE B CA  1 
ATOM   3985 C  C   . ILE B 1 39  ? -4.221  -26.636 84.094  1.00 35.49  ? 39   ILE B C   1 
ATOM   3986 O  O   . ILE B 1 39  ? -4.978  -27.163 84.915  1.00 36.27  ? 39   ILE B O   1 
ATOM   3987 C  CB  . ILE B 1 39  ? -2.864  -24.817 85.227  1.00 33.23  ? 39   ILE B CB  1 
ATOM   3988 C  CG1 . ILE B 1 39  ? -1.528  -25.510 84.915  1.00 34.10  ? 39   ILE B CG1 1 
ATOM   3989 C  CG2 . ILE B 1 39  ? -3.355  -25.189 86.625  1.00 36.48  ? 39   ILE B CG2 1 
ATOM   3990 C  CD1 . ILE B 1 39  ? -0.345  -24.899 85.679  1.00 38.01  ? 39   ILE B CD1 1 
ATOM   3991 N  N   . PHE B 1 40  ? -3.630  -27.325 83.123  1.00 31.47  ? 40   PHE B N   1 
ATOM   3992 C  CA  . PHE B 1 40  ? -3.699  -28.777 83.140  1.00 33.44  ? 40   PHE B CA  1 
ATOM   3993 C  C   . PHE B 1 40  ? -2.397  -29.327 82.594  1.00 36.20  ? 40   PHE B C   1 
ATOM   3994 O  O   . PHE B 1 40  ? -1.729  -28.692 81.778  1.00 33.41  ? 40   PHE B O   1 
ATOM   3995 C  CB  . PHE B 1 40  ? -4.921  -29.344 82.379  1.00 33.81  ? 40   PHE B CB  1 
ATOM   3996 C  CG  . PHE B 1 40  ? -4.960  -29.025 80.902  1.00 34.50  ? 40   PHE B CG  1 
ATOM   3997 C  CD1 . PHE B 1 40  ? -4.341  -29.855 79.973  1.00 31.30  ? 40   PHE B CD1 1 
ATOM   3998 C  CD2 . PHE B 1 40  ? -5.690  -27.937 80.440  1.00 32.19  ? 40   PHE B CD2 1 
ATOM   3999 C  CE1 . PHE B 1 40  ? -4.395  -29.555 78.613  1.00 32.98  ? 40   PHE B CE1 1 
ATOM   4000 C  CE2 . PHE B 1 40  ? -5.767  -27.639 79.093  1.00 30.89  ? 40   PHE B CE2 1 
ATOM   4001 C  CZ  . PHE B 1 40  ? -5.115  -28.447 78.173  1.00 34.50  ? 40   PHE B CZ  1 
ATOM   4002 N  N   . LYS B 1 41  ? -2.020  -30.488 83.112  1.00 35.66  ? 41   LYS B N   1 
ATOM   4003 C  CA  . LYS B 1 41  ? -0.858  -31.206 82.619  1.00 35.80  ? 41   LYS B CA  1 
ATOM   4004 C  C   . LYS B 1 41  ? -1.229  -32.007 81.379  1.00 37.02  ? 41   LYS B C   1 
ATOM   4005 O  O   . LYS B 1 41  ? -2.339  -32.540 81.266  1.00 35.64  ? 41   LYS B O   1 
ATOM   4006 C  CB  . LYS B 1 41  ? -0.316  -32.133 83.710  1.00 40.65  ? 41   LYS B CB  1 
ATOM   4007 C  CG  . LYS B 1 41  ? 0.852   -32.996 83.277  1.00 42.71  ? 41   LYS B CG  1 
ATOM   4008 C  CD  . LYS B 1 41  ? 0.924   -34.248 84.139  1.00 47.80  ? 41   LYS B CD  1 
ATOM   4009 C  CE  . LYS B 1 41  ? 2.058   -34.161 85.137  1.00 58.54  ? 41   LYS B CE  1 
ATOM   4010 N  NZ  . LYS B 1 41  ? 2.821   -35.443 85.269  1.00 58.36  ? 41   LYS B NZ  1 
ATOM   4011 N  N   . PHE B 1 42  ? -0.295  -32.087 80.438  1.00 34.31  ? 42   PHE B N   1 
ATOM   4012 C  CA  . PHE B 1 42  ? -0.495  -32.841 79.213  1.00 33.68  ? 42   PHE B CA  1 
ATOM   4013 C  C   . PHE B 1 42  ? 0.761   -33.651 78.964  1.00 34.78  ? 42   PHE B C   1 
ATOM   4014 O  O   . PHE B 1 42  ? 1.852   -33.086 78.859  1.00 35.67  ? 42   PHE B O   1 
ATOM   4015 C  CB  . PHE B 1 42  ? -0.805  -31.906 78.039  1.00 34.13  ? 42   PHE B CB  1 
ATOM   4016 C  CG  . PHE B 1 42  ? -1.199  -32.621 76.794  1.00 35.98  ? 42   PHE B CG  1 
ATOM   4017 C  CD1 . PHE B 1 42  ? -0.242  -33.220 75.992  1.00 39.08  ? 42   PHE B CD1 1 
ATOM   4018 C  CD2 . PHE B 1 42  ? -2.531  -32.721 76.432  1.00 34.93  ? 42   PHE B CD2 1 
ATOM   4019 C  CE1 . PHE B 1 42  ? -0.605  -33.904 74.835  1.00 38.99  ? 42   PHE B CE1 1 
ATOM   4020 C  CE2 . PHE B 1 42  ? -2.904  -33.395 75.279  1.00 35.86  ? 42   PHE B CE2 1 
ATOM   4021 C  CZ  . PHE B 1 42  ? -1.946  -33.983 74.481  1.00 37.13  ? 42   PHE B CZ  1 
ATOM   4022 N  N   . GLU B 1 43  ? 0.612   -34.965 78.886  1.00 36.43  ? 43   GLU B N   1 
ATOM   4023 C  CA  . GLU B 1 43  ? 1.742   -35.877 78.787  1.00 37.94  ? 43   GLU B CA  1 
ATOM   4024 C  C   . GLU B 1 43  ? 1.670   -36.654 77.487  1.00 37.34  ? 43   GLU B C   1 
ATOM   4025 O  O   . GLU B 1 43  ? 0.593   -37.064 77.048  1.00 37.59  ? 43   GLU B O   1 
ATOM   4026 C  CB  . GLU B 1 43  ? 1.774   -36.886 79.941  1.00 36.77  ? 43   GLU B CB  1 
ATOM   4027 C  CG  . GLU B 1 43  ? 2.165   -36.343 81.269  1.00 44.65  ? 43   GLU B CG  1 
ATOM   4028 C  CD  . GLU B 1 43  ? 2.336   -37.461 82.272  1.00 51.16  ? 43   GLU B CD  1 
ATOM   4029 O  OE1 . GLU B 1 43  ? 1.429   -38.311 82.366  1.00 51.07  ? 43   GLU B OE1 1 
ATOM   4030 O  OE2 . GLU B 1 43  ? 3.375   -37.497 82.950  1.00 57.47  ? 43   GLU B OE2 1 
ATOM   4031 N  N   . ALA B 1 44  ? 2.820   -36.854 76.875  1.00 36.63  ? 44   ALA B N   1 
ATOM   4032 C  CA  . ALA B 1 44  ? 2.986   -37.800 75.781  1.00 34.15  ? 44   ALA B CA  1 
ATOM   4033 C  C   . ALA B 1 44  ? 4.226   -38.610 76.094  1.00 32.74  ? 44   ALA B C   1 
ATOM   4034 O  O   . ALA B 1 44  ? 5.008   -38.250 76.979  1.00 35.91  ? 44   ALA B O   1 
ATOM   4035 C  CB  . ALA B 1 44  ? 3.133   -37.081 74.436  1.00 38.00  ? 44   ALA B CB  1 
ATOM   4036 N  N   . PRO B 1 45  ? 4.433   -39.715 75.401  1.00 37.26  ? 45   PRO B N   1 
ATOM   4037 C  CA  . PRO B 1 45  ? 5.644   -40.503 75.656  1.00 37.10  ? 45   PRO B CA  1 
ATOM   4038 C  C   . PRO B 1 45  ? 6.880   -39.631 75.553  1.00 40.04  ? 45   PRO B C   1 
ATOM   4039 O  O   . PRO B 1 45  ? 7.138   -39.043 74.498  1.00 42.82  ? 45   PRO B O   1 
ATOM   4040 C  CB  . PRO B 1 45  ? 5.612   -41.572 74.562  1.00 37.60  ? 45   PRO B CB  1 
ATOM   4041 C  CG  . PRO B 1 45  ? 4.142   -41.710 74.216  1.00 40.57  ? 45   PRO B CG  1 
ATOM   4042 C  CD  . PRO B 1 45  ? 3.584   -40.311 74.353  1.00 36.93  ? 45   PRO B CD  1 
ATOM   4043 N  N   . GLY B 1 46  ? 7.625   -39.530 76.647  1.00 44.17  ? 46   GLY B N   1 
ATOM   4044 C  CA  . GLY B 1 46  ? 8.854   -38.761 76.673  1.00 44.71  ? 46   GLY B CA  1 
ATOM   4045 C  C   . GLY B 1 46  ? 8.700   -37.264 76.841  1.00 46.31  ? 46   GLY B C   1 
ATOM   4046 O  O   . GLY B 1 46  ? 9.702   -36.550 76.744  1.00 45.65  ? 46   GLY B O   1 
ATOM   4047 N  N   . ARG B 1 47  ? 7.495   -36.754 77.095  1.00 37.94  ? 47   ARG B N   1 
ATOM   4048 C  CA  . ARG B 1 47  ? 7.332   -35.307 77.182  1.00 40.44  ? 47   ARG B CA  1 
ATOM   4049 C  C   . ARG B 1 47  ? 6.178   -34.935 78.102  1.00 39.68  ? 47   ARG B C   1 
ATOM   4050 O  O   . ARG B 1 47  ? 5.154   -35.624 78.148  1.00 39.17  ? 47   ARG B O   1 
ATOM   4051 C  CB  . ARG B 1 47  ? 7.083   -34.672 75.807  1.00 43.25  ? 47   ARG B CB  1 
ATOM   4052 C  CG  . ARG B 1 47  ? 6.677   -33.195 75.924  1.00 51.60  ? 47   ARG B CG  1 
ATOM   4053 C  CD  . ARG B 1 47  ? 6.673   -32.449 74.588  1.00 51.01  ? 47   ARG B CD  1 
ATOM   4054 N  NE  . ARG B 1 47  ? 6.281   -31.044 74.722  1.00 42.58  ? 47   ARG B NE  1 
ATOM   4055 C  CZ  . ARG B 1 47  ? 5.740   -30.350 73.727  1.00 44.30  ? 47   ARG B CZ  1 
ATOM   4056 N  NH1 . ARG B 1 47  ? 5.499   -30.913 72.550  1.00 48.42  ? 47   ARG B NH1 1 
ATOM   4057 N  NH2 . ARG B 1 47  ? 5.397   -29.076 73.923  1.00 40.01  ? 47   ARG B NH2 1 
ATOM   4058 N  N   . VAL B 1 48  ? 6.358   -33.834 78.823  1.00 36.57  ? 48   VAL B N   1 
ATOM   4059 C  CA  . VAL B 1 48  ? 5.313   -33.214 79.633  1.00 34.30  ? 48   VAL B CA  1 
ATOM   4060 C  C   . VAL B 1 48  ? 5.267   -31.729 79.309  1.00 37.40  ? 48   VAL B C   1 
ATOM   4061 O  O   . VAL B 1 48  ? 6.311   -31.079 79.165  1.00 36.85  ? 48   VAL B O   1 
ATOM   4062 C  CB  . VAL B 1 48  ? 5.559   -33.417 81.140  1.00 40.17  ? 48   VAL B CB  1 
ATOM   4063 C  CG1 . VAL B 1 48  ? 4.408   -32.840 81.953  1.00 41.80  ? 48   VAL B CG1 1 
ATOM   4064 C  CG2 . VAL B 1 48  ? 5.731   -34.881 81.452  1.00 50.80  ? 48   VAL B CG2 1 
ATOM   4065 N  N   . THR B 1 49  ? 4.058   -31.182 79.216  1.00 35.55  ? 49   THR B N   1 
ATOM   4066 C  CA  . THR B 1 49  ? 3.894   -29.736 79.220  1.00 33.51  ? 49   THR B CA  1 
ATOM   4067 C  C   . THR B 1 49  ? 2.668   -29.384 80.062  1.00 34.73  ? 49   THR B C   1 
ATOM   4068 O  O   . THR B 1 49  ? 1.948   -30.260 80.553  1.00 36.85  ? 49   THR B O   1 
ATOM   4069 C  CB  . THR B 1 49  ? 3.806   -29.160 77.797  1.00 35.53  ? 49   THR B CB  1 
ATOM   4070 O  OG1 . THR B 1 49  ? 4.030   -27.740 77.843  1.00 34.72  ? 49   THR B OG1 1 
ATOM   4071 C  CG2 . THR B 1 49  ? 2.432   -29.447 77.158  1.00 36.44  ? 49   THR B CG2 1 
ATOM   4072 N  N   . ARG B 1 50  ? 2.472   -28.089 80.273  1.00 33.31  ? 50   ARG B N   1 
ATOM   4073 C  CA  . ARG B 1 50  ? 1.384   -27.569 81.099  1.00 32.47  ? 50   ARG B CA  1 
ATOM   4074 C  C   . ARG B 1 50  ? 0.679   -26.470 80.319  1.00 34.78  ? 50   ARG B C   1 
ATOM   4075 O  O   . ARG B 1 50  ? 1.316   -25.492 79.919  1.00 35.50  ? 50   ARG B O   1 
ATOM   4076 C  CB  . ARG B 1 50  ? 1.910   -27.032 82.438  1.00 35.91  ? 50   ARG B CB  1 
ATOM   4077 C  CG  . ARG B 1 50  ? 2.592   -28.092 83.292  1.00 36.31  ? 50   ARG B CG  1 
ATOM   4078 C  CD  . ARG B 1 50  ? 3.910   -27.565 83.830  1.00 39.64  ? 50   ARG B CD  1 
ATOM   4079 N  NE  . ARG B 1 50  ? 4.716   -28.641 84.387  1.00 40.37  ? 50   ARG B NE  1 
ATOM   4080 C  CZ  . ARG B 1 50  ? 5.697   -29.264 83.744  1.00 41.17  ? 50   ARG B CZ  1 
ATOM   4081 N  NH1 . ARG B 1 50  ? 6.068   -28.904 82.515  1.00 38.44  ? 50   ARG B NH1 1 
ATOM   4082 N  NH2 . ARG B 1 50  ? 6.321   -30.276 84.343  1.00 40.11  ? 50   ARG B NH2 1 
ATOM   4083 N  N   . TYR B 1 51  ? -0.629  -26.623 80.110  1.00 32.45  ? 51   TYR B N   1 
ATOM   4084 C  CA  . TYR B 1 51  ? -1.421  -25.651 79.348  1.00 35.09  ? 51   TYR B CA  1 
ATOM   4085 C  C   . TYR B 1 51  ? -2.027  -24.603 80.279  1.00 35.25  ? 51   TYR B C   1 
ATOM   4086 O  O   . TYR B 1 51  ? -2.760  -24.941 81.214  1.00 33.04  ? 51   TYR B O   1 
ATOM   4087 C  CB  . TYR B 1 51  ? -2.523  -26.349 78.548  1.00 33.87  ? 51   TYR B CB  1 
ATOM   4088 C  CG  . TYR B 1 51  ? -1.993  -27.018 77.300  1.00 31.97  ? 51   TYR B CG  1 
ATOM   4089 C  CD1 . TYR B 1 51  ? -1.487  -28.310 77.354  1.00 32.37  ? 51   TYR B CD1 1 
ATOM   4090 C  CD2 . TYR B 1 51  ? -1.948  -26.335 76.081  1.00 32.64  ? 51   TYR B CD2 1 
ATOM   4091 C  CE1 . TYR B 1 51  ? -0.972  -28.924 76.228  1.00 33.64  ? 51   TYR B CE1 1 
ATOM   4092 C  CE2 . TYR B 1 51  ? -1.421  -26.942 74.936  1.00 33.75  ? 51   TYR B CE2 1 
ATOM   4093 C  CZ  . TYR B 1 51  ? -0.937  -28.249 75.025  1.00 34.25  ? 51   TYR B CZ  1 
ATOM   4094 O  OH  . TYR B 1 51  ? -0.406  -28.905 73.930  1.00 33.92  ? 51   TYR B OH  1 
ATOM   4095 N  N   . LEU B 1 52  ? -1.736  -23.332 80.008  1.00 32.82  ? 52   LEU B N   1 
ATOM   4096 C  CA  . LEU B 1 52  ? -2.189  -22.217 80.829  1.00 33.06  ? 52   LEU B CA  1 
ATOM   4097 C  C   . LEU B 1 52  ? -3.277  -21.429 80.105  1.00 34.19  ? 52   LEU B C   1 
ATOM   4098 O  O   . LEU B 1 52  ? -3.142  -21.110 78.915  1.00 33.54  ? 52   LEU B O   1 
ATOM   4099 C  CB  . LEU B 1 52  ? -1.035  -21.279 81.174  1.00 32.86  ? 52   LEU B CB  1 
ATOM   4100 C  CG  . LEU B 1 52  ? 0.195   -21.877 81.846  1.00 32.98  ? 52   LEU B CG  1 
ATOM   4101 C  CD1 . LEU B 1 52  ? 1.175   -20.774 82.123  1.00 35.80  ? 52   LEU B CD1 1 
ATOM   4102 C  CD2 . LEU B 1 52  ? -0.205  -22.560 83.141  1.00 35.34  ? 52   LEU B CD2 1 
ATOM   4103 N  N   . SER B 1 53  ? -4.337  -21.084 80.845  1.00 31.66  ? 53   SER B N   1 
ATOM   4104 C  CA  . SER B 1 53  ? -5.501  -20.418 80.281  1.00 31.79  ? 53   SER B CA  1 
ATOM   4105 C  C   . SER B 1 53  ? -5.915  -19.147 81.014  1.00 32.68  ? 53   SER B C   1 
ATOM   4106 O  O   . SER B 1 53  ? -6.737  -18.403 80.473  1.00 34.39  ? 53   SER B O   1 
ATOM   4107 C  CB  . SER B 1 53  ? -6.705  -21.374 80.251  1.00 34.30  ? 53   SER B CB  1 
ATOM   4108 O  OG  . SER B 1 53  ? -6.451  -22.416 79.335  1.00 35.46  ? 53   SER B OG  1 
ATOM   4109 N  N   . SER B 1 54  ? -5.417  -18.888 82.225  1.00 32.05  ? 54   SER B N   1 
ATOM   4110 C  CA  . SER B 1 54  ? -5.843  -17.721 82.991  1.00 32.75  ? 54   SER B CA  1 
ATOM   4111 C  C   . SER B 1 54  ? -4.825  -16.589 82.905  1.00 31.99  ? 54   SER B C   1 
ATOM   4112 O  O   . SER B 1 54  ? -3.619  -16.814 82.779  1.00 35.32  ? 54   SER B O   1 
ATOM   4113 C  CB  . SER B 1 54  ? -6.084  -18.081 84.460  1.00 31.37  ? 54   SER B CB  1 
ATOM   4114 O  OG  . SER B 1 54  ? -4.866  -18.463 85.074  1.00 32.52  ? 54   SER B OG  1 
ATOM   4115 N  N   . GLN B 1 55  ? -5.330  -15.353 82.961  1.00 35.64  ? 55   GLN B N   1 
ATOM   4116 C  CA  . GLN B 1 55  ? -4.432  -14.206 83.010  1.00 36.15  ? 55   GLN B CA  1 
ATOM   4117 C  C   . GLN B 1 55  ? -3.580  -14.249 84.267  1.00 32.05  ? 55   GLN B C   1 
ATOM   4118 O  O   . GLN B 1 55  ? -2.418  -13.817 84.251  1.00 32.87  ? 55   GLN B O   1 
ATOM   4119 C  CB  . GLN B 1 55  ? -5.249  -12.911 82.931  1.00 33.18  ? 55   GLN B CB  1 
ATOM   4120 C  CG  . GLN B 1 55  ? -4.437  -11.622 82.810  1.00 37.28  ? 55   GLN B CG  1 
ATOM   4121 C  CD  . GLN B 1 55  ? -4.025  -11.051 84.169  1.00 36.71  ? 55   GLN B CD  1 
ATOM   4122 O  OE1 . GLN B 1 55  ? -4.430  -11.546 85.227  1.00 36.15  ? 55   GLN B OE1 1 
ATOM   4123 N  NE2 . GLN B 1 55  ? -3.226  -9.992  84.138  1.00 41.92  ? 55   GLN B NE2 1 
ATOM   4124 N  N   . ARG B 1 56  ? -4.124  -14.816 85.341  1.00 33.48  ? 56   ARG B N   1 
ATOM   4125 C  CA  . ARG B 1 56  ? -3.389  -14.925 86.602  1.00 33.65  ? 56   ARG B CA  1 
ATOM   4126 C  C   . ARG B 1 56  ? -2.070  -15.660 86.407  1.00 36.03  ? 56   ARG B C   1 
ATOM   4127 O  O   . ARG B 1 56  ? -1.016  -15.202 86.868  1.00 38.60  ? 56   ARG B O   1 
ATOM   4128 C  CB  . ARG B 1 56  ? -4.248  -15.658 87.647  1.00 38.70  ? 56   ARG B CB  1 
ATOM   4129 C  CG  . ARG B 1 56  ? -3.629  -15.696 89.045  1.00 47.43  ? 56   ARG B CG  1 
ATOM   4130 C  CD  . ARG B 1 56  ? -4.438  -16.545 90.053  1.00 44.31  ? 56   ARG B CD  1 
ATOM   4131 N  NE  . ARG B 1 56  ? -4.306  -17.986 89.841  1.00 43.07  ? 56   ARG B NE  1 
ATOM   4132 C  CZ  . ARG B 1 56  ? -3.504  -18.763 90.562  1.00 43.84  ? 56   ARG B CZ  1 
ATOM   4133 N  NH1 . ARG B 1 56  ? -2.718  -18.260 91.498  1.00 43.93  ? 56   ARG B NH1 1 
ATOM   4134 N  NH2 . ARG B 1 56  ? -3.506  -20.078 90.354  1.00 44.73  ? 56   ARG B NH2 1 
ATOM   4135 N  N   . LEU B 1 57  ? -2.113  -16.820 85.745  1.00 34.00  ? 57   LEU B N   1 
ATOM   4136 C  CA  . LEU B 1 57  ? -0.897  -17.591 85.529  1.00 30.62  ? 57   LEU B CA  1 
ATOM   4137 C  C   . LEU B 1 57  ? -0.126  -17.109 84.305  1.00 34.82  ? 57   LEU B C   1 
ATOM   4138 O  O   . LEU B 1 57  ? 1.115   -17.133 84.302  1.00 31.51  ? 57   LEU B O   1 
ATOM   4139 C  CB  . LEU B 1 57  ? -1.223  -19.078 85.385  1.00 34.77  ? 57   LEU B CB  1 
ATOM   4140 C  CG  . LEU B 1 57  ? -1.868  -19.712 86.630  1.00 33.21  ? 57   LEU B CG  1 
ATOM   4141 C  CD1 . LEU B 1 57  ? -2.124  -21.199 86.434  1.00 36.94  ? 57   LEU B CD1 1 
ATOM   4142 C  CD2 . LEU B 1 57  ? -0.997  -19.441 87.865  1.00 37.07  ? 57   LEU B CD2 1 
ATOM   4143 N  N   . ILE B 1 58  ? -0.825  -16.660 83.263  1.00 32.82  ? 58   ILE B N   1 
ATOM   4144 C  CA  . ILE B 1 58  ? -0.096  -16.278 82.055  1.00 33.05  ? 58   ILE B CA  1 
ATOM   4145 C  C   . ILE B 1 58  ? 0.731   -15.017 82.289  1.00 34.19  ? 58   ILE B C   1 
ATOM   4146 O  O   . ILE B 1 58  ? 1.819   -14.862 81.714  1.00 33.44  ? 58   ILE B O   1 
ATOM   4147 C  CB  . ILE B 1 58  ? -1.079  -16.153 80.870  1.00 31.94  ? 58   ILE B CB  1 
ATOM   4148 C  CG1 . ILE B 1 58  ? -1.561  -17.564 80.489  1.00 31.71  ? 58   ILE B CG1 1 
ATOM   4149 C  CG2 . ILE B 1 58  ? -0.401  -15.522 79.671  1.00 32.28  ? 58   ILE B CG2 1 
ATOM   4150 C  CD1 . ILE B 1 58  ? -2.742  -17.572 79.516  1.00 32.10  ? 58   ILE B CD1 1 
ATOM   4151 N  N   . LYS B 1 59  ? 0.287   -14.127 83.178  1.00 32.83  ? 59   LYS B N   1 
ATOM   4152 C  CA  . LYS B 1 59  ? 1.103   -12.950 83.453  1.00 34.90  ? 59   LYS B CA  1 
ATOM   4153 C  C   . LYS B 1 59  ? 2.424   -13.347 84.096  1.00 34.81  ? 59   LYS B C   1 
ATOM   4154 O  O   . LYS B 1 59  ? 3.453   -12.720 83.833  1.00 34.85  ? 59   LYS B O   1 
ATOM   4155 C  CB  . LYS B 1 59  ? 0.355   -11.944 84.332  1.00 36.67  ? 59   LYS B CB  1 
ATOM   4156 C  CG  . LYS B 1 59  ? 0.330   -12.279 85.796  1.00 41.88  ? 59   LYS B CG  1 
ATOM   4157 C  CD  . LYS B 1 59  ? -0.506  -11.281 86.569  1.00 42.92  ? 59   LYS B CD  1 
ATOM   4158 C  CE  . LYS B 1 59  ? -0.649  -11.702 88.018  1.00 47.51  ? 59   LYS B CE  1 
ATOM   4159 N  NZ  . LYS B 1 59  ? -1.501  -10.705 88.735  1.00 51.15  ? 59   LYS B NZ  1 
ATOM   4160 N  N   . GLU B 1 60  ? 2.427   -14.391 84.929  1.00 33.73  ? 60   GLU B N   1 
ATOM   4161 C  CA  . GLU B 1 60  ? 3.704   -14.859 85.471  1.00 34.45  ? 60   GLU B CA  1 
ATOM   4162 C  C   . GLU B 1 60  ? 4.547   -15.532 84.393  1.00 36.66  ? 60   GLU B C   1 
ATOM   4163 O  O   . GLU B 1 60  ? 5.765   -15.330 84.333  1.00 37.49  ? 60   GLU B O   1 
ATOM   4164 C  CB  . GLU B 1 60  ? 3.477   -15.820 86.633  1.00 34.12  ? 60   GLU B CB  1 
ATOM   4165 C  CG  . GLU B 1 60  ? 2.868   -15.174 87.859  1.00 41.00  ? 60   GLU B CG  1 
ATOM   4166 C  CD  . GLU B 1 60  ? 2.910   -16.089 89.077  1.00 45.24  ? 60   GLU B CD  1 
ATOM   4167 O  OE1 . GLU B 1 60  ? 3.833   -16.933 89.180  1.00 40.52  ? 60   GLU B OE1 1 
ATOM   4168 O  OE2 . GLU B 1 60  ? 2.022   -15.952 89.937  1.00 46.64  ? 60   GLU B OE2 1 
ATOM   4169 N  N   . ALA B 1 61  ? 3.923   -16.339 83.532  1.00 32.40  ? 61   ALA B N   1 
ATOM   4170 C  CA  . ALA B 1 61  ? 4.667   -16.986 82.457  1.00 35.65  ? 61   ALA B CA  1 
ATOM   4171 C  C   . ALA B 1 61  ? 5.342   -15.966 81.543  1.00 36.11  ? 61   ALA B C   1 
ATOM   4172 O  O   . ALA B 1 61  ? 6.375   -16.270 80.929  1.00 34.94  ? 61   ALA B O   1 
ATOM   4173 C  CB  . ALA B 1 61  ? 3.731   -17.888 81.648  1.00 35.47  ? 61   ALA B CB  1 
ATOM   4174 N  N   . CYS B 1 62  ? 4.773   -14.759 81.438  1.00 35.68  ? 62   CYS B N   1 
ATOM   4175 C  CA  . CYS B 1 62  ? 5.283   -13.674 80.603  1.00 33.45  ? 62   CYS B CA  1 
ATOM   4176 C  C   . CYS B 1 62  ? 6.364   -12.853 81.287  1.00 36.08  ? 62   CYS B C   1 
ATOM   4177 O  O   . CYS B 1 62  ? 6.828   -11.852 80.720  1.00 34.31  ? 62   CYS B O   1 
ATOM   4178 C  CB  . CYS B 1 62  ? 4.133   -12.764 80.185  1.00 34.33  ? 62   CYS B CB  1 
ATOM   4179 S  SG  . CYS B 1 62  ? 3.063   -13.521 78.942  1.00 35.51  ? 62   CYS B SG  1 
ATOM   4180 N  N   . ASP B 1 63  ? 6.767   -13.240 82.486  1.00 34.87  ? 63   ASP B N   1 
ATOM   4181 C  CA  . ASP B 1 63  ? 7.864   -12.579 83.174  1.00 35.87  ? 63   ASP B CA  1 
ATOM   4182 C  C   . ASP B 1 63  ? 9.163   -13.109 82.580  1.00 33.96  ? 63   ASP B C   1 
ATOM   4183 O  O   . ASP B 1 63  ? 9.529   -14.263 82.807  1.00 34.93  ? 63   ASP B O   1 
ATOM   4184 C  CB  . ASP B 1 63  ? 7.748   -12.852 84.674  1.00 35.71  ? 63   ASP B CB  1 
ATOM   4185 C  CG  . ASP B 1 63  ? 8.860   -12.230 85.491  1.00 40.43  ? 63   ASP B CG  1 
ATOM   4186 O  OD1 . ASP B 1 63  ? 9.903   -11.805 84.929  1.00 35.95  ? 63   ASP B OD1 1 
ATOM   4187 O  OD2 . ASP B 1 63  ? 8.679   -12.196 86.728  1.00 40.14  ? 63   ASP B OD2 1 
ATOM   4188 N  N   . GLU B 1 64  ? 9.862   -12.271 81.809  1.00 34.12  ? 64   GLU B N   1 
ATOM   4189 C  CA  . GLU B 1 64  ? 11.027  -12.742 81.065  1.00 35.67  ? 64   GLU B CA  1 
ATOM   4190 C  C   . GLU B 1 64  ? 12.227  -13.039 81.951  1.00 36.48  ? 64   GLU B C   1 
ATOM   4191 O  O   . GLU B 1 64  ? 13.187  -13.657 81.477  1.00 34.83  ? 64   GLU B O   1 
ATOM   4192 C  CB  . GLU B 1 64  ? 11.437  -11.710 80.020  1.00 37.96  ? 64   GLU B CB  1 
ATOM   4193 C  CG  . GLU B 1 64  ? 10.407  -11.508 78.940  1.00 35.02  ? 64   GLU B CG  1 
ATOM   4194 C  CD  . GLU B 1 64  ? 10.817  -10.433 77.966  1.00 41.45  ? 64   GLU B CD  1 
ATOM   4195 O  OE1 . GLU B 1 64  ? 10.660  -9.243  78.304  1.00 45.69  ? 64   GLU B OE1 1 
ATOM   4196 O  OE2 . GLU B 1 64  ? 11.281  -10.777 76.861  1.00 35.43  ? 64   GLU B OE2 1 
ATOM   4197 N  N   . SER B 1 65  ? 12.224  -12.577 83.205  1.00 35.95  ? 65   SER B N   1 
ATOM   4198 C  CA  . SER B 1 65  ? 13.293  -12.977 84.108  1.00 37.44  ? 65   SER B CA  1 
ATOM   4199 C  C   . SER B 1 65  ? 13.107  -14.408 84.561  1.00 37.32  ? 65   SER B C   1 
ATOM   4200 O  O   . SER B 1 65  ? 14.063  -15.023 85.034  1.00 38.90  ? 65   SER B O   1 
ATOM   4201 C  CB  . SER B 1 65  ? 13.357  -12.054 85.332  1.00 39.68  ? 65   SER B CB  1 
ATOM   4202 O  OG  . SER B 1 65  ? 12.307  -12.338 86.244  1.00 41.03  ? 65   SER B OG  1 
ATOM   4203 N  N   . ARG B 1 66  ? 11.898  -14.951 84.422  1.00 33.01  ? 66   ARG B N   1 
ATOM   4204 C  CA  . ARG B 1 66  ? 11.619  -16.298 84.891  1.00 35.37  ? 66   ARG B CA  1 
ATOM   4205 C  C   . ARG B 1 66  ? 11.424  -17.305 83.776  1.00 35.23  ? 66   ARG B C   1 
ATOM   4206 O  O   . ARG B 1 66  ? 11.709  -18.488 83.975  1.00 38.11  ? 66   ARG B O   1 
ATOM   4207 C  CB  . ARG B 1 66  ? 10.367  -16.306 85.780  1.00 34.52  ? 66   ARG B CB  1 
ATOM   4208 C  CG  . ARG B 1 66  ? 10.501  -15.448 87.031  1.00 38.58  ? 66   ARG B CG  1 
ATOM   4209 C  CD  . ARG B 1 66  ? 9.160   -15.268 87.744  1.00 39.42  ? 66   ARG B CD  1 
ATOM   4210 N  NE  . ARG B 1 66  ? 8.702   -16.522 88.328  1.00 38.36  ? 66   ARG B NE  1 
ATOM   4211 C  CZ  . ARG B 1 66  ? 7.450   -16.774 88.689  1.00 39.17  ? 66   ARG B CZ  1 
ATOM   4212 N  NH1 . ARG B 1 66  ? 6.491   -15.872 88.539  1.00 36.35  ? 66   ARG B NH1 1 
ATOM   4213 N  NH2 . ARG B 1 66  ? 7.150   -17.968 89.198  1.00 40.33  ? 66   ARG B NH2 1 
ATOM   4214 N  N   . PHE B 1 67  ? 10.935  -16.872 82.615  1.00 33.54  ? 67   PHE B N   1 
ATOM   4215 C  CA  . PHE B 1 67  ? 10.610  -17.775 81.523  1.00 30.84  ? 67   PHE B CA  1 
ATOM   4216 C  C   . PHE B 1 67  ? 11.094  -17.196 80.204  1.00 31.60  ? 67   PHE B C   1 
ATOM   4217 O  O   . PHE B 1 67  ? 10.966  -15.992 79.964  1.00 33.83  ? 67   PHE B O   1 
ATOM   4218 C  CB  . PHE B 1 67  ? 9.100   -18.020 81.437  1.00 33.40  ? 67   PHE B CB  1 
ATOM   4219 C  CG  . PHE B 1 67  ? 8.512   -18.576 82.693  1.00 34.09  ? 67   PHE B CG  1 
ATOM   4220 C  CD1 . PHE B 1 67  ? 8.489   -19.948 82.905  1.00 34.71  ? 67   PHE B CD1 1 
ATOM   4221 C  CD2 . PHE B 1 67  ? 7.990   -17.736 83.664  1.00 37.72  ? 67   PHE B CD2 1 
ATOM   4222 C  CE1 . PHE B 1 67  ? 7.936   -20.475 84.082  1.00 34.17  ? 67   PHE B CE1 1 
ATOM   4223 C  CE2 . PHE B 1 67  ? 7.452   -18.256 84.842  1.00 37.89  ? 67   PHE B CE2 1 
ATOM   4224 C  CZ  . PHE B 1 67  ? 7.422   -19.616 85.042  1.00 33.42  ? 67   PHE B CZ  1 
ATOM   4225 N  N   . ASP B 1 68  ? 11.628  -18.068 79.349  1.00 33.26  ? 68   ASP B N   1 
ATOM   4226 C  CA  . ASP B 1 68  ? 12.065  -17.718 78.002  1.00 32.81  ? 68   ASP B CA  1 
ATOM   4227 C  C   . ASP B 1 68  ? 11.223  -18.465 76.975  1.00 31.64  ? 68   ASP B C   1 
ATOM   4228 O  O   . ASP B 1 68  ? 10.579  -19.471 77.284  1.00 31.92  ? 68   ASP B O   1 
ATOM   4229 C  CB  . ASP B 1 68  ? 13.563  -18.061 77.841  1.00 30.91  ? 68   ASP B CB  1 
ATOM   4230 C  CG  . ASP B 1 68  ? 14.156  -17.639 76.499  1.00 35.13  ? 68   ASP B CG  1 
ATOM   4231 O  OD1 . ASP B 1 68  ? 13.642  -16.714 75.828  1.00 32.69  ? 68   ASP B OD1 1 
ATOM   4232 O  OD2 . ASP B 1 68  ? 15.186  -18.256 76.131  1.00 33.15  ? 68   ASP B OD2 1 
ATOM   4233 N  N   . LYS B 1 69  ? 11.263  -17.994 75.730  1.00 31.16  ? 69   LYS B N   1 
ATOM   4234 C  CA  . LYS B 1 69  ? 10.553  -18.683 74.654  1.00 30.52  ? 69   LYS B CA  1 
ATOM   4235 C  C   . LYS B 1 69  ? 11.077  -20.105 74.477  1.00 32.42  ? 69   LYS B C   1 
ATOM   4236 O  O   . LYS B 1 69  ? 12.285  -20.335 74.409  1.00 32.90  ? 69   LYS B O   1 
ATOM   4237 C  CB  . LYS B 1 69  ? 10.693  -17.922 73.322  1.00 32.91  ? 69   LYS B CB  1 
ATOM   4238 C  CG  . LYS B 1 69  ? 10.321  -18.777 72.100  1.00 30.98  ? 69   LYS B CG  1 
ATOM   4239 C  CD  . LYS B 1 69  ? 9.965   -17.928 70.860  1.00 28.65  ? 69   LYS B CD  1 
ATOM   4240 C  CE  . LYS B 1 69  ? 9.809   -18.802 69.593  1.00 29.08  ? 69   LYS B CE  1 
ATOM   4241 N  NZ  . LYS B 1 69  ? 8.954   -18.143 68.515  1.00 30.48  ? 69   LYS B NZ  1 
ATOM   4242 N  N   . ASN B 1 70  ? 10.151  -21.053 74.376  1.00 30.72  ? 70   ASN B N   1 
ATOM   4243 C  CA  . ASN B 1 70  ? 10.432  -22.438 74.043  1.00 29.28  ? 70   ASN B CA  1 
ATOM   4244 C  C   . ASN B 1 70  ? 9.965   -22.718 72.625  1.00 29.90  ? 70   ASN B C   1 
ATOM   4245 O  O   . ASN B 1 70  ? 8.982   -22.134 72.153  1.00 33.51  ? 70   ASN B O   1 
ATOM   4246 C  CB  . ASN B 1 70  ? 9.715   -23.390 75.013  1.00 32.79  ? 70   ASN B CB  1 
ATOM   4247 C  CG  . ASN B 1 70  ? 10.023  -24.830 74.726  1.00 33.62  ? 70   ASN B CG  1 
ATOM   4248 O  OD1 . ASN B 1 70  ? 11.188  -25.208 74.632  1.00 34.84  ? 70   ASN B OD1 1 
ATOM   4249 N  ND2 . ASN B 1 70  ? 8.990   -25.647 74.557  1.00 33.04  ? 70   ASN B ND2 1 
ATOM   4250 N  N   . LEU B 1 71  ? 10.670  -23.610 71.935  1.00 30.48  ? 71   LEU B N   1 
ATOM   4251 C  CA  . LEU B 1 71  ? 10.175  -24.138 70.668  1.00 32.84  ? 71   LEU B CA  1 
ATOM   4252 C  C   . LEU B 1 71  ? 9.246   -25.309 70.971  1.00 35.10  ? 71   LEU B C   1 
ATOM   4253 O  O   . LEU B 1 71  ? 9.687   -26.372 71.423  1.00 33.21  ? 71   LEU B O   1 
ATOM   4254 C  CB  . LEU B 1 71  ? 11.321  -24.550 69.751  1.00 34.39  ? 71   LEU B CB  1 
ATOM   4255 C  CG  . LEU B 1 71  ? 12.313  -23.451 69.359  1.00 33.01  ? 71   LEU B CG  1 
ATOM   4256 C  CD1 . LEU B 1 71  ? 13.318  -23.986 68.326  1.00 34.71  ? 71   LEU B CD1 1 
ATOM   4257 C  CD2 . LEU B 1 71  ? 11.638  -22.148 68.845  1.00 33.39  ? 71   LEU B CD2 1 
ATOM   4258 N  N   . SER B 1 72  ? 7.949   -25.093 70.768  1.00 29.84  ? 72   SER B N   1 
ATOM   4259 C  CA  . SER B 1 72  ? 7.000   -26.188 70.773  1.00 33.15  ? 72   SER B CA  1 
ATOM   4260 C  C   . SER B 1 72  ? 7.398   -27.230 69.733  1.00 30.20  ? 72   SER B C   1 
ATOM   4261 O  O   . SER B 1 72  ? 8.229   -26.988 68.856  1.00 35.78  ? 72   SER B O   1 
ATOM   4262 C  CB  . SER B 1 72  ? 5.607   -25.665 70.453  1.00 28.83  ? 72   SER B CB  1 
ATOM   4263 O  OG  . SER B 1 72  ? 5.658   -24.932 69.246  1.00 31.82  ? 72   SER B OG  1 
ATOM   4264 N  N   . GLN B 1 73  ? 6.808   -28.416 69.844  1.00 35.31  ? 73   GLN B N   1 
ATOM   4265 C  CA  . GLN B 1 73  ? 7.010   -29.402 68.791  1.00 34.31  ? 73   GLN B CA  1 
ATOM   4266 C  C   . GLN B 1 73  ? 6.579   -28.833 67.449  1.00 34.83  ? 73   GLN B C   1 
ATOM   4267 O  O   . GLN B 1 73  ? 7.251   -29.031 66.425  1.00 34.82  ? 73   GLN B O   1 
ATOM   4268 C  CB  . GLN B 1 73  ? 6.249   -30.689 69.113  1.00 37.11  ? 73   GLN B CB  1 
ATOM   4269 C  CG  . GLN B 1 73  ? 6.706   -31.855 68.283  1.00 41.13  ? 73   GLN B CG  1 
ATOM   4270 C  CD  . GLN B 1 73  ? 8.150   -32.189 68.568  1.00 47.92  ? 73   GLN B CD  1 
ATOM   4271 O  OE1 . GLN B 1 73  ? 8.490   -32.595 69.689  1.00 44.34  ? 73   GLN B OE1 1 
ATOM   4272 N  NE2 . GLN B 1 73  ? 9.018   -31.988 67.575  1.00 41.31  ? 73   GLN B NE2 1 
ATOM   4273 N  N   . ALA B 1 74  ? 5.476   -28.089 67.438  1.00 33.56  ? 74   ALA B N   1 
ATOM   4274 C  CA  . ALA B 1 74  ? 5.044   -27.445 66.201  1.00 34.28  ? 74   ALA B CA  1 
ATOM   4275 C  C   . ALA B 1 74  ? 6.171   -26.610 65.602  1.00 34.59  ? 74   ALA B C   1 
ATOM   4276 O  O   . ALA B 1 74  ? 6.507   -26.753 64.418  1.00 33.22  ? 74   ALA B O   1 
ATOM   4277 C  CB  . ALA B 1 74  ? 3.804   -26.583 66.470  1.00 34.47  ? 74   ALA B CB  1 
ATOM   4278 N  N   . LEU B 1 75  ? 6.782   -25.735 66.415  1.00 30.41  ? 75   LEU B N   1 
ATOM   4279 C  CA  . LEU B 1 75  ? 7.844   -24.881 65.890  1.00 30.86  ? 75   LEU B CA  1 
ATOM   4280 C  C   . LEU B 1 75  ? 9.094   -25.684 65.554  1.00 32.54  ? 75   LEU B C   1 
ATOM   4281 O  O   . LEU B 1 75  ? 9.804   -25.332 64.606  1.00 32.91  ? 75   LEU B O   1 
ATOM   4282 C  CB  . LEU B 1 75  ? 8.189   -23.759 66.879  1.00 32.87  ? 75   LEU B CB  1 
ATOM   4283 C  CG  . LEU B 1 75  ? 7.166   -22.624 67.054  1.00 31.83  ? 75   LEU B CG  1 
ATOM   4284 C  CD1 . LEU B 1 75  ? 7.721   -21.511 67.951  1.00 31.91  ? 75   LEU B CD1 1 
ATOM   4285 C  CD2 . LEU B 1 75  ? 6.663   -22.062 65.700  1.00 31.18  ? 75   LEU B CD2 1 
ATOM   4286 N  N   . LYS B 1 76  ? 9.381   -26.765 66.298  1.00 31.60  ? 76   LYS B N   1 
ATOM   4287 C  CA  . LYS B 1 76  ? 10.515  -27.602 65.911  1.00 36.92  ? 76   LYS B CA  1 
ATOM   4288 C  C   . LYS B 1 76  ? 10.304  -28.177 64.518  1.00 35.29  ? 76   LYS B C   1 
ATOM   4289 O  O   . LYS B 1 76  ? 11.245  -28.258 63.714  1.00 33.93  ? 76   LYS B O   1 
ATOM   4290 C  CB  . LYS B 1 76  ? 10.737  -28.708 66.943  1.00 35.48  ? 76   LYS B CB  1 
ATOM   4291 C  CG  . LYS B 1 76  ? 11.392  -28.175 68.228  1.00 38.87  ? 76   LYS B CG  1 
ATOM   4292 C  CD  . LYS B 1 76  ? 11.571  -29.265 69.268  1.00 38.33  ? 76   LYS B CD  1 
ATOM   4293 C  CE  . LYS B 1 76  ? 12.201  -28.710 70.536  1.00 47.43  ? 76   LYS B CE  1 
ATOM   4294 N  NZ  . LYS B 1 76  ? 12.066  -29.653 71.668  1.00 48.84  ? 76   LYS B NZ  1 
ATOM   4295 N  N   . PHE B 1 77  ? 9.066   -28.545 64.200  1.00 33.47  ? 77   PHE B N   1 
ATOM   4296 C  CA  . PHE B 1 77  ? 8.784   -29.097 62.883  1.00 33.76  ? 77   PHE B CA  1 
ATOM   4297 C  C   . PHE B 1 77  ? 8.815   -28.011 61.816  1.00 35.82  ? 77   PHE B C   1 
ATOM   4298 O  O   . PHE B 1 77  ? 9.285   -28.248 60.699  1.00 35.60  ? 77   PHE B O   1 
ATOM   4299 C  CB  . PHE B 1 77  ? 7.434   -29.814 62.898  1.00 36.04  ? 77   PHE B CB  1 
ATOM   4300 C  CG  . PHE B 1 77  ? 7.445   -31.106 63.672  1.00 37.32  ? 77   PHE B CG  1 
ATOM   4301 C  CD1 . PHE B 1 77  ? 8.629   -31.810 63.842  1.00 39.33  ? 77   PHE B CD1 1 
ATOM   4302 C  CD2 . PHE B 1 77  ? 6.282   -31.608 64.238  1.00 35.51  ? 77   PHE B CD2 1 
ATOM   4303 C  CE1 . PHE B 1 77  ? 8.643   -33.002 64.541  1.00 46.05  ? 77   PHE B CE1 1 
ATOM   4304 C  CE2 . PHE B 1 77  ? 6.286   -32.800 64.938  1.00 41.88  ? 77   PHE B CE2 1 
ATOM   4305 C  CZ  . PHE B 1 77  ? 7.471   -33.496 65.097  1.00 41.53  ? 77   PHE B CZ  1 
ATOM   4306 N  N   . VAL B 1 78  ? 8.316   -26.811 62.135  1.00 31.85  ? 78   VAL B N   1 
ATOM   4307 C  CA  . VAL B 1 78  ? 8.419   -25.708 61.183  1.00 32.32  ? 78   VAL B CA  1 
ATOM   4308 C  C   . VAL B 1 78  ? 9.886   -25.348 60.968  1.00 31.82  ? 78   VAL B C   1 
ATOM   4309 O  O   . VAL B 1 78  ? 10.282  -24.945 59.872  1.00 32.21  ? 78   VAL B O   1 
ATOM   4310 C  CB  . VAL B 1 78  ? 7.589   -24.501 61.671  1.00 36.97  ? 78   VAL B CB  1 
ATOM   4311 C  CG1 . VAL B 1 78  ? 7.884   -23.286 60.848  1.00 36.08  ? 78   VAL B CG1 1 
ATOM   4312 C  CG2 . VAL B 1 78  ? 6.083   -24.825 61.632  1.00 32.86  ? 78   VAL B CG2 1 
ATOM   4313 N  N   . ARG B 1 79  ? 10.722  -25.537 61.992  1.00 31.61  ? 79   ARG B N   1 
ATOM   4314 C  CA  . ARG B 1 79  ? 12.147  -25.244 61.839  1.00 33.71  ? 79   ARG B CA  1 
ATOM   4315 C  C   . ARG B 1 79  ? 12.804  -26.090 60.749  1.00 37.10  ? 79   ARG B C   1 
ATOM   4316 O  O   . ARG B 1 79  ? 13.861  -25.704 60.228  1.00 34.30  ? 79   ARG B O   1 
ATOM   4317 C  CB  . ARG B 1 79  ? 12.867  -25.449 63.178  1.00 33.77  ? 79   ARG B CB  1 
ATOM   4318 C  CG  . ARG B 1 79  ? 14.395  -25.186 63.128  1.00 34.68  ? 79   ARG B CG  1 
ATOM   4319 C  CD  . ARG B 1 79  ? 14.958  -24.942 64.506  1.00 34.91  ? 79   ARG B CD  1 
ATOM   4320 N  NE  . ARG B 1 79  ? 16.416  -24.852 64.477  1.00 38.13  ? 79   ARG B NE  1 
ATOM   4321 C  CZ  . ARG B 1 79  ? 17.131  -23.963 65.156  1.00 39.66  ? 79   ARG B CZ  1 
ATOM   4322 N  NH1 . ARG B 1 79  ? 16.554  -23.047 65.917  1.00 32.45  ? 79   ARG B NH1 1 
ATOM   4323 N  NH2 . ARG B 1 79  ? 18.462  -23.996 65.070  1.00 37.39  ? 79   ARG B NH2 1 
ATOM   4324 N  N   . ASP B 1 80  ? 12.217  -27.238 60.394  1.00 35.97  ? 80   ASP B N   1 
ATOM   4325 C  CA  . ASP B 1 80  ? 12.793  -28.033 59.314  1.00 36.02  ? 80   ASP B CA  1 
ATOM   4326 C  C   . ASP B 1 80  ? 12.868  -27.243 58.013  1.00 37.70  ? 80   ASP B C   1 
ATOM   4327 O  O   . ASP B 1 80  ? 13.733  -27.519 57.172  1.00 41.25  ? 80   ASP B O   1 
ATOM   4328 C  CB  . ASP B 1 80  ? 11.995  -29.326 59.117  1.00 37.73  ? 80   ASP B CB  1 
ATOM   4329 C  CG  . ASP B 1 80  ? 12.263  -30.350 60.210  1.00 44.68  ? 80   ASP B CG  1 
ATOM   4330 O  OD1 . ASP B 1 80  ? 13.311  -30.255 60.869  1.00 44.62  ? 80   ASP B OD1 1 
ATOM   4331 O  OD2 . ASP B 1 80  ? 11.423  -31.246 60.416  1.00 51.28  ? 80   ASP B OD2 1 
ATOM   4332 N  N   . PHE B 1 81  ? 11.998  -26.246 57.822  1.00 34.49  ? 81   PHE B N   1 
ATOM   4333 C  CA  . PHE B 1 81  ? 12.170  -25.361 56.682  1.00 36.55  ? 81   PHE B CA  1 
ATOM   4334 C  C   . PHE B 1 81  ? 12.434  -23.901 57.050  1.00 34.90  ? 81   PHE B C   1 
ATOM   4335 O  O   . PHE B 1 81  ? 12.996  -23.179 56.225  1.00 33.71  ? 81   PHE B O   1 
ATOM   4336 C  CB  . PHE B 1 81  ? 10.969  -25.465 55.716  1.00 34.86  ? 81   PHE B CB  1 
ATOM   4337 C  CG  . PHE B 1 81  ? 9.611   -25.343 56.361  1.00 34.77  ? 81   PHE B CG  1 
ATOM   4338 C  CD1 . PHE B 1 81  ? 8.928   -26.471 56.813  1.00 35.25  ? 81   PHE B CD1 1 
ATOM   4339 C  CD2 . PHE B 1 81  ? 8.985   -24.108 56.457  1.00 33.87  ? 81   PHE B CD2 1 
ATOM   4340 C  CE1 . PHE B 1 81  ? 7.654   -26.353 57.379  1.00 34.74  ? 81   PHE B CE1 1 
ATOM   4341 C  CE2 . PHE B 1 81  ? 7.718   -23.987 57.036  1.00 37.00  ? 81   PHE B CE2 1 
ATOM   4342 C  CZ  . PHE B 1 81  ? 7.058   -25.109 57.498  1.00 39.05  ? 81   PHE B CZ  1 
ATOM   4343 N  N   . ALA B 1 82  ? 12.107  -23.463 58.268  1.00 31.73  ? 82   ALA B N   1 
ATOM   4344 C  CA  . ALA B 1 82  ? 12.383  -22.090 58.667  1.00 32.20  ? 82   ALA B CA  1 
ATOM   4345 C  C   . ALA B 1 82  ? 13.703  -21.915 59.415  1.00 32.20  ? 82   ALA B C   1 
ATOM   4346 O  O   . ALA B 1 82  ? 14.073  -20.769 59.706  1.00 35.08  ? 82   ALA B O   1 
ATOM   4347 C  CB  . ALA B 1 82  ? 11.237  -21.557 59.537  1.00 32.45  ? 82   ALA B CB  1 
ATOM   4348 N  N   . GLY B 1 83  ? 14.391  -23.002 59.755  1.00 34.31  ? 83   GLY B N   1 
ATOM   4349 C  CA  . GLY B 1 83  ? 15.753  -22.921 60.276  1.00 34.73  ? 83   GLY B CA  1 
ATOM   4350 C  C   . GLY B 1 83  ? 15.878  -22.038 61.499  1.00 34.83  ? 83   GLY B C   1 
ATOM   4351 O  O   . GLY B 1 83  ? 15.025  -22.048 62.405  1.00 32.86  ? 83   GLY B O   1 
ATOM   4352 N  N   . ASP B 1 84  ? 16.960  -21.255 61.543  1.00 31.76  ? 84   ASP B N   1 
ATOM   4353 C  CA  . ASP B 1 84  ? 17.126  -20.292 62.628  1.00 33.32  ? 84   ASP B CA  1 
ATOM   4354 C  C   . ASP B 1 84  ? 16.728  -18.892 62.201  1.00 31.63  ? 84   ASP B C   1 
ATOM   4355 O  O   . ASP B 1 84  ? 17.343  -17.908 62.615  1.00 31.94  ? 84   ASP B O   1 
ATOM   4356 C  CB  . ASP B 1 84  ? 18.552  -20.322 63.195  1.00 30.72  ? 84   ASP B CB  1 
ATOM   4357 C  CG  . ASP B 1 84  ? 19.615  -19.998 62.169  1.00 35.90  ? 84   ASP B CG  1 
ATOM   4358 O  OD1 . ASP B 1 84  ? 19.312  -19.871 60.965  1.00 34.18  ? 84   ASP B OD1 1 
ATOM   4359 O  OD2 . ASP B 1 84  ? 20.788  -19.890 62.583  1.00 34.16  ? 84   ASP B OD2 1 
ATOM   4360 N  N   . GLY B 1 85  ? 15.681  -18.793 61.378  1.00 33.27  ? 85   GLY B N   1 
ATOM   4361 C  CA  . GLY B 1 85  ? 14.966  -17.547 61.216  1.00 31.23  ? 85   GLY B CA  1 
ATOM   4362 C  C   . GLY B 1 85  ? 14.380  -17.085 62.539  1.00 35.01  ? 85   GLY B C   1 
ATOM   4363 O  O   . GLY B 1 85  ? 14.386  -17.797 63.542  1.00 30.99  ? 85   GLY B O   1 
ATOM   4364 N  N   . LEU B 1 86  ? 13.846  -15.858 62.525  1.00 30.83  ? 86   LEU B N   1 
ATOM   4365 C  CA  . LEU B 1 86  ? 13.483  -15.192 63.780  1.00 28.73  ? 86   LEU B CA  1 
ATOM   4366 C  C   . LEU B 1 86  ? 12.457  -15.977 64.585  1.00 31.98  ? 86   LEU B C   1 
ATOM   4367 O  O   . LEU B 1 86  ? 12.490  -15.957 65.820  1.00 32.00  ? 86   LEU B O   1 
ATOM   4368 C  CB  . LEU B 1 86  ? 12.944  -13.782 63.510  1.00 33.51  ? 86   LEU B CB  1 
ATOM   4369 C  CG  . LEU B 1 86  ? 13.994  -12.682 63.348  1.00 31.20  ? 86   LEU B CG  1 
ATOM   4370 C  CD1 . LEU B 1 86  ? 13.245  -11.405 62.992  1.00 33.08  ? 86   LEU B CD1 1 
ATOM   4371 C  CD2 . LEU B 1 86  ? 14.811  -12.507 64.641  1.00 31.74  ? 86   LEU B CD2 1 
ATOM   4372 N  N   . ALA B 1 87  ? 11.502  -16.627 63.916  1.00 31.07  ? 87   ALA B N   1 
ATOM   4373 C  CA  . ALA B 1 87  ? 10.406  -17.231 64.669  1.00 31.93  ? 87   ALA B CA  1 
ATOM   4374 C  C   . ALA B 1 87  ? 10.750  -18.604 65.229  1.00 31.41  ? 87   ALA B C   1 
ATOM   4375 O  O   . ALA B 1 87  ? 10.075  -19.070 66.156  1.00 32.31  ? 87   ALA B O   1 
ATOM   4376 C  CB  . ALA B 1 87  ? 9.160   -17.351 63.791  1.00 32.03  ? 87   ALA B CB  1 
ATOM   4377 N  N   . THR B 1 88  ? 11.776  -19.265 64.697  1.00 30.28  ? 88   THR B N   1 
ATOM   4378 C  CA  . THR B 1 88  ? 12.093  -20.631 65.092  1.00 28.64  ? 88   THR B CA  1 
ATOM   4379 C  C   . THR B 1 88  ? 13.490  -20.746 65.678  1.00 29.86  ? 88   THR B C   1 
ATOM   4380 O  O   . THR B 1 88  ? 13.989  -21.859 65.848  1.00 34.00  ? 88   THR B O   1 
ATOM   4381 C  CB  . THR B 1 88  ? 11.941  -21.600 63.908  1.00 30.63  ? 88   THR B CB  1 
ATOM   4382 O  OG1 . THR B 1 88  ? 12.557  -21.059 62.723  1.00 31.37  ? 88   THR B OG1 1 
ATOM   4383 C  CG2 . THR B 1 88  ? 10.459  -21.842 63.654  1.00 32.56  ? 88   THR B CG2 1 
ATOM   4384 N  N   . SER B 1 89  ? 14.123  -19.628 65.998  1.00 32.49  ? 89   SER B N   1 
ATOM   4385 C  CA  . SER B 1 89  ? 15.403  -19.659 66.698  1.00 31.02  ? 89   SER B CA  1 
ATOM   4386 C  C   . SER B 1 89  ? 15.208  -19.557 68.206  1.00 33.41  ? 89   SER B C   1 
ATOM   4387 O  O   . SER B 1 89  ? 14.229  -18.989 68.704  1.00 31.51  ? 89   SER B O   1 
ATOM   4388 C  CB  . SER B 1 89  ? 16.308  -18.531 66.195  1.00 34.41  ? 89   SER B CB  1 
ATOM   4389 O  OG  . SER B 1 89  ? 15.614  -17.293 66.174  1.00 39.38  ? 89   SER B OG  1 
ATOM   4390 N  N   . TRP B 1 90  ? 16.152  -20.137 68.940  1.00 30.80  ? 90   TRP B N   1 
ATOM   4391 C  CA  . TRP B 1 90  ? 16.181  -19.949 70.380  1.00 30.69  ? 90   TRP B CA  1 
ATOM   4392 C  C   . TRP B 1 90  ? 16.759  -18.577 70.685  1.00 31.87  ? 90   TRP B C   1 
ATOM   4393 O  O   . TRP B 1 90  ? 17.611  -18.065 69.946  1.00 30.91  ? 90   TRP B O   1 
ATOM   4394 C  CB  . TRP B 1 90  ? 17.031  -21.023 71.063  1.00 30.70  ? 90   TRP B CB  1 
ATOM   4395 C  CG  . TRP B 1 90  ? 16.551  -22.424 70.818  1.00 33.20  ? 90   TRP B CG  1 
ATOM   4396 C  CD1 . TRP B 1 90  ? 16.914  -23.245 69.796  1.00 32.98  ? 90   TRP B CD1 1 
ATOM   4397 C  CD2 . TRP B 1 90  ? 15.606  -23.158 71.609  1.00 35.75  ? 90   TRP B CD2 1 
ATOM   4398 N  NE1 . TRP B 1 90  ? 16.273  -24.451 69.905  1.00 32.40  ? 90   TRP B NE1 1 
ATOM   4399 C  CE2 . TRP B 1 90  ? 15.457  -24.423 71.007  1.00 34.92  ? 90   TRP B CE2 1 
ATOM   4400 C  CE3 . TRP B 1 90  ? 14.880  -22.871 72.773  1.00 35.21  ? 90   TRP B CE3 1 
ATOM   4401 C  CZ2 . TRP B 1 90  ? 14.607  -25.410 71.527  1.00 34.27  ? 90   TRP B CZ2 1 
ATOM   4402 C  CZ3 . TRP B 1 90  ? 14.019  -23.862 73.294  1.00 33.28  ? 90   TRP B CZ3 1 
ATOM   4403 C  CH2 . TRP B 1 90  ? 13.898  -25.110 72.667  1.00 37.20  ? 90   TRP B CH2 1 
ATOM   4404 N  N   . THR B 1 91  ? 16.286  -17.985 71.779  1.00 29.23  ? 91   THR B N   1 
ATOM   4405 C  CA  . THR B 1 91  ? 16.753  -16.661 72.161  1.00 30.49  ? 91   THR B CA  1 
ATOM   4406 C  C   . THR B 1 91  ? 18.272  -16.615 72.307  1.00 34.87  ? 91   THR B C   1 
ATOM   4407 O  O   . THR B 1 91  ? 18.882  -15.566 72.055  1.00 32.60  ? 91   THR B O   1 
ATOM   4408 C  CB  . THR B 1 91  ? 16.075  -16.212 73.460  1.00 34.97  ? 91   THR B CB  1 
ATOM   4409 O  OG1 . THR B 1 91  ? 14.651  -16.243 73.291  1.00 33.48  ? 91   THR B OG1 1 
ATOM   4410 C  CG2 . THR B 1 91  ? 16.510  -14.799 73.819  1.00 34.21  ? 91   THR B CG2 1 
ATOM   4411 N  N   . HIS B 1 92  ? 18.893  -17.735 72.705  1.00 31.62  ? 92   HIS B N   1 
ATOM   4412 C  CA  . HIS B 1 92  ? 20.326  -17.795 72.949  1.00 32.86  ? 92   HIS B CA  1 
ATOM   4413 C  C   . HIS B 1 92  ? 21.145  -18.102 71.703  1.00 32.92  ? 92   HIS B C   1 
ATOM   4414 O  O   . HIS B 1 92  ? 22.377  -18.018 71.762  1.00 32.74  ? 92   HIS B O   1 
ATOM   4415 C  CB  . HIS B 1 92  ? 20.637  -18.838 74.034  1.00 34.42  ? 92   HIS B CB  1 
ATOM   4416 C  CG  . HIS B 1 92  ? 20.021  -20.180 73.785  1.00 34.13  ? 92   HIS B CG  1 
ATOM   4417 N  ND1 . HIS B 1 92  ? 20.533  -21.087 72.878  1.00 35.21  ? 92   HIS B ND1 1 
ATOM   4418 C  CD2 . HIS B 1 92  ? 18.929  -20.771 74.334  1.00 31.84  ? 92   HIS B CD2 1 
ATOM   4419 C  CE1 . HIS B 1 92  ? 19.788  -22.180 72.887  1.00 35.43  ? 92   HIS B CE1 1 
ATOM   4420 N  NE2 . HIS B 1 92  ? 18.812  -22.016 73.762  1.00 34.75  ? 92   HIS B NE2 1 
ATOM   4421 N  N   . GLU B 1 93  ? 20.516  -18.433 70.577  1.00 33.09  ? 93   GLU B N   1 
ATOM   4422 C  CA  . GLU B 1 93  ? 21.274  -18.621 69.347  1.00 30.52  ? 93   GLU B CA  1 
ATOM   4423 C  C   . GLU B 1 93  ? 21.743  -17.269 68.818  1.00 32.57  ? 93   GLU B C   1 
ATOM   4424 O  O   . GLU B 1 93  ? 20.970  -16.310 68.768  1.00 31.38  ? 93   GLU B O   1 
ATOM   4425 C  CB  . GLU B 1 93  ? 20.419  -19.324 68.300  1.00 32.79  ? 93   GLU B CB  1 
ATOM   4426 C  CG  . GLU B 1 93  ? 20.136  -20.789 68.615  1.00 29.88  ? 93   GLU B CG  1 
ATOM   4427 C  CD  . GLU B 1 93  ? 19.360  -21.447 67.505  1.00 33.48  ? 93   GLU B CD  1 
ATOM   4428 O  OE1 . GLU B 1 93  ? 18.117  -21.308 67.459  1.00 36.69  ? 93   GLU B OE1 1 
ATOM   4429 O  OE2 . GLU B 1 93  ? 19.992  -22.111 66.656  1.00 34.82  ? 93   GLU B OE2 1 
ATOM   4430 N  N   . LYS B 1 94  ? 23.023  -17.188 68.434  1.00 31.49  ? 94   LYS B N   1 
ATOM   4431 C  CA  . LYS B 1 94  ? 23.588  -15.915 67.979  1.00 32.22  ? 94   LYS B CA  1 
ATOM   4432 C  C   . LYS B 1 94  ? 22.692  -15.232 66.944  1.00 30.97  ? 94   LYS B C   1 
ATOM   4433 O  O   . LYS B 1 94  ? 22.490  -14.008 66.995  1.00 33.84  ? 94   LYS B O   1 
ATOM   4434 C  CB  . LYS B 1 94  ? 24.987  -16.159 67.403  1.00 32.62  ? 94   LYS B CB  1 
ATOM   4435 C  CG  . LYS B 1 94  ? 25.637  -14.916 66.773  1.00 36.88  ? 94   LYS B CG  1 
ATOM   4436 C  CD  . LYS B 1 94  ? 27.086  -15.219 66.367  1.00 34.00  ? 94   LYS B CD  1 
ATOM   4437 C  CE  . LYS B 1 94  ? 27.738  -14.042 65.664  1.00 40.56  ? 94   LYS B CE  1 
ATOM   4438 N  NZ  . LYS B 1 94  ? 29.198  -14.302 65.394  1.00 39.46  ? 94   LYS B NZ  1 
ATOM   4439 N  N   . ASN B 1 95  ? 22.132  -16.011 66.012  1.00 30.26  ? 95   ASN B N   1 
ATOM   4440 C  CA  . ASN B 1 95  ? 21.370  -15.430 64.911  1.00 32.74  ? 95   ASN B CA  1 
ATOM   4441 C  C   . ASN B 1 95  ? 20.027  -14.845 65.346  1.00 34.05  ? 95   ASN B C   1 
ATOM   4442 O  O   . ASN B 1 95  ? 19.414  -14.116 64.553  1.00 33.72  ? 95   ASN B O   1 
ATOM   4443 C  CB  . ASN B 1 95  ? 21.128  -16.469 63.818  1.00 33.06  ? 95   ASN B CB  1 
ATOM   4444 C  CG  . ASN B 1 95  ? 22.269  -16.551 62.815  1.00 36.33  ? 95   ASN B CG  1 
ATOM   4445 O  OD1 . ASN B 1 95  ? 23.020  -15.595 62.642  1.00 41.08  ? 95   ASN B OD1 1 
ATOM   4446 N  ND2 . ASN B 1 95  ? 22.388  -17.697 62.132  1.00 33.39  ? 95   ASN B ND2 1 
ATOM   4447 N  N   . TRP B 1 96  ? 19.521  -15.156 66.543  1.00 34.22  ? 96   TRP B N   1 
ATOM   4448 C  CA  . TRP B 1 96  ? 18.266  -14.512 66.943  1.00 32.93  ? 96   TRP B CA  1 
ATOM   4449 C  C   . TRP B 1 96  ? 18.474  -13.017 67.176  1.00 32.37  ? 96   TRP B C   1 
ATOM   4450 O  O   . TRP B 1 96  ? 17.893  -12.178 66.479  1.00 33.98  ? 96   TRP B O   1 
ATOM   4451 C  CB  . TRP B 1 96  ? 17.620  -15.152 68.187  1.00 30.24  ? 96   TRP B CB  1 
ATOM   4452 C  CG  . TRP B 1 96  ? 16.399  -14.308 68.453  1.00 30.06  ? 96   TRP B CG  1 
ATOM   4453 C  CD1 . TRP B 1 96  ? 15.263  -14.258 67.672  1.00 32.44  ? 96   TRP B CD1 1 
ATOM   4454 C  CD2 . TRP B 1 96  ? 16.260  -13.261 69.418  1.00 32.59  ? 96   TRP B CD2 1 
ATOM   4455 N  NE1 . TRP B 1 96  ? 14.414  -13.293 68.137  1.00 33.79  ? 96   TRP B NE1 1 
ATOM   4456 C  CE2 . TRP B 1 96  ? 14.996  -12.658 69.204  1.00 32.78  ? 96   TRP B CE2 1 
ATOM   4457 C  CE3 . TRP B 1 96  ? 17.058  -12.798 70.469  1.00 34.34  ? 96   TRP B CE3 1 
ATOM   4458 C  CZ2 . TRP B 1 96  ? 14.519  -11.608 69.999  1.00 33.52  ? 96   TRP B CZ2 1 
ATOM   4459 C  CZ3 . TRP B 1 96  ? 16.585  -11.760 71.255  1.00 33.69  ? 96   TRP B CZ3 1 
ATOM   4460 C  CH2 . TRP B 1 96  ? 15.318  -11.178 71.019  1.00 34.98  ? 96   TRP B CH2 1 
ATOM   4461 N  N   . LYS B 1 97  ? 19.324  -12.657 68.136  1.00 31.72  ? 97   LYS B N   1 
ATOM   4462 C  CA  . LYS B 1 97  ? 19.462  -11.236 68.441  1.00 30.90  ? 97   LYS B CA  1 
ATOM   4463 C  C   . LYS B 1 97  ? 20.064  -10.482 67.270  1.00 31.22  ? 97   LYS B C   1 
ATOM   4464 O  O   . LYS B 1 97  ? 19.710  -9.323  67.030  1.00 32.48  ? 97   LYS B O   1 
ATOM   4465 C  CB  . LYS B 1 97  ? 20.309  -11.015 69.692  1.00 31.09  ? 97   LYS B CB  1 
ATOM   4466 C  CG  . LYS B 1 97  ? 20.291  -9.563  70.199  1.00 36.19  ? 97   LYS B CG  1 
ATOM   4467 C  CD  . LYS B 1 97  ? 18.875  -9.102  70.581  1.00 39.20  ? 97   LYS B CD  1 
ATOM   4468 C  CE  . LYS B 1 97  ? 18.855  -7.686  71.135  1.00 46.69  ? 97   LYS B CE  1 
ATOM   4469 N  NZ  . LYS B 1 97  ? 19.616  -7.623  72.401  1.00 46.00  ? 97   LYS B NZ  1 
ATOM   4470 N  N   . LYS B 1 98  ? 20.962  -11.126 66.524  1.00 30.09  ? 98   LYS B N   1 
ATOM   4471 C  CA  . LYS B 1 98  ? 21.580  -10.474 65.373  1.00 33.03  ? 98   LYS B CA  1 
ATOM   4472 C  C   . LYS B 1 98  ? 20.536  -10.094 64.333  1.00 35.78  ? 98   LYS B C   1 
ATOM   4473 O  O   . LYS B 1 98  ? 20.501  -8.953  63.855  1.00 31.97  ? 98   LYS B O   1 
ATOM   4474 C  CB  . LYS B 1 98  ? 22.629  -11.406 64.774  1.00 34.56  ? 98   LYS B CB  1 
ATOM   4475 C  CG  . LYS B 1 98  ? 23.292  -10.908 63.529  1.00 35.83  ? 98   LYS B CG  1 
ATOM   4476 C  CD  . LYS B 1 98  ? 24.382  -11.893 63.125  1.00 34.43  ? 98   LYS B CD  1 
ATOM   4477 C  CE  . LYS B 1 98  ? 24.918  -11.622 61.754  1.00 34.21  ? 98   LYS B CE  1 
ATOM   4478 N  NZ  . LYS B 1 98  ? 25.971  -12.630 61.469  1.00 35.41  ? 98   LYS B NZ  1 
ATOM   4479 N  N   . ALA B 1 99  ? 19.694  -11.056 63.940  1.00 32.39  ? 99   ALA B N   1 
ATOM   4480 C  CA  . ALA B 1 99  ? 18.658  -10.758 62.959  1.00 31.46  ? 99   ALA B CA  1 
ATOM   4481 C  C   . ALA B 1 99  ? 17.621  -9.795  63.525  1.00 32.28  ? 99   ALA B C   1 
ATOM   4482 O  O   . ALA B 1 99  ? 17.069  -8.966  62.789  1.00 34.11  ? 99   ALA B O   1 
ATOM   4483 C  CB  . ALA B 1 99  ? 17.980  -12.048 62.506  1.00 31.07  ? 99   ALA B CB  1 
ATOM   4484 N  N   . HIS B 1 100 ? 17.321  -9.910  64.820  1.00 30.33  ? 100  HIS B N   1 
ATOM   4485 C  CA  . HIS B 1 100 ? 16.371  -8.994  65.445  1.00 32.40  ? 100  HIS B CA  1 
ATOM   4486 C  C   . HIS B 1 100 ? 16.868  -7.556  65.354  1.00 35.69  ? 100  HIS B C   1 
ATOM   4487 O  O   . HIS B 1 100 ? 16.121  -6.650  64.973  1.00 34.57  ? 100  HIS B O   1 
ATOM   4488 C  CB  . HIS B 1 100 ? 16.127  -9.407  66.899  1.00 33.04  ? 100  HIS B CB  1 
ATOM   4489 C  CG  . HIS B 1 100 ? 15.330  -8.414  67.690  1.00 39.98  ? 100  HIS B CG  1 
ATOM   4490 N  ND1 . HIS B 1 100 ? 13.950  -8.390  67.682  1.00 38.66  ? 100  HIS B ND1 1 
ATOM   4491 C  CD2 . HIS B 1 100 ? 15.719  -7.421  68.529  1.00 43.67  ? 100  HIS B CD2 1 
ATOM   4492 C  CE1 . HIS B 1 100 ? 13.524  -7.429  68.483  1.00 41.81  ? 100  HIS B CE1 1 
ATOM   4493 N  NE2 . HIS B 1 100 ? 14.576  -6.826  69.010  1.00 47.91  ? 100  HIS B NE2 1 
ATOM   4494 N  N   . ASN B 1 101 ? 18.148  -7.330  65.668  1.00 33.71  ? 101  ASN B N   1 
ATOM   4495 C  CA  . ASN B 1 101 ? 18.694  -5.976  65.586  1.00 38.65  ? 101  ASN B CA  1 
ATOM   4496 C  C   . ASN B 1 101 ? 18.690  -5.456  64.153  1.00 33.26  ? 101  ASN B C   1 
ATOM   4497 O  O   . ASN B 1 101 ? 18.434  -4.268  63.910  1.00 37.95  ? 101  ASN B O   1 
ATOM   4498 C  CB  . ASN B 1 101 ? 20.117  -5.948  66.159  1.00 31.69  ? 101  ASN B CB  1 
ATOM   4499 C  CG  . ASN B 1 101 ? 20.144  -6.060  67.676  1.00 36.28  ? 101  ASN B CG  1 
ATOM   4500 O  OD1 . ASN B 1 101 ? 19.137  -5.842  68.346  1.00 33.94  ? 101  ASN B OD1 1 
ATOM   4501 N  ND2 . ASN B 1 101 ? 21.307  -6.386  68.227  1.00 35.21  ? 101  ASN B ND2 1 
ATOM   4502 N  N   . ILE B 1 102 ? 18.959  -6.333  63.194  1.00 33.42  ? 102  ILE B N   1 
ATOM   4503 C  CA  . ILE B 1 102 ? 19.090  -5.933  61.805  1.00 33.22  ? 102  ILE B CA  1 
ATOM   4504 C  C   . ILE B 1 102 ? 17.727  -5.612  61.209  1.00 38.31  ? 102  ILE B C   1 
ATOM   4505 O  O   . ILE B 1 102 ? 17.585  -4.658  60.436  1.00 37.15  ? 102  ILE B O   1 
ATOM   4506 C  CB  . ILE B 1 102 ? 19.812  -7.038  61.009  1.00 35.09  ? 102  ILE B CB  1 
ATOM   4507 C  CG1 . ILE B 1 102 ? 21.305  -7.102  61.392  1.00 35.24  ? 102  ILE B CG1 1 
ATOM   4508 C  CG2 . ILE B 1 102 ? 19.651  -6.818  59.495  1.00 35.79  ? 102  ILE B CG2 1 
ATOM   4509 C  CD1 . ILE B 1 102 ? 21.999  -8.368  60.907  1.00 34.99  ? 102  ILE B CD1 1 
ATOM   4510 N  N   . LEU B 1 103 ? 16.703  -6.384  61.569  1.00 33.73  ? 103  LEU B N   1 
ATOM   4511 C  CA  . LEU B 1 103 ? 15.404  -6.267  60.915  1.00 33.35  ? 103  LEU B CA  1 
ATOM   4512 C  C   . LEU B 1 103 ? 14.401  -5.394  61.663  1.00 36.99  ? 103  LEU B C   1 
ATOM   4513 O  O   . LEU B 1 103 ? 13.430  -4.941  61.041  1.00 38.77  ? 103  LEU B O   1 
ATOM   4514 C  CB  . LEU B 1 103 ? 14.797  -7.663  60.695  1.00 32.68  ? 103  LEU B CB  1 
ATOM   4515 C  CG  . LEU B 1 103 ? 15.666  -8.537  59.779  1.00 35.27  ? 103  LEU B CG  1 
ATOM   4516 C  CD1 . LEU B 1 103 ? 15.200  -10.005 59.756  1.00 37.42  ? 103  LEU B CD1 1 
ATOM   4517 C  CD2 . LEU B 1 103 ? 15.737  -7.973  58.343  1.00 38.83  ? 103  LEU B CD2 1 
ATOM   4518 N  N   . LEU B 1 104 ? 14.586  -5.141  62.955  1.00 34.59  ? 104  LEU B N   1 
ATOM   4519 C  CA  . LEU B 1 104 ? 13.619  -4.321  63.687  1.00 39.94  ? 104  LEU B CA  1 
ATOM   4520 C  C   . LEU B 1 104 ? 13.364  -2.977  63.011  1.00 44.40  ? 104  LEU B C   1 
ATOM   4521 O  O   . LEU B 1 104 ? 12.199  -2.536  62.989  1.00 41.94  ? 104  LEU B O   1 
ATOM   4522 C  CB  . LEU B 1 104 ? 14.088  -4.110  65.138  1.00 40.44  ? 104  LEU B CB  1 
ATOM   4523 C  CG  . LEU B 1 104 ? 13.070  -3.572  66.150  1.00 43.21  ? 104  LEU B CG  1 
ATOM   4524 C  CD1 . LEU B 1 104 ? 11.792  -4.414  66.199  1.00 44.18  ? 104  LEU B CD1 1 
ATOM   4525 C  CD2 . LEU B 1 104 ? 13.688  -3.424  67.552  1.00 46.47  ? 104  LEU B CD2 1 
ATOM   4526 N  N   . PRO B 1 105 ? 14.367  -2.298  62.449  1.00 45.87  ? 105  PRO B N   1 
ATOM   4527 C  CA  . PRO B 1 105 ? 14.099  -1.039  61.739  1.00 45.21  ? 105  PRO B CA  1 
ATOM   4528 C  C   . PRO B 1 105 ? 13.173  -1.190  60.551  1.00 46.18  ? 105  PRO B C   1 
ATOM   4529 O  O   . PRO B 1 105 ? 12.528  -0.205  60.176  1.00 49.14  ? 105  PRO B O   1 
ATOM   4530 C  CB  . PRO B 1 105 ? 15.494  -0.587  61.291  1.00 48.90  ? 105  PRO B CB  1 
ATOM   4531 C  CG  . PRO B 1 105 ? 16.412  -1.182  62.318  1.00 49.55  ? 105  PRO B CG  1 
ATOM   4532 C  CD  . PRO B 1 105 ? 15.813  -2.535  62.616  1.00 44.85  ? 105  PRO B CD  1 
ATOM   4533 N  N   . SER B 1 106 ? 13.107  -2.371  59.925  1.00 39.67  ? 106  SER B N   1 
ATOM   4534 C  CA  . SER B 1 106 ? 12.220  -2.556  58.778  1.00 40.92  ? 106  SER B CA  1 
ATOM   4535 C  C   . SER B 1 106 ? 10.761  -2.439  59.158  1.00 37.96  ? 106  SER B C   1 
ATOM   4536 O  O   . SER B 1 106 ? 9.900   -2.504  58.273  1.00 39.64  ? 106  SER B O   1 
ATOM   4537 C  CB  . SER B 1 106 ? 12.437  -3.919  58.125  1.00 39.81  ? 106  SER B CB  1 
ATOM   4538 O  OG  . SER B 1 106 ? 13.773  -4.051  57.689  1.00 50.41  ? 106  SER B OG  1 
ATOM   4539 N  N   . PHE B 1 107 ? 10.469  -2.304  60.447  1.00 37.80  ? 107  PHE B N   1 
ATOM   4540 C  CA  . PHE B 1 107 ? 9.108   -2.195  60.947  1.00 42.27  ? 107  PHE B CA  1 
ATOM   4541 C  C   . PHE B 1 107 ? 8.917   -0.927  61.777  1.00 45.16  ? 107  PHE B C   1 
ATOM   4542 O  O   . PHE B 1 107 ? 8.073   -0.878  62.669  1.00 52.13  ? 107  PHE B O   1 
ATOM   4543 C  CB  . PHE B 1 107 ? 8.749   -3.455  61.730  1.00 43.95  ? 107  PHE B CB  1 
ATOM   4544 C  CG  . PHE B 1 107 ? 8.824   -4.691  60.896  1.00 40.95  ? 107  PHE B CG  1 
ATOM   4545 C  CD1 . PHE B 1 107 ? 7.757   -5.055  60.080  1.00 41.65  ? 107  PHE B CD1 1 
ATOM   4546 C  CD2 . PHE B 1 107 ? 9.981   -5.443  60.846  1.00 38.92  ? 107  PHE B CD2 1 
ATOM   4547 C  CE1 . PHE B 1 107 ? 7.836   -6.171  59.280  1.00 41.45  ? 107  PHE B CE1 1 
ATOM   4548 C  CE2 . PHE B 1 107 ? 10.071  -6.547  60.033  1.00 36.92  ? 107  PHE B CE2 1 
ATOM   4549 C  CZ  . PHE B 1 107 ? 8.991   -6.922  59.251  1.00 40.56  ? 107  PHE B CZ  1 
ATOM   4550 N  N   . SER B 1 108 ? 9.682   0.115   61.464  1.00 46.46  ? 108  SER B N   1 
ATOM   4551 C  CA  . SER B 1 108 ? 9.513   1.434   62.060  1.00 49.91  ? 108  SER B CA  1 
ATOM   4552 C  C   . SER B 1 108 ? 8.441   2.228   61.314  1.00 55.34  ? 108  SER B C   1 
ATOM   4553 O  O   . SER B 1 108 ? 8.135   1.967   60.144  1.00 51.30  ? 108  SER B O   1 
ATOM   4554 C  CB  . SER B 1 108 ? 10.830  2.210   62.032  1.00 51.89  ? 108  SER B CB  1 
ATOM   4555 O  OG  . SER B 1 108 ? 11.154  2.623   60.709  1.00 52.36  ? 108  SER B OG  1 
ATOM   4556 N  N   . GLN B 1 109 ? 7.892   3.238   61.996  1.00 56.50  ? 109  GLN B N   1 
ATOM   4557 C  CA  . GLN B 1 109 ? 6.863   4.057   61.365  1.00 53.48  ? 109  GLN B CA  1 
ATOM   4558 C  C   . GLN B 1 109 ? 7.330   4.555   60.000  1.00 50.75  ? 109  GLN B C   1 
ATOM   4559 O  O   . GLN B 1 109 ? 6.590   4.490   59.013  1.00 51.50  ? 109  GLN B O   1 
ATOM   4560 C  CB  . GLN B 1 109 ? 6.470   5.228   62.276  1.00 61.98  ? 109  GLN B CB  1 
ATOM   4561 C  CG  . GLN B 1 109 ? 7.534   6.311   62.457  1.00 62.72  ? 109  GLN B CG  1 
ATOM   4562 C  CD  . GLN B 1 109 ? 6.928   7.714   62.577  1.00 72.36  ? 109  GLN B CD  1 
ATOM   4563 O  OE1 . GLN B 1 109 ? 7.427   8.675   61.983  1.00 74.65  ? 109  GLN B OE1 1 
ATOM   4564 N  NE2 . GLN B 1 109 ? 5.849   7.831   63.346  1.00 70.62  ? 109  GLN B NE2 1 
ATOM   4565 N  N   . GLN B 1 110 ? 8.570   5.036   59.913  1.00 53.62  ? 110  GLN B N   1 
ATOM   4566 C  CA  . GLN B 1 110 ? 9.062   5.509   58.624  1.00 55.48  ? 110  GLN B CA  1 
ATOM   4567 C  C   . GLN B 1 110 ? 9.065   4.384   57.593  1.00 54.80  ? 110  GLN B C   1 
ATOM   4568 O  O   . GLN B 1 110 ? 8.799   4.616   56.405  1.00 47.35  ? 110  GLN B O   1 
ATOM   4569 C  CB  . GLN B 1 110 ? 10.454  6.120   58.781  1.00 58.43  ? 110  GLN B CB  1 
ATOM   4570 C  CG  . GLN B 1 110 ? 10.451  7.440   59.559  1.00 69.43  ? 110  GLN B CG  1 
ATOM   4571 C  CD  . GLN B 1 110 ? 9.317   8.377   59.146  1.00 63.43  ? 110  GLN B CD  1 
ATOM   4572 O  OE1 . GLN B 1 110 ? 9.349   8.968   58.067  1.00 68.78  ? 110  GLN B OE1 1 
ATOM   4573 N  NE2 . GLN B 1 110 ? 8.314   8.520   60.012  1.00 61.53  ? 110  GLN B NE2 1 
ATOM   4574 N  N   . ALA B 1 111 ? 9.364   3.157   58.032  1.00 47.46  ? 111  ALA B N   1 
ATOM   4575 C  CA  . ALA B 1 111 ? 9.238   2.009   57.142  1.00 48.14  ? 111  ALA B CA  1 
ATOM   4576 C  C   . ALA B 1 111 ? 7.778   1.753   56.781  1.00 40.89  ? 111  ALA B C   1 
ATOM   4577 O  O   . ALA B 1 111 ? 7.461   1.469   55.619  1.00 44.21  ? 111  ALA B O   1 
ATOM   4578 C  CB  . ALA B 1 111 ? 9.859   0.775   57.794  1.00 47.03  ? 111  ALA B CB  1 
ATOM   4579 N  N   . MET B 1 112 ? 6.879   1.847   57.758  1.00 42.47  ? 112  MET B N   1 
ATOM   4580 C  CA  . MET B 1 112 ? 5.471   1.587   57.477  1.00 42.40  ? 112  MET B CA  1 
ATOM   4581 C  C   . MET B 1 112 ? 4.900   2.626   56.522  1.00 42.48  ? 112  MET B C   1 
ATOM   4582 O  O   . MET B 1 112 ? 4.127   2.291   55.615  1.00 39.42  ? 112  MET B O   1 
ATOM   4583 C  CB  . MET B 1 112 ? 4.668   1.544   58.767  1.00 46.08  ? 112  MET B CB  1 
ATOM   4584 C  CG  . MET B 1 112 ? 4.994   0.321   59.602  1.00 52.95  ? 112  MET B CG  1 
ATOM   4585 S  SD  . MET B 1 112 ? 4.375   -1.233  58.918  1.00 41.88  ? 112  MET B SD  1 
ATOM   4586 C  CE  . MET B 1 112 ? 3.123   -0.696  57.777  1.00 43.63  ? 112  MET B CE  1 
ATOM   4587 N  N   . LYS B 1 113 ? 5.262   3.896   56.707  1.00 38.70  ? 113  LYS B N   1 
ATOM   4588 C  CA  . LYS B 1 113 ? 4.884   4.899   55.718  1.00 38.70  ? 113  LYS B CA  1 
ATOM   4589 C  C   . LYS B 1 113 ? 5.392   4.523   54.339  1.00 38.35  ? 113  LYS B C   1 
ATOM   4590 O  O   . LYS B 1 113 ? 4.711   4.777   53.339  1.00 38.74  ? 113  LYS B O   1 
ATOM   4591 C  CB  . LYS B 1 113 ? 5.401   6.279   56.116  1.00 41.76  ? 113  LYS B CB  1 
ATOM   4592 C  CG  . LYS B 1 113 ? 4.816   6.764   57.420  1.00 42.22  ? 113  LYS B CG  1 
ATOM   4593 C  CD  . LYS B 1 113 ? 5.404   8.098   57.836  1.00 43.49  ? 113  LYS B CD  1 
ATOM   4594 C  CE  . LYS B 1 113 ? 4.740   8.581   59.122  1.00 54.69  ? 113  LYS B CE  1 
ATOM   4595 N  NZ  . LYS B 1 113 ? 5.322   9.849   59.644  1.00 57.10  ? 113  LYS B NZ  1 
ATOM   4596 N  N   . GLY B 1 114 ? 6.571   3.901   54.269  1.00 39.57  ? 114  GLY B N   1 
ATOM   4597 C  CA  . GLY B 1 114 ? 7.123   3.515   52.984  1.00 41.57  ? 114  GLY B CA  1 
ATOM   4598 C  C   . GLY B 1 114 ? 6.481   2.288   52.371  1.00 39.64  ? 114  GLY B C   1 
ATOM   4599 O  O   . GLY B 1 114 ? 6.517   2.123   51.144  1.00 41.95  ? 114  GLY B O   1 
ATOM   4600 N  N   . TYR B 1 115 ? 5.909   1.401   53.198  1.00 35.82  ? 115  TYR B N   1 
ATOM   4601 C  CA  . TYR B 1 115 ? 5.199   0.227   52.679  1.00 35.79  ? 115  TYR B CA  1 
ATOM   4602 C  C   . TYR B 1 115 ? 3.800   0.568   52.200  1.00 34.28  ? 115  TYR B C   1 
ATOM   4603 O  O   . TYR B 1 115 ? 3.215   -0.195  51.418  1.00 33.89  ? 115  TYR B O   1 
ATOM   4604 C  CB  . TYR B 1 115 ? 5.061   -0.871  53.745  1.00 34.73  ? 115  TYR B CB  1 
ATOM   4605 C  CG  . TYR B 1 115 ? 6.356   -1.448  54.272  1.00 34.84  ? 115  TYR B CG  1 
ATOM   4606 C  CD1 . TYR B 1 115 ? 7.402   -1.766  53.414  1.00 36.22  ? 115  TYR B CD1 1 
ATOM   4607 C  CD2 . TYR B 1 115 ? 6.530   -1.676  55.633  1.00 37.62  ? 115  TYR B CD2 1 
ATOM   4608 C  CE1 . TYR B 1 115 ? 8.597   -2.302  53.912  1.00 41.21  ? 115  TYR B CE1 1 
ATOM   4609 C  CE2 . TYR B 1 115 ? 7.716   -2.210  56.136  1.00 38.37  ? 115  TYR B CE2 1 
ATOM   4610 C  CZ  . TYR B 1 115 ? 8.740   -2.522  55.272  1.00 40.59  ? 115  TYR B CZ  1 
ATOM   4611 O  OH  . TYR B 1 115 ? 9.912   -3.046  55.785  1.00 39.29  ? 115  TYR B OH  1 
ATOM   4612 N  N   . HIS B 1 116 ? 3.263   1.695   52.653  1.00 32.58  ? 116  HIS B N   1 
ATOM   4613 C  CA  . HIS B 1 116 ? 1.847   1.990   52.462  1.00 33.38  ? 116  HIS B CA  1 
ATOM   4614 C  C   . HIS B 1 116 ? 1.418   1.921   51.000  1.00 35.70  ? 116  HIS B C   1 
ATOM   4615 O  O   . HIS B 1 116 ? 0.369   1.350   50.680  1.00 34.60  ? 116  HIS B O   1 
ATOM   4616 C  CB  . HIS B 1 116 ? 1.523   3.364   53.027  1.00 35.16  ? 116  HIS B CB  1 
ATOM   4617 C  CG  . HIS B 1 116 ? 0.084   3.716   52.883  1.00 34.85  ? 116  HIS B CG  1 
ATOM   4618 N  ND1 . HIS B 1 116 ? -0.866  3.335   53.804  1.00 33.44  ? 116  HIS B ND1 1 
ATOM   4619 C  CD2 . HIS B 1 116 ? -0.576  4.374   51.905  1.00 34.50  ? 116  HIS B CD2 1 
ATOM   4620 C  CE1 . HIS B 1 116 ? -2.052  3.750   53.401  1.00 33.64  ? 116  HIS B CE1 1 
ATOM   4621 N  NE2 . HIS B 1 116 ? -1.901  4.384   52.252  1.00 34.32  ? 116  HIS B NE2 1 
ATOM   4622 N  N   . ALA B 1 117 ? 2.162   2.571   50.102  1.00 33.35  ? 117  ALA B N   1 
ATOM   4623 C  CA  . ALA B 1 117 ? 1.716   2.621   48.709  1.00 36.56  ? 117  ALA B CA  1 
ATOM   4624 C  C   . ALA B 1 117 ? 1.579   1.222   48.112  1.00 35.96  ? 117  ALA B C   1 
ATOM   4625 O  O   . ALA B 1 117 ? 0.649   0.958   47.340  1.00 33.30  ? 117  ALA B O   1 
ATOM   4626 C  CB  . ALA B 1 117 ? 2.674   3.467   47.863  1.00 37.29  ? 117  ALA B CB  1 
ATOM   4627 N  N   . MET B 1 118 ? 2.522   0.325   48.415  1.00 33.28  ? 118  MET B N   1 
ATOM   4628 C  CA  . MET B 1 118 ? 2.451   -1.023  47.859  1.00 34.47  ? 118  MET B CA  1 
ATOM   4629 C  C   . MET B 1 118 ? 1.337   -1.840  48.516  1.00 33.18  ? 118  MET B C   1 
ATOM   4630 O  O   . MET B 1 118 ? 0.772   -2.740  47.889  1.00 33.41  ? 118  MET B O   1 
ATOM   4631 C  CB  . MET B 1 118 ? 3.807   -1.714  48.014  1.00 35.80  ? 118  MET B CB  1 
ATOM   4632 C  CG  . MET B 1 118 ? 4.869   -1.238  47.017  1.00 34.87  ? 118  MET B CG  1 
ATOM   4633 S  SD  . MET B 1 118 ? 6.505   -1.919  47.416  1.00 51.61  ? 118  MET B SD  1 
ATOM   4634 C  CE  . MET B 1 118 ? 7.423   -1.580  45.906  1.00 49.82  ? 118  MET B CE  1 
ATOM   4635 N  N   . MET B 1 119 ? 1.044   -1.585  49.789  1.00 32.74  ? 119  MET B N   1 
ATOM   4636 C  CA  . MET B 1 119 ? -0.163  -2.155  50.391  1.00 33.52  ? 119  MET B CA  1 
ATOM   4637 C  C   . MET B 1 119 ? -1.408  -1.740  49.611  1.00 31.53  ? 119  MET B C   1 
ATOM   4638 O  O   . MET B 1 119 ? -2.272  -2.574  49.296  1.00 32.68  ? 119  MET B O   1 
ATOM   4639 C  CB  . MET B 1 119 ? -0.235  -1.678  51.829  1.00 32.29  ? 119  MET B CB  1 
ATOM   4640 C  CG  . MET B 1 119 ? 0.788   -2.371  52.731  1.00 31.63  ? 119  MET B CG  1 
ATOM   4641 S  SD  . MET B 1 119 ? 0.282   -2.265  54.445  1.00 32.74  ? 119  MET B SD  1 
ATOM   4642 C  CE  . MET B 1 119 ? 1.828   -2.754  55.230  1.00 30.30  ? 119  MET B CE  1 
ATOM   4643 N  N   . VAL B 1 120 ? -1.495  -0.458  49.253  1.00 30.71  ? 120  VAL B N   1 
ATOM   4644 C  CA  . VAL B 1 120 ? -2.645  0.026   48.498  1.00 33.68  ? 120  VAL B CA  1 
ATOM   4645 C  C   . VAL B 1 120 ? -2.730  -0.680  47.151  1.00 32.41  ? 120  VAL B C   1 
ATOM   4646 O  O   . VAL B 1 120 ? -3.822  -1.042  46.703  1.00 33.66  ? 120  VAL B O   1 
ATOM   4647 C  CB  . VAL B 1 120 ? -2.572  1.561   48.339  1.00 35.13  ? 120  VAL B CB  1 
ATOM   4648 C  CG1 . VAL B 1 120 ? -3.660  2.059   47.387  1.00 35.62  ? 120  VAL B CG1 1 
ATOM   4649 C  CG2 . VAL B 1 120 ? -2.724  2.261   49.690  1.00 32.04  ? 120  VAL B CG2 1 
ATOM   4650 N  N   . ASP B 1 121 ? -1.579  -0.893  46.494  1.00 31.81  ? 121  ASP B N   1 
ATOM   4651 C  CA  . ASP B 1 121 ? -1.534  -1.570  45.196  1.00 32.67  ? 121  ASP B CA  1 
ATOM   4652 C  C   . ASP B 1 121 ? -2.284  -2.907  45.233  1.00 33.36  ? 121  ASP B C   1 
ATOM   4653 O  O   . ASP B 1 121 ? -3.172  -3.159  44.409  1.00 35.10  ? 121  ASP B O   1 
ATOM   4654 C  CB  . ASP B 1 121 ? -0.058  -1.757  44.786  1.00 31.10  ? 121  ASP B CB  1 
ATOM   4655 C  CG  . ASP B 1 121 ? 0.120   -2.403  43.404  1.00 37.74  ? 121  ASP B CG  1 
ATOM   4656 O  OD1 . ASP B 1 121 ? -0.309  -3.560  43.213  1.00 34.20  ? 121  ASP B OD1 1 
ATOM   4657 O  OD2 . ASP B 1 121 ? 0.748   -1.769  42.516  1.00 35.52  ? 121  ASP B OD2 1 
ATOM   4658 N  N   . ILE B 1 122 ? -1.971  -3.759  46.219  1.00 32.33  ? 122  ILE B N   1 
ATOM   4659 C  CA  . ILE B 1 122 ? -2.604  -5.076  46.303  1.00 32.03  ? 122  ILE B CA  1 
ATOM   4660 C  C   . ILE B 1 122 ? -4.063  -4.942  46.734  1.00 34.55  ? 122  ILE B C   1 
ATOM   4661 O  O   . ILE B 1 122 ? -4.944  -5.695  46.277  1.00 32.90  ? 122  ILE B O   1 
ATOM   4662 C  CB  . ILE B 1 122 ? -1.815  -5.982  47.272  1.00 31.67  ? 122  ILE B CB  1 
ATOM   4663 C  CG1 . ILE B 1 122 ? -0.314  -6.024  46.915  1.00 30.00  ? 122  ILE B CG1 1 
ATOM   4664 C  CG2 . ILE B 1 122 ? -2.432  -7.384  47.316  1.00 28.78  ? 122  ILE B CG2 1 
ATOM   4665 C  CD1 . ILE B 1 122 ? -0.029  -6.397  45.457  1.00 30.74  ? 122  ILE B CD1 1 
ATOM   4666 N  N   . ALA B 1 123 ? -4.335  -4.008  47.647  1.00 30.64  ? 123  ALA B N   1 
ATOM   4667 C  CA  . ALA B 1 123 ? -5.703  -3.795  48.117  1.00 32.40  ? 123  ALA B CA  1 
ATOM   4668 C  C   . ALA B 1 123 ? -6.600  -3.358  46.972  1.00 30.40  ? 123  ALA B C   1 
ATOM   4669 O  O   . ALA B 1 123 ? -7.748  -3.798  46.870  1.00 32.48  ? 123  ALA B O   1 
ATOM   4670 C  CB  . ALA B 1 123 ? -5.721  -2.761  49.249  1.00 32.70  ? 123  ALA B CB  1 
ATOM   4671 N  N   . VAL B 1 124 ? -6.092  -2.495  46.092  1.00 31.64  ? 124  VAL B N   1 
ATOM   4672 C  CA  . VAL B 1 124 ? -6.883  -2.084  44.931  1.00 33.02  ? 124  VAL B CA  1 
ATOM   4673 C  C   . VAL B 1 124 ? -7.156  -3.275  44.020  1.00 31.86  ? 124  VAL B C   1 
ATOM   4674 O  O   . VAL B 1 124 ? -8.256  -3.412  43.462  1.00 32.24  ? 124  VAL B O   1 
ATOM   4675 C  CB  . VAL B 1 124 ? -6.171  -0.947  44.178  1.00 32.95  ? 124  VAL B CB  1 
ATOM   4676 C  CG1 . VAL B 1 124 ? -6.829  -0.724  42.804  1.00 34.01  ? 124  VAL B CG1 1 
ATOM   4677 C  CG2 . VAL B 1 124 ? -6.210  0.331   45.009  1.00 31.52  ? 124  VAL B CG2 1 
ATOM   4678 N  N   . GLN B 1 125 ? -6.170  -4.165  43.861  1.00 31.38  ? 125  GLN B N   1 
ATOM   4679 C  CA  . GLN B 1 125 ? -6.412  -5.370  43.065  1.00 31.65  ? 125  GLN B CA  1 
ATOM   4680 C  C   . GLN B 1 125 ? -7.540  -6.200  43.657  1.00 34.50  ? 125  GLN B C   1 
ATOM   4681 O  O   . GLN B 1 125 ? -8.360  -6.758  42.917  1.00 31.46  ? 125  GLN B O   1 
ATOM   4682 C  CB  . GLN B 1 125 ? -5.135  -6.206  42.949  1.00 29.35  ? 125  GLN B CB  1 
ATOM   4683 C  CG  . GLN B 1 125 ? -4.038  -5.535  42.137  1.00 30.51  ? 125  GLN B CG  1 
ATOM   4684 C  CD  . GLN B 1 125 ? -2.897  -6.498  41.851  1.00 32.39  ? 125  GLN B CD  1 
ATOM   4685 O  OE1 . GLN B 1 125 ? -3.122  -7.619  41.397  1.00 30.61  ? 125  GLN B OE1 1 
ATOM   4686 N  NE2 . GLN B 1 125 ? -1.660  -6.071  42.139  1.00 31.38  ? 125  GLN B NE2 1 
ATOM   4687 N  N   . LEU B 1 126 ? -7.622  -6.273  44.996  1.00 32.09  ? 126  LEU B N   1 
ATOM   4688 C  CA  . LEU B 1 126 ? -8.707  -7.023  45.625  1.00 30.40  ? 126  LEU B CA  1 
ATOM   4689 C  C   . LEU B 1 126 ? -10.055 -6.384  45.323  1.00 30.91  ? 126  LEU B C   1 
ATOM   4690 O  O   . LEU B 1 126 ? -11.000 -7.057  44.886  1.00 32.08  ? 126  LEU B O   1 
ATOM   4691 C  CB  . LEU B 1 126 ? -8.490  -7.104  47.147  1.00 29.92  ? 126  LEU B CB  1 
ATOM   4692 C  CG  . LEU B 1 126 ? -9.690  -7.698  47.922  1.00 33.56  ? 126  LEU B CG  1 
ATOM   4693 C  CD1 . LEU B 1 126 ? -9.756  -9.190  47.688  1.00 34.74  ? 126  LEU B CD1 1 
ATOM   4694 C  CD2 . LEU B 1 126 ? -9.578  -7.420  49.434  1.00 32.91  ? 126  LEU B CD2 1 
ATOM   4695 N  N   . VAL B 1 127 ? -10.168 -5.080  45.565  1.00 31.27  ? 127  VAL B N   1 
ATOM   4696 C  CA  . VAL B 1 127 ? -11.433 -4.388  45.323  1.00 30.86  ? 127  VAL B CA  1 
ATOM   4697 C  C   . VAL B 1 127 ? -11.858 -4.534  43.860  1.00 33.12  ? 127  VAL B C   1 
ATOM   4698 O  O   . VAL B 1 127 ? -13.046 -4.723  43.553  1.00 32.38  ? 127  VAL B O   1 
ATOM   4699 C  CB  . VAL B 1 127 ? -11.298 -2.911  45.739  1.00 28.51  ? 127  VAL B CB  1 
ATOM   4700 C  CG1 . VAL B 1 127 ? -12.532 -2.103  45.347  1.00 33.82  ? 127  VAL B CG1 1 
ATOM   4701 C  CG2 . VAL B 1 127 ? -11.042 -2.805  47.260  1.00 30.70  ? 127  VAL B CG2 1 
ATOM   4702 N  N   . GLN B 1 128 ? -10.905 -4.433  42.932  1.00 30.92  ? 128  GLN B N   1 
ATOM   4703 C  CA  . GLN B 1 128 ? -11.267 -4.525  41.519  1.00 31.54  ? 128  GLN B CA  1 
ATOM   4704 C  C   . GLN B 1 128 ? -11.725 -5.930  41.168  1.00 32.40  ? 128  GLN B C   1 
ATOM   4705 O  O   . GLN B 1 128 ? -12.650 -6.108  40.362  1.00 32.88  ? 128  GLN B O   1 
ATOM   4706 C  CB  . GLN B 1 128 ? -10.090 -4.096  40.645  1.00 31.48  ? 128  GLN B CB  1 
ATOM   4707 C  CG  . GLN B 1 128 ? -9.845  -2.610  40.807  1.00 38.15  ? 128  GLN B CG  1 
ATOM   4708 C  CD  . GLN B 1 128 ? -9.012  -2.009  39.712  1.00 50.02  ? 128  GLN B CD  1 
ATOM   4709 O  OE1 . GLN B 1 128 ? -7.885  -2.446  39.468  1.00 47.79  ? 128  GLN B OE1 1 
ATOM   4710 N  NE2 . GLN B 1 128 ? -9.541  -0.965  39.066  1.00 49.20  ? 128  GLN B NE2 1 
ATOM   4711 N  N   . LYS B 1 129 ? -11.110 -6.949  41.773  1.00 30.47  ? 129  LYS B N   1 
ATOM   4712 C  CA  . LYS B 1 129 ? -11.605 -8.298  41.545  1.00 32.60  ? 129  LYS B CA  1 
ATOM   4713 C  C   . LYS B 1 129 ? -13.079 -8.396  41.918  1.00 34.03  ? 129  LYS B C   1 
ATOM   4714 O  O   . LYS B 1 129 ? -13.899 -8.904  41.147  1.00 33.90  ? 129  LYS B O   1 
ATOM   4715 C  CB  . LYS B 1 129 ? -10.781 -9.316  42.332  1.00 34.25  ? 129  LYS B CB  1 
ATOM   4716 C  CG  . LYS B 1 129 ? -11.397 -10.712 42.259  1.00 34.11  ? 129  LYS B CG  1 
ATOM   4717 C  CD  . LYS B 1 129 ? -10.476 -11.786 42.784  1.00 35.23  ? 129  LYS B CD  1 
ATOM   4718 C  CE  . LYS B 1 129 ? -11.201 -13.130 42.859  1.00 38.12  ? 129  LYS B CE  1 
ATOM   4719 N  NZ  . LYS B 1 129 ? -10.280 -14.261 43.206  1.00 36.20  ? 129  LYS B NZ  1 
ATOM   4720 N  N   . TRP B 1 130 ? -13.435 -7.901  43.102  1.00 33.23  ? 130  TRP B N   1 
ATOM   4721 C  CA  . TRP B 1 130 ? -14.814 -8.016  43.568  1.00 31.87  ? 130  TRP B CA  1 
ATOM   4722 C  C   . TRP B 1 130 ? -15.755 -7.113  42.778  1.00 31.92  ? 130  TRP B C   1 
ATOM   4723 O  O   . TRP B 1 130 ? -16.920 -7.472  42.562  1.00 33.66  ? 130  TRP B O   1 
ATOM   4724 C  CB  . TRP B 1 130 ? -14.876 -7.697  45.066  1.00 33.66  ? 130  TRP B CB  1 
ATOM   4725 C  CG  . TRP B 1 130 ? -14.171 -8.707  45.912  1.00 35.82  ? 130  TRP B CG  1 
ATOM   4726 C  CD1 . TRP B 1 130 ? -13.559 -9.859  45.485  1.00 31.68  ? 130  TRP B CD1 1 
ATOM   4727 C  CD2 . TRP B 1 130 ? -14.019 -8.676  47.335  1.00 30.28  ? 130  TRP B CD2 1 
ATOM   4728 N  NE1 . TRP B 1 130 ? -13.034 -10.539 46.559  1.00 33.76  ? 130  TRP B NE1 1 
ATOM   4729 C  CE2 . TRP B 1 130 ? -13.302 -9.836  47.705  1.00 34.04  ? 130  TRP B CE2 1 
ATOM   4730 C  CE3 . TRP B 1 130 ? -14.414 -7.773  48.338  1.00 29.41  ? 130  TRP B CE3 1 
ATOM   4731 C  CZ2 . TRP B 1 130 ? -12.962 -10.115 49.026  1.00 30.88  ? 130  TRP B CZ2 1 
ATOM   4732 C  CZ3 . TRP B 1 130 ? -14.077 -8.068  49.670  1.00 30.00  ? 130  TRP B CZ3 1 
ATOM   4733 C  CH2 . TRP B 1 130 ? -13.362 -9.218  49.989  1.00 31.93  ? 130  TRP B CH2 1 
ATOM   4734 N  N   . GLU B 1 131 ? -15.293 -5.923  42.368  1.00 32.39  ? 131  GLU B N   1 
ATOM   4735 C  CA  . GLU B 1 131 ? -16.121 -5.082  41.507  1.00 34.59  ? 131  GLU B CA  1 
ATOM   4736 C  C   . GLU B 1 131 ? -16.451 -5.788  40.202  1.00 36.53  ? 131  GLU B C   1 
ATOM   4737 O  O   . GLU B 1 131 ? -17.478 -5.494  39.579  1.00 35.41  ? 131  GLU B O   1 
ATOM   4738 C  CB  . GLU B 1 131 ? -15.432 -3.751  41.175  1.00 36.03  ? 131  GLU B CB  1 
ATOM   4739 C  CG  . GLU B 1 131 ? -15.171 -2.839  42.370  1.00 36.87  ? 131  GLU B CG  1 
ATOM   4740 C  CD  . GLU B 1 131 ? -16.401 -2.051  42.788  1.00 40.27  ? 131  GLU B CD  1 
ATOM   4741 O  OE1 . GLU B 1 131 ? -17.530 -2.507  42.495  1.00 40.85  ? 131  GLU B OE1 1 
ATOM   4742 O  OE2 . GLU B 1 131 ? -16.237 -0.984  43.420  1.00 43.55  ? 131  GLU B OE2 1 
ATOM   4743 N  N   . ARG B 1 132 ? -15.602 -6.714  39.769  1.00 31.38  ? 132  ARG B N   1 
ATOM   4744 C  CA  . ARG B 1 132 ? -15.743 -7.297  38.440  1.00 33.78  ? 132  ARG B CA  1 
ATOM   4745 C  C   . ARG B 1 132 ? -16.505 -8.612  38.448  1.00 34.67  ? 132  ARG B C   1 
ATOM   4746 O  O   . ARG B 1 132 ? -16.704 -9.203  37.381  1.00 34.65  ? 132  ARG B O   1 
ATOM   4747 C  CB  . ARG B 1 132 ? -14.358 -7.473  37.796  1.00 32.69  ? 132  ARG B CB  1 
ATOM   4748 C  CG  . ARG B 1 132 ? -13.761 -6.130  37.417  1.00 29.97  ? 132  ARG B CG  1 
ATOM   4749 C  CD  . ARG B 1 132 ? -12.289 -6.197  37.086  1.00 33.59  ? 132  ARG B CD  1 
ATOM   4750 N  NE  . ARG B 1 132 ? -11.832 -4.882  36.658  1.00 31.19  ? 132  ARG B NE  1 
ATOM   4751 C  CZ  . ARG B 1 132 ? -10.562 -4.521  36.528  1.00 35.64  ? 132  ARG B CZ  1 
ATOM   4752 N  NH1 . ARG B 1 132 ? -9.580  -5.327  36.874  1.00 34.02  ? 132  ARG B NH1 1 
ATOM   4753 N  NH2 . ARG B 1 132 ? -10.275 -3.320  36.024  1.00 39.00  ? 132  ARG B NH2 1 
ATOM   4754 N  N   . LEU B 1 133 ? -16.944 -9.079  39.615  1.00 34.11  ? 133  LEU B N   1 
ATOM   4755 C  CA  . LEU B 1 133 ? -17.763 -10.278 39.670  1.00 35.00  ? 133  LEU B CA  1 
ATOM   4756 C  C   . LEU B 1 133 ? -19.127 -10.023 39.030  1.00 35.76  ? 133  LEU B C   1 
ATOM   4757 O  O   . LEU B 1 133 ? -19.656 -8.907  39.061  1.00 37.12  ? 133  LEU B O   1 
ATOM   4758 C  CB  . LEU B 1 133 ? -17.936 -10.730 41.118  1.00 37.49  ? 133  LEU B CB  1 
ATOM   4759 C  CG  . LEU B 1 133 ? -16.651 -11.110 41.852  1.00 32.32  ? 133  LEU B CG  1 
ATOM   4760 C  CD1 . LEU B 1 133 ? -16.948 -11.511 43.301  1.00 36.29  ? 133  LEU B CD1 1 
ATOM   4761 C  CD2 . LEU B 1 133 ? -15.952 -12.255 41.126  1.00 36.54  ? 133  LEU B CD2 1 
ATOM   4762 N  N   . ASN B 1 134 ? -19.687 -11.069 38.428  1.00 32.92  ? 134  ASN B N   1 
ATOM   4763 C  CA  . ASN B 1 134 ? -20.997 -10.973 37.798  1.00 36.32  ? 134  ASN B CA  1 
ATOM   4764 C  C   . ASN B 1 134 ? -22.104 -11.157 38.827  1.00 40.29  ? 134  ASN B C   1 
ATOM   4765 O  O   . ASN B 1 134 ? -21.872 -11.578 39.959  1.00 35.78  ? 134  ASN B O   1 
ATOM   4766 C  CB  . ASN B 1 134 ? -21.144 -12.016 36.697  1.00 36.75  ? 134  ASN B CB  1 
ATOM   4767 C  CG  . ASN B 1 134 ? -20.100 -11.856 35.624  1.00 36.93  ? 134  ASN B CG  1 
ATOM   4768 O  OD1 . ASN B 1 134 ? -20.067 -10.838 34.918  1.00 35.28  ? 134  ASN B OD1 1 
ATOM   4769 N  ND2 . ASN B 1 134 ? -19.202 -12.830 35.528  1.00 37.51  ? 134  ASN B ND2 1 
ATOM   4770 N  N   . ALA B 1 135 ? -23.331 -10.858 38.395  1.00 41.14  ? 135  ALA B N   1 
ATOM   4771 C  CA  . ALA B 1 135 ? -24.524 -11.063 39.205  1.00 46.69  ? 135  ALA B CA  1 
ATOM   4772 C  C   . ALA B 1 135 ? -24.478 -12.392 39.943  1.00 39.62  ? 135  ALA B C   1 
ATOM   4773 O  O   . ALA B 1 135 ? -24.303 -13.455 39.338  1.00 42.81  ? 135  ALA B O   1 
ATOM   4774 C  CB  . ALA B 1 135 ? -25.767 -11.004 38.309  1.00 47.24  ? 135  ALA B CB  1 
ATOM   4775 N  N   . ASP B 1 136 ? -24.617 -12.322 41.259  1.00 46.07  ? 136  ASP B N   1 
ATOM   4776 C  CA  . ASP B 1 136 ? -24.816 -13.460 42.148  1.00 48.13  ? 136  ASP B CA  1 
ATOM   4777 C  C   . ASP B 1 136 ? -23.648 -14.446 42.184  1.00 45.84  ? 136  ASP B C   1 
ATOM   4778 O  O   . ASP B 1 136 ? -23.799 -15.543 42.732  1.00 47.11  ? 136  ASP B O   1 
ATOM   4779 C  CB  . ASP B 1 136 ? -26.126 -14.181 41.814  1.00 56.12  ? 136  ASP B CB  1 
ATOM   4780 C  CG  . ASP B 1 136 ? -27.341 -13.386 42.261  1.00 56.17  ? 136  ASP B CG  1 
ATOM   4781 O  OD1 . ASP B 1 136 ? -27.319 -12.874 43.408  1.00 56.63  ? 136  ASP B OD1 1 
ATOM   4782 O  OD2 . ASP B 1 136 ? -28.294 -13.249 41.463  1.00 55.15  ? 136  ASP B OD2 1 
ATOM   4783 N  N   . GLU B 1 137 ? -22.490 -14.097 41.622  1.00 37.03  ? 137  GLU B N   1 
ATOM   4784 C  CA  . GLU B 1 137 ? -21.260 -14.787 41.998  1.00 35.12  ? 137  GLU B CA  1 
ATOM   4785 C  C   . GLU B 1 137 ? -20.897 -14.429 43.442  1.00 38.18  ? 137  GLU B C   1 
ATOM   4786 O  O   . GLU B 1 137 ? -21.316 -13.397 43.973  1.00 42.24  ? 137  GLU B O   1 
ATOM   4787 C  CB  . GLU B 1 137 ? -20.117 -14.412 41.043  1.00 34.26  ? 137  GLU B CB  1 
ATOM   4788 C  CG  . GLU B 1 137 ? -20.424 -14.842 39.601  1.00 40.33  ? 137  GLU B CG  1 
ATOM   4789 C  CD  . GLU B 1 137 ? -19.332 -14.512 38.593  1.00 38.31  ? 137  GLU B CD  1 
ATOM   4790 O  OE1 . GLU B 1 137 ? -18.433 -13.690 38.881  1.00 36.16  ? 137  GLU B OE1 1 
ATOM   4791 O  OE2 . GLU B 1 137 ? -19.392 -15.078 37.483  1.00 43.61  ? 137  GLU B OE2 1 
ATOM   4792 N  N   . HIS B 1 138 ? -20.102 -15.279 44.081  1.00 39.05  ? 138  HIS B N   1 
ATOM   4793 C  CA  . HIS B 1 138 ? -19.756 -15.043 45.477  1.00 34.80  ? 138  HIS B CA  1 
ATOM   4794 C  C   . HIS B 1 138 ? -18.242 -14.951 45.628  1.00 35.03  ? 138  HIS B C   1 
ATOM   4795 O  O   . HIS B 1 138 ? -17.483 -15.123 44.671  1.00 33.28  ? 138  HIS B O   1 
ATOM   4796 C  CB  . HIS B 1 138 ? -20.352 -16.128 46.383  1.00 36.22  ? 138  HIS B CB  1 
ATOM   4797 C  CG  . HIS B 1 138 ? -19.830 -17.499 46.104  1.00 37.93  ? 138  HIS B CG  1 
ATOM   4798 N  ND1 . HIS B 1 138 ? -20.448 -18.361 45.224  1.00 41.57  ? 138  HIS B ND1 1 
ATOM   4799 C  CD2 . HIS B 1 138 ? -18.742 -18.156 46.577  1.00 35.99  ? 138  HIS B CD2 1 
ATOM   4800 C  CE1 . HIS B 1 138 ? -19.771 -19.495 45.178  1.00 45.22  ? 138  HIS B CE1 1 
ATOM   4801 N  NE2 . HIS B 1 138 ? -18.726 -19.393 45.981  1.00 41.04  ? 138  HIS B NE2 1 
ATOM   4802 N  N   . ILE B 1 139 ? -17.824 -14.639 46.849  1.00 33.19  ? 139  ILE B N   1 
ATOM   4803 C  CA  . ILE B 1 139 ? -16.422 -14.452 47.205  1.00 33.77  ? 139  ILE B CA  1 
ATOM   4804 C  C   . ILE B 1 139 ? -16.029 -15.585 48.133  1.00 33.10  ? 139  ILE B C   1 
ATOM   4805 O  O   . ILE B 1 139 ? -16.744 -15.876 49.096  1.00 33.20  ? 139  ILE B O   1 
ATOM   4806 C  CB  . ILE B 1 139 ? -16.179 -13.095 47.892  1.00 34.73  ? 139  ILE B CB  1 
ATOM   4807 C  CG1 . ILE B 1 139 ? -16.388 -11.926 46.918  1.00 35.04  ? 139  ILE B CG1 1 
ATOM   4808 C  CG2 . ILE B 1 139 ? -14.780 -13.079 48.558  1.00 31.36  ? 139  ILE B CG2 1 
ATOM   4809 C  CD1 . ILE B 1 139 ? -16.839 -10.644 47.590  1.00 31.83  ? 139  ILE B CD1 1 
ATOM   4810 N  N   . GLU B 1 140 ? -14.898 -16.227 47.837  1.00 31.27  ? 140  GLU B N   1 
ATOM   4811 C  CA  . GLU B 1 140 ? -14.279 -17.179 48.748  1.00 34.61  ? 140  GLU B CA  1 
ATOM   4812 C  C   . GLU B 1 140 ? -13.347 -16.378 49.649  1.00 33.16  ? 140  GLU B C   1 
ATOM   4813 O  O   . GLU B 1 140 ? -12.287 -15.912 49.206  1.00 33.69  ? 140  GLU B O   1 
ATOM   4814 C  CB  . GLU B 1 140 ? -13.542 -18.269 47.970  1.00 35.83  ? 140  GLU B CB  1 
ATOM   4815 C  CG  . GLU B 1 140 ? -14.478 -19.032 47.035  1.00 39.35  ? 140  GLU B CG  1 
ATOM   4816 C  CD  . GLU B 1 140 ? -13.754 -20.089 46.212  1.00 41.63  ? 140  GLU B CD  1 
ATOM   4817 O  OE1 . GLU B 1 140 ? -12.574 -19.866 45.876  1.00 43.03  ? 140  GLU B OE1 1 
ATOM   4818 O  OE2 . GLU B 1 140 ? -14.367 -21.130 45.898  1.00 42.35  ? 140  GLU B OE2 1 
ATOM   4819 N  N   . VAL B 1 141 ? -13.753 -16.190 50.898  1.00 30.11  ? 141  VAL B N   1 
ATOM   4820 C  CA  . VAL B 1 141 ? -13.152 -15.138 51.714  1.00 30.03  ? 141  VAL B CA  1 
ATOM   4821 C  C   . VAL B 1 141 ? -11.708 -15.486 52.059  1.00 27.67  ? 141  VAL B C   1 
ATOM   4822 O  O   . VAL B 1 141 ? -10.808 -14.714 51.699  1.00 30.76  ? 141  VAL B O   1 
ATOM   4823 C  CB  . VAL B 1 141 ? -13.984 -14.849 52.970  1.00 32.62  ? 141  VAL B CB  1 
ATOM   4824 C  CG1 . VAL B 1 141 ? -13.227 -13.890 53.873  1.00 31.67  ? 141  VAL B CG1 1 
ATOM   4825 C  CG2 . VAL B 1 141 ? -15.341 -14.228 52.556  1.00 31.56  ? 141  VAL B CG2 1 
ATOM   4826 N  N   . PRO B 1 142 ? -11.435 -16.598 52.750  1.00 29.31  ? 142  PRO B N   1 
ATOM   4827 C  CA  . PRO B 1 142 ? -10.041 -16.880 53.140  1.00 30.78  ? 142  PRO B CA  1 
ATOM   4828 C  C   . PRO B 1 142 ? -9.127  -17.032 51.941  1.00 33.40  ? 142  PRO B C   1 
ATOM   4829 O  O   . PRO B 1 142 ? -7.950  -16.634 51.995  1.00 30.05  ? 142  PRO B O   1 
ATOM   4830 C  CB  . PRO B 1 142 ? -10.142 -18.179 53.954  1.00 32.36  ? 142  PRO B CB  1 
ATOM   4831 C  CG  . PRO B 1 142 ? -11.496 -18.773 53.597  1.00 34.69  ? 142  PRO B CG  1 
ATOM   4832 C  CD  . PRO B 1 142 ? -12.379 -17.578 53.313  1.00 31.87  ? 142  PRO B CD  1 
ATOM   4833 N  N   . GLU B 1 143 ? -9.654  -17.570 50.841  1.00 31.21  ? 143  GLU B N   1 
ATOM   4834 C  CA  . GLU B 1 143 ? -8.863  -17.708 49.623  1.00 32.56  ? 143  GLU B CA  1 
ATOM   4835 C  C   . GLU B 1 143 ? -8.402  -16.350 49.107  1.00 31.35  ? 143  GLU B C   1 
ATOM   4836 O  O   . GLU B 1 143 ? -7.223  -16.164 48.783  1.00 34.11  ? 143  GLU B O   1 
ATOM   4837 C  CB  . GLU B 1 143 ? -9.690  -18.440 48.564  1.00 32.55  ? 143  GLU B CB  1 
ATOM   4838 C  CG  . GLU B 1 143 ? -9.856  -19.930 48.848  1.00 37.69  ? 143  GLU B CG  1 
ATOM   4839 C  CD  . GLU B 1 143 ? -10.877 -20.256 49.945  1.00 39.19  ? 143  GLU B CD  1 
ATOM   4840 O  OE1 . GLU B 1 143 ? -11.704 -19.390 50.305  1.00 35.09  ? 143  GLU B OE1 1 
ATOM   4841 O  OE2 . GLU B 1 143 ? -10.840 -21.399 50.457  1.00 43.50  ? 143  GLU B OE2 1 
ATOM   4842 N  N   . ASP B 1 144 ? -9.327  -15.386 49.010  1.00 29.93  ? 144  ASP B N   1 
ATOM   4843 C  CA  . ASP B 1 144 ? -8.951  -14.061 48.532  1.00 31.57  ? 144  ASP B CA  1 
ATOM   4844 C  C   . ASP B 1 144 ? -8.137  -13.285 49.564  1.00 30.73  ? 144  ASP B C   1 
ATOM   4845 O  O   . ASP B 1 144 ? -7.285  -12.461 49.192  1.00 28.98  ? 144  ASP B O   1 
ATOM   4846 C  CB  . ASP B 1 144 ? -10.196 -13.266 48.149  1.00 30.89  ? 144  ASP B CB  1 
ATOM   4847 C  CG  . ASP B 1 144 ? -10.588 -13.470 46.698  1.00 34.37  ? 144  ASP B CG  1 
ATOM   4848 O  OD1 . ASP B 1 144 ? -9.771  -14.000 45.923  1.00 33.72  ? 144  ASP B OD1 1 
ATOM   4849 O  OD2 . ASP B 1 144 ? -11.719 -13.102 46.331  1.00 36.20  ? 144  ASP B OD2 1 
ATOM   4850 N  N   . MET B 1 145 ? -8.395  -13.516 50.850  1.00 30.84  ? 145  MET B N   1 
ATOM   4851 C  CA  . MET B 1 145 ? -7.615  -12.844 51.879  1.00 29.29  ? 145  MET B CA  1 
ATOM   4852 C  C   . MET B 1 145 ? -6.161  -13.303 51.808  1.00 30.45  ? 145  MET B C   1 
ATOM   4853 O  O   . MET B 1 145 ? -5.235  -12.517 52.019  1.00 32.94  ? 145  MET B O   1 
ATOM   4854 C  CB  . MET B 1 145 ? -8.224  -13.166 53.243  1.00 32.62  ? 145  MET B CB  1 
ATOM   4855 C  CG  . MET B 1 145 ? -9.452  -12.319 53.616  1.00 30.49  ? 145  MET B CG  1 
ATOM   4856 S  SD  . MET B 1 145 ? -9.557  -10.593 53.123  1.00 31.87  ? 145  MET B SD  1 
ATOM   4857 C  CE  . MET B 1 145 ? -10.187 -10.678 51.444  1.00 35.47  ? 145  MET B CE  1 
ATOM   4858 N  N   . THR B 1 146 ? -5.948  -14.581 51.486  1.00 29.99  ? 146  THR B N   1 
ATOM   4859 C  CA  . THR B 1 146 ? -4.590  -15.108 51.331  1.00 31.58  ? 146  THR B CA  1 
ATOM   4860 C  C   . THR B 1 146 ? -3.926  -14.585 50.060  1.00 32.15  ? 146  THR B C   1 
ATOM   4861 O  O   . THR B 1 146 ? -2.715  -14.323 50.047  1.00 33.33  ? 146  THR B O   1 
ATOM   4862 C  CB  . THR B 1 146 ? -4.641  -16.637 51.322  1.00 34.47  ? 146  THR B CB  1 
ATOM   4863 O  OG1 . THR B 1 146 ? -4.854  -17.103 52.652  1.00 35.78  ? 146  THR B OG1 1 
ATOM   4864 C  CG2 . THR B 1 146 ? -3.322  -17.214 50.773  1.00 34.29  ? 146  THR B CG2 1 
ATOM   4865 N  N   . ARG B 1 147 ? -4.677  -14.472 48.962  1.00 32.59  ? 147  ARG B N   1 
ATOM   4866 C  CA  . ARG B 1 147 ? -4.127  -13.801 47.787  1.00 31.94  ? 147  ARG B CA  1 
ATOM   4867 C  C   . ARG B 1 147 ? -3.611  -12.415 48.158  1.00 32.63  ? 147  ARG B C   1 
ATOM   4868 O  O   . ARG B 1 147 ? -2.502  -12.023 47.776  1.00 34.51  ? 147  ARG B O   1 
ATOM   4869 C  CB  . ARG B 1 147 ? -5.179  -13.686 46.684  1.00 32.43  ? 147  ARG B CB  1 
ATOM   4870 C  CG  . ARG B 1 147 ? -5.574  -14.992 46.015  1.00 33.29  ? 147  ARG B CG  1 
ATOM   4871 C  CD  . ARG B 1 147 ? -6.572  -14.674 44.878  1.00 31.06  ? 147  ARG B CD  1 
ATOM   4872 N  NE  . ARG B 1 147 ? -6.857  -15.857 44.067  1.00 36.42  ? 147  ARG B NE  1 
ATOM   4873 C  CZ  . ARG B 1 147 ? -7.788  -16.758 44.358  1.00 40.71  ? 147  ARG B CZ  1 
ATOM   4874 N  NH1 . ARG B 1 147 ? -8.638  -16.585 45.366  1.00 34.83  ? 147  ARG B NH1 1 
ATOM   4875 N  NH2 . ARG B 1 147 ? -7.862  -17.872 43.629  1.00 43.50  ? 147  ARG B NH2 1 
ATOM   4876 N  N   . LEU B 1 148 ? -4.407  -11.665 48.926  1.00 30.96  ? 148  LEU B N   1 
ATOM   4877 C  CA  . LEU B 1 148 ? -4.015  -10.311 49.296  1.00 31.30  ? 148  LEU B CA  1 
ATOM   4878 C  C   . LEU B 1 148 ? -2.792  -10.315 50.203  1.00 29.46  ? 148  LEU B C   1 
ATOM   4879 O  O   . LEU B 1 148 ? -1.818  -9.597  49.949  1.00 34.48  ? 148  LEU B O   1 
ATOM   4880 C  CB  . LEU B 1 148 ? -5.168  -9.582  49.988  1.00 32.57  ? 148  LEU B CB  1 
ATOM   4881 C  CG  . LEU B 1 148 ? -4.706  -8.189  50.448  1.00 35.37  ? 148  LEU B CG  1 
ATOM   4882 C  CD1 . LEU B 1 148 ? -5.653  -7.113  49.929  1.00 38.52  ? 148  LEU B CD1 1 
ATOM   4883 C  CD2 . LEU B 1 148 ? -4.538  -8.111  51.991  1.00 34.83  ? 148  LEU B CD2 1 
ATOM   4884 N  N   . THR B 1 149 ? -2.825  -11.086 51.285  1.00 31.09  ? 149  THR B N   1 
ATOM   4885 C  CA  . THR B 1 149 ? -1.758  -10.919 52.268  1.00 29.86  ? 149  THR B CA  1 
ATOM   4886 C  C   . THR B 1 149 ? -0.432  -11.486 51.763  1.00 31.33  ? 149  THR B C   1 
ATOM   4887 O  O   . THR B 1 149 ? 0.627   -10.899 52.020  1.00 30.68  ? 149  THR B O   1 
ATOM   4888 C  CB  . THR B 1 149 ? -2.153  -11.540 53.612  1.00 30.03  ? 149  THR B CB  1 
ATOM   4889 O  OG1 . THR B 1 149 ? -2.468  -12.922 53.421  1.00 30.14  ? 149  THR B OG1 1 
ATOM   4890 C  CG2 . THR B 1 149 ? -3.392  -10.829 54.194  1.00 31.64  ? 149  THR B CG2 1 
ATOM   4891 N  N   . LEU B 1 150 ? -0.455  -12.605 51.031  1.00 32.99  ? 150  LEU B N   1 
ATOM   4892 C  CA  . LEU B 1 150 ? 0.788   -13.091 50.424  1.00 32.23  ? 150  LEU B CA  1 
ATOM   4893 C  C   . LEU B 1 150 ? 1.367   -12.058 49.467  1.00 34.46  ? 150  LEU B C   1 
ATOM   4894 O  O   . LEU B 1 150 ? 2.576   -11.782 49.469  1.00 32.16  ? 150  LEU B O   1 
ATOM   4895 C  CB  . LEU B 1 150 ? 0.559   -14.407 49.674  1.00 33.37  ? 150  LEU B CB  1 
ATOM   4896 C  CG  . LEU B 1 150 ? 1.833   -14.898 48.967  1.00 34.54  ? 150  LEU B CG  1 
ATOM   4897 C  CD1 . LEU B 1 150 ? 2.819   -15.464 49.975  1.00 38.03  ? 150  LEU B CD1 1 
ATOM   4898 C  CD2 . LEU B 1 150 ? 1.518   -15.924 47.886  1.00 40.19  ? 150  LEU B CD2 1 
ATOM   4899 N  N   . ASP B 1 151 ? 0.520   -11.494 48.606  1.00 32.42  ? 151  ASP B N   1 
ATOM   4900 C  CA  . ASP B 1 151 ? 1.036   -10.531 47.642  1.00 29.83  ? 151  ASP B CA  1 
ATOM   4901 C  C   . ASP B 1 151 ? 1.557   -9.275  48.335  1.00 31.20  ? 151  ASP B C   1 
ATOM   4902 O  O   . ASP B 1 151 ? 2.526   -8.657  47.873  1.00 32.72  ? 151  ASP B O   1 
ATOM   4903 C  CB  . ASP B 1 151 ? -0.054  -10.186 46.631  1.00 31.01  ? 151  ASP B CB  1 
ATOM   4904 C  CG  . ASP B 1 151 ? -0.131  -11.201 45.497  1.00 31.59  ? 151  ASP B CG  1 
ATOM   4905 O  OD1 . ASP B 1 151 ? 0.236   -12.372 45.714  1.00 34.95  ? 151  ASP B OD1 1 
ATOM   4906 O  OD2 . ASP B 1 151 ? -0.567  -10.816 44.404  1.00 34.59  ? 151  ASP B OD2 1 
ATOM   4907 N  N   . THR B 1 152 ? 0.940   -8.883  49.441  1.00 30.94  ? 152  THR B N   1 
ATOM   4908 C  CA  . THR B 1 152 ? 1.412   -7.701  50.152  1.00 31.75  ? 152  THR B CA  1 
ATOM   4909 C  C   . THR B 1 152 ? 2.799   -7.922  50.765  1.00 30.68  ? 152  THR B C   1 
ATOM   4910 O  O   . THR B 1 152 ? 3.666   -7.047  50.664  1.00 33.19  ? 152  THR B O   1 
ATOM   4911 C  CB  . THR B 1 152 ? 0.390   -7.295  51.208  1.00 32.20  ? 152  THR B CB  1 
ATOM   4912 O  OG1 . THR B 1 152 ? -0.864  -7.028  50.558  1.00 30.98  ? 152  THR B OG1 1 
ATOM   4913 C  CG2 . THR B 1 152 ? 0.841   -6.006  51.933  1.00 30.35  ? 152  THR B CG2 1 
ATOM   4914 N  N   . ILE B 1 153 ? 3.027   -9.059  51.442  1.00 30.20  ? 153  ILE B N   1 
ATOM   4915 C  CA  . ILE B 1 153 ? 4.367   -9.242  52.011  1.00 28.83  ? 153  ILE B CA  1 
ATOM   4916 C  C   . ILE B 1 153 ? 5.383   -9.447  50.879  1.00 30.94  ? 153  ILE B C   1 
ATOM   4917 O  O   . ILE B 1 153 ? 6.533   -8.992  50.973  1.00 32.18  ? 153  ILE B O   1 
ATOM   4918 C  CB  . ILE B 1 153 ? 4.409   -10.383 53.056  1.00 31.40  ? 153  ILE B CB  1 
ATOM   4919 C  CG1 . ILE B 1 153 ? 5.769   -10.396 53.772  1.00 34.28  ? 153  ILE B CG1 1 
ATOM   4920 C  CG2 . ILE B 1 153 ? 4.156   -11.750 52.396  1.00 30.80  ? 153  ILE B CG2 1 
ATOM   4921 C  CD1 . ILE B 1 153 ? 6.110   -9.067  54.450  1.00 33.66  ? 153  ILE B CD1 1 
ATOM   4922 N  N   . GLY B 1 154 ? 4.989   -10.103 49.787  1.00 31.51  ? 154  GLY B N   1 
ATOM   4923 C  CA  . GLY B 1 154 ? 5.908   -10.234 48.658  1.00 31.77  ? 154  GLY B CA  1 
ATOM   4924 C  C   . GLY B 1 154 ? 6.345   -8.887  48.101  1.00 30.15  ? 154  GLY B C   1 
ATOM   4925 O  O   . GLY B 1 154 ? 7.541   -8.633  47.897  1.00 32.79  ? 154  GLY B O   1 
ATOM   4926 N  N   . LEU B 1 155 ? 5.379   -8.004  47.834  1.00 30.20  ? 155  LEU B N   1 
ATOM   4927 C  CA  . LEU B 1 155 ? 5.694   -6.720  47.222  1.00 30.78  ? 155  LEU B CA  1 
ATOM   4928 C  C   . LEU B 1 155 ? 6.382   -5.796  48.219  1.00 32.13  ? 155  LEU B C   1 
ATOM   4929 O  O   . LEU B 1 155 ? 7.478   -5.282  47.959  1.00 34.50  ? 155  LEU B O   1 
ATOM   4930 C  CB  . LEU B 1 155 ? 4.419   -6.080  46.675  1.00 33.95  ? 155  LEU B CB  1 
ATOM   4931 C  CG  . LEU B 1 155 ? 4.561   -4.780  45.873  1.00 33.74  ? 155  LEU B CG  1 
ATOM   4932 C  CD1 . LEU B 1 155 ? 5.504   -4.955  44.699  1.00 30.10  ? 155  LEU B CD1 1 
ATOM   4933 C  CD2 . LEU B 1 155 ? 3.177   -4.323  45.394  1.00 32.18  ? 155  LEU B CD2 1 
ATOM   4934 N  N   . CYS B 1 156 ? 5.747   -5.557  49.370  1.00 33.36  ? 156  CYS B N   1 
ATOM   4935 C  CA  . CYS B 1 156 ? 6.328   -4.654  50.361  1.00 32.39  ? 156  CYS B CA  1 
ATOM   4936 C  C   . CYS B 1 156 ? 7.683   -5.149  50.828  1.00 36.48  ? 156  CYS B C   1 
ATOM   4937 O  O   . CYS B 1 156 ? 8.632   -4.366  50.957  1.00 37.46  ? 156  CYS B O   1 
ATOM   4938 C  CB  . CYS B 1 156 ? 5.407   -4.501  51.579  1.00 31.28  ? 156  CYS B CB  1 
ATOM   4939 S  SG  . CYS B 1 156 ? 3.814   -3.783  51.189  1.00 36.22  ? 156  CYS B SG  1 
ATOM   4940 N  N   . GLY B 1 157 ? 7.779   -6.444  51.133  1.00 31.71  ? 157  GLY B N   1 
ATOM   4941 C  CA  . GLY B 1 157 ? 8.985   -6.950  51.755  1.00 32.07  ? 157  GLY B CA  1 
ATOM   4942 C  C   . GLY B 1 157 ? 10.097  -7.220  50.772  1.00 35.96  ? 157  GLY B C   1 
ATOM   4943 O  O   . GLY B 1 157 ? 11.275  -7.013  51.091  1.00 35.26  ? 157  GLY B O   1 
ATOM   4944 N  N   . PHE B 1 158 ? 9.751   -7.643  49.553  1.00 31.96  ? 158  PHE B N   1 
ATOM   4945 C  CA  . PHE B 1 158 ? 10.757  -8.176  48.649  1.00 33.96  ? 158  PHE B CA  1 
ATOM   4946 C  C   . PHE B 1 158 ? 10.657  -7.617  47.234  1.00 32.45  ? 158  PHE B C   1 
ATOM   4947 O  O   . PHE B 1 158 ? 11.380  -8.088  46.349  1.00 34.40  ? 158  PHE B O   1 
ATOM   4948 C  CB  . PHE B 1 158 ? 10.676  -9.708  48.645  1.00 34.71  ? 158  PHE B CB  1 
ATOM   4949 C  CG  . PHE B 1 158 ? 10.729  -10.297 50.041  1.00 32.29  ? 158  PHE B CG  1 
ATOM   4950 C  CD1 . PHE B 1 158 ? 11.942  -10.594 50.634  1.00 33.75  ? 158  PHE B CD1 1 
ATOM   4951 C  CD2 . PHE B 1 158 ? 9.565   -10.493 50.771  1.00 33.01  ? 158  PHE B CD2 1 
ATOM   4952 C  CE1 . PHE B 1 158 ? 11.998  -11.100 51.942  1.00 36.04  ? 158  PHE B CE1 1 
ATOM   4953 C  CE2 . PHE B 1 158 ? 9.620   -10.993 52.081  1.00 35.12  ? 158  PHE B CE2 1 
ATOM   4954 C  CZ  . PHE B 1 158 ? 10.842  -11.299 52.656  1.00 35.84  ? 158  PHE B CZ  1 
ATOM   4955 N  N   . ASN B 1 159 ? 9.809   -6.621  47.004  1.00 33.56  ? 159  ASN B N   1 
ATOM   4956 C  CA  . ASN B 1 159 ? 9.593   -6.089  45.657  1.00 36.50  ? 159  ASN B CA  1 
ATOM   4957 C  C   . ASN B 1 159 ? 9.374   -7.214  44.642  1.00 38.76  ? 159  ASN B C   1 
ATOM   4958 O  O   . ASN B 1 159 ? 9.875   -7.178  43.512  1.00 41.00  ? 159  ASN B O   1 
ATOM   4959 C  CB  . ASN B 1 159 ? 10.754  -5.191  45.231  1.00 37.44  ? 159  ASN B CB  1 
ATOM   4960 C  CG  . ASN B 1 159 ? 10.353  -4.216  44.144  1.00 48.42  ? 159  ASN B CG  1 
ATOM   4961 O  OD1 . ASN B 1 159 ? 9.167   -3.913  43.982  1.00 40.66  ? 159  ASN B OD1 1 
ATOM   4962 N  ND2 . ASN B 1 159 ? 11.330  -3.748  43.366  1.00 49.27  ? 159  ASN B ND2 1 
ATOM   4963 N  N   . TYR B 1 160 ? 8.619   -8.232  45.049  1.00 34.67  ? 160  TYR B N   1 
ATOM   4964 C  CA  . TYR B 1 160 ? 8.337   -9.394  44.214  1.00 33.64  ? 160  TYR B CA  1 
ATOM   4965 C  C   . TYR B 1 160 ? 6.831   -9.555  44.079  1.00 33.73  ? 160  TYR B C   1 
ATOM   4966 O  O   . TYR B 1 160 ? 6.123   -9.540  45.089  1.00 31.59  ? 160  TYR B O   1 
ATOM   4967 C  CB  . TYR B 1 160 ? 8.925   -10.666 44.818  1.00 34.81  ? 160  TYR B CB  1 
ATOM   4968 C  CG  . TYR B 1 160 ? 8.816   -11.863 43.904  1.00 40.54  ? 160  TYR B CG  1 
ATOM   4969 C  CD1 . TYR B 1 160 ? 9.721   -12.040 42.869  1.00 40.90  ? 160  TYR B CD1 1 
ATOM   4970 C  CD2 . TYR B 1 160 ? 7.825   -12.830 44.092  1.00 36.19  ? 160  TYR B CD2 1 
ATOM   4971 C  CE1 . TYR B 1 160 ? 9.649   -13.133 42.029  1.00 43.48  ? 160  TYR B CE1 1 
ATOM   4972 C  CE2 . TYR B 1 160 ? 7.739   -13.930 43.252  1.00 40.60  ? 160  TYR B CE2 1 
ATOM   4973 C  CZ  . TYR B 1 160 ? 8.660   -14.070 42.215  1.00 45.15  ? 160  TYR B CZ  1 
ATOM   4974 O  OH  . TYR B 1 160 ? 8.609   -15.164 41.372  1.00 53.08  ? 160  TYR B OH  1 
ATOM   4975 N  N   . ARG B 1 161 ? 6.334   -9.726  42.841  1.00 34.21  ? 161  ARG B N   1 
ATOM   4976 C  CA  . ARG B 1 161 ? 4.886   -9.838  42.625  1.00 32.42  ? 161  ARG B CA  1 
ATOM   4977 C  C   . ARG B 1 161 ? 4.500   -11.306 42.449  1.00 31.23  ? 161  ARG B C   1 
ATOM   4978 O  O   . ARG B 1 161 ? 4.829   -11.923 41.432  1.00 32.86  ? 161  ARG B O   1 
ATOM   4979 C  CB  . ARG B 1 161 ? 4.445   -8.990  41.431  1.00 32.92  ? 161  ARG B CB  1 
ATOM   4980 C  CG  . ARG B 1 161 ? 4.465   -7.509  41.763  1.00 36.96  ? 161  ARG B CG  1 
ATOM   4981 C  CD  . ARG B 1 161 ? 3.870   -6.656  40.678  1.00 37.73  ? 161  ARG B CD  1 
ATOM   4982 N  NE  . ARG B 1 161 ? 4.001   -5.247  41.010  1.00 35.19  ? 161  ARG B NE  1 
ATOM   4983 C  CZ  . ARG B 1 161 ? 3.052   -4.495  41.548  1.00 33.13  ? 161  ARG B CZ  1 
ATOM   4984 N  NH1 . ARG B 1 161 ? 1.847   -4.978  41.802  1.00 33.39  ? 161  ARG B NH1 1 
ATOM   4985 N  NH2 . ARG B 1 161 ? 3.310   -3.213  41.810  1.00 34.01  ? 161  ARG B NH2 1 
ATOM   4986 N  N   . PHE B 1 162 ? 3.801   -11.869 43.455  1.00 30.82  ? 162  PHE B N   1 
ATOM   4987 C  CA  . PHE B 1 162 ? 3.259   -13.215 43.321  1.00 34.33  ? 162  PHE B CA  1 
ATOM   4988 C  C   . PHE B 1 162 ? 2.086   -13.249 42.348  1.00 31.77  ? 162  PHE B C   1 
ATOM   4989 O  O   . PHE B 1 162 ? 1.723   -14.328 41.865  1.00 33.14  ? 162  PHE B O   1 
ATOM   4990 C  CB  . PHE B 1 162 ? 2.794   -13.762 44.679  1.00 36.17  ? 162  PHE B CB  1 
ATOM   4991 C  CG  . PHE B 1 162 ? 3.917   -14.097 45.612  1.00 37.05  ? 162  PHE B CG  1 
ATOM   4992 C  CD1 . PHE B 1 162 ? 4.629   -15.273 45.459  1.00 40.88  ? 162  PHE B CD1 1 
ATOM   4993 C  CD2 . PHE B 1 162 ? 4.250   -13.243 46.643  1.00 34.89  ? 162  PHE B CD2 1 
ATOM   4994 C  CE1 . PHE B 1 162 ? 5.660   -15.590 46.325  1.00 45.17  ? 162  PHE B CE1 1 
ATOM   4995 C  CE2 . PHE B 1 162 ? 5.288   -13.548 47.514  1.00 35.45  ? 162  PHE B CE2 1 
ATOM   4996 C  CZ  . PHE B 1 162 ? 5.998   -14.722 47.354  1.00 39.07  ? 162  PHE B CZ  1 
ATOM   4997 N  N   . ASN B 1 163 ? 1.483   -12.097 42.074  1.00 30.10  ? 163  ASN B N   1 
ATOM   4998 C  CA  . ASN B 1 163 ? 0.352   -11.988 41.152  1.00 30.09  ? 163  ASN B CA  1 
ATOM   4999 C  C   . ASN B 1 163 ? -0.737  -13.022 41.447  1.00 33.63  ? 163  ASN B C   1 
ATOM   5000 O  O   . ASN B 1 163 ? -1.288  -13.666 40.556  1.00 35.26  ? 163  ASN B O   1 
ATOM   5001 C  CB  . ASN B 1 163 ? 0.847   -12.058 39.711  1.00 31.15  ? 163  ASN B CB  1 
ATOM   5002 C  CG  . ASN B 1 163 ? 1.588   -10.805 39.325  1.00 33.50  ? 163  ASN B CG  1 
ATOM   5003 O  OD1 . ASN B 1 163 ? 1.107   -9.704  39.580  1.00 36.03  ? 163  ASN B OD1 1 
ATOM   5004 N  ND2 . ASN B 1 163 ? 2.773   -10.954 38.736  1.00 34.97  ? 163  ASN B ND2 1 
ATOM   5005 N  N   . SER B 1 164 ? -1.095  -13.122 42.733  1.00 31.93  ? 164  SER B N   1 
ATOM   5006 C  CA  . SER B 1 164 ? -2.084  -14.103 43.166  1.00 32.38  ? 164  SER B CA  1 
ATOM   5007 C  C   . SER B 1 164 ? -3.463  -13.833 42.577  1.00 31.98  ? 164  SER B C   1 
ATOM   5008 O  O   . SER B 1 164 ? -4.264  -14.763 42.443  1.00 33.85  ? 164  SER B O   1 
ATOM   5009 C  CB  . SER B 1 164 ? -2.174  -14.115 44.689  1.00 34.60  ? 164  SER B CB  1 
ATOM   5010 O  OG  . SER B 1 164 ? -0.950  -14.525 45.262  1.00 32.80  ? 164  SER B OG  1 
ATOM   5011 N  N   . PHE B 1 165 ? -3.782  -12.570 42.281  1.00 32.11  ? 165  PHE B N   1 
ATOM   5012 C  CA  . PHE B 1 165 ? -5.091  -12.262 41.719  1.00 35.12  ? 165  PHE B CA  1 
ATOM   5013 C  C   . PHE B 1 165 ? -5.168  -12.588 40.240  1.00 38.80  ? 165  PHE B C   1 
ATOM   5014 O  O   . PHE B 1 165 ? -6.257  -12.497 39.661  1.00 36.73  ? 165  PHE B O   1 
ATOM   5015 C  CB  . PHE B 1 165 ? -5.456  -10.793 41.981  1.00 32.15  ? 165  PHE B CB  1 
ATOM   5016 C  CG  . PHE B 1 165 ? -5.827  -10.525 43.422  1.00 32.78  ? 165  PHE B CG  1 
ATOM   5017 C  CD1 . PHE B 1 165 ? -6.962  -11.099 43.969  1.00 31.21  ? 165  PHE B CD1 1 
ATOM   5018 C  CD2 . PHE B 1 165 ? -5.011  -9.749  44.233  1.00 29.89  ? 165  PHE B CD2 1 
ATOM   5019 C  CE1 . PHE B 1 165 ? -7.298  -10.889 45.313  1.00 34.41  ? 165  PHE B CE1 1 
ATOM   5020 C  CE2 . PHE B 1 165 ? -5.328  -9.513  45.581  1.00 32.70  ? 165  PHE B CE2 1 
ATOM   5021 C  CZ  . PHE B 1 165 ? -6.473  -10.089 46.122  1.00 33.29  ? 165  PHE B CZ  1 
ATOM   5022 N  N   . TYR B 1 166 ? -4.050  -12.991 39.628  1.00 34.87  ? 166  TYR B N   1 
ATOM   5023 C  CA  . TYR B 1 166 ? -4.053  -13.495 38.255  1.00 35.84  ? 166  TYR B CA  1 
ATOM   5024 C  C   . TYR B 1 166 ? -4.219  -15.007 38.187  1.00 41.25  ? 166  TYR B C   1 
ATOM   5025 O  O   . TYR B 1 166 ? -4.075  -15.583 37.102  1.00 42.14  ? 166  TYR B O   1 
ATOM   5026 C  CB  . TYR B 1 166 ? -2.771  -13.057 37.532  1.00 34.05  ? 166  TYR B CB  1 
ATOM   5027 C  CG  . TYR B 1 166 ? -2.767  -11.572 37.357  1.00 32.54  ? 166  TYR B CG  1 
ATOM   5028 C  CD1 . TYR B 1 166 ? -2.362  -10.732 38.396  1.00 32.47  ? 166  TYR B CD1 1 
ATOM   5029 C  CD2 . TYR B 1 166 ? -3.246  -10.996 36.178  1.00 36.42  ? 166  TYR B CD2 1 
ATOM   5030 C  CE1 . TYR B 1 166 ? -2.398  -9.347  38.250  1.00 30.46  ? 166  TYR B CE1 1 
ATOM   5031 C  CE2 . TYR B 1 166 ? -3.286  -9.638  36.016  1.00 33.21  ? 166  TYR B CE2 1 
ATOM   5032 C  CZ  . TYR B 1 166 ? -2.867  -8.811  37.053  1.00 31.54  ? 166  TYR B CZ  1 
ATOM   5033 O  OH  . TYR B 1 166 ? -2.926  -7.454  36.893  1.00 32.09  ? 166  TYR B OH  1 
ATOM   5034 N  N   . ARG B 1 167 ? -4.549  -15.657 39.310  1.00 39.58  ? 167  ARG B N   1 
ATOM   5035 C  CA  . ARG B 1 167 ? -4.662  -17.107 39.368  1.00 40.65  ? 167  ARG B CA  1 
ATOM   5036 C  C   . ARG B 1 167 ? -5.980  -17.494 40.018  1.00 45.52  ? 167  ARG B C   1 
ATOM   5037 O  O   . ARG B 1 167 ? -6.325  -16.983 41.087  1.00 42.04  ? 167  ARG B O   1 
ATOM   5038 C  CB  . ARG B 1 167 ? -3.507  -17.719 40.156  1.00 45.64  ? 167  ARG B CB  1 
ATOM   5039 C  CG  . ARG B 1 167 ? -2.160  -17.196 39.756  1.00 43.81  ? 167  ARG B CG  1 
ATOM   5040 C  CD  . ARG B 1 167 ? -1.150  -17.473 40.848  1.00 47.53  ? 167  ARG B CD  1 
ATOM   5041 N  NE  . ARG B 1 167 ? 0.101   -16.768 40.615  1.00 47.91  ? 167  ARG B NE  1 
ATOM   5042 C  CZ  . ARG B 1 167 ? 1.186   -17.318 40.085  1.00 53.52  ? 167  ARG B CZ  1 
ATOM   5043 N  NH1 . ARG B 1 167 ? 1.196   -18.584 39.685  1.00 50.49  ? 167  ARG B NH1 1 
ATOM   5044 N  NH2 . ARG B 1 167 ? 2.285   -16.582 39.951  1.00 48.41  ? 167  ARG B NH2 1 
ATOM   5045 N  N   . ASP B 1 168 ? -6.715  -18.395 39.366  1.00 46.00  ? 168  ASP B N   1 
ATOM   5046 C  CA  . ASP B 1 168 ? -7.956  -18.926 39.924  1.00 47.95  ? 168  ASP B CA  1 
ATOM   5047 C  C   . ASP B 1 168 ? -7.712  -20.023 40.954  1.00 49.40  ? 168  ASP B C   1 
ATOM   5048 O  O   . ASP B 1 168 ? -8.586  -20.268 41.794  1.00 49.14  ? 168  ASP B O   1 
ATOM   5049 C  CB  . ASP B 1 168 ? -8.855  -19.432 38.786  1.00 49.32  ? 168  ASP B CB  1 
ATOM   5050 C  CG  . ASP B 1 168 ? -8.231  -20.596 38.023  1.00 55.52  ? 168  ASP B CG  1 
ATOM   5051 O  OD1 . ASP B 1 168 ? -8.514  -21.764 38.359  1.00 68.82  ? 168  ASP B OD1 1 
ATOM   5052 O  OD2 . ASP B 1 168 ? -7.443  -20.341 37.086  1.00 61.33  ? 168  ASP B OD2 1 
ATOM   5053 N  N   . GLN B 1 169 ? -6.544  -20.677 40.907  1.00 48.73  ? 169  GLN B N   1 
ATOM   5054 C  CA  . GLN B 1 169 ? -6.052  -21.655 41.862  1.00 54.27  ? 169  GLN B CA  1 
ATOM   5055 C  C   . GLN B 1 169 ? -5.121  -20.986 42.866  1.00 52.81  ? 169  GLN B C   1 
ATOM   5056 O  O   . GLN B 1 169 ? -4.608  -19.892 42.616  1.00 48.60  ? 169  GLN B O   1 
ATOM   5057 C  CB  . GLN B 1 169 ? -5.306  -22.774 41.125  1.00 58.61  ? 169  GLN B CB  1 
ATOM   5058 C  CG  . GLN B 1 169 ? -5.969  -24.151 41.197  1.00 68.32  ? 169  GLN B CG  1 
ATOM   5059 C  CD  . GLN B 1 169 ? -4.989  -25.284 40.906  1.00 75.22  ? 169  GLN B CD  1 
ATOM   5060 O  OE1 . GLN B 1 169 ? -4.826  -25.693 39.751  1.00 78.44  ? 169  GLN B OE1 1 
ATOM   5061 N  NE2 . GLN B 1 169 ? -4.323  -25.787 41.951  1.00 67.44  ? 169  GLN B NE2 1 
ATOM   5062 N  N   . PRO B 1 170 ? -4.873  -21.613 44.018  1.00 52.82  ? 170  PRO B N   1 
ATOM   5063 C  CA  . PRO B 1 170 ? -3.887  -21.049 44.950  1.00 48.85  ? 170  PRO B CA  1 
ATOM   5064 C  C   . PRO B 1 170 ? -2.515  -20.969 44.298  1.00 51.52  ? 170  PRO B C   1 
ATOM   5065 O  O   . PRO B 1 170 ? -2.154  -21.797 43.456  1.00 48.65  ? 170  PRO B O   1 
ATOM   5066 C  CB  . PRO B 1 170 ? -3.890  -22.038 46.127  1.00 49.55  ? 170  PRO B CB  1 
ATOM   5067 C  CG  . PRO B 1 170 ? -5.129  -22.855 45.969  1.00 54.63  ? 170  PRO B CG  1 
ATOM   5068 C  CD  . PRO B 1 170 ? -5.430  -22.887 44.500  1.00 51.95  ? 170  PRO B CD  1 
ATOM   5069 N  N   . HIS B 1 171 ? -1.747  -19.940 44.683  1.00 45.49  ? 171  HIS B N   1 
ATOM   5070 C  CA  . HIS B 1 171 ? -0.361  -19.851 44.238  1.00 46.59  ? 171  HIS B CA  1 
ATOM   5071 C  C   . HIS B 1 171 ? 0.365   -21.134 44.629  1.00 48.70  ? 171  HIS B C   1 
ATOM   5072 O  O   . HIS B 1 171 ? 0.065   -21.708 45.683  1.00 44.93  ? 171  HIS B O   1 
ATOM   5073 C  CB  . HIS B 1 171 ? 0.339   -18.632 44.857  1.00 47.46  ? 171  HIS B CB  1 
ATOM   5074 C  CG  . HIS B 1 171 ? 1.676   -18.326 44.251  1.00 50.04  ? 171  HIS B CG  1 
ATOM   5075 N  ND1 . HIS B 1 171 ? 2.803   -19.084 44.495  1.00 49.16  ? 171  HIS B ND1 1 
ATOM   5076 C  CD2 . HIS B 1 171 ? 2.066   -17.337 43.410  1.00 45.97  ? 171  HIS B CD2 1 
ATOM   5077 C  CE1 . HIS B 1 171 ? 3.827   -18.578 43.830  1.00 46.82  ? 171  HIS B CE1 1 
ATOM   5078 N  NE2 . HIS B 1 171 ? 3.405   -17.518 43.162  1.00 46.76  ? 171  HIS B NE2 1 
ATOM   5079 N  N   . PRO B 1 172 ? 1.321   -21.610 43.820  1.00 47.63  ? 172  PRO B N   1 
ATOM   5080 C  CA  . PRO B 1 172 ? 2.071   -22.826 44.197  1.00 45.58  ? 172  PRO B CA  1 
ATOM   5081 C  C   . PRO B 1 172 ? 2.783   -22.729 45.545  1.00 47.15  ? 172  PRO B C   1 
ATOM   5082 O  O   . PRO B 1 172 ? 2.920   -23.745 46.250  1.00 42.79  ? 172  PRO B O   1 
ATOM   5083 C  CB  . PRO B 1 172 ? 3.077   -22.983 43.047  1.00 47.63  ? 172  PRO B CB  1 
ATOM   5084 C  CG  . PRO B 1 172 ? 2.422   -22.319 41.882  1.00 47.41  ? 172  PRO B CG  1 
ATOM   5085 C  CD  . PRO B 1 172 ? 1.590   -21.189 42.431  1.00 49.64  ? 172  PRO B CD  1 
ATOM   5086 N  N   . PHE B 1 173 ? 3.284   -21.547 45.915  1.00 47.76  ? 173  PHE B N   1 
ATOM   5087 C  CA  . PHE B 1 173 ? 3.856   -21.402 47.251  1.00 42.46  ? 173  PHE B CA  1 
ATOM   5088 C  C   . PHE B 1 173 ? 2.817   -21.732 48.305  1.00 41.07  ? 173  PHE B C   1 
ATOM   5089 O  O   . PHE B 1 173 ? 3.110   -22.433 49.277  1.00 41.25  ? 173  PHE B O   1 
ATOM   5090 C  CB  . PHE B 1 173 ? 4.397   -19.986 47.463  1.00 43.07  ? 173  PHE B CB  1 
ATOM   5091 C  CG  . PHE B 1 173 ? 5.171   -19.810 48.762  1.00 45.95  ? 173  PHE B CG  1 
ATOM   5092 C  CD1 . PHE B 1 173 ? 6.543   -20.047 48.817  1.00 40.33  ? 173  PHE B CD1 1 
ATOM   5093 C  CD2 . PHE B 1 173 ? 4.522   -19.400 49.922  1.00 46.69  ? 173  PHE B CD2 1 
ATOM   5094 C  CE1 . PHE B 1 173 ? 7.251   -19.878 49.998  1.00 42.14  ? 173  PHE B CE1 1 
ATOM   5095 C  CE2 . PHE B 1 173 ? 5.226   -19.237 51.127  1.00 39.45  ? 173  PHE B CE2 1 
ATOM   5096 C  CZ  . PHE B 1 173 ? 6.589   -19.475 51.159  1.00 43.30  ? 173  PHE B CZ  1 
ATOM   5097 N  N   . ILE B 1 174 ? 1.589   -21.249 48.116  1.00 40.69  ? 174  ILE B N   1 
ATOM   5098 C  CA  . ILE B 1 174 ? 0.538   -21.455 49.108  1.00 41.76  ? 174  ILE B CA  1 
ATOM   5099 C  C   . ILE B 1 174 ? 0.200   -22.939 49.235  1.00 41.17  ? 174  ILE B C   1 
ATOM   5100 O  O   . ILE B 1 174 ? 0.044   -23.466 50.347  1.00 41.12  ? 174  ILE B O   1 
ATOM   5101 C  CB  . ILE B 1 174 ? -0.701  -20.607 48.746  1.00 41.54  ? 174  ILE B CB  1 
ATOM   5102 C  CG1 . ILE B 1 174 ? -0.384  -19.107 48.877  1.00 41.98  ? 174  ILE B CG1 1 
ATOM   5103 C  CG2 . ILE B 1 174 ? -1.884  -20.987 49.606  1.00 39.57  ? 174  ILE B CG2 1 
ATOM   5104 C  CD1 . ILE B 1 174 ? 0.121   -18.698 50.275  1.00 39.61  ? 174  ILE B CD1 1 
ATOM   5105 N  N   . THR B 1 175 ? 0.090   -23.640 48.100  1.00 42.52  ? 175  THR B N   1 
ATOM   5106 C  CA  . THR B 1 175 ? -0.227  -25.066 48.131  1.00 44.16  ? 175  THR B CA  1 
ATOM   5107 C  C   . THR B 1 175 ? 0.814   -25.844 48.930  1.00 43.62  ? 175  THR B C   1 
ATOM   5108 O  O   . THR B 1 175 ? 0.471   -26.682 49.775  1.00 41.66  ? 175  THR B O   1 
ATOM   5109 C  CB  . THR B 1 175 ? -0.324  -25.613 46.704  1.00 45.09  ? 175  THR B CB  1 
ATOM   5110 O  OG1 . THR B 1 175 ? -1.421  -24.985 46.033  1.00 44.95  ? 175  THR B OG1 1 
ATOM   5111 C  CG2 . THR B 1 175 ? -0.541  -27.129 46.733  1.00 44.55  ? 175  THR B CG2 1 
ATOM   5112 N  N   . SER B 1 176 ? 2.099   -25.568 48.677  1.00 43.33  ? 176  SER B N   1 
ATOM   5113 C  CA  . SER B 1 176 ? 3.170   -26.261 49.383  1.00 40.47  ? 176  SER B CA  1 
ATOM   5114 C  C   . SER B 1 176 ? 3.253   -25.818 50.849  1.00 39.58  ? 176  SER B C   1 
ATOM   5115 O  O   . SER B 1 176 ? 3.404   -26.657 51.741  1.00 36.82  ? 176  SER B O   1 
ATOM   5116 C  CB  . SER B 1 176 ? 4.495   -26.029 48.657  1.00 43.64  ? 176  SER B CB  1 
ATOM   5117 O  OG  . SER B 1 176 ? 4.587   -26.891 47.545  1.00 43.82  ? 176  SER B OG  1 
ATOM   5118 N  N   . MET B 1 177 ? 3.159   -24.509 51.115  1.00 38.95  ? 177  MET B N   1 
ATOM   5119 C  CA  . MET B 1 177 ? 3.080   -24.019 52.492  1.00 37.26  ? 177  MET B CA  1 
ATOM   5120 C  C   . MET B 1 177 ? 2.006   -24.729 53.293  1.00 38.49  ? 177  MET B C   1 
ATOM   5121 O  O   . MET B 1 177 ? 2.247   -25.199 54.411  1.00 37.09  ? 177  MET B O   1 
ATOM   5122 C  CB  . MET B 1 177 ? 2.746   -22.529 52.530  1.00 36.95  ? 177  MET B CB  1 
ATOM   5123 C  CG  . MET B 1 177 ? 3.172   -21.876 53.828  1.00 44.92  ? 177  MET B CG  1 
ATOM   5124 S  SD  . MET B 1 177 ? 2.243   -20.358 54.173  1.00 41.29  ? 177  MET B SD  1 
ATOM   5125 C  CE  . MET B 1 177 ? 0.533   -20.840 53.817  1.00 38.06  ? 177  MET B CE  1 
ATOM   5126 N  N   . VAL B 1 178 ? 0.775   -24.691 52.785  1.00 39.96  ? 178  VAL B N   1 
ATOM   5127 C  CA  . VAL B 1 178 ? -0.342  -25.251 53.534  1.00 40.19  ? 178  VAL B CA  1 
ATOM   5128 C  C   . VAL B 1 178 ? -0.096  -26.723 53.819  1.00 41.68  ? 178  VAL B C   1 
ATOM   5129 O  O   . VAL B 1 178 ? -0.285  -27.200 54.950  1.00 41.62  ? 178  VAL B O   1 
ATOM   5130 C  CB  . VAL B 1 178 ? -1.655  -25.034 52.768  1.00 37.78  ? 178  VAL B CB  1 
ATOM   5131 C  CG1 . VAL B 1 178 ? -2.755  -25.910 53.364  1.00 41.67  ? 178  VAL B CG1 1 
ATOM   5132 C  CG2 . VAL B 1 178 ? -2.035  -23.548 52.788  1.00 39.30  ? 178  VAL B CG2 1 
ATOM   5133 N  N   . ARG B 1 179 ? 0.348   -27.461 52.801  1.00 41.18  ? 179  ARG B N   1 
ATOM   5134 C  CA  . ARG B 1 179 ? 0.610   -28.883 52.973  1.00 40.51  ? 179  ARG B CA  1 
ATOM   5135 C  C   . ARG B 1 179 ? 1.699   -29.124 54.010  1.00 42.19  ? 179  ARG B C   1 
ATOM   5136 O  O   . ARG B 1 179 ? 1.626   -30.094 54.777  1.00 41.85  ? 179  ARG B O   1 
ATOM   5137 C  CB  . ARG B 1 179 ? 0.983   -29.500 51.624  1.00 42.95  ? 179  ARG B CB  1 
ATOM   5138 C  CG  . ARG B 1 179 ? 0.783   -30.997 51.537  1.00 46.52  ? 179  ARG B CG  1 
ATOM   5139 C  CD  . ARG B 1 179 ? 0.483   -31.408 50.085  1.00 49.58  ? 179  ARG B CD  1 
ATOM   5140 N  NE  . ARG B 1 179 ? 1.505   -30.948 49.150  1.00 45.41  ? 179  ARG B NE  1 
ATOM   5141 C  CZ  . ARG B 1 179 ? 1.268   -30.619 47.885  1.00 53.57  ? 179  ARG B CZ  1 
ATOM   5142 N  NH1 . ARG B 1 179 ? 0.052   -30.710 47.359  1.00 50.01  ? 179  ARG B NH1 1 
ATOM   5143 N  NH2 . ARG B 1 179 ? 2.273   -30.191 47.126  1.00 46.07  ? 179  ARG B NH2 1 
ATOM   5144 N  N   . ALA B 1 180 ? 2.712   -28.246 54.056  1.00 38.81  ? 180  ALA B N   1 
ATOM   5145 C  CA  . ALA B 1 180 ? 3.787   -28.394 55.036  1.00 40.17  ? 180  ALA B CA  1 
ATOM   5146 C  C   . ALA B 1 180 ? 3.287   -28.119 56.451  1.00 43.40  ? 180  ALA B C   1 
ATOM   5147 O  O   . ALA B 1 180 ? 3.660   -28.817 57.401  1.00 40.57  ? 180  ALA B O   1 
ATOM   5148 C  CB  . ALA B 1 180 ? 4.945   -27.462 54.691  1.00 40.09  ? 180  ALA B CB  1 
ATOM   5149 N  N   . LEU B 1 181 ? 2.466   -27.086 56.613  1.00 35.48  ? 181  LEU B N   1 
ATOM   5150 C  CA  . LEU B 1 181 ? 1.881   -26.814 57.920  1.00 39.36  ? 181  LEU B CA  1 
ATOM   5151 C  C   . LEU B 1 181 ? 0.955   -27.943 58.336  1.00 43.27  ? 181  LEU B C   1 
ATOM   5152 O  O   . LEU B 1 181 ? 0.924   -28.330 59.512  1.00 40.82  ? 181  LEU B O   1 
ATOM   5153 C  CB  . LEU B 1 181 ? 1.125   -25.483 57.883  1.00 36.12  ? 181  LEU B CB  1 
ATOM   5154 C  CG  . LEU B 1 181 ? 2.009   -24.255 57.633  1.00 34.65  ? 181  LEU B CG  1 
ATOM   5155 C  CD1 . LEU B 1 181 ? 1.154   -22.992 57.458  1.00 36.35  ? 181  LEU B CD1 1 
ATOM   5156 C  CD2 . LEU B 1 181 ? 2.988   -24.067 58.790  1.00 37.33  ? 181  LEU B CD2 1 
ATOM   5157 N  N   . ASP B 1 182 ? 0.178   -28.469 57.380  1.00 41.13  ? 182  ASP B N   1 
ATOM   5158 C  CA  . ASP B 1 182 ? -0.670  -29.632 57.632  1.00 44.42  ? 182  ASP B CA  1 
ATOM   5159 C  C   . ASP B 1 182 ? 0.162   -30.778 58.176  1.00 39.47  ? 182  ASP B C   1 
ATOM   5160 O  O   . ASP B 1 182 ? -0.201  -31.435 59.162  1.00 43.18  ? 182  ASP B O   1 
ATOM   5161 C  CB  . ASP B 1 182 ? -1.349  -30.078 56.331  1.00 44.06  ? 182  ASP B CB  1 
ATOM   5162 C  CG  . ASP B 1 182 ? -2.645  -29.356 56.061  1.00 52.81  ? 182  ASP B CG  1 
ATOM   5163 O  OD1 . ASP B 1 182 ? -3.039  -29.305 54.871  1.00 58.16  ? 182  ASP B OD1 1 
ATOM   5164 O  OD2 . ASP B 1 182 ? -3.268  -28.841 57.015  1.00 59.36  ? 182  ASP B OD2 1 
ATOM   5165 N  N   . GLU B 1 183 ? 1.271   -31.053 57.499  1.00 37.11  ? 183  GLU B N   1 
ATOM   5166 C  CA  . GLU B 1 183 ? 2.138   -32.146 57.895  1.00 42.27  ? 183  GLU B CA  1 
ATOM   5167 C  C   . GLU B 1 183 ? 2.720   -31.888 59.280  1.00 43.05  ? 183  GLU B C   1 
ATOM   5168 O  O   . GLU B 1 183 ? 2.740   -32.788 60.131  1.00 38.81  ? 183  GLU B O   1 
ATOM   5169 C  CB  . GLU B 1 183 ? 3.228   -32.315 56.833  1.00 38.82  ? 183  GLU B CB  1 
ATOM   5170 C  CG  . GLU B 1 183 ? 4.350   -33.303 57.172  1.00 47.25  ? 183  GLU B CG  1 
ATOM   5171 C  CD  . GLU B 1 183 ? 3.902   -34.769 57.223  1.00 45.38  ? 183  GLU B CD  1 
ATOM   5172 O  OE1 . GLU B 1 183 ? 2.703   -35.062 57.004  1.00 47.22  ? 183  GLU B OE1 1 
ATOM   5173 O  OE2 . GLU B 1 183 ? 4.766   -35.623 57.505  1.00 46.29  ? 183  GLU B OE2 1 
ATOM   5174 N  N   . ALA B 1 184 ? 3.157   -30.650 59.541  1.00 41.54  ? 184  ALA B N   1 
ATOM   5175 C  CA  . ALA B 1 184 ? 3.700   -30.343 60.861  1.00 40.44  ? 184  ALA B CA  1 
ATOM   5176 C  C   . ALA B 1 184 ? 2.662   -30.594 61.944  1.00 42.46  ? 184  ALA B C   1 
ATOM   5177 O  O   . ALA B 1 184 ? 2.974   -31.168 62.993  1.00 39.85  ? 184  ALA B O   1 
ATOM   5178 C  CB  . ALA B 1 184 ? 4.203   -28.900 60.908  1.00 41.19  ? 184  ALA B CB  1 
ATOM   5179 N  N   . MET B 1 185 ? 1.412   -30.205 61.711  1.00 38.79  ? 185  MET B N   1 
ATOM   5180 C  CA  . MET B 1 185 ? 0.465   -30.402 62.803  1.00 40.35  ? 185  MET B CA  1 
ATOM   5181 C  C   . MET B 1 185 ? -0.010  -31.857 62.856  1.00 41.92  ? 185  MET B C   1 
ATOM   5182 O  O   . MET B 1 185 ? -0.255  -32.376 63.953  1.00 40.70  ? 185  MET B O   1 
ATOM   5183 C  CB  . MET B 1 185 ? -0.672  -29.368 62.723  1.00 45.37  ? 185  MET B CB  1 
ATOM   5184 C  CG  . MET B 1 185 ? -1.995  -29.682 63.432  1.00 35.90  ? 185  MET B CG  1 
ATOM   5185 S  SD  . MET B 1 185 ? -3.454  -28.739 62.847  1.00 39.09  ? 185  MET B SD  1 
ATOM   5186 C  CE  . MET B 1 185 ? -4.263  -30.028 61.891  1.00 37.00  ? 185  MET B CE  1 
ATOM   5187 N  N   . ASN B 1 186 ? -0.086  -32.556 61.709  1.00 40.89  ? 186  ASN B N   1 
ATOM   5188 C  CA  . ASN B 1 186 ? -0.371  -33.997 61.741  1.00 42.01  ? 186  ASN B CA  1 
ATOM   5189 C  C   . ASN B 1 186 ? 0.763   -34.789 62.381  1.00 43.55  ? 186  ASN B C   1 
ATOM   5190 O  O   . ASN B 1 186 ? 0.512   -35.788 63.065  1.00 43.12  ? 186  ASN B O   1 
ATOM   5191 C  CB  . ASN B 1 186 ? -0.653  -34.545 60.335  1.00 44.22  ? 186  ASN B CB  1 
ATOM   5192 C  CG  . ASN B 1 186 ? -1.380  -35.902 60.363  1.00 51.28  ? 186  ASN B CG  1 
ATOM   5193 O  OD1 . ASN B 1 186 ? -0.753  -36.965 60.198  1.00 53.97  ? 186  ASN B OD1 1 
ATOM   5194 N  ND2 . ASN B 1 186 ? -2.694  -35.873 60.569  1.00 54.26  ? 186  ASN B ND2 1 
ATOM   5195 N  N   . LYS B 1 187 ? 2.007   -34.358 62.182  1.00 40.36  ? 187  LYS B N   1 
ATOM   5196 C  CA  . LYS B 1 187 ? 3.135   -35.054 62.784  1.00 42.36  ? 187  LYS B CA  1 
ATOM   5197 C  C   . LYS B 1 187 ? 3.090   -34.993 64.312  1.00 43.25  ? 187  LYS B C   1 
ATOM   5198 O  O   . LYS B 1 187 ? 3.616   -35.893 64.981  1.00 40.82  ? 187  LYS B O   1 
ATOM   5199 C  CB  . LYS B 1 187 ? 4.438   -34.467 62.239  1.00 40.19  ? 187  LYS B CB  1 
ATOM   5200 C  CG  . LYS B 1 187 ? 5.565   -35.467 62.214  1.00 49.68  ? 187  LYS B CG  1 
ATOM   5201 C  CD  . LYS B 1 187 ? 6.897   -34.850 61.817  1.00 51.65  ? 187  LYS B CD  1 
ATOM   5202 C  CE  . LYS B 1 187 ? 6.791   -34.028 60.549  1.00 49.67  ? 187  LYS B CE  1 
ATOM   5203 N  NZ  . LYS B 1 187 ? 8.170   -33.691 60.076  1.00 55.05  ? 187  LYS B NZ  1 
ATOM   5204 N  N   . LEU B 1 188 ? 2.434   -33.967 64.878  1.00 40.96  ? 188  LEU B N   1 
ATOM   5205 C  CA  . LEU B 1 188 ? 2.397   -33.793 66.330  1.00 44.95  ? 188  LEU B CA  1 
ATOM   5206 C  C   . LEU B 1 188 ? 1.823   -35.016 67.026  1.00 38.57  ? 188  LEU B C   1 
ATOM   5207 O  O   . LEU B 1 188 ? 2.265   -35.379 68.121  1.00 42.94  ? 188  LEU B O   1 
ATOM   5208 C  CB  . LEU B 1 188 ? 1.566   -32.559 66.706  1.00 40.41  ? 188  LEU B CB  1 
ATOM   5209 C  CG  . LEU B 1 188 ? 2.101   -31.229 66.191  1.00 38.37  ? 188  LEU B CG  1 
ATOM   5210 C  CD1 . LEU B 1 188 ? 1.107   -30.111 66.493  1.00 41.39  ? 188  LEU B CD1 1 
ATOM   5211 C  CD2 . LEU B 1 188 ? 3.457   -30.968 66.841  1.00 42.60  ? 188  LEU B CD2 1 
ATOM   5212 N  N   . GLN B 1 189 ? 0.829   -35.654 66.423  1.00 40.19  ? 189  GLN B N   1 
ATOM   5213 C  CA  . GLN B 1 189 ? 0.102   -36.723 67.092  1.00 38.88  ? 189  GLN B CA  1 
ATOM   5214 C  C   . GLN B 1 189 ? 0.601   -38.119 66.737  1.00 46.71  ? 189  GLN B C   1 
ATOM   5215 O  O   . GLN B 1 189 ? 0.032   -39.104 67.230  1.00 46.81  ? 189  GLN B O   1 
ATOM   5216 C  CB  . GLN B 1 189 ? -1.399  -36.618 66.775  1.00 43.61  ? 189  GLN B CB  1 
ATOM   5217 C  CG  . GLN B 1 189 ? -1.730  -36.506 65.282  1.00 43.79  ? 189  GLN B CG  1 
ATOM   5218 C  CD  . GLN B 1 189 ? -1.975  -37.862 64.633  1.00 49.91  ? 189  GLN B CD  1 
ATOM   5219 O  OE1 . GLN B 1 189 ? -2.824  -38.634 65.089  1.00 49.07  ? 189  GLN B OE1 1 
ATOM   5220 N  NE2 . GLN B 1 189 ? -1.249  -38.150 63.547  1.00 47.66  ? 189  GLN B NE2 1 
ATOM   5221 N  N   . ARG B 1 190 ? 1.631   -38.245 65.896  1.00 41.85  ? 190  ARG B N   1 
ATOM   5222 C  CA  . ARG B 1 190 ? 2.086   -39.571 65.476  1.00 42.01  ? 190  ARG B CA  1 
ATOM   5223 C  C   . ARG B 1 190 ? 2.898   -40.224 66.587  1.00 46.93  ? 190  ARG B C   1 
ATOM   5224 O  O   . ARG B 1 190 ? 3.970   -39.732 66.953  1.00 47.21  ? 190  ARG B O   1 
ATOM   5225 C  CB  . ARG B 1 190 ? 2.915   -39.490 64.194  1.00 45.29  ? 190  ARG B CB  1 
ATOM   5226 C  CG  . ARG B 1 190 ? 2.123   -39.059 62.983  1.00 43.49  ? 190  ARG B CG  1 
ATOM   5227 C  CD  . ARG B 1 190 ? 2.987   -38.882 61.745  1.00 39.82  ? 190  ARG B CD  1 
ATOM   5228 N  NE  . ARG B 1 190 ? 2.198   -38.234 60.707  1.00 41.69  ? 190  ARG B NE  1 
ATOM   5229 C  CZ  . ARG B 1 190 ? 2.691   -37.681 59.608  1.00 43.32  ? 190  ARG B CZ  1 
ATOM   5230 N  NH1 . ARG B 1 190 ? 3.986   -37.733 59.325  1.00 42.42  ? 190  ARG B NH1 1 
ATOM   5231 N  NH2 . ARG B 1 190 ? 1.866   -37.054 58.773  1.00 42.41  ? 190  ARG B NH2 1 
ATOM   5232 N  N   . ALA B 1 191 ? 2.397   -41.341 67.117  1.00 48.20  ? 191  ALA B N   1 
ATOM   5233 C  CA  . ALA B 1 191 ? 3.146   -42.061 68.141  1.00 49.05  ? 191  ALA B CA  1 
ATOM   5234 C  C   . ALA B 1 191 ? 4.403   -42.705 67.560  1.00 52.14  ? 191  ALA B C   1 
ATOM   5235 O  O   . ALA B 1 191 ? 5.440   -42.775 68.235  1.00 50.07  ? 191  ALA B O   1 
ATOM   5236 C  CB  . ALA B 1 191 ? 2.254   -43.114 68.794  1.00 50.66  ? 191  ALA B CB  1 
ATOM   5237 N  N   . ASN B 1 192 ? 4.333   -43.182 66.310  1.00 47.36  ? 192  ASN B N   1 
ATOM   5238 C  CA  . ASN B 1 192 ? 5.459   -43.816 65.623  1.00 47.68  ? 192  ASN B CA  1 
ATOM   5239 C  C   . ASN B 1 192 ? 5.742   -43.049 64.337  1.00 50.32  ? 192  ASN B C   1 
ATOM   5240 O  O   . ASN B 1 192 ? 5.322   -43.467 63.247  1.00 47.15  ? 192  ASN B O   1 
ATOM   5241 C  CB  . ASN B 1 192 ? 5.183   -45.289 65.320  1.00 50.67  ? 192  ASN B CB  1 
ATOM   5242 C  CG  . ASN B 1 192 ? 4.501   -45.993 66.460  1.00 53.62  ? 192  ASN B CG  1 
ATOM   5243 O  OD1 . ASN B 1 192 ? 5.086   -46.160 67.528  1.00 60.65  ? 192  ASN B OD1 1 
ATOM   5244 N  ND2 . ASN B 1 192 ? 3.256   -46.410 66.248  1.00 59.91  ? 192  ASN B ND2 1 
ATOM   5245 N  N   . PRO B 1 193 ? 6.485   -41.944 64.423  1.00 49.46  ? 193  PRO B N   1 
ATOM   5246 C  CA  . PRO B 1 193 ? 6.755   -41.142 63.218  1.00 49.43  ? 193  PRO B CA  1 
ATOM   5247 C  C   . PRO B 1 193 ? 7.418   -41.924 62.092  1.00 50.13  ? 193  PRO B C   1 
ATOM   5248 O  O   . PRO B 1 193 ? 7.305   -41.519 60.928  1.00 46.99  ? 193  PRO B O   1 
ATOM   5249 C  CB  . PRO B 1 193 ? 7.677   -40.026 63.731  1.00 48.53  ? 193  PRO B CB  1 
ATOM   5250 C  CG  . PRO B 1 193 ? 7.583   -40.062 65.209  1.00 53.36  ? 193  PRO B CG  1 
ATOM   5251 C  CD  . PRO B 1 193 ? 7.216   -41.454 65.600  1.00 55.15  ? 193  PRO B CD  1 
ATOM   5252 N  N   . ASP B 1 194 ? 8.116   -43.020 62.392  1.00 49.24  ? 194  ASP B N   1 
ATOM   5253 C  CA  . ASP B 1 194 ? 8.862   -43.750 61.377  1.00 51.10  ? 194  ASP B CA  1 
ATOM   5254 C  C   . ASP B 1 194 ? 8.095   -44.941 60.825  1.00 51.31  ? 194  ASP B C   1 
ATOM   5255 O  O   . ASP B 1 194 ? 8.645   -45.699 60.018  1.00 49.63  ? 194  ASP B O   1 
ATOM   5256 C  CB  . ASP B 1 194 ? 10.212  -44.203 61.939  1.00 56.31  ? 194  ASP B CB  1 
ATOM   5257 C  CG  . ASP B 1 194 ? 11.192  -43.057 62.072  1.00 59.71  ? 194  ASP B CG  1 
ATOM   5258 O  OD1 . ASP B 1 194 ? 10.898  -41.946 61.559  1.00 58.30  ? 194  ASP B OD1 1 
ATOM   5259 O  OD2 . ASP B 1 194 ? 12.251  -43.257 62.701  1.00 69.02  ? 194  ASP B OD2 1 
ATOM   5260 N  N   . ASP B 1 195 ? 6.848   -45.115 61.235  1.00 47.98  ? 195  ASP B N   1 
ATOM   5261 C  CA  . ASP B 1 195 ? 5.952   -46.053 60.580  1.00 47.67  ? 195  ASP B CA  1 
ATOM   5262 C  C   . ASP B 1 195 ? 5.996   -45.847 59.063  1.00 52.06  ? 195  ASP B C   1 
ATOM   5263 O  O   . ASP B 1 195 ? 5.918   -44.701 58.597  1.00 50.42  ? 195  ASP B O   1 
ATOM   5264 C  CB  . ASP B 1 195 ? 4.536   -45.833 61.110  1.00 50.42  ? 195  ASP B CB  1 
ATOM   5265 C  CG  . ASP B 1 195 ? 3.576   -46.931 60.714  1.00 50.02  ? 195  ASP B CG  1 
ATOM   5266 O  OD1 . ASP B 1 195 ? 3.414   -47.192 59.504  1.00 54.62  ? 195  ASP B OD1 1 
ATOM   5267 O  OD2 . ASP B 1 195 ? 2.959   -47.519 61.629  1.00 57.25  ? 195  ASP B OD2 1 
ATOM   5268 N  N   . PRO B 1 196 ? 6.118   -46.916 58.265  1.00 51.89  ? 196  PRO B N   1 
ATOM   5269 C  CA  . PRO B 1 196 ? 6.151   -46.740 56.800  1.00 48.18  ? 196  PRO B CA  1 
ATOM   5270 C  C   . PRO B 1 196 ? 4.909   -46.069 56.249  1.00 46.49  ? 196  PRO B C   1 
ATOM   5271 O  O   . PRO B 1 196 ? 4.955   -45.511 55.147  1.00 50.25  ? 196  PRO B O   1 
ATOM   5272 C  CB  . PRO B 1 196 ? 6.291   -48.177 56.274  1.00 49.40  ? 196  PRO B CB  1 
ATOM   5273 C  CG  . PRO B 1 196 ? 6.873   -48.948 57.421  1.00 50.42  ? 196  PRO B CG  1 
ATOM   5274 C  CD  . PRO B 1 196 ? 6.275   -48.328 58.656  1.00 51.52  ? 196  PRO B CD  1 
ATOM   5275 N  N   . ALA B 1 197 ? 3.797   -46.098 56.985  1.00 48.89  ? 197  ALA B N   1 
ATOM   5276 C  CA  . ALA B 1 197 ? 2.606   -45.387 56.547  1.00 50.34  ? 197  ALA B CA  1 
ATOM   5277 C  C   . ALA B 1 197 ? 2.885   -43.909 56.281  1.00 48.90  ? 197  ALA B C   1 
ATOM   5278 O  O   . ALA B 1 197 ? 2.151   -43.278 55.512  1.00 48.25  ? 197  ALA B O   1 
ATOM   5279 C  CB  . ALA B 1 197 ? 1.498   -45.550 57.593  1.00 50.03  ? 197  ALA B CB  1 
ATOM   5280 N  N   . TYR B 1 198 ? 3.942   -43.348 56.875  1.00 44.10  ? 198  TYR B N   1 
ATOM   5281 C  CA  . TYR B 1 198 ? 4.273   -41.934 56.708  1.00 47.25  ? 198  TYR B CA  1 
ATOM   5282 C  C   . TYR B 1 198 ? 5.389   -41.674 55.704  1.00 47.89  ? 198  TYR B C   1 
ATOM   5283 O  O   . TYR B 1 198 ? 5.826   -40.524 55.582  1.00 43.24  ? 198  TYR B O   1 
ATOM   5284 C  CB  . TYR B 1 198 ? 4.657   -41.318 58.057  1.00 41.89  ? 198  TYR B CB  1 
ATOM   5285 C  CG  . TYR B 1 198 ? 3.627   -41.542 59.133  1.00 40.89  ? 198  TYR B CG  1 
ATOM   5286 C  CD1 . TYR B 1 198 ? 2.313   -41.132 58.954  1.00 44.84  ? 198  TYR B CD1 1 
ATOM   5287 C  CD2 . TYR B 1 198 ? 3.959   -42.183 60.309  1.00 44.76  ? 198  TYR B CD2 1 
ATOM   5288 C  CE1 . TYR B 1 198 ? 1.366   -41.335 59.929  1.00 45.66  ? 198  TYR B CE1 1 
ATOM   5289 C  CE2 . TYR B 1 198 ? 3.021   -42.395 61.292  1.00 47.61  ? 198  TYR B CE2 1 
ATOM   5290 C  CZ  . TYR B 1 198 ? 1.724   -41.969 61.098  1.00 47.68  ? 198  TYR B CZ  1 
ATOM   5291 O  OH  . TYR B 1 198 ? 0.787   -42.179 62.087  1.00 52.35  ? 198  TYR B OH  1 
ATOM   5292 N  N   . ASP B 1 199 ? 5.866   -42.700 54.987  1.00 44.01  ? 199  ASP B N   1 
ATOM   5293 C  CA  . ASP B 1 199 ? 6.959   -42.491 54.037  1.00 48.15  ? 199  ASP B CA  1 
ATOM   5294 C  C   . ASP B 1 199 ? 6.579   -41.457 52.982  1.00 47.60  ? 199  ASP B C   1 
ATOM   5295 O  O   . ASP B 1 199 ? 7.372   -40.569 52.650  1.00 47.03  ? 199  ASP B O   1 
ATOM   5296 C  CB  . ASP B 1 199 ? 7.348   -43.811 53.365  1.00 45.29  ? 199  ASP B CB  1 
ATOM   5297 C  CG  . ASP B 1 199 ? 8.030   -44.774 54.318  1.00 50.25  ? 199  ASP B CG  1 
ATOM   5298 O  OD1 . ASP B 1 199 ? 8.407   -44.353 55.436  1.00 49.46  ? 199  ASP B OD1 1 
ATOM   5299 O  OD2 . ASP B 1 199 ? 8.208   -45.953 53.944  1.00 55.45  ? 199  ASP B OD2 1 
ATOM   5300 N  N   . GLU B 1 200 ? 5.367   -41.569 52.437  1.00 45.97  ? 200  GLU B N   1 
ATOM   5301 C  CA  . GLU B 1 200 ? 4.921   -40.629 51.417  1.00 50.26  ? 200  GLU B CA  1 
ATOM   5302 C  C   . GLU B 1 200 ? 4.740   -39.227 51.996  1.00 48.78  ? 200  GLU B C   1 
ATOM   5303 O  O   . GLU B 1 200 ? 5.095   -38.237 51.349  1.00 48.21  ? 200  GLU B O   1 
ATOM   5304 C  CB  . GLU B 1 200 ? 3.626   -41.134 50.774  1.00 49.35  ? 200  GLU B CB  1 
ATOM   5305 C  CG  . GLU B 1 200 ? 3.039   -40.215 49.722  1.00 54.29  ? 200  GLU B CG  1 
ATOM   5306 C  CD  . GLU B 1 200 ? 3.992   -39.947 48.566  1.00 59.19  ? 200  GLU B CD  1 
ATOM   5307 O  OE1 . GLU B 1 200 ? 4.978   -40.698 48.409  1.00 64.44  ? 200  GLU B OE1 1 
ATOM   5308 O  OE2 . GLU B 1 200 ? 3.748   -38.983 47.808  1.00 65.27  ? 200  GLU B OE2 1 
ATOM   5309 N  N   . ASN B 1 201 ? 4.195   -39.119 53.211  1.00 45.56  ? 201  ASN B N   1 
ATOM   5310 C  CA  . ASN B 1 201 ? 4.123   -37.816 53.870  1.00 45.16  ? 201  ASN B CA  1 
ATOM   5311 C  C   . ASN B 1 201 ? 5.494   -37.152 53.903  1.00 45.74  ? 201  ASN B C   1 
ATOM   5312 O  O   . ASN B 1 201 ? 5.629   -35.961 53.593  1.00 49.26  ? 201  ASN B O   1 
ATOM   5313 C  CB  . ASN B 1 201 ? 3.568   -37.964 55.287  1.00 47.78  ? 201  ASN B CB  1 
ATOM   5314 C  CG  . ASN B 1 201 ? 2.158   -38.498 55.303  1.00 49.74  ? 201  ASN B CG  1 
ATOM   5315 O  OD1 . ASN B 1 201 ? 1.913   -39.618 55.746  1.00 54.31  ? 201  ASN B OD1 1 
ATOM   5316 N  ND2 . ASN B 1 201 ? 1.220   -37.702 54.807  1.00 53.24  ? 201  ASN B ND2 1 
ATOM   5317 N  N   . LYS B 1 202 ? 6.529   -37.914 54.270  1.00 44.58  ? 202  LYS B N   1 
ATOM   5318 C  CA  . LYS B 1 202 ? 7.877   -37.357 54.331  1.00 47.43  ? 202  LYS B CA  1 
ATOM   5319 C  C   . LYS B 1 202 ? 8.363   -36.933 52.949  1.00 46.13  ? 202  LYS B C   1 
ATOM   5320 O  O   . LYS B 1 202 ? 8.922   -35.843 52.783  1.00 44.20  ? 202  LYS B O   1 
ATOM   5321 C  CB  . LYS B 1 202 ? 8.826   -38.374 54.966  1.00 44.37  ? 202  LYS B CB  1 
ATOM   5322 C  CG  . LYS B 1 202 ? 8.472   -38.694 56.421  1.00 44.65  ? 202  LYS B CG  1 
ATOM   5323 C  CD  . LYS B 1 202 ? 9.235   -39.909 56.960  1.00 48.36  ? 202  LYS B CD  1 
ATOM   5324 C  CE  . LYS B 1 202 ? 8.847   -40.180 58.416  1.00 44.95  ? 202  LYS B CE  1 
ATOM   5325 N  NZ  . LYS B 1 202 ? 9.503   -41.412 58.938  1.00 46.44  ? 202  LYS B NZ  1 
ATOM   5326 N  N   . ARG B 1 203 ? 8.161   -37.786 51.942  1.00 48.39  ? 203  ARG B N   1 
ATOM   5327 C  CA  . ARG B 1 203 ? 8.467   -37.406 50.565  1.00 46.58  ? 203  ARG B CA  1 
ATOM   5328 C  C   . ARG B 1 203 ? 7.759   -36.114 50.169  1.00 45.52  ? 203  ARG B C   1 
ATOM   5329 O  O   . ARG B 1 203 ? 8.374   -35.186 49.638  1.00 42.19  ? 203  ARG B O   1 
ATOM   5330 C  CB  . ARG B 1 203 ? 8.068   -38.536 49.615  1.00 51.04  ? 203  ARG B CB  1 
ATOM   5331 C  CG  . ARG B 1 203 ? 8.979   -38.676 48.396  1.00 57.56  ? 203  ARG B CG  1 
ATOM   5332 C  CD  . ARG B 1 203 ? 8.200   -39.242 47.204  1.00 61.16  ? 203  ARG B CD  1 
ATOM   5333 N  NE  . ARG B 1 203 ? 6.915   -38.566 47.025  1.00 64.47  ? 203  ARG B NE  1 
ATOM   5334 C  CZ  . ARG B 1 203 ? 6.752   -37.391 46.425  1.00 63.76  ? 203  ARG B CZ  1 
ATOM   5335 N  NH1 . ARG B 1 203 ? 7.774   -36.730 45.899  1.00 62.37  ? 203  ARG B NH1 1 
ATOM   5336 N  NH2 . ARG B 1 203 ? 5.532   -36.865 46.353  1.00 62.51  ? 203  ARG B NH2 1 
ATOM   5337 N  N   . GLN B 1 204 ? 6.447   -36.051 50.391  1.00 45.10  ? 204  GLN B N   1 
ATOM   5338 C  CA  . GLN B 1 204 ? 5.705   -34.851 50.029  1.00 45.49  ? 204  GLN B CA  1 
ATOM   5339 C  C   . GLN B 1 204 ? 6.224   -33.642 50.792  1.00 45.65  ? 204  GLN B C   1 
ATOM   5340 O  O   . GLN B 1 204 ? 6.322   -32.539 50.238  1.00 43.10  ? 204  GLN B O   1 
ATOM   5341 C  CB  . GLN B 1 204 ? 4.216   -35.052 50.303  1.00 45.09  ? 204  GLN B CB  1 
ATOM   5342 C  CG  . GLN B 1 204 ? 3.402   -33.829 49.993  1.00 48.65  ? 204  GLN B CG  1 
ATOM   5343 C  CD  . GLN B 1 204 ? 3.407   -33.522 48.513  1.00 49.80  ? 204  GLN B CD  1 
ATOM   5344 O  OE1 . GLN B 1 204 ? 4.116   -32.621 48.050  1.00 50.20  ? 204  GLN B OE1 1 
ATOM   5345 N  NE2 . GLN B 1 204 ? 2.631   -34.283 47.758  1.00 53.59  ? 204  GLN B NE2 1 
ATOM   5346 N  N   . PHE B 1 205 ? 6.549   -33.834 52.074  1.00 41.65  ? 205  PHE B N   1 
ATOM   5347 C  CA  . PHE B 1 205 ? 7.103   -32.759 52.887  1.00 43.17  ? 205  PHE B CA  1 
ATOM   5348 C  C   . PHE B 1 205 ? 8.376   -32.194 52.263  1.00 44.12  ? 205  PHE B C   1 
ATOM   5349 O  O   . PHE B 1 205 ? 8.507   -30.980 52.079  1.00 43.19  ? 205  PHE B O   1 
ATOM   5350 C  CB  . PHE B 1 205 ? 7.364   -33.280 54.302  1.00 43.87  ? 205  PHE B CB  1 
ATOM   5351 C  CG  . PHE B 1 205 ? 7.673   -32.204 55.313  1.00 45.07  ? 205  PHE B CG  1 
ATOM   5352 C  CD1 . PHE B 1 205 ? 6.744   -31.217 55.614  1.00 41.88  ? 205  PHE B CD1 1 
ATOM   5353 C  CD2 . PHE B 1 205 ? 8.883   -32.215 56.002  1.00 43.12  ? 205  PHE B CD2 1 
ATOM   5354 C  CE1 . PHE B 1 205 ? 7.031   -30.242 56.567  1.00 38.64  ? 205  PHE B CE1 1 
ATOM   5355 C  CE2 . PHE B 1 205 ? 9.175   -31.245 56.953  1.00 41.11  ? 205  PHE B CE2 1 
ATOM   5356 C  CZ  . PHE B 1 205 ? 8.251   -30.265 57.236  1.00 45.34  ? 205  PHE B CZ  1 
ATOM   5357 N  N   . GLN B 1 206 ? 9.323   -33.060 51.912  1.00 45.67  ? 206  GLN B N   1 
ATOM   5358 C  CA  . GLN B 1 206 ? 10.560  -32.552 51.335  1.00 45.43  ? 206  GLN B CA  1 
ATOM   5359 C  C   . GLN B 1 206 ? 10.294  -31.859 50.012  1.00 44.46  ? 206  GLN B C   1 
ATOM   5360 O  O   . GLN B 1 206 ? 10.953  -30.869 49.678  1.00 46.08  ? 206  GLN B O   1 
ATOM   5361 C  CB  . GLN B 1 206 ? 11.565  -33.682 51.166  1.00 45.01  ? 206  GLN B CB  1 
ATOM   5362 C  CG  . GLN B 1 206 ? 12.012  -34.245 52.500  1.00 52.36  ? 206  GLN B CG  1 
ATOM   5363 C  CD  . GLN B 1 206 ? 12.808  -33.242 53.318  1.00 54.20  ? 206  GLN B CD  1 
ATOM   5364 O  OE1 . GLN B 1 206 ? 13.665  -32.525 52.789  1.00 57.12  ? 206  GLN B OE1 1 
ATOM   5365 N  NE2 . GLN B 1 206 ? 12.511  -33.172 54.616  1.00 49.44  ? 206  GLN B NE2 1 
ATOM   5366 N  N   . GLU B 1 207 ? 9.312   -32.345 49.260  1.00 42.96  ? 207  GLU B N   1 
ATOM   5367 C  CA  . GLU B 1 207 ? 8.985   -31.709 47.991  1.00 45.06  ? 207  GLU B CA  1 
ATOM   5368 C  C   . GLU B 1 207 ? 8.378   -30.327 48.210  1.00 45.32  ? 207  GLU B C   1 
ATOM   5369 O  O   . GLU B 1 207 ? 8.699   -29.379 47.482  1.00 43.23  ? 207  GLU B O   1 
ATOM   5370 C  CB  . GLU B 1 207 ? 8.048   -32.617 47.198  1.00 49.30  ? 207  GLU B CB  1 
ATOM   5371 C  CG  . GLU B 1 207 ? 7.644   -32.091 45.838  1.00 56.27  ? 207  GLU B CG  1 
ATOM   5372 C  CD  . GLU B 1 207 ? 6.250   -32.550 45.459  1.00 66.70  ? 207  GLU B CD  1 
ATOM   5373 O  OE1 . GLU B 1 207 ? 5.326   -31.707 45.434  1.00 67.96  ? 207  GLU B OE1 1 
ATOM   5374 O  OE2 . GLU B 1 207 ? 6.084   -33.763 45.194  1.00 68.56  ? 207  GLU B OE2 1 
ATOM   5375 N  N   . ASP B 1 208 ? 7.512   -30.192 49.220  1.00 42.77  ? 208  ASP B N   1 
ATOM   5376 C  CA  . ASP B 1 208 ? 6.951   -28.886 49.533  1.00 40.83  ? 208  ASP B CA  1 
ATOM   5377 C  C   . ASP B 1 208 ? 8.029   -27.931 50.028  1.00 40.86  ? 208  ASP B C   1 
ATOM   5378 O  O   . ASP B 1 208 ? 7.994   -26.732 49.725  1.00 40.79  ? 208  ASP B O   1 
ATOM   5379 C  CB  . ASP B 1 208 ? 5.830   -29.031 50.562  1.00 39.39  ? 208  ASP B CB  1 
ATOM   5380 C  CG  . ASP B 1 208 ? 4.565   -29.604 49.956  1.00 44.71  ? 208  ASP B CG  1 
ATOM   5381 O  OD1 . ASP B 1 208 ? 4.330   -29.350 48.749  1.00 44.20  ? 208  ASP B OD1 1 
ATOM   5382 O  OD2 . ASP B 1 208 ? 3.815   -30.312 50.679  1.00 43.66  ? 208  ASP B OD2 1 
ATOM   5383 N  N   . ILE B 1 209 ? 8.998   -28.440 50.792  1.00 40.16  ? 209  ILE B N   1 
ATOM   5384 C  CA  . ILE B 1 209 ? 10.100  -27.587 51.225  1.00 42.22  ? 209  ILE B CA  1 
ATOM   5385 C  C   . ILE B 1 209 ? 10.886  -27.087 50.020  1.00 42.84  ? 209  ILE B C   1 
ATOM   5386 O  O   . ILE B 1 209 ? 11.340  -25.934 49.985  1.00 41.22  ? 209  ILE B O   1 
ATOM   5387 C  CB  . ILE B 1 209 ? 10.999  -28.343 52.220  1.00 41.38  ? 209  ILE B CB  1 
ATOM   5388 C  CG1 . ILE B 1 209 ? 10.268  -28.538 53.555  1.00 41.41  ? 209  ILE B CG1 1 
ATOM   5389 C  CG2 . ILE B 1 209 ? 12.311  -27.595 52.433  1.00 42.59  ? 209  ILE B CG2 1 
ATOM   5390 C  CD1 . ILE B 1 209 ? 11.089  -29.278 54.578  1.00 43.01  ? 209  ILE B CD1 1 
ATOM   5391 N  N   . LYS B 1 210 ? 11.063  -27.946 49.017  1.00 42.22  ? 210  LYS B N   1 
ATOM   5392 C  CA  . LYS B 1 210 ? 11.812  -27.559 47.825  1.00 41.73  ? 210  LYS B CA  1 
ATOM   5393 C  C   . LYS B 1 210 ? 11.077  -26.479 47.037  1.00 44.19  ? 210  LYS B C   1 
ATOM   5394 O  O   . LYS B 1 210 ? 11.690  -25.509 46.571  1.00 45.59  ? 210  LYS B O   1 
ATOM   5395 C  CB  . LYS B 1 210 ? 12.061  -28.780 46.943  1.00 43.95  ? 210  LYS B CB  1 
ATOM   5396 C  CG  . LYS B 1 210 ? 12.598  -28.403 45.567  1.00 52.00  ? 210  LYS B CG  1 
ATOM   5397 C  CD  . LYS B 1 210 ? 12.799  -29.609 44.662  1.00 59.66  ? 210  LYS B CD  1 
ATOM   5398 C  CE  . LYS B 1 210 ? 13.351  -29.164 43.311  1.00 56.86  ? 210  LYS B CE  1 
ATOM   5399 N  NZ  . LYS B 1 210 ? 14.414  -28.127 43.496  1.00 56.21  ? 210  LYS B NZ  1 
ATOM   5400 N  N   . VAL B 1 211 ? 9.759   -26.631 46.889  1.00 40.15  ? 211  VAL B N   1 
ATOM   5401 C  CA  . VAL B 1 211 ? 8.946   -25.615 46.222  1.00 43.93  ? 211  VAL B CA  1 
ATOM   5402 C  C   . VAL B 1 211 ? 9.121   -24.270 46.908  1.00 44.10  ? 211  VAL B C   1 
ATOM   5403 O  O   . VAL B 1 211 ? 9.266   -23.224 46.256  1.00 42.41  ? 211  VAL B O   1 
ATOM   5404 C  CB  . VAL B 1 211 ? 7.464   -26.053 46.195  1.00 41.93  ? 211  VAL B CB  1 
ATOM   5405 C  CG1 . VAL B 1 211 ? 6.549   -24.879 45.857  1.00 45.25  ? 211  VAL B CG1 1 
ATOM   5406 C  CG2 . VAL B 1 211 ? 7.256   -27.178 45.183  1.00 45.47  ? 211  VAL B CG2 1 
ATOM   5407 N  N   . MET B 1 212 ? 9.112   -24.276 48.239  1.00 41.79  ? 212  MET B N   1 
ATOM   5408 C  CA  . MET B 1 212 ? 9.243   -23.025 48.969  1.00 41.88  ? 212  MET B CA  1 
ATOM   5409 C  C   . MET B 1 212 ? 10.627  -22.424 48.748  1.00 41.64  ? 212  MET B C   1 
ATOM   5410 O  O   . MET B 1 212 ? 10.752  -21.212 48.535  1.00 45.58  ? 212  MET B O   1 
ATOM   5411 C  CB  . MET B 1 212 ? 8.944   -23.278 50.454  1.00 38.87  ? 212  MET B CB  1 
ATOM   5412 C  CG  . MET B 1 212 ? 7.423   -23.361 50.700  1.00 42.27  ? 212  MET B CG  1 
ATOM   5413 S  SD  . MET B 1 212 ? 6.860   -23.386 52.420  1.00 47.84  ? 212  MET B SD  1 
ATOM   5414 C  CE  . MET B 1 212 ? 8.297   -24.151 53.169  1.00 45.13  ? 212  MET B CE  1 
ATOM   5415 N  N   . ASN B 1 213 ? 11.670  -23.262 48.756  1.00 39.98  ? 213  ASN B N   1 
ATOM   5416 C  CA  . ASN B 1 213 ? 13.036  -22.780 48.551  1.00 42.20  ? 213  ASN B CA  1 
ATOM   5417 C  C   . ASN B 1 213 ? 13.280  -22.344 47.112  1.00 46.61  ? 213  ASN B C   1 
ATOM   5418 O  O   . ASN B 1 213 ? 14.100  -21.449 46.872  1.00 49.77  ? 213  ASN B O   1 
ATOM   5419 C  CB  . ASN B 1 213 ? 14.046  -23.862 48.932  1.00 44.57  ? 213  ASN B CB  1 
ATOM   5420 C  CG  . ASN B 1 213 ? 14.435  -23.807 50.395  1.00 50.97  ? 213  ASN B CG  1 
ATOM   5421 O  OD1 . ASN B 1 213 ? 15.414  -23.160 50.766  1.00 59.61  ? 213  ASN B OD1 1 
ATOM   5422 N  ND2 . ASN B 1 213 ? 13.660  -24.470 51.235  1.00 46.62  ? 213  ASN B ND2 1 
ATOM   5423 N  N   . ASP B 1 214 ? 12.606  -22.969 46.142  1.00 42.86  ? 214  ASP B N   1 
ATOM   5424 C  CA  . ASP B 1 214 ? 12.733  -22.507 44.760  1.00 44.98  ? 214  ASP B CA  1 
ATOM   5425 C  C   . ASP B 1 214 ? 12.234  -21.072 44.618  1.00 45.61  ? 214  ASP B C   1 
ATOM   5426 O  O   . ASP B 1 214 ? 12.881  -20.234 43.975  1.00 44.88  ? 214  ASP B O   1 
ATOM   5427 C  CB  . ASP B 1 214 ? 11.977  -23.445 43.819  1.00 49.86  ? 214  ASP B CB  1 
ATOM   5428 C  CG  . ASP B 1 214 ? 12.713  -24.754 43.591  1.00 52.88  ? 214  ASP B CG  1 
ATOM   5429 O  OD1 . ASP B 1 214 ? 13.889  -24.854 44.016  1.00 54.03  ? 214  ASP B OD1 1 
ATOM   5430 O  OD2 . ASP B 1 214 ? 12.118  -25.675 42.983  1.00 52.95  ? 214  ASP B OD2 1 
ATOM   5431 N  N   . LEU B 1 215 ? 11.093  -20.763 45.232  1.00 44.66  ? 215  LEU B N   1 
ATOM   5432 C  CA  . LEU B 1 215 ? 10.595  -19.391 45.212  1.00 43.07  ? 215  LEU B CA  1 
ATOM   5433 C  C   . LEU B 1 215 ? 11.570  -18.432 45.877  1.00 44.36  ? 215  LEU B C   1 
ATOM   5434 O  O   . LEU B 1 215 ? 11.774  -17.307 45.399  1.00 43.83  ? 215  LEU B O   1 
ATOM   5435 C  CB  . LEU B 1 215 ? 9.246   -19.319 45.910  1.00 45.37  ? 215  LEU B CB  1 
ATOM   5436 C  CG  . LEU B 1 215 ? 8.762   -17.884 46.043  1.00 45.50  ? 215  LEU B CG  1 
ATOM   5437 C  CD1 . LEU B 1 215 ? 8.560   -17.277 44.666  1.00 52.11  ? 215  LEU B CD1 1 
ATOM   5438 C  CD2 . LEU B 1 215 ? 7.485   -17.881 46.821  1.00 50.52  ? 215  LEU B CD2 1 
ATOM   5439 N  N   . VAL B 1 216 ? 12.146  -18.840 47.011  1.00 42.76  ? 216  VAL B N   1 
ATOM   5440 C  CA  . VAL B 1 216 ? 13.178  -18.033 47.659  1.00 44.38  ? 216  VAL B CA  1 
ATOM   5441 C  C   . VAL B 1 216 ? 14.346  -17.785 46.711  1.00 47.23  ? 216  VAL B C   1 
ATOM   5442 O  O   . VAL B 1 216 ? 14.927  -16.692 46.696  1.00 49.90  ? 216  VAL B O   1 
ATOM   5443 C  CB  . VAL B 1 216 ? 13.635  -18.709 48.964  1.00 39.85  ? 216  VAL B CB  1 
ATOM   5444 C  CG1 . VAL B 1 216 ? 14.836  -17.986 49.546  1.00 41.47  ? 216  VAL B CG1 1 
ATOM   5445 C  CG2 . VAL B 1 216 ? 12.492  -18.748 49.939  1.00 41.51  ? 216  VAL B CG2 1 
ATOM   5446 N  N   . ASP B 1 217 ? 14.714  -18.789 45.908  1.00 48.54  ? 217  ASP B N   1 
ATOM   5447 C  CA  . ASP B 1 217 ? 15.784  -18.591 44.934  1.00 48.80  ? 217  ASP B CA  1 
ATOM   5448 C  C   . ASP B 1 217 ? 15.422  -17.479 43.954  1.00 51.00  ? 217  ASP B C   1 
ATOM   5449 O  O   . ASP B 1 217 ? 16.238  -16.591 43.669  1.00 49.11  ? 217  ASP B O   1 
ATOM   5450 C  CB  . ASP B 1 217 ? 16.075  -19.893 44.178  1.00 54.15  ? 217  ASP B CB  1 
ATOM   5451 C  CG  . ASP B 1 217 ? 16.683  -20.980 45.061  1.00 53.91  ? 217  ASP B CG  1 
ATOM   5452 O  OD1 . ASP B 1 217 ? 17.225  -20.657 46.136  1.00 55.75  ? 217  ASP B OD1 1 
ATOM   5453 O  OD2 . ASP B 1 217 ? 16.627  -22.165 44.660  1.00 56.60  ? 217  ASP B OD2 1 
ATOM   5454 N  N   . LYS B 1 218 ? 14.194  -17.516 43.424  1.00 49.50  ? 218  LYS B N   1 
ATOM   5455 C  CA  . LYS B 1 218 ? 13.744  -16.485 42.490  1.00 50.08  ? 218  LYS B CA  1 
ATOM   5456 C  C   . LYS B 1 218 ? 13.828  -15.097 43.107  1.00 52.05  ? 218  LYS B C   1 
ATOM   5457 O  O   . LYS B 1 218 ? 14.238  -14.133 42.446  1.00 47.99  ? 218  LYS B O   1 
ATOM   5458 C  CB  . LYS B 1 218 ? 12.305  -16.762 42.045  1.00 53.46  ? 218  LYS B CB  1 
ATOM   5459 C  CG  . LYS B 1 218 ? 12.165  -17.268 40.624  1.00 60.59  ? 218  LYS B CG  1 
ATOM   5460 C  CD  . LYS B 1 218 ? 11.216  -18.445 40.529  1.00 59.18  ? 218  LYS B CD  1 
ATOM   5461 C  CE  . LYS B 1 218 ? 11.295  -19.072 39.143  1.00 63.67  ? 218  LYS B CE  1 
ATOM   5462 N  NZ  . LYS B 1 218 ? 10.715  -20.446 39.097  1.00 70.12  ? 218  LYS B NZ  1 
ATOM   5463 N  N   . ILE B 1 219 ? 13.408  -14.968 44.365  1.00 40.91  ? 219  ILE B N   1 
ATOM   5464 C  CA  . ILE B 1 219 ? 13.381  -13.655 44.994  1.00 43.39  ? 219  ILE B CA  1 
ATOM   5465 C  C   . ILE B 1 219 ? 14.792  -13.101 45.135  1.00 43.33  ? 219  ILE B C   1 
ATOM   5466 O  O   . ILE B 1 219 ? 15.032  -11.913 44.889  1.00 43.89  ? 219  ILE B O   1 
ATOM   5467 C  CB  . ILE B 1 219 ? 12.654  -13.732 46.348  1.00 41.74  ? 219  ILE B CB  1 
ATOM   5468 C  CG1 . ILE B 1 219 ? 11.160  -14.001 46.109  1.00 40.16  ? 219  ILE B CG1 1 
ATOM   5469 C  CG2 . ILE B 1 219 ? 12.903  -12.466 47.151  1.00 40.91  ? 219  ILE B CG2 1 
ATOM   5470 C  CD1 . ILE B 1 219 ? 10.340  -14.209 47.380  1.00 35.18  ? 219  ILE B CD1 1 
ATOM   5471 N  N   . ILE B 1 220 ? 15.750  -13.947 45.526  1.00 45.12  ? 220  ILE B N   1 
ATOM   5472 C  CA  . ILE B 1 220 ? 17.120  -13.464 45.695  1.00 42.53  ? 220  ILE B CA  1 
ATOM   5473 C  C   . ILE B 1 220 ? 17.731  -13.103 44.347  1.00 47.28  ? 220  ILE B C   1 
ATOM   5474 O  O   . ILE B 1 220 ? 18.419  -12.082 44.217  1.00 49.74  ? 220  ILE B O   1 
ATOM   5475 C  CB  . ILE B 1 220 ? 17.978  -14.501 46.439  1.00 48.29  ? 220  ILE B CB  1 
ATOM   5476 C  CG1 . ILE B 1 220 ? 17.489  -14.671 47.878  1.00 48.59  ? 220  ILE B CG1 1 
ATOM   5477 C  CG2 . ILE B 1 220 ? 19.458  -14.092 46.410  1.00 47.57  ? 220  ILE B CG2 1 
ATOM   5478 C  CD1 . ILE B 1 220 ? 18.149  -15.832 48.609  1.00 55.20  ? 220  ILE B CD1 1 
ATOM   5479 N  N   . ALA B 1 221 ? 17.508  -13.939 43.332  1.00 51.60  ? 221  ALA B N   1 
ATOM   5480 C  CA  . ALA B 1 221 ? 18.009  -13.636 41.991  1.00 59.95  ? 221  ALA B CA  1 
ATOM   5481 C  C   . ALA B 1 221 ? 17.385  -12.353 41.446  1.00 58.42  ? 221  ALA B C   1 
ATOM   5482 O  O   . ALA B 1 221 ? 18.076  -11.513 40.857  1.00 61.11  ? 221  ALA B O   1 
ATOM   5483 C  CB  . ALA B 1 221 ? 17.736  -14.814 41.050  1.00 54.34  ? 221  ALA B CB  1 
ATOM   5484 N  N   . ASP B 1 222 ? 16.070  -12.195 41.625  1.00 56.30  ? 222  ASP B N   1 
ATOM   5485 C  CA  . ASP B 1 222 ? 15.385  -10.976 41.203  1.00 55.57  ? 222  ASP B CA  1 
ATOM   5486 C  C   . ASP B 1 222 ? 16.076  -9.740  41.769  1.00 61.80  ? 222  ASP B C   1 
ATOM   5487 O  O   . ASP B 1 222 ? 16.415  -8.808  41.030  1.00 62.46  ? 222  ASP B O   1 
ATOM   5488 C  CB  . ASP B 1 222 ? 13.913  -11.046 41.640  1.00 57.45  ? 222  ASP B CB  1 
ATOM   5489 C  CG  . ASP B 1 222 ? 13.085  -9.851  41.169  1.00 58.30  ? 222  ASP B CG  1 
ATOM   5490 O  OD1 . ASP B 1 222 ? 13.129  -8.785  41.827  1.00 62.33  ? 222  ASP B OD1 1 
ATOM   5491 O  OD2 . ASP B 1 222 ? 12.384  -9.981  40.138  1.00 55.34  ? 222  ASP B OD2 1 
ATOM   5492 N  N   . ARG B 1 223 ? 16.313  -9.725  43.083  1.00 52.95  ? 223  ARG B N   1 
ATOM   5493 C  CA  . ARG B 1 223 ? 16.930  -8.563  43.713  1.00 54.36  ? 223  ARG B CA  1 
ATOM   5494 C  C   . ARG B 1 223 ? 18.356  -8.348  43.218  1.00 61.78  ? 223  ARG B C   1 
ATOM   5495 O  O   . ARG B 1 223 ? 18.752  -7.218  42.914  1.00 62.38  ? 223  ARG B O   1 
ATOM   5496 C  CB  . ARG B 1 223 ? 16.927  -8.716  45.232  1.00 44.27  ? 223  ARG B CB  1 
ATOM   5497 C  CG  . ARG B 1 223 ? 17.683  -7.608  45.931  1.00 45.82  ? 223  ARG B CG  1 
ATOM   5498 C  CD  . ARG B 1 223 ? 16.994  -6.290  45.681  1.00 44.40  ? 223  ARG B CD  1 
ATOM   5499 N  NE  . ARG B 1 223 ? 15.559  -6.381  45.933  1.00 45.12  ? 223  ARG B NE  1 
ATOM   5500 C  CZ  . ARG B 1 223 ? 14.945  -5.864  46.990  1.00 43.15  ? 223  ARG B CZ  1 
ATOM   5501 N  NH1 . ARG B 1 223 ? 15.609  -5.199  47.922  1.00 40.13  ? 223  ARG B NH1 1 
ATOM   5502 N  NH2 . ARG B 1 223 ? 13.624  -6.004  47.109  1.00 44.15  ? 223  ARG B NH2 1 
ATOM   5503 N  N   . LYS B 1 224 ? 19.157  -9.418  43.164  1.00 60.51  ? 224  LYS B N   1 
ATOM   5504 C  CA  . LYS B 1 224 ? 20.544  -9.255  42.742  1.00 68.65  ? 224  LYS B CA  1 
ATOM   5505 C  C   . LYS B 1 224 ? 20.636  -8.787  41.295  1.00 72.61  ? 224  LYS B C   1 
ATOM   5506 O  O   . LYS B 1 224 ? 21.586  -8.085  40.928  1.00 75.34  ? 224  LYS B O   1 
ATOM   5507 C  CB  . LYS B 1 224 ? 21.324  -10.557 42.930  1.00 72.29  ? 224  LYS B CB  1 
ATOM   5508 C  CG  . LYS B 1 224 ? 22.834  -10.372 42.777  1.00 81.29  ? 224  LYS B CG  1 
ATOM   5509 C  CD  . LYS B 1 224 ? 23.611  -11.565 43.309  1.00 87.44  ? 224  LYS B CD  1 
ATOM   5510 C  CE  . LYS B 1 224 ? 24.478  -12.183 42.226  1.00 90.61  ? 224  LYS B CE  1 
ATOM   5511 N  NZ  . LYS B 1 224 ? 23.777  -13.299 41.533  1.00 93.47  ? 224  LYS B NZ  1 
ATOM   5512 N  N   . ALA B 1 225 ? 19.661  -9.153  40.465  1.00 70.93  ? 225  ALA B N   1 
ATOM   5513 C  CA  . ALA B 1 225 ? 19.623  -8.754  39.065  1.00 72.06  ? 225  ALA B CA  1 
ATOM   5514 C  C   . ALA B 1 225 ? 18.904  -7.431  38.853  1.00 78.16  ? 225  ALA B C   1 
ATOM   5515 O  O   . ALA B 1 225 ? 18.700  -7.028  37.704  1.00 79.89  ? 225  ALA B O   1 
ATOM   5516 C  CB  . ALA B 1 225 ? 18.952  -9.843  38.223  1.00 68.87  ? 225  ALA B CB  1 
ATOM   5517 N  N   . SER B 1 226 ? 18.517  -6.752  39.929  1.00 75.74  ? 226  SER B N   1 
ATOM   5518 C  CA  . SER B 1 226 ? 17.716  -5.537  39.839  1.00 81.59  ? 226  SER B CA  1 
ATOM   5519 C  C   . SER B 1 226 ? 18.644  -4.326  39.842  1.00 89.51  ? 226  SER B C   1 
ATOM   5520 O  O   . SER B 1 226 ? 19.276  -4.022  40.860  1.00 88.69  ? 226  SER B O   1 
ATOM   5521 C  CB  . SER B 1 226 ? 16.719  -5.470  40.993  1.00 79.43  ? 226  SER B CB  1 
ATOM   5522 O  OG  . SER B 1 226 ? 16.029  -4.235  40.995  1.00 89.59  ? 226  SER B OG  1 
ATOM   5523 N  N   . GLY B 1 227 ? 18.737  -3.646  38.694  1.00 96.26  ? 227  GLY B N   1 
ATOM   5524 C  CA  . GLY B 1 227 ? 19.448  -2.380  38.647  1.00 95.39  ? 227  GLY B CA  1 
ATOM   5525 C  C   . GLY B 1 227 ? 18.701  -1.274  39.360  1.00 97.75  ? 227  GLY B C   1 
ATOM   5526 O  O   . GLY B 1 227 ? 19.316  -0.339  39.884  1.00 96.75  ? 227  GLY B O   1 
ATOM   5527 N  N   . GLU B 1 228 ? 17.371  -1.359  39.380  1.00 97.09  ? 228  GLU B N   1 
ATOM   5528 C  CA  . GLU B 1 228 ? 16.564  -0.510  40.244  1.00 97.62  ? 228  GLU B CA  1 
ATOM   5529 C  C   . GLU B 1 228 ? 16.901  -0.782  41.706  1.00 97.54  ? 228  GLU B C   1 
ATOM   5530 O  O   . GLU B 1 228 ? 16.925  -1.936  42.146  1.00 96.75  ? 228  GLU B O   1 
ATOM   5531 C  CB  . GLU B 1 228 ? 15.078  -0.771  39.980  1.00 96.36  ? 228  GLU B CB  1 
ATOM   5532 C  CG  . GLU B 1 228 ? 14.214  -0.847  41.235  1.00 95.51  ? 228  GLU B CG  1 
ATOM   5533 C  CD  . GLU B 1 228 ? 12.762  -1.183  40.929  1.00 93.99  ? 228  GLU B CD  1 
ATOM   5534 O  OE1 . GLU B 1 228 ? 12.519  -1.972  39.991  1.00 94.37  ? 228  GLU B OE1 1 
ATOM   5535 O  OE2 . GLU B 1 228 ? 11.865  -0.668  41.630  1.00 87.81  ? 228  GLU B OE2 1 
ATOM   5536 N  N   . GLN B 1 229 ? 17.174  0.279   42.462  1.00 94.95  ? 229  GLN B N   1 
ATOM   5537 C  CA  . GLN B 1 229 ? 17.480  0.120   43.876  1.00 93.08  ? 229  GLN B CA  1 
ATOM   5538 C  C   . GLN B 1 229 ? 16.199  0.140   44.706  1.00 89.00  ? 229  GLN B C   1 
ATOM   5539 O  O   . GLN B 1 229 ? 15.210  0.789   44.348  1.00 89.32  ? 229  GLN B O   1 
ATOM   5540 C  CB  . GLN B 1 229 ? 18.441  1.209   44.363  1.00 93.33  ? 229  GLN B CB  1 
ATOM   5541 C  CG  . GLN B 1 229 ? 17.972  2.637   44.149  1.00 95.20  ? 229  GLN B CG  1 
ATOM   5542 C  CD  . GLN B 1 229 ? 18.945  3.652   44.731  1.00 100.58 ? 229  GLN B CD  1 
ATOM   5543 O  OE1 . GLN B 1 229 ? 20.084  3.769   44.274  1.00 98.77  ? 229  GLN B OE1 1 
ATOM   5544 N  NE2 . GLN B 1 229 ? 18.502  4.382   45.753  1.00 93.07  ? 229  GLN B NE2 1 
ATOM   5545 N  N   . SER B 1 230 ? 16.226  -0.592  45.820  1.00 80.18  ? 230  SER B N   1 
ATOM   5546 C  CA  . SER B 1 230 ? 15.098  -0.692  46.735  1.00 70.92  ? 230  SER B CA  1 
ATOM   5547 C  C   . SER B 1 230 ? 15.567  -0.367  48.150  1.00 70.33  ? 230  SER B C   1 
ATOM   5548 O  O   . SER B 1 230 ? 16.765  -0.213  48.418  1.00 66.96  ? 230  SER B O   1 
ATOM   5549 C  CB  . SER B 1 230 ? 14.459  -2.091  46.688  1.00 65.81  ? 230  SER B CB  1 
ATOM   5550 O  OG  . SER B 1 230 ? 13.990  -2.419  45.389  1.00 61.73  ? 230  SER B OG  1 
ATOM   5551 N  N   . ASP B 1 231 ? 14.601  -0.256  49.069  1.00 59.83  ? 231  ASP B N   1 
ATOM   5552 C  CA  . ASP B 1 231 ? 14.916  -0.013  50.477  1.00 61.95  ? 231  ASP B CA  1 
ATOM   5553 C  C   . ASP B 1 231 ? 13.816  -0.668  51.322  1.00 62.00  ? 231  ASP B C   1 
ATOM   5554 O  O   . ASP B 1 231 ? 13.054  -0.022  52.042  1.00 65.57  ? 231  ASP B O   1 
ATOM   5555 C  CB  . ASP B 1 231 ? 15.061  1.480   50.780  1.00 65.16  ? 231  ASP B CB  1 
ATOM   5556 C  CG  . ASP B 1 231 ? 15.719  1.743   52.130  1.00 72.57  ? 231  ASP B CG  1 
ATOM   5557 O  OD1 . ASP B 1 231 ? 16.267  0.785   52.724  1.00 70.13  ? 231  ASP B OD1 1 
ATOM   5558 O  OD2 . ASP B 1 231 ? 15.704  2.909   52.592  1.00 72.31  ? 231  ASP B OD2 1 
ATOM   5559 N  N   . ASP B 1 232 ? 13.739  -1.995  51.250  1.00 51.92  ? 232  ASP B N   1 
ATOM   5560 C  CA  . ASP B 1 232 ? 12.687  -2.767  51.900  1.00 48.19  ? 232  ASP B CA  1 
ATOM   5561 C  C   . ASP B 1 232 ? 13.299  -3.816  52.833  1.00 46.87  ? 232  ASP B C   1 
ATOM   5562 O  O   . ASP B 1 232 ? 14.489  -3.770  53.166  1.00 42.37  ? 232  ASP B O   1 
ATOM   5563 C  CB  . ASP B 1 232 ? 11.796  -3.408  50.839  1.00 42.71  ? 232  ASP B CB  1 
ATOM   5564 C  CG  . ASP B 1 232 ? 12.585  -4.231  49.851  1.00 45.23  ? 232  ASP B CG  1 
ATOM   5565 O  OD1 . ASP B 1 232 ? 13.784  -4.482  50.099  1.00 47.28  ? 232  ASP B OD1 1 
ATOM   5566 O  OD2 . ASP B 1 232 ? 12.009  -4.640  48.826  1.00 43.23  ? 232  ASP B OD2 1 
ATOM   5567 N  N   . LEU B 1 233 ? 12.466  -4.772  53.259  1.00 40.74  ? 233  LEU B N   1 
ATOM   5568 C  CA  . LEU B 1 233 ? 12.925  -5.801  54.190  1.00 40.94  ? 233  LEU B CA  1 
ATOM   5569 C  C   . LEU B 1 233 ? 14.106  -6.580  53.611  1.00 41.06  ? 233  LEU B C   1 
ATOM   5570 O  O   . LEU B 1 233 ? 15.132  -6.784  54.279  1.00 40.07  ? 233  LEU B O   1 
ATOM   5571 C  CB  . LEU B 1 233 ? 11.750  -6.720  54.543  1.00 38.59  ? 233  LEU B CB  1 
ATOM   5572 C  CG  . LEU B 1 233 ? 11.891  -7.836  55.575  1.00 41.84  ? 233  LEU B CG  1 
ATOM   5573 C  CD1 . LEU B 1 233 ? 12.156  -7.334  57.014  1.00 38.33  ? 233  LEU B CD1 1 
ATOM   5574 C  CD2 . LEU B 1 233 ? 10.641  -8.705  55.539  1.00 39.42  ? 233  LEU B CD2 1 
ATOM   5575 N  N   . LEU B 1 234 ? 14.002  -6.990  52.347  1.00 38.73  ? 234  LEU B N   1 
ATOM   5576 C  CA  . LEU B 1 234 ? 15.107  -7.720  51.740  1.00 34.95  ? 234  LEU B CA  1 
ATOM   5577 C  C   . LEU B 1 234 ? 16.376  -6.870  51.700  1.00 41.25  ? 234  LEU B C   1 
ATOM   5578 O  O   . LEU B 1 234 ? 17.485  -7.393  51.872  1.00 41.10  ? 234  LEU B O   1 
ATOM   5579 C  CB  . LEU B 1 234 ? 14.722  -8.184  50.336  1.00 40.59  ? 234  LEU B CB  1 
ATOM   5580 C  CG  . LEU B 1 234 ? 15.785  -8.991  49.594  1.00 34.99  ? 234  LEU B CG  1 
ATOM   5581 C  CD1 . LEU B 1 234 ? 16.249  -10.219 50.397  1.00 39.13  ? 234  LEU B CD1 1 
ATOM   5582 C  CD2 . LEU B 1 234 ? 15.282  -9.410  48.200  1.00 38.82  ? 234  LEU B CD2 1 
ATOM   5583 N  N   . THR B 1 235 ? 16.236  -5.559  51.472  1.00 38.22  ? 235  THR B N   1 
ATOM   5584 C  CA  . THR B 1 235 ? 17.408  -4.685  51.473  1.00 41.36  ? 235  THR B CA  1 
ATOM   5585 C  C   . THR B 1 235 ? 18.147  -4.800  52.797  1.00 40.17  ? 235  THR B C   1 
ATOM   5586 O  O   . THR B 1 235 ? 19.373  -4.959  52.832  1.00 42.14  ? 235  THR B O   1 
ATOM   5587 C  CB  . THR B 1 235 ? 16.997  -3.231  51.244  1.00 42.19  ? 235  THR B CB  1 
ATOM   5588 O  OG1 . THR B 1 235 ? 16.461  -3.082  49.928  1.00 43.26  ? 235  THR B OG1 1 
ATOM   5589 C  CG2 . THR B 1 235 ? 18.222  -2.338  51.350  1.00 50.28  ? 235  THR B CG2 1 
ATOM   5590 N  N   . HIS B 1 236 ? 17.403  -4.735  53.900  1.00 40.96  ? 236  HIS B N   1 
ATOM   5591 C  CA  . HIS B 1 236 ? 18.011  -4.841  55.220  1.00 40.95  ? 236  HIS B CA  1 
ATOM   5592 C  C   . HIS B 1 236 ? 18.618  -6.221  55.431  1.00 43.08  ? 236  HIS B C   1 
ATOM   5593 O  O   . HIS B 1 236 ? 19.698  -6.344  56.020  1.00 46.46  ? 236  HIS B O   1 
ATOM   5594 C  CB  . HIS B 1 236 ? 16.967  -4.545  56.297  1.00 45.76  ? 236  HIS B CB  1 
ATOM   5595 C  CG  . HIS B 1 236 ? 16.607  -3.098  56.400  1.00 47.22  ? 236  HIS B CG  1 
ATOM   5596 N  ND1 . HIS B 1 236 ? 17.357  -2.189  57.117  1.00 58.59  ? 236  HIS B ND1 1 
ATOM   5597 C  CD2 . HIS B 1 236 ? 15.592  -2.395  55.844  1.00 49.44  ? 236  HIS B CD2 1 
ATOM   5598 C  CE1 . HIS B 1 236 ? 16.802  -0.993  57.020  1.00 58.95  ? 236  HIS B CE1 1 
ATOM   5599 N  NE2 . HIS B 1 236 ? 15.734  -1.089  56.248  1.00 61.14  ? 236  HIS B NE2 1 
ATOM   5600 N  N   . MET B 1 237 ? 17.936  -7.280  54.983  1.00 41.19  ? 237  MET B N   1 
ATOM   5601 C  CA  . MET B 1 237 ? 18.535  -8.606  55.116  1.00 39.55  ? 237  MET B CA  1 
ATOM   5602 C  C   . MET B 1 237 ? 19.893  -8.671  54.423  1.00 45.64  ? 237  MET B C   1 
ATOM   5603 O  O   . MET B 1 237 ? 20.847  -9.241  54.964  1.00 45.10  ? 237  MET B O   1 
ATOM   5604 C  CB  . MET B 1 237 ? 17.623  -9.719  54.580  1.00 44.79  ? 237  MET B CB  1 
ATOM   5605 C  CG  . MET B 1 237 ? 16.396  -10.113 55.433  1.00 37.34  ? 237  MET B CG  1 
ATOM   5606 S  SD  . MET B 1 237 ? 15.309  -11.155 54.402  1.00 41.33  ? 237  MET B SD  1 
ATOM   5607 C  CE  . MET B 1 237 ? 13.813  -11.179 55.407  1.00 39.53  ? 237  MET B CE  1 
ATOM   5608 N  N   . LEU B 1 238 ? 20.007  -8.078  53.233  1.00 45.05  ? 238  LEU B N   1 
ATOM   5609 C  CA  . LEU B 1 238 ? 21.237  -8.218  52.463  1.00 44.38  ? 238  LEU B CA  1 
ATOM   5610 C  C   . LEU B 1 238 ? 22.327  -7.255  52.913  1.00 41.27  ? 238  LEU B C   1 
ATOM   5611 O  O   . LEU B 1 238 ? 23.514  -7.561  52.753  1.00 50.17  ? 238  LEU B O   1 
ATOM   5612 C  CB  . LEU B 1 238 ? 20.955  -8.007  50.973  1.00 43.77  ? 238  LEU B CB  1 
ATOM   5613 C  CG  . LEU B 1 238 ? 20.034  -9.031  50.309  1.00 44.73  ? 238  LEU B CG  1 
ATOM   5614 C  CD1 . LEU B 1 238 ? 19.628  -8.551  48.924  1.00 41.66  ? 238  LEU B CD1 1 
ATOM   5615 C  CD2 . LEU B 1 238 ? 20.674  -10.427 50.251  1.00 43.80  ? 238  LEU B CD2 1 
ATOM   5616 N  N   . ASN B 1 239 ? 21.972  -6.104  53.478  1.00 44.09  ? 239  ASN B N   1 
ATOM   5617 C  CA  . ASN B 1 239 ? 22.961  -5.059  53.689  1.00 43.09  ? 239  ASN B CA  1 
ATOM   5618 C  C   . ASN B 1 239 ? 23.095  -4.581  55.122  1.00 47.36  ? 239  ASN B C   1 
ATOM   5619 O  O   . ASN B 1 239 ? 24.128  -3.996  55.447  1.00 48.14  ? 239  ASN B O   1 
ATOM   5620 C  CB  . ASN B 1 239 ? 22.647  -3.844  52.806  1.00 48.06  ? 239  ASN B CB  1 
ATOM   5621 C  CG  . ASN B 1 239 ? 22.616  -4.204  51.339  1.00 52.43  ? 239  ASN B CG  1 
ATOM   5622 O  OD1 . ASN B 1 239 ? 23.659  -4.313  50.694  1.00 53.41  ? 239  ASN B OD1 1 
ATOM   5623 N  ND2 . ASN B 1 239 ? 21.418  -4.434  50.812  1.00 53.11  ? 239  ASN B ND2 1 
ATOM   5624 N  N   . GLY B 1 240 ? 22.097  -4.794  55.978  1.00 43.85  ? 240  GLY B N   1 
ATOM   5625 C  CA  . GLY B 1 240 ? 22.150  -4.229  57.311  1.00 41.44  ? 240  GLY B CA  1 
ATOM   5626 C  C   . GLY B 1 240 ? 23.178  -4.927  58.182  1.00 40.44  ? 240  GLY B C   1 
ATOM   5627 O  O   . GLY B 1 240 ? 23.418  -6.126  58.060  1.00 40.79  ? 240  GLY B O   1 
ATOM   5628 N  N   . LYS B 1 241 ? 23.794  -4.157  59.078  1.00 38.97  ? 241  LYS B N   1 
ATOM   5629 C  CA  . LYS B 1 241 ? 24.761  -4.683  60.034  1.00 40.69  ? 241  LYS B CA  1 
ATOM   5630 C  C   . LYS B 1 241 ? 24.175  -4.651  61.436  1.00 35.71  ? 241  LYS B C   1 
ATOM   5631 O  O   . LYS B 1 241 ? 23.637  -3.624  61.866  1.00 39.94  ? 241  LYS B O   1 
ATOM   5632 C  CB  . LYS B 1 241 ? 26.058  -3.868  60.029  1.00 39.65  ? 241  LYS B CB  1 
ATOM   5633 C  CG  . LYS B 1 241 ? 26.723  -3.728  58.697  1.00 43.54  ? 241  LYS B CG  1 
ATOM   5634 C  CD  . LYS B 1 241 ? 27.115  -5.062  58.132  1.00 47.64  ? 241  LYS B CD  1 
ATOM   5635 C  CE  . LYS B 1 241 ? 28.046  -4.869  56.936  1.00 51.22  ? 241  LYS B CE  1 
ATOM   5636 N  NZ  . LYS B 1 241 ? 29.036  -3.777  57.172  1.00 60.67  ? 241  LYS B NZ  1 
ATOM   5637 N  N   . ASP B 1 242 ? 24.334  -5.750  62.158  1.00 34.38  ? 242  ASP B N   1 
ATOM   5638 C  CA  . ASP B 1 242 ? 23.965  -5.807  63.563  1.00 35.36  ? 242  ASP B CA  1 
ATOM   5639 C  C   . ASP B 1 242 ? 24.927  -4.944  64.360  1.00 36.83  ? 242  ASP B C   1 
ATOM   5640 O  O   . ASP B 1 242 ? 26.133  -5.221  64.348  1.00 35.86  ? 242  ASP B O   1 
ATOM   5641 C  CB  . ASP B 1 242 ? 24.025  -7.244  64.058  1.00 32.71  ? 242  ASP B CB  1 
ATOM   5642 C  CG  . ASP B 1 242 ? 24.034  -7.347  65.574  1.00 31.18  ? 242  ASP B CG  1 
ATOM   5643 O  OD1 . ASP B 1 242 ? 23.440  -6.469  66.250  1.00 36.11  ? 242  ASP B OD1 1 
ATOM   5644 O  OD2 . ASP B 1 242 ? 24.610  -8.336  66.089  1.00 34.62  ? 242  ASP B OD2 1 
ATOM   5645 N  N   . PRO B 1 243 ? 24.461  -3.906  65.054  1.00 36.24  ? 243  PRO B N   1 
ATOM   5646 C  CA  . PRO B 1 243 ? 25.392  -3.049  65.814  1.00 36.27  ? 243  PRO B CA  1 
ATOM   5647 C  C   . PRO B 1 243 ? 26.174  -3.787  66.878  1.00 39.10  ? 243  PRO B C   1 
ATOM   5648 O  O   . PRO B 1 243 ? 27.290  -3.361  67.223  1.00 37.85  ? 243  PRO B O   1 
ATOM   5649 C  CB  . PRO B 1 243 ? 24.467  -1.998  66.450  1.00 40.36  ? 243  PRO B CB  1 
ATOM   5650 C  CG  . PRO B 1 243 ? 23.213  -2.057  65.651  1.00 44.46  ? 243  PRO B CG  1 
ATOM   5651 C  CD  . PRO B 1 243 ? 23.063  -3.470  65.206  1.00 34.97  ? 243  PRO B CD  1 
ATOM   5652 N  N   . GLU B 1 244 ? 25.631  -4.874  67.427  1.00 36.09  ? 244  GLU B N   1 
ATOM   5653 C  CA  . GLU B 1 244 ? 26.332  -5.589  68.484  1.00 35.85  ? 244  GLU B CA  1 
ATOM   5654 C  C   . GLU B 1 244 ? 27.523  -6.361  67.915  1.00 35.35  ? 244  GLU B C   1 
ATOM   5655 O  O   . GLU B 1 244 ? 28.679  -6.032  68.209  1.00 37.14  ? 244  GLU B O   1 
ATOM   5656 C  CB  . GLU B 1 244 ? 25.380  -6.529  69.228  1.00 36.39  ? 244  GLU B CB  1 
ATOM   5657 C  CG  . GLU B 1 244 ? 26.072  -7.258  70.376  1.00 39.85  ? 244  GLU B CG  1 
ATOM   5658 C  CD  . GLU B 1 244 ? 25.144  -8.170  71.156  1.00 48.57  ? 244  GLU B CD  1 
ATOM   5659 O  OE1 . GLU B 1 244 ? 24.013  -8.434  70.702  1.00 41.47  ? 244  GLU B OE1 1 
ATOM   5660 O  OE2 . GLU B 1 244 ? 25.550  -8.619  72.239  1.00 52.60  ? 244  GLU B OE2 1 
ATOM   5661 N  N   . THR B 1 245 ? 27.259  -7.378  67.087  1.00 33.63  ? 245  THR B N   1 
ATOM   5662 C  CA  . THR B 1 245 ? 28.344  -8.154  66.493  1.00 37.69  ? 245  THR B CA  1 
ATOM   5663 C  C   . THR B 1 245 ? 29.057  -7.399  65.389  1.00 39.31  ? 245  THR B C   1 
ATOM   5664 O  O   . THR B 1 245 ? 30.196  -7.750  65.062  1.00 37.02  ? 245  THR B O   1 
ATOM   5665 C  CB  . THR B 1 245 ? 27.826  -9.481  65.933  1.00 39.91  ? 245  THR B CB  1 
ATOM   5666 O  OG1 . THR B 1 245 ? 26.959  -9.236  64.810  1.00 36.12  ? 245  THR B OG1 1 
ATOM   5667 C  CG2 . THR B 1 245 ? 27.088  -10.265 67.014  1.00 37.37  ? 245  THR B CG2 1 
ATOM   5668 N  N   . GLY B 1 246 ? 28.422  -6.368  64.826  1.00 36.16  ? 246  GLY B N   1 
ATOM   5669 C  CA  . GLY B 1 246 ? 28.919  -5.651  63.675  1.00 35.63  ? 246  GLY B CA  1 
ATOM   5670 C  C   . GLY B 1 246 ? 28.752  -6.374  62.360  1.00 34.41  ? 246  GLY B C   1 
ATOM   5671 O  O   . GLY B 1 246 ? 29.174  -5.846  61.326  1.00 38.72  ? 246  GLY B O   1 
ATOM   5672 N  N   . GLU B 1 247 ? 28.127  -7.624  62.361  1.00 34.30  ? 247  GLU B N   1 
ATOM   5673 C  CA  . GLU B 1 247 ? 28.073  -8.489  61.190  1.00 35.09  ? 247  GLU B CA  1 
ATOM   5674 C  C   . GLU B 1 247 ? 26.741  -8.352  60.464  1.00 34.08  ? 247  GLU B C   1 
ATOM   5675 O  O   . GLU B 1 247 ? 25.735  -8.003  61.079  1.00 35.17  ? 247  GLU B O   1 
ATOM   5676 C  CB  . GLU B 1 247 ? 28.236  -9.955  61.589  1.00 34.69  ? 247  GLU B CB  1 
ATOM   5677 C  CG  . GLU B 1 247 ? 29.441  -10.271 62.462  1.00 38.55  ? 247  GLU B CG  1 
ATOM   5678 C  CD  . GLU B 1 247 ? 29.299  -11.611 63.168  1.00 40.38  ? 247  GLU B CD  1 
ATOM   5679 O  OE1 . GLU B 1 247 ? 28.319  -12.337 62.897  1.00 37.48  ? 247  GLU B OE1 1 
ATOM   5680 O  OE2 . GLU B 1 247 ? 30.155  -11.935 64.015  1.00 36.97  ? 247  GLU B OE2 1 
ATOM   5681 N  N   . PRO B 1 248 ? 26.717  -8.649  59.172  1.00 35.95  ? 248  PRO B N   1 
ATOM   5682 C  CA  . PRO B 1 248 ? 25.452  -8.836  58.458  1.00 40.00  ? 248  PRO B CA  1 
ATOM   5683 C  C   . PRO B 1 248 ? 25.012  -10.292 58.554  1.00 38.98  ? 248  PRO B C   1 
ATOM   5684 O  O   . PRO B 1 248 ? 25.776  -11.175 58.945  1.00 35.59  ? 248  PRO B O   1 
ATOM   5685 C  CB  . PRO B 1 248 ? 25.817  -8.473  57.014  1.00 40.50  ? 248  PRO B CB  1 
ATOM   5686 C  CG  . PRO B 1 248 ? 27.255  -8.955  56.891  1.00 39.97  ? 248  PRO B CG  1 
ATOM   5687 C  CD  . PRO B 1 248 ? 27.883  -8.720  58.269  1.00 38.79  ? 248  PRO B CD  1 
ATOM   5688 N  N   . LEU B 1 249 ? 23.751  -10.536 58.188  1.00 36.51  ? 249  LEU B N   1 
ATOM   5689 C  CA  . LEU B 1 249 ? 23.300  -11.918 58.099  1.00 37.24  ? 249  LEU B CA  1 
ATOM   5690 C  C   . LEU B 1 249 ? 24.080  -12.644 57.014  1.00 36.84  ? 249  LEU B C   1 
ATOM   5691 O  O   . LEU B 1 249 ? 24.437  -12.059 55.990  1.00 37.81  ? 249  LEU B O   1 
ATOM   5692 C  CB  . LEU B 1 249 ? 21.808  -11.982 57.783  1.00 40.99  ? 249  LEU B CB  1 
ATOM   5693 C  CG  . LEU B 1 249 ? 20.897  -11.308 58.800  1.00 35.03  ? 249  LEU B CG  1 
ATOM   5694 C  CD1 . LEU B 1 249 ? 19.436  -11.369 58.290  1.00 35.69  ? 249  LEU B CD1 1 
ATOM   5695 C  CD2 . LEU B 1 249 ? 21.047  -11.919 60.176  1.00 33.30  ? 249  LEU B CD2 1 
ATOM   5696 N  N   . ASP B 1 250 ? 24.329  -13.933 57.225  1.00 37.39  ? 250  ASP B N   1 
ATOM   5697 C  CA  . ASP B 1 250 ? 24.921  -14.719 56.152  1.00 41.06  ? 250  ASP B CA  1 
ATOM   5698 C  C   . ASP B 1 250 ? 23.829  -15.237 55.211  1.00 40.55  ? 250  ASP B C   1 
ATOM   5699 O  O   . ASP B 1 250 ? 22.627  -15.146 55.486  1.00 36.51  ? 250  ASP B O   1 
ATOM   5700 C  CB  . ASP B 1 250 ? 25.721  -15.901 56.686  1.00 40.82  ? 250  ASP B CB  1 
ATOM   5701 C  CG  . ASP B 1 250 ? 24.980  -16.658 57.740  1.00 46.32  ? 250  ASP B CG  1 
ATOM   5702 O  OD1 . ASP B 1 250 ? 24.307  -17.640 57.363  1.00 46.43  ? 250  ASP B OD1 1 
ATOM   5703 O  OD2 . ASP B 1 250 ? 25.085  -16.303 58.939  1.00 53.18  ? 250  ASP B OD2 1 
ATOM   5704 N  N   . ASP B 1 251 ? 24.267  -15.815 54.089  1.00 42.68  ? 251  ASP B N   1 
ATOM   5705 C  CA  . ASP B 1 251 ? 23.312  -16.209 53.058  1.00 45.98  ? 251  ASP B CA  1 
ATOM   5706 C  C   . ASP B 1 251 ? 22.340  -17.262 53.575  1.00 40.66  ? 251  ASP B C   1 
ATOM   5707 O  O   . ASP B 1 251 ? 21.137  -17.198 53.296  1.00 42.28  ? 251  ASP B O   1 
ATOM   5708 C  CB  . ASP B 1 251 ? 24.052  -16.730 51.824  1.00 46.99  ? 251  ASP B CB  1 
ATOM   5709 C  CG  . ASP B 1 251 ? 24.595  -15.609 50.956  1.00 54.86  ? 251  ASP B CG  1 
ATOM   5710 O  OD1 . ASP B 1 251 ? 24.102  -14.466 51.083  1.00 54.20  ? 251  ASP B OD1 1 
ATOM   5711 O  OD2 . ASP B 1 251 ? 25.504  -15.878 50.137  1.00 56.44  ? 251  ASP B OD2 1 
ATOM   5712 N  N   . GLU B 1 252 ? 22.845  -18.255 54.305  1.00 39.14  ? 252  GLU B N   1 
ATOM   5713 C  CA  . GLU B 1 252 ? 21.974  -19.320 54.787  1.00 40.82  ? 252  GLU B CA  1 
ATOM   5714 C  C   . GLU B 1 252 ? 20.872  -18.760 55.686  1.00 38.07  ? 252  GLU B C   1 
ATOM   5715 O  O   . GLU B 1 252 ? 19.699  -19.137 55.560  1.00 38.09  ? 252  GLU B O   1 
ATOM   5716 C  CB  . GLU B 1 252 ? 22.798  -20.374 55.525  1.00 46.48  ? 252  GLU B CB  1 
ATOM   5717 C  CG  . GLU B 1 252 ? 21.970  -21.504 56.096  1.00 45.12  ? 252  GLU B CG  1 
ATOM   5718 C  CD  . GLU B 1 252 ? 22.766  -22.386 57.029  1.00 56.62  ? 252  GLU B CD  1 
ATOM   5719 O  OE1 . GLU B 1 252 ? 23.874  -22.802 56.626  1.00 65.18  ? 252  GLU B OE1 1 
ATOM   5720 O  OE2 . GLU B 1 252 ? 22.291  -22.653 58.163  1.00 54.29  ? 252  GLU B OE2 1 
ATOM   5721 N  N   . ASN B 1 253 ? 21.225  -17.852 56.599  1.00 35.42  ? 253  ASN B N   1 
ATOM   5722 C  CA  . ASN B 1 253 ? 20.202  -17.285 57.478  1.00 33.90  ? 253  ASN B CA  1 
ATOM   5723 C  C   . ASN B 1 253 ? 19.238  -16.380 56.709  1.00 35.08  ? 253  ASN B C   1 
ATOM   5724 O  O   . ASN B 1 253 ? 18.028  -16.383 56.979  1.00 33.01  ? 253  ASN B O   1 
ATOM   5725 C  CB  . ASN B 1 253 ? 20.847  -16.523 58.635  1.00 35.50  ? 253  ASN B CB  1 
ATOM   5726 C  CG  . ASN B 1 253 ? 19.818  -16.063 59.670  1.00 30.72  ? 253  ASN B CG  1 
ATOM   5727 O  OD1 . ASN B 1 253 ? 19.494  -14.877 59.764  1.00 33.41  ? 253  ASN B OD1 1 
ATOM   5728 N  ND2 . ASN B 1 253 ? 19.280  -17.005 60.424  1.00 33.31  ? 253  ASN B ND2 1 
ATOM   5729 N  N   . ILE B 1 254 ? 19.746  -15.605 55.747  1.00 34.63  ? 254  ILE B N   1 
ATOM   5730 C  CA  . ILE B 1 254 ? 18.862  -14.810 54.895  1.00 34.26  ? 254  ILE B CA  1 
ATOM   5731 C  C   . ILE B 1 254 ? 17.771  -15.693 54.286  1.00 35.44  ? 254  ILE B C   1 
ATOM   5732 O  O   . ILE B 1 254 ? 16.585  -15.342 54.297  1.00 33.67  ? 254  ILE B O   1 
ATOM   5733 C  CB  . ILE B 1 254 ? 19.666  -14.086 53.797  1.00 36.05  ? 254  ILE B CB  1 
ATOM   5734 C  CG1 . ILE B 1 254 ? 20.546  -12.971 54.384  1.00 34.50  ? 254  ILE B CG1 1 
ATOM   5735 C  CG2 . ILE B 1 254 ? 18.714  -13.528 52.743  1.00 38.75  ? 254  ILE B CG2 1 
ATOM   5736 C  CD1 . ILE B 1 254 ? 21.599  -12.477 53.416  1.00 41.66  ? 254  ILE B CD1 1 
ATOM   5737 N  N   . ARG B 1 255 ? 18.155  -16.857 53.749  1.00 32.61  ? 255  ARG B N   1 
ATOM   5738 C  CA  . ARG B 1 255 ? 17.156  -17.727 53.125  1.00 36.75  ? 255  ARG B CA  1 
ATOM   5739 C  C   . ARG B 1 255 ? 16.083  -18.120 54.125  1.00 34.38  ? 255  ARG B C   1 
ATOM   5740 O  O   . ARG B 1 255 ? 14.890  -18.133 53.800  1.00 38.54  ? 255  ARG B O   1 
ATOM   5741 C  CB  . ARG B 1 255 ? 17.799  -18.986 52.543  1.00 37.88  ? 255  ARG B CB  1 
ATOM   5742 C  CG  . ARG B 1 255 ? 18.780  -18.751 51.392  1.00 47.42  ? 255  ARG B CG  1 
ATOM   5743 C  CD  . ARG B 1 255 ? 19.298  -20.078 50.813  1.00 53.28  ? 255  ARG B CD  1 
ATOM   5744 N  NE  . ARG B 1 255 ? 18.239  -20.866 50.192  1.00 58.06  ? 255  ARG B NE  1 
ATOM   5745 C  CZ  . ARG B 1 255 ? 17.838  -20.740 48.933  1.00 59.85  ? 255  ARG B CZ  1 
ATOM   5746 N  NH1 . ARG B 1 255 ? 18.418  -19.883 48.101  1.00 56.28  ? 255  ARG B NH1 1 
ATOM   5747 N  NH2 . ARG B 1 255 ? 16.826  -21.490 48.496  1.00 52.53  ? 255  ARG B NH2 1 
ATOM   5748 N  N   . TYR B 1 256 ? 16.495  -18.461 55.348  1.00 33.51  ? 256  TYR B N   1 
ATOM   5749 C  CA  . TYR B 1 256 ? 15.520  -18.798 56.378  1.00 34.01  ? 256  TYR B CA  1 
ATOM   5750 C  C   . TYR B 1 256 ? 14.639  -17.610 56.731  1.00 31.75  ? 256  TYR B C   1 
ATOM   5751 O  O   . TYR B 1 256 ? 13.456  -17.786 57.034  1.00 31.16  ? 256  TYR B O   1 
ATOM   5752 C  CB  . TYR B 1 256 ? 16.222  -19.295 57.639  1.00 29.84  ? 256  TYR B CB  1 
ATOM   5753 C  CG  . TYR B 1 256 ? 16.813  -20.674 57.528  1.00 34.13  ? 256  TYR B CG  1 
ATOM   5754 C  CD1 . TYR B 1 256 ? 16.124  -21.712 56.908  1.00 33.93  ? 256  TYR B CD1 1 
ATOM   5755 C  CD2 . TYR B 1 256 ? 18.067  -20.951 58.074  1.00 38.56  ? 256  TYR B CD2 1 
ATOM   5756 C  CE1 . TYR B 1 256 ? 16.681  -22.989 56.823  1.00 37.47  ? 256  TYR B CE1 1 
ATOM   5757 C  CE2 . TYR B 1 256 ? 18.622  -22.212 57.992  1.00 40.17  ? 256  TYR B CE2 1 
ATOM   5758 C  CZ  . TYR B 1 256 ? 17.931  -23.226 57.370  1.00 41.76  ? 256  TYR B CZ  1 
ATOM   5759 O  OH  . TYR B 1 256 ? 18.504  -24.479 57.301  1.00 46.49  ? 256  TYR B OH  1 
ATOM   5760 N  N   . GLN B 1 257 ? 15.207  -16.401 56.774  1.00 32.49  ? 257  GLN B N   1 
ATOM   5761 C  CA  . GLN B 1 257 ? 14.375  -15.246 57.101  1.00 32.63  ? 257  GLN B CA  1 
ATOM   5762 C  C   . GLN B 1 257 ? 13.331  -15.004 56.022  1.00 33.97  ? 257  GLN B C   1 
ATOM   5763 O  O   . GLN B 1 257 ? 12.189  -14.649 56.330  1.00 33.74  ? 257  GLN B O   1 
ATOM   5764 C  CB  . GLN B 1 257 ? 15.221  -13.986 57.308  1.00 34.35  ? 257  GLN B CB  1 
ATOM   5765 C  CG  . GLN B 1 257 ? 16.320  -14.092 58.394  1.00 30.50  ? 257  GLN B CG  1 
ATOM   5766 C  CD  . GLN B 1 257 ? 15.796  -14.326 59.818  1.00 34.60  ? 257  GLN B CD  1 
ATOM   5767 O  OE1 . GLN B 1 257 ? 14.586  -14.324 60.076  1.00 29.40  ? 257  GLN B OE1 1 
ATOM   5768 N  NE2 . GLN B 1 257 ? 16.729  -14.527 60.758  1.00 31.49  ? 257  GLN B NE2 1 
ATOM   5769 N  N   . ILE B 1 258 ? 13.700  -15.187 54.753  1.00 33.35  ? 258  ILE B N   1 
ATOM   5770 C  CA  . ILE B 1 258 ? 12.733  -14.970 53.677  1.00 33.05  ? 258  ILE B CA  1 
ATOM   5771 C  C   . ILE B 1 258 ? 11.581  -15.960 53.795  1.00 33.23  ? 258  ILE B C   1 
ATOM   5772 O  O   . ILE B 1 258 ? 10.406  -15.581 53.705  1.00 33.99  ? 258  ILE B O   1 
ATOM   5773 C  CB  . ILE B 1 258 ? 13.424  -15.046 52.306  1.00 37.24  ? 258  ILE B CB  1 
ATOM   5774 C  CG1 . ILE B 1 258 ? 14.440  -13.894 52.198  1.00 36.37  ? 258  ILE B CG1 1 
ATOM   5775 C  CG2 . ILE B 1 258 ? 12.375  -14.944 51.183  1.00 36.45  ? 258  ILE B CG2 1 
ATOM   5776 C  CD1 . ILE B 1 258 ? 15.323  -13.938 50.938  1.00 38.52  ? 258  ILE B CD1 1 
ATOM   5777 N  N   . ILE B 1 259 ? 11.893  -17.239 54.015  1.00 33.11  ? 259  ILE B N   1 
ATOM   5778 C  CA  . ILE B 1 259 ? 10.836  -18.227 54.229  1.00 34.90  ? 259  ILE B CA  1 
ATOM   5779 C  C   . ILE B 1 259 ? 9.985   -17.838 55.429  1.00 34.86  ? 259  ILE B C   1 
ATOM   5780 O  O   . ILE B 1 259 ? 8.742   -17.890 55.384  1.00 30.81  ? 259  ILE B O   1 
ATOM   5781 C  CB  . ILE B 1 259 ? 11.444  -19.633 54.405  1.00 33.54  ? 259  ILE B CB  1 
ATOM   5782 C  CG1 . ILE B 1 259 ? 12.050  -20.132 53.088  1.00 38.79  ? 259  ILE B CG1 1 
ATOM   5783 C  CG2 . ILE B 1 259 ? 10.412  -20.606 54.953  1.00 38.34  ? 259  ILE B CG2 1 
ATOM   5784 C  CD1 . ILE B 1 259 ? 12.962  -21.309 53.274  1.00 43.66  ? 259  ILE B CD1 1 
ATOM   5785 N  N   . THR B 1 260 ? 10.641  -17.436 56.519  1.00 29.34  ? 260  THR B N   1 
ATOM   5786 C  CA  . THR B 1 260 ? 9.916   -17.071 57.733  1.00 30.16  ? 260  THR B CA  1 
ATOM   5787 C  C   . THR B 1 260 ? 8.946   -15.926 57.456  1.00 32.12  ? 260  THR B C   1 
ATOM   5788 O  O   . THR B 1 260 ? 7.759   -15.989 57.809  1.00 31.97  ? 260  THR B O   1 
ATOM   5789 C  CB  . THR B 1 260 ? 10.924  -16.689 58.819  1.00 30.68  ? 260  THR B CB  1 
ATOM   5790 O  OG1 . THR B 1 260 ? 11.730  -17.831 59.129  1.00 32.57  ? 260  THR B OG1 1 
ATOM   5791 C  CG2 . THR B 1 260 ? 10.214  -16.200 60.086  1.00 31.18  ? 260  THR B CG2 1 
ATOM   5792 N  N   . PHE B 1 261 ? 9.427   -14.878 56.792  1.00 31.07  ? 261  PHE B N   1 
ATOM   5793 C  CA  . PHE B 1 261 ? 8.562   -13.719 56.584  1.00 33.57  ? 261  PHE B CA  1 
ATOM   5794 C  C   . PHE B 1 261 ? 7.497   -13.968 55.517  1.00 35.05  ? 261  PHE B C   1 
ATOM   5795 O  O   . PHE B 1 261 ? 6.395   -13.407 55.597  1.00 34.37  ? 261  PHE B O   1 
ATOM   5796 C  CB  . PHE B 1 261 ? 9.417   -12.489 56.260  1.00 32.21  ? 261  PHE B CB  1 
ATOM   5797 C  CG  . PHE B 1 261 ? 10.024  -11.852 57.486  1.00 35.84  ? 261  PHE B CG  1 
ATOM   5798 C  CD1 . PHE B 1 261 ? 9.339   -10.883 58.197  1.00 35.76  ? 261  PHE B CD1 1 
ATOM   5799 C  CD2 . PHE B 1 261 ? 11.266  -12.259 57.956  1.00 39.17  ? 261  PHE B CD2 1 
ATOM   5800 C  CE1 . PHE B 1 261 ? 9.879   -10.316 59.329  1.00 35.51  ? 261  PHE B CE1 1 
ATOM   5801 C  CE2 . PHE B 1 261 ? 11.806  -11.693 59.086  1.00 36.64  ? 261  PHE B CE2 1 
ATOM   5802 C  CZ  . PHE B 1 261 ? 11.109  -10.720 59.779  1.00 38.37  ? 261  PHE B CZ  1 
ATOM   5803 N  N   . LEU B 1 262 ? 7.777   -14.803 54.519  1.00 32.83  ? 262  LEU B N   1 
ATOM   5804 C  CA  . LEU B 1 262 ? 6.720   -15.096 53.558  1.00 35.90  ? 262  LEU B CA  1 
ATOM   5805 C  C   . LEU B 1 262 ? 5.570   -15.826 54.239  1.00 37.40  ? 262  LEU B C   1 
ATOM   5806 O  O   . LEU B 1 262 ? 4.392   -15.554 53.953  1.00 37.22  ? 262  LEU B O   1 
ATOM   5807 C  CB  . LEU B 1 262 ? 7.265   -15.920 52.390  1.00 33.32  ? 262  LEU B CB  1 
ATOM   5808 C  CG  . LEU B 1 262 ? 8.155   -15.138 51.417  1.00 33.81  ? 262  LEU B CG  1 
ATOM   5809 C  CD1 . LEU B 1 262 ? 8.690   -16.080 50.361  1.00 32.73  ? 262  LEU B CD1 1 
ATOM   5810 C  CD2 . LEU B 1 262 ? 7.431   -13.931 50.800  1.00 33.80  ? 262  LEU B CD2 1 
ATOM   5811 N  N   . ILE B 1 263 ? 5.896   -16.709 55.187  1.00 33.04  ? 263  ILE B N   1 
ATOM   5812 C  CA  . ILE B 1 263 ? 4.878   -17.481 55.903  1.00 33.44  ? 263  ILE B CA  1 
ATOM   5813 C  C   . ILE B 1 263 ? 4.251   -16.662 57.020  1.00 34.83  ? 263  ILE B C   1 
ATOM   5814 O  O   . ILE B 1 263 ? 3.046   -16.382 57.011  1.00 35.50  ? 263  ILE B O   1 
ATOM   5815 C  CB  . ILE B 1 263 ? 5.487   -18.781 56.445  1.00 34.22  ? 263  ILE B CB  1 
ATOM   5816 C  CG1 . ILE B 1 263 ? 5.837   -19.712 55.279  1.00 38.39  ? 263  ILE B CG1 1 
ATOM   5817 C  CG2 . ILE B 1 263 ? 4.535   -19.482 57.409  1.00 36.30  ? 263  ILE B CG2 1 
ATOM   5818 C  CD1 . ILE B 1 263 ? 6.597   -20.929 55.719  1.00 36.28  ? 263  ILE B CD1 1 
ATOM   5819 N  N   . ALA B 1 264 ? 5.051   -16.295 58.021  1.00 32.81  ? 264  ALA B N   1 
ATOM   5820 C  CA  . ALA B 1 264 ? 4.520   -15.533 59.140  1.00 36.90  ? 264  ALA B CA  1 
ATOM   5821 C  C   . ALA B 1 264 ? 4.037   -14.159 58.714  1.00 34.09  ? 264  ALA B C   1 
ATOM   5822 O  O   . ALA B 1 264 ? 3.176   -13.579 59.389  1.00 34.87  ? 264  ALA B O   1 
ATOM   5823 C  CB  . ALA B 1 264 ? 5.586   -15.402 60.239  1.00 34.56  ? 264  ALA B CB  1 
ATOM   5824 N  N   . GLY B 1 265 ? 4.560   -13.631 57.603  1.00 33.82  ? 265  GLY B N   1 
ATOM   5825 C  CA  . GLY B 1 265 ? 4.193   -12.335 57.106  1.00 34.65  ? 265  GLY B CA  1 
ATOM   5826 C  C   . GLY B 1 265 ? 2.889   -12.266 56.348  1.00 36.09  ? 265  GLY B C   1 
ATOM   5827 O  O   . GLY B 1 265 ? 2.520   -11.168 55.927  1.00 36.32  ? 265  GLY B O   1 
ATOM   5828 N  N   . HIS B 1 266 ? 2.181   -13.385 56.162  1.00 34.53  ? 266  HIS B N   1 
ATOM   5829 C  CA  . HIS B 1 266 ? 0.890   -13.324 55.472  1.00 34.66  ? 266  HIS B CA  1 
ATOM   5830 C  C   . HIS B 1 266 ? -0.184  -14.238 56.051  1.00 35.38  ? 266  HIS B C   1 
ATOM   5831 O  O   . HIS B 1 266 ? -1.362  -13.854 56.079  1.00 33.72  ? 266  HIS B O   1 
ATOM   5832 C  CB  . HIS B 1 266 ? 1.061   -13.647 53.989  1.00 34.42  ? 266  HIS B CB  1 
ATOM   5833 C  CG  . HIS B 1 266 ? 0.784   -15.077 53.643  1.00 36.07  ? 266  HIS B CG  1 
ATOM   5834 N  ND1 . HIS B 1 266 ? 1.764   -16.045 53.649  1.00 35.20  ? 266  HIS B ND1 1 
ATOM   5835 C  CD2 . HIS B 1 266 ? -0.359  -15.703 53.263  1.00 32.72  ? 266  HIS B CD2 1 
ATOM   5836 C  CE1 . HIS B 1 266 ? 1.240   -17.210 53.305  1.00 33.82  ? 266  HIS B CE1 1 
ATOM   5837 N  NE2 . HIS B 1 266 ? -0.048  -17.029 53.061  1.00 36.08  ? 266  HIS B NE2 1 
ATOM   5838 N  N   . GLU B 1 267 ? 0.186   -15.455 56.472  1.00 33.56  ? 267  GLU B N   1 
ATOM   5839 C  CA  . GLU B 1 267 ? -0.831  -16.457 56.805  1.00 33.89  ? 267  GLU B CA  1 
ATOM   5840 C  C   . GLU B 1 267 ? -1.767  -15.999 57.917  1.00 33.67  ? 267  GLU B C   1 
ATOM   5841 O  O   . GLU B 1 267 ? -2.996  -16.086 57.786  1.00 33.70  ? 267  GLU B O   1 
ATOM   5842 C  CB  . GLU B 1 267 ? -0.173  -17.785 57.154  1.00 32.98  ? 267  GLU B CB  1 
ATOM   5843 C  CG  . GLU B 1 267 ? -1.109  -18.647 57.988  1.00 37.17  ? 267  GLU B CG  1 
ATOM   5844 C  CD  . GLU B 1 267 ? -2.233  -19.310 57.223  1.00 43.19  ? 267  GLU B CD  1 
ATOM   5845 O  OE1 . GLU B 1 267 ? -3.206  -19.748 57.889  1.00 43.83  ? 267  GLU B OE1 1 
ATOM   5846 O  OE2 . GLU B 1 267 ? -2.160  -19.399 55.988  1.00 39.45  ? 267  GLU B OE2 1 
ATOM   5847 N  N   . THR B 1 268 ? -1.210  -15.513 59.011  1.00 30.23  ? 268  THR B N   1 
ATOM   5848 C  CA  . THR B 1 268 ? -2.041  -15.122 60.136  1.00 33.62  ? 268  THR B CA  1 
ATOM   5849 C  C   . THR B 1 268 ? -2.846  -13.869 59.845  1.00 32.25  ? 268  THR B C   1 
ATOM   5850 O  O   . THR B 1 268 ? -3.910  -13.670 60.447  1.00 34.23  ? 268  THR B O   1 
ATOM   5851 C  CB  . THR B 1 268 ? -1.164  -14.899 61.353  1.00 36.08  ? 268  THR B CB  1 
ATOM   5852 O  OG1 . THR B 1 268 ? -0.009  -14.147 60.947  1.00 33.35  ? 268  THR B OG1 1 
ATOM   5853 C  CG2 . THR B 1 268 ? -0.745  -16.262 61.960  1.00 34.02  ? 268  THR B CG2 1 
ATOM   5854 N  N   . THR B 1 269 ? -2.341  -12.998 58.972  1.00 29.04  ? 269  THR B N   1 
ATOM   5855 C  CA  . THR B 1 269 ? -3.104  -11.806 58.614  1.00 27.63  ? 269  THR B CA  1 
ATOM   5856 C  C   . THR B 1 269 ? -4.292  -12.173 57.731  1.00 31.96  ? 269  THR B C   1 
ATOM   5857 O  O   . THR B 1 269 ? -5.364  -11.556 57.831  1.00 28.91  ? 269  THR B O   1 
ATOM   5858 C  CB  . THR B 1 269 ? -2.182  -10.793 57.930  1.00 29.11  ? 269  THR B CB  1 
ATOM   5859 O  OG1 . THR B 1 269 ? -1.093  -10.486 58.807  1.00 29.95  ? 269  THR B OG1 1 
ATOM   5860 C  CG2 . THR B 1 269 ? -2.926  -9.508  57.626  1.00 26.96  ? 269  THR B CG2 1 
ATOM   5861 N  N   . SER B 1 270 ? -4.120  -13.175 56.866  1.00 30.00  ? 270  SER B N   1 
ATOM   5862 C  CA  . SER B 1 270 ? -5.260  -13.686 56.107  1.00 29.72  ? 270  SER B CA  1 
ATOM   5863 C  C   . SER B 1 270 ? -6.327  -14.254 57.042  1.00 31.59  ? 270  SER B C   1 
ATOM   5864 O  O   . SER B 1 270 ? -7.526  -14.018 56.848  1.00 32.06  ? 270  SER B O   1 
ATOM   5865 C  CB  . SER B 1 270 ? -4.774  -14.745 55.110  1.00 30.04  ? 270  SER B CB  1 
ATOM   5866 O  OG  . SER B 1 270 ? -5.875  -15.490 54.631  1.00 39.72  ? 270  SER B OG  1 
ATOM   5867 N  N   . GLY B 1 271 ? -5.909  -14.990 58.077  1.00 29.71  ? 271  GLY B N   1 
ATOM   5868 C  CA  . GLY B 1 271 ? -6.868  -15.484 59.049  1.00 30.37  ? 271  GLY B CA  1 
ATOM   5869 C  C   . GLY B 1 271 ? -7.567  -14.360 59.790  1.00 28.50  ? 271  GLY B C   1 
ATOM   5870 O  O   . GLY B 1 271 ? -8.784  -14.396 59.980  1.00 31.38  ? 271  GLY B O   1 
ATOM   5871 N  N   . LEU B 1 272 ? -6.818  -13.326 60.177  1.00 29.88  ? 272  LEU B N   1 
ATOM   5872 C  CA  . LEU B 1 272 ? -7.434  -12.201 60.889  1.00 30.96  ? 272  LEU B CA  1 
ATOM   5873 C  C   . LEU B 1 272 ? -8.511  -11.536 60.036  1.00 30.04  ? 272  LEU B C   1 
ATOM   5874 O  O   . LEU B 1 272 ? -9.644  -11.318 60.491  1.00 30.97  ? 272  LEU B O   1 
ATOM   5875 C  CB  . LEU B 1 272 ? -6.365  -11.179 61.284  1.00 32.32  ? 272  LEU B CB  1 
ATOM   5876 C  CG  . LEU B 1 272 ? -6.856  -9.812  61.813  1.00 29.18  ? 272  LEU B CG  1 
ATOM   5877 C  CD1 . LEU B 1 272 ? -7.845  -9.964  62.986  1.00 28.79  ? 272  LEU B CD1 1 
ATOM   5878 C  CD2 . LEU B 1 272 ? -5.650  -8.964  62.249  1.00 31.82  ? 272  LEU B CD2 1 
ATOM   5879 N  N   . LEU B 1 273 ? -8.161  -11.173 58.802  1.00 27.93  ? 273  LEU B N   1 
ATOM   5880 C  CA  . LEU B 1 273 ? -9.134  -10.546 57.916  1.00 27.17  ? 273  LEU B CA  1 
ATOM   5881 C  C   . LEU B 1 273 ? -10.352 -11.439 57.727  1.00 30.97  ? 273  LEU B C   1 
ATOM   5882 O  O   . LEU B 1 273 ? -11.487 -10.951 57.714  1.00 32.09  ? 273  LEU B O   1 
ATOM   5883 C  CB  . LEU B 1 273 ? -8.473  -10.217 56.572  1.00 28.94  ? 273  LEU B CB  1 
ATOM   5884 C  CG  . LEU B 1 273 ? -7.583  -8.978  56.620  1.00 31.72  ? 273  LEU B CG  1 
ATOM   5885 C  CD1 . LEU B 1 273 ? -6.658  -8.900  55.400  1.00 30.37  ? 273  LEU B CD1 1 
ATOM   5886 C  CD2 . LEU B 1 273 ? -8.465  -7.717  56.734  1.00 32.00  ? 273  LEU B CD2 1 
ATOM   5887 N  N   . SER B 1 274 ? -10.135 -12.756 57.604  1.00 28.86  ? 274  SER B N   1 
ATOM   5888 C  CA  . SER B 1 274 ? -11.250 -13.679 57.406  1.00 31.02  ? 274  SER B CA  1 
ATOM   5889 C  C   . SER B 1 274 ? -12.158 -13.719 58.632  1.00 32.01  ? 274  SER B C   1 
ATOM   5890 O  O   . SER B 1 274 ? -13.387 -13.653 58.503  1.00 31.08  ? 274  SER B O   1 
ATOM   5891 C  CB  . SER B 1 274 ? -10.723 -15.081 57.061  1.00 32.78  ? 274  SER B CB  1 
ATOM   5892 O  OG  . SER B 1 274 ? -9.970  -15.075 55.844  1.00 31.44  ? 274  SER B OG  1 
ATOM   5893 N  N   . PHE B 1 275 ? -11.572 -13.847 59.834  1.00 29.47  ? 275  PHE B N   1 
ATOM   5894 C  CA  . PHE B 1 275 ? -12.380 -13.829 61.051  1.00 28.92  ? 275  PHE B CA  1 
ATOM   5895 C  C   . PHE B 1 275 ? -13.097 -12.495 61.216  1.00 32.29  ? 275  PHE B C   1 
ATOM   5896 O  O   . PHE B 1 275 ? -14.266 -12.449 61.629  1.00 29.53  ? 275  PHE B O   1 
ATOM   5897 C  CB  . PHE B 1 275 ? -11.500 -14.123 62.271  1.00 27.39  ? 275  PHE B CB  1 
ATOM   5898 C  CG  . PHE B 1 275 ? -11.258 -15.589 62.515  1.00 32.20  ? 275  PHE B CG  1 
ATOM   5899 C  CD1 . PHE B 1 275 ? -12.301 -16.427 62.911  1.00 31.12  ? 275  PHE B CD1 1 
ATOM   5900 C  CD2 . PHE B 1 275 ? -9.979  -16.125 62.369  1.00 29.72  ? 275  PHE B CD2 1 
ATOM   5901 C  CE1 . PHE B 1 275 ? -12.082 -17.785 63.154  1.00 31.38  ? 275  PHE B CE1 1 
ATOM   5902 C  CE2 . PHE B 1 275 ? -9.738  -17.474 62.613  1.00 33.31  ? 275  PHE B CE2 1 
ATOM   5903 C  CZ  . PHE B 1 275 ? -10.795 -18.311 63.001  1.00 35.72  ? 275  PHE B CZ  1 
ATOM   5904 N  N   . ALA B 1 276 ? -12.418 -11.395 60.891  1.00 31.30  ? 276  ALA B N   1 
ATOM   5905 C  CA  . ALA B 1 276 ? -13.038 -10.084 61.046  1.00 30.23  ? 276  ALA B CA  1 
ATOM   5906 C  C   . ALA B 1 276 ? -14.284 -9.958  60.173  1.00 31.92  ? 276  ALA B C   1 
ATOM   5907 O  O   . ALA B 1 276 ? -15.348 -9.523  60.641  1.00 31.62  ? 276  ALA B O   1 
ATOM   5908 C  CB  . ALA B 1 276 ? -12.029 -8.985  60.709  1.00 31.32  ? 276  ALA B CB  1 
ATOM   5909 N  N   . LEU B 1 277 ? -14.175 -10.331 58.896  1.00 29.25  ? 277  LEU B N   1 
ATOM   5910 C  CA  . LEU B 1 277 ? -15.358 -10.243 58.039  1.00 30.08  ? 277  LEU B CA  1 
ATOM   5911 C  C   . LEU B 1 277 ? -16.449 -11.192 58.514  1.00 27.90  ? 277  LEU B C   1 
ATOM   5912 O  O   . LEU B 1 277 ? -17.647 -10.853 58.467  1.00 31.44  ? 277  LEU B O   1 
ATOM   5913 C  CB  . LEU B 1 277 ? -14.985 -10.534 56.589  1.00 28.57  ? 277  LEU B CB  1 
ATOM   5914 C  CG  . LEU B 1 277 ? -16.161 -10.326 55.618  1.00 33.43  ? 277  LEU B CG  1 
ATOM   5915 C  CD1 . LEU B 1 277 ? -16.646 -8.878  55.654  1.00 31.76  ? 277  LEU B CD1 1 
ATOM   5916 C  CD2 . LEU B 1 277 ? -15.708 -10.694 54.212  1.00 33.24  ? 277  LEU B CD2 1 
ATOM   5917 N  N   . TYR B 1 278 ? -16.065 -12.393 58.954  1.00 28.72  ? 278  TYR B N   1 
ATOM   5918 C  CA  . TYR B 1 278 ? -17.050 -13.299 59.541  1.00 28.28  ? 278  TYR B CA  1 
ATOM   5919 C  C   . TYR B 1 278 ? -17.792 -12.611 60.677  1.00 32.12  ? 278  TYR B C   1 
ATOM   5920 O  O   . TYR B 1 278 ? -19.027 -12.576 60.698  1.00 29.57  ? 278  TYR B O   1 
ATOM   5921 C  CB  . TYR B 1 278 ? -16.385 -14.588 60.046  1.00 28.62  ? 278  TYR B CB  1 
ATOM   5922 C  CG  . TYR B 1 278 ? -17.296 -15.391 60.946  1.00 29.70  ? 278  TYR B CG  1 
ATOM   5923 C  CD1 . TYR B 1 278 ? -18.220 -16.279 60.408  1.00 31.74  ? 278  TYR B CD1 1 
ATOM   5924 C  CD2 . TYR B 1 278 ? -17.251 -15.241 62.337  1.00 31.69  ? 278  TYR B CD2 1 
ATOM   5925 C  CE1 . TYR B 1 278 ? -19.081 -16.998 61.234  1.00 32.29  ? 278  TYR B CE1 1 
ATOM   5926 C  CE2 . TYR B 1 278 ? -18.109 -15.946 63.167  1.00 34.28  ? 278  TYR B CE2 1 
ATOM   5927 C  CZ  . TYR B 1 278 ? -19.024 -16.824 62.608  1.00 32.89  ? 278  TYR B CZ  1 
ATOM   5928 O  OH  . TYR B 1 278 ? -19.865 -17.533 63.440  1.00 35.24  ? 278  TYR B OH  1 
ATOM   5929 N  N   . PHE B 1 279 ? -17.055 -12.037 61.635  1.00 30.52  ? 279  PHE B N   1 
ATOM   5930 C  CA  . PHE B 1 279 ? -17.761 -11.425 62.756  1.00 31.27  ? 279  PHE B CA  1 
ATOM   5931 C  C   . PHE B 1 279 ? -18.586 -10.226 62.318  1.00 30.05  ? 279  PHE B C   1 
ATOM   5932 O  O   . PHE B 1 279 ? -19.657 -9.984  62.879  1.00 30.41  ? 279  PHE B O   1 
ATOM   5933 C  CB  . PHE B 1 279 ? -16.781 -11.037 63.859  1.00 31.65  ? 279  PHE B CB  1 
ATOM   5934 C  CG  . PHE B 1 279 ? -16.387 -12.201 64.713  1.00 32.06  ? 279  PHE B CG  1 
ATOM   5935 C  CD1 . PHE B 1 279 ? -17.353 -12.919 65.404  1.00 29.46  ? 279  PHE B CD1 1 
ATOM   5936 C  CD2 . PHE B 1 279 ? -15.058 -12.612 64.788  1.00 34.69  ? 279  PHE B CD2 1 
ATOM   5937 C  CE1 . PHE B 1 279 ? -16.994 -14.002 66.189  1.00 32.77  ? 279  PHE B CE1 1 
ATOM   5938 C  CE2 . PHE B 1 279 ? -14.692 -13.706 65.567  1.00 34.12  ? 279  PHE B CE2 1 
ATOM   5939 C  CZ  . PHE B 1 279 ? -15.656 -14.394 66.279  1.00 33.01  ? 279  PHE B CZ  1 
ATOM   5940 N  N   . LEU B 1 280 ? -18.136 -9.485  61.306  1.00 31.68  ? 280  LEU B N   1 
ATOM   5941 C  CA  . LEU B 1 280 ? -18.914 -8.332  60.876  1.00 30.12  ? 280  LEU B CA  1 
ATOM   5942 C  C   . LEU B 1 280 ? -20.254 -8.764  60.285  1.00 32.01  ? 280  LEU B C   1 
ATOM   5943 O  O   . LEU B 1 280 ? -21.293 -8.186  60.611  1.00 32.77  ? 280  LEU B O   1 
ATOM   5944 C  CB  . LEU B 1 280 ? -18.129 -7.496  59.872  1.00 32.94  ? 280  LEU B CB  1 
ATOM   5945 C  CG  . LEU B 1 280 ? -16.934 -6.749  60.469  1.00 32.37  ? 280  LEU B CG  1 
ATOM   5946 C  CD1 . LEU B 1 280 ? -16.143 -6.060  59.365  1.00 33.96  ? 280  LEU B CD1 1 
ATOM   5947 C  CD2 . LEU B 1 280 ? -17.378 -5.747  61.509  1.00 37.39  ? 280  LEU B CD2 1 
ATOM   5948 N  N   . VAL B 1 281 ? -20.259 -9.784  59.420  1.00 33.13  ? 281  VAL B N   1 
ATOM   5949 C  CA  . VAL B 1 281 ? -21.537 -10.160 58.802  1.00 31.86  ? 281  VAL B CA  1 
ATOM   5950 C  C   . VAL B 1 281 ? -22.479 -10.828 59.799  1.00 34.49  ? 281  VAL B C   1 
ATOM   5951 O  O   . VAL B 1 281 ? -23.705 -10.828 59.585  1.00 35.03  ? 281  VAL B O   1 
ATOM   5952 C  CB  . VAL B 1 281 ? -21.328 -11.046 57.550  1.00 32.45  ? 281  VAL B CB  1 
ATOM   5953 C  CG1 . VAL B 1 281 ? -20.428 -10.350 56.552  1.00 32.92  ? 281  VAL B CG1 1 
ATOM   5954 C  CG2 . VAL B 1 281 ? -20.809 -12.460 57.898  1.00 32.06  ? 281  VAL B CG2 1 
ATOM   5955 N  N   . LYS B 1 282 ? -21.956 -11.391 60.884  1.00 31.62  ? 282  LYS B N   1 
ATOM   5956 C  CA  . LYS B 1 282 ? -22.783 -11.975 61.935  1.00 32.96  ? 282  LYS B CA  1 
ATOM   5957 C  C   . LYS B 1 282 ? -23.252 -10.955 62.966  1.00 32.23  ? 282  LYS B C   1 
ATOM   5958 O  O   . LYS B 1 282 ? -24.058 -11.306 63.839  1.00 34.30  ? 282  LYS B O   1 
ATOM   5959 C  CB  . LYS B 1 282 ? -22.017 -13.087 62.675  1.00 31.83  ? 282  LYS B CB  1 
ATOM   5960 C  CG  . LYS B 1 282 ? -21.648 -14.314 61.819  1.00 32.21  ? 282  LYS B CG  1 
ATOM   5961 C  CD  . LYS B 1 282 ? -22.873 -14.943 61.131  1.00 36.46  ? 282  LYS B CD  1 
ATOM   5962 C  CE  . LYS B 1 282 ? -22.534 -16.353 60.604  1.00 35.34  ? 282  LYS B CE  1 
ATOM   5963 N  NZ  . LYS B 1 282 ? -23.698 -17.003 59.897  1.00 31.74  ? 282  LYS B NZ  1 
ATOM   5964 N  N   . ASN B 1 283 ? -22.761 -9.717  62.907  1.00 33.24  ? 283  ASN B N   1 
ATOM   5965 C  CA  . ASN B 1 283 ? -23.070 -8.697  63.914  1.00 30.12  ? 283  ASN B CA  1 
ATOM   5966 C  C   . ASN B 1 283 ? -23.340 -7.390  63.189  1.00 30.85  ? 283  ASN B C   1 
ATOM   5967 O  O   . ASN B 1 283 ? -22.497 -6.487  63.151  1.00 31.40  ? 283  ASN B O   1 
ATOM   5968 C  CB  . ASN B 1 283 ? -21.928 -8.570  64.938  1.00 28.96  ? 283  ASN B CB  1 
ATOM   5969 C  CG  . ASN B 1 283 ? -21.788 -9.809  65.780  1.00 35.36  ? 283  ASN B CG  1 
ATOM   5970 O  OD1 . ASN B 1 283 ? -22.468 -9.952  66.785  1.00 33.66  ? 283  ASN B OD1 1 
ATOM   5971 N  ND2 . ASN B 1 283 ? -20.902 -10.733 65.365  1.00 31.54  ? 283  ASN B ND2 1 
ATOM   5972 N  N   . PRO B 1 284 ? -24.510 -7.271  62.563  1.00 33.44  ? 284  PRO B N   1 
ATOM   5973 C  CA  . PRO B 1 284 ? -24.756 -6.122  61.679  1.00 33.09  ? 284  PRO B CA  1 
ATOM   5974 C  C   . PRO B 1 284 ? -24.682 -4.764  62.361  1.00 32.60  ? 284  PRO B C   1 
ATOM   5975 O  O   . PRO B 1 284 ? -24.362 -3.785  61.676  1.00 31.51  ? 284  PRO B O   1 
ATOM   5976 C  CB  . PRO B 1 284 ? -26.160 -6.403  61.112  1.00 36.08  ? 284  PRO B CB  1 
ATOM   5977 C  CG  . PRO B 1 284 ? -26.696 -7.578  61.866  1.00 37.19  ? 284  PRO B CG  1 
ATOM   5978 C  CD  . PRO B 1 284 ? -25.520 -8.328  62.398  1.00 33.46  ? 284  PRO B CD  1 
ATOM   5979 N  N   . HIS B 1 285 ? -24.974 -4.661  63.666  1.00 29.42  ? 285  HIS B N   1 
ATOM   5980 C  CA  . HIS B 1 285 ? -24.766 -3.390  64.360  1.00 31.56  ? 285  HIS B CA  1 
ATOM   5981 C  C   . HIS B 1 285 ? -23.304 -2.980  64.299  1.00 32.19  ? 285  HIS B C   1 
ATOM   5982 O  O   . HIS B 1 285 ? -22.984 -1.803  64.129  1.00 32.72  ? 285  HIS B O   1 
ATOM   5983 C  CB  . HIS B 1 285 ? -25.188 -3.478  65.835  1.00 35.18  ? 285  HIS B CB  1 
ATOM   5984 C  CG  . HIS B 1 285 ? -26.665 -3.558  66.054  1.00 37.10  ? 285  HIS B CG  1 
ATOM   5985 N  ND1 . HIS B 1 285 ? -27.536 -2.590  65.604  1.00 38.23  ? 285  HIS B ND1 1 
ATOM   5986 C  CD2 . HIS B 1 285 ? -27.422 -4.480  66.693  1.00 35.90  ? 285  HIS B CD2 1 
ATOM   5987 C  CE1 . HIS B 1 285 ? -28.769 -2.920  65.948  1.00 37.37  ? 285  HIS B CE1 1 
ATOM   5988 N  NE2 . HIS B 1 285 ? -28.728 -4.062  66.608  1.00 37.37  ? 285  HIS B NE2 1 
ATOM   5989 N  N   . VAL B 1 286 ? -22.404 -3.935  64.509  1.00 30.00  ? 286  VAL B N   1 
ATOM   5990 C  CA  . VAL B 1 286 ? -20.981 -3.615  64.448  1.00 32.54  ? 286  VAL B CA  1 
ATOM   5991 C  C   . VAL B 1 286 ? -20.569 -3.287  63.020  1.00 31.70  ? 286  VAL B C   1 
ATOM   5992 O  O   . VAL B 1 286 ? -19.801 -2.347  62.768  1.00 32.57  ? 286  VAL B O   1 
ATOM   5993 C  CB  . VAL B 1 286 ? -20.162 -4.784  65.008  1.00 33.00  ? 286  VAL B CB  1 
ATOM   5994 C  CG1 . VAL B 1 286 ? -18.670 -4.490  64.843  1.00 29.94  ? 286  VAL B CG1 1 
ATOM   5995 C  CG2 . VAL B 1 286 ? -20.530 -5.052  66.468  1.00 29.91  ? 286  VAL B CG2 1 
ATOM   5996 N  N   . LEU B 1 287 ? -21.060 -4.062  62.062  1.00 31.11  ? 287  LEU B N   1 
ATOM   5997 C  CA  . LEU B 1 287 ? -20.740 -3.784  60.671  1.00 30.58  ? 287  LEU B CA  1 
ATOM   5998 C  C   . LEU B 1 287 ? -21.136 -2.361  60.306  1.00 32.97  ? 287  LEU B C   1 
ATOM   5999 O  O   . LEU B 1 287 ? -20.374 -1.643  59.660  1.00 33.01  ? 287  LEU B O   1 
ATOM   6000 C  CB  . LEU B 1 287 ? -21.438 -4.809  59.774  1.00 32.39  ? 287  LEU B CB  1 
ATOM   6001 C  CG  . LEU B 1 287 ? -21.363 -4.612  58.269  1.00 37.21  ? 287  LEU B CG  1 
ATOM   6002 C  CD1 . LEU B 1 287 ? -19.963 -4.283  57.878  1.00 38.11  ? 287  LEU B CD1 1 
ATOM   6003 C  CD2 . LEU B 1 287 ? -21.815 -5.889  57.557  1.00 42.66  ? 287  LEU B CD2 1 
ATOM   6004 N  N   . GLN B 1 288 ? -22.315 -1.919  60.746  1.00 33.81  ? 288  GLN B N   1 
ATOM   6005 C  CA  . GLN B 1 288 ? -22.752 -0.565  60.415  1.00 31.69  ? 288  GLN B CA  1 
ATOM   6006 C  C   . GLN B 1 288 ? -21.810 0.487   60.988  1.00 33.31  ? 288  GLN B C   1 
ATOM   6007 O  O   . GLN B 1 288 ? -21.469 1.459   60.302  1.00 31.28  ? 288  GLN B O   1 
ATOM   6008 C  CB  . GLN B 1 288 ? -24.181 -0.328  60.913  1.00 37.02  ? 288  GLN B CB  1 
ATOM   6009 C  CG  . GLN B 1 288 ? -24.731 1.061   60.618  1.00 43.95  ? 288  GLN B CG  1 
ATOM   6010 C  CD  . GLN B 1 288 ? -26.158 1.243   61.127  1.00 54.61  ? 288  GLN B CD  1 
ATOM   6011 O  OE1 . GLN B 1 288 ? -27.115 0.730   60.535  1.00 63.16  ? 288  GLN B OE1 1 
ATOM   6012 N  NE2 . GLN B 1 288 ? -26.304 1.969   62.236  1.00 58.80  ? 288  GLN B NE2 1 
ATOM   6013 N  N   . LYS B 1 289 ? -21.389 0.323   62.249  1.00 32.86  ? 289  LYS B N   1 
ATOM   6014 C  CA  . LYS B 1 289 ? -20.477 1.302   62.844  1.00 32.82  ? 289  LYS B CA  1 
ATOM   6015 C  C   . LYS B 1 289 ? -19.139 1.313   62.118  1.00 32.65  ? 289  LYS B C   1 
ATOM   6016 O  O   . LYS B 1 289 ? -18.547 2.376   61.897  1.00 32.05  ? 289  LYS B O   1 
ATOM   6017 C  CB  . LYS B 1 289 ? -20.260 1.008   64.336  1.00 33.53  ? 289  LYS B CB  1 
ATOM   6018 C  CG  . LYS B 1 289 ? -21.424 1.438   65.237  1.00 41.96  ? 289  LYS B CG  1 
ATOM   6019 C  CD  . LYS B 1 289 ? -21.215 1.040   66.710  1.00 37.18  ? 289  LYS B CD  1 
ATOM   6020 C  CE  . LYS B 1 289 ? -20.156 1.897   67.426  1.00 36.04  ? 289  LYS B CE  1 
ATOM   6021 N  NZ  . LYS B 1 289 ? -20.281 1.826   68.950  1.00 33.71  ? 289  LYS B NZ  1 
ATOM   6022 N  N   . ALA B 1 290 ? -18.638 0.134   61.743  1.00 32.15  ? 290  ALA B N   1 
ATOM   6023 C  CA  . ALA B 1 290 ? -17.356 0.097   61.048  1.00 33.06  ? 290  ALA B CA  1 
ATOM   6024 C  C   . ALA B 1 290 ? -17.472 0.695   59.651  1.00 30.71  ? 290  ALA B C   1 
ATOM   6025 O  O   . ALA B 1 290 ? -16.587 1.432   59.199  1.00 32.28  ? 290  ALA B O   1 
ATOM   6026 C  CB  . ALA B 1 290 ? -16.840 -1.342  60.981  1.00 30.14  ? 290  ALA B CB  1 
ATOM   6027 N  N   . ALA B 1 291 ? -18.565 0.409   58.959  1.00 29.60  ? 291  ALA B N   1 
ATOM   6028 C  CA  . ALA B 1 291 ? -18.721 0.932   57.607  1.00 32.25  ? 291  ALA B CA  1 
ATOM   6029 C  C   . ALA B 1 291 ? -18.929 2.447   57.619  1.00 30.18  ? 291  ALA B C   1 
ATOM   6030 O  O   . ALA B 1 291 ? -18.462 3.151   56.723  1.00 32.18  ? 291  ALA B O   1 
ATOM   6031 C  CB  . ALA B 1 291 ? -19.878 0.206   56.915  1.00 31.74  ? 291  ALA B CB  1 
ATOM   6032 N  N   . GLU B 1 292 ? -19.630 2.971   58.621  1.00 30.81  ? 292  GLU B N   1 
ATOM   6033 C  CA  . GLU B 1 292 ? -19.750 4.421   58.754  1.00 35.33  ? 292  GLU B CA  1 
ATOM   6034 C  C   . GLU B 1 292 ? -18.382 5.069   58.832  1.00 34.05  ? 292  GLU B C   1 
ATOM   6035 O  O   . GLU B 1 292 ? -18.113 6.073   58.161  1.00 33.13  ? 292  GLU B O   1 
ATOM   6036 C  CB  . GLU B 1 292 ? -20.559 4.776   60.006  1.00 34.90  ? 292  GLU B CB  1 
ATOM   6037 C  CG  . GLU B 1 292 ? -20.939 6.267   60.130  1.00 34.83  ? 292  GLU B CG  1 
ATOM   6038 C  CD  . GLU B 1 292 ? -19.795 7.181   60.594  1.00 35.78  ? 292  GLU B CD  1 
ATOM   6039 O  OE1 . GLU B 1 292 ? -18.885 6.725   61.329  1.00 35.39  ? 292  GLU B OE1 1 
ATOM   6040 O  OE2 . GLU B 1 292 ? -19.825 8.382   60.235  1.00 35.86  ? 292  GLU B OE2 1 
ATOM   6041 N  N   . GLU B 1 293 ? -17.519 4.526   59.690  1.00 32.14  ? 293  GLU B N   1 
ATOM   6042 C  CA  . GLU B 1 293 ? -16.186 5.091   59.839  1.00 32.05  ? 293  GLU B CA  1 
ATOM   6043 C  C   . GLU B 1 293 ? -15.425 5.040   58.528  1.00 32.37  ? 293  GLU B C   1 
ATOM   6044 O  O   . GLU B 1 293 ? -14.825 6.035   58.106  1.00 31.35  ? 293  GLU B O   1 
ATOM   6045 C  CB  . GLU B 1 293 ? -15.419 4.348   60.922  1.00 31.78  ? 293  GLU B CB  1 
ATOM   6046 C  CG  . GLU B 1 293 ? -14.067 4.977   61.212  1.00 30.94  ? 293  GLU B CG  1 
ATOM   6047 C  CD  . GLU B 1 293 ? -13.354 4.220   62.302  1.00 32.23  ? 293  GLU B CD  1 
ATOM   6048 O  OE1 . GLU B 1 293 ? -12.818 3.121   62.000  1.00 32.77  ? 293  GLU B OE1 1 
ATOM   6049 O  OE2 . GLU B 1 293 ? -13.353 4.706   63.460  1.00 32.27  ? 293  GLU B OE2 1 
ATOM   6050 N  N   . ALA B 1 294 ? -15.416 3.871   57.880  1.00 27.77  ? 294  ALA B N   1 
ATOM   6051 C  CA  . ALA B 1 294 ? -14.665 3.734   56.636  1.00 32.65  ? 294  ALA B CA  1 
ATOM   6052 C  C   . ALA B 1 294 ? -15.154 4.725   55.587  1.00 34.43  ? 294  ALA B C   1 
ATOM   6053 O  O   . ALA B 1 294 ? -14.345 5.361   54.904  1.00 33.99  ? 294  ALA B O   1 
ATOM   6054 C  CB  . ALA B 1 294 ? -14.760 2.297   56.114  1.00 33.70  ? 294  ALA B CB  1 
ATOM   6055 N  N   . ALA B 1 295 ? -16.480 4.884   55.455  1.00 33.91  ? 295  ALA B N   1 
ATOM   6056 C  CA  . ALA B 1 295 ? -17.012 5.803   54.450  1.00 36.68  ? 295  ALA B CA  1 
ATOM   6057 C  C   . ALA B 1 295 ? -16.638 7.247   54.771  1.00 35.21  ? 295  ALA B C   1 
ATOM   6058 O  O   . ALA B 1 295 ? -16.346 8.041   53.866  1.00 37.49  ? 295  ALA B O   1 
ATOM   6059 C  CB  . ALA B 1 295 ? -18.531 5.647   54.353  1.00 38.03  ? 295  ALA B CB  1 
ATOM   6060 N  N   . ARG B 1 296 ? -16.610 7.595   56.058  1.00 34.94  ? 296  ARG B N   1 
ATOM   6061 C  CA  . ARG B 1 296 ? -16.363 8.971   56.474  1.00 35.05  ? 296  ARG B CA  1 
ATOM   6062 C  C   . ARG B 1 296 ? -14.884 9.338   56.380  1.00 37.92  ? 296  ARG B C   1 
ATOM   6063 O  O   . ARG B 1 296 ? -14.541 10.475  56.033  1.00 35.51  ? 296  ARG B O   1 
ATOM   6064 C  CB  . ARG B 1 296 ? -16.870 9.164   57.905  1.00 36.46  ? 296  ARG B CB  1 
ATOM   6065 C  CG  . ARG B 1 296 ? -16.372 10.440  58.576  1.00 36.20  ? 296  ARG B CG  1 
ATOM   6066 C  CD  . ARG B 1 296 ? -17.208 10.756  59.810  1.00 38.87  ? 296  ARG B CD  1 
ATOM   6067 N  NE  . ARG B 1 296 ? -17.313 9.601   60.697  1.00 37.61  ? 296  ARG B NE  1 
ATOM   6068 C  CZ  . ARG B 1 296 ? -16.441 9.325   61.658  1.00 37.67  ? 296  ARG B CZ  1 
ATOM   6069 N  NH1 . ARG B 1 296 ? -15.391 10.103  61.879  1.00 38.89  ? 296  ARG B NH1 1 
ATOM   6070 N  NH2 . ARG B 1 296 ? -16.611 8.232   62.400  1.00 36.83  ? 296  ARG B NH2 1 
ATOM   6071 N  N   . VAL B 1 297 ? -13.999 8.398   56.699  1.00 34.46  ? 297  VAL B N   1 
ATOM   6072 C  CA  . VAL B 1 297 ? -12.570 8.687   56.791  1.00 34.65  ? 297  VAL B CA  1 
ATOM   6073 C  C   . VAL B 1 297 ? -11.876 8.535   55.441  1.00 35.84  ? 297  VAL B C   1 
ATOM   6074 O  O   . VAL B 1 297 ? -11.048 9.374   55.060  1.00 35.12  ? 297  VAL B O   1 
ATOM   6075 C  CB  . VAL B 1 297 ? -11.949 7.770   57.867  1.00 33.10  ? 297  VAL B CB  1 
ATOM   6076 C  CG1 . VAL B 1 297 ? -10.397 7.704   57.751  1.00 32.75  ? 297  VAL B CG1 1 
ATOM   6077 C  CG2 . VAL B 1 297 ? -12.368 8.243   59.263  1.00 33.54  ? 297  VAL B CG2 1 
ATOM   6078 N  N   . LEU B 1 298 ? -12.195 7.474   54.693  1.00 30.95  ? 298  LEU B N   1 
ATOM   6079 C  CA  . LEU B 1 298 ? -11.512 7.196   53.427  1.00 33.96  ? 298  LEU B CA  1 
ATOM   6080 C  C   . LEU B 1 298 ? -12.172 7.996   52.302  1.00 35.24  ? 298  LEU B C   1 
ATOM   6081 O  O   . LEU B 1 298 ? -12.848 7.466   51.418  1.00 35.35  ? 298  LEU B O   1 
ATOM   6082 C  CB  . LEU B 1 298 ? -11.526 5.704   53.139  1.00 34.94  ? 298  LEU B CB  1 
ATOM   6083 C  CG  . LEU B 1 298 ? -10.891 4.847   54.227  1.00 31.96  ? 298  LEU B CG  1 
ATOM   6084 C  CD1 . LEU B 1 298 ? -11.014 3.358   53.880  1.00 35.75  ? 298  LEU B CD1 1 
ATOM   6085 C  CD2 . LEU B 1 298 ? -9.440  5.230   54.419  1.00 33.68  ? 298  LEU B CD2 1 
ATOM   6086 N  N   . VAL B 1 299 ? -11.954 9.315   52.346  1.00 34.41  ? 299  VAL B N   1 
ATOM   6087 C  CA  . VAL B 1 299 ? -12.626 10.207  51.403  1.00 38.57  ? 299  VAL B CA  1 
ATOM   6088 C  C   . VAL B 1 299 ? -11.967 10.251  50.038  1.00 39.34  ? 299  VAL B C   1 
ATOM   6089 O  O   . VAL B 1 299 ? -12.546 10.821  49.100  1.00 40.47  ? 299  VAL B O   1 
ATOM   6090 C  CB  . VAL B 1 299 ? -12.687 11.640  51.963  1.00 38.91  ? 299  VAL B CB  1 
ATOM   6091 C  CG1 . VAL B 1 299 ? -13.602 11.663  53.168  1.00 40.52  ? 299  VAL B CG1 1 
ATOM   6092 C  CG2 . VAL B 1 299 ? -11.303 12.106  52.335  1.00 37.72  ? 299  VAL B CG2 1 
ATOM   6093 N  N   . ASP B 1 300 ? -10.769 9.682   49.899  1.00 35.83  ? 300  ASP B N   1 
ATOM   6094 C  CA  . ASP B 1 300 ? -10.073 9.737   48.626  1.00 39.74  ? 300  ASP B CA  1 
ATOM   6095 C  C   . ASP B 1 300 ? -10.050 8.368   47.955  1.00 37.00  ? 300  ASP B C   1 
ATOM   6096 O  O   . ASP B 1 300 ? -10.056 7.338   48.635  1.00 36.90  ? 300  ASP B O   1 
ATOM   6097 C  CB  . ASP B 1 300 ? -8.631  10.220  48.827  1.00 36.69  ? 300  ASP B CB  1 
ATOM   6098 C  CG  . ASP B 1 300 ? -8.565  11.614  49.421  1.00 39.78  ? 300  ASP B CG  1 
ATOM   6099 O  OD1 . ASP B 1 300 ? -9.293  12.493  48.931  1.00 42.02  ? 300  ASP B OD1 1 
ATOM   6100 O  OD2 . ASP B 1 300 ? -7.794  11.828  50.379  1.00 40.23  ? 300  ASP B OD2 1 
ATOM   6101 N  N   . PRO B 1 301 ? -9.983  8.319   46.623  1.00 37.75  ? 301  PRO B N   1 
ATOM   6102 C  CA  . PRO B 1 301 ? -9.917  7.009   45.951  1.00 37.75  ? 301  PRO B CA  1 
ATOM   6103 C  C   . PRO B 1 301 ? -8.722  6.172   46.374  1.00 39.32  ? 301  PRO B C   1 
ATOM   6104 O  O   . PRO B 1 301 ? -8.817  4.939   46.411  1.00 41.15  ? 301  PRO B O   1 
ATOM   6105 C  CB  . PRO B 1 301 ? -9.842  7.378   44.458  1.00 43.21  ? 301  PRO B CB  1 
ATOM   6106 C  CG  . PRO B 1 301 ? -10.389 8.771   44.373  1.00 48.61  ? 301  PRO B CG  1 
ATOM   6107 C  CD  . PRO B 1 301 ? -10.050 9.441   45.675  1.00 44.05  ? 301  PRO B CD  1 
ATOM   6108 N  N   . VAL B 1 302 ? -7.596  6.804   46.676  1.00 37.61  ? 302  VAL B N   1 
ATOM   6109 C  CA  . VAL B 1 302 ? -6.400  6.129   47.164  1.00 41.04  ? 302  VAL B CA  1 
ATOM   6110 C  C   . VAL B 1 302 ? -6.262  6.473   48.647  1.00 39.63  ? 302  VAL B C   1 
ATOM   6111 O  O   . VAL B 1 302 ? -6.007  7.637   48.984  1.00 41.94  ? 302  VAL B O   1 
ATOM   6112 C  CB  . VAL B 1 302 ? -5.154  6.553   46.374  1.00 41.62  ? 302  VAL B CB  1 
ATOM   6113 C  CG1 . VAL B 1 302 ? -3.924  5.793   46.844  1.00 41.38  ? 302  VAL B CG1 1 
ATOM   6114 C  CG2 . VAL B 1 302 ? -5.378  6.390   44.855  1.00 45.39  ? 302  VAL B CG2 1 
ATOM   6115 N  N   . PRO B 1 303 ? -6.461  5.524   49.562  1.00 37.87  ? 303  PRO B N   1 
ATOM   6116 C  CA  . PRO B 1 303 ? -6.290  5.833   50.991  1.00 36.82  ? 303  PRO B CA  1 
ATOM   6117 C  C   . PRO B 1 303 ? -4.855  6.217   51.318  1.00 35.81  ? 303  PRO B C   1 
ATOM   6118 O  O   . PRO B 1 303 ? -3.902  5.628   50.805  1.00 35.07  ? 303  PRO B O   1 
ATOM   6119 C  CB  . PRO B 1 303 ? -6.689  4.527   51.687  1.00 41.14  ? 303  PRO B CB  1 
ATOM   6120 C  CG  . PRO B 1 303 ? -7.590  3.833   50.682  1.00 38.80  ? 303  PRO B CG  1 
ATOM   6121 C  CD  . PRO B 1 303 ? -7.024  4.182   49.342  1.00 38.69  ? 303  PRO B CD  1 
ATOM   6122 N  N   . SER B 1 304 ? -4.710  7.204   52.195  1.00 34.98  ? 304  SER B N   1 
ATOM   6123 C  CA  . SER B 1 304 ? -3.393  7.611   52.669  1.00 36.79  ? 304  SER B CA  1 
ATOM   6124 C  C   . SER B 1 304 ? -3.037  6.919   53.986  1.00 32.86  ? 304  SER B C   1 
ATOM   6125 O  O   . SER B 1 304 ? -3.894  6.408   54.705  1.00 33.32  ? 304  SER B O   1 
ATOM   6126 C  CB  . SER B 1 304 ? -3.334  9.129   52.860  1.00 36.92  ? 304  SER B CB  1 
ATOM   6127 O  OG  . SER B 1 304 ? -4.146  9.524   53.960  1.00 34.41  ? 304  SER B OG  1 
ATOM   6128 N  N   . TYR B 1 305 ? -1.737  6.926   54.300  1.00 33.40  ? 305  TYR B N   1 
ATOM   6129 C  CA  . TYR B 1 305 ? -1.273  6.404   55.580  1.00 35.02  ? 305  TYR B CA  1 
ATOM   6130 C  C   . TYR B 1 305 ? -2.014  7.055   56.743  1.00 36.34  ? 305  TYR B C   1 
ATOM   6131 O  O   . TYR B 1 305 ? -2.519  6.365   57.638  1.00 36.35  ? 305  TYR B O   1 
ATOM   6132 C  CB  . TYR B 1 305 ? 0.238   6.633   55.695  1.00 35.32  ? 305  TYR B CB  1 
ATOM   6133 C  CG  . TYR B 1 305 ? 0.841   6.184   56.992  1.00 36.90  ? 305  TYR B CG  1 
ATOM   6134 C  CD1 . TYR B 1 305 ? 1.294   4.881   57.161  1.00 37.39  ? 305  TYR B CD1 1 
ATOM   6135 C  CD2 . TYR B 1 305 ? 0.993   7.080   58.047  1.00 41.09  ? 305  TYR B CD2 1 
ATOM   6136 C  CE1 . TYR B 1 305 ? 1.844   4.469   58.363  1.00 41.91  ? 305  TYR B CE1 1 
ATOM   6137 C  CE2 . TYR B 1 305 ? 1.542   6.681   59.240  1.00 46.33  ? 305  TYR B CE2 1 
ATOM   6138 C  CZ  . TYR B 1 305 ? 1.969   5.375   59.395  1.00 45.70  ? 305  TYR B CZ  1 
ATOM   6139 O  OH  . TYR B 1 305 ? 2.520   4.995   60.591  1.00 55.17  ? 305  TYR B OH  1 
ATOM   6140 N  N   . LYS B 1 306 ? -2.093  8.392   56.736  1.00 32.21  ? 306  LYS B N   1 
ATOM   6141 C  CA  . LYS B 1 306 ? -2.760  9.119   57.813  1.00 38.46  ? 306  LYS B CA  1 
ATOM   6142 C  C   . LYS B 1 306 ? -4.221  8.714   57.942  1.00 32.57  ? 306  LYS B C   1 
ATOM   6143 O  O   . LYS B 1 306 ? -4.739  8.590   59.058  1.00 34.81  ? 306  LYS B O   1 
ATOM   6144 C  CB  . LYS B 1 306 ? -2.657  10.623  57.566  1.00 43.55  ? 306  LYS B CB  1 
ATOM   6145 C  CG  . LYS B 1 306 ? -1.529  11.305  58.333  1.00 48.50  ? 306  LYS B CG  1 
ATOM   6146 C  CD  . LYS B 1 306 ? -1.596  12.817  58.172  1.00 54.32  ? 306  LYS B CD  1 
ATOM   6147 C  CE  . LYS B 1 306 ? -0.345  13.372  57.505  1.00 60.74  ? 306  LYS B CE  1 
ATOM   6148 N  NZ  . LYS B 1 306 ? 0.697   13.705  58.511  1.00 62.76  ? 306  LYS B NZ  1 
ATOM   6149 N  N   . GLN B 1 307 ? -4.904  8.523   56.809  1.00 34.16  ? 307  GLN B N   1 
ATOM   6150 C  CA  . GLN B 1 307 ? -6.308  8.120   56.851  1.00 33.99  ? 307  GLN B CA  1 
ATOM   6151 C  C   . GLN B 1 307 ? -6.474  6.743   57.485  1.00 33.74  ? 307  GLN B C   1 
ATOM   6152 O  O   . GLN B 1 307 ? -7.375  6.531   58.313  1.00 33.39  ? 307  GLN B O   1 
ATOM   6153 C  CB  . GLN B 1 307 ? -6.896  8.153   55.438  1.00 36.03  ? 307  GLN B CB  1 
ATOM   6154 C  CG  . GLN B 1 307 ? -7.178  9.572   54.909  1.00 36.65  ? 307  GLN B CG  1 
ATOM   6155 C  CD  . GLN B 1 307 ? -7.466  9.592   53.410  1.00 37.53  ? 307  GLN B CD  1 
ATOM   6156 O  OE1 . GLN B 1 307 ? -7.243  8.606   52.710  1.00 36.91  ? 307  GLN B OE1 1 
ATOM   6157 N  NE2 . GLN B 1 307 ? -7.968  10.715  52.921  1.00 38.40  ? 307  GLN B NE2 1 
ATOM   6158 N  N   . VAL B 1 308 ? -5.603  5.791   57.138  1.00 31.50  ? 308  VAL B N   1 
ATOM   6159 C  CA  . VAL B 1 308 ? -5.702  4.474   57.769  1.00 33.25  ? 308  VAL B CA  1 
ATOM   6160 C  C   . VAL B 1 308 ? -5.532  4.596   59.278  1.00 33.42  ? 308  VAL B C   1 
ATOM   6161 O  O   . VAL B 1 308 ? -6.214  3.915   60.058  1.00 33.39  ? 308  VAL B O   1 
ATOM   6162 C  CB  . VAL B 1 308 ? -4.683  3.498   57.151  1.00 32.76  ? 308  VAL B CB  1 
ATOM   6163 C  CG1 . VAL B 1 308 ? -4.679  2.160   57.927  1.00 34.53  ? 308  VAL B CG1 1 
ATOM   6164 C  CG2 . VAL B 1 308 ? -5.005  3.262   55.668  1.00 31.59  ? 308  VAL B CG2 1 
ATOM   6165 N  N   . LYS B 1 309 ? -4.640  5.482   59.723  1.00 31.42  ? 309  LYS B N   1 
ATOM   6166 C  CA  . LYS B 1 309 ? -4.461  5.635   61.163  1.00 34.50  ? 309  LYS B CA  1 
ATOM   6167 C  C   . LYS B 1 309 ? -5.722  6.160   61.844  1.00 34.73  ? 309  LYS B C   1 
ATOM   6168 O  O   . LYS B 1 309 ? -5.873  5.994   63.060  1.00 35.82  ? 309  LYS B O   1 
ATOM   6169 C  CB  . LYS B 1 309 ? -3.290  6.572   61.460  1.00 35.97  ? 309  LYS B CB  1 
ATOM   6170 C  CG  . LYS B 1 309 ? -1.950  6.053   60.949  1.00 40.10  ? 309  LYS B CG  1 
ATOM   6171 C  CD  . LYS B 1 309 ? -1.713  4.636   61.433  1.00 44.49  ? 309  LYS B CD  1 
ATOM   6172 C  CE  . LYS B 1 309 ? -0.256  4.261   61.407  1.00 52.50  ? 309  LYS B CE  1 
ATOM   6173 N  NZ  . LYS B 1 309 ? -0.057  2.898   61.986  1.00 59.44  ? 309  LYS B NZ  1 
ATOM   6174 N  N   . GLN B 1 310 ? -6.611  6.806   61.100  1.00 32.62  ? 310  GLN B N   1 
ATOM   6175 C  CA  . GLN B 1 310 ? -7.840  7.323   61.685  1.00 32.78  ? 310  GLN B CA  1 
ATOM   6176 C  C   . GLN B 1 310 ? -8.946  6.282   61.778  1.00 34.35  ? 310  GLN B C   1 
ATOM   6177 O  O   . GLN B 1 310 ? -10.022 6.594   62.306  1.00 37.09  ? 310  GLN B O   1 
ATOM   6178 C  CB  . GLN B 1 310 ? -8.365  8.503   60.868  1.00 35.19  ? 310  GLN B CB  1 
ATOM   6179 C  CG  . GLN B 1 310 ? -7.538  9.775   60.912  1.00 37.43  ? 310  GLN B CG  1 
ATOM   6180 C  CD  . GLN B 1 310 ? -8.094  10.796  59.937  1.00 38.43  ? 310  GLN B CD  1 
ATOM   6181 O  OE1 . GLN B 1 310 ? -7.970  10.639  58.721  1.00 42.95  ? 310  GLN B OE1 1 
ATOM   6182 N  NE2 . GLN B 1 310 ? -8.741  11.827  60.463  1.00 42.16  ? 310  GLN B NE2 1 
ATOM   6183 N  N   . LEU B 1 311 ? -8.747  5.077   61.243  1.00 33.04  ? 311  LEU B N   1 
ATOM   6184 C  CA  . LEU B 1 311 ? -9.785  4.037   61.294  1.00 31.43  ? 311  LEU B CA  1 
ATOM   6185 C  C   . LEU B 1 311 ? -9.742  3.347   62.660  1.00 32.37  ? 311  LEU B C   1 
ATOM   6186 O  O   . LEU B 1 311 ? -9.411  2.167   62.800  1.00 33.21  ? 311  LEU B O   1 
ATOM   6187 C  CB  . LEU B 1 311 ? -9.605  3.044   60.155  1.00 31.38  ? 311  LEU B CB  1 
ATOM   6188 C  CG  . LEU B 1 311 ? -9.783  3.709   58.794  1.00 29.25  ? 311  LEU B CG  1 
ATOM   6189 C  CD1 . LEU B 1 311 ? -9.420  2.723   57.688  1.00 33.31  ? 311  LEU B CD1 1 
ATOM   6190 C  CD2 . LEU B 1 311 ? -11.231 4.247   58.640  1.00 30.47  ? 311  LEU B CD2 1 
ATOM   6191 N  N   . LYS B 1 312 ? -10.118 4.114   63.686  1.00 33.81  ? 312  LYS B N   1 
ATOM   6192 C  CA  . LYS B 1 312 ? -10.018 3.620   65.060  1.00 31.80  ? 312  LYS B CA  1 
ATOM   6193 C  C   . LYS B 1 312 ? -10.956 2.437   65.301  1.00 31.36  ? 312  LYS B C   1 
ATOM   6194 O  O   . LYS B 1 312 ? -10.554 1.423   65.883  1.00 33.42  ? 312  LYS B O   1 
ATOM   6195 C  CB  . LYS B 1 312 ? -10.319 4.759   66.046  1.00 33.73  ? 312  LYS B CB  1 
ATOM   6196 C  CG  . LYS B 1 312 ? -10.365 4.320   67.513  1.00 44.39  ? 312  LYS B CG  1 
ATOM   6197 C  CD  . LYS B 1 312 ? -10.911 5.436   68.422  1.00 48.66  ? 312  LYS B CD  1 
ATOM   6198 C  CE  . LYS B 1 312 ? -10.321 5.363   69.840  1.00 51.77  ? 312  LYS B CE  1 
ATOM   6199 N  NZ  . LYS B 1 312 ? -10.376 4.002   70.434  1.00 47.48  ? 312  LYS B NZ  1 
ATOM   6200 N  N   . TYR B 1 313 ? -12.229 2.562   64.893  1.00 31.25  ? 313  TYR B N   1 
ATOM   6201 C  CA  . TYR B 1 313 ? -13.187 1.485   65.150  1.00 30.59  ? 313  TYR B CA  1 
ATOM   6202 C  C   . TYR B 1 313 ? -12.888 0.261   64.291  1.00 30.45  ? 313  TYR B C   1 
ATOM   6203 O  O   . TYR B 1 313 ? -13.058 -0.876  64.747  1.00 31.34  ? 313  TYR B O   1 
ATOM   6204 C  CB  . TYR B 1 313 ? -14.629 1.976   64.936  1.00 30.39  ? 313  TYR B CB  1 
ATOM   6205 C  CG  . TYR B 1 313 ? -15.659 0.992   65.467  1.00 33.08  ? 313  TYR B CG  1 
ATOM   6206 C  CD1 . TYR B 1 313 ? -16.052 1.016   66.813  1.00 32.07  ? 313  TYR B CD1 1 
ATOM   6207 C  CD2 . TYR B 1 313 ? -16.224 0.019   64.633  1.00 30.67  ? 313  TYR B CD2 1 
ATOM   6208 C  CE1 . TYR B 1 313 ? -16.974 0.106   67.310  1.00 32.24  ? 313  TYR B CE1 1 
ATOM   6209 C  CE2 . TYR B 1 313 ? -17.166 -0.894  65.129  1.00 30.42  ? 313  TYR B CE2 1 
ATOM   6210 C  CZ  . TYR B 1 313 ? -17.539 -0.840  66.469  1.00 31.27  ? 313  TYR B CZ  1 
ATOM   6211 O  OH  . TYR B 1 313 ? -18.468 -1.742  66.972  1.00 31.40  ? 313  TYR B OH  1 
ATOM   6212 N  N   . VAL B 1 314 ? -12.440 0.462   63.043  1.00 29.38  ? 314  VAL B N   1 
ATOM   6213 C  CA  . VAL B 1 314 ? -11.944 -0.674  62.272  1.00 30.99  ? 314  VAL B CA  1 
ATOM   6214 C  C   . VAL B 1 314 ? -10.844 -1.383  63.052  1.00 32.12  ? 314  VAL B C   1 
ATOM   6215 O  O   . VAL B 1 314 ? -10.820 -2.617  63.135  1.00 30.46  ? 314  VAL B O   1 
ATOM   6216 C  CB  . VAL B 1 314 ? -11.467 -0.218  60.882  1.00 29.94  ? 314  VAL B CB  1 
ATOM   6217 C  CG1 . VAL B 1 314 ? -10.862 -1.391  60.101  1.00 29.08  ? 314  VAL B CG1 1 
ATOM   6218 C  CG2 . VAL B 1 314 ? -12.663 0.367   60.111  1.00 29.64  ? 314  VAL B CG2 1 
ATOM   6219 N  N   . GLY B 1 315 ? -9.924  -0.607  63.646  1.00 31.48  ? 315  GLY B N   1 
ATOM   6220 C  CA  . GLY B 1 315 ? -8.884  -1.189  64.493  1.00 34.05  ? 315  GLY B CA  1 
ATOM   6221 C  C   . GLY B 1 315 ? -9.442  -1.994  65.654  1.00 32.09  ? 315  GLY B C   1 
ATOM   6222 O  O   . GLY B 1 315 ? -8.927  -3.070  65.984  1.00 33.41  ? 315  GLY B O   1 
ATOM   6223 N  N   . MET B 1 316 ? -10.494 -1.487  66.300  1.00 30.29  ? 316  MET B N   1 
ATOM   6224 C  CA  . MET B 1 316 ? -11.073 -2.251  67.404  1.00 30.52  ? 316  MET B CA  1 
ATOM   6225 C  C   . MET B 1 316 ? -11.750 -3.528  66.932  1.00 26.86  ? 316  MET B C   1 
ATOM   6226 O  O   . MET B 1 316 ? -11.711 -4.547  67.637  1.00 30.57  ? 316  MET B O   1 
ATOM   6227 C  CB  . MET B 1 316 ? -12.023 -1.386  68.243  1.00 34.07  ? 316  MET B CB  1 
ATOM   6228 C  CG  . MET B 1 316 ? -11.482 0.001   68.642  1.00 33.28  ? 316  MET B CG  1 
ATOM   6229 S  SD  . MET B 1 316 ? -12.748 1.255   69.021  1.00 38.76  ? 316  MET B SD  1 
ATOM   6230 C  CE  . MET B 1 316 ? -13.789 0.397   70.178  1.00 42.19  ? 316  MET B CE  1 
ATOM   6231 N  N   . VAL B 1 317 ? -12.382 -3.503  65.753  1.00 28.67  ? 317  VAL B N   1 
ATOM   6232 C  CA  . VAL B 1 317 ? -12.926 -4.734  65.172  1.00 30.71  ? 317  VAL B CA  1 
ATOM   6233 C  C   . VAL B 1 317 ? -11.834 -5.786  65.045  1.00 31.93  ? 317  VAL B C   1 
ATOM   6234 O  O   . VAL B 1 317 ? -12.005 -6.951  65.432  1.00 31.00  ? 317  VAL B O   1 
ATOM   6235 C  CB  . VAL B 1 317 ? -13.566 -4.450  63.796  1.00 28.70  ? 317  VAL B CB  1 
ATOM   6236 C  CG1 . VAL B 1 317 ? -13.843 -5.782  63.043  1.00 26.63  ? 317  VAL B CG1 1 
ATOM   6237 C  CG2 . VAL B 1 317 ? -14.849 -3.632  63.939  1.00 29.84  ? 317  VAL B CG2 1 
ATOM   6238 N  N   . LEU B 1 318 ? -10.694 -5.388  64.480  1.00 29.53  ? 318  LEU B N   1 
ATOM   6239 C  CA  . LEU B 1 318 ? -9.599  -6.334  64.285  1.00 28.96  ? 318  LEU B CA  1 
ATOM   6240 C  C   . LEU B 1 318 ? -9.064  -6.868  65.617  1.00 31.29  ? 318  LEU B C   1 
ATOM   6241 O  O   . LEU B 1 318 ? -8.811  -8.070  65.759  1.00 29.72  ? 318  LEU B O   1 
ATOM   6242 C  CB  . LEU B 1 318 ? -8.493  -5.655  63.475  1.00 31.26  ? 318  LEU B CB  1 
ATOM   6243 C  CG  . LEU B 1 318 ? -8.880  -5.327  62.028  1.00 30.49  ? 318  LEU B CG  1 
ATOM   6244 C  CD1 . LEU B 1 318 ? -7.848  -4.377  61.399  1.00 31.68  ? 318  LEU B CD1 1 
ATOM   6245 C  CD2 . LEU B 1 318 ? -8.994  -6.614  61.225  1.00 28.85  ? 318  LEU B CD2 1 
ATOM   6246 N  N   . ASN B 1 319 ? -8.910  -6.001  66.617  1.00 28.34  ? 319  ASN B N   1 
ATOM   6247 C  CA  . ASN B 1 319 ? -8.482  -6.493  67.925  1.00 29.29  ? 319  ASN B CA  1 
ATOM   6248 C  C   . ASN B 1 319 ? -9.501  -7.446  68.538  1.00 30.47  ? 319  ASN B C   1 
ATOM   6249 O  O   . ASN B 1 319 ? -9.130  -8.445  69.171  1.00 31.77  ? 319  ASN B O   1 
ATOM   6250 C  CB  . ASN B 1 319 ? -8.220  -5.317  68.852  1.00 32.85  ? 319  ASN B CB  1 
ATOM   6251 C  CG  . ASN B 1 319 ? -6.835  -4.753  68.657  1.00 39.98  ? 319  ASN B CG  1 
ATOM   6252 O  OD1 . ASN B 1 319 ? -5.900  -5.491  68.321  1.00 37.73  ? 319  ASN B OD1 1 
ATOM   6253 N  ND2 . ASN B 1 319 ? -6.694  -3.442  68.829  1.00 40.64  ? 319  ASN B ND2 1 
ATOM   6254 N  N   . GLU B 1 320 ? -10.792 -7.131  68.411  1.00 29.89  ? 320  GLU B N   1 
ATOM   6255 C  CA  . GLU B 1 320 ? -11.799 -8.034  68.954  1.00 29.24  ? 320  GLU B CA  1 
ATOM   6256 C  C   . GLU B 1 320 ? -11.802 -9.370  68.205  1.00 29.89  ? 320  GLU B C   1 
ATOM   6257 O  O   . GLU B 1 320 ? -12.068 -10.419 68.805  1.00 30.63  ? 320  GLU B O   1 
ATOM   6258 C  CB  . GLU B 1 320 ? -13.180 -7.350  68.914  1.00 29.60  ? 320  GLU B CB  1 
ATOM   6259 C  CG  . GLU B 1 320 ? -14.349 -8.191  69.454  1.00 32.59  ? 320  GLU B CG  1 
ATOM   6260 C  CD  . GLU B 1 320 ? -14.333 -8.379  70.973  1.00 34.64  ? 320  GLU B CD  1 
ATOM   6261 O  OE1 . GLU B 1 320 ? -13.275 -8.196  71.606  1.00 29.28  ? 320  GLU B OE1 1 
ATOM   6262 O  OE2 . GLU B 1 320 ? -15.392 -8.731  71.547  1.00 31.15  ? 320  GLU B OE2 1 
ATOM   6263 N  N   . ALA B 1 321 ? -11.491 -9.354  66.907  1.00 32.38  ? 321  ALA B N   1 
ATOM   6264 C  CA  . ALA B 1 321 ? -11.328 -10.599 66.161  1.00 29.40  ? 321  ALA B CA  1 
ATOM   6265 C  C   . ALA B 1 321 ? -10.100 -11.369 66.646  1.00 29.50  ? 321  ALA B C   1 
ATOM   6266 O  O   . ALA B 1 321 ? -10.145 -12.596 66.801  1.00 28.92  ? 321  ALA B O   1 
ATOM   6267 C  CB  . ALA B 1 321 ? -11.251 -10.302 64.652  1.00 31.40  ? 321  ALA B CB  1 
ATOM   6268 N  N   . LEU B 1 322 ? -8.999  -10.661 66.907  1.00 29.79  ? 322  LEU B N   1 
ATOM   6269 C  CA  . LEU B 1 322 ? -7.830  -11.285 67.525  1.00 29.66  ? 322  LEU B CA  1 
ATOM   6270 C  C   . LEU B 1 322 ? -8.124  -11.784 68.938  1.00 30.45  ? 322  LEU B C   1 
ATOM   6271 O  O   . LEU B 1 322 ? -7.529  -12.772 69.387  1.00 32.12  ? 322  LEU B O   1 
ATOM   6272 C  CB  . LEU B 1 322 ? -6.683  -10.285 67.562  1.00 32.21  ? 322  LEU B CB  1 
ATOM   6273 C  CG  . LEU B 1 322 ? -6.005  -10.042 66.212  1.00 31.53  ? 322  LEU B CG  1 
ATOM   6274 C  CD1 . LEU B 1 322 ? -4.831  -9.101  66.412  1.00 33.91  ? 322  LEU B CD1 1 
ATOM   6275 C  CD2 . LEU B 1 322 ? -5.546  -11.375 65.602  1.00 31.12  ? 322  LEU B CD2 1 
ATOM   6276 N  N   . ARG B 1 323 ? -9.010  -11.110 69.666  1.00 28.59  ? 323  ARG B N   1 
ATOM   6277 C  CA  . ARG B 1 323 ? -9.367  -11.620 70.986  1.00 28.85  ? 323  ARG B CA  1 
ATOM   6278 C  C   . ARG B 1 323 ? -9.975  -13.007 70.874  1.00 31.41  ? 323  ARG B C   1 
ATOM   6279 O  O   . ARG B 1 323 ? -9.521  -13.955 71.521  1.00 32.45  ? 323  ARG B O   1 
ATOM   6280 C  CB  . ARG B 1 323 ? -10.332 -10.664 71.697  1.00 31.27  ? 323  ARG B CB  1 
ATOM   6281 C  CG  . ARG B 1 323 ? -10.520 -11.056 73.189  1.00 30.90  ? 323  ARG B CG  1 
ATOM   6282 C  CD  . ARG B 1 323 ? -11.482 -10.125 73.923  1.00 29.19  ? 323  ARG B CD  1 
ATOM   6283 N  NE  . ARG B 1 323 ? -12.833 -10.217 73.373  1.00 32.53  ? 323  ARG B NE  1 
ATOM   6284 C  CZ  . ARG B 1 323 ? -13.693 -11.194 73.633  1.00 33.65  ? 323  ARG B CZ  1 
ATOM   6285 N  NH1 . ARG B 1 323 ? -13.397 -12.184 74.468  1.00 33.56  ? 323  ARG B NH1 1 
ATOM   6286 N  NH2 . ARG B 1 323 ? -14.887 -11.178 73.044  1.00 31.40  ? 323  ARG B NH2 1 
ATOM   6287 N  N   . LEU B 1 324 ? -11.022 -13.148 70.056  1.00 31.91  ? 324  LEU B N   1 
ATOM   6288 C  CA  . LEU B 1 324 ? -11.761 -14.409 70.047  1.00 29.57  ? 324  LEU B CA  1 
ATOM   6289 C  C   . LEU B 1 324 ? -10.998 -15.515 69.331  1.00 33.15  ? 324  LEU B C   1 
ATOM   6290 O  O   . LEU B 1 324 ? -10.968 -16.660 69.798  1.00 31.09  ? 324  LEU B O   1 
ATOM   6291 C  CB  . LEU B 1 324 ? -13.131 -14.193 69.411  1.00 31.39  ? 324  LEU B CB  1 
ATOM   6292 C  CG  . LEU B 1 324 ? -14.117 -13.567 70.401  1.00 32.36  ? 324  LEU B CG  1 
ATOM   6293 C  CD1 . LEU B 1 324 ? -15.333 -13.034 69.672  1.00 35.84  ? 324  LEU B CD1 1 
ATOM   6294 C  CD2 . LEU B 1 324 ? -14.525 -14.563 71.531  1.00 34.17  ? 324  LEU B CD2 1 
ATOM   6295 N  N   . TRP B 1 325 ? -10.329 -15.196 68.227  1.00 30.44  ? 325  TRP B N   1 
ATOM   6296 C  CA  . TRP B 1 325 ? -9.643  -16.202 67.414  1.00 28.77  ? 325  TRP B CA  1 
ATOM   6297 C  C   . TRP B 1 325 ? -8.249  -15.716 67.036  1.00 30.07  ? 325  TRP B C   1 
ATOM   6298 O  O   . TRP B 1 325 ? -7.976  -15.437 65.868  1.00 30.53  ? 325  TRP B O   1 
ATOM   6299 C  CB  . TRP B 1 325 ? -10.488 -16.552 66.180  1.00 32.90  ? 325  TRP B CB  1 
ATOM   6300 C  CG  . TRP B 1 325 ? -11.696 -17.316 66.650  1.00 30.85  ? 325  TRP B CG  1 
ATOM   6301 C  CD1 . TRP B 1 325 ? -13.012 -16.912 66.637  1.00 34.85  ? 325  TRP B CD1 1 
ATOM   6302 C  CD2 . TRP B 1 325 ? -11.676 -18.604 67.283  1.00 31.92  ? 325  TRP B CD2 1 
ATOM   6303 N  NE1 . TRP B 1 325 ? -13.803 -17.889 67.213  1.00 31.17  ? 325  TRP B NE1 1 
ATOM   6304 C  CE2 . TRP B 1 325 ? -13.006 -18.932 67.614  1.00 32.99  ? 325  TRP B CE2 1 
ATOM   6305 C  CE3 . TRP B 1 325 ? -10.654 -19.513 67.597  1.00 31.20  ? 325  TRP B CE3 1 
ATOM   6306 C  CZ2 . TRP B 1 325 ? -13.340 -20.136 68.234  1.00 36.41  ? 325  TRP B CZ2 1 
ATOM   6307 C  CZ3 . TRP B 1 325 ? -10.986 -20.711 68.212  1.00 34.79  ? 325  TRP B CZ3 1 
ATOM   6308 C  CH2 . TRP B 1 325 ? -12.320 -21.012 68.520  1.00 34.33  ? 325  TRP B CH2 1 
ATOM   6309 N  N   . PRO B 1 326 ? -7.332  -15.625 68.003  1.00 31.68  ? 326  PRO B N   1 
ATOM   6310 C  CA  . PRO B 1 326 ? -5.953  -15.236 67.661  1.00 26.63  ? 326  PRO B CA  1 
ATOM   6311 C  C   . PRO B 1 326 ? -5.366  -16.285 66.729  1.00 30.08  ? 326  PRO B C   1 
ATOM   6312 O  O   . PRO B 1 326 ? -5.372  -17.479 67.036  1.00 30.68  ? 326  PRO B O   1 
ATOM   6313 C  CB  . PRO B 1 326 ? -5.241  -15.202 69.018  1.00 30.93  ? 326  PRO B CB  1 
ATOM   6314 C  CG  . PRO B 1 326 ? -6.044  -16.162 69.878  1.00 29.95  ? 326  PRO B CG  1 
ATOM   6315 C  CD  . PRO B 1 326 ? -7.469  -15.983 69.430  1.00 31.78  ? 326  PRO B CD  1 
ATOM   6316 N  N   . THR B 1 327 ? -4.880  -15.837 65.569  1.00 28.82  ? 327  THR B N   1 
ATOM   6317 C  CA  . THR B 1 327 ? -4.666  -16.781 64.478  1.00 30.35  ? 327  THR B CA  1 
ATOM   6318 C  C   . THR B 1 327 ? -3.365  -17.549 64.612  1.00 32.70  ? 327  THR B C   1 
ATOM   6319 O  O   . THR B 1 327 ? -3.186  -18.543 63.907  1.00 30.68  ? 327  THR B O   1 
ATOM   6320 C  CB  . THR B 1 327 ? -4.714  -16.064 63.130  1.00 31.05  ? 327  THR B CB  1 
ATOM   6321 O  OG1 . THR B 1 327 ? -3.937  -14.864 63.210  1.00 32.80  ? 327  THR B OG1 1 
ATOM   6322 C  CG2 . THR B 1 327 ? -6.171  -15.665 62.806  1.00 31.61  ? 327  THR B CG2 1 
ATOM   6323 N  N   . ALA B 1 328 ? -2.452  -17.107 65.482  1.00 30.66  ? 328  ALA B N   1 
ATOM   6324 C  CA  . ALA B 1 328 ? -1.339  -17.940 65.927  1.00 32.63  ? 328  ALA B CA  1 
ATOM   6325 C  C   . ALA B 1 328 ? -1.634  -18.280 67.384  1.00 31.93  ? 328  ALA B C   1 
ATOM   6326 O  O   . ALA B 1 328 ? -1.276  -17.522 68.293  1.00 33.09  ? 328  ALA B O   1 
ATOM   6327 C  CB  . ALA B 1 328 ? 0.004   -17.217 65.772  1.00 31.20  ? 328  ALA B CB  1 
ATOM   6328 N  N   . PRO B 1 329 ? -2.327  -19.388 67.652  1.00 30.11  ? 329  PRO B N   1 
ATOM   6329 C  CA  . PRO B 1 329 ? -3.151  -19.484 68.867  1.00 32.26  ? 329  PRO B CA  1 
ATOM   6330 C  C   . PRO B 1 329 ? -2.419  -19.910 70.127  1.00 32.40  ? 329  PRO B C   1 
ATOM   6331 O  O   . PRO B 1 329 ? -3.062  -20.067 71.173  1.00 30.85  ? 329  PRO B O   1 
ATOM   6332 C  CB  . PRO B 1 329 ? -4.203  -20.528 68.480  1.00 35.19  ? 329  PRO B CB  1 
ATOM   6333 C  CG  . PRO B 1 329 ? -3.523  -21.388 67.478  1.00 33.66  ? 329  PRO B CG  1 
ATOM   6334 C  CD  . PRO B 1 329 ? -2.635  -20.448 66.675  1.00 32.94  ? 329  PRO B CD  1 
ATOM   6335 N  N   . ALA B 1 330 ? -1.115  -20.134 70.077  1.00 30.56  ? 330  ALA B N   1 
ATOM   6336 C  CA  . ALA B 1 330 ? -0.420  -20.528 71.293  1.00 30.68  ? 330  ALA B CA  1 
ATOM   6337 C  C   . ALA B 1 330 ? 1.031   -20.129 71.133  1.00 30.37  ? 330  ALA B C   1 
ATOM   6338 O  O   . ALA B 1 330 ? 1.511   -19.922 70.018  1.00 31.87  ? 330  ALA B O   1 
ATOM   6339 C  CB  . ALA B 1 330 ? -0.538  -22.036 71.554  1.00 29.00  ? 330  ALA B CB  1 
ATOM   6340 N  N   . PHE B 1 331 ? 1.720   -20.026 72.262  1.00 30.25  ? 331  PHE B N   1 
ATOM   6341 C  CA  . PHE B 1 331 ? 3.172   -19.928 72.264  1.00 29.64  ? 331  PHE B CA  1 
ATOM   6342 C  C   . PHE B 1 331 ? 3.666   -20.674 73.489  1.00 33.98  ? 331  PHE B C   1 
ATOM   6343 O  O   . PHE B 1 331 ? 2.908   -20.937 74.427  1.00 33.09  ? 331  PHE B O   1 
ATOM   6344 C  CB  . PHE B 1 331 ? 3.690   -18.471 72.222  1.00 30.27  ? 331  PHE B CB  1 
ATOM   6345 C  CG  . PHE B 1 331 ? 3.174   -17.557 73.319  1.00 31.88  ? 331  PHE B CG  1 
ATOM   6346 C  CD1 . PHE B 1 331 ? 1.979   -16.865 73.166  1.00 31.55  ? 331  PHE B CD1 1 
ATOM   6347 C  CD2 . PHE B 1 331 ? 3.947   -17.307 74.451  1.00 34.02  ? 331  PHE B CD2 1 
ATOM   6348 C  CE1 . PHE B 1 331 ? 1.510   -16.004 74.154  1.00 32.58  ? 331  PHE B CE1 1 
ATOM   6349 C  CE2 . PHE B 1 331 ? 3.506   -16.447 75.448  1.00 33.11  ? 331  PHE B CE2 1 
ATOM   6350 C  CZ  . PHE B 1 331 ? 2.284   -15.782 75.308  1.00 31.44  ? 331  PHE B CZ  1 
ATOM   6351 N  N   . SER B 1 332 ? 4.944   -21.040 73.457  1.00 32.74  ? 332  SER B N   1 
ATOM   6352 C  CA  . SER B 1 332 ? 5.518   -21.935 74.452  1.00 30.94  ? 332  SER B CA  1 
ATOM   6353 C  C   . SER B 1 332 ? 6.652   -21.234 75.198  1.00 32.93  ? 332  SER B C   1 
ATOM   6354 O  O   . SER B 1 332 ? 7.348   -20.392 74.630  1.00 31.67  ? 332  SER B O   1 
ATOM   6355 C  CB  . SER B 1 332 ? 6.027   -23.221 73.782  1.00 31.11  ? 332  SER B CB  1 
ATOM   6356 O  OG  . SER B 1 332 ? 6.363   -24.165 74.778  1.00 33.93  ? 332  SER B OG  1 
ATOM   6357 N  N   . LEU B 1 333 ? 6.836   -21.605 76.472  1.00 31.71  ? 333  LEU B N   1 
ATOM   6358 C  CA  . LEU B 1 333 ? 7.870   -21.063 77.351  1.00 33.08  ? 333  LEU B CA  1 
ATOM   6359 C  C   . LEU B 1 333 ? 8.530   -22.196 78.126  1.00 34.65  ? 333  LEU B C   1 
ATOM   6360 O  O   . LEU B 1 333 ? 7.949   -23.269 78.313  1.00 34.65  ? 333  LEU B O   1 
ATOM   6361 C  CB  . LEU B 1 333 ? 7.284   -20.058 78.361  1.00 34.81  ? 333  LEU B CB  1 
ATOM   6362 C  CG  . LEU B 1 333 ? 6.484   -18.945 77.675  1.00 37.55  ? 333  LEU B CG  1 
ATOM   6363 C  CD1 . LEU B 1 333 ? 5.379   -18.398 78.559  1.00 38.88  ? 333  LEU B CD1 1 
ATOM   6364 C  CD2 . LEU B 1 333 ? 7.413   -17.845 77.177  1.00 32.92  ? 333  LEU B CD2 1 
ATOM   6365 N  N   . TYR B 1 334 ? 9.749   -21.942 78.601  1.00 33.77  ? 334  TYR B N   1 
ATOM   6366 C  CA  . TYR B 1 334 ? 10.402  -22.846 79.536  1.00 36.43  ? 334  TYR B CA  1 
ATOM   6367 C  C   . TYR B 1 334 ? 10.910  -22.049 80.730  1.00 33.81  ? 334  TYR B C   1 
ATOM   6368 O  O   . TYR B 1 334 ? 11.238  -20.867 80.611  1.00 32.78  ? 334  TYR B O   1 
ATOM   6369 C  CB  . TYR B 1 334 ? 11.567  -23.628 78.875  1.00 35.33  ? 334  TYR B CB  1 
ATOM   6370 C  CG  . TYR B 1 334 ? 12.768  -22.774 78.548  1.00 34.09  ? 334  TYR B CG  1 
ATOM   6371 C  CD1 . TYR B 1 334 ? 12.871  -22.145 77.320  1.00 32.32  ? 334  TYR B CD1 1 
ATOM   6372 C  CD2 . TYR B 1 334 ? 13.812  -22.611 79.474  1.00 32.29  ? 334  TYR B CD2 1 
ATOM   6373 C  CE1 . TYR B 1 334 ? 13.967  -21.355 77.004  1.00 34.06  ? 334  TYR B CE1 1 
ATOM   6374 C  CE2 . TYR B 1 334 ? 14.907  -21.822 79.175  1.00 34.74  ? 334  TYR B CE2 1 
ATOM   6375 C  CZ  . TYR B 1 334 ? 14.975  -21.192 77.936  1.00 36.63  ? 334  TYR B CZ  1 
ATOM   6376 O  OH  . TYR B 1 334 ? 16.055  -20.401 77.613  1.00 37.06  ? 334  TYR B OH  1 
ATOM   6377 N  N   . ALA B 1 335 ? 10.958  -22.707 81.885  1.00 32.52  ? 335  ALA B N   1 
ATOM   6378 C  CA  . ALA B 1 335 ? 11.415  -22.054 83.110  1.00 33.26  ? 335  ALA B CA  1 
ATOM   6379 C  C   . ALA B 1 335 ? 12.928  -21.911 83.074  1.00 30.71  ? 335  ALA B C   1 
ATOM   6380 O  O   . ALA B 1 335 ? 13.637  -22.909 82.949  1.00 35.02  ? 335  ALA B O   1 
ATOM   6381 C  CB  . ALA B 1 335 ? 10.996  -22.869 84.333  1.00 35.04  ? 335  ALA B CB  1 
ATOM   6382 N  N   . LYS B 1 336 ? 13.424  -20.680 83.214  1.00 34.49  ? 336  LYS B N   1 
ATOM   6383 C  CA  . LYS B 1 336 ? 14.874  -20.469 83.216  1.00 34.17  ? 336  LYS B CA  1 
ATOM   6384 C  C   . LYS B 1 336 ? 15.537  -21.078 84.458  1.00 36.80  ? 336  LYS B C   1 
ATOM   6385 O  O   . LYS B 1 336 ? 16.691  -21.533 84.395  1.00 37.29  ? 336  LYS B O   1 
ATOM   6386 C  CB  . LYS B 1 336 ? 15.174  -18.966 83.124  1.00 32.56  ? 336  LYS B CB  1 
ATOM   6387 C  CG  . LYS B 1 336 ? 14.785  -18.342 81.785  1.00 37.19  ? 336  LYS B CG  1 
ATOM   6388 C  CD  . LYS B 1 336 ? 14.605  -16.836 81.889  1.00 37.92  ? 336  LYS B CD  1 
ATOM   6389 C  CE  . LYS B 1 336 ? 15.899  -16.144 82.378  1.00 41.52  ? 336  LYS B CE  1 
ATOM   6390 N  NZ  . LYS B 1 336 ? 17.027  -16.301 81.410  1.00 44.82  ? 336  LYS B NZ  1 
ATOM   6391 N  N   . GLU B 1 337 ? 14.839  -21.071 85.589  1.00 36.60  ? 337  GLU B N   1 
ATOM   6392 C  CA  . GLU B 1 337 ? 15.315  -21.671 86.830  1.00 39.20  ? 337  GLU B CA  1 
ATOM   6393 C  C   . GLU B 1 337 ? 14.128  -22.307 87.538  1.00 39.95  ? 337  GLU B C   1 
ATOM   6394 O  O   . GLU B 1 337 ? 12.971  -22.102 87.158  1.00 38.93  ? 337  GLU B O   1 
ATOM   6395 C  CB  . GLU B 1 337 ? 15.979  -20.639 87.766  1.00 40.79  ? 337  GLU B CB  1 
ATOM   6396 C  CG  . GLU B 1 337 ? 17.161  -19.873 87.173  1.00 43.12  ? 337  GLU B CG  1 
ATOM   6397 C  CD  . GLU B 1 337 ? 18.404  -20.730 86.870  1.00 46.97  ? 337  GLU B CD  1 
ATOM   6398 O  OE1 . GLU B 1 337 ? 18.545  -21.860 87.397  1.00 39.91  ? 337  GLU B OE1 1 
ATOM   6399 O  OE2 . GLU B 1 337 ? 19.255  -20.255 86.092  1.00 49.28  ? 337  GLU B OE2 1 
ATOM   6400 N  N   . ASP B 1 338 ? 14.413  -23.079 88.591  1.00 38.75  ? 338  ASP B N   1 
ATOM   6401 C  CA  . ASP B 1 338 ? 13.337  -23.518 89.473  1.00 38.05  ? 338  ASP B CA  1 
ATOM   6402 C  C   . ASP B 1 338 ? 12.530  -22.309 89.919  1.00 38.90  ? 338  ASP B C   1 
ATOM   6403 O  O   . ASP B 1 338 ? 13.084  -21.256 90.249  1.00 43.77  ? 338  ASP B O   1 
ATOM   6404 C  CB  . ASP B 1 338 ? 13.879  -24.235 90.715  1.00 41.87  ? 338  ASP B CB  1 
ATOM   6405 C  CG  . ASP B 1 338 ? 14.641  -25.506 90.402  1.00 43.83  ? 338  ASP B CG  1 
ATOM   6406 O  OD1 . ASP B 1 338 ? 14.609  -26.019 89.261  1.00 42.57  ? 338  ASP B OD1 1 
ATOM   6407 O  OD2 . ASP B 1 338 ? 15.307  -26.000 91.339  1.00 45.97  ? 338  ASP B OD2 1 
ATOM   6408 N  N   . THR B 1 339 ? 11.208  -22.460 89.932  1.00 38.46  ? 339  THR B N   1 
ATOM   6409 C  CA  . THR B 1 339 ? 10.337  -21.353 90.294  1.00 40.21  ? 339  THR B CA  1 
ATOM   6410 C  C   . THR B 1 339 ? 8.966   -21.932 90.600  1.00 40.01  ? 339  THR B C   1 
ATOM   6411 O  O   . THR B 1 339 ? 8.643   -23.047 90.184  1.00 43.50  ? 339  THR B O   1 
ATOM   6412 C  CB  . THR B 1 339 ? 10.252  -20.314 89.171  1.00 43.87  ? 339  THR B CB  1 
ATOM   6413 O  OG1 . THR B 1 339 ? 9.710   -19.095 89.681  1.00 40.94  ? 339  THR B OG1 1 
ATOM   6414 C  CG2 . THR B 1 339 ? 9.348   -20.831 88.037  1.00 38.89  ? 339  THR B CG2 1 
ATOM   6415 N  N   . VAL B 1 340 ? 8.167   -21.175 91.343  1.00 40.61  ? 340  VAL B N   1 
ATOM   6416 C  CA  . VAL B 1 340 ? 6.819   -21.600 91.707  1.00 42.30  ? 340  VAL B CA  1 
ATOM   6417 C  C   . VAL B 1 340 ? 5.829   -20.726 90.958  1.00 39.89  ? 340  VAL B C   1 
ATOM   6418 O  O   . VAL B 1 340 ? 5.813   -19.501 91.135  1.00 43.25  ? 340  VAL B O   1 
ATOM   6419 C  CB  . VAL B 1 340 ? 6.584   -21.526 93.225  1.00 43.22  ? 340  VAL B CB  1 
ATOM   6420 C  CG1 . VAL B 1 340 ? 5.135   -21.873 93.553  1.00 42.84  ? 340  VAL B CG1 1 
ATOM   6421 C  CG2 . VAL B 1 340 ? 7.528   -22.474 93.944  1.00 41.99  ? 340  VAL B CG2 1 
ATOM   6422 N  N   . LEU B 1 341 ? 4.978   -21.360 90.150  1.00 42.80  ? 341  LEU B N   1 
ATOM   6423 C  CA  . LEU B 1 341 ? 3.975   -20.655 89.369  1.00 43.16  ? 341  LEU B CA  1 
ATOM   6424 C  C   . LEU B 1 341 ? 2.718   -20.450 90.207  1.00 39.56  ? 341  LEU B C   1 
ATOM   6425 O  O   . LEU B 1 341 ? 2.157   -21.411 90.743  1.00 38.23  ? 341  LEU B O   1 
ATOM   6426 C  CB  . LEU B 1 341 ? 3.645   -21.436 88.097  1.00 37.64  ? 341  LEU B CB  1 
ATOM   6427 C  CG  . LEU B 1 341 ? 2.798   -20.724 87.051  1.00 38.42  ? 341  LEU B CG  1 
ATOM   6428 C  CD1 . LEU B 1 341 ? 3.563   -19.544 86.454  1.00 40.43  ? 341  LEU B CD1 1 
ATOM   6429 C  CD2 . LEU B 1 341 ? 2.434   -21.733 85.976  1.00 37.72  ? 341  LEU B CD2 1 
ATOM   6430 N  N   . GLY B 1 342 ? 2.276   -19.200 90.304  1.00 39.59  ? 342  GLY B N   1 
ATOM   6431 C  CA  . GLY B 1 342 ? 1.016   -18.891 90.955  1.00 43.73  ? 342  GLY B CA  1 
ATOM   6432 C  C   . GLY B 1 342 ? 0.949   -19.219 92.428  1.00 45.88  ? 342  GLY B C   1 
ATOM   6433 O  O   . GLY B 1 342 ? -0.150  -19.360 92.965  1.00 41.20  ? 342  GLY B O   1 
ATOM   6434 N  N   . GLY B 1 343 ? 2.092   -19.339 93.096  1.00 40.59  ? 343  GLY B N   1 
ATOM   6435 C  CA  . GLY B 1 343 ? 2.091   -19.715 94.492  1.00 43.20  ? 343  GLY B CA  1 
ATOM   6436 C  C   . GLY B 1 343 ? 1.668   -21.136 94.763  1.00 45.63  ? 343  GLY B C   1 
ATOM   6437 O  O   . GLY B 1 343 ? 1.488   -21.500 95.931  1.00 49.44  ? 343  GLY B O   1 
ATOM   6438 N  N   . GLU B 1 344 ? 1.529   -21.966 93.729  1.00 42.59  ? 344  GLU B N   1 
ATOM   6439 C  CA  . GLU B 1 344 ? 0.877   -23.264 93.882  1.00 43.66  ? 344  GLU B CA  1 
ATOM   6440 C  C   . GLU B 1 344 ? 1.500   -24.386 93.070  1.00 44.07  ? 344  GLU B C   1 
ATOM   6441 O  O   . GLU B 1 344 ? 1.337   -25.547 93.455  1.00 45.18  ? 344  GLU B O   1 
ATOM   6442 C  CB  . GLU B 1 344 ? -0.608  -23.153 93.503  1.00 45.46  ? 344  GLU B CB  1 
ATOM   6443 C  CG  . GLU B 1 344 ? -1.374  -22.156 94.362  1.00 51.67  ? 344  GLU B CG  1 
ATOM   6444 C  CD  . GLU B 1 344 ? -2.774  -21.860 93.841  1.00 57.31  ? 344  GLU B CD  1 
ATOM   6445 O  OE1 . GLU B 1 344 ? -3.044  -22.126 92.653  1.00 50.90  ? 344  GLU B OE1 1 
ATOM   6446 O  OE2 . GLU B 1 344 ? -3.605  -21.351 94.621  1.00 61.22  ? 344  GLU B OE2 1 
ATOM   6447 N  N   . TYR B 1 345 ? 2.196   -24.106 91.968  1.00 40.99  ? 345  TYR B N   1 
ATOM   6448 C  CA  . TYR B 1 345 ? 2.673   -25.142 91.053  1.00 43.45  ? 345  TYR B CA  1 
ATOM   6449 C  C   . TYR B 1 345 ? 4.184   -25.052 90.912  1.00 41.79  ? 345  TYR B C   1 
ATOM   6450 O  O   . TYR B 1 345 ? 4.695   -24.214 90.147  1.00 39.36  ? 345  TYR B O   1 
ATOM   6451 C  CB  . TYR B 1 345 ? 1.986   -25.006 89.693  1.00 42.00  ? 345  TYR B CB  1 
ATOM   6452 C  CG  . TYR B 1 345 ? 0.475   -25.063 89.805  1.00 39.80  ? 345  TYR B CG  1 
ATOM   6453 C  CD1 . TYR B 1 345 ? -0.173  -26.274 90.021  1.00 43.72  ? 345  TYR B CD1 1 
ATOM   6454 C  CD2 . TYR B 1 345 ? -0.295  -23.911 89.714  1.00 38.19  ? 345  TYR B CD2 1 
ATOM   6455 C  CE1 . TYR B 1 345 ? -1.551  -26.348 90.142  1.00 44.46  ? 345  TYR B CE1 1 
ATOM   6456 C  CE2 . TYR B 1 345 ? -1.685  -23.967 89.839  1.00 41.90  ? 345  TYR B CE2 1 
ATOM   6457 C  CZ  . TYR B 1 345 ? -2.302  -25.192 90.056  1.00 46.44  ? 345  TYR B CZ  1 
ATOM   6458 O  OH  . TYR B 1 345 ? -3.673  -25.262 90.178  1.00 46.92  ? 345  TYR B OH  1 
ATOM   6459 N  N   . PRO B 1 346 ? 4.941   -25.871 91.634  1.00 44.71  ? 346  PRO B N   1 
ATOM   6460 C  CA  . PRO B 1 346 ? 6.401   -25.809 91.518  1.00 42.18  ? 346  PRO B CA  1 
ATOM   6461 C  C   . PRO B 1 346 ? 6.871   -26.325 90.167  1.00 39.86  ? 346  PRO B C   1 
ATOM   6462 O  O   . PRO B 1 346 ? 6.394   -27.344 89.664  1.00 41.17  ? 346  PRO B O   1 
ATOM   6463 C  CB  . PRO B 1 346 ? 6.892   -26.701 92.672  1.00 43.74  ? 346  PRO B CB  1 
ATOM   6464 C  CG  . PRO B 1 346 ? 5.707   -26.875 93.572  1.00 44.65  ? 346  PRO B CG  1 
ATOM   6465 C  CD  . PRO B 1 346 ? 4.511   -26.827 92.669  1.00 43.19  ? 346  PRO B CD  1 
ATOM   6466 N  N   . LEU B 1 347 ? 7.809   -25.600 89.575  1.00 40.13  ? 347  LEU B N   1 
ATOM   6467 C  CA  . LEU B 1 347 ? 8.411   -25.976 88.308  1.00 39.54  ? 347  LEU B CA  1 
ATOM   6468 C  C   . LEU B 1 347 ? 9.921   -26.083 88.480  1.00 37.72  ? 347  LEU B C   1 
ATOM   6469 O  O   . LEU B 1 347 ? 10.530  -25.309 89.227  1.00 39.90  ? 347  LEU B O   1 
ATOM   6470 C  CB  . LEU B 1 347 ? 8.085   -24.950 87.211  1.00 41.10  ? 347  LEU B CB  1 
ATOM   6471 C  CG  . LEU B 1 347 ? 6.611   -24.682 86.912  1.00 35.46  ? 347  LEU B CG  1 
ATOM   6472 C  CD1 . LEU B 1 347 ? 6.516   -23.577 85.878  1.00 36.21  ? 347  LEU B CD1 1 
ATOM   6473 C  CD2 . LEU B 1 347 ? 5.902   -25.935 86.417  1.00 37.45  ? 347  LEU B CD2 1 
ATOM   6474 N  N   . GLU B 1 348 ? 10.509  -27.038 87.781  1.00 40.95  ? 348  GLU B N   1 
ATOM   6475 C  CA  . GLU B 1 348 ? 11.952  -27.192 87.728  1.00 39.68  ? 348  GLU B CA  1 
ATOM   6476 C  C   . GLU B 1 348 ? 12.498  -26.506 86.488  1.00 39.19  ? 348  GLU B C   1 
ATOM   6477 O  O   . GLU B 1 348 ? 11.827  -26.420 85.456  1.00 34.90  ? 348  GLU B O   1 
ATOM   6478 C  CB  . GLU B 1 348 ? 12.358  -28.669 87.703  1.00 41.00  ? 348  GLU B CB  1 
ATOM   6479 C  CG  . GLU B 1 348 ? 11.830  -29.507 88.871  1.00 46.97  ? 348  GLU B CG  1 
ATOM   6480 C  CD  . GLU B 1 348 ? 12.208  -30.961 88.725  1.00 56.39  ? 348  GLU B CD  1 
ATOM   6481 O  OE1 . GLU B 1 348 ? 13.329  -31.326 89.145  1.00 61.25  ? 348  GLU B OE1 1 
ATOM   6482 O  OE2 . GLU B 1 348 ? 11.392  -31.743 88.191  1.00 64.19  ? 348  GLU B OE2 1 
ATOM   6483 N  N   . LYS B 1 349 ? 13.730  -26.027 86.602  1.00 37.97  ? 349  LYS B N   1 
ATOM   6484 C  CA  . LYS B 1 349 ? 14.451  -25.503 85.457  1.00 37.50  ? 349  LYS B CA  1 
ATOM   6485 C  C   . LYS B 1 349 ? 14.203  -26.386 84.246  1.00 37.76  ? 349  LYS B C   1 
ATOM   6486 O  O   . LYS B 1 349 ? 14.344  -27.614 84.313  1.00 38.51  ? 349  LYS B O   1 
ATOM   6487 C  CB  . LYS B 1 349 ? 15.948  -25.442 85.776  1.00 40.74  ? 349  LYS B CB  1 
ATOM   6488 C  CG  . LYS B 1 349 ? 16.824  -25.044 84.611  1.00 38.89  ? 349  LYS B CG  1 
ATOM   6489 C  CD  . LYS B 1 349 ? 18.278  -24.883 85.055  1.00 44.72  ? 349  LYS B CD  1 
ATOM   6490 C  CE  . LYS B 1 349 ? 19.120  -24.334 83.920  1.00 46.17  ? 349  LYS B CE  1 
ATOM   6491 N  NZ  . LYS B 1 349 ? 20.557  -24.297 84.308  1.00 49.01  ? 349  LYS B NZ  1 
ATOM   6492 N  N   . GLY B 1 350 ? 13.819  -25.757 83.134  1.00 33.88  ? 350  GLY B N   1 
ATOM   6493 C  CA  . GLY B 1 350 ? 13.584  -26.473 81.905  1.00 30.74  ? 350  GLY B CA  1 
ATOM   6494 C  C   . GLY B 1 350 ? 12.149  -26.918 81.679  1.00 35.34  ? 350  GLY B C   1 
ATOM   6495 O  O   . GLY B 1 350 ? 11.813  -27.302 80.555  1.00 36.02  ? 350  GLY B O   1 
ATOM   6496 N  N   . ASP B 1 351 ? 11.303  -26.890 82.710  1.00 33.91  ? 351  ASP B N   1 
ATOM   6497 C  CA  . ASP B 1 351 ? 9.900   -27.261 82.541  1.00 33.75  ? 351  ASP B CA  1 
ATOM   6498 C  C   . ASP B 1 351 ? 9.222   -26.316 81.549  1.00 36.86  ? 351  ASP B C   1 
ATOM   6499 O  O   . ASP B 1 351 ? 9.460   -25.105 81.563  1.00 34.74  ? 351  ASP B O   1 
ATOM   6500 C  CB  . ASP B 1 351 ? 9.167   -27.197 83.886  1.00 38.50  ? 351  ASP B CB  1 
ATOM   6501 C  CG  . ASP B 1 351 ? 9.427   -28.409 84.779  1.00 38.28  ? 351  ASP B CG  1 
ATOM   6502 O  OD1 . ASP B 1 351 ? 10.085  -29.363 84.325  1.00 36.41  ? 351  ASP B OD1 1 
ATOM   6503 O  OD2 . ASP B 1 351 ? 8.928   -28.406 85.939  1.00 40.97  ? 351  ASP B OD2 1 
ATOM   6504 N  N   . GLU B 1 352 ? 8.341   -26.875 80.717  1.00 35.02  ? 352  GLU B N   1 
ATOM   6505 C  CA  . GLU B 1 352 ? 7.703   -26.180 79.611  1.00 38.00  ? 352  GLU B CA  1 
ATOM   6506 C  C   . GLU B 1 352 ? 6.278   -25.770 79.969  1.00 37.22  ? 352  GLU B C   1 
ATOM   6507 O  O   . GLU B 1 352 ? 5.585   -26.451 80.732  1.00 35.47  ? 352  GLU B O   1 
ATOM   6508 C  CB  . GLU B 1 352 ? 7.674   -27.090 78.384  1.00 37.00  ? 352  GLU B CB  1 
ATOM   6509 C  CG  . GLU B 1 352 ? 9.055   -27.537 77.952  1.00 43.11  ? 352  GLU B CG  1 
ATOM   6510 C  CD  . GLU B 1 352 ? 9.036   -28.356 76.681  1.00 49.56  ? 352  GLU B CD  1 
ATOM   6511 O  OE1 . GLU B 1 352 ? 10.137  -28.747 76.234  1.00 53.69  ? 352  GLU B OE1 1 
ATOM   6512 O  OE2 . GLU B 1 352 ? 7.932   -28.627 76.146  1.00 46.36  ? 352  GLU B OE2 1 
ATOM   6513 N  N   . LEU B 1 353 ? 5.846   -24.656 79.382  1.00 33.32  ? 353  LEU B N   1 
ATOM   6514 C  CA  . LEU B 1 353 ? 4.488   -24.147 79.478  1.00 32.39  ? 353  LEU B CA  1 
ATOM   6515 C  C   . LEU B 1 353 ? 3.960   -23.870 78.079  1.00 33.37  ? 353  LEU B C   1 
ATOM   6516 O  O   . LEU B 1 353 ? 4.712   -23.472 77.180  1.00 34.17  ? 353  LEU B O   1 
ATOM   6517 C  CB  . LEU B 1 353 ? 4.410   -22.839 80.282  1.00 33.77  ? 353  LEU B CB  1 
ATOM   6518 C  CG  . LEU B 1 353 ? 4.991   -22.843 81.693  1.00 32.11  ? 353  LEU B CG  1 
ATOM   6519 C  CD1 . LEU B 1 353 ? 5.033   -21.421 82.225  1.00 34.27  ? 353  LEU B CD1 1 
ATOM   6520 C  CD2 . LEU B 1 353 ? 4.118   -23.716 82.579  1.00 36.80  ? 353  LEU B CD2 1 
ATOM   6521 N  N   . MET B 1 354 ? 2.658   -24.079 77.906  1.00 33.46  ? 354  MET B N   1 
ATOM   6522 C  CA  . MET B 1 354 ? 1.955   -23.699 76.684  1.00 33.74  ? 354  MET B CA  1 
ATOM   6523 C  C   . MET B 1 354 ? 0.904   -22.668 77.053  1.00 33.39  ? 354  MET B C   1 
ATOM   6524 O  O   . MET B 1 354 ? 0.078   -22.911 77.936  1.00 33.68  ? 354  MET B O   1 
ATOM   6525 C  CB  . MET B 1 354 ? 1.287   -24.898 76.010  1.00 34.93  ? 354  MET B CB  1 
ATOM   6526 C  CG  . MET B 1 354 ? 2.198   -25.946 75.428  1.00 34.80  ? 354  MET B CG  1 
ATOM   6527 S  SD  . MET B 1 354 ? 3.241   -25.388 74.068  1.00 37.80  ? 354  MET B SD  1 
ATOM   6528 C  CE  . MET B 1 354 ? 2.038   -24.629 72.974  1.00 34.62  ? 354  MET B CE  1 
ATOM   6529 N  N   . VAL B 1 355 ? 0.926   -21.531 76.372  1.00 31.64  ? 355  VAL B N   1 
ATOM   6530 C  CA  . VAL B 1 355 ? -0.049  -20.466 76.573  1.00 31.56  ? 355  VAL B CA  1 
ATOM   6531 C  C   . VAL B 1 355 ? -1.151  -20.636 75.539  1.00 31.36  ? 355  VAL B C   1 
ATOM   6532 O  O   . VAL B 1 355 ? -0.913  -20.488 74.335  1.00 30.88  ? 355  VAL B O   1 
ATOM   6533 C  CB  . VAL B 1 355 ? 0.601   -19.078 76.461  1.00 30.79  ? 355  VAL B CB  1 
ATOM   6534 C  CG1 . VAL B 1 355 ? -0.478  -18.010 76.504  1.00 30.82  ? 355  VAL B CG1 1 
ATOM   6535 C  CG2 . VAL B 1 355 ? 1.581   -18.848 77.613  1.00 31.08  ? 355  VAL B CG2 1 
ATOM   6536 N  N   . LEU B 1 356 ? -2.364  -20.930 76.002  1.00 30.68  ? 356  LEU B N   1 
ATOM   6537 C  CA  . LEU B 1 356 ? -3.503  -21.143 75.114  1.00 33.06  ? 356  LEU B CA  1 
ATOM   6538 C  C   . LEU B 1 356 ? -4.211  -19.807 74.931  1.00 33.55  ? 356  LEU B C   1 
ATOM   6539 O  O   . LEU B 1 356 ? -5.095  -19.448 75.702  1.00 33.49  ? 356  LEU B O   1 
ATOM   6540 C  CB  . LEU B 1 356 ? -4.424  -22.200 75.711  1.00 34.12  ? 356  LEU B CB  1 
ATOM   6541 C  CG  . LEU B 1 356 ? -5.241  -23.152 74.858  1.00 46.29  ? 356  LEU B CG  1 
ATOM   6542 C  CD1 . LEU B 1 356 ? -4.410  -23.727 73.703  1.00 42.43  ? 356  LEU B CD1 1 
ATOM   6543 C  CD2 . LEU B 1 356 ? -5.725  -24.275 75.796  1.00 39.68  ? 356  LEU B CD2 1 
ATOM   6544 N  N   . ILE B 1 357 ? -3.832  -19.060 73.885  1.00 29.07  ? 357  ILE B N   1 
ATOM   6545 C  CA  . ILE B 1 357 ? -4.263  -17.662 73.781  1.00 29.17  ? 357  ILE B CA  1 
ATOM   6546 C  C   . ILE B 1 357 ? -5.776  -17.532 73.693  1.00 31.77  ? 357  ILE B C   1 
ATOM   6547 O  O   . ILE B 1 357 ? -6.332  -16.603 74.297  1.00 30.62  ? 357  ILE B O   1 
ATOM   6548 C  CB  . ILE B 1 357 ? -3.548  -16.968 72.615  1.00 29.73  ? 357  ILE B CB  1 
ATOM   6549 C  CG1 . ILE B 1 357 ? -2.033  -17.155 72.716  1.00 27.61  ? 357  ILE B CG1 1 
ATOM   6550 C  CG2 . ILE B 1 357 ? -3.885  -15.467 72.627  1.00 32.18  ? 357  ILE B CG2 1 
ATOM   6551 C  CD1 . ILE B 1 357 ? -1.330  -16.670 71.446  1.00 30.31  ? 357  ILE B CD1 1 
ATOM   6552 N  N   . PRO B 1 358 ? -6.495  -18.358 72.931  1.00 30.90  ? 358  PRO B N   1 
ATOM   6553 C  CA  . PRO B 1 358 ? -7.957  -18.192 72.888  1.00 31.35  ? 358  PRO B CA  1 
ATOM   6554 C  C   . PRO B 1 358 ? -8.602  -18.305 74.258  1.00 33.41  ? 358  PRO B C   1 
ATOM   6555 O  O   . PRO B 1 358 ? -9.649  -17.684 74.507  1.00 31.73  ? 358  PRO B O   1 
ATOM   6556 C  CB  . PRO B 1 358 ? -8.409  -19.320 71.948  1.00 33.61  ? 358  PRO B CB  1 
ATOM   6557 C  CG  . PRO B 1 358 ? -7.209  -19.589 71.078  1.00 31.36  ? 358  PRO B CG  1 
ATOM   6558 C  CD  . PRO B 1 358 ? -6.035  -19.426 72.021  1.00 29.68  ? 358  PRO B CD  1 
ATOM   6559 N  N   . GLN B 1 359 ? -8.019  -19.101 75.159  1.00 32.27  ? 359  GLN B N   1 
ATOM   6560 C  CA  . GLN B 1 359 ? -8.599  -19.251 76.486  1.00 33.07  ? 359  GLN B CA  1 
ATOM   6561 C  C   . GLN B 1 359 ? -8.241  -18.070 77.369  1.00 32.28  ? 359  GLN B C   1 
ATOM   6562 O  O   . GLN B 1 359 ? -9.084  -17.582 78.118  1.00 33.36  ? 359  GLN B O   1 
ATOM   6563 C  CB  . GLN B 1 359 ? -8.152  -20.570 77.126  1.00 33.25  ? 359  GLN B CB  1 
ATOM   6564 C  CG  . GLN B 1 359 ? -8.735  -21.824 76.477  1.00 37.06  ? 359  GLN B CG  1 
ATOM   6565 C  CD  . GLN B 1 359 ? -10.261 -21.851 76.465  1.00 36.70  ? 359  GLN B CD  1 
ATOM   6566 O  OE1 . GLN B 1 359 ? -10.883 -21.769 75.407  1.00 37.49  ? 359  GLN B OE1 1 
ATOM   6567 N  NE2 . GLN B 1 359 ? -10.864 -21.985 77.639  1.00 42.90  ? 359  GLN B NE2 1 
ATOM   6568 N  N   . LEU B 1 360 ? -6.993  -17.600 77.304  1.00 31.21  ? 360  LEU B N   1 
ATOM   6569 C  CA  . LEU B 1 360 ? -6.639  -16.345 77.955  1.00 33.21  ? 360  LEU B CA  1 
ATOM   6570 C  C   . LEU B 1 360 ? -7.662  -15.263 77.623  1.00 33.62  ? 360  LEU B C   1 
ATOM   6571 O  O   . LEU B 1 360 ? -8.125  -14.523 78.502  1.00 32.87  ? 360  LEU B O   1 
ATOM   6572 C  CB  . LEU B 1 360 ? -5.235  -15.906 77.506  1.00 29.66  ? 360  LEU B CB  1 
ATOM   6573 C  CG  . LEU B 1 360 ? -4.830  -14.494 77.960  1.00 35.08  ? 360  LEU B CG  1 
ATOM   6574 C  CD1 . LEU B 1 360 ? -4.588  -14.422 79.463  1.00 34.17  ? 360  LEU B CD1 1 
ATOM   6575 C  CD2 . LEU B 1 360 ? -3.603  -14.020 77.216  1.00 30.84  ? 360  LEU B CD2 1 
ATOM   6576 N  N   . HIS B 1 361 ? -8.010  -15.156 76.347  1.00 29.59  ? 361  HIS B N   1 
ATOM   6577 C  CA  . HIS B 1 361 ? -8.883  -14.104 75.850  1.00 30.98  ? 361  HIS B CA  1 
ATOM   6578 C  C   . HIS B 1 361 ? -10.343 -14.331 76.213  1.00 33.78  ? 361  HIS B C   1 
ATOM   6579 O  O   . HIS B 1 361 ? -11.184 -13.482 75.891  1.00 32.82  ? 361  HIS B O   1 
ATOM   6580 C  CB  . HIS B 1 361 ? -8.716  -13.986 74.333  1.00 30.31  ? 361  HIS B CB  1 
ATOM   6581 C  CG  . HIS B 1 361 ? -7.378  -13.440 73.925  1.00 30.97  ? 361  HIS B CG  1 
ATOM   6582 N  ND1 . HIS B 1 361 ? -6.970  -13.379 72.610  1.00 31.92  ? 361  HIS B ND1 1 
ATOM   6583 C  CD2 . HIS B 1 361 ? -6.364  -12.921 74.659  1.00 34.76  ? 361  HIS B CD2 1 
ATOM   6584 C  CE1 . HIS B 1 361 ? -5.760  -12.842 72.549  1.00 31.10  ? 361  HIS B CE1 1 
ATOM   6585 N  NE2 . HIS B 1 361 ? -5.369  -12.554 73.779  1.00 31.00  ? 361  HIS B NE2 1 
ATOM   6586 N  N   . ARG B 1 362 ? -10.652 -15.448 76.877  1.00 32.00  ? 362  ARG B N   1 
ATOM   6587 C  CA  . ARG B 1 362 ? -11.997 -15.732 77.372  1.00 30.53  ? 362  ARG B CA  1 
ATOM   6588 C  C   . ARG B 1 362 ? -12.052 -15.767 78.905  1.00 30.51  ? 362  ARG B C   1 
ATOM   6589 O  O   . ARG B 1 362 ? -13.016 -16.286 79.481  1.00 34.53  ? 362  ARG B O   1 
ATOM   6590 C  CB  . ARG B 1 362 ? -12.495 -17.051 76.779  1.00 32.36  ? 362  ARG B CB  1 
ATOM   6591 C  CG  . ARG B 1 362 ? -12.860 -16.969 75.289  1.00 31.19  ? 362  ARG B CG  1 
ATOM   6592 C  CD  . ARG B 1 362 ? -12.875 -18.359 74.641  1.00 30.88  ? 362  ARG B CD  1 
ATOM   6593 N  NE  . ARG B 1 362 ? -13.443 -18.323 73.294  1.00 34.08  ? 362  ARG B NE  1 
ATOM   6594 C  CZ  . ARG B 1 362 ? -12.785 -17.927 72.212  1.00 33.88  ? 362  ARG B CZ  1 
ATOM   6595 N  NH1 . ARG B 1 362 ? -11.528 -17.504 72.281  1.00 31.54  ? 362  ARG B NH1 1 
ATOM   6596 N  NH2 . ARG B 1 362 ? -13.404 -17.953 71.033  1.00 32.05  ? 362  ARG B NH2 1 
ATOM   6597 N  N   . ASP B 1 363 ? -11.016 -15.250 79.573  1.00 33.30  ? 363  ASP B N   1 
ATOM   6598 C  CA  . ASP B 1 363 ? -10.932 -15.225 81.037  1.00 32.69  ? 363  ASP B CA  1 
ATOM   6599 C  C   . ASP B 1 363 ? -11.975 -14.252 81.568  1.00 32.93  ? 363  ASP B C   1 
ATOM   6600 O  O   . ASP B 1 363 ? -11.843 -13.033 81.405  1.00 36.08  ? 363  ASP B O   1 
ATOM   6601 C  CB  . ASP B 1 363 ? -9.513  -14.832 81.467  1.00 32.44  ? 363  ASP B CB  1 
ATOM   6602 C  CG  . ASP B 1 363 ? -9.291  -14.888 82.983  1.00 37.16  ? 363  ASP B CG  1 
ATOM   6603 O  OD1 . ASP B 1 363 ? -10.261 -14.848 83.763  1.00 35.77  ? 363  ASP B OD1 1 
ATOM   6604 O  OD2 . ASP B 1 363 ? -8.117  -14.929 83.404  1.00 32.18  ? 363  ASP B OD2 1 
ATOM   6605 N  N   . LYS B 1 364 ? -13.039 -14.793 82.167  1.00 35.39  ? 364  LYS B N   1 
ATOM   6606 C  CA  . LYS B 1 364 ? -14.148 -13.944 82.596  1.00 35.90  ? 364  LYS B CA  1 
ATOM   6607 C  C   . LYS B 1 364 ? -13.750 -13.000 83.725  1.00 34.39  ? 364  LYS B C   1 
ATOM   6608 O  O   . LYS B 1 364 ? -14.369 -11.942 83.879  1.00 34.43  ? 364  LYS B O   1 
ATOM   6609 C  CB  . LYS B 1 364 ? -15.333 -14.808 83.018  1.00 38.23  ? 364  LYS B CB  1 
ATOM   6610 C  CG  . LYS B 1 364 ? -15.959 -15.551 81.867  1.00 37.99  ? 364  LYS B CG  1 
ATOM   6611 C  CD  . LYS B 1 364 ? -17.168 -16.360 82.319  1.00 44.99  ? 364  LYS B CD  1 
ATOM   6612 C  CE  . LYS B 1 364 ? -17.736 -17.178 81.160  1.00 49.67  ? 364  LYS B CE  1 
ATOM   6613 N  NZ  . LYS B 1 364 ? -18.838 -18.092 81.575  1.00 61.60  ? 364  LYS B NZ  1 
ATOM   6614 N  N   . THR B 1 365 ? -12.738 -13.348 84.527  1.00 36.38  ? 365  THR B N   1 
ATOM   6615 C  CA  . THR B 1 365 ? -12.304 -12.424 85.575  1.00 37.82  ? 365  THR B CA  1 
ATOM   6616 C  C   . THR B 1 365 ? -11.672 -11.159 84.999  1.00 39.76  ? 365  THR B C   1 
ATOM   6617 O  O   . THR B 1 365 ? -11.587 -10.145 85.699  1.00 41.27  ? 365  THR B O   1 
ATOM   6618 C  CB  . THR B 1 365 ? -11.312 -13.089 86.533  1.00 41.06  ? 365  THR B CB  1 
ATOM   6619 O  OG1 . THR B 1 365 ? -10.046 -13.219 85.882  1.00 39.77  ? 365  THR B OG1 1 
ATOM   6620 C  CG2 . THR B 1 365 ? -11.805 -14.467 86.986  1.00 41.75  ? 365  THR B CG2 1 
ATOM   6621 N  N   . ILE B 1 366 ? -11.244 -11.199 83.743  1.00 35.09  ? 366  ILE B N   1 
ATOM   6622 C  CA  . ILE B 1 366 ? -10.684 -10.042 83.047  1.00 36.28  ? 366  ILE B CA  1 
ATOM   6623 C  C   . ILE B 1 366 ? -11.738 -9.328  82.228  1.00 37.39  ? 366  ILE B C   1 
ATOM   6624 O  O   . ILE B 1 366 ? -11.909 -8.112  82.335  1.00 38.56  ? 366  ILE B O   1 
ATOM   6625 C  CB  . ILE B 1 366 ? -9.514  -10.485 82.140  1.00 33.67  ? 366  ILE B CB  1 
ATOM   6626 C  CG1 . ILE B 1 366 ? -8.382  -11.066 82.981  1.00 35.77  ? 366  ILE B CG1 1 
ATOM   6627 C  CG2 . ILE B 1 366 ? -9.069  -9.319  81.245  1.00 35.42  ? 366  ILE B CG2 1 
ATOM   6628 C  CD1 . ILE B 1 366 ? -7.680  -10.043 83.848  1.00 38.76  ? 366  ILE B CD1 1 
ATOM   6629 N  N   . TRP B 1 367 ? -12.433 -10.078 81.375  1.00 35.88  ? 367  TRP B N   1 
ATOM   6630 C  CA  . TRP B 1 367 ? -13.240 -9.505  80.314  1.00 33.18  ? 367  TRP B CA  1 
ATOM   6631 C  C   . TRP B 1 367 ? -14.716 -9.381  80.668  1.00 39.15  ? 367  TRP B C   1 
ATOM   6632 O  O   . TRP B 1 367 ? -15.461 -8.749  79.914  1.00 40.14  ? 367  TRP B O   1 
ATOM   6633 C  CB  . TRP B 1 367 ? -13.083 -10.355 79.050  1.00 33.13  ? 367  TRP B CB  1 
ATOM   6634 C  CG  . TRP B 1 367 ? -11.658 -10.413 78.563  1.00 32.82  ? 367  TRP B CG  1 
ATOM   6635 C  CD1 . TRP B 1 367 ? -10.747 -11.391 78.806  1.00 32.90  ? 367  TRP B CD1 1 
ATOM   6636 C  CD2 . TRP B 1 367 ? -10.999 -9.439  77.743  1.00 33.24  ? 367  TRP B CD2 1 
ATOM   6637 N  NE1 . TRP B 1 367 ? -9.551  -11.094 78.180  1.00 31.90  ? 367  TRP B NE1 1 
ATOM   6638 C  CE2 . TRP B 1 367 ? -9.679  -9.893  77.531  1.00 33.43  ? 367  TRP B CE2 1 
ATOM   6639 C  CE3 . TRP B 1 367 ? -11.399 -8.226  77.168  1.00 34.66  ? 367  TRP B CE3 1 
ATOM   6640 C  CZ2 . TRP B 1 367 ? -8.756  -9.183  76.755  1.00 32.27  ? 367  TRP B CZ2 1 
ATOM   6641 C  CZ3 . TRP B 1 367 ? -10.476 -7.508  76.415  1.00 34.09  ? 367  TRP B CZ3 1 
ATOM   6642 C  CH2 . TRP B 1 367 ? -9.169  -7.984  76.221  1.00 31.79  ? 367  TRP B CH2 1 
ATOM   6643 N  N   . GLY B 1 368 ? -15.157 -9.970  81.779  1.00 40.26  ? 368  GLY B N   1 
ATOM   6644 C  CA  . GLY B 1 368 ? -16.566 -9.966  82.118  1.00 38.84  ? 368  GLY B CA  1 
ATOM   6645 C  C   . GLY B 1 368 ? -17.280 -11.202 81.616  1.00 41.49  ? 368  GLY B C   1 
ATOM   6646 O  O   . GLY B 1 368 ? -16.700 -12.112 81.025  1.00 37.98  ? 368  GLY B O   1 
ATOM   6647 N  N   . ASP B 1 369 ? -18.593 -11.225 81.849  1.00 39.77  ? 369  ASP B N   1 
ATOM   6648 C  CA  . ASP B 1 369 ? -19.373 -12.424 81.565  1.00 41.72  ? 369  ASP B CA  1 
ATOM   6649 C  C   . ASP B 1 369 ? -19.627 -12.634 80.077  1.00 45.14  ? 369  ASP B C   1 
ATOM   6650 O  O   . ASP B 1 369 ? -19.885 -13.766 79.662  1.00 47.58  ? 369  ASP B O   1 
ATOM   6651 C  CB  . ASP B 1 369 ? -20.707 -12.346 82.299  1.00 46.84  ? 369  ASP B CB  1 
ATOM   6652 C  CG  . ASP B 1 369 ? -20.536 -12.273 83.798  1.00 52.33  ? 369  ASP B CG  1 
ATOM   6653 O  OD1 . ASP B 1 369 ? -19.831 -13.140 84.360  1.00 51.92  ? 369  ASP B OD1 1 
ATOM   6654 O  OD2 . ASP B 1 369 ? -21.077 -11.322 84.408  1.00 56.79  ? 369  ASP B OD2 1 
ATOM   6655 N  N   . ASP B 1 370 ? -19.573 -11.582 79.271  1.00 38.96  ? 370  ASP B N   1 
ATOM   6656 C  CA  . ASP B 1 370 ? -19.983 -11.674 77.867  1.00 41.07  ? 370  ASP B CA  1 
ATOM   6657 C  C   . ASP B 1 370 ? -18.820 -12.010 76.926  1.00 38.30  ? 370  ASP B C   1 
ATOM   6658 O  O   . ASP B 1 370 ? -18.771 -11.476 75.815  1.00 39.23  ? 370  ASP B O   1 
ATOM   6659 C  CB  . ASP B 1 370 ? -20.653 -10.359 77.469  1.00 41.78  ? 370  ASP B CB  1 
ATOM   6660 C  CG  . ASP B 1 370 ? -19.711 -9.160  77.593  1.00 45.19  ? 370  ASP B CG  1 
ATOM   6661 O  OD1 . ASP B 1 370 ? -18.582 -9.348  78.109  1.00 44.49  ? 370  ASP B OD1 1 
ATOM   6662 O  OD2 . ASP B 1 370 ? -20.091 -8.031  77.182  1.00 47.25  ? 370  ASP B OD2 1 
ATOM   6663 N  N   . VAL B 1 371 ? -17.897 -12.907 77.317  1.00 36.73  ? 371  VAL B N   1 
ATOM   6664 C  CA  . VAL B 1 371 ? -16.634 -13.081 76.591  1.00 34.57  ? 371  VAL B CA  1 
ATOM   6665 C  C   . VAL B 1 371 ? -16.849 -13.649 75.199  1.00 35.62  ? 371  VAL B C   1 
ATOM   6666 O  O   . VAL B 1 371 ? -16.011 -13.450 74.310  1.00 36.62  ? 371  VAL B O   1 
ATOM   6667 C  CB  . VAL B 1 371 ? -15.643 -13.985 77.364  1.00 38.64  ? 371  VAL B CB  1 
ATOM   6668 C  CG1 . VAL B 1 371 ? -15.093 -13.285 78.576  1.00 44.01  ? 371  VAL B CG1 1 
ATOM   6669 C  CG2 . VAL B 1 371 ? -16.319 -15.306 77.769  1.00 41.42  ? 371  VAL B CG2 1 
ATOM   6670 N  N   . GLU B 1 372 ? -17.939 -14.389 74.982  1.00 32.46  ? 372  GLU B N   1 
ATOM   6671 C  CA  . GLU B 1 372 ? -18.176 -14.971 73.667  1.00 33.54  ? 372  GLU B CA  1 
ATOM   6672 C  C   . GLU B 1 372 ? -18.774 -13.974 72.678  1.00 36.25  ? 372  GLU B C   1 
ATOM   6673 O  O   . GLU B 1 372 ? -18.797 -14.251 71.469  1.00 34.94  ? 372  GLU B O   1 
ATOM   6674 C  CB  . GLU B 1 372 ? -19.088 -16.194 73.802  1.00 35.70  ? 372  GLU B CB  1 
ATOM   6675 C  CG  . GLU B 1 372 ? -18.451 -17.357 74.551  1.00 36.64  ? 372  GLU B CG  1 
ATOM   6676 C  CD  . GLU B 1 372 ? -17.292 -17.976 73.781  1.00 42.61  ? 372  GLU B CD  1 
ATOM   6677 O  OE1 . GLU B 1 372 ? -17.363 -18.030 72.534  1.00 42.98  ? 372  GLU B OE1 1 
ATOM   6678 O  OE2 . GLU B 1 372 ? -16.312 -18.398 74.429  1.00 43.38  ? 372  GLU B OE2 1 
ATOM   6679 N  N   . GLU B 1 373 ? -19.247 -12.825 73.149  1.00 33.11  ? 373  GLU B N   1 
ATOM   6680 C  CA  . GLU B 1 373 ? -19.861 -11.857 72.253  1.00 33.69  ? 373  GLU B CA  1 
ATOM   6681 C  C   . GLU B 1 373 ? -18.793 -11.026 71.547  1.00 33.09  ? 373  GLU B C   1 
ATOM   6682 O  O   . GLU B 1 373 ? -17.722 -10.757 72.093  1.00 34.24  ? 373  GLU B O   1 
ATOM   6683 C  CB  . GLU B 1 373 ? -20.836 -10.963 73.033  1.00 36.56  ? 373  GLU B CB  1 
ATOM   6684 C  CG  . GLU B 1 373 ? -22.124 -11.728 73.361  1.00 41.29  ? 373  GLU B CG  1 
ATOM   6685 C  CD  . GLU B 1 373 ? -23.036 -11.044 74.368  1.00 49.42  ? 373  GLU B CD  1 
ATOM   6686 O  OE1 . GLU B 1 373 ? -22.796 -9.873  74.747  1.00 44.11  ? 373  GLU B OE1 1 
ATOM   6687 O  OE2 . GLU B 1 373 ? -23.998 -11.711 74.800  1.00 50.44  ? 373  GLU B OE2 1 
ATOM   6688 N  N   . PHE B 1 374 ? -19.094 -10.639 70.311  1.00 33.54  ? 374  PHE B N   1 
ATOM   6689 C  CA  . PHE B 1 374 ? -18.185 -9.843  69.492  1.00 30.02  ? 374  PHE B CA  1 
ATOM   6690 C  C   . PHE B 1 374 ? -18.522 -8.378  69.734  1.00 33.59  ? 374  PHE B C   1 
ATOM   6691 O  O   . PHE B 1 374 ? -19.495 -7.851  69.178  1.00 31.22  ? 374  PHE B O   1 
ATOM   6692 C  CB  . PHE B 1 374 ? -18.310 -10.217 68.015  1.00 33.44  ? 374  PHE B CB  1 
ATOM   6693 C  CG  . PHE B 1 374 ? -17.290 -9.551  67.157  1.00 32.68  ? 374  PHE B CG  1 
ATOM   6694 C  CD1 . PHE B 1 374 ? -15.989 -10.054 67.099  1.00 32.59  ? 374  PHE B CD1 1 
ATOM   6695 C  CD2 . PHE B 1 374 ? -17.595 -8.395  66.452  1.00 31.15  ? 374  PHE B CD2 1 
ATOM   6696 C  CE1 . PHE B 1 374 ? -15.033 -9.431  66.339  1.00 30.53  ? 374  PHE B CE1 1 
ATOM   6697 C  CE2 . PHE B 1 374 ? -16.618 -7.765  65.683  1.00 30.22  ? 374  PHE B CE2 1 
ATOM   6698 C  CZ  . PHE B 1 374 ? -15.339 -8.286  65.636  1.00 33.80  ? 374  PHE B CZ  1 
ATOM   6699 N  N   . ARG B 1 375 ? -17.730 -7.720  70.585  1.00 31.89  ? 375  ARG B N   1 
ATOM   6700 C  CA  . ARG B 1 375 ? -17.995 -6.344  71.016  1.00 31.59  ? 375  ARG B CA  1 
ATOM   6701 C  C   . ARG B 1 375 ? -16.716 -5.526  70.899  1.00 33.39  ? 375  ARG B C   1 
ATOM   6702 O  O   . ARG B 1 375 ? -15.938 -5.425  71.858  1.00 34.00  ? 375  ARG B O   1 
ATOM   6703 C  CB  . ARG B 1 375 ? -18.535 -6.303  72.449  1.00 30.12  ? 375  ARG B CB  1 
ATOM   6704 C  CG  . ARG B 1 375 ? -19.862 -7.022  72.593  1.00 35.81  ? 375  ARG B CG  1 
ATOM   6705 C  CD  . ARG B 1 375 ? -20.423 -6.904  74.009  1.00 38.41  ? 375  ARG B CD  1 
ATOM   6706 N  NE  . ARG B 1 375 ? -21.762 -7.478  74.040  1.00 42.06  ? 375  ARG B NE  1 
ATOM   6707 C  CZ  . ARG B 1 375 ? -22.835 -6.869  73.556  1.00 47.37  ? 375  ARG B CZ  1 
ATOM   6708 N  NH1 . ARG B 1 375 ? -22.767 -5.644  73.047  1.00 40.20  ? 375  ARG B NH1 1 
ATOM   6709 N  NH2 . ARG B 1 375 ? -24.005 -7.504  73.576  1.00 44.76  ? 375  ARG B NH2 1 
ATOM   6710 N  N   . PRO B 1 376 ? -16.466 -4.919  69.738  1.00 31.92  ? 376  PRO B N   1 
ATOM   6711 C  CA  . PRO B 1 376 ? -15.245 -4.109  69.597  1.00 31.16  ? 376  PRO B CA  1 
ATOM   6712 C  C   . PRO B 1 376 ? -15.163 -2.957  70.593  1.00 31.83  ? 376  PRO B C   1 
ATOM   6713 O  O   . PRO B 1 376 ? -14.061 -2.465  70.872  1.00 33.12  ? 376  PRO B O   1 
ATOM   6714 C  CB  . PRO B 1 376 ? -15.332 -3.597  68.154  1.00 28.67  ? 376  PRO B CB  1 
ATOM   6715 C  CG  . PRO B 1 376 ? -16.206 -4.632  67.438  1.00 34.11  ? 376  PRO B CG  1 
ATOM   6716 C  CD  . PRO B 1 376 ? -17.241 -4.975  68.480  1.00 30.89  ? 376  PRO B CD  1 
ATOM   6717 N  N   . GLU B 1 377 ? -16.294 -2.515  71.142  1.00 34.82  ? 377  GLU B N   1 
ATOM   6718 C  CA  . GLU B 1 377 ? -16.270 -1.463  72.149  1.00 35.57  ? 377  GLU B CA  1 
ATOM   6719 C  C   . GLU B 1 377 ? -15.397 -1.807  73.354  1.00 37.13  ? 377  GLU B C   1 
ATOM   6720 O  O   . GLU B 1 377 ? -15.005 -0.891  74.088  1.00 37.32  ? 377  GLU B O   1 
ATOM   6721 C  CB  . GLU B 1 377 ? -17.703 -1.167  72.594  1.00 35.40  ? 377  GLU B CB  1 
ATOM   6722 C  CG  . GLU B 1 377 ? -18.522 -0.501  71.486  1.00 34.56  ? 377  GLU B CG  1 
ATOM   6723 C  CD  . GLU B 1 377 ? -18.993 -1.475  70.397  1.00 33.41  ? 377  GLU B CD  1 
ATOM   6724 O  OE1 . GLU B 1 377 ? -18.998 -2.703  70.630  1.00 32.87  ? 377  GLU B OE1 1 
ATOM   6725 O  OE2 . GLU B 1 377 ? -19.412 -1.002  69.317  1.00 35.14  ? 377  GLU B OE2 1 
ATOM   6726 N  N   . ARG B 1 378 ? -15.103 -3.099  73.586  1.00 34.40  ? 378  ARG B N   1 
ATOM   6727 C  CA  . ARG B 1 378 ? -14.132 -3.486  74.613  1.00 35.98  ? 378  ARG B CA  1 
ATOM   6728 C  C   . ARG B 1 378 ? -12.824 -2.730  74.489  1.00 36.85  ? 378  ARG B C   1 
ATOM   6729 O  O   . ARG B 1 378 ? -12.129 -2.524  75.490  1.00 38.46  ? 378  ARG B O   1 
ATOM   6730 C  CB  . ARG B 1 378 ? -13.795 -4.977  74.528  1.00 37.70  ? 378  ARG B CB  1 
ATOM   6731 C  CG  . ARG B 1 378 ? -14.903 -5.890  74.870  1.00 37.34  ? 378  ARG B CG  1 
ATOM   6732 C  CD  . ARG B 1 378 ? -14.419 -7.301  74.634  1.00 31.77  ? 378  ARG B CD  1 
ATOM   6733 N  NE  . ARG B 1 378 ? -15.524 -8.147  74.236  1.00 33.06  ? 378  ARG B NE  1 
ATOM   6734 C  CZ  . ARG B 1 378 ? -16.389 -8.690  75.077  1.00 35.79  ? 378  ARG B CZ  1 
ATOM   6735 N  NH1 . ARG B 1 378 ? -16.280 -8.522  76.389  1.00 35.81  ? 378  ARG B NH1 1 
ATOM   6736 N  NH2 . ARG B 1 378 ? -17.378 -9.433  74.592  1.00 35.90  ? 378  ARG B NH2 1 
ATOM   6737 N  N   . PHE B 1 379 ? -12.432 -2.380  73.266  1.00 32.82  ? 379  PHE B N   1 
ATOM   6738 C  CA  . PHE B 1 379 ? -11.117 -1.823  72.997  1.00 35.14  ? 379  PHE B CA  1 
ATOM   6739 C  C   . PHE B 1 379 ? -11.155 -0.310  72.830  1.00 40.35  ? 379  PHE B C   1 
ATOM   6740 O  O   . PHE B 1 379 ? -10.145 0.291   72.438  1.00 41.59  ? 379  PHE B O   1 
ATOM   6741 C  CB  . PHE B 1 379 ? -10.510 -2.510  71.761  1.00 36.65  ? 379  PHE B CB  1 
ATOM   6742 C  CG  . PHE B 1 379 ? -10.094 -3.939  72.017  1.00 35.09  ? 379  PHE B CG  1 
ATOM   6743 C  CD1 . PHE B 1 379 ? -8.836  -4.230  72.536  1.00 34.95  ? 379  PHE B CD1 1 
ATOM   6744 C  CD2 . PHE B 1 379 ? -10.973 -4.986  71.783  1.00 32.31  ? 379  PHE B CD2 1 
ATOM   6745 C  CE1 . PHE B 1 379 ? -8.451  -5.537  72.803  1.00 34.51  ? 379  PHE B CE1 1 
ATOM   6746 C  CE2 . PHE B 1 379 ? -10.597 -6.303  72.037  1.00 32.62  ? 379  PHE B CE2 1 
ATOM   6747 C  CZ  . PHE B 1 379 ? -9.322  -6.582  72.554  1.00 31.29  ? 379  PHE B CZ  1 
ATOM   6748 N  N   . GLU B 1 380 ? -12.292 0.321   73.136  1.00 40.02  ? 380  GLU B N   1 
ATOM   6749 C  CA  . GLU B 1 380 ? -12.392 1.771   72.976  1.00 39.50  ? 380  GLU B CA  1 
ATOM   6750 C  C   . GLU B 1 380 ? -11.332 2.499   73.775  1.00 47.06  ? 380  GLU B C   1 
ATOM   6751 O  O   . GLU B 1 380 ? -10.728 3.458   73.283  1.00 47.18  ? 380  GLU B O   1 
ATOM   6752 C  CB  . GLU B 1 380 ? -13.784 2.258   73.369  1.00 42.89  ? 380  GLU B CB  1 
ATOM   6753 C  CG  . GLU B 1 380 ? -14.601 2.721   72.188  1.00 54.07  ? 380  GLU B CG  1 
ATOM   6754 C  CD  . GLU B 1 380 ? -16.101 2.565   72.369  1.00 53.40  ? 380  GLU B CD  1 
ATOM   6755 O  OE1 . GLU B 1 380 ? -16.578 2.675   73.524  1.00 52.02  ? 380  GLU B OE1 1 
ATOM   6756 O  OE2 . GLU B 1 380 ? -16.792 2.415   71.324  1.00 52.96  ? 380  GLU B OE2 1 
ATOM   6757 N  N   . ASN B 1 381 ? -11.082 2.041   74.998  1.00 47.57  ? 381  ASN B N   1 
ATOM   6758 C  CA  . ASN B 1 381 ? -10.126 2.636   75.924  1.00 50.22  ? 381  ASN B CA  1 
ATOM   6759 C  C   . ASN B 1 381 ? -8.976  1.661   76.134  1.00 44.72  ? 381  ASN B C   1 
ATOM   6760 O  O   . ASN B 1 381 ? -9.048  0.783   77.002  1.00 47.03  ? 381  ASN B O   1 
ATOM   6761 C  CB  . ASN B 1 381 ? -10.811 2.972   77.250  1.00 50.21  ? 381  ASN B CB  1 
ATOM   6762 C  CG  . ASN B 1 381 ? -9.901  3.711   78.204  1.00 57.27  ? 381  ASN B CG  1 
ATOM   6763 O  OD1 . ASN B 1 381 ? -8.730  3.963   77.895  1.00 50.05  ? 381  ASN B OD1 1 
ATOM   6764 N  ND2 . ASN B 1 381 ? -10.428 4.048   79.381  1.00 52.17  ? 381  ASN B ND2 1 
ATOM   6765 N  N   . PRO B 1 382 ? -7.889  1.778   75.374  1.00 51.14  ? 382  PRO B N   1 
ATOM   6766 C  CA  . PRO B 1 382 ? -6.814  0.778   75.473  1.00 51.02  ? 382  PRO B CA  1 
ATOM   6767 C  C   . PRO B 1 382 ? -6.206  0.674   76.864  1.00 53.79  ? 382  PRO B C   1 
ATOM   6768 O  O   . PRO B 1 382 ? -5.630  -0.375  77.192  1.00 49.98  ? 382  PRO B O   1 
ATOM   6769 C  CB  . PRO B 1 382 ? -5.786  1.264   74.441  1.00 54.87  ? 382  PRO B CB  1 
ATOM   6770 C  CG  . PRO B 1 382 ? -6.053  2.738   74.319  1.00 53.95  ? 382  PRO B CG  1 
ATOM   6771 C  CD  . PRO B 1 382 ? -7.532  2.909   74.499  1.00 54.68  ? 382  PRO B CD  1 
ATOM   6772 N  N   . SER B 1 383 ? -6.329  1.723   77.689  1.00 52.58  ? 383  SER B N   1 
ATOM   6773 C  CA  . SER B 1 383 ? -5.792  1.696   79.049  1.00 55.72  ? 383  SER B CA  1 
ATOM   6774 C  C   . SER B 1 383 ? -6.552  0.728   79.940  1.00 54.17  ? 383  SER B C   1 
ATOM   6775 O  O   . SER B 1 383 ? -5.992  0.214   80.914  1.00 55.71  ? 383  SER B O   1 
ATOM   6776 C  CB  . SER B 1 383 ? -5.836  3.093   79.672  1.00 48.88  ? 383  SER B CB  1 
ATOM   6777 O  OG  . SER B 1 383 ? -4.987  3.988   78.992  1.00 56.69  ? 383  SER B OG  1 
ATOM   6778 N  N   . ALA B 1 384 ? -7.822  0.480   79.631  1.00 53.44  ? 384  ALA B N   1 
ATOM   6779 C  CA  . ALA B 1 384 ? -8.640  -0.409  80.439  1.00 54.79  ? 384  ALA B CA  1 
ATOM   6780 C  C   . ALA B 1 384 ? -8.158  -1.858  80.398  1.00 53.87  ? 384  ALA B C   1 
ATOM   6781 O  O   . ALA B 1 384 ? -8.484  -2.627  81.307  1.00 53.55  ? 384  ALA B O   1 
ATOM   6782 C  CB  . ALA B 1 384 ? -10.097 -0.320  79.978  1.00 56.59  ? 384  ALA B CB  1 
ATOM   6783 N  N   . ILE B 1 385 ? -7.395  -2.246  79.381  1.00 47.28  ? 385  ILE B N   1 
ATOM   6784 C  CA  . ILE B 1 385 ? -6.966  -3.635  79.203  1.00 50.11  ? 385  ILE B CA  1 
ATOM   6785 C  C   . ILE B 1 385 ? -5.806  -3.935  80.147  1.00 49.22  ? 385  ILE B C   1 
ATOM   6786 O  O   . ILE B 1 385 ? -4.729  -3.340  80.006  1.00 48.20  ? 385  ILE B O   1 
ATOM   6787 C  CB  . ILE B 1 385 ? -6.545  -3.917  77.749  1.00 47.20  ? 385  ILE B CB  1 
ATOM   6788 C  CG1 . ILE B 1 385 ? -7.529  -3.310  76.736  1.00 53.84  ? 385  ILE B CG1 1 
ATOM   6789 C  CG2 . ILE B 1 385 ? -6.377  -5.417  77.522  1.00 46.89  ? 385  ILE B CG2 1 
ATOM   6790 C  CD1 . ILE B 1 385 ? -8.828  -4.077  76.563  1.00 45.81  ? 385  ILE B CD1 1 
ATOM   6791 N  N   . PRO B 1 386 ? -5.966  -4.847  81.106  1.00 47.30  ? 386  PRO B N   1 
ATOM   6792 C  CA  . PRO B 1 386 ? -4.858  -5.167  82.018  1.00 43.45  ? 386  PRO B CA  1 
ATOM   6793 C  C   . PRO B 1 386 ? -3.663  -5.762  81.286  1.00 48.47  ? 386  PRO B C   1 
ATOM   6794 O  O   . PRO B 1 386 ? -3.802  -6.385  80.237  1.00 44.45  ? 386  PRO B O   1 
ATOM   6795 C  CB  . PRO B 1 386 ? -5.479  -6.187  82.981  1.00 44.82  ? 386  PRO B CB  1 
ATOM   6796 C  CG  . PRO B 1 386 ? -6.950  -5.932  82.904  1.00 44.26  ? 386  PRO B CG  1 
ATOM   6797 C  CD  . PRO B 1 386 ? -7.223  -5.507  81.494  1.00 44.98  ? 386  PRO B CD  1 
ATOM   6798 N  N   . GLN B 1 387 ? -2.473  -5.569  81.868  1.00 45.78  ? 387  GLN B N   1 
ATOM   6799 C  CA  . GLN B 1 387 ? -1.243  -6.151  81.342  1.00 47.28  ? 387  GLN B CA  1 
ATOM   6800 C  C   . GLN B 1 387 ? -1.362  -7.663  81.195  1.00 42.88  ? 387  GLN B C   1 
ATOM   6801 O  O   . GLN B 1 387 ? -1.823  -8.354  82.107  1.00 45.20  ? 387  GLN B O   1 
ATOM   6802 C  CB  . GLN B 1 387 ? -0.071  -5.838  82.279  1.00 52.52  ? 387  GLN B CB  1 
ATOM   6803 C  CG  . GLN B 1 387 ? 1.271   -6.406  81.822  1.00 56.98  ? 387  GLN B CG  1 
ATOM   6804 C  CD  . GLN B 1 387 ? 2.447   -5.839  82.616  1.00 62.04  ? 387  GLN B CD  1 
ATOM   6805 O  OE1 . GLN B 1 387 ? 3.604   -5.968  82.219  1.00 63.37  ? 387  GLN B OE1 1 
ATOM   6806 N  NE2 . GLN B 1 387 ? 2.146   -5.226  83.756  1.00 64.70  ? 387  GLN B NE2 1 
ATOM   6807 N  N   . HIS B 1 388 ? -0.890  -8.178  80.057  1.00 40.59  ? 388  HIS B N   1 
ATOM   6808 C  CA  . HIS B 1 388 ? -0.846  -9.609  79.743  1.00 40.50  ? 388  HIS B CA  1 
ATOM   6809 C  C   . HIS B 1 388 ? -2.229  -10.253 79.684  1.00 38.59  ? 388  HIS B C   1 
ATOM   6810 O  O   . HIS B 1 388 ? -2.336  -11.479 79.733  1.00 40.84  ? 388  HIS B O   1 
ATOM   6811 C  CB  . HIS B 1 388 ? 0.049   -10.378 80.723  1.00 44.53  ? 388  HIS B CB  1 
ATOM   6812 C  CG  . HIS B 1 388 ? 1.449   -9.852  80.794  1.00 44.44  ? 388  HIS B CG  1 
ATOM   6813 N  ND1 . HIS B 1 388 ? 2.173   -9.526  79.667  1.00 42.34  ? 388  HIS B ND1 1 
ATOM   6814 C  CD2 . HIS B 1 388 ? 2.256   -9.591  81.849  1.00 47.83  ? 388  HIS B CD2 1 
ATOM   6815 C  CE1 . HIS B 1 388 ? 3.368   -9.088  80.026  1.00 49.13  ? 388  HIS B CE1 1 
ATOM   6816 N  NE2 . HIS B 1 388 ? 3.445   -9.120  81.345  1.00 44.74  ? 388  HIS B NE2 1 
ATOM   6817 N  N   . ALA B 1 389 ? -3.293  -9.457  79.545  1.00 36.78  ? 389  ALA B N   1 
ATOM   6818 C  CA  . ALA B 1 389 ? -4.628  -10.000 79.308  1.00 37.62  ? 389  ALA B CA  1 
ATOM   6819 C  C   . ALA B 1 389 ? -4.917  -10.279 77.837  1.00 34.45  ? 389  ALA B C   1 
ATOM   6820 O  O   . ALA B 1 389 ? -5.801  -11.084 77.537  1.00 35.05  ? 389  ALA B O   1 
ATOM   6821 C  CB  . ALA B 1 389 ? -5.691  -9.037  79.820  1.00 37.16  ? 389  ALA B CB  1 
ATOM   6822 N  N   . PHE B 1 390 ? -4.210  -9.616  76.927  1.00 33.15  ? 390  PHE B N   1 
ATOM   6823 C  CA  . PHE B 1 390 ? -4.498  -9.655  75.495  1.00 34.48  ? 390  PHE B CA  1 
ATOM   6824 C  C   . PHE B 1 390 ? -3.163  -9.879  74.804  1.00 32.40  ? 390  PHE B C   1 
ATOM   6825 O  O   . PHE B 1 390 ? -2.317  -8.977  74.778  1.00 34.17  ? 390  PHE B O   1 
ATOM   6826 C  CB  . PHE B 1 390 ? -5.167  -8.345  75.059  1.00 31.64  ? 390  PHE B CB  1 
ATOM   6827 C  CG  . PHE B 1 390 ? -5.511  -8.265  73.587  1.00 33.15  ? 390  PHE B CG  1 
ATOM   6828 C  CD1 . PHE B 1 390 ? -6.483  -9.091  73.038  1.00 31.53  ? 390  PHE B CD1 1 
ATOM   6829 C  CD2 . PHE B 1 390 ? -4.889  -7.330  72.768  1.00 32.75  ? 390  PHE B CD2 1 
ATOM   6830 C  CE1 . PHE B 1 390 ? -6.814  -8.999  71.686  1.00 29.42  ? 390  PHE B CE1 1 
ATOM   6831 C  CE2 . PHE B 1 390 ? -5.214  -7.218  71.414  1.00 32.41  ? 390  PHE B CE2 1 
ATOM   6832 C  CZ  . PHE B 1 390 ? -6.175  -8.048  70.869  1.00 33.90  ? 390  PHE B CZ  1 
ATOM   6833 N  N   . LYS B 1 391 ? -2.944  -11.089 74.299  1.00 32.41  ? 391  LYS B N   1 
ATOM   6834 C  CA  . LYS B 1 391 ? -1.613  -11.441 73.825  1.00 30.49  ? 391  LYS B CA  1 
ATOM   6835 C  C   . LYS B 1 391 ? -1.603  -12.112 72.454  1.00 29.99  ? 391  LYS B C   1 
ATOM   6836 O  O   . LYS B 1 391 ? -0.884  -13.104 72.271  1.00 31.98  ? 391  LYS B O   1 
ATOM   6837 C  CB  . LYS B 1 391 ? -0.933  -12.362 74.842  1.00 31.59  ? 391  LYS B CB  1 
ATOM   6838 C  CG  . LYS B 1 391 ? -0.840  -11.750 76.227  1.00 34.83  ? 391  LYS B CG  1 
ATOM   6839 C  CD  . LYS B 1 391 ? 0.131   -10.607 76.239  1.00 41.26  ? 391  LYS B CD  1 
ATOM   6840 C  CE  . LYS B 1 391 ? 1.546   -11.128 76.416  1.00 39.61  ? 391  LYS B CE  1 
ATOM   6841 N  NZ  . LYS B 1 391 ? 2.467   -9.999  76.710  1.00 42.29  ? 391  LYS B NZ  1 
ATOM   6842 N  N   . PRO B 1 392 ? -2.362  -11.614 71.469  1.00 31.45  ? 392  PRO B N   1 
ATOM   6843 C  CA  . PRO B 1 392 ? -2.345  -12.250 70.143  1.00 29.17  ? 392  PRO B CA  1 
ATOM   6844 C  C   . PRO B 1 392 ? -1.007  -12.130 69.446  1.00 31.46  ? 392  PRO B C   1 
ATOM   6845 O  O   . PRO B 1 392 ? -0.809  -12.802 68.436  1.00 30.21  ? 392  PRO B O   1 
ATOM   6846 C  CB  . PRO B 1 392 ? -3.422  -11.486 69.361  1.00 33.92  ? 392  PRO B CB  1 
ATOM   6847 C  CG  . PRO B 1 392 ? -3.365  -10.101 69.953  1.00 32.20  ? 392  PRO B CG  1 
ATOM   6848 C  CD  . PRO B 1 392 ? -3.105  -10.335 71.455  1.00 29.78  ? 392  PRO B CD  1 
ATOM   6849 N  N   . HIS B 1 393 ? -0.112  -11.273 69.929  1.00 30.15  ? 393  HIS B N   1 
ATOM   6850 C  CA  . HIS B 1 393 ? 1.185   -11.058 69.294  1.00 34.16  ? 393  HIS B CA  1 
ATOM   6851 C  C   . HIS B 1 393 ? 2.333   -11.615 70.130  1.00 32.69  ? 393  HIS B C   1 
ATOM   6852 O  O   . HIS B 1 393 ? 3.488   -11.222 69.931  1.00 33.70  ? 393  HIS B O   1 
ATOM   6853 C  CB  . HIS B 1 393 ? 1.393   -9.569  69.032  1.00 34.11  ? 393  HIS B CB  1 
ATOM   6854 C  CG  . HIS B 1 393 ? 0.335   -8.968  68.155  1.00 40.92  ? 393  HIS B CG  1 
ATOM   6855 N  ND1 . HIS B 1 393 ? 0.107   -9.391  66.866  1.00 43.57  ? 393  HIS B ND1 1 
ATOM   6856 C  CD2 . HIS B 1 393 ? -0.590  -8.014  68.408  1.00 47.73  ? 393  HIS B CD2 1 
ATOM   6857 C  CE1 . HIS B 1 393 ? -0.901  -8.706  66.353  1.00 46.64  ? 393  HIS B CE1 1 
ATOM   6858 N  NE2 . HIS B 1 393 ? -1.340  -7.864  67.269  1.00 48.20  ? 393  HIS B NE2 1 
ATOM   6859 N  N   . GLY B 1 394 ? 2.046   -12.508 71.075  1.00 31.87  ? 394  GLY B N   1 
ATOM   6860 C  CA  . GLY B 1 394 ? 3.139   -13.065 71.852  1.00 32.97  ? 394  GLY B CA  1 
ATOM   6861 C  C   . GLY B 1 394 ? 3.607   -12.116 72.947  1.00 34.02  ? 394  GLY B C   1 
ATOM   6862 O  O   . GLY B 1 394 ? 2.868   -11.238 73.415  1.00 32.11  ? 394  GLY B O   1 
ATOM   6863 N  N   . ASN B 1 395 ? 4.863   -12.309 73.377  1.00 32.22  ? 395  ASN B N   1 
ATOM   6864 C  CA  . ASN B 1 395 ? 5.303   -11.661 74.602  1.00 32.57  ? 395  ASN B CA  1 
ATOM   6865 C  C   . ASN B 1 395 ? 6.756   -11.209 74.533  1.00 35.51  ? 395  ASN B C   1 
ATOM   6866 O  O   . ASN B 1 395 ? 7.628   -11.935 74.040  1.00 31.80  ? 395  ASN B O   1 
ATOM   6867 C  CB  . ASN B 1 395 ? 5.155   -12.576 75.818  1.00 31.90  ? 395  ASN B CB  1 
ATOM   6868 C  CG  . ASN B 1 395 ? 5.571   -11.887 77.095  1.00 36.69  ? 395  ASN B CG  1 
ATOM   6869 O  OD1 . ASN B 1 395 ? 4.894   -10.968 77.564  1.00 35.66  ? 395  ASN B OD1 1 
ATOM   6870 N  ND2 . ASN B 1 395 ? 6.693   -12.316 77.665  1.00 35.05  ? 395  ASN B ND2 1 
ATOM   6871 N  N   . GLY B 1 396 ? 7.001   -10.016 75.077  1.00 30.79  ? 396  GLY B N   1 
ATOM   6872 C  CA  . GLY B 1 396 ? 8.331   -9.524  75.422  1.00 32.26  ? 396  GLY B CA  1 
ATOM   6873 C  C   . GLY B 1 396 ? 9.221   -9.357  74.206  1.00 30.90  ? 396  GLY B C   1 
ATOM   6874 O  O   . GLY B 1 396 ? 8.773   -8.980  73.117  1.00 31.65  ? 396  GLY B O   1 
ATOM   6875 N  N   . GLN B 1 397 ? 10.518  -9.623  74.400  1.00 31.53  ? 397  GLN B N   1 
ATOM   6876 C  CA  . GLN B 1 397 ? 11.463  -9.483  73.298  1.00 30.60  ? 397  GLN B CA  1 
ATOM   6877 C  C   . GLN B 1 397 ? 11.219  -10.499 72.191  1.00 30.82  ? 397  GLN B C   1 
ATOM   6878 O  O   . GLN B 1 397 ? 11.706  -10.298 71.074  1.00 32.85  ? 397  GLN B O   1 
ATOM   6879 C  CB  . GLN B 1 397 ? 12.908  -9.613  73.803  1.00 33.84  ? 397  GLN B CB  1 
ATOM   6880 C  CG  . GLN B 1 397 ? 13.336  -11.010 74.242  1.00 32.30  ? 397  GLN B CG  1 
ATOM   6881 C  CD  . GLN B 1 397 ? 14.784  -11.028 74.757  1.00 37.63  ? 397  GLN B CD  1 
ATOM   6882 O  OE1 . GLN B 1 397 ? 15.589  -10.174 74.402  1.00 37.24  ? 397  GLN B OE1 1 
ATOM   6883 N  NE2 . GLN B 1 397 ? 15.114  -12.020 75.566  1.00 35.33  ? 397  GLN B NE2 1 
ATOM   6884 N  N   . ARG B 1 398 ? 10.497  -11.585 72.474  1.00 30.88  ? 398  ARG B N   1 
ATOM   6885 C  CA  . ARG B 1 398 ? 10.127  -12.553 71.451  1.00 30.75  ? 398  ARG B CA  1 
ATOM   6886 C  C   . ARG B 1 398 ? 8.713   -12.313 70.929  1.00 29.06  ? 398  ARG B C   1 
ATOM   6887 O  O   . ARG B 1 398 ? 8.096   -13.232 70.391  1.00 30.73  ? 398  ARG B O   1 
ATOM   6888 C  CB  . ARG B 1 398 ? 10.256  -13.982 71.986  1.00 31.13  ? 398  ARG B CB  1 
ATOM   6889 C  CG  . ARG B 1 398 ? 11.685  -14.382 72.446  1.00 30.06  ? 398  ARG B CG  1 
ATOM   6890 C  CD  . ARG B 1 398 ? 12.739  -14.157 71.346  1.00 30.20  ? 398  ARG B CD  1 
ATOM   6891 N  NE  . ARG B 1 398 ? 12.422  -14.823 70.090  1.00 29.98  ? 398  ARG B NE  1 
ATOM   6892 C  CZ  . ARG B 1 398 ? 12.816  -16.046 69.761  1.00 31.82  ? 398  ARG B CZ  1 
ATOM   6893 N  NH1 . ARG B 1 398 ? 13.510  -16.797 70.602  1.00 31.13  ? 398  ARG B NH1 1 
ATOM   6894 N  NH2 . ARG B 1 398 ? 12.522  -16.518 68.550  1.00 30.32  ? 398  ARG B NH2 1 
ATOM   6895 N  N   . ALA B 1 399 ? 8.194   -11.099 71.095  1.00 33.04  ? 399  ALA B N   1 
ATOM   6896 C  CA  . ALA B 1 399 ? 6.884   -10.752 70.561  1.00 32.25  ? 399  ALA B CA  1 
ATOM   6897 C  C   . ALA B 1 399 ? 6.948   -10.619 69.044  1.00 30.01  ? 399  ALA B C   1 
ATOM   6898 O  O   . ALA B 1 399 ? 8.024   -10.517 68.446  1.00 31.71  ? 399  ALA B O   1 
ATOM   6899 C  CB  . ALA B 1 399 ? 6.395   -9.444  71.173  1.00 31.61  ? 399  ALA B CB  1 
ATOM   6900 N  N   . CYS B 1 400 ? 5.776   -10.610 68.421  1.00 31.19  ? 400  CYS B N   1 
ATOM   6901 C  CA  . CYS B 1 400 ? 5.674   -10.484 66.970  1.00 29.85  ? 400  CYS B CA  1 
ATOM   6902 C  C   . CYS B 1 400 ? 6.375   -9.227  66.461  1.00 31.93  ? 400  CYS B C   1 
ATOM   6903 O  O   . CYS B 1 400 ? 6.032   -8.105  66.845  1.00 31.61  ? 400  CYS B O   1 
ATOM   6904 C  CB  . CYS B 1 400 ? 4.195   -10.463 66.575  1.00 30.21  ? 400  CYS B CB  1 
ATOM   6905 S  SG  . CYS B 1 400 ? 3.991   -10.215 64.808  1.00 31.17  ? 400  CYS B SG  1 
ATOM   6906 N  N   . ILE B 1 401 ? 7.349   -9.410  65.574  1.00 29.67  ? 401  ILE B N   1 
ATOM   6907 C  CA  . ILE B 1 401 ? 8.048   -8.263  65.005  1.00 31.86  ? 401  ILE B CA  1 
ATOM   6908 C  C   . ILE B 1 401 ? 7.206   -7.547  63.964  1.00 32.99  ? 401  ILE B C   1 
ATOM   6909 O  O   . ILE B 1 401 ? 7.461   -6.372  63.676  1.00 35.19  ? 401  ILE B O   1 
ATOM   6910 C  CB  . ILE B 1 401 ? 9.395   -8.687  64.392  1.00 28.95  ? 401  ILE B CB  1 
ATOM   6911 C  CG1 . ILE B 1 401 ? 10.322  -7.477  64.226  1.00 30.31  ? 401  ILE B CG1 1 
ATOM   6912 C  CG2 . ILE B 1 401 ? 9.195   -9.377  63.039  1.00 31.61  ? 401  ILE B CG2 1 
ATOM   6913 C  CD1 . ILE B 1 401 ? 11.773  -7.858  63.756  1.00 31.87  ? 401  ILE B CD1 1 
ATOM   6914 N  N   . GLY B 1 402 ? 6.219   -8.225  63.381  1.00 33.06  ? 402  GLY B N   1 
ATOM   6915 C  CA  . GLY B 1 402 ? 5.452   -7.657  62.281  1.00 33.16  ? 402  GLY B CA  1 
ATOM   6916 C  C   . GLY B 1 402 ? 4.076   -7.156  62.674  1.00 32.89  ? 402  GLY B C   1 
ATOM   6917 O  O   . GLY B 1 402 ? 3.214   -6.962  61.812  1.00 32.14  ? 402  GLY B O   1 
ATOM   6918 N  N   . GLN B 1 403 ? 3.869   -6.924  63.975  1.00 31.04  ? 403  GLN B N   1 
ATOM   6919 C  CA  . GLN B 1 403 ? 2.536   -6.597  64.472  1.00 31.35  ? 403  GLN B CA  1 
ATOM   6920 C  C   . GLN B 1 403 ? 1.990   -5.329  63.825  1.00 34.83  ? 403  GLN B C   1 
ATOM   6921 O  O   . GLN B 1 403 ? 0.807   -5.271  63.457  1.00 33.92  ? 403  GLN B O   1 
ATOM   6922 C  CB  . GLN B 1 403 ? 2.576   -6.456  65.999  1.00 34.92  ? 403  GLN B CB  1 
ATOM   6923 C  CG  . GLN B 1 403 ? 1.272   -5.941  66.615  1.00 42.10  ? 403  GLN B CG  1 
ATOM   6924 C  CD  . GLN B 1 403 ? 1.461   -5.496  68.061  1.00 52.05  ? 403  GLN B CD  1 
ATOM   6925 O  OE1 . GLN B 1 403 ? 2.365   -5.977  68.750  1.00 41.70  ? 403  GLN B OE1 1 
ATOM   6926 N  NE2 . GLN B 1 403 ? 0.616   -4.562  68.521  1.00 53.75  ? 403  GLN B NE2 1 
ATOM   6927 N  N   . GLN B 1 404 ? 2.824   -4.288  63.710  1.00 33.54  ? 404  GLN B N   1 
ATOM   6928 C  CA  . GLN B 1 404 ? 2.371   -3.044  63.088  1.00 37.30  ? 404  GLN B CA  1 
ATOM   6929 C  C   . GLN B 1 404 ? 2.085   -3.241  61.609  1.00 32.07  ? 404  GLN B C   1 
ATOM   6930 O  O   . GLN B 1 404 ? 1.115   -2.678  61.077  1.00 35.32  ? 404  GLN B O   1 
ATOM   6931 C  CB  . GLN B 1 404 ? 3.415   -1.937  63.280  1.00 40.18  ? 404  GLN B CB  1 
ATOM   6932 C  CG  . GLN B 1 404 ? 3.635   -1.564  64.723  1.00 44.09  ? 404  GLN B CG  1 
ATOM   6933 C  CD  . GLN B 1 404 ? 2.345   -1.123  65.380  1.00 56.25  ? 404  GLN B CD  1 
ATOM   6934 O  OE1 . GLN B 1 404 ? 1.551   -1.951  65.844  1.00 62.87  ? 404  GLN B OE1 1 
ATOM   6935 N  NE2 . GLN B 1 404 ? 2.117   0.191   65.413  1.00 64.95  ? 404  GLN B NE2 1 
ATOM   6936 N  N   . PHE B 1 405 ? 2.920   -4.038  60.934  1.00 30.93  ? 405  PHE B N   1 
ATOM   6937 C  CA  . PHE B 1 405 ? 2.696   -4.358  59.525  1.00 32.16  ? 405  PHE B CA  1 
ATOM   6938 C  C   . PHE B 1 405 ? 1.344   -5.031  59.342  1.00 31.02  ? 405  PHE B C   1 
ATOM   6939 O  O   . PHE B 1 405 ? 0.522   -4.603  58.518  1.00 31.91  ? 405  PHE B O   1 
ATOM   6940 C  CB  . PHE B 1 405 ? 3.837   -5.260  59.016  1.00 31.08  ? 405  PHE B CB  1 
ATOM   6941 C  CG  . PHE B 1 405 ? 3.846   -5.479  57.512  1.00 32.57  ? 405  PHE B CG  1 
ATOM   6942 C  CD1 . PHE B 1 405 ? 3.025   -6.434  56.930  1.00 32.36  ? 405  PHE B CD1 1 
ATOM   6943 C  CD2 . PHE B 1 405 ? 4.693   -4.752  56.689  1.00 30.80  ? 405  PHE B CD2 1 
ATOM   6944 C  CE1 . PHE B 1 405 ? 3.034   -6.643  55.526  1.00 33.61  ? 405  PHE B CE1 1 
ATOM   6945 C  CE2 . PHE B 1 405 ? 4.715   -4.949  55.306  1.00 33.56  ? 405  PHE B CE2 1 
ATOM   6946 C  CZ  . PHE B 1 405 ? 3.888   -5.885  54.721  1.00 33.56  ? 405  PHE B CZ  1 
ATOM   6947 N  N   . ALA B 1 406 ? 1.106   -6.103  60.094  1.00 29.94  ? 406  ALA B N   1 
ATOM   6948 C  CA  . ALA B 1 406 ? -0.155  -6.830  60.000  1.00 31.66  ? 406  ALA B CA  1 
ATOM   6949 C  C   . ALA B 1 406 ? -1.344  -5.908  60.230  1.00 34.48  ? 406  ALA B C   1 
ATOM   6950 O  O   . ALA B 1 406 ? -2.310  -5.918  59.459  1.00 31.62  ? 406  ALA B O   1 
ATOM   6951 C  CB  . ALA B 1 406 ? -0.175  -7.969  61.022  1.00 32.75  ? 406  ALA B CB  1 
ATOM   6952 N  N   . LEU B 1 407 ? -1.318  -5.133  61.320  1.00 31.10  ? 407  LEU B N   1 
ATOM   6953 C  CA  . LEU B 1 407 ? -2.501  -4.332  61.648  1.00 33.80  ? 407  LEU B CA  1 
ATOM   6954 C  C   . LEU B 1 407 ? -2.697  -3.171  60.667  1.00 34.41  ? 407  LEU B C   1 
ATOM   6955 O  O   . LEU B 1 407 ? -3.842  -2.805  60.354  1.00 32.88  ? 407  LEU B O   1 
ATOM   6956 C  CB  . LEU B 1 407 ? -2.408  -3.831  63.092  1.00 33.93  ? 407  LEU B CB  1 
ATOM   6957 C  CG  . LEU B 1 407 ? -2.611  -4.938  64.136  1.00 41.01  ? 407  LEU B CG  1 
ATOM   6958 C  CD1 . LEU B 1 407 ? -2.471  -4.362  65.553  1.00 42.38  ? 407  LEU B CD1 1 
ATOM   6959 C  CD2 . LEU B 1 407 ? -3.953  -5.640  63.941  1.00 42.13  ? 407  LEU B CD2 1 
ATOM   6960 N  N   . HIS B 1 408 ? -1.612  -2.584  60.155  1.00 32.59  ? 408  HIS B N   1 
ATOM   6961 C  CA  . HIS B 1 408 ? -1.786  -1.523  59.172  1.00 32.74  ? 408  HIS B CA  1 
ATOM   6962 C  C   . HIS B 1 408 ? -2.401  -2.074  57.890  1.00 32.52  ? 408  HIS B C   1 
ATOM   6963 O  O   . HIS B 1 408 ? -3.337  -1.489  57.332  1.00 32.63  ? 408  HIS B O   1 
ATOM   6964 C  CB  . HIS B 1 408 ? -0.451  -0.840  58.867  1.00 35.47  ? 408  HIS B CB  1 
ATOM   6965 C  CG  . HIS B 1 408 ? -0.597  0.392   58.024  1.00 36.51  ? 408  HIS B CG  1 
ATOM   6966 N  ND1 . HIS B 1 408 ? -1.005  1.599   58.543  1.00 33.71  ? 408  HIS B ND1 1 
ATOM   6967 C  CD2 . HIS B 1 408 ? -0.448  0.588   56.692  1.00 35.29  ? 408  HIS B CD2 1 
ATOM   6968 C  CE1 . HIS B 1 408 ? -1.074  2.496   57.574  1.00 38.70  ? 408  HIS B CE1 1 
ATOM   6969 N  NE2 . HIS B 1 408 ? -0.732  1.909   56.441  1.00 33.07  ? 408  HIS B NE2 1 
ATOM   6970 N  N   . GLU B 1 409 ? -1.877  -3.202  57.413  1.00 29.02  ? 409  GLU B N   1 
ATOM   6971 C  CA  . GLU B 1 409 ? -2.431  -3.847  56.231  1.00 28.64  ? 409  GLU B CA  1 
ATOM   6972 C  C   . GLU B 1 409 ? -3.904  -4.183  56.439  1.00 28.43  ? 409  GLU B C   1 
ATOM   6973 O  O   . GLU B 1 409 ? -4.757  -3.872  55.594  1.00 32.49  ? 409  GLU B O   1 
ATOM   6974 C  CB  . GLU B 1 409 ? -1.636  -5.113  55.912  1.00 31.86  ? 409  GLU B CB  1 
ATOM   6975 C  CG  . GLU B 1 409 ? -2.238  -5.909  54.759  1.00 30.63  ? 409  GLU B CG  1 
ATOM   6976 C  CD  . GLU B 1 409 ? -1.454  -7.165  54.446  1.00 31.12  ? 409  GLU B CD  1 
ATOM   6977 O  OE1 . GLU B 1 409 ? -0.535  -7.499  55.219  1.00 33.16  ? 409  GLU B OE1 1 
ATOM   6978 O  OE2 . GLU B 1 409 ? -1.734  -7.800  53.414  1.00 34.05  ? 409  GLU B OE2 1 
ATOM   6979 N  N   . ALA B 1 410 ? -4.213  -4.840  57.563  1.00 30.45  ? 410  ALA B N   1 
ATOM   6980 C  CA  . ALA B 1 410 ? -5.576  -5.326  57.779  1.00 32.62  ? 410  ALA B CA  1 
ATOM   6981 C  C   . ALA B 1 410 ? -6.558  -4.172  57.941  1.00 31.24  ? 410  ALA B C   1 
ATOM   6982 O  O   . ALA B 1 410 ? -7.717  -4.272  57.509  1.00 30.39  ? 410  ALA B O   1 
ATOM   6983 C  CB  . ALA B 1 410 ? -5.620  -6.249  59.004  1.00 30.56  ? 410  ALA B CB  1 
ATOM   6984 N  N   . THR B 1 411 ? -6.124  -3.082  58.580  1.00 31.31  ? 411  THR B N   1 
ATOM   6985 C  CA  . THR B 1 411 ? -6.992  -1.916  58.742  1.00 31.19  ? 411  THR B CA  1 
ATOM   6986 C  C   . THR B 1 411 ? -7.252  -1.241  57.405  1.00 29.91  ? 411  THR B C   1 
ATOM   6987 O  O   . THR B 1 411 ? -8.393  -0.886  57.087  1.00 31.82  ? 411  THR B O   1 
ATOM   6988 C  CB  . THR B 1 411 ? -6.362  -0.924  59.727  1.00 33.63  ? 411  THR B CB  1 
ATOM   6989 O  OG1 . THR B 1 411 ? -6.069  -1.600  60.955  1.00 32.82  ? 411  THR B OG1 1 
ATOM   6990 C  CG2 . THR B 1 411 ? -7.300  0.264   59.987  1.00 29.49  ? 411  THR B CG2 1 
ATOM   6991 N  N   . LEU B 1 412 ? -6.202  -1.077  56.604  1.00 31.29  ? 412  LEU B N   1 
ATOM   6992 C  CA  . LEU B 1 412 ? -6.367  -0.512  55.274  1.00 29.97  ? 412  LEU B CA  1 
ATOM   6993 C  C   . LEU B 1 412 ? -7.348  -1.341  54.469  1.00 31.40  ? 412  LEU B C   1 
ATOM   6994 O  O   . LEU B 1 412 ? -8.294  -0.810  53.881  1.00 32.50  ? 412  LEU B O   1 
ATOM   6995 C  CB  . LEU B 1 412 ? -5.014  -0.456  54.561  1.00 31.01  ? 412  LEU B CB  1 
ATOM   6996 C  CG  . LEU B 1 412 ? -5.136  -0.287  53.038  1.00 32.58  ? 412  LEU B CG  1 
ATOM   6997 C  CD1 . LEU B 1 412 ? -5.652  1.117   52.669  1.00 35.27  ? 412  LEU B CD1 1 
ATOM   6998 C  CD2 . LEU B 1 412 ? -3.797  -0.547  52.379  1.00 35.95  ? 412  LEU B CD2 1 
ATOM   6999 N  N   . VAL B 1 413 ? -7.131  -2.657  54.435  1.00 31.21  ? 413  VAL B N   1 
ATOM   7000 C  CA  . VAL B 1 413 ? -7.898  -3.521  53.548  1.00 30.52  ? 413  VAL B CA  1 
ATOM   7001 C  C   . VAL B 1 413 ? -9.339  -3.628  54.025  1.00 31.81  ? 413  VAL B C   1 
ATOM   7002 O  O   . VAL B 1 413 ? -10.279 -3.471  53.238  1.00 32.20  ? 413  VAL B O   1 
ATOM   7003 C  CB  . VAL B 1 413 ? -7.218  -4.898  53.447  1.00 34.40  ? 413  VAL B CB  1 
ATOM   7004 C  CG1 . VAL B 1 413 ? -8.102  -5.896  52.744  1.00 36.17  ? 413  VAL B CG1 1 
ATOM   7005 C  CG2 . VAL B 1 413 ? -5.882  -4.749  52.710  1.00 36.00  ? 413  VAL B CG2 1 
ATOM   7006 N  N   . LEU B 1 414 ? -9.535  -3.917  55.312  1.00 29.21  ? 414  LEU B N   1 
ATOM   7007 C  CA  . LEU B 1 414 ? -10.901 -3.974  55.833  1.00 29.68  ? 414  LEU B CA  1 
ATOM   7008 C  C   . LEU B 1 414 ? -11.600 -2.628  55.654  1.00 32.89  ? 414  LEU B C   1 
ATOM   7009 O  O   . LEU B 1 414 ? -12.790 -2.578  55.333  1.00 31.37  ? 414  LEU B O   1 
ATOM   7010 C  CB  . LEU B 1 414 ? -10.893 -4.402  57.301  1.00 28.73  ? 414  LEU B CB  1 
ATOM   7011 C  CG  . LEU B 1 414 ? -12.253 -4.673  57.960  1.00 31.64  ? 414  LEU B CG  1 
ATOM   7012 C  CD1 . LEU B 1 414 ? -13.076 -5.629  57.120  1.00 35.12  ? 414  LEU B CD1 1 
ATOM   7013 C  CD2 . LEU B 1 414 ? -12.042 -5.252  59.342  1.00 30.13  ? 414  LEU B CD2 1 
ATOM   7014 N  N   . GLY B 1 415 ? -10.865 -1.527  55.835  1.00 30.37  ? 415  GLY B N   1 
ATOM   7015 C  CA  . GLY B 1 415 ? -11.440 -0.213  55.569  1.00 34.45  ? 415  GLY B CA  1 
ATOM   7016 C  C   . GLY B 1 415 ? -11.930 -0.063  54.139  1.00 31.73  ? 415  GLY B C   1 
ATOM   7017 O  O   . GLY B 1 415 ? -13.062 0.374   53.899  1.00 30.35  ? 415  GLY B O   1 
ATOM   7018 N  N   . MET B 1 416 ? -11.091 -0.422  53.162  1.00 30.92  ? 416  MET B N   1 
ATOM   7019 C  CA  . MET B 1 416 ? -11.558 -0.293  51.778  1.00 31.00  ? 416  MET B CA  1 
ATOM   7020 C  C   . MET B 1 416 ? -12.692 -1.264  51.472  1.00 29.39  ? 416  MET B C   1 
ATOM   7021 O  O   . MET B 1 416 ? -13.606 -0.926  50.706  1.00 32.20  ? 416  MET B O   1 
ATOM   7022 C  CB  . MET B 1 416 ? -10.423 -0.457  50.756  1.00 33.00  ? 416  MET B CB  1 
ATOM   7023 C  CG  . MET B 1 416 ? -9.330  0.583   50.875  1.00 33.19  ? 416  MET B CG  1 
ATOM   7024 S  SD  . MET B 1 416 ? -7.911  0.221   49.797  1.00 36.97  ? 416  MET B SD  1 
ATOM   7025 C  CE  . MET B 1 416 ? -8.701  0.514   48.202  1.00 36.15  ? 416  MET B CE  1 
ATOM   7026 N  N   . MET B 1 417 ? -12.646 -2.480  52.031  1.00 31.10  ? 417  MET B N   1 
ATOM   7027 C  CA  . MET B 1 417 ? -13.742 -3.424  51.805  1.00 32.71  ? 417  MET B CA  1 
ATOM   7028 C  C   . MET B 1 417 ? -15.069 -2.829  52.252  1.00 35.77  ? 417  MET B C   1 
ATOM   7029 O  O   . MET B 1 417 ? -16.066 -2.861  51.515  1.00 31.26  ? 417  MET B O   1 
ATOM   7030 C  CB  . MET B 1 417 ? -13.488 -4.754  52.527  1.00 30.08  ? 417  MET B CB  1 
ATOM   7031 C  CG  . MET B 1 417 ? -12.311 -5.549  51.945  1.00 32.08  ? 417  MET B CG  1 
ATOM   7032 S  SD  . MET B 1 417 ? -11.751 -6.885  53.018  1.00 33.51  ? 417  MET B SD  1 
ATOM   7033 C  CE  . MET B 1 417 ? -13.294 -7.679  53.471  1.00 35.61  ? 417  MET B CE  1 
ATOM   7034 N  N   . LEU B 1 418 ? -15.087 -2.245  53.447  1.00 33.21  ? 418  LEU B N   1 
ATOM   7035 C  CA  . LEU B 1 418 ? -16.322 -1.675  53.978  1.00 33.21  ? 418  LEU B CA  1 
ATOM   7036 C  C   . LEU B 1 418 ? -16.734 -0.402  53.246  1.00 33.70  ? 418  LEU B C   1 
ATOM   7037 O  O   . LEU B 1 418 ? -17.933 -0.092  53.178  1.00 32.36  ? 418  LEU B O   1 
ATOM   7038 C  CB  . LEU B 1 418 ? -16.151 -1.410  55.475  1.00 30.56  ? 418  LEU B CB  1 
ATOM   7039 C  CG  . LEU B 1 418 ? -15.978 -2.705  56.283  1.00 34.10  ? 418  LEU B CG  1 
ATOM   7040 C  CD1 . LEU B 1 418 ? -15.733 -2.440  57.782  1.00 35.31  ? 418  LEU B CD1 1 
ATOM   7041 C  CD2 . LEU B 1 418 ? -17.165 -3.638  56.108  1.00 35.85  ? 418  LEU B CD2 1 
ATOM   7042 N  N   . LYS B 1 419 ? -15.769 0.349   52.711  1.00 31.51  ? 419  LYS B N   1 
ATOM   7043 C  CA  . LYS B 1 419 ? -16.098 1.539   51.927  1.00 30.51  ? 419  LYS B CA  1 
ATOM   7044 C  C   . LYS B 1 419 ? -16.800 1.168   50.636  1.00 36.11  ? 419  LYS B C   1 
ATOM   7045 O  O   . LYS B 1 419 ? -17.755 1.837   50.227  1.00 34.59  ? 419  LYS B O   1 
ATOM   7046 C  CB  . LYS B 1 419 ? -14.834 2.336   51.592  1.00 31.98  ? 419  LYS B CB  1 
ATOM   7047 C  CG  . LYS B 1 419 ? -15.052 3.531   50.614  1.00 30.77  ? 419  LYS B CG  1 
ATOM   7048 C  CD  . LYS B 1 419 ? -13.694 4.181   50.235  1.00 33.25  ? 419  LYS B CD  1 
ATOM   7049 C  CE  . LYS B 1 419 ? -13.836 5.273   49.157  1.00 32.39  ? 419  LYS B CE  1 
ATOM   7050 N  NZ  . LYS B 1 419 ? -12.533 5.990   48.981  1.00 33.84  ? 419  LYS B NZ  1 
ATOM   7051 N  N   . HIS B 1 420 ? -16.320 0.121   49.968  1.00 32.68  ? 420  HIS B N   1 
ATOM   7052 C  CA  . HIS B 1 420 ? -16.698 -0.118  48.587  1.00 31.25  ? 420  HIS B CA  1 
ATOM   7053 C  C   . HIS B 1 420 ? -17.832 -1.118  48.407  1.00 33.15  ? 420  HIS B C   1 
ATOM   7054 O  O   . HIS B 1 420 ? -18.426 -1.151  47.315  1.00 35.47  ? 420  HIS B O   1 
ATOM   7055 C  CB  . HIS B 1 420 ? -15.462 -0.563  47.795  1.00 33.77  ? 420  HIS B CB  1 
ATOM   7056 C  CG  . HIS B 1 420 ? -14.525 0.564   47.496  1.00 34.14  ? 420  HIS B CG  1 
ATOM   7057 N  ND1 . HIS B 1 420 ? -14.741 1.453   46.460  1.00 34.14  ? 420  HIS B ND1 1 
ATOM   7058 C  CD2 . HIS B 1 420 ? -13.381 0.963   48.104  1.00 34.04  ? 420  HIS B CD2 1 
ATOM   7059 C  CE1 . HIS B 1 420 ? -13.765 2.348   46.440  1.00 37.71  ? 420  HIS B CE1 1 
ATOM   7060 N  NE2 . HIS B 1 420 ? -12.924 2.070   47.423  1.00 35.81  ? 420  HIS B NE2 1 
ATOM   7061 N  N   . PHE B 1 421 ? -18.172 -1.913  49.428  1.00 32.31  ? 421  PHE B N   1 
ATOM   7062 C  CA  . PHE B 1 421 ? -19.212 -2.928  49.273  1.00 34.42  ? 421  PHE B CA  1 
ATOM   7063 C  C   . PHE B 1 421 ? -20.090 -3.027  50.510  1.00 34.69  ? 421  PHE B C   1 
ATOM   7064 O  O   . PHE B 1 421 ? -19.654 -2.750  51.631  1.00 33.52  ? 421  PHE B O   1 
ATOM   7065 C  CB  . PHE B 1 421 ? -18.631 -4.331  49.027  1.00 31.81  ? 421  PHE B CB  1 
ATOM   7066 C  CG  . PHE B 1 421 ? -17.641 -4.382  47.901  1.00 33.35  ? 421  PHE B CG  1 
ATOM   7067 C  CD1 . PHE B 1 421 ? -18.062 -4.594  46.608  1.00 34.47  ? 421  PHE B CD1 1 
ATOM   7068 C  CD2 . PHE B 1 421 ? -16.299 -4.172  48.143  1.00 33.28  ? 421  PHE B CD2 1 
ATOM   7069 C  CE1 . PHE B 1 421 ? -17.153 -4.616  45.550  1.00 35.07  ? 421  PHE B CE1 1 
ATOM   7070 C  CE2 . PHE B 1 421 ? -15.371 -4.195  47.104  1.00 33.09  ? 421  PHE B CE2 1 
ATOM   7071 C  CZ  . PHE B 1 421 ? -15.797 -4.417  45.804  1.00 34.29  ? 421  PHE B CZ  1 
ATOM   7072 N  N   . ASP B 1 422 ? -21.325 -3.477  50.287  1.00 34.33  ? 422  ASP B N   1 
ATOM   7073 C  CA  . ASP B 1 422 ? -22.127 -4.104  51.326  1.00 37.18  ? 422  ASP B CA  1 
ATOM   7074 C  C   . ASP B 1 422 ? -21.950 -5.616  51.223  1.00 36.91  ? 422  ASP B C   1 
ATOM   7075 O  O   . ASP B 1 422 ? -21.802 -6.168  50.132  1.00 38.22  ? 422  ASP B O   1 
ATOM   7076 C  CB  . ASP B 1 422 ? -23.608 -3.755  51.174  1.00 37.09  ? 422  ASP B CB  1 
ATOM   7077 C  CG  . ASP B 1 422 ? -23.892 -2.309  51.455  1.00 39.32  ? 422  ASP B CG  1 
ATOM   7078 O  OD1 . ASP B 1 422 ? -23.718 -1.895  52.615  1.00 39.45  ? 422  ASP B OD1 1 
ATOM   7079 O  OD2 . ASP B 1 422 ? -24.267 -1.585  50.510  1.00 45.35  ? 422  ASP B OD2 1 
ATOM   7080 N  N   . PHE B 1 423 ? -21.973 -6.289  52.360  1.00 34.69  ? 423  PHE B N   1 
ATOM   7081 C  CA  . PHE B 1 423 ? -21.700 -7.715  52.385  1.00 33.96  ? 423  PHE B CA  1 
ATOM   7082 C  C   . PHE B 1 423 ? -22.920 -8.490  52.859  1.00 38.96  ? 423  PHE B C   1 
ATOM   7083 O  O   . PHE B 1 423 ? -23.642 -8.043  53.754  1.00 39.16  ? 423  PHE B O   1 
ATOM   7084 C  CB  . PHE B 1 423 ? -20.492 -8.003  53.268  1.00 36.51  ? 423  PHE B CB  1 
ATOM   7085 C  CG  . PHE B 1 423 ? -19.215 -7.456  52.705  1.00 35.76  ? 423  PHE B CG  1 
ATOM   7086 C  CD1 . PHE B 1 423 ? -18.503 -8.172  51.768  1.00 34.96  ? 423  PHE B CD1 1 
ATOM   7087 C  CD2 . PHE B 1 423 ? -18.761 -6.203  53.078  1.00 37.81  ? 423  PHE B CD2 1 
ATOM   7088 C  CE1 . PHE B 1 423 ? -17.339 -7.661  51.223  1.00 37.52  ? 423  PHE B CE1 1 
ATOM   7089 C  CE2 . PHE B 1 423 ? -17.597 -5.691  52.541  1.00 33.66  ? 423  PHE B CE2 1 
ATOM   7090 C  CZ  . PHE B 1 423 ? -16.888 -6.423  51.605  1.00 35.55  ? 423  PHE B CZ  1 
ATOM   7091 N  N   . GLU B 1 424 ? -23.140 -9.651  52.249  1.00 34.86  ? 424  GLU B N   1 
ATOM   7092 C  CA  . GLU B 1 424 ? -24.265 -10.518 52.573  1.00 38.94  ? 424  GLU B CA  1 
ATOM   7093 C  C   . GLU B 1 424 ? -23.755 -11.909 52.920  1.00 36.97  ? 424  GLU B C   1 
ATOM   7094 O  O   . GLU B 1 424 ? -22.991 -12.506 52.154  1.00 36.34  ? 424  GLU B O   1 
ATOM   7095 C  CB  . GLU B 1 424 ? -25.259 -10.608 51.406  1.00 36.59  ? 424  GLU B CB  1 
ATOM   7096 C  CG  . GLU B 1 424 ? -26.513 -11.423 51.747  1.00 41.29  ? 424  GLU B CG  1 
ATOM   7097 C  CD  . GLU B 1 424 ? -27.325 -11.829 50.521  1.00 46.65  ? 424  GLU B CD  1 
ATOM   7098 O  OE1 . GLU B 1 424 ? -26.931 -11.489 49.381  1.00 46.33  ? 424  GLU B OE1 1 
ATOM   7099 O  OE2 . GLU B 1 424 ? -28.361 -12.503 50.707  1.00 48.62  ? 424  GLU B OE2 1 
ATOM   7100 N  N   . ASP B 1 425 ? -24.186 -12.417 54.072  1.00 34.41  ? 425  ASP B N   1 
ATOM   7101 C  CA  . ASP B 1 425 ? -23.928 -13.793 54.499  1.00 35.26  ? 425  ASP B CA  1 
ATOM   7102 C  C   . ASP B 1 425 ? -25.013 -14.693 53.896  1.00 33.61  ? 425  ASP B C   1 
ATOM   7103 O  O   . ASP B 1 425 ? -25.916 -15.198 54.568  1.00 33.37  ? 425  ASP B O   1 
ATOM   7104 C  CB  . ASP B 1 425 ? -23.879 -13.844 56.025  1.00 35.27  ? 425  ASP B CB  1 
ATOM   7105 C  CG  . ASP B 1 425 ? -23.800 -15.251 56.594  1.00 35.45  ? 425  ASP B CG  1 
ATOM   7106 O  OD1 . ASP B 1 425 ? -23.271 -16.156 55.924  1.00 36.85  ? 425  ASP B OD1 1 
ATOM   7107 O  OD2 . ASP B 1 425 ? -24.259 -15.421 57.754  1.00 35.37  ? 425  ASP B OD2 1 
ATOM   7108 N  N   . HIS B 1 426 ? -24.903 -14.884 52.581  1.00 36.00  ? 426  HIS B N   1 
ATOM   7109 C  CA  . HIS B 1 426 ? -26.005 -15.468 51.820  1.00 38.50  ? 426  HIS B CA  1 
ATOM   7110 C  C   . HIS B 1 426 ? -26.214 -16.957 52.105  1.00 37.72  ? 426  HIS B C   1 
ATOM   7111 O  O   . HIS B 1 426 ? -27.308 -17.472 51.843  1.00 37.57  ? 426  HIS B O   1 
ATOM   7112 C  CB  . HIS B 1 426 ? -25.783 -15.226 50.328  1.00 37.29  ? 426  HIS B CB  1 
ATOM   7113 C  CG  . HIS B 1 426 ? -24.603 -15.952 49.770  1.00 36.52  ? 426  HIS B CG  1 
ATOM   7114 N  ND1 . HIS B 1 426 ? -23.311 -15.709 50.189  1.00 36.35  ? 426  HIS B ND1 1 
ATOM   7115 C  CD2 . HIS B 1 426 ? -24.520 -16.923 48.832  1.00 36.82  ? 426  HIS B CD2 1 
ATOM   7116 C  CE1 . HIS B 1 426 ? -22.484 -16.507 49.538  1.00 38.89  ? 426  HIS B CE1 1 
ATOM   7117 N  NE2 . HIS B 1 426 ? -23.192 -17.251 48.704  1.00 37.19  ? 426  HIS B NE2 1 
ATOM   7118 N  N   . THR B 1 427 ? -25.221 -17.665 52.640  1.00 33.31  ? 427  THR B N   1 
ATOM   7119 C  CA  . THR B 1 427 ? -25.415 -19.070 52.979  1.00 33.80  ? 427  THR B CA  1 
ATOM   7120 C  C   . THR B 1 427 ? -25.705 -19.282 54.458  1.00 32.24  ? 427  THR B C   1 
ATOM   7121 O  O   . THR B 1 427 ? -25.872 -20.429 54.883  1.00 35.25  ? 427  THR B O   1 
ATOM   7122 C  CB  . THR B 1 427 ? -24.199 -19.910 52.573  1.00 36.25  ? 427  THR B CB  1 
ATOM   7123 O  OG1 . THR B 1 427 ? -23.117 -19.671 53.493  1.00 36.11  ? 427  THR B OG1 1 
ATOM   7124 C  CG2 . THR B 1 427 ? -23.777 -19.592 51.137  1.00 33.43  ? 427  THR B CG2 1 
ATOM   7125 N  N   . ASN B 1 428 ? -25.794 -18.216 55.246  1.00 31.46  ? 428  ASN B N   1 
ATOM   7126 C  CA  . ASN B 1 428 ? -25.867 -18.325 56.704  1.00 36.96  ? 428  ASN B CA  1 
ATOM   7127 C  C   . ASN B 1 428 ? -24.764 -19.259 57.207  1.00 37.25  ? 428  ASN B C   1 
ATOM   7128 O  O   . ASN B 1 428 ? -25.000 -20.288 57.854  1.00 36.13  ? 428  ASN B O   1 
ATOM   7129 C  CB  . ASN B 1 428 ? -27.251 -18.796 57.161  1.00 38.60  ? 428  ASN B CB  1 
ATOM   7130 C  CG  . ASN B 1 428 ? -27.419 -18.730 58.662  1.00 47.08  ? 428  ASN B CG  1 
ATOM   7131 O  OD1 . ASN B 1 428 ? -26.639 -18.086 59.359  1.00 43.91  ? 428  ASN B OD1 1 
ATOM   7132 N  ND2 . ASN B 1 428 ? -28.450 -19.397 59.171  1.00 50.54  ? 428  ASN B ND2 1 
ATOM   7133 N  N   . TYR B 1 429 ? -23.538 -18.858 56.889  1.00 32.57  ? 429  TYR B N   1 
ATOM   7134 C  CA  . TYR B 1 429 ? -22.369 -19.710 57.043  1.00 34.56  ? 429  TYR B CA  1 
ATOM   7135 C  C   . TYR B 1 429 ? -22.165 -20.149 58.490  1.00 32.46  ? 429  TYR B C   1 
ATOM   7136 O  O   . TYR B 1 429 ? -22.252 -19.347 59.424  1.00 33.14  ? 429  TYR B O   1 
ATOM   7137 C  CB  . TYR B 1 429 ? -21.139 -18.955 56.530  1.00 31.80  ? 429  TYR B CB  1 
ATOM   7138 C  CG  . TYR B 1 429 ? -19.798 -19.546 56.955  1.00 32.59  ? 429  TYR B CG  1 
ATOM   7139 C  CD1 . TYR B 1 429 ? -19.288 -20.685 56.341  1.00 33.68  ? 429  TYR B CD1 1 
ATOM   7140 C  CD2 . TYR B 1 429 ? -19.041 -18.941 57.968  1.00 32.50  ? 429  TYR B CD2 1 
ATOM   7141 C  CE1 . TYR B 1 429 ? -18.044 -21.223 56.728  1.00 33.32  ? 429  TYR B CE1 1 
ATOM   7142 C  CE2 . TYR B 1 429 ? -17.810 -19.459 58.355  1.00 32.87  ? 429  TYR B CE2 1 
ATOM   7143 C  CZ  . TYR B 1 429 ? -17.317 -20.601 57.729  1.00 31.97  ? 429  TYR B CZ  1 
ATOM   7144 O  OH  . TYR B 1 429 ? -16.091 -21.121 58.124  1.00 32.31  ? 429  TYR B OH  1 
ATOM   7145 N  N   . GLU B 1 430 ? -21.877 -21.439 58.678  1.00 31.74  ? 430  GLU B N   1 
ATOM   7146 C  CA  . GLU B 1 430 ? -21.566 -21.968 60.002  1.00 34.71  ? 430  GLU B CA  1 
ATOM   7147 C  C   . GLU B 1 430 ? -20.057 -21.960 60.197  1.00 35.93  ? 430  GLU B C   1 
ATOM   7148 O  O   . GLU B 1 430 ? -19.335 -22.619 59.441  1.00 34.73  ? 430  GLU B O   1 
ATOM   7149 C  CB  . GLU B 1 430 ? -22.086 -23.393 60.169  1.00 35.45  ? 430  GLU B CB  1 
ATOM   7150 C  CG  . GLU B 1 430 ? -21.894 -23.928 61.570  1.00 41.55  ? 430  GLU B CG  1 
ATOM   7151 C  CD  . GLU B 1 430 ? -22.591 -25.258 61.774  1.00 55.71  ? 430  GLU B CD  1 
ATOM   7152 O  OE1 . GLU B 1 430 ? -23.504 -25.572 60.978  1.00 63.43  ? 430  GLU B OE1 1 
ATOM   7153 O  OE2 . GLU B 1 430 ? -22.252 -25.969 62.744  1.00 66.55  ? 430  GLU B OE2 1 
ATOM   7154 N  N   . LEU B 1 431 ? -19.584 -21.230 61.205  1.00 35.69  ? 431  LEU B N   1 
ATOM   7155 C  CA  . LEU B 1 431 ? -18.146 -21.129 61.419  1.00 34.02  ? 431  LEU B CA  1 
ATOM   7156 C  C   . LEU B 1 431 ? -17.514 -22.513 61.482  1.00 36.31  ? 431  LEU B C   1 
ATOM   7157 O  O   . LEU B 1 431 ? -17.932 -23.380 62.260  1.00 36.51  ? 431  LEU B O   1 
ATOM   7158 C  CB  . LEU B 1 431 ? -17.838 -20.348 62.699  1.00 35.06  ? 431  LEU B CB  1 
ATOM   7159 C  CG  . LEU B 1 431 ? -16.340 -20.126 62.941  1.00 36.27  ? 431  LEU B CG  1 
ATOM   7160 C  CD1 . LEU B 1 431 ? -15.718 -19.390 61.763  1.00 35.86  ? 431  LEU B CD1 1 
ATOM   7161 C  CD2 . LEU B 1 431 ? -16.122 -19.369 64.260  1.00 37.78  ? 431  LEU B CD2 1 
ATOM   7162 N  N   . ASP B 1 432 ? -16.483 -22.702 60.660  1.00 32.05  ? 432  ASP B N   1 
ATOM   7163 C  CA  . ASP B 1 432 ? -15.723 -23.943 60.579  1.00 34.64  ? 432  ASP B CA  1 
ATOM   7164 C  C   . ASP B 1 432 ? -14.266 -23.509 60.551  1.00 32.28  ? 432  ASP B C   1 
ATOM   7165 O  O   . ASP B 1 432 ? -13.822 -22.908 59.567  1.00 32.71  ? 432  ASP B O   1 
ATOM   7166 C  CB  . ASP B 1 432 ? -16.120 -24.722 59.325  1.00 35.53  ? 432  ASP B CB  1 
ATOM   7167 C  CG  . ASP B 1 432 ? -15.437 -26.061 59.204  1.00 38.50  ? 432  ASP B CG  1 
ATOM   7168 O  OD1 . ASP B 1 432 ? -14.686 -26.454 60.117  1.00 41.73  ? 432  ASP B OD1 1 
ATOM   7169 O  OD2 . ASP B 1 432 ? -15.674 -26.726 58.170  1.00 40.05  ? 432  ASP B OD2 1 
ATOM   7170 N  N   . ILE B 1 433 ? -13.543 -23.764 61.635  1.00 33.10  ? 433  ILE B N   1 
ATOM   7171 C  CA  . ILE B 1 433 ? -12.187 -23.242 61.794  1.00 31.18  ? 433  ILE B CA  1 
ATOM   7172 C  C   . ILE B 1 433 ? -11.185 -24.336 61.435  1.00 34.14  ? 433  ILE B C   1 
ATOM   7173 O  O   . ILE B 1 433 ? -11.031 -25.324 62.162  1.00 34.78  ? 433  ILE B O   1 
ATOM   7174 C  CB  . ILE B 1 433 ? -11.951 -22.711 63.208  1.00 32.47  ? 433  ILE B CB  1 
ATOM   7175 C  CG1 . ILE B 1 433 ? -12.925 -21.564 63.495  1.00 34.42  ? 433  ILE B CG1 1 
ATOM   7176 C  CG2 . ILE B 1 433 ? -10.476 -22.257 63.343  1.00 32.03  ? 433  ILE B CG2 1 
ATOM   7177 C  CD1 . ILE B 1 433 ? -12.859 -21.058 64.918  1.00 34.62  ? 433  ILE B CD1 1 
ATOM   7178 N  N   . LYS B 1 434 ? -10.492 -24.143 60.312  1.00 33.07  ? 434  LYS B N   1 
ATOM   7179 C  CA  . LYS B 1 434 ? -9.475  -25.082 59.859  1.00 30.80  ? 434  LYS B CA  1 
ATOM   7180 C  C   . LYS B 1 434 ? -8.170  -24.808 60.592  1.00 32.21  ? 434  LYS B C   1 
ATOM   7181 O  O   . LYS B 1 434 ? -7.794  -23.650 60.805  1.00 34.81  ? 434  LYS B O   1 
ATOM   7182 C  CB  . LYS B 1 434 ? -9.260  -24.957 58.350  1.00 34.91  ? 434  LYS B CB  1 
ATOM   7183 C  CG  . LYS B 1 434 ? -8.217  -25.906 57.770  1.00 32.88  ? 434  LYS B CG  1 
ATOM   7184 C  CD  . LYS B 1 434 ? -8.212  -25.788 56.233  1.00 39.87  ? 434  LYS B CD  1 
ATOM   7185 C  CE  . LYS B 1 434 ? -7.128  -26.637 55.572  1.00 46.51  ? 434  LYS B CE  1 
ATOM   7186 N  NZ  . LYS B 1 434 ? -7.278  -28.079 55.929  1.00 42.86  ? 434  LYS B NZ  1 
ATOM   7187 N  N   . GLU B 1 435 ? -7.476  -25.873 60.971  1.00 29.53  ? 435  GLU B N   1 
ATOM   7188 C  CA  . GLU B 1 435 ? -6.240  -25.750 61.734  1.00 32.06  ? 435  GLU B CA  1 
ATOM   7189 C  C   . GLU B 1 435 ? -5.063  -26.206 60.882  1.00 34.18  ? 435  GLU B C   1 
ATOM   7190 O  O   . GLU B 1 435 ? -5.101  -27.294 60.296  1.00 33.75  ? 435  GLU B O   1 
ATOM   7191 C  CB  . GLU B 1 435 ? -6.337  -26.542 63.034  1.00 31.69  ? 435  GLU B CB  1 
ATOM   7192 C  CG  . GLU B 1 435 ? -7.395  -25.955 63.951  1.00 29.64  ? 435  GLU B CG  1 
ATOM   7193 C  CD  . GLU B 1 435 ? -7.238  -26.366 65.401  1.00 33.45  ? 435  GLU B CD  1 
ATOM   7194 O  OE1 . GLU B 1 435 ? -6.114  -26.726 65.826  1.00 31.58  ? 435  GLU B OE1 1 
ATOM   7195 O  OE2 . GLU B 1 435 ? -8.256  -26.327 66.119  1.00 32.51  ? 435  GLU B OE2 1 
ATOM   7196 N  N   . THR B 1 436 ? -4.066  -25.323 60.750  1.00 32.33  ? 436  THR B N   1 
ATOM   7197 C  CA  . THR B 1 436 ? -2.778  -25.560 60.096  1.00 34.81  ? 436  THR B CA  1 
ATOM   7198 C  C   . THR B 1 436 ? -1.668  -25.019 60.988  1.00 31.62  ? 436  THR B C   1 
ATOM   7199 O  O   . THR B 1 436 ? -0.809  -24.249 60.559  1.00 33.28  ? 436  THR B O   1 
ATOM   7200 C  CB  . THR B 1 436 ? -2.720  -24.912 58.714  1.00 34.09  ? 436  THR B CB  1 
ATOM   7201 O  OG1 . THR B 1 436 ? -3.011  -23.510 58.825  1.00 35.22  ? 436  THR B OG1 1 
ATOM   7202 C  CG2 . THR B 1 436 ? -3.751  -25.558 57.774  1.00 33.53  ? 436  THR B CG2 1 
ATOM   7203 N  N   . LEU B 1 437 ? -1.707  -25.413 62.263  1.00 32.80  ? 437  LEU B N   1 
ATOM   7204 C  CA  . LEU B 1 437 ? -1.016  -24.699 63.327  1.00 35.06  ? 437  LEU B CA  1 
ATOM   7205 C  C   . LEU B 1 437 ? -1.735  -23.365 63.565  1.00 37.77  ? 437  LEU B C   1 
ATOM   7206 O  O   . LEU B 1 437 ? -2.286  -23.142 64.650  1.00 33.82  ? 437  LEU B O   1 
ATOM   7207 C  CB  . LEU B 1 437 ? 0.473   -24.522 62.984  1.00 34.24  ? 437  LEU B CB  1 
ATOM   7208 C  CG  . LEU B 1 437 ? 1.265   -25.835 62.738  1.00 33.11  ? 437  LEU B CG  1 
ATOM   7209 C  CD1 . LEU B 1 437 ? 2.743   -25.529 62.638  1.00 35.52  ? 437  LEU B CD1 1 
ATOM   7210 C  CD2 . LEU B 1 437 ? 1.005   -26.930 63.809  1.00 33.62  ? 437  LEU B CD2 1 
ATOM   7211 N  N   . THR B 1 438 ? -1.774  -22.496 62.550  1.00 34.44  ? 438  THR B N   1 
ATOM   7212 C  CA  . THR B 1 438 ? -2.603  -21.292 62.564  1.00 32.04  ? 438  THR B CA  1 
ATOM   7213 C  C   . THR B 1 438 ? -4.080  -21.631 62.333  1.00 30.28  ? 438  THR B C   1 
ATOM   7214 O  O   . THR B 1 438 ? -4.433  -22.748 61.959  1.00 33.01  ? 438  THR B O   1 
ATOM   7215 C  CB  . THR B 1 438 ? -2.138  -20.336 61.484  1.00 35.65  ? 438  THR B CB  1 
ATOM   7216 O  OG1 . THR B 1 438 ? -2.238  -21.018 60.227  1.00 34.77  ? 438  THR B OG1 1 
ATOM   7217 C  CG2 . THR B 1 438 ? -0.675  -19.966 61.727  1.00 30.43  ? 438  THR B CG2 1 
ATOM   7218 N  N   . LEU B 1 439 ? -4.950  -20.646 62.568  1.00 32.27  ? 439  LEU B N   1 
ATOM   7219 C  CA  . LEU B 1 439 ? -6.400  -20.839 62.497  1.00 31.19  ? 439  LEU B CA  1 
ATOM   7220 C  C   . LEU B 1 439 ? -7.005  -19.953 61.419  1.00 33.94  ? 439  LEU B C   1 
ATOM   7221 O  O   . LEU B 1 439 ? -6.645  -18.777 61.291  1.00 33.28  ? 439  LEU B O   1 
ATOM   7222 C  CB  . LEU B 1 439 ? -7.072  -20.516 63.824  1.00 29.38  ? 439  LEU B CB  1 
ATOM   7223 C  CG  . LEU B 1 439 ? -6.531  -21.170 65.100  1.00 29.41  ? 439  LEU B CG  1 
ATOM   7224 C  CD1 . LEU B 1 439 ? -7.316  -20.658 66.309  1.00 30.83  ? 439  LEU B CD1 1 
ATOM   7225 C  CD2 . LEU B 1 439 ? -6.627  -22.691 64.981  1.00 29.99  ? 439  LEU B CD2 1 
ATOM   7226 N  N   . LYS B 1 440 ? -7.979  -20.500 60.676  1.00 32.18  ? 440  LYS B N   1 
ATOM   7227 C  CA  . LYS B 1 440 ? -8.627  -19.693 59.643  1.00 29.61  ? 440  LYS B CA  1 
ATOM   7228 C  C   . LYS B 1 440 ? -9.996  -20.290 59.357  1.00 31.77  ? 440  LYS B C   1 
ATOM   7229 O  O   . LYS B 1 440 ? -10.108 -21.521 59.315  1.00 29.94  ? 440  LYS B O   1 
ATOM   7230 C  CB  . LYS B 1 440 ? -7.783  -19.667 58.359  1.00 33.71  ? 440  LYS B CB  1 
ATOM   7231 C  CG  . LYS B 1 440 ? -8.131  -18.557 57.384  1.00 37.92  ? 440  LYS B CG  1 
ATOM   7232 C  CD  . LYS B 1 440 ? -7.226  -18.588 56.156  1.00 41.00  ? 440  LYS B CD  1 
ATOM   7233 C  CE  . LYS B 1 440 ? -5.774  -18.572 56.558  1.00 45.23  ? 440  LYS B CE  1 
ATOM   7234 N  NZ  . LYS B 1 440 ? -5.072  -19.805 56.068  1.00 48.43  ? 440  LYS B NZ  1 
ATOM   7235 N  N   . PRO B 1 441 ? -11.033 -19.481 59.130  1.00 34.01  ? 441  PRO B N   1 
ATOM   7236 C  CA  . PRO B 1 441 ? -12.302 -20.050 58.651  1.00 33.65  ? 441  PRO B CA  1 
ATOM   7237 C  C   . PRO B 1 441 ? -12.104 -20.825 57.351  1.00 34.17  ? 441  PRO B C   1 
ATOM   7238 O  O   . PRO B 1 441 ? -11.335 -20.423 56.472  1.00 34.94  ? 441  PRO B O   1 
ATOM   7239 C  CB  . PRO B 1 441 ? -13.189 -18.816 58.433  1.00 32.82  ? 441  PRO B CB  1 
ATOM   7240 C  CG  . PRO B 1 441 ? -12.628 -17.760 59.333  1.00 34.68  ? 441  PRO B CG  1 
ATOM   7241 C  CD  . PRO B 1 441 ? -11.120 -18.016 59.322  1.00 31.51  ? 441  PRO B CD  1 
ATOM   7242 N  N   . GLU B 1 442 ? -12.796 -21.952 57.240  1.00 32.59  ? 442  GLU B N   1 
ATOM   7243 C  CA  . GLU B 1 442 ? -12.860 -22.730 56.007  1.00 33.92  ? 442  GLU B CA  1 
ATOM   7244 C  C   . GLU B 1 442 ? -14.249 -22.638 55.386  1.00 28.81  ? 442  GLU B C   1 
ATOM   7245 O  O   . GLU B 1 442 ? -15.250 -22.716 56.095  1.00 31.76  ? 442  GLU B O   1 
ATOM   7246 C  CB  . GLU B 1 442 ? -12.492 -24.196 56.275  1.00 35.14  ? 442  GLU B CB  1 
ATOM   7247 C  CG  . GLU B 1 442 ? -12.519 -25.058 55.033  1.00 42.24  ? 442  GLU B CG  1 
ATOM   7248 C  CD  . GLU B 1 442 ? -11.898 -26.428 55.252  1.00 43.52  ? 442  GLU B CD  1 
ATOM   7249 O  OE1 . GLU B 1 442 ? -11.959 -26.983 56.371  1.00 46.06  ? 442  GLU B OE1 1 
ATOM   7250 O  OE2 . GLU B 1 442 ? -11.352 -26.956 54.269  1.00 55.56  ? 442  GLU B OE2 1 
ATOM   7251 N  N   . GLY B 1 443 ? -14.302 -22.491 54.058  1.00 31.55  ? 443  GLY B N   1 
ATOM   7252 C  CA  . GLY B 1 443 ? -15.592 -22.495 53.380  1.00 36.60  ? 443  GLY B CA  1 
ATOM   7253 C  C   . GLY B 1 443 ? -16.423 -21.250 53.589  1.00 38.04  ? 443  GLY B C   1 
ATOM   7254 O  O   . GLY B 1 443 ? -17.607 -21.239 53.232  1.00 36.26  ? 443  GLY B O   1 
ATOM   7255 N  N   . PHE B 1 444 ? -15.844 -20.205 54.170  1.00 33.29  ? 444  PHE B N   1 
ATOM   7256 C  CA  . PHE B 1 444 ? -16.563 -18.959 54.407  1.00 35.31  ? 444  PHE B CA  1 
ATOM   7257 C  C   . PHE B 1 444 ? -16.730 -18.211 53.086  1.00 35.25  ? 444  PHE B C   1 
ATOM   7258 O  O   . PHE B 1 444 ? -15.744 -17.842 52.443  1.00 33.22  ? 444  PHE B O   1 
ATOM   7259 C  CB  . PHE B 1 444 ? -15.796 -18.121 55.430  1.00 36.02  ? 444  PHE B CB  1 
ATOM   7260 C  CG  . PHE B 1 444 ? -16.406 -16.768 55.718  1.00 32.81  ? 444  PHE B CG  1 
ATOM   7261 C  CD1 . PHE B 1 444 ? -17.786 -16.594 55.752  1.00 32.82  ? 444  PHE B CD1 1 
ATOM   7262 C  CD2 . PHE B 1 444 ? -15.587 -15.671 55.975  1.00 32.73  ? 444  PHE B CD2 1 
ATOM   7263 C  CE1 . PHE B 1 444 ? -18.334 -15.343 56.029  1.00 31.46  ? 444  PHE B CE1 1 
ATOM   7264 C  CE2 . PHE B 1 444 ? -16.117 -14.442 56.247  1.00 31.43  ? 444  PHE B CE2 1 
ATOM   7265 C  CZ  . PHE B 1 444 ? -17.502 -14.267 56.272  1.00 33.91  ? 444  PHE B CZ  1 
ATOM   7266 N  N   . VAL B 1 445 ? -17.981 -18.002 52.670  1.00 35.45  ? 445  VAL B N   1 
ATOM   7267 C  CA  . VAL B 1 445 ? -18.286 -17.290 51.440  1.00 31.45  ? 445  VAL B CA  1 
ATOM   7268 C  C   . VAL B 1 445 ? -19.293 -16.198 51.765  1.00 34.17  ? 445  VAL B C   1 
ATOM   7269 O  O   . VAL B 1 445 ? -20.087 -16.322 52.703  1.00 32.84  ? 445  VAL B O   1 
ATOM   7270 C  CB  . VAL B 1 445 ? -18.833 -18.229 50.334  1.00 33.01  ? 445  VAL B CB  1 
ATOM   7271 C  CG1 . VAL B 1 445 ? -17.753 -19.236 49.902  1.00 34.08  ? 445  VAL B CG1 1 
ATOM   7272 C  CG2 . VAL B 1 445 ? -20.098 -18.964 50.811  1.00 37.81  ? 445  VAL B CG2 1 
ATOM   7273 N  N   . VAL B 1 446 ? -19.247 -15.121 50.974  1.00 34.28  ? 446  VAL B N   1 
ATOM   7274 C  CA  . VAL B 1 446 ? -20.162 -13.996 51.081  1.00 36.74  ? 446  VAL B CA  1 
ATOM   7275 C  C   . VAL B 1 446 ? -20.471 -13.513 49.669  1.00 32.95  ? 446  VAL B C   1 
ATOM   7276 O  O   . VAL B 1 446 ? -19.783 -13.854 48.700  1.00 33.03  ? 446  VAL B O   1 
ATOM   7277 C  CB  . VAL B 1 446 ? -19.588 -12.828 51.923  1.00 31.88  ? 446  VAL B CB  1 
ATOM   7278 C  CG1 . VAL B 1 446 ? -19.298 -13.263 53.362  1.00 32.69  ? 446  VAL B CG1 1 
ATOM   7279 C  CG2 . VAL B 1 446 ? -18.334 -12.242 51.252  1.00 32.52  ? 446  VAL B CG2 1 
ATOM   7280 N  N   . LYS B 1 447 ? -21.516 -12.696 49.567  1.00 34.22  ? 447  LYS B N   1 
ATOM   7281 C  CA  . LYS B 1 447 ? -21.787 -11.905 48.379  1.00 34.31  ? 447  LYS B CA  1 
ATOM   7282 C  C   . LYS B 1 447 ? -21.530 -10.439 48.691  1.00 34.52  ? 447  LYS B C   1 
ATOM   7283 O  O   . LYS B 1 447 ? -21.866 -9.952  49.776  1.00 38.30  ? 447  LYS B O   1 
ATOM   7284 C  CB  . LYS B 1 447 ? -23.236 -12.082 47.908  1.00 34.68  ? 447  LYS B CB  1 
ATOM   7285 C  CG  . LYS B 1 447 ? -23.508 -13.450 47.325  1.00 38.96  ? 447  LYS B CG  1 
ATOM   7286 C  CD  . LYS B 1 447 ? -24.891 -13.551 46.704  1.00 36.43  ? 447  LYS B CD  1 
ATOM   7287 C  CE  . LYS B 1 447 ? -24.976 -14.822 45.880  1.00 43.63  ? 447  LYS B CE  1 
ATOM   7288 N  NZ  . LYS B 1 447 ? -26.376 -15.166 45.529  1.00 51.15  ? 447  LYS B NZ  1 
ATOM   7289 N  N   . ALA B 1 448 ? -20.941 -9.736  47.739  1.00 35.29  ? 448  ALA B N   1 
ATOM   7290 C  CA  . ALA B 1 448 ? -20.642 -8.324  47.892  1.00 35.79  ? 448  ALA B CA  1 
ATOM   7291 C  C   . ALA B 1 448 ? -21.482 -7.541  46.899  1.00 44.30  ? 448  ALA B C   1 
ATOM   7292 O  O   . ALA B 1 448 ? -21.510 -7.871  45.709  1.00 51.87  ? 448  ALA B O   1 
ATOM   7293 C  CB  . ALA B 1 448 ? -19.146 -8.048  47.683  1.00 42.67  ? 448  ALA B CB  1 
ATOM   7294 N  N   . LYS B 1 449 ? -22.187 -6.531  47.390  1.00 40.50  ? 449  LYS B N   1 
ATOM   7295 C  CA  . LYS B 1 449 ? -22.939 -5.620  46.537  1.00 42.01  ? 449  LYS B CA  1 
ATOM   7296 C  C   . LYS B 1 449 ? -22.159 -4.312  46.487  1.00 40.81  ? 449  LYS B C   1 
ATOM   7297 O  O   . LYS B 1 449 ? -22.009 -3.631  47.507  1.00 36.92  ? 449  LYS B O   1 
ATOM   7298 C  CB  . LYS B 1 449 ? -24.356 -5.425  47.072  1.00 47.18  ? 449  LYS B CB  1 
ATOM   7299 C  CG  . LYS B 1 449 ? -25.137 -4.293  46.426  1.00 54.10  ? 449  LYS B CG  1 
ATOM   7300 C  CD  . LYS B 1 449 ? -26.636 -4.478  46.629  1.00 61.22  ? 449  LYS B CD  1 
ATOM   7301 C  CE  . LYS B 1 449 ? -27.447 -3.622  45.659  1.00 61.61  ? 449  LYS B CE  1 
ATOM   7302 N  NZ  . LYS B 1 449 ? -27.890 -2.348  46.307  1.00 64.48  ? 449  LYS B NZ  1 
ATOM   7303 N  N   . SER B 1 450 ? -21.645 -3.977  45.309  1.00 37.50  ? 450  SER B N   1 
ATOM   7304 C  CA  . SER B 1 450 ? -20.844 -2.770  45.155  1.00 35.59  ? 450  SER B CA  1 
ATOM   7305 C  C   . SER B 1 450 ? -21.642 -1.527  45.528  1.00 38.50  ? 450  SER B C   1 
ATOM   7306 O  O   . SER B 1 450 ? -22.819 -1.390  45.183  1.00 39.64  ? 450  SER B O   1 
ATOM   7307 C  CB  . SER B 1 450 ? -20.353 -2.642  43.712  1.00 37.72  ? 450  SER B CB  1 
ATOM   7308 O  OG  . SER B 1 450 ? -19.579 -1.470  43.545  1.00 35.75  ? 450  SER B OG  1 
ATOM   7309 N  N   . LYS B 1 451 ? -20.996 -0.619  46.242  1.00 33.87  ? 451  LYS B N   1 
ATOM   7310 C  CA  . LYS B 1 451 ? -21.542 0.716   46.444  1.00 37.38  ? 451  LYS B CA  1 
ATOM   7311 C  C   . LYS B 1 451 ? -21.178 1.651   45.302  1.00 40.71  ? 451  LYS B C   1 
ATOM   7312 O  O   . LYS B 1 451 ? -21.483 2.842   45.375  1.00 42.74  ? 451  LYS B O   1 
ATOM   7313 C  CB  . LYS B 1 451 ? -21.058 1.304   47.774  1.00 37.37  ? 451  LYS B CB  1 
ATOM   7314 C  CG  . LYS B 1 451 ? -21.377 0.472   49.013  1.00 39.02  ? 451  LYS B CG  1 
ATOM   7315 C  CD  . LYS B 1 451 ? -20.845 1.163   50.257  1.00 41.59  ? 451  LYS B CD  1 
ATOM   7316 C  CE  . LYS B 1 451 ? -21.229 0.433   51.526  1.00 44.50  ? 451  LYS B CE  1 
ATOM   7317 N  NZ  . LYS B 1 451 ? -22.628 0.715   51.915  1.00 51.02  ? 451  LYS B NZ  1 
ATOM   7318 N  N   . LYS B 1 452 ? -20.518 1.140   44.262  1.00 36.94  ? 452  LYS B N   1 
ATOM   7319 C  CA  . LYS B 1 452 ? -20.218 1.897   43.038  1.00 44.49  ? 452  LYS B CA  1 
ATOM   7320 C  C   . LYS B 1 452 ? -19.468 3.197   43.336  1.00 46.93  ? 452  LYS B C   1 
ATOM   7321 O  O   . LYS B 1 452 ? -19.800 4.276   42.831  1.00 44.57  ? 452  LYS B O   1 
ATOM   7322 C  CB  . LYS B 1 452 ? -21.494 2.177   42.242  1.00 44.77  ? 452  LYS B CB  1 
ATOM   7323 C  CG  . LYS B 1 452 ? -22.304 0.944   41.866  1.00 47.33  ? 452  LYS B CG  1 
ATOM   7324 C  CD  . LYS B 1 452 ? -21.533 0.001   40.954  1.00 50.73  ? 452  LYS B CD  1 
ATOM   7325 C  CE  . LYS B 1 452 ? -22.405 -1.194  40.538  1.00 52.29  ? 452  LYS B CE  1 
ATOM   7326 N  NZ  . LYS B 1 452 ? -21.620 -2.352  39.991  1.00 49.76  ? 452  LYS B NZ  1 
ATOM   7327 N  N   . ILE B 1 453 ? -18.431 3.091   44.155  1.00 40.73  ? 453  ILE B N   1 
ATOM   7328 C  CA  . ILE B 1 453 ? -17.569 4.219   44.489  1.00 38.65  ? 453  ILE B CA  1 
ATOM   7329 C  C   . ILE B 1 453 ? -16.277 4.066   43.694  1.00 43.06  ? 453  ILE B C   1 
ATOM   7330 O  O   . ILE B 1 453 ? -15.595 3.039   43.838  1.00 38.95  ? 453  ILE B O   1 
ATOM   7331 C  CB  . ILE B 1 453 ? -17.295 4.288   46.000  1.00 41.23  ? 453  ILE B CB  1 
ATOM   7332 C  CG1 . ILE B 1 453 ? -18.621 4.447   46.749  1.00 41.88  ? 453  ILE B CG1 1 
ATOM   7333 C  CG2 . ILE B 1 453 ? -16.365 5.451   46.329  1.00 41.02  ? 453  ILE B CG2 1 
ATOM   7334 C  CD1 . ILE B 1 453 ? -18.525 4.220   48.240  1.00 44.12  ? 453  ILE B CD1 1 
ATOM   7335 N  N   . PRO B 1 454 ? -15.922 5.025   42.838  1.00 46.25  ? 454  PRO B N   1 
ATOM   7336 C  CA  . PRO B 1 454 ? -14.774 4.826   41.949  1.00 46.03  ? 454  PRO B CA  1 
ATOM   7337 C  C   . PRO B 1 454 ? -13.471 4.709   42.719  1.00 44.33  ? 454  PRO B C   1 
ATOM   7338 O  O   . PRO B 1 454 ? -13.327 5.232   43.830  1.00 43.75  ? 454  PRO B O   1 
ATOM   7339 C  CB  . PRO B 1 454 ? -14.792 6.081   41.064  1.00 44.86  ? 454  PRO B CB  1 
ATOM   7340 C  CG  . PRO B 1 454 ? -16.210 6.529   41.086  1.00 50.54  ? 454  PRO B CG  1 
ATOM   7341 C  CD  . PRO B 1 454 ? -16.685 6.235   42.482  1.00 49.93  ? 454  PRO B CD  1 
ATOM   7342 N  N   . LEU B 1 455 ? -12.523 3.998   42.112  1.00 41.27  ? 455  LEU B N   1 
ATOM   7343 C  CA  . LEU B 1 455 ? -11.149 3.947   42.591  1.00 45.33  ? 455  LEU B CA  1 
ATOM   7344 C  C   . LEU B 1 455 ? -10.310 4.942   41.799  1.00 48.60  ? 455  LEU B C   1 
ATOM   7345 O  O   . LEU B 1 455 ? -10.803 5.567   40.858  1.00 46.95  ? 455  LEU B O   1 
ATOM   7346 C  CB  . LEU B 1 455 ? -10.565 2.539   42.450  1.00 46.08  ? 455  LEU B CB  1 
ATOM   7347 C  CG  . LEU B 1 455 ? -11.020 1.494   43.471  1.00 44.63  ? 455  LEU B CG  1 
ATOM   7348 C  CD1 . LEU B 1 455 ? -10.755 0.084   42.929  1.00 37.94  ? 455  LEU B CD1 1 
ATOM   7349 C  CD2 . LEU B 1 455 ? -10.334 1.719   44.845  1.00 41.56  ? 455  LEU B CD2 1 
ATOM   7350 O  OXT . LEU B 1 455 ? -9.128  5.142   42.079  1.00 49.24  ? 455  LEU B OXT 1 
HETATM 7351 C  CHA . HEM C 2 .   ? -17.835 -14.045 8.966   1.00 29.68  ? 501  HEM A CHA 1 
HETATM 7352 C  CHB . HEM C 2 .   ? -13.035 -13.302 9.320   1.00 31.74  ? 501  HEM A CHB 1 
HETATM 7353 C  CHC . HEM C 2 .   ? -13.669 -11.113 13.679  1.00 31.02  ? 501  HEM A CHC 1 
HETATM 7354 C  CHD . HEM C 2 .   ? -18.406 -12.069 13.394  1.00 33.14  ? 501  HEM A CHD 1 
HETATM 7355 C  C1A . HEM C 2 .   ? -16.478 -14.014 8.697   1.00 27.63  ? 501  HEM A C1A 1 
HETATM 7356 C  C2A . HEM C 2 .   ? -15.880 -14.536 7.507   1.00 30.71  ? 501  HEM A C2A 1 
HETATM 7357 C  C3A . HEM C 2 .   ? -14.537 -14.329 7.613   1.00 31.08  ? 501  HEM A C3A 1 
HETATM 7358 C  C4A . HEM C 2 .   ? -14.290 -13.680 8.853   1.00 31.08  ? 501  HEM A C4A 1 
HETATM 7359 C  CMA . HEM C 2 .   ? -13.502 -14.735 6.587   1.00 29.85  ? 501  HEM A CMA 1 
HETATM 7360 C  CAA . HEM C 2 .   ? -16.555 -15.205 6.314   1.00 28.85  ? 501  HEM A CAA 1 
HETATM 7361 C  CBA . HEM C 2 .   ? -16.801 -16.701 6.568   1.00 28.48  ? 501  HEM A CBA 1 
HETATM 7362 C  CGA . HEM C 2 .   ? -17.422 -17.443 5.401   1.00 29.72  ? 501  HEM A CGA 1 
HETATM 7363 O  O1A . HEM C 2 .   ? -17.763 -18.652 5.578   1.00 31.10  ? 501  HEM A O1A 1 
HETATM 7364 O  O2A . HEM C 2 .   ? -17.564 -16.880 4.287   1.00 28.11  ? 501  HEM A O2A 1 
HETATM 7365 C  C1B . HEM C 2 .   ? -12.827 -12.653 10.554  1.00 35.52  ? 501  HEM A C1B 1 
HETATM 7366 C  C2B . HEM C 2 .   ? -11.527 -12.272 11.027  1.00 31.68  ? 501  HEM A C2B 1 
HETATM 7367 C  C3B . HEM C 2 .   ? -11.698 -11.667 12.249  1.00 28.98  ? 501  HEM A C3B 1 
HETATM 7368 C  C4B . HEM C 2 .   ? -13.143 -11.664 12.511  1.00 31.35  ? 501  HEM A C4B 1 
HETATM 7369 C  CMB . HEM C 2 .   ? -10.218 -12.532 10.286  1.00 33.21  ? 501  HEM A CMB 1 
HETATM 7370 C  CAB . HEM C 2 .   ? -10.706 -11.085 13.190  1.00 33.09  ? 501  HEM A CAB 1 
HETATM 7371 C  CBB . HEM C 2 .   ? -9.558  -10.545 12.769  1.00 31.25  ? 501  HEM A CBB 1 
HETATM 7372 C  C1C . HEM C 2 .   ? -15.019 -11.179 13.984  1.00 28.70  ? 501  HEM A C1C 1 
HETATM 7373 C  C2C . HEM C 2 .   ? -15.626 -10.638 15.135  1.00 33.84  ? 501  HEM A C2C 1 
HETATM 7374 C  C3C . HEM C 2 .   ? -16.976 -10.924 15.060  1.00 35.87  ? 501  HEM A C3C 1 
HETATM 7375 C  C4C . HEM C 2 .   ? -17.181 -11.609 13.827  1.00 32.86  ? 501  HEM A C4C 1 
HETATM 7376 C  CMC . HEM C 2 .   ? -14.904 -9.925  16.247  1.00 33.12  ? 501  HEM A CMC 1 
HETATM 7377 C  CAC . HEM C 2 .   ? -18.019 -10.544 16.044  1.00 33.54  ? 501  HEM A CAC 1 
HETATM 7378 C  CBC . HEM C 2 .   ? -17.987 -9.356  16.656  1.00 34.75  ? 501  HEM A CBC 1 
HETATM 7379 C  C1D . HEM C 2 .   ? -18.573 -12.699 12.167  1.00 31.49  ? 501  HEM A C1D 1 
HETATM 7380 C  C2D . HEM C 2 .   ? -19.910 -13.160 11.754  1.00 34.46  ? 501  HEM A C2D 1 
HETATM 7381 C  C3D . HEM C 2 .   ? -19.763 -13.710 10.531  1.00 31.86  ? 501  HEM A C3D 1 
HETATM 7382 C  C4D . HEM C 2 .   ? -18.336 -13.572 10.184  1.00 30.22  ? 501  HEM A C4D 1 
HETATM 7383 C  CMD . HEM C 2 .   ? -21.207 -13.047 12.533  1.00 31.99  ? 501  HEM A CMD 1 
HETATM 7384 C  CAD . HEM C 2 .   ? -20.883 -14.273 9.680   1.00 29.44  ? 501  HEM A CAD 1 
HETATM 7385 C  CBD . HEM C 2 .   ? -21.383 -13.096 8.821   1.00 31.40  ? 501  HEM A CBD 1 
HETATM 7386 C  CGD . HEM C 2 .   ? -22.568 -13.392 7.925   1.00 31.52  ? 501  HEM A CGD 1 
HETATM 7387 O  O1D . HEM C 2 .   ? -22.488 -14.293 7.041   1.00 32.11  ? 501  HEM A O1D 1 
HETATM 7388 O  O2D . HEM C 2 .   ? -23.617 -12.706 8.048   1.00 33.52  ? 501  HEM A O2D 1 
HETATM 7389 N  NA  . HEM C 2 .   ? -15.483 -13.474 9.513   1.00 32.36  ? 501  HEM A NA  1 
HETATM 7390 N  NB  . HEM C 2 .   ? -13.743 -12.275 11.467  1.00 29.01  ? 501  HEM A NB  1 
HETATM 7391 N  NC  . HEM C 2 .   ? -15.969 -11.750 13.192  1.00 30.31  ? 501  HEM A NC  1 
HETATM 7392 N  ND  . HEM C 2 .   ? -17.668 -12.957 11.199  1.00 28.65  ? 501  HEM A ND  1 
HETATM 7393 FE FE  . HEM C 2 .   ? -15.805 -12.502 11.252  1.00 30.02  ? 501  HEM A FE  1 
HETATM 7394 C  C1  . D0L D 3 .   ? -12.695 -30.476 1.800   1.00 40.28  ? 502  D0L A C1  1 
HETATM 7395 C  C2  . D0L D 3 .   ? -12.749 -30.632 3.182   1.00 37.59  ? 502  D0L A C2  1 
HETATM 7396 C  C15 . D0L D 3 .   ? -11.191 -24.497 6.620   1.00 42.33  ? 502  D0L A C15 1 
HETATM 7397 C  C14 . D0L D 3 .   ? -10.315 -26.257 8.031   1.00 42.85  ? 502  D0L A C14 1 
HETATM 7398 C  C7  . D0L D 3 .   ? -12.070 -29.642 4.104   1.00 38.88  ? 502  D0L A C7  1 
HETATM 7399 C  C12 . D0L D 3 .   ? -8.990  -27.305 6.301   1.00 36.54  ? 502  D0L A C12 1 
HETATM 7400 C  C10 . D0L D 3 .   ? -10.724 -26.814 4.548   1.00 35.28  ? 502  D0L A C10 1 
HETATM 7401 C  C3  . D0L D 3 .   ? -13.399 -31.739 3.723   1.00 41.19  ? 502  D0L A C3  1 
HETATM 7402 C  C13 . D0L D 3 .   ? -9.474  -27.494 7.736   1.00 39.29  ? 502  D0L A C13 1 
HETATM 7403 C  C11 . D0L D 3 .   ? -9.949  -26.274 5.708   1.00 37.29  ? 502  D0L A C11 1 
HETATM 7404 C  C6  . D0L D 3 .   ? -13.318 -31.415 0.970   1.00 37.96  ? 502  D0L A C6  1 
HETATM 7405 C  C8  . D0L D 3 .   ? -12.672 -28.238 4.004   1.00 39.68  ? 502  D0L A C8  1 
HETATM 7406 C  C5  . D0L D 3 .   ? -13.978 -32.518 1.509   1.00 44.48  ? 502  D0L A C5  1 
HETATM 7407 C  C9  . D0L D 3 .   ? -14.094 -28.289 4.483   1.00 38.00  ? 502  D0L A C9  1 
HETATM 7408 C  C4  . D0L D 3 .   ? -14.021 -32.675 2.895   1.00 41.88  ? 502  D0L A C4  1 
HETATM 7409 O  O2  . D0L D 3 .   ? -14.319 -28.051 5.697   1.00 36.61  ? 502  D0L A O2  1 
HETATM 7410 O  O3  . D0L D 3 .   ? -10.262 -26.735 3.409   1.00 36.49  ? 502  D0L A O3  1 
HETATM 7411 O  O1  . D0L D 3 .   ? -15.005 -28.560 3.669   1.00 35.76  ? 502  D0L A O1  1 
HETATM 7412 N  N2  . D0L D 3 .   ? -10.928 -25.933 6.742   1.00 39.24  ? 502  D0L A N2  1 
HETATM 7413 C  C16 . D0L D 3 .   ? -12.479 -24.146 7.330   1.00 44.16  ? 502  D0L A C16 1 
HETATM 7414 C  C17 . D0L D 3 .   ? -12.450 -22.666 7.649   1.00 46.05  ? 502  D0L A C17 1 
HETATM 7415 C  C18 . D0L D 3 .   ? -13.819 -22.213 8.124   1.00 54.49  ? 502  D0L A C18 1 
HETATM 7416 C  C19 . D0L D 3 .   ? -13.782 -21.879 9.603   1.00 44.84  ? 502  D0L A C19 1 
HETATM 7417 C  C20 . D0L D 3 .   ? -13.066 -20.568 9.860   1.00 47.33  ? 502  D0L A C20 1 
HETATM 7418 C  C21 . D0L D 3 .   ? -13.342 -20.143 11.281  1.00 47.39  ? 502  D0L A C21 1 
HETATM 7419 N  N1  . D0L D 3 .   ? -11.909 -27.340 4.861   1.00 35.06  ? 502  D0L A N1  1 
HETATM 7420 C  CAF A SYN E 4 .   ? -17.212 -18.998 11.141  0.43 38.24  ? 503  SYN A CAF 1 
HETATM 7421 C  CAF B SYN E 4 .   ? -14.890 -17.809 13.387  0.42 38.75  ? 503  SYN A CAF 1 
HETATM 7422 C  CAD A SYN E 4 .   ? -16.602 -18.588 9.969   0.43 37.93  ? 503  SYN A CAD 1 
HETATM 7423 C  CAD B SYN E 4 .   ? -14.227 -18.615 14.296  0.42 36.80  ? 503  SYN A CAD 1 
HETATM 7424 C  CAC A SYN E 4 .   ? -15.890 -17.412 9.937   0.43 38.89  ? 503  SYN A CAC 1 
HETATM 7425 C  CAC B SYN E 4 .   ? -14.679 -19.889 14.552  0.42 39.28  ? 503  SYN A CAC 1 
HETATM 7426 C  CAE A SYN E 4 .   ? -15.781 -16.645 11.074  0.43 36.99  ? 503  SYN A CAE 1 
HETATM 7427 C  CAE B SYN E 4 .   ? -15.803 -20.359 13.910  0.42 39.91  ? 503  SYN A CAE 1 
HETATM 7428 C  CAG A SYN E 4 .   ? -16.394 -17.047 12.246  0.43 40.38  ? 503  SYN A CAG 1 
HETATM 7429 C  CAG B SYN E 4 .   ? -16.472 -19.556 13.002  0.42 41.24  ? 503  SYN A CAG 1 
HETATM 7430 C  CAH A SYN E 4 .   ? -17.121 -18.236 12.304  0.43 39.96  ? 503  SYN A CAH 1 
HETATM 7431 C  CAH B SYN E 4 .   ? -16.025 -18.267 12.718  0.42 38.80  ? 503  SYN A CAH 1 
HETATM 7432 C  CAB A SYN E 4 .   ? -17.770 -18.672 13.553  0.43 39.71  ? 503  SYN A CAB 1 
HETATM 7433 C  CAB B SYN E 4 .   ? -16.742 -17.414 11.752  0.42 39.19  ? 503  SYN A CAB 1 
HETATM 7434 C  CAA A SYN E 4 .   ? -18.474 -19.749 13.736  0.43 39.29  ? 503  SYN A CAA 1 
HETATM 7435 C  CAA B SYN E 4 .   ? -16.228 -16.724 10.781  0.42 37.18  ? 503  SYN A CAA 1 
HETATM 7436 C  CHA . HEM F 2 .   ? 6.134   -13.959 66.178  1.00 30.47  ? 501  HEM B CHA 1 
HETATM 7437 C  CHB . HEM F 2 .   ? 1.301   -13.572 66.013  1.00 29.10  ? 501  HEM B CHB 1 
HETATM 7438 C  CHC . HEM F 2 .   ? 1.652   -11.190 61.720  1.00 30.86  ? 501  HEM B CHC 1 
HETATM 7439 C  CHD . HEM F 2 .   ? 6.463   -11.869 61.783  1.00 31.13  ? 501  HEM B CHD 1 
HETATM 7440 C  C1A . HEM F 2 .   ? 4.795   -14.024 66.496  1.00 31.08  ? 501  HEM B C1A 1 
HETATM 7441 C  C2A . HEM F 2 .   ? 4.288   -14.602 67.702  1.00 31.70  ? 501  HEM B C2A 1 
HETATM 7442 C  C3A . HEM F 2 .   ? 2.924   -14.507 67.647  1.00 30.70  ? 501  HEM B C3A 1 
HETATM 7443 C  C4A . HEM F 2 .   ? 2.592   -13.853 66.433  1.00 32.10  ? 501  HEM B C4A 1 
HETATM 7444 C  CMA . HEM F 2 .   ? 1.921   -14.959 68.685  1.00 31.31  ? 501  HEM B CMA 1 
HETATM 7445 C  CAA . HEM F 2 .   ? 5.093   -15.219 68.831  1.00 28.12  ? 501  HEM B CAA 1 
HETATM 7446 C  CBA . HEM F 2 .   ? 5.235   -16.721 68.607  1.00 29.93  ? 501  HEM B CBA 1 
HETATM 7447 C  CGA . HEM F 2 .   ? 5.967   -17.444 69.724  1.00 28.61  ? 501  HEM B CGA 1 
HETATM 7448 O  O1A . HEM F 2 .   ? 6.312   -18.636 69.527  1.00 30.01  ? 501  HEM B O1A 1 
HETATM 7449 O  O2A . HEM F 2 .   ? 6.225   -16.894 70.827  1.00 29.56  ? 501  HEM B O2A 1 
HETATM 7450 C  C1B . HEM F 2 .   ? 0.999   -12.895 64.808  1.00 34.25  ? 501  HEM B C1B 1 
HETATM 7451 C  C2B . HEM F 2 .   ? -0.338  -12.605 64.381  1.00 31.92  ? 501  HEM B C2B 1 
HETATM 7452 C  C3B . HEM F 2 .   ? -0.249  -11.941 63.189  1.00 27.48  ? 501  HEM B C3B 1 
HETATM 7453 C  C4B . HEM F 2 .   ? 1.192   -11.832 62.876  1.00 33.17  ? 501  HEM B C4B 1 
HETATM 7454 C  CMB . HEM F 2 .   ? -1.616  -12.981 65.120  1.00 31.07  ? 501  HEM B CMB 1 
HETATM 7455 C  CAB . HEM F 2 .   ? -1.294  -11.405 62.278  1.00 30.00  ? 501  HEM B CAB 1 
HETATM 7456 C  CBB . HEM F 2 .   ? -2.450  -10.959 62.759  1.00 32.75  ? 501  HEM B CBB 1 
HETATM 7457 C  C1C . HEM F 2 .   ? 3.001   -11.145 61.352  1.00 31.27  ? 501  HEM B C1C 1 
HETATM 7458 C  C2C . HEM F 2 .   ? 3.540   -10.529 60.197  1.00 34.24  ? 501  HEM B C2C 1 
HETATM 7459 C  C3C . HEM F 2 .   ? 4.914   -10.743 60.214  1.00 30.33  ? 501  HEM B C3C 1 
HETATM 7460 C  C4C . HEM F 2 .   ? 5.196   -11.456 61.419  1.00 33.21  ? 501  HEM B C4C 1 
HETATM 7461 C  CMC . HEM F 2 .   ? 2.750   -9.815  59.122  1.00 33.60  ? 501  HEM B CMC 1 
HETATM 7462 C  CAC . HEM F 2 .   ? 5.933   -10.281 59.232  1.00 30.77  ? 501  HEM B CAC 1 
HETATM 7463 C  CBC . HEM F 2 .   ? 5.818   -9.163  58.500  1.00 34.01  ? 501  HEM B CBC 1 
HETATM 7464 C  C1D . HEM F 2 .   ? 6.715   -12.524 62.990  1.00 31.44  ? 501  HEM B C1D 1 
HETATM 7465 C  C2D . HEM F 2 .   ? 8.089   -12.927 63.363  1.00 32.45  ? 501  HEM B C2D 1 
HETATM 7466 C  C3D . HEM F 2 .   ? 7.997   -13.501 64.575  1.00 32.35  ? 501  HEM B C3D 1 
HETATM 7467 C  C4D . HEM F 2 .   ? 6.571   -13.444 64.951  1.00 31.65  ? 501  HEM B C4D 1 
HETATM 7468 C  CMD . HEM F 2 .   ? 9.360   -12.738 62.568  1.00 32.24  ? 501  HEM B CMD 1 
HETATM 7469 C  CAD . HEM F 2 .   ? 9.159   -14.025 65.403  1.00 32.14  ? 501  HEM B CAD 1 
HETATM 7470 C  CBD . HEM F 2 .   ? 9.639   -12.815 66.245  1.00 29.78  ? 501  HEM B CBD 1 
HETATM 7471 C  CGD . HEM F 2 .   ? 10.899  -13.085 67.050  1.00 33.58  ? 501  HEM B CGD 1 
HETATM 7472 O  O1D . HEM F 2 .   ? 10.873  -13.982 67.911  1.00 32.09  ? 501  HEM B O1D 1 
HETATM 7473 O  O2D . HEM F 2 .   ? 11.948  -12.415 66.866  1.00 32.33  ? 501  HEM B O2D 1 
HETATM 7474 N  NA  . HEM F 2 .   ? 3.741   -13.550 65.731  1.00 31.12  ? 501  HEM B NA  1 
HETATM 7475 N  NB  . HEM F 2 .   ? 1.849   -12.420 63.879  1.00 30.82  ? 501  HEM B NB  1 
HETATM 7476 N  NC  . HEM F 2 .   ? 4.011   -11.696 62.088  1.00 30.37  ? 501  HEM B NC  1 
HETATM 7477 N  ND  . HEM F 2 .   ? 5.838   -12.849 63.971  1.00 27.34  ? 501  HEM B ND  1 
HETATM 7478 FE FE  . HEM F 2 .   ? 3.941   -12.506 64.022  1.00 30.39  ? 501  HEM B FE  1 
HETATM 7479 C  C1  . D0L G 3 .   ? 2.053   -30.928 73.289  1.00 39.86  ? 502  D0L B C1  1 
HETATM 7480 C  C2  . D0L G 3 .   ? 2.015   -31.085 71.900  1.00 38.34  ? 502  D0L B C2  1 
HETATM 7481 C  C15 . D0L G 3 .   ? 0.260   -24.787 68.698  1.00 41.30  ? 502  D0L B C15 1 
HETATM 7482 C  C14 . D0L G 3 .   ? -0.775  -26.398 67.186  1.00 42.24  ? 502  D0L B C14 1 
HETATM 7483 C  C7  . D0L G 3 .   ? 1.366   -30.050 71.000  1.00 39.26  ? 502  D0L B C7  1 
HETATM 7484 C  C12 . D0L G 3 .   ? -1.905  -27.697 68.895  1.00 42.29  ? 502  D0L B C12 1 
HETATM 7485 C  C10 . D0L G 3 .   ? -0.100  -27.331 70.622  1.00 37.93  ? 502  D0L B C10 1 
HETATM 7486 C  C3  . D0L G 3 .   ? 2.556   -32.235 71.328  1.00 39.12  ? 502  D0L B C3  1 
HETATM 7487 C  C13 . D0L G 3 .   ? -1.566  -27.684 67.402  1.00 44.04  ? 502  D0L B C13 1 
HETATM 7488 C  C11 . D0L G 3 .   ? -0.923  -26.710 69.527  1.00 38.84  ? 502  D0L B C11 1 
HETATM 7489 C  C6  . D0L G 3 .   ? 2.629   -31.916 74.096  1.00 41.56  ? 502  D0L B C6  1 
HETATM 7490 C  C8  . D0L G 3 .   ? 1.918   -28.628 71.098  1.00 37.44  ? 502  D0L B C8  1 
HETATM 7491 C  C5  . D0L G 3 .   ? 3.174   -33.065 73.527  1.00 40.26  ? 502  D0L B C5  1 
HETATM 7492 C  C9  . D0L G 3 .   ? 3.332   -28.575 70.583  1.00 36.66  ? 502  D0L B C9  1 
HETATM 7493 C  C4  . D0L G 3 .   ? 3.131   -33.221 72.138  1.00 43.04  ? 502  D0L B C4  1 
HETATM 7494 O  O2  . D0L G 3 .   ? 4.279   -28.819 71.364  1.00 35.28  ? 502  D0L B O2  1 
HETATM 7495 O  O3  . D0L G 3 .   ? -0.506  -27.377 71.775  1.00 36.47  ? 502  D0L B O3  1 
HETATM 7496 O  O1  . D0L G 3 .   ? 3.496   -28.290 69.369  1.00 34.33  ? 502  D0L B O1  1 
HETATM 7497 N  N2  . D0L G 3 .   ? -0.047  -26.211 68.438  1.00 39.28  ? 502  D0L B N2  1 
HETATM 7498 C  C16 . D0L G 3 .   ? 1.395   -24.241 67.839  1.00 43.85  ? 502  D0L B C16 1 
HETATM 7499 C  C17 . D0L G 3 .   ? 1.177   -22.752 67.588  1.00 42.11  ? 502  D0L B C17 1 
HETATM 7500 C  C18 . D0L G 3 .   ? 2.076   -22.202 66.485  1.00 42.51  ? 502  D0L B C18 1 
HETATM 7501 C  C19 . D0L G 3 .   ? 1.338   -21.151 65.674  1.00 44.68  ? 502  D0L B C19 1 
HETATM 7502 C  C20 . D0L G 3 .   ? 2.258   -20.431 64.694  1.00 42.35  ? 502  D0L B C20 1 
HETATM 7503 C  C21 . D0L G 3 .   ? 2.707   -21.306 63.543  1.00 47.39  ? 502  D0L B C21 1 
HETATM 7504 N  N1  . D0L G 3 .   ? 1.082   -27.803 70.252  1.00 34.44  ? 502  D0L B N1  1 
HETATM 7505 C  CAF A SYN H 4 .   ? 5.712   -18.992 63.980  0.46 36.39  ? 503  SYN B CAF 1 
HETATM 7506 C  CAF B SYN H 4 .   ? 3.224   -18.343 61.705  0.39 38.43  ? 503  SYN B CAF 1 
HETATM 7507 C  CAD A SYN H 4 .   ? 5.348   -18.516 65.228  0.46 37.19  ? 503  SYN B CAD 1 
HETATM 7508 C  CAD B SYN H 4 .   ? 2.924   -19.278 60.728  0.39 37.10  ? 503  SYN B CAD 1 
HETATM 7509 C  CAC A SYN H 4 .   ? 4.769   -17.274 65.351  0.46 37.33  ? 503  SYN B CAC 1 
HETATM 7510 C  CAC B SYN H 4 .   ? 3.759   -20.351 60.515  0.39 36.14  ? 503  SYN B CAC 1 
HETATM 7511 C  CAE A SYN H 4 .   ? 4.553   -16.504 64.232  0.46 34.96  ? 503  SYN B CAE 1 
HETATM 7512 C  CAE B SYN H 4 .   ? 4.903   -20.489 61.269  0.39 38.86  ? 503  SYN B CAE 1 
HETATM 7513 C  CAG A SYN H 4 .   ? 4.916   -16.975 62.984  0.46 38.08  ? 503  SYN B CAG 1 
HETATM 7514 C  CAG B SYN H 4 .   ? 5.208   -19.557 62.245  0.39 38.84  ? 503  SYN B CAG 1 
HETATM 7515 C  CAH A SYN H 4 .   ? 5.504   -18.229 62.833  0.46 36.91  ? 503  SYN B CAH 1 
HETATM 7516 C  CAH B SYN H 4 .   ? 4.374   -18.467 62.485  0.39 38.40  ? 503  SYN B CAH 1 
HETATM 7517 C  CAB A SYN H 4 .   ? 5.891   -18.732 61.502  0.46 39.05  ? 503  SYN B CAB 1 
HETATM 7518 C  CAB B SYN H 4 .   ? 4.702   -17.479 63.529  0.39 38.27  ? 503  SYN B CAB 1 
HETATM 7519 C  CAA A SYN H 4 .   ? 6.820   -19.606 61.235  0.46 38.06  ? 503  SYN B CAA 1 
HETATM 7520 C  CAA B SYN H 4 .   ? 3.899   -17.008 64.436  0.39 36.06  ? 503  SYN B CAA 1 
HETATM 7521 C  C1  . GOL I 5 .   ? -3.029  1.072   61.578  1.00 52.81  ? 504  GOL B C1  1 
HETATM 7522 O  O1  . GOL I 5 .   ? -1.704  1.572   61.479  1.00 49.23  ? 504  GOL B O1  1 
HETATM 7523 C  C2  . GOL I 5 .   ? -3.562  1.324   63.013  1.00 56.85  ? 504  GOL B C2  1 
HETATM 7524 O  O2  . GOL I 5 .   ? -3.156  2.571   63.511  1.00 56.86  ? 504  GOL B O2  1 
HETATM 7525 C  C3  . GOL I 5 .   ? -5.110  1.229   62.864  1.00 50.14  ? 504  GOL B C3  1 
HETATM 7526 O  O3  . GOL I 5 .   ? -5.564  -0.078  63.315  1.00 41.35  ? 504  GOL B O3  1 
HETATM 7527 H  H11 . GOL I 5 .   ? -3.076  0.121   61.392  1.00 63.39  ? 504  GOL B H11 1 
HETATM 7528 H  H12 . GOL I 5 .   ? -3.629  1.496   60.945  1.00 63.39  ? 504  GOL B H12 1 
HETATM 7529 H  HO1 . GOL I 5 .   ? -1.451  1.397   60.710  1.00 59.10  ? 504  GOL B HO1 1 
HETATM 7530 H  H2  . GOL I 5 .   ? -3.219  0.664   63.635  1.00 68.24  ? 504  GOL B H2  1 
HETATM 7531 H  HO2 . GOL I 5 .   ? -2.411  2.752   63.164  1.00 68.26  ? 504  GOL B HO2 1 
HETATM 7532 H  H31 . GOL I 5 .   ? -5.334  1.406   61.937  1.00 60.19  ? 504  GOL B H31 1 
HETATM 7533 H  H32 . GOL I 5 .   ? -5.505  1.958   63.367  1.00 60.19  ? 504  GOL B H32 1 
HETATM 7534 H  HO3 . GOL I 5 .   ? -5.096  -0.654  62.896  1.00 49.65  ? 504  GOL B HO3 1 
HETATM 7535 C  C1  . GOL J 5 .   ? 3.004   -7.730  72.344  1.00 54.09  ? 505  GOL B C1  1 
HETATM 7536 O  O1  . GOL J 5 .   ? 2.108   -6.968  71.567  1.00 56.60  ? 505  GOL B O1  1 
HETATM 7537 C  C2  . GOL J 5 .   ? 2.889   -7.202  73.824  1.00 60.41  ? 505  GOL B C2  1 
HETATM 7538 O  O2  . GOL J 5 .   ? 2.134   -8.013  74.660  1.00 56.63  ? 505  GOL B O2  1 
HETATM 7539 C  C3  . GOL J 5 .   ? 4.372   -7.096  74.317  1.00 57.36  ? 505  GOL B C3  1 
HETATM 7540 O  O3  . GOL J 5 .   ? 4.653   -8.168  75.237  1.00 45.47  ? 505  GOL B O3  1 
HETATM 7541 H  H11 . GOL J 5 .   ? 3.923   -7.648  72.043  1.00 64.93  ? 505  GOL B H11 1 
HETATM 7542 H  H12 . GOL J 5 .   ? 2.802   -8.679  72.324  1.00 64.93  ? 505  GOL B H12 1 
HETATM 7543 H  HO1 . GOL J 5 .   ? 1.472   -6.770  72.082  1.00 67.94  ? 505  GOL B HO1 1 
HETATM 7544 H  H2  . GOL J 5 .   ? 2.431   -6.346  73.823  1.00 72.52  ? 505  GOL B H2  1 
HETATM 7545 H  HO2 . GOL J 5 .   ? 2.486   -8.767  74.644  1.00 67.98  ? 505  GOL B HO2 1 
HETATM 7546 H  H31 . GOL J 5 .   ? 4.495   -6.219  74.712  1.00 68.86  ? 505  GOL B H31 1 
HETATM 7547 H  H32 . GOL J 5 .   ? 4.949   -7.109  73.537  1.00 68.86  ? 505  GOL B H32 1 
HETATM 7548 H  HO3 . GOL J 5 .   ? 4.133   -8.050  75.901  1.00 54.58  ? 505  GOL B HO3 1 
HETATM 7549 C  C1  . GOL K 5 .   ? 18.505  -17.473 77.020  1.00 46.49  ? 506  GOL B C1  1 
HETATM 7550 O  O1  . GOL K 5 .   ? 19.687  -18.158 77.326  1.00 53.45  ? 506  GOL B O1  1 
HETATM 7551 C  C2  . GOL K 5 .   ? 18.043  -16.760 78.307  1.00 49.33  ? 506  GOL B C2  1 
HETATM 7552 O  O2  . GOL K 5 .   ? 19.006  -15.990 78.915  1.00 53.76  ? 506  GOL B O2  1 
HETATM 7553 C  C3  . GOL K 5 .   ? 16.865  -15.906 77.768  1.00 48.89  ? 506  GOL B C3  1 
HETATM 7554 O  O3  . GOL K 5 .   ? 16.150  -15.452 78.850  1.00 45.47  ? 506  GOL B O3  1 
HETATM 7555 H  H11 . GOL K 5 .   ? 17.801  -18.065 76.712  1.00 55.81  ? 506  GOL B H11 1 
HETATM 7556 H  H12 . GOL K 5 .   ? 18.626  -16.817 76.316  1.00 55.81  ? 506  GOL B H12 1 
HETATM 7557 H  HO1 . GOL K 5 .   ? 19.607  -18.393 78.131  1.00 64.16  ? 506  GOL B HO1 1 
HETATM 7558 H  H2  . GOL K 5 .   ? 17.800  -17.398 78.996  1.00 59.22  ? 506  GOL B H2  1 
HETATM 7559 H  HO2 . GOL K 5 .   ? 18.609  -15.456 79.429  1.00 64.54  ? 506  GOL B HO2 1 
HETATM 7560 H  H31 . GOL K 5 .   ? 16.338  -16.451 77.163  1.00 58.69  ? 506  GOL B H31 1 
HETATM 7561 H  H32 . GOL K 5 .   ? 17.226  -15.191 77.221  1.00 58.69  ? 506  GOL B H32 1 
HETATM 7562 H  HO3 . GOL K 5 .   ? 15.738  -16.126 79.158  1.00 54.59  ? 506  GOL B HO3 1 
HETATM 7563 O  O   . HOH L 6 .   ? -16.419 -6.964  6.397   1.00 41.29  ? 601  HOH A O   1 
HETATM 7564 O  O   . HOH L 6 .   ? -8.621  9.716   26.157  1.00 48.54  ? 602  HOH A O   1 
HETATM 7565 O  O   . HOH L 6 .   ? -27.439 -23.273 -14.402 1.00 49.58  ? 603  HOH A O   1 
HETATM 7566 O  O   . HOH L 6 .   ? -11.268 1.687   14.185  1.00 46.41  ? 604  HOH A O   1 
HETATM 7567 O  O   . HOH L 6 .   ? -16.609 -26.819 -0.934  1.00 40.16  ? 605  HOH A O   1 
HETATM 7568 O  O   . HOH L 6 .   ? -4.742  -22.034 -17.222 1.00 63.70  ? 606  HOH A O   1 
HETATM 7569 O  O   . HOH L 6 .   ? -10.186 -14.239 -14.393 1.00 43.20  ? 607  HOH A O   1 
HETATM 7570 O  O   . HOH L 6 .   ? -18.733 -29.928 -12.731 1.00 49.22  ? 608  HOH A O   1 
HETATM 7571 O  O   . HOH L 6 .   ? -14.222 0.312   33.026  1.00 48.04  ? 609  HOH A O   1 
HETATM 7572 O  O   . HOH L 6 .   ? 5.283   -17.563 -0.575  1.00 47.21  ? 610  HOH A O   1 
HETATM 7573 O  O   . HOH L 6 .   ? 11.458  -16.120 31.142  1.00 52.81  ? 611  HOH A O   1 
HETATM 7574 O  O   . HOH L 6 .   ? -13.107 2.206   30.247  1.00 44.31  ? 612  HOH A O   1 
HETATM 7575 O  O   . HOH L 6 .   ? -23.518 -27.593 -3.689  1.00 51.88  ? 613  HOH A O   1 
HETATM 7576 O  O   . HOH L 6 .   ? -12.731 -9.459  10.283  1.00 40.27  ? 614  HOH A O   1 
HETATM 7577 O  O   . HOH L 6 .   ? 9.359   -0.004  21.219  1.00 46.66  ? 615  HOH A O   1 
HETATM 7578 O  O   . HOH L 6 .   ? -15.354 -34.971 5.807   1.00 50.73  ? 616  HOH A O   1 
HETATM 7579 O  O   . HOH L 6 .   ? -20.340 -15.471 6.452   1.00 28.58  ? 617  HOH A O   1 
HETATM 7580 O  O   . HOH L 6 .   ? -4.604  -22.932 -14.455 1.00 47.83  ? 618  HOH A O   1 
HETATM 7581 O  O   . HOH L 6 .   ? -22.970 -29.411 -8.862  1.00 49.57  ? 619  HOH A O   1 
HETATM 7582 O  O   . HOH L 6 .   ? 1.450   1.822   33.006  1.00 47.11  ? 620  HOH A O   1 
HETATM 7583 O  O   . HOH L 6 .   ? 7.487   7.839   12.632  1.00 55.70  ? 621  HOH A O   1 
HETATM 7584 O  O   . HOH L 6 .   ? -22.484 -6.988  -1.624  1.00 47.42  ? 622  HOH A O   1 
HETATM 7585 O  O   . HOH L 6 .   ? -12.443 -12.643 16.354  1.00 37.88  ? 623  HOH A O   1 
HETATM 7586 O  O   . HOH L 6 .   ? -23.817 -10.022 8.411   1.00 40.11  ? 624  HOH A O   1 
HETATM 7587 O  O   . HOH L 6 .   ? 11.615  5.800   17.852  1.00 56.84  ? 625  HOH A O   1 
HETATM 7588 O  O   . HOH L 6 .   ? 0.706   -21.658 23.026  1.00 39.49  ? 626  HOH A O   1 
HETATM 7589 O  O   . HOH L 6 .   ? -30.499 -4.883  26.845  1.00 59.60  ? 627  HOH A O   1 
HETATM 7590 O  O   . HOH L 6 .   ? -22.197 -17.272 -15.729 1.00 49.62  ? 628  HOH A O   1 
HETATM 7591 O  O   . HOH L 6 .   ? -10.869 -7.324  2.013   1.00 45.50  ? 629  HOH A O   1 
HETATM 7592 O  O   . HOH L 6 .   ? 9.833   -17.748 12.802  1.00 41.08  ? 630  HOH A O   1 
HETATM 7593 O  O   . HOH L 6 .   ? -6.097  -10.974 -12.366 1.00 44.07  ? 631  HOH A O   1 
HETATM 7594 O  O   . HOH L 6 .   ? -3.574  -25.546 -10.934 1.00 36.58  ? 632  HOH A O   1 
HETATM 7595 O  O   . HOH L 6 .   ? -13.880 -9.845  31.880  1.00 32.77  ? 633  HOH A O   1 
HETATM 7596 O  O   . HOH L 6 .   ? -8.290  -35.910 -11.405 1.00 55.02  ? 634  HOH A O   1 
HETATM 7597 O  O   . HOH L 6 .   ? -34.452 -9.377  17.509  1.00 38.74  ? 635  HOH A O   1 
HETATM 7598 O  O   . HOH L 6 .   ? 10.857  -15.298 21.991  1.00 34.49  ? 636  HOH A O   1 
HETATM 7599 O  O   . HOH L 6 .   ? 4.184   1.724   30.639  1.00 39.84  ? 637  HOH A O   1 
HETATM 7600 O  O   . HOH L 6 .   ? -15.557 2.328   13.391  1.00 58.78  ? 638  HOH A O   1 
HETATM 7601 O  O   . HOH L 6 .   ? -33.903 -7.260  3.615   1.00 48.11  ? 639  HOH A O   1 
HETATM 7602 O  O   . HOH L 6 .   ? -29.078 -18.749 -7.074  1.00 48.10  ? 640  HOH A O   1 
HETATM 7603 O  O   . HOH L 6 .   ? -14.217 -14.672 13.389  1.00 36.64  ? 641  HOH A O   1 
HETATM 7604 O  O   . HOH L 6 .   ? 6.129   -2.216  35.078  1.00 40.93  ? 642  HOH A O   1 
HETATM 7605 O  O   . HOH L 6 .   ? -24.745 -29.221 10.275  1.00 46.77  ? 643  HOH A O   1 
HETATM 7606 O  O   . HOH L 6 .   ? 1.932   9.269   24.131  1.00 45.11  ? 644  HOH A O   1 
HETATM 7607 O  O   . HOH L 6 .   ? -8.611  13.278  24.409  1.00 53.07  ? 645  HOH A O   1 
HETATM 7608 O  O   . HOH L 6 .   ? -32.031 -14.863 4.240   1.00 36.26  ? 646  HOH A O   1 
HETATM 7609 O  O   . HOH L 6 .   ? -33.101 -21.509 9.638   1.00 43.50  ? 647  HOH A O   1 
HETATM 7610 O  O   . HOH L 6 .   ? -4.843  2.204   8.372   1.00 40.01  ? 648  HOH A O   1 
HETATM 7611 O  O   . HOH L 6 .   ? 6.473   -14.728 5.776   1.00 48.43  ? 649  HOH A O   1 
HETATM 7612 O  O   . HOH L 6 .   ? -14.979 -17.330 -17.804 1.00 47.65  ? 650  HOH A O   1 
HETATM 7613 O  O   . HOH L 6 .   ? -3.825  -40.034 -7.145  1.00 36.65  ? 651  HOH A O   1 
HETATM 7614 O  O   . HOH L 6 .   ? -7.750  -6.997  40.345  1.00 34.35  ? 652  HOH A O   1 
HETATM 7615 O  O   . HOH L 6 .   ? -23.019 -19.224 -11.668 1.00 43.20  ? 653  HOH A O   1 
HETATM 7616 O  O   . HOH L 6 .   ? -10.288 -10.324 33.123  1.00 30.67  ? 654  HOH A O   1 
HETATM 7617 O  O   . HOH L 6 .   ? 14.123  -10.614 12.545  1.00 44.53  ? 655  HOH A O   1 
HETATM 7618 O  O   . HOH L 6 .   ? -3.586  -14.099 -10.206 1.00 35.23  ? 656  HOH A O   1 
HETATM 7619 O  O   . HOH L 6 .   ? -13.092 -9.647  20.944  1.00 31.90  ? 657  HOH A O   1 
HETATM 7620 O  O   . HOH L 6 .   ? -10.003 10.473  14.613  1.00 46.30  ? 658  HOH A O   1 
HETATM 7621 O  O   . HOH L 6 .   ? -29.712 -10.659 0.643   1.00 50.68  ? 659  HOH A O   1 
HETATM 7622 O  O   . HOH L 6 .   ? -15.799 -10.200 29.787  1.00 31.46  ? 660  HOH A O   1 
HETATM 7623 O  O   . HOH L 6 .   ? -9.593  -1.751  33.425  1.00 40.10  ? 661  HOH A O   1 
HETATM 7624 O  O   . HOH L 6 .   ? -8.222  -2.438  -2.447  1.00 42.37  ? 662  HOH A O   1 
HETATM 7625 O  O   . HOH L 6 .   ? 3.273   4.997   5.988   1.00 55.75  ? 663  HOH A O   1 
HETATM 7626 O  O   . HOH L 6 .   ? -21.865 3.777   10.969  1.00 46.10  ? 664  HOH A O   1 
HETATM 7627 O  O   . HOH L 6 .   ? -7.778  -1.990  35.644  1.00 42.01  ? 665  HOH A O   1 
HETATM 7628 O  O   . HOH L 6 .   ? 5.409   -20.438 28.841  1.00 48.47  ? 666  HOH A O   1 
HETATM 7629 O  O   . HOH L 6 .   ? -9.542  12.355  22.080  1.00 43.77  ? 667  HOH A O   1 
HETATM 7630 O  O   . HOH L 6 .   ? -35.199 -10.557 6.369   1.00 38.67  ? 668  HOH A O   1 
HETATM 7631 O  O   . HOH L 6 .   ? -13.323 -2.634  35.594  1.00 37.46  ? 669  HOH A O   1 
HETATM 7632 O  O   . HOH L 6 .   ? -2.471  -27.738 14.838  1.00 34.99  ? 670  HOH A O   1 
HETATM 7633 O  O   . HOH L 6 .   ? -8.509  -15.087 -16.572 1.00 51.61  ? 671  HOH A O   1 
HETATM 7634 O  O   . HOH L 6 .   ? -36.092 -10.935 20.092  1.00 43.40  ? 672  HOH A O   1 
HETATM 7635 O  O   . HOH L 6 .   ? 11.144  -5.719  19.396  1.00 48.67  ? 673  HOH A O   1 
HETATM 7636 O  O   . HOH L 6 .   ? -29.920 -3.172  9.203   1.00 49.54  ? 674  HOH A O   1 
HETATM 7637 O  O   . HOH L 6 .   ? -18.699 -29.530 -5.993  1.00 39.75  ? 675  HOH A O   1 
HETATM 7638 O  O   . HOH L 6 .   ? -2.490  4.672   27.551  1.00 41.50  ? 676  HOH A O   1 
HETATM 7639 O  O   . HOH L 6 .   ? -1.217  -22.851 26.260  1.00 52.79  ? 677  HOH A O   1 
HETATM 7640 O  O   . HOH L 6 .   ? -34.855 -17.450 0.755   1.00 47.82  ? 678  HOH A O   1 
HETATM 7641 O  O   . HOH L 6 .   ? 10.342  5.259   12.064  1.00 59.15  ? 679  HOH A O   1 
HETATM 7642 O  O   . HOH L 6 .   ? -3.691  -11.594 -3.643  1.00 34.56  ? 680  HOH A O   1 
HETATM 7643 O  O   . HOH L 6 .   ? -2.370  8.929   34.863  1.00 57.78  ? 681  HOH A O   1 
HETATM 7644 O  O   . HOH L 6 .   ? -21.413 7.969   15.327  1.00 56.53  ? 682  HOH A O   1 
HETATM 7645 O  O   . HOH L 6 .   ? -2.995  -11.355 -11.231 1.00 47.46  ? 683  HOH A O   1 
HETATM 7646 O  O   . HOH L 6 .   ? 8.454   -1.433  6.195   1.00 50.06  ? 684  HOH A O   1 
HETATM 7647 O  O   . HOH L 6 .   ? 3.594   -23.251 7.743   1.00 46.32  ? 685  HOH A O   1 
HETATM 7648 O  O   . HOH L 6 .   ? -9.063  -4.711  6.349   1.00 40.99  ? 686  HOH A O   1 
HETATM 7649 O  O   . HOH L 6 .   ? 11.053  -7.713  38.791  1.00 56.61  ? 687  HOH A O   1 
HETATM 7650 O  O   . HOH L 6 .   ? -39.723 -14.077 16.193  1.00 46.75  ? 688  HOH A O   1 
HETATM 7651 O  O   . HOH L 6 .   ? -42.762 -7.819  15.324  1.00 46.50  ? 689  HOH A O   1 
HETATM 7652 O  O   . HOH L 6 .   ? 2.591   -19.005 24.097  1.00 37.57  ? 690  HOH A O   1 
HETATM 7653 O  O   . HOH L 6 .   ? -4.437  -0.422  6.233   1.00 43.95  ? 691  HOH A O   1 
HETATM 7654 O  O   . HOH L 6 .   ? -5.121  0.865   3.964   1.00 55.27  ? 692  HOH A O   1 
HETATM 7655 O  O   . HOH L 6 .   ? -13.349 -43.274 9.995   1.00 65.77  ? 693  HOH A O   1 
HETATM 7656 O  O   . HOH L 6 .   ? -7.275  -20.217 22.045  1.00 50.72  ? 694  HOH A O   1 
HETATM 7657 O  O   . HOH L 6 .   ? -25.982 -24.916 20.579  1.00 47.07  ? 695  HOH A O   1 
HETATM 7658 O  O   . HOH L 6 .   ? -4.409  8.543   24.576  1.00 38.54  ? 696  HOH A O   1 
HETATM 7659 O  O   . HOH L 6 .   ? -7.088  0.425   12.303  1.00 41.93  ? 697  HOH A O   1 
HETATM 7660 O  O   . HOH L 6 .   ? -25.869 -19.775 1.004   1.00 32.89  ? 698  HOH A O   1 
HETATM 7661 O  O   . HOH L 6 .   ? -21.886 1.948   25.854  1.00 54.86  ? 699  HOH A O   1 
HETATM 7662 O  O   . HOH L 6 .   ? -15.961 -22.331 5.090   1.00 33.79  ? 700  HOH A O   1 
HETATM 7663 O  O   . HOH L 6 .   ? -23.278 -19.036 13.142  1.00 33.02  ? 701  HOH A O   1 
HETATM 7664 O  O   . HOH L 6 .   ? -7.516  -25.519 10.234  1.00 34.92  ? 702  HOH A O   1 
HETATM 7665 O  O   . HOH L 6 .   ? 1.799   -8.769  -12.182 1.00 53.46  ? 703  HOH A O   1 
HETATM 7666 O  O   . HOH L 6 .   ? 6.420   9.520   18.433  1.00 42.67  ? 704  HOH A O   1 
HETATM 7667 O  O   . HOH L 6 .   ? -20.500 -4.758  9.806   1.00 44.93  ? 705  HOH A O   1 
HETATM 7668 O  O   . HOH L 6 .   ? -6.735  -4.856  36.484  1.00 35.80  ? 706  HOH A O   1 
HETATM 7669 O  O   . HOH L 6 .   ? -18.359 0.654   26.560  1.00 38.34  ? 707  HOH A O   1 
HETATM 7670 O  O   . HOH L 6 .   ? -25.109 -14.197 -4.011  1.00 34.73  ? 708  HOH A O   1 
HETATM 7671 O  O   . HOH L 6 .   ? -14.003 -27.289 -14.090 1.00 43.21  ? 709  HOH A O   1 
HETATM 7672 O  O   . HOH L 6 .   ? -3.231  -12.478 11.424  1.00 34.76  ? 710  HOH A O   1 
HETATM 7673 O  O   . HOH L 6 .   ? 1.096   -26.141 16.510  1.00 44.70  ? 711  HOH A O   1 
HETATM 7674 O  O   . HOH L 6 .   ? 3.422   -24.352 11.595  1.00 34.80  ? 712  HOH A O   1 
HETATM 7675 O  O   . HOH L 6 .   ? 4.440   -16.629 -3.317  1.00 45.36  ? 713  HOH A O   1 
HETATM 7676 O  O   . HOH L 6 .   ? -13.308 -14.989 -17.355 1.00 50.56  ? 714  HOH A O   1 
HETATM 7677 O  O   . HOH L 6 .   ? -17.935 -20.597 3.681   1.00 29.20  ? 715  HOH A O   1 
HETATM 7678 O  O   . HOH L 6 .   ? 4.899   -17.979 5.061   1.00 45.33  ? 716  HOH A O   1 
HETATM 7679 O  O   . HOH L 6 .   ? -0.168  -28.436 -11.722 1.00 49.92  ? 717  HOH A O   1 
HETATM 7680 O  O   . HOH L 6 .   ? -4.950  -23.837 -5.388  1.00 35.32  ? 718  HOH A O   1 
HETATM 7681 O  O   . HOH L 6 .   ? 4.265   -26.920 4.974   1.00 52.87  ? 719  HOH A O   1 
HETATM 7682 O  O   . HOH L 6 .   ? -21.995 -13.093 -0.626  1.00 33.99  ? 720  HOH A O   1 
HETATM 7683 O  O   . HOH L 6 .   ? 2.989   -13.982 31.842  1.00 39.67  ? 721  HOH A O   1 
HETATM 7684 O  O   . HOH L 6 .   ? -0.810  0.577   -1.530  1.00 47.53  ? 722  HOH A O   1 
HETATM 7685 O  O   . HOH L 6 .   ? -7.147  -7.965  35.684  1.00 31.90  ? 723  HOH A O   1 
HETATM 7686 O  O   . HOH L 6 .   ? -37.395 -16.613 11.794  1.00 43.48  ? 724  HOH A O   1 
HETATM 7687 O  O   . HOH L 6 .   ? 9.324   -4.050  6.108   1.00 47.68  ? 725  HOH A O   1 
HETATM 7688 O  O   . HOH L 6 .   ? -24.283 -12.718 -13.719 1.00 43.75  ? 726  HOH A O   1 
HETATM 7689 O  O   . HOH L 6 .   ? -6.538  -43.931 -5.591  1.00 36.05  ? 727  HOH A O   1 
HETATM 7690 O  O   . HOH L 6 .   ? -6.514  -2.769  9.945   1.00 43.88  ? 728  HOH A O   1 
HETATM 7691 O  O   . HOH L 6 .   ? -26.157 -28.658 -11.746 1.00 48.56  ? 729  HOH A O   1 
HETATM 7692 O  O   . HOH L 6 .   ? 2.509   -24.858 4.156   1.00 45.38  ? 730  HOH A O   1 
HETATM 7693 O  O   . HOH L 6 .   ? 5.755   4.129   21.964  1.00 41.83  ? 731  HOH A O   1 
HETATM 7694 O  O   . HOH L 6 .   ? 0.724   -31.069 1.679   1.00 36.55  ? 732  HOH A O   1 
HETATM 7695 O  O   . HOH L 6 .   ? -17.818 -14.432 3.060   1.00 33.33  ? 733  HOH A O   1 
HETATM 7696 O  O   . HOH L 6 .   ? -9.187  -14.511 7.742   1.00 33.29  ? 734  HOH A O   1 
HETATM 7697 O  O   . HOH L 6 .   ? -0.289  -16.691 30.422  1.00 40.48  ? 735  HOH A O   1 
HETATM 7698 O  O   . HOH L 6 .   ? -13.853 -4.479  -5.273  1.00 39.33  ? 736  HOH A O   1 
HETATM 7699 O  O   . HOH L 6 .   ? -33.056 -20.981 15.203  1.00 41.72  ? 737  HOH A O   1 
HETATM 7700 O  O   . HOH L 6 .   ? 6.982   -0.218  21.547  1.00 40.51  ? 738  HOH A O   1 
HETATM 7701 O  O   . HOH L 6 .   ? -9.470  -27.569 25.459  1.00 56.35  ? 739  HOH A O   1 
HETATM 7702 O  O   . HOH L 6 .   ? -13.253 -8.248  33.910  1.00 32.89  ? 740  HOH A O   1 
HETATM 7703 O  O   . HOH L 6 .   ? -25.568 -10.488 30.520  1.00 52.21  ? 741  HOH A O   1 
HETATM 7704 O  O   . HOH L 6 .   ? 8.451   -22.974 18.046  1.00 41.75  ? 742  HOH A O   1 
HETATM 7705 O  O   . HOH L 6 .   ? -17.433 -12.218 -12.745 1.00 47.73  ? 743  HOH A O   1 
HETATM 7706 O  O   . HOH L 6 .   ? -5.167  -2.104  40.030  1.00 41.52  ? 744  HOH A O   1 
HETATM 7707 O  O   . HOH L 6 .   ? -27.284 -15.913 -3.869  1.00 42.52  ? 745  HOH A O   1 
HETATM 7708 O  O   . HOH L 6 .   ? -35.155 -19.888 15.113  1.00 45.25  ? 746  HOH A O   1 
HETATM 7709 O  O   . HOH L 6 .   ? -18.897 -31.228 -8.676  1.00 47.97  ? 747  HOH A O   1 
HETATM 7710 O  O   . HOH L 6 .   ? -32.013 -3.982  15.366  1.00 45.16  ? 748  HOH A O   1 
HETATM 7711 O  O   . HOH L 6 .   ? -17.532 4.113   25.033  1.00 36.85  ? 749  HOH A O   1 
HETATM 7712 O  O   . HOH L 6 .   ? -2.177  -21.254 20.033  1.00 39.88  ? 750  HOH A O   1 
HETATM 7713 O  O   . HOH L 6 .   ? 9.197   -13.003 -0.800  1.00 44.72  ? 751  HOH A O   1 
HETATM 7714 O  O   . HOH L 6 .   ? -8.424  -22.038 19.140  1.00 43.96  ? 752  HOH A O   1 
HETATM 7715 O  O   . HOH L 6 .   ? 7.672   -16.217 9.465   1.00 50.76  ? 753  HOH A O   1 
HETATM 7716 O  O   . HOH L 6 .   ? -16.157 -6.861  -7.593  1.00 40.53  ? 754  HOH A O   1 
HETATM 7717 O  O   . HOH L 6 .   ? -18.521 -17.990 1.807   1.00 30.17  ? 755  HOH A O   1 
HETATM 7718 O  O   . HOH L 6 .   ? 13.913  -8.912  20.145  1.00 40.05  ? 756  HOH A O   1 
HETATM 7719 O  O   . HOH L 6 .   ? 1.682   -40.348 0.803   1.00 42.87  ? 757  HOH A O   1 
HETATM 7720 O  O   . HOH L 6 .   ? -3.846  12.554  19.526  1.00 40.65  ? 758  HOH A O   1 
HETATM 7721 O  O   . HOH L 6 .   ? 1.314   -14.468 29.799  1.00 35.57  ? 759  HOH A O   1 
HETATM 7722 O  O   . HOH L 6 .   ? -29.541 -20.945 -3.822  1.00 47.53  ? 760  HOH A O   1 
HETATM 7723 O  O   . HOH L 6 .   ? 8.995   -11.238 9.174   1.00 39.46  ? 761  HOH A O   1 
HETATM 7724 O  O   . HOH L 6 .   ? -22.655 -0.335  23.963  1.00 49.81  ? 762  HOH A O   1 
HETATM 7725 O  O   . HOH L 6 .   ? -35.464 -16.002 27.139  1.00 68.90  ? 763  HOH A O   1 
HETATM 7726 O  O   . HOH L 6 .   ? 2.452   -21.255 0.622   1.00 45.98  ? 764  HOH A O   1 
HETATM 7727 O  O   . HOH L 6 .   ? 12.798  -7.325  18.128  1.00 42.32  ? 765  HOH A O   1 
HETATM 7728 O  O   . HOH L 6 .   ? -27.482 -7.882  1.714   1.00 48.97  ? 766  HOH A O   1 
HETATM 7729 O  O   . HOH L 6 .   ? -14.153 -28.918 -11.931 1.00 44.67  ? 767  HOH A O   1 
HETATM 7730 O  O   . HOH L 6 .   ? -6.978  0.172   36.607  1.00 53.43  ? 768  HOH A O   1 
HETATM 7731 O  O   . HOH L 6 .   ? -19.498 -14.736 -4.382  1.00 34.91  ? 769  HOH A O   1 
HETATM 7732 O  O   . HOH L 6 .   ? 4.642   -9.284  -9.804  1.00 53.91  ? 770  HOH A O   1 
HETATM 7733 O  O   . HOH L 6 .   ? -35.480 -13.076 6.148   1.00 39.69  ? 771  HOH A O   1 
HETATM 7734 O  O   . HOH L 6 .   ? 6.741   -5.564  37.935  1.00 47.36  ? 772  HOH A O   1 
HETATM 7735 O  O   . HOH L 6 .   ? -4.726  -37.670 -8.122  1.00 45.08  ? 773  HOH A O   1 
HETATM 7736 O  O   . HOH L 6 .   ? -37.219 -20.210 19.769  1.00 49.12  ? 774  HOH A O   1 
HETATM 7737 O  O   . HOH L 6 .   ? 2.999   -5.433  -2.515  1.00 41.74  ? 775  HOH A O   1 
HETATM 7738 O  O   . HOH L 6 .   ? -1.356  -22.268 -11.495 1.00 47.20  ? 776  HOH A O   1 
HETATM 7739 O  O   . HOH L 6 .   ? 12.014  -1.435  17.368  1.00 42.64  ? 777  HOH A O   1 
HETATM 7740 O  O   . HOH L 6 .   ? -17.900 -29.118 -15.045 1.00 46.25  ? 778  HOH A O   1 
HETATM 7741 O  O   . HOH L 6 .   ? -0.382  -16.019 33.181  1.00 44.71  ? 779  HOH A O   1 
HETATM 7742 O  O   . HOH L 6 .   ? -16.482 -15.008 35.139  1.00 43.40  ? 780  HOH A O   1 
HETATM 7743 O  O   . HOH L 6 .   ? -15.225 -31.453 21.586  1.00 56.32  ? 781  HOH A O   1 
HETATM 7744 O  O   . HOH L 6 .   ? -20.277 -24.624 -17.257 1.00 50.51  ? 782  HOH A O   1 
HETATM 7745 O  O   . HOH L 6 .   ? 9.797   -9.001  6.608   1.00 39.58  ? 783  HOH A O   1 
HETATM 7746 O  O   . HOH L 6 .   ? 18.344  -18.901 17.720  1.00 49.18  ? 784  HOH A O   1 
HETATM 7747 O  O   . HOH L 6 .   ? -7.522  -46.264 1.277   1.00 50.22  ? 785  HOH A O   1 
HETATM 7748 O  O   . HOH L 6 .   ? -17.724 -8.986  -3.835  1.00 42.43  ? 786  HOH A O   1 
HETATM 7749 O  O   . HOH L 6 .   ? -26.588 -6.055  3.551   1.00 56.10  ? 787  HOH A O   1 
HETATM 7750 O  O   . HOH L 6 .   ? -26.405 -27.913 -14.235 1.00 50.52  ? 788  HOH A O   1 
HETATM 7751 O  O   . HOH L 6 .   ? 5.056   6.588   12.656  1.00 47.41  ? 789  HOH A O   1 
HETATM 7752 O  O   . HOH L 6 .   ? 3.821   -13.453 37.599  1.00 47.26  ? 790  HOH A O   1 
HETATM 7753 O  O   . HOH L 6 .   ? 2.659   -16.586 -6.836  1.00 42.27  ? 791  HOH A O   1 
HETATM 7754 O  O   . HOH L 6 .   ? 1.602   -35.750 2.073   1.00 50.25  ? 792  HOH A O   1 
HETATM 7755 O  O   . HOH L 6 .   ? -22.419 -3.989  27.456  1.00 45.69  ? 793  HOH A O   1 
HETATM 7756 O  O   . HOH L 6 .   ? -10.105 -4.630  24.294  1.00 34.53  ? 794  HOH A O   1 
HETATM 7757 O  O   . HOH L 6 .   ? -12.533 -0.333  13.216  1.00 45.46  ? 795  HOH A O   1 
HETATM 7758 O  O   . HOH L 6 .   ? -12.277 -9.614  3.005   1.00 32.34  ? 796  HOH A O   1 
HETATM 7759 O  O   . HOH L 6 .   ? -11.808 -5.878  -3.861  1.00 34.35  ? 797  HOH A O   1 
HETATM 7760 O  O   . HOH L 6 .   ? -28.660 -15.883 11.285  1.00 32.12  ? 798  HOH A O   1 
HETATM 7761 O  O   . HOH L 6 .   ? 16.056  -12.312 19.048  1.00 45.18  ? 799  HOH A O   1 
HETATM 7762 O  O   . HOH L 6 .   ? -8.946  -4.794  -3.574  1.00 40.24  ? 800  HOH A O   1 
HETATM 7763 O  O   . HOH L 6 .   ? -22.571 0.407   21.517  1.00 42.41  ? 801  HOH A O   1 
HETATM 7764 O  O   . HOH L 6 .   ? -18.696 -2.734  33.945  1.00 51.39  ? 802  HOH A O   1 
HETATM 7765 O  O   . HOH L 6 .   ? -7.353  -17.291 15.291  1.00 39.90  ? 803  HOH A O   1 
HETATM 7766 O  O   . HOH L 6 .   ? 7.718   -9.532  30.222  1.00 40.85  ? 804  HOH A O   1 
HETATM 7767 O  O   . HOH L 6 .   ? -6.052  -18.017 27.284  1.00 43.54  ? 805  HOH A O   1 
HETATM 7768 O  O   . HOH L 6 .   ? 5.348   5.731   24.392  1.00 38.48  ? 806  HOH A O   1 
HETATM 7769 O  O   . HOH L 6 .   ? -11.075 -32.041 20.586  1.00 61.03  ? 807  HOH A O   1 
HETATM 7770 O  O   . HOH L 6 .   ? 10.470  -20.374 21.708  1.00 43.66  ? 808  HOH A O   1 
HETATM 7771 O  O   . HOH L 6 .   ? -12.322 -28.359 -16.140 1.00 51.88  ? 809  HOH A O   1 
HETATM 7772 O  O   . HOH L 6 .   ? 8.763   -7.243  40.390  1.00 52.02  ? 810  HOH A O   1 
HETATM 7773 O  O   . HOH L 6 .   ? -20.440 -9.290  -6.798  1.00 39.39  ? 811  HOH A O   1 
HETATM 7774 O  O   . HOH L 6 .   ? -16.518 6.790   22.367  1.00 42.39  ? 812  HOH A O   1 
HETATM 7775 O  O   . HOH L 6 .   ? -41.006 -5.439  4.253   1.00 56.40  ? 813  HOH A O   1 
HETATM 7776 O  O   . HOH L 6 .   ? -34.607 -22.104 12.679  1.00 47.91  ? 814  HOH A O   1 
HETATM 7777 O  O   . HOH L 6 .   ? -35.916 -2.504  15.947  1.00 51.49  ? 815  HOH A O   1 
HETATM 7778 O  O   . HOH L 6 .   ? -1.243  -34.082 4.364   1.00 43.91  ? 816  HOH A O   1 
HETATM 7779 O  O   . HOH L 6 .   ? 0.716   -10.146 36.272  1.00 35.15  ? 817  HOH A O   1 
HETATM 7780 O  O   . HOH L 6 .   ? -19.741 -14.189 -1.618  1.00 32.10  ? 818  HOH A O   1 
HETATM 7781 O  O   . HOH L 6 .   ? -8.386  -5.417  -10.368 1.00 33.25  ? 819  HOH A O   1 
HETATM 7782 O  O   . HOH L 6 .   ? 10.776  -21.474 19.006  1.00 43.52  ? 820  HOH A O   1 
HETATM 7783 O  O   . HOH L 6 .   ? -19.342 -28.563 1.774   1.00 44.29  ? 821  HOH A O   1 
HETATM 7784 O  O   . HOH L 6 .   ? 6.147   -25.809 -0.523  1.00 58.28  ? 822  HOH A O   1 
HETATM 7785 O  O   . HOH L 6 .   ? 10.431  -2.869  21.350  1.00 43.63  ? 823  HOH A O   1 
HETATM 7786 O  O   . HOH L 6 .   ? -2.983  -33.833 -11.166 1.00 44.33  ? 824  HOH A O   1 
HETATM 7787 O  O   . HOH L 6 .   ? -44.909 -13.314 11.707  1.00 49.81  ? 825  HOH A O   1 
HETATM 7788 O  O   . HOH L 6 .   ? -17.269 -33.320 3.238   1.00 47.54  ? 826  HOH A O   1 
HETATM 7789 O  O   . HOH L 6 .   ? -5.934  13.632  21.075  1.00 45.45  ? 827  HOH A O   1 
HETATM 7790 O  O   . HOH L 6 .   ? -5.504  -22.235 16.467  1.00 36.45  ? 828  HOH A O   1 
HETATM 7791 O  O   . HOH L 6 .   ? -0.455  -1.460  -8.489  1.00 57.87  ? 829  HOH A O   1 
HETATM 7792 O  O   . HOH L 6 .   ? -24.236 -14.036 -1.510  1.00 36.67  ? 830  HOH A O   1 
HETATM 7793 O  O   . HOH L 6 .   ? 11.149  -18.043 28.174  1.00 52.97  ? 831  HOH A O   1 
HETATM 7794 O  O   . HOH L 6 .   ? -13.958 7.930   23.229  1.00 45.02  ? 832  HOH A O   1 
HETATM 7795 O  O   . HOH L 6 .   ? -0.324  -16.635 -9.324  1.00 54.78  ? 833  HOH A O   1 
HETATM 7796 O  O   . HOH L 6 .   ? 5.258   -16.256 8.000   1.00 45.31  ? 834  HOH A O   1 
HETATM 7797 O  O   . HOH L 6 .   ? 13.985  -14.928 13.546  1.00 48.26  ? 835  HOH A O   1 
HETATM 7798 O  O   . HOH L 6 .   ? -15.435 -20.223 6.449   1.00 33.77  ? 836  HOH A O   1 
HETATM 7799 O  O   . HOH L 6 .   ? 0.880   -29.363 7.348   1.00 45.00  ? 837  HOH A O   1 
HETATM 7800 O  O   . HOH L 6 .   ? -15.992 -31.268 -11.993 1.00 48.36  ? 838  HOH A O   1 
HETATM 7801 O  O   . HOH L 6 .   ? -27.572 -27.640 -16.926 1.00 62.05  ? 839  HOH A O   1 
HETATM 7802 O  O   . HOH L 6 .   ? -1.034  -17.508 -5.123  1.00 46.86  ? 840  HOH A O   1 
HETATM 7803 O  O   . HOH L 6 .   ? 13.660  -18.792 14.805  1.00 46.33  ? 841  HOH A O   1 
HETATM 7804 O  O   . HOH L 6 .   ? 10.992  -8.223  31.449  1.00 49.37  ? 842  HOH A O   1 
HETATM 7805 O  O   . HOH L 6 .   ? -9.379  -7.193  -2.003  1.00 38.68  ? 843  HOH A O   1 
HETATM 7806 O  O   . HOH L 6 .   ? -34.453 -19.729 8.835   1.00 40.55  ? 844  HOH A O   1 
HETATM 7807 O  O   . HOH L 6 .   ? -16.017 -10.435 -10.677 1.00 47.68  ? 845  HOH A O   1 
HETATM 7808 O  O   . HOH L 6 .   ? 2.437   -18.236 -4.147  1.00 53.58  ? 846  HOH A O   1 
HETATM 7809 O  O   . HOH L 6 .   ? 5.070   -29.060 12.958  1.00 59.32  ? 847  HOH A O   1 
HETATM 7810 O  O   . HOH L 6 .   ? -27.779 -27.428 6.145   1.00 43.72  ? 848  HOH A O   1 
HETATM 7811 O  O   . HOH L 6 .   ? -16.226 -8.170  -0.191  1.00 43.47  ? 849  HOH A O   1 
HETATM 7812 O  O   . HOH L 6 .   ? -19.068 -6.481  1.587   1.00 51.89  ? 850  HOH A O   1 
HETATM 7813 O  O   . HOH L 6 .   ? 8.172   4.614   4.808   1.00 64.76  ? 851  HOH A O   1 
HETATM 7814 O  O   . HOH L 6 .   ? -35.658 -15.881 14.541  1.00 42.51  ? 852  HOH A O   1 
HETATM 7815 O  O   . HOH L 6 .   ? -9.468  -41.797 -5.551  1.00 50.89  ? 853  HOH A O   1 
HETATM 7816 O  O   . HOH L 6 .   ? 16.654  -13.181 15.150  1.00 45.49  ? 854  HOH A O   1 
HETATM 7817 O  O   . HOH L 6 .   ? -19.232 -18.194 -17.922 1.00 46.73  ? 855  HOH A O   1 
HETATM 7818 O  O   . HOH L 6 .   ? 14.762  -20.978 18.072  1.00 54.75  ? 856  HOH A O   1 
HETATM 7819 O  O   . HOH L 6 .   ? 4.194   -28.416 16.486  1.00 61.77  ? 857  HOH A O   1 
HETATM 7820 O  O   . HOH L 6 .   ? -7.566  -7.844  -11.551 1.00 33.81  ? 858  HOH A O   1 
HETATM 7821 O  O   . HOH L 6 .   ? 9.148   -6.998  34.273  1.00 54.03  ? 859  HOH A O   1 
HETATM 7822 O  O   . HOH L 6 .   ? -0.191  -34.814 -3.719  1.00 39.70  ? 860  HOH A O   1 
HETATM 7823 O  O   . HOH L 6 .   ? -19.907 -32.152 -3.627  1.00 47.35  ? 861  HOH A O   1 
HETATM 7824 O  O   . HOH L 6 .   ? -39.065 -16.147 14.680  1.00 48.58  ? 862  HOH A O   1 
HETATM 7825 O  O   . HOH L 6 .   ? -13.457 9.890   21.129  1.00 40.87  ? 863  HOH A O   1 
HETATM 7826 O  O   . HOH L 6 .   ? -23.028 -32.935 11.517  1.00 61.18  ? 864  HOH A O   1 
HETATM 7827 O  O   . HOH L 6 .   ? -0.744  -5.356  -8.285  1.00 54.58  ? 865  HOH A O   1 
HETATM 7828 O  O   . HOH L 6 .   ? 2.649   -28.409 18.568  1.00 60.85  ? 866  HOH A O   1 
HETATM 7829 O  O   . HOH L 6 .   ? 6.801   -16.335 32.911  1.00 45.60  ? 867  HOH A O   1 
HETATM 7830 O  O   . HOH L 6 .   ? -21.097 -31.433 -0.141  1.00 56.72  ? 868  HOH A O   1 
HETATM 7831 O  O   . HOH L 6 .   ? -7.935  -17.401 31.267  1.00 43.62  ? 869  HOH A O   1 
HETATM 7832 O  O   . HOH L 6 .   ? -27.859 -27.327 15.346  1.00 49.76  ? 870  HOH A O   1 
HETATM 7833 O  O   . HOH L 6 .   ? -26.856 -27.225 19.818  1.00 52.26  ? 871  HOH A O   1 
HETATM 7834 O  O   . HOH L 6 .   ? -10.710 -20.930 34.990  1.00 53.53  ? 872  HOH A O   1 
HETATM 7835 O  O   . HOH L 6 .   ? 18.916  -10.517 34.515  1.00 73.52  ? 873  HOH A O   1 
HETATM 7836 O  O   . HOH L 6 .   ? -26.461 -8.361  31.480  1.00 52.85  ? 874  HOH A O   1 
HETATM 7837 O  O   . HOH L 6 .   ? -8.568  -12.127 -15.895 1.00 49.49  ? 875  HOH A O   1 
HETATM 7838 O  O   . HOH L 6 .   ? -29.562 -12.663 -1.530  1.00 53.35  ? 876  HOH A O   1 
HETATM 7839 O  O   . HOH L 6 .   ? -6.181  -9.962  37.723  1.00 33.98  ? 877  HOH A O   1 
HETATM 7840 O  O   . HOH L 6 .   ? -3.995  -14.072 33.954  1.00 39.53  ? 878  HOH A O   1 
HETATM 7841 O  O   . HOH L 6 .   ? -10.990 -37.160 -10.581 1.00 61.95  ? 879  HOH A O   1 
HETATM 7842 O  O   . HOH L 6 .   ? 17.356  -11.136 22.388  1.00 52.21  ? 880  HOH A O   1 
HETATM 7843 O  O   . HOH L 6 .   ? -19.275 11.268  18.306  1.00 62.69  ? 881  HOH A O   1 
HETATM 7844 O  O   . HOH L 6 .   ? -16.392 -37.864 3.162   1.00 48.15  ? 882  HOH A O   1 
HETATM 7845 O  O   . HOH L 6 .   ? 14.901  -0.286  14.847  1.00 58.74  ? 883  HOH A O   1 
HETATM 7846 O  O   . HOH L 6 .   ? -0.327  -28.324 16.031  1.00 43.31  ? 884  HOH A O   1 
HETATM 7847 O  O   . HOH L 6 .   ? -28.728 -21.802 -6.972  1.00 52.19  ? 885  HOH A O   1 
HETATM 7848 O  O   . HOH L 6 .   ? -10.641 -15.464 -18.608 1.00 54.72  ? 886  HOH A O   1 
HETATM 7849 O  O   . HOH L 6 .   ? 0.189   -32.961 -5.221  1.00 48.90  ? 887  HOH A O   1 
HETATM 7850 O  O   . HOH L 6 .   ? -7.986  2.665   12.902  1.00 56.91  ? 888  HOH A O   1 
HETATM 7851 O  O   . HOH L 6 .   ? -38.754 -9.998  21.034  1.00 56.87  ? 889  HOH A O   1 
HETATM 7852 O  O   . HOH L 6 .   ? -15.908 -6.752  3.718   1.00 50.82  ? 890  HOH A O   1 
HETATM 7853 O  O   . HOH L 6 .   ? 12.463  -17.461 13.108  1.00 45.72  ? 891  HOH A O   1 
HETATM 7854 O  O   . HOH L 6 .   ? -8.732  -17.782 28.808  1.00 50.00  ? 892  HOH A O   1 
HETATM 7855 O  O   . HOH L 6 .   ? -12.355 -15.865 38.054  1.00 55.24  ? 893  HOH A O   1 
HETATM 7856 O  O   . HOH L 6 .   ? -7.708  12.230  17.606  1.00 48.30  ? 894  HOH A O   1 
HETATM 7857 O  O   . HOH L 6 .   ? -5.465  6.415   -6.325  1.00 44.74  ? 895  HOH A O   1 
HETATM 7858 O  O   . HOH L 6 .   ? -18.788 -15.418 0.608   1.00 33.17  ? 896  HOH A O   1 
HETATM 7859 O  O   . HOH L 6 .   ? -19.567 4.230   26.707  1.00 51.07  ? 897  HOH A O   1 
HETATM 7860 O  O   . HOH L 6 .   ? -2.089  14.375  18.910  1.00 53.62  ? 898  HOH A O   1 
HETATM 7861 O  O   . HOH L 6 .   ? -15.816 10.319  19.864  1.00 54.84  ? 899  HOH A O   1 
HETATM 7862 O  O   . HOH L 6 .   ? -11.047 -45.865 -5.869  1.00 50.69  ? 900  HOH A O   1 
HETATM 7863 O  O   . HOH L 6 .   ? -3.201  -24.843 -13.446 1.00 45.18  ? 901  HOH A O   1 
HETATM 7864 O  O   . HOH L 6 .   ? 4.207   2.135   35.131  1.00 53.63  ? 902  HOH A O   1 
HETATM 7865 O  O   . HOH L 6 .   ? -28.512 -24.144 -3.254  1.00 53.64  ? 903  HOH A O   1 
HETATM 7866 O  O   . HOH L 6 .   ? 8.994   -24.722 16.650  1.00 51.44  ? 904  HOH A O   1 
HETATM 7867 O  O   . HOH L 6 .   ? -24.200 3.068   21.886  1.00 59.71  ? 905  HOH A O   1 
HETATM 7868 O  O   . HOH L 6 .   ? -12.487 12.387  22.024  1.00 51.12  ? 906  HOH A O   1 
HETATM 7869 O  O   . HOH L 6 .   ? 4.400   -20.392 3.796   1.00 55.33  ? 907  HOH A O   1 
HETATM 7870 O  O   . HOH L 6 .   ? -28.587 -26.215 -14.330 1.00 48.66  ? 908  HOH A O   1 
HETATM 7871 O  O   . HOH L 6 .   ? 2.655   -28.995 5.673   1.00 49.95  ? 909  HOH A O   1 
HETATM 7872 O  O   . HOH L 6 .   ? -31.371 -12.839 0.903   1.00 56.02  ? 910  HOH A O   1 
HETATM 7873 O  O   . HOH L 6 .   ? -13.223 -13.673 39.258  1.00 45.50  ? 911  HOH A O   1 
HETATM 7874 O  O   . HOH L 6 .   ? -8.934  -44.337 -6.924  1.00 43.80  ? 912  HOH A O   1 
HETATM 7875 O  O   . HOH L 6 .   ? -13.453 -45.339 -5.138  1.00 55.83  ? 913  HOH A O   1 
HETATM 7876 O  O   . HOH L 6 .   ? 2.343   -23.804 24.366  1.00 57.17  ? 914  HOH A O   1 
HETATM 7877 O  O   . HOH L 6 .   ? -9.238  -48.562 -4.462  1.00 55.91  ? 915  HOH A O   1 
HETATM 7878 O  O   . HOH L 6 .   ? -24.412 -17.493 -13.513 1.00 50.38  ? 916  HOH A O   1 
HETATM 7879 O  O   . HOH L 6 .   ? 9.787   -19.200 10.563  1.00 57.03  ? 917  HOH A O   1 
HETATM 7880 O  O   . HOH L 6 .   ? 10.739  1.024   19.019  1.00 49.10  ? 918  HOH A O   1 
HETATM 7881 O  O   . HOH L 6 .   ? 6.139   11.596  19.913  1.00 54.26  ? 919  HOH A O   1 
HETATM 7882 O  O   . HOH L 6 .   ? 0.197   -34.134 -0.932  1.00 46.12  ? 920  HOH A O   1 
HETATM 7883 O  O   . HOH L 6 .   ? 13.114  -22.858 18.595  1.00 57.56  ? 921  HOH A O   1 
HETATM 7884 O  O   . HOH L 6 .   ? 0.081   6.204   -2.414  1.00 57.23  ? 922  HOH A O   1 
HETATM 7885 O  O   . HOH L 6 .   ? 2.286   -31.628 -0.635  1.00 48.18  ? 923  HOH A O   1 
HETATM 7886 O  O   . HOH L 6 .   ? -4.284  12.893  15.119  1.00 47.17  ? 924  HOH A O   1 
HETATM 7887 O  O   . HOH L 6 .   ? -32.880 -15.589 -0.361  1.00 53.19  ? 925  HOH A O   1 
HETATM 7888 O  O   . HOH L 6 .   ? 3.782   -21.025 25.608  1.00 43.30  ? 926  HOH A O   1 
HETATM 7889 O  O   . HOH L 6 .   ? -27.235 -25.111 -5.590  1.00 52.02  ? 927  HOH A O   1 
HETATM 7890 O  O   . HOH L 6 .   ? 12.480  -21.593 23.363  1.00 59.33  ? 928  HOH A O   1 
HETATM 7891 O  O   . HOH L 6 .   ? -2.130  -15.782 -11.989 1.00 47.19  ? 929  HOH A O   1 
HETATM 7892 O  O   . HOH L 6 .   ? -5.817  -41.003 -10.117 1.00 57.66  ? 930  HOH A O   1 
HETATM 7893 O  O   . HOH L 6 .   ? -15.996 6.374   25.605  1.00 51.64  ? 931  HOH A O   1 
HETATM 7894 O  O   . HOH L 6 .   ? 0.630   -33.022 5.736   1.00 45.42  ? 932  HOH A O   1 
HETATM 7895 O  O   . HOH L 6 .   ? 11.785  -3.263  19.066  1.00 52.48  ? 933  HOH A O   1 
HETATM 7896 O  O   . HOH L 6 .   ? -9.157  13.201  15.549  1.00 51.37  ? 934  HOH A O   1 
HETATM 7897 O  O   . HOH L 6 .   ? 18.206  -14.205 18.931  1.00 49.60  ? 935  HOH A O   1 
HETATM 7898 O  O   . HOH L 6 .   ? 1.932   -14.694 34.261  1.00 47.21  ? 936  HOH A O   1 
HETATM 7899 O  O   . HOH L 6 .   ? 16.527  -9.715  19.872  1.00 50.57  ? 937  HOH A O   1 
HETATM 7900 O  O   . HOH L 6 .   ? -34.448 -13.856 3.504   1.00 40.92  ? 938  HOH A O   1 
HETATM 7901 O  O   . HOH L 6 .   ? -8.355  13.629  20.011  1.00 41.60  ? 939  HOH A O   1 
HETATM 7902 O  O   . HOH L 6 .   ? -3.066  -8.631  -11.742 1.00 50.35  ? 940  HOH A O   1 
HETATM 7903 O  O   . HOH L 6 .   ? 4.380   7.982   25.024  1.00 49.45  ? 941  HOH A O   1 
HETATM 7904 O  O   . HOH L 6 .   ? -4.751  -22.043 19.078  1.00 38.39  ? 942  HOH A O   1 
HETATM 7905 O  O   . HOH L 6 .   ? -9.958  -4.477  3.876   1.00 53.09  ? 943  HOH A O   1 
HETATM 7906 O  O   . HOH L 6 .   ? -19.513 1.624   28.720  1.00 48.54  ? 944  HOH A O   1 
HETATM 7907 O  O   . HOH L 6 .   ? -5.876  -19.956 25.505  1.00 49.20  ? 945  HOH A O   1 
HETATM 7908 O  O   . HOH L 6 .   ? -37.195 -19.877 9.618   1.00 50.70  ? 946  HOH A O   1 
HETATM 7909 O  O   . HOH L 6 .   ? -5.331  11.657  17.324  1.00 45.38  ? 947  HOH A O   1 
HETATM 7910 O  O   . HOH L 6 .   ? -16.086 -17.935 -20.402 1.00 54.33  ? 948  HOH A O   1 
HETATM 7911 O  O   . HOH L 6 .   ? 2.117   -31.285 4.125   1.00 42.43  ? 949  HOH A O   1 
HETATM 7912 O  O   . HOH L 6 .   ? -5.055  -7.312  -12.703 1.00 45.12  ? 950  HOH A O   1 
HETATM 7913 O  O   . HOH L 6 .   ? -12.559 5.038   29.465  1.00 58.11  ? 951  HOH A O   1 
HETATM 7914 O  O   . HOH L 6 .   ? 5.502   -21.075 8.716   1.00 56.96  ? 952  HOH A O   1 
HETATM 7915 O  O   . HOH L 6 .   ? -0.268  -33.500 1.698   1.00 43.03  ? 953  HOH A O   1 
HETATM 7916 O  O   . HOH L 6 .   ? -17.569 8.989   21.516  1.00 55.31  ? 954  HOH A O   1 
HETATM 7917 O  O   . HOH L 6 .   ? 1.375   6.045   7.477   1.00 62.24  ? 955  HOH A O   1 
HETATM 7918 O  O   . HOH L 6 .   ? -7.410  -3.719  0.153   1.00 49.85  ? 956  HOH A O   1 
HETATM 7919 O  O   . HOH M 6 .   ? 0.977   -9.829  64.990  1.00 43.69  ? 601  HOH B O   1 
HETATM 7920 O  O   . HOH M 6 .   ? -5.666  11.862  50.937  1.00 49.40  ? 602  HOH B O   1 
HETATM 7921 O  O   . HOH M 6 .   ? 9.631   -40.847 52.556  1.00 54.69  ? 603  HOH B O   1 
HETATM 7922 O  O   . HOH M 6 .   ? 23.945  -14.661 60.056  1.00 39.70  ? 604  HOH B O   1 
HETATM 7923 O  O   . HOH M 6 .   ? 4.411   -7.059  68.882  1.00 38.74  ? 605  HOH B O   1 
HETATM 7924 O  O   . HOH M 6 .   ? -12.432 -40.650 74.326  1.00 44.29  ? 606  HOH B O   1 
HETATM 7925 O  O   . HOH M 6 .   ? -16.456 -19.043 76.666  1.00 45.79  ? 607  HOH B O   1 
HETATM 7926 O  O   . HOH M 6 .   ? 8.868   6.595   55.124  1.00 55.99  ? 608  HOH B O   1 
HETATM 7927 O  O   . HOH M 6 .   ? -6.297  12.177  58.048  1.00 53.92  ? 609  HOH B O   1 
HETATM 7928 O  O   . HOH M 6 .   ? -13.073 -29.813 69.660  1.00 53.29  ? 610  HOH B O   1 
HETATM 7929 O  O   . HOH M 6 .   ? 13.289  -30.614 50.273  1.00 50.06  ? 611  HOH B O   1 
HETATM 7930 O  O   . HOH M 6 .   ? -5.510  -23.677 90.225  1.00 53.22  ? 612  HOH B O   1 
HETATM 7931 O  O   . HOH M 6 .   ? -0.634  -20.136 39.257  1.00 54.30  ? 613  HOH B O   1 
HETATM 7932 O  O   . HOH M 6 .   ? 16.054  -24.090 46.046  1.00 55.81  ? 614  HOH B O   1 
HETATM 7933 O  O   . HOH M 6 .   ? -0.179  -14.918 89.632  1.00 45.65  ? 615  HOH B O   1 
HETATM 7934 O  O   . HOH M 6 .   ? 11.464  -17.819 90.832  1.00 50.31  ? 616  HOH B O   1 
HETATM 7935 O  O   . HOH M 6 .   ? 9.269   -15.034 39.007  1.00 52.90  ? 617  HOH B O   1 
HETATM 7936 O  O   . HOH M 6 .   ? 5.893   -27.244 76.001  1.00 42.50  ? 618  HOH B O   1 
HETATM 7937 O  O   . HOH M 6 .   ? 7.566   -29.519 89.773  1.00 50.65  ? 619  HOH B O   1 
HETATM 7938 O  O   . HOH M 6 .   ? -16.787 -21.404 46.350  1.00 50.71  ? 620  HOH B O   1 
HETATM 7939 O  O   . HOH M 6 .   ? -2.368  -36.481 86.563  1.00 52.27  ? 621  HOH B O   1 
HETATM 7940 O  O   . HOH M 6 .   ? -3.205  -46.654 74.123  1.00 54.47  ? 622  HOH B O   1 
HETATM 7941 O  O   . HOH M 6 .   ? 7.541   -6.824  73.031  1.00 46.72  ? 623  HOH B O   1 
HETATM 7942 O  O   . HOH M 6 .   ? -19.486 -22.717 52.524  1.00 45.90  ? 624  HOH B O   1 
HETATM 7943 O  O   . HOH M 6 .   ? -25.902 -17.467 61.663  1.00 54.32  ? 625  HOH B O   1 
HETATM 7944 O  O   . HOH M 6 .   ? -2.503  -18.389 53.727  1.00 41.84  ? 626  HOH B O   1 
HETATM 7945 O  O   . HOH M 6 .   ? -5.064  9.873   49.591  1.00 48.68  ? 627  HOH B O   1 
HETATM 7946 O  O   . HOH M 6 .   ? -8.502  2.377   70.017  1.00 50.72  ? 628  HOH B O   1 
HETATM 7947 O  O   . HOH M 6 .   ? 7.968   -2.285  42.485  1.00 50.45  ? 629  HOH B O   1 
HETATM 7948 O  O   . HOH M 6 .   ? 13.974  -14.185 78.967  1.00 40.45  ? 630  HOH B O   1 
HETATM 7949 O  O   . HOH M 6 .   ? -9.203  -34.674 70.775  1.00 41.37  ? 631  HOH B O   1 
HETATM 7950 O  O   . HOH M 6 .   ? 0.562   -12.798 58.881  1.00 34.01  ? 632  HOH B O   1 
HETATM 7951 O  O   . HOH M 6 .   ? -4.505  12.024  53.690  1.00 44.94  ? 633  HOH B O   1 
HETATM 7952 O  O   . HOH M 6 .   ? -1.218  -24.389 43.564  1.00 52.06  ? 634  HOH B O   1 
HETATM 7953 O  O   . HOH M 6 .   ? -13.026 -32.234 63.863  1.00 50.96  ? 635  HOH B O   1 
HETATM 7954 O  O   . HOH M 6 .   ? 2.231   -41.503 53.683  1.00 54.20  ? 636  HOH B O   1 
HETATM 7955 O  O   . HOH M 6 .   ? 21.650  -20.736 64.830  1.00 38.97  ? 637  HOH B O   1 
HETATM 7956 O  O   . HOH M 6 .   ? 5.322   1.262   49.061  1.00 42.03  ? 638  HOH B O   1 
HETATM 7957 O  O   . HOH M 6 .   ? -16.233 -13.986 37.618  1.00 37.83  ? 639  HOH B O   1 
HETATM 7958 O  O   . HOH M 6 .   ? -21.340 9.284   58.385  1.00 50.73  ? 640  HOH B O   1 
HETATM 7959 O  O   . HOH M 6 .   ? 5.476   -1.876  42.051  1.00 50.83  ? 641  HOH B O   1 
HETATM 7960 O  O   . HOH M 6 .   ? 6.621   -13.130 87.942  1.00 43.21  ? 642  HOH B O   1 
HETATM 7961 O  O   . HOH M 6 .   ? -18.186 -7.679  80.018  1.00 45.44  ? 643  HOH B O   1 
HETATM 7962 O  O   . HOH M 6 .   ? 18.698  -17.324 43.793  1.00 56.64  ? 644  HOH B O   1 
HETATM 7963 O  O   . HOH M 6 .   ? -9.726  -23.485 49.448  1.00 51.96  ? 645  HOH B O   1 
HETATM 7964 O  O   . HOH M 6 .   ? -7.770  -0.100  71.529  1.00 50.03  ? 646  HOH B O   1 
HETATM 7965 O  O   . HOH M 6 .   ? -11.473 8.051   40.814  1.00 51.89  ? 647  HOH B O   1 
HETATM 7966 O  O   . HOH M 6 .   ? -6.284  -12.434 86.775  1.00 43.99  ? 648  HOH B O   1 
HETATM 7967 O  O   . HOH M 6 .   ? 24.063  -9.694  54.084  1.00 47.01  ? 649  HOH B O   1 
HETATM 7968 O  O   . HOH M 6 .   ? -7.034  -14.856 85.740  1.00 35.38  ? 650  HOH B O   1 
HETATM 7969 O  O   . HOH M 6 .   ? -21.345 -8.603  34.829  1.00 50.62  ? 651  HOH B O   1 
HETATM 7970 O  O   . HOH M 6 .   ? 11.932  -9.844  66.680  1.00 34.99  ? 652  HOH B O   1 
HETATM 7971 O  O   . HOH M 6 .   ? -18.634 4.674   63.067  1.00 33.83  ? 653  HOH B O   1 
HETATM 7972 O  O   . HOH M 6 .   ? -7.770  7.261   41.493  1.00 53.91  ? 654  HOH B O   1 
HETATM 7973 O  O   . HOH M 6 .   ? -19.909 -9.283  83.330  1.00 52.98  ? 655  HOH B O   1 
HETATM 7974 O  O   . HOH M 6 .   ? 7.837   -43.092 57.894  1.00 43.33  ? 656  HOH B O   1 
HETATM 7975 O  O   . HOH M 6 .   ? 8.608   -30.434 87.525  1.00 49.97  ? 657  HOH B O   1 
HETATM 7976 O  O   . HOH M 6 .   ? -4.778  -6.866  35.171  1.00 35.34  ? 658  HOH B O   1 
HETATM 7977 O  O   . HOH M 6 .   ? 0.833   -9.585  54.479  1.00 32.00  ? 659  HOH B O   1 
HETATM 7978 O  O   . HOH M 6 .   ? -12.145 -27.156 58.963  1.00 41.42  ? 660  HOH B O   1 
HETATM 7979 O  O   . HOH M 6 .   ? -22.262 -1.231  54.670  1.00 46.22  ? 661  HOH B O   1 
HETATM 7980 O  O   . HOH M 6 .   ? -5.654  -24.412 80.807  1.00 33.64  ? 662  HOH B O   1 
HETATM 7981 O  O   . HOH M 6 .   ? 23.713  -18.900 59.566  1.00 46.46  ? 663  HOH B O   1 
HETATM 7982 O  O   . HOH M 6 .   ? -8.329  1.166   67.222  1.00 39.67  ? 664  HOH B O   1 
HETATM 7983 O  O   . HOH M 6 .   ? -18.846 3.896   51.402  1.00 39.35  ? 665  HOH B O   1 
HETATM 7984 O  O   . HOH M 6 .   ? -2.004  -27.483 49.989  1.00 48.36  ? 666  HOH B O   1 
HETATM 7985 O  O   . HOH M 6 .   ? 29.494  -4.570  70.215  1.00 43.81  ? 667  HOH B O   1 
HETATM 7986 O  O   . HOH M 6 .   ? -8.402  -28.560 60.429  1.00 38.13  ? 668  HOH B O   1 
HETATM 7987 O  O   . HOH M 6 .   ? -13.383 -22.271 74.830  1.00 39.02  ? 669  HOH B O   1 
HETATM 7988 O  O   . HOH M 6 .   ? 3.147   -16.192 92.286  1.00 49.58  ? 670  HOH B O   1 
HETATM 7989 O  O   . HOH M 6 .   ? -25.958 -9.411  48.117  1.00 44.90  ? 671  HOH B O   1 
HETATM 7990 O  O   . HOH M 6 .   ? 4.698   -18.144 93.085  1.00 49.47  ? 672  HOH B O   1 
HETATM 7991 O  O   . HOH M 6 .   ? -12.039 -22.647 52.433  1.00 37.62  ? 673  HOH B O   1 
HETATM 7992 O  O   . HOH M 6 .   ? -15.623 7.580   51.381  1.00 40.34  ? 674  HOH B O   1 
HETATM 7993 O  O   . HOH M 6 .   ? -21.294 -19.658 62.842  1.00 35.04  ? 675  HOH B O   1 
HETATM 7994 O  O   . HOH M 6 .   ? -10.801 -29.341 59.582  1.00 45.75  ? 676  HOH B O   1 
HETATM 7995 O  O   . HOH M 6 .   ? -4.477  -20.499 53.602  1.00 47.13  ? 677  HOH B O   1 
HETATM 7996 O  O   . HOH M 6 .   ? 10.354  -9.334  68.781  1.00 35.86  ? 678  HOH B O   1 
HETATM 7997 O  O   . HOH M 6 .   ? 20.603  -14.272 70.400  1.00 33.34  ? 679  HOH B O   1 
HETATM 7998 O  O   . HOH M 6 .   ? 8.135   -4.611  65.519  1.00 47.55  ? 680  HOH B O   1 
HETATM 7999 O  O   . HOH M 6 .   ? -11.697 -0.130  76.508  1.00 47.07  ? 681  HOH B O   1 
HETATM 8000 O  O   . HOH M 6 .   ? 12.927  -13.297 88.621  1.00 55.04  ? 682  HOH B O   1 
HETATM 8001 O  O   . HOH M 6 .   ? -13.186 7.918   47.301  1.00 43.37  ? 683  HOH B O   1 
HETATM 8002 O  O   . HOH M 6 .   ? -10.440 -29.140 56.289  1.00 57.07  ? 684  HOH B O   1 
HETATM 8003 O  O   . HOH M 6 .   ? 13.372  -32.136 56.890  1.00 51.91  ? 685  HOH B O   1 
HETATM 8004 O  O   . HOH M 6 .   ? -21.827 -6.660  69.559  1.00 34.95  ? 686  HOH B O   1 
HETATM 8005 O  O   . HOH M 6 .   ? 2.377   -14.792 61.897  1.00 35.80  ? 687  HOH B O   1 
HETATM 8006 O  O   . HOH M 6 .   ? 12.331  -19.169 86.458  1.00 40.64  ? 688  HOH B O   1 
HETATM 8007 O  O   . HOH M 6 .   ? -22.745 -17.721 43.811  1.00 44.69  ? 689  HOH B O   1 
HETATM 8008 O  O   . HOH M 6 .   ? 1.513   -9.455  43.486  1.00 31.75  ? 690  HOH B O   1 
HETATM 8009 O  O   . HOH M 6 .   ? -24.340 -1.722  47.863  1.00 45.59  ? 691  HOH B O   1 
HETATM 8010 O  O   . HOH M 6 .   ? 10.600  -13.020 75.621  1.00 32.89  ? 692  HOH B O   1 
HETATM 8011 O  O   . HOH M 6 .   ? -15.080 -14.620 43.668  1.00 41.58  ? 693  HOH B O   1 
HETATM 8012 O  O   . HOH M 6 .   ? -1.911  -40.319 68.578  1.00 51.56  ? 694  HOH B O   1 
HETATM 8013 O  O   . HOH M 6 .   ? 22.238  -23.434 67.180  1.00 37.80  ? 695  HOH B O   1 
HETATM 8014 O  O   . HOH M 6 .   ? 4.911   -22.511 70.057  1.00 31.04  ? 696  HOH B O   1 
HETATM 8015 O  O   . HOH M 6 .   ? 11.745  -18.729 61.727  1.00 32.37  ? 697  HOH B O   1 
HETATM 8016 O  O   . HOH M 6 .   ? -3.755  9.948   61.125  1.00 41.71  ? 698  HOH B O   1 
HETATM 8017 O  O   . HOH M 6 .   ? -22.530 -17.074 53.492  1.00 34.05  ? 699  HOH B O   1 
HETATM 8018 O  O   . HOH M 6 .   ? 13.032  -27.409 78.189  1.00 49.69  ? 700  HOH B O   1 
HETATM 8019 O  O   . HOH M 6 .   ? 15.451  -20.709 91.352  1.00 45.99  ? 701  HOH B O   1 
HETATM 8020 O  O   . HOH M 6 .   ? 23.816  -16.817 73.662  1.00 50.89  ? 702  HOH B O   1 
HETATM 8021 O  O   . HOH M 6 .   ? -7.217  -12.256 79.582  1.00 36.44  ? 703  HOH B O   1 
HETATM 8022 O  O   . HOH M 6 .   ? -13.235 -15.178 45.602  1.00 33.70  ? 704  HOH B O   1 
HETATM 8023 O  O   . HOH M 6 .   ? -21.896 -22.026 53.818  1.00 39.67  ? 705  HOH B O   1 
HETATM 8024 O  O   . HOH M 6 .   ? 4.674   -35.100 69.248  1.00 43.93  ? 706  HOH B O   1 
HETATM 8025 O  O   . HOH M 6 .   ? -14.925 -18.164 79.572  1.00 44.79  ? 707  HOH B O   1 
HETATM 8026 O  O   . HOH M 6 .   ? -17.392 0.602   45.245  1.00 35.97  ? 708  HOH B O   1 
HETATM 8027 O  O   . HOH M 6 .   ? 8.730   -15.475 68.644  1.00 29.82  ? 709  HOH B O   1 
HETATM 8028 O  O   . HOH M 6 .   ? 0.344   -34.357 55.944  1.00 48.45  ? 710  HOH B O   1 
HETATM 8029 O  O   . HOH M 6 .   ? -26.467 -14.192 58.655  1.00 46.77  ? 711  HOH B O   1 
HETATM 8030 O  O   . HOH M 6 .   ? -6.902  -25.975 86.362  1.00 36.87  ? 712  HOH B O   1 
HETATM 8031 O  O   . HOH M 6 .   ? 8.137   -29.866 80.717  1.00 36.83  ? 713  HOH B O   1 
HETATM 8032 O  O   . HOH M 6 .   ? -14.519 -25.332 63.968  1.00 34.88  ? 714  HOH B O   1 
HETATM 8033 O  O   . HOH M 6 .   ? 16.170  -7.742  73.416  1.00 48.84  ? 715  HOH B O   1 
HETATM 8034 O  O   . HOH M 6 .   ? -13.742 7.320   63.950  1.00 42.42  ? 716  HOH B O   1 
HETATM 8035 O  O   . HOH M 6 .   ? -14.412 0.827   42.636  1.00 42.96  ? 717  HOH B O   1 
HETATM 8036 O  O   . HOH M 6 .   ? -19.794 -1.985  54.207  1.00 37.61  ? 718  HOH B O   1 
HETATM 8037 O  O   . HOH M 6 .   ? -9.324  7.585   51.342  1.00 35.42  ? 719  HOH B O   1 
HETATM 8038 O  O   . HOH M 6 .   ? 2.529   -49.488 58.406  1.00 52.55  ? 720  HOH B O   1 
HETATM 8039 O  O   . HOH M 6 .   ? 5.682   -37.311 65.972  1.00 53.00  ? 721  HOH B O   1 
HETATM 8040 O  O   . HOH M 6 .   ? 4.040   -31.345 53.158  1.00 42.96  ? 722  HOH B O   1 
HETATM 8041 O  O   . HOH M 6 .   ? 22.129  -8.387  57.177  1.00 41.52  ? 723  HOH B O   1 
HETATM 8042 O  O   . HOH M 6 .   ? -19.901 -14.042 69.015  1.00 46.42  ? 724  HOH B O   1 
HETATM 8043 O  O   . HOH M 6 .   ? -11.385 -30.507 68.048  1.00 39.94  ? 725  HOH B O   1 
HETATM 8044 O  O   . HOH M 6 .   ? -20.130 7.507   57.072  1.00 41.66  ? 726  HOH B O   1 
HETATM 8045 O  O   . HOH M 6 .   ? 6.327   -14.402 72.071  1.00 31.70  ? 727  HOH B O   1 
HETATM 8046 O  O   . HOH M 6 .   ? 6.054   11.582  57.698  1.00 61.39  ? 728  HOH B O   1 
HETATM 8047 O  O   . HOH M 6 .   ? -2.214  -15.049 67.717  1.00 32.13  ? 729  HOH B O   1 
HETATM 8048 O  O   . HOH M 6 .   ? -0.270  2.700   45.482  1.00 43.34  ? 730  HOH B O   1 
HETATM 8049 O  O   . HOH M 6 .   ? 21.299  -2.349  61.371  1.00 52.75  ? 731  HOH B O   1 
HETATM 8050 O  O   . HOH M 6 .   ? -14.679 -6.764  78.244  1.00 36.45  ? 732  HOH B O   1 
HETATM 8051 O  O   . HOH M 6 .   ? 5.046   -10.562 84.228  1.00 47.69  ? 733  HOH B O   1 
HETATM 8052 O  O   . HOH M 6 .   ? -19.021 -8.547  43.901  1.00 44.38  ? 734  HOH B O   1 
HETATM 8053 O  O   . HOH M 6 .   ? 23.896  -12.302 68.569  1.00 34.67  ? 735  HOH B O   1 
HETATM 8054 O  O   . HOH M 6 .   ? -19.598 -24.391 57.402  1.00 37.96  ? 736  HOH B O   1 
HETATM 8055 O  O   . HOH M 6 .   ? -1.495  -40.721 62.275  1.00 50.70  ? 737  HOH B O   1 
HETATM 8056 O  O   . HOH M 6 .   ? -8.666  -13.438 64.163  1.00 34.79  ? 738  HOH B O   1 
HETATM 8057 O  O   . HOH M 6 .   ? 9.738   -3.372  48.037  1.00 41.82  ? 739  HOH B O   1 
HETATM 8058 O  O   . HOH M 6 .   ? -5.775  -28.896 58.206  1.00 50.36  ? 740  HOH B O   1 
HETATM 8059 O  O   . HOH M 6 .   ? 14.857  -19.499 73.736  1.00 32.20  ? 741  HOH B O   1 
HETATM 8060 O  O   . HOH M 6 .   ? -12.270 -9.815  88.310  1.00 50.32  ? 742  HOH B O   1 
HETATM 8061 O  O   . HOH M 6 .   ? 3.420   -9.748  45.546  1.00 32.21  ? 743  HOH B O   1 
HETATM 8062 O  O   . HOH M 6 .   ? -17.651 -16.588 70.244  1.00 40.33  ? 744  HOH B O   1 
HETATM 8063 O  O   . HOH M 6 .   ? -8.599  -11.280 87.133  1.00 45.98  ? 745  HOH B O   1 
HETATM 8064 O  O   . HOH M 6 .   ? 6.274   -39.005 60.731  1.00 44.59  ? 746  HOH B O   1 
HETATM 8065 O  O   . HOH M 6 .   ? 0.104   -42.506 66.217  1.00 47.28  ? 747  HOH B O   1 
HETATM 8066 O  O   . HOH M 6 .   ? -21.828 -10.985 69.224  1.00 35.11  ? 748  HOH B O   1 
HETATM 8067 O  O   . HOH M 6 .   ? 13.829  -28.793 64.396  1.00 43.36  ? 749  HOH B O   1 
HETATM 8068 O  O   . HOH M 6 .   ? -3.434  -1.577  42.204  1.00 34.95  ? 750  HOH B O   1 
HETATM 8069 O  O   . HOH M 6 .   ? 0.774   -7.769  41.474  1.00 31.62  ? 751  HOH B O   1 
HETATM 8070 O  O   . HOH M 6 .   ? 4.067   -29.442 86.913  1.00 46.05  ? 752  HOH B O   1 
HETATM 8071 O  O   . HOH M 6 .   ? -14.413 -24.113 67.965  1.00 47.09  ? 753  HOH B O   1 
HETATM 8072 O  O   . HOH M 6 .   ? -25.117 -9.505  57.652  1.00 48.40  ? 754  HOH B O   1 
HETATM 8073 O  O   . HOH M 6 .   ? -13.224 -25.549 71.262  1.00 40.80  ? 755  HOH B O   1 
HETATM 8074 O  O   . HOH M 6 .   ? 0.449   -2.086  39.814  1.00 40.86  ? 756  HOH B O   1 
HETATM 8075 O  O   . HOH M 6 .   ? 21.405  -20.234 59.238  1.00 41.65  ? 757  HOH B O   1 
HETATM 8076 O  O   . HOH M 6 .   ? 12.676  -29.682 83.496  1.00 44.04  ? 758  HOH B O   1 
HETATM 8077 O  O   . HOH M 6 .   ? 9.781   -48.131 54.493  1.00 57.51  ? 759  HOH B O   1 
HETATM 8078 O  O   . HOH M 6 .   ? 18.625  -18.113 84.498  1.00 50.82  ? 760  HOH B O   1 
HETATM 8079 O  O   . HOH M 6 .   ? 1.685   0.804   42.684  1.00 53.54  ? 761  HOH B O   1 
HETATM 8080 O  O   . HOH M 6 .   ? 14.404  -24.242 54.123  1.00 41.04  ? 762  HOH B O   1 
HETATM 8081 O  O   . HOH M 6 .   ? 6.723   -20.698 71.395  1.00 29.42  ? 763  HOH B O   1 
HETATM 8082 O  O   . HOH M 6 .   ? 22.065  -6.523  71.027  1.00 41.72  ? 764  HOH B O   1 
HETATM 8083 O  O   . HOH M 6 .   ? -27.203 3.258   64.492  1.00 53.74  ? 765  HOH B O   1 
HETATM 8084 O  O   . HOH M 6 .   ? -14.629 -35.898 82.507  1.00 51.16  ? 766  HOH B O   1 
HETATM 8085 O  O   . HOH M 6 .   ? 8.459   -15.016 79.381  1.00 31.49  ? 767  HOH B O   1 
HETATM 8086 O  O   . HOH M 6 .   ? -15.777 -19.567 70.889  1.00 37.29  ? 768  HOH B O   1 
HETATM 8087 O  O   . HOH M 6 .   ? -2.079  -10.212 42.183  1.00 30.78  ? 769  HOH B O   1 
HETATM 8088 O  O   . HOH M 6 .   ? -3.255  -5.118  69.004  1.00 37.49  ? 770  HOH B O   1 
HETATM 8089 O  O   . HOH M 6 .   ? -14.040 7.768   44.653  1.00 45.31  ? 771  HOH B O   1 
HETATM 8090 O  O   . HOH M 6 .   ? -11.175 8.702   63.664  1.00 43.71  ? 772  HOH B O   1 
HETATM 8091 O  O   . HOH M 6 .   ? 23.520  -9.650  68.258  1.00 34.92  ? 773  HOH B O   1 
HETATM 8092 O  O   . HOH M 6 .   ? -10.323 -29.042 87.326  1.00 47.85  ? 774  HOH B O   1 
HETATM 8093 O  O   . HOH M 6 .   ? -19.206 -3.587  40.584  1.00 45.78  ? 775  HOH B O   1 
HETATM 8094 O  O   . HOH M 6 .   ? 20.843  -23.378 87.148  1.00 54.09  ? 776  HOH B O   1 
HETATM 8095 O  O   . HOH M 6 .   ? -0.537  -40.081 56.944  1.00 57.40  ? 777  HOH B O   1 
HETATM 8096 O  O   . HOH M 6 .   ? -5.284  -8.014  39.708  1.00 33.32  ? 778  HOH B O   1 
HETATM 8097 O  O   . HOH M 6 .   ? 3.143   -26.447 45.220  1.00 45.11  ? 779  HOH B O   1 
HETATM 8098 O  O   . HOH M 6 .   ? -26.930 -0.105  64.527  1.00 47.69  ? 780  HOH B O   1 
HETATM 8099 O  O   . HOH M 6 .   ? 4.085   4.691   50.636  1.00 38.16  ? 781  HOH B O   1 
HETATM 8100 O  O   . HOH M 6 .   ? 17.157  -23.525 89.131  1.00 42.61  ? 782  HOH B O   1 
HETATM 8101 O  O   . HOH M 6 .   ? -20.133 -10.897 45.349  1.00 42.26  ? 783  HOH B O   1 
HETATM 8102 O  O   . HOH M 6 .   ? -1.607  -15.734 91.826  1.00 47.34  ? 784  HOH B O   1 
HETATM 8103 O  O   . HOH M 6 .   ? -0.150  -0.475  62.542  1.00 40.12  ? 785  HOH B O   1 
HETATM 8104 O  O   . HOH M 6 .   ? -7.560  3.904   44.156  1.00 42.83  ? 786  HOH B O   1 
HETATM 8105 O  O   . HOH M 6 .   ? -16.356 12.446  55.284  1.00 48.67  ? 787  HOH B O   1 
HETATM 8106 O  O   . HOH M 6 .   ? 27.847  -0.984  68.559  1.00 47.60  ? 788  HOH B O   1 
HETATM 8107 O  O   . HOH M 6 .   ? 4.622   -14.344 40.072  1.00 40.66  ? 789  HOH B O   1 
HETATM 8108 O  O   . HOH M 6 .   ? -8.327  -1.206  69.132  1.00 40.63  ? 790  HOH B O   1 
HETATM 8109 O  O   . HOH M 6 .   ? -26.559 -6.436  73.886  1.00 47.34  ? 791  HOH B O   1 
HETATM 8110 O  O   . HOH M 6 .   ? -10.851 3.758   48.207  1.00 37.26  ? 792  HOH B O   1 
HETATM 8111 O  O   . HOH M 6 .   ? -13.260 -17.504 82.771  1.00 37.22  ? 793  HOH B O   1 
HETATM 8112 O  O   . HOH M 6 .   ? -25.001 -3.656  58.966  1.00 41.49  ? 794  HOH B O   1 
HETATM 8113 O  O   . HOH M 6 .   ? 3.990   10.267  62.057  1.00 69.43  ? 795  HOH B O   1 
HETATM 8114 O  O   . HOH M 6 .   ? 19.630  -3.024  59.476  1.00 52.66  ? 796  HOH B O   1 
HETATM 8115 O  O   . HOH M 6 .   ? -11.461 -31.747 73.607  1.00 37.51  ? 797  HOH B O   1 
HETATM 8116 O  O   . HOH M 6 .   ? 8.639   -31.637 83.600  1.00 49.52  ? 798  HOH B O   1 
HETATM 8117 O  O   . HOH M 6 .   ? -4.395  -17.709 60.034  1.00 35.26  ? 799  HOH B O   1 
HETATM 8118 O  O   . HOH M 6 .   ? 17.677  -2.485  65.922  1.00 54.13  ? 800  HOH B O   1 
HETATM 8119 O  O   . HOH M 6 .   ? -25.131 -20.860 60.588  1.00 45.10  ? 801  HOH B O   1 
HETATM 8120 O  O   . HOH M 6 .   ? 12.985  -14.061 76.438  1.00 36.50  ? 802  HOH B O   1 
HETATM 8121 O  O   . HOH M 6 .   ? -14.223 -20.055 51.334  1.00 34.57  ? 803  HOH B O   1 
HETATM 8122 O  O   . HOH M 6 .   ? -11.551 -17.423 44.960  1.00 43.54  ? 804  HOH B O   1 
HETATM 8123 O  O   . HOH M 6 .   ? 5.460   -4.367  62.758  1.00 45.47  ? 805  HOH B O   1 
HETATM 8124 O  O   . HOH M 6 .   ? -24.544 0.302   65.128  1.00 44.04  ? 806  HOH B O   1 
HETATM 8125 O  O   . HOH M 6 .   ? -26.527 -22.532 57.138  1.00 49.88  ? 807  HOH B O   1 
HETATM 8126 O  O   . HOH M 6 .   ? 9.723   1.124   53.991  1.00 50.72  ? 808  HOH B O   1 
HETATM 8127 O  O   . HOH M 6 .   ? 5.365   -16.246 41.597  1.00 49.46  ? 809  HOH B O   1 
HETATM 8128 O  O   . HOH M 6 .   ? 25.819  -15.350 62.793  1.00 41.84  ? 810  HOH B O   1 
HETATM 8129 O  O   . HOH M 6 .   ? -11.564 -16.424 41.944  1.00 42.38  ? 811  HOH B O   1 
HETATM 8130 O  O   . HOH M 6 .   ? 8.423   -14.310 76.688  1.00 32.97  ? 812  HOH B O   1 
HETATM 8131 O  O   . HOH M 6 .   ? 15.881  -29.236 86.027  1.00 42.59  ? 813  HOH B O   1 
HETATM 8132 O  O   . HOH M 6 .   ? 17.039  -15.216 63.506  1.00 32.51  ? 814  HOH B O   1 
HETATM 8133 O  O   . HOH M 6 .   ? -10.155 11.566  56.594  1.00 42.31  ? 815  HOH B O   1 
HETATM 8134 O  O   . HOH M 6 .   ? 7.232   -17.927 73.252  1.00 28.69  ? 816  HOH B O   1 
HETATM 8135 O  O   . HOH M 6 .   ? 23.070  -18.613 65.444  1.00 33.40  ? 817  HOH B O   1 
HETATM 8136 O  O   . HOH M 6 .   ? -5.737  -22.792 59.067  1.00 37.01  ? 818  HOH B O   1 
HETATM 8137 O  O   . HOH M 6 .   ? -13.152 -10.767 39.157  1.00 34.26  ? 819  HOH B O   1 
HETATM 8138 O  O   . HOH M 6 .   ? 8.209   -44.696 64.668  1.00 54.83  ? 820  HOH B O   1 
HETATM 8139 O  O   . HOH M 6 .   ? -17.449 10.436  52.842  1.00 51.39  ? 821  HOH B O   1 
HETATM 8140 O  O   . HOH M 6 .   ? -26.082 -10.947 55.576  1.00 45.44  ? 822  HOH B O   1 
HETATM 8141 O  O   . HOH M 6 .   ? 16.482  -26.626 59.679  1.00 47.60  ? 823  HOH B O   1 
HETATM 8142 O  O   . HOH M 6 .   ? -26.314 -11.674 60.292  1.00 45.22  ? 824  HOH B O   1 
HETATM 8143 O  O   . HOH M 6 .   ? 24.802  -19.370 68.766  1.00 33.79  ? 825  HOH B O   1 
HETATM 8144 O  O   . HOH M 6 .   ? -19.204 2.319   53.960  1.00 40.22  ? 826  HOH B O   1 
HETATM 8145 O  O   . HOH M 6 .   ? -9.126  -21.823 55.376  1.00 37.67  ? 827  HOH B O   1 
HETATM 8146 O  O   . HOH M 6 .   ? 11.482  -33.674 58.951  1.00 60.04  ? 828  HOH B O   1 
HETATM 8147 O  O   . HOH M 6 .   ? 20.110  -12.684 39.255  1.00 60.57  ? 829  HOH B O   1 
HETATM 8148 O  O   . HOH M 6 .   ? 0.285   8.011   52.620  1.00 42.78  ? 830  HOH B O   1 
HETATM 8149 O  O   . HOH M 6 .   ? 2.003   -43.344 64.685  1.00 51.57  ? 831  HOH B O   1 
HETATM 8150 O  O   . HOH M 6 .   ? 18.429  -10.369 74.405  1.00 49.08  ? 832  HOH B O   1 
HETATM 8151 O  O   . HOH M 6 .   ? 5.539   -38.336 79.852  1.00 48.60  ? 833  HOH B O   1 
HETATM 8152 O  O   . HOH M 6 .   ? 25.612  -18.874 54.584  1.00 46.74  ? 834  HOH B O   1 
HETATM 8153 O  O   . HOH M 6 .   ? -24.386 -2.713  43.205  1.00 51.69  ? 835  HOH B O   1 
HETATM 8154 O  O   . HOH M 6 .   ? 0.659   -9.839  72.280  1.00 34.25  ? 836  HOH B O   1 
HETATM 8155 O  O   . HOH M 6 .   ? 25.236  -1.397  62.651  1.00 51.01  ? 837  HOH B O   1 
HETATM 8156 O  O   . HOH M 6 .   ? -23.037 2.382   58.106  1.00 47.36  ? 838  HOH B O   1 
HETATM 8157 O  O   . HOH M 6 .   ? -22.576 -19.651 47.292  1.00 47.35  ? 839  HOH B O   1 
HETATM 8158 O  O   . HOH M 6 .   ? -23.035 -13.597 76.711  1.00 57.56  ? 840  HOH B O   1 
HETATM 8159 O  O   . HOH M 6 .   ? 5.815   -31.472 86.884  1.00 54.09  ? 841  HOH B O   1 
HETATM 8160 O  O   . HOH M 6 .   ? 3.464   -34.102 53.531  1.00 44.22  ? 842  HOH B O   1 
HETATM 8161 O  O   . HOH M 6 .   ? 27.022  -15.411 53.456  1.00 52.24  ? 843  HOH B O   1 
HETATM 8162 O  O   . HOH M 6 .   ? -1.305  -42.851 80.913  1.00 45.67  ? 844  HOH B O   1 
HETATM 8163 O  O   . HOH M 6 .   ? -6.254  -4.757  39.033  1.00 37.00  ? 845  HOH B O   1 
HETATM 8164 O  O   . HOH M 6 .   ? -3.772  -17.453 43.858  1.00 38.66  ? 846  HOH B O   1 
HETATM 8165 O  O   . HOH M 6 .   ? 8.742   -28.527 73.057  1.00 49.90  ? 847  HOH B O   1 
HETATM 8166 O  O   . HOH M 6 .   ? 15.942  -28.519 88.814  1.00 50.04  ? 848  HOH B O   1 
HETATM 8167 O  O   . HOH M 6 .   ? 31.122  -2.992  58.978  1.00 49.77  ? 849  HOH B O   1 
HETATM 8168 O  O   . HOH M 6 .   ? 12.478  -1.871  55.260  1.00 50.85  ? 850  HOH B O   1 
HETATM 8169 O  O   . HOH M 6 .   ? 6.444   1.266   63.665  1.00 52.29  ? 851  HOH B O   1 
HETATM 8170 O  O   . HOH M 6 .   ? 4.095   -20.231 68.633  1.00 32.61  ? 852  HOH B O   1 
HETATM 8171 O  O   . HOH M 6 .   ? -0.977  -48.924 76.725  1.00 50.63  ? 853  HOH B O   1 
HETATM 8172 O  O   . HOH M 6 .   ? -19.995 -15.115 76.866  1.00 46.37  ? 854  HOH B O   1 
HETATM 8173 O  O   . HOH M 6 .   ? 4.010   -44.087 52.790  1.00 53.27  ? 855  HOH B O   1 
HETATM 8174 O  O   . HOH M 6 .   ? 0.067   -32.514 54.606  1.00 51.73  ? 856  HOH B O   1 
HETATM 8175 O  O   . HOH M 6 .   ? -22.317 -5.393  42.883  1.00 50.17  ? 857  HOH B O   1 
HETATM 8176 O  O   . HOH M 6 .   ? -1.635  -16.060 47.611  1.00 41.61  ? 858  HOH B O   1 
HETATM 8177 O  O   . HOH M 6 .   ? -2.553  -4.775  51.222  1.00 35.56  ? 859  HOH B O   1 
HETATM 8178 O  O   . HOH M 6 .   ? -22.817 -7.159  77.607  1.00 55.44  ? 860  HOH B O   1 
HETATM 8179 O  O   . HOH M 6 .   ? -21.982 -23.312 56.459  1.00 40.18  ? 861  HOH B O   1 
HETATM 8180 O  O   . HOH M 6 .   ? -20.700 -3.600  72.991  1.00 37.34  ? 862  HOH B O   1 
HETATM 8181 O  O   . HOH M 6 .   ? 31.701  -10.157 65.723  1.00 49.74  ? 863  HOH B O   1 
HETATM 8182 O  O   . HOH M 6 .   ? 10.319  -24.950 92.112  1.00 50.41  ? 864  HOH B O   1 
HETATM 8183 O  O   . HOH M 6 .   ? -8.082  -14.277 41.291  1.00 38.36  ? 865  HOH B O   1 
HETATM 8184 O  O   . HOH M 6 .   ? -18.912 -17.356 42.415  1.00 45.55  ? 866  HOH B O   1 
HETATM 8185 O  O   . HOH M 6 .   ? -23.082 -4.580  54.451  1.00 45.26  ? 867  HOH B O   1 
HETATM 8186 O  O   . HOH M 6 .   ? -5.702  -18.497 47.902  1.00 43.21  ? 868  HOH B O   1 
HETATM 8187 O  O   . HOH M 6 .   ? -20.751 -13.404 66.547  1.00 35.79  ? 869  HOH B O   1 
HETATM 8188 O  O   . HOH M 6 .   ? -10.395 -35.438 79.091  1.00 38.45  ? 870  HOH B O   1 
HETATM 8189 O  O   . HOH M 6 .   ? 19.073  -21.805 54.529  1.00 46.94  ? 871  HOH B O   1 
HETATM 8190 O  O   . HOH M 6 .   ? -9.609  -18.325 81.042  1.00 40.02  ? 872  HOH B O   1 
HETATM 8191 O  O   . HOH M 6 .   ? 11.795  -32.822 67.993  1.00 55.34  ? 873  HOH B O   1 
HETATM 8192 O  O   . HOH M 6 .   ? 5.562   -38.553 72.077  1.00 45.21  ? 874  HOH B O   1 
HETATM 8193 O  O   . HOH M 6 .   ? -6.934  -19.593 90.890  1.00 55.40  ? 875  HOH B O   1 
HETATM 8194 O  O   . HOH M 6 .   ? -2.918  -22.467 56.088  1.00 41.34  ? 876  HOH B O   1 
HETATM 8195 O  O   . HOH M 6 .   ? -19.125 -17.785 66.265  1.00 50.69  ? 877  HOH B O   1 
HETATM 8196 O  O   . HOH M 6 .   ? -25.470 -6.879  65.520  1.00 39.39  ? 878  HOH B O   1 
HETATM 8197 O  O   . HOH M 6 .   ? 23.515  -1.241  58.922  1.00 50.90  ? 879  HOH B O   1 
HETATM 8198 O  O   . HOH M 6 .   ? -3.454  -25.896 64.904  1.00 32.22  ? 880  HOH B O   1 
HETATM 8199 O  O   . HOH M 6 .   ? 3.603   -27.991 89.000  1.00 45.71  ? 881  HOH B O   1 
HETATM 8200 O  O   . HOH M 6 .   ? -1.615  -16.486 35.747  1.00 54.90  ? 882  HOH B O   1 
HETATM 8201 O  O   . HOH M 6 .   ? 9.178   -18.951 92.998  1.00 47.17  ? 883  HOH B O   1 
HETATM 8202 O  O   . HOH M 6 .   ? -10.866 -17.524 84.850  1.00 49.30  ? 884  HOH B O   1 
HETATM 8203 O  O   . HOH M 6 .   ? -19.093 -6.542  37.340  1.00 44.16  ? 885  HOH B O   1 
HETATM 8204 O  O   . HOH M 6 .   ? -3.596  -33.693 63.399  1.00 51.36  ? 886  HOH B O   1 
HETATM 8205 O  O   . HOH M 6 .   ? 8.277   3.804   64.875  1.00 58.29  ? 887  HOH B O   1 
HETATM 8206 O  O   . HOH M 6 .   ? -10.481 6.342   73.911  1.00 52.50  ? 888  HOH B O   1 
HETATM 8207 O  O   . HOH M 6 .   ? 2.915   7.135   53.283  1.00 46.68  ? 889  HOH B O   1 
HETATM 8208 O  O   . HOH M 6 .   ? -13.531 -35.249 79.187  1.00 56.80  ? 890  HOH B O   1 
HETATM 8209 O  O   . HOH M 6 .   ? -13.064 2.865   39.425  1.00 52.79  ? 891  HOH B O   1 
HETATM 8210 O  O   . HOH M 6 .   ? -7.205  -34.778 86.654  1.00 46.60  ? 892  HOH B O   1 
HETATM 8211 O  O   . HOH M 6 .   ? -13.412 12.751  57.571  1.00 53.70  ? 893  HOH B O   1 
HETATM 8212 O  O   . HOH M 6 .   ? 9.097   -9.402  81.720  1.00 48.52  ? 894  HOH B O   1 
HETATM 8213 O  O   . HOH M 6 .   ? 17.861  -12.307 76.663  1.00 51.08  ? 895  HOH B O   1 
HETATM 8214 O  O   . HOH M 6 .   ? -6.262  -38.550 83.475  1.00 42.82  ? 896  HOH B O   1 
HETATM 8215 O  O   . HOH M 6 .   ? -8.256  12.934  54.882  1.00 44.99  ? 897  HOH B O   1 
HETATM 8216 O  O   . HOH M 6 .   ? -0.478  10.074  54.880  1.00 40.70  ? 898  HOH B O   1 
HETATM 8217 O  O   . HOH M 6 .   ? 9.127   -32.732 78.804  1.00 50.85  ? 899  HOH B O   1 
HETATM 8218 O  O   . HOH M 6 .   ? 7.197   -42.465 49.326  1.00 61.79  ? 900  HOH B O   1 
HETATM 8219 O  O   . HOH M 6 .   ? -9.242  -22.980 87.194  1.00 39.91  ? 901  HOH B O   1 
HETATM 8220 O  O   . HOH M 6 .   ? 0.461   -6.896  77.727  1.00 54.23  ? 902  HOH B O   1 
HETATM 8221 O  O   . HOH M 6 .   ? 23.092  -10.744 72.350  1.00 48.51  ? 903  HOH B O   1 
HETATM 8222 O  O   . HOH M 6 .   ? 16.599  -26.939 68.276  1.00 45.40  ? 904  HOH B O   1 
HETATM 8223 O  O   . HOH M 6 .   ? -16.711 -24.393 64.800  1.00 52.04  ? 905  HOH B O   1 
HETATM 8224 O  O   . HOH M 6 .   ? -13.919 12.262  60.404  1.00 44.05  ? 906  HOH B O   1 
HETATM 8225 O  O   . HOH M 6 .   ? -16.739 -17.652 67.797  1.00 40.76  ? 907  HOH B O   1 
HETATM 8226 O  O   . HOH M 6 .   ? 6.351   -33.630 71.529  1.00 49.02  ? 908  HOH B O   1 
HETATM 8227 O  O   . HOH M 6 .   ? -6.670  9.592   45.994  1.00 45.64  ? 909  HOH B O   1 
HETATM 8228 O  O   . HOH M 6 .   ? -15.372 -21.225 73.876  1.00 50.77  ? 910  HOH B O   1 
HETATM 8229 O  O   . HOH M 6 .   ? 6.688   -8.918  78.915  1.00 54.12  ? 911  HOH B O   1 
HETATM 8230 O  O   . HOH M 6 .   ? -15.019 -30.694 62.612  1.00 54.65  ? 912  HOH B O   1 
HETATM 8231 O  O   . HOH M 6 .   ? 26.294  -8.502  53.588  1.00 47.36  ? 913  HOH B O   1 
HETATM 8232 O  O   . HOH M 6 .   ? 13.897  -9.330  77.511  1.00 52.52  ? 914  HOH B O   1 
HETATM 8233 O  O   . HOH M 6 .   ? -3.202  -17.824 46.379  1.00 45.27  ? 915  HOH B O   1 
HETATM 8234 O  O   . HOH M 6 .   ? -15.779 -28.532 77.592  1.00 52.79  ? 916  HOH B O   1 
HETATM 8235 O  O   . HOH M 6 .   ? -11.382 -35.418 64.703  1.00 49.43  ? 917  HOH B O   1 
HETATM 8236 O  O   . HOH M 6 .   ? -2.409  -7.169  77.457  1.00 41.74  ? 918  HOH B O   1 
HETATM 8237 O  O   . HOH M 6 .   ? 6.248   -9.085  82.634  1.00 50.90  ? 919  HOH B O   1 
HETATM 8238 O  O   . HOH M 6 .   ? 20.786  -18.100 49.008  1.00 56.13  ? 920  HOH B O   1 
HETATM 8239 O  O   . HOH M 6 .   ? -19.407 1.753   74.414  1.00 45.57  ? 921  HOH B O   1 
HETATM 8240 O  O   . HOH M 6 .   ? -4.552  -1.495  67.701  1.00 49.09  ? 922  HOH B O   1 
HETATM 8241 O  O   . HOH M 6 .   ? -9.975  -22.304 81.089  1.00 45.13  ? 923  HOH B O   1 
HETATM 8242 O  O   . HOH M 6 .   ? -24.584 -7.520  49.721  1.00 47.22  ? 924  HOH B O   1 
HETATM 8243 O  O   . HOH M 6 .   ? -1.346  6.086   49.071  1.00 53.04  ? 925  HOH B O   1 
HETATM 8244 O  O   . HOH M 6 .   ? -6.850  -22.344 56.445  1.00 38.08  ? 926  HOH B O   1 
HETATM 8245 O  O   . HOH M 6 .   ? 10.464  -8.789  84.270  1.00 57.22  ? 927  HOH B O   1 
HETATM 8246 O  O   . HOH M 6 .   ? -23.053 -8.887  70.916  1.00 44.34  ? 928  HOH B O   1 
HETATM 8247 O  O   . HOH M 6 .   ? -5.778  -2.332  65.501  1.00 51.18  ? 929  HOH B O   1 
HETATM 8248 O  O   . HOH M 6 .   ? -2.084  -2.926  68.469  1.00 50.10  ? 930  HOH B O   1 
HETATM 8249 O  O   . HOH M 6 .   ? 24.517  -15.692 71.697  1.00 50.02  ? 931  HOH B O   1 
HETATM 8250 O  O   . HOH M 6 .   ? -6.595  -19.711 52.193  1.00 40.73  ? 932  HOH B O   1 
HETATM 8251 O  O   . HOH M 6 .   ? -8.479  -21.158 52.569  1.00 45.76  ? 933  HOH B O   1 
HETATM 8252 O  O   . HOH M 6 .   ? -24.669 2.605   64.885  1.00 46.69  ? 934  HOH B O   1 
HETATM 8253 O  O   . HOH M 6 .   ? 7.126   -5.239  40.376  1.00 57.76  ? 935  HOH B O   1 
HETATM 8254 O  O   . HOH M 6 .   ? -23.759 -19.118 62.328  1.00 49.24  ? 936  HOH B O   1 
HETATM 8255 O  O   . HOH M 6 .   ? 20.582  -24.780 54.854  1.00 66.19  ? 937  HOH B O   1 
HETATM 8256 O  O   . HOH M 6 .   ? 24.605  -0.817  55.876  1.00 61.32  ? 938  HOH B O   1 
HETATM 8257 O  O   . HOH M 6 .   ? 2.414   -29.196 91.294  1.00 50.21  ? 939  HOH B O   1 
HETATM 8258 O  O   . HOH M 6 .   ? -25.391 -9.623  71.543  1.00 56.39  ? 940  HOH B O   1 
HETATM 8259 O  O   . HOH M 6 .   ? -12.348 -36.004 73.236  1.00 46.03  ? 941  HOH B O   1 
HETATM 8260 O  O   . HOH M 6 .   ? 30.572  -6.736  58.510  1.00 47.43  ? 942  HOH B O   1 
HETATM 8261 O  O   . HOH M 6 .   ? -10.706 -33.299 80.647  1.00 47.57  ? 943  HOH B O   1 
HETATM 8262 O  O   . HOH M 6 .   ? -17.431 -11.074 85.222  1.00 58.74  ? 944  HOH B O   1 
HETATM 8263 O  O   . HOH M 6 .   ? 9.806   0.405   51.757  1.00 52.32  ? 945  HOH B O   1 
HETATM 8264 O  O   . HOH M 6 .   ? -13.524 -35.805 76.826  1.00 46.21  ? 946  HOH B O   1 
HETATM 8265 O  O   . HOH M 6 .   ? -16.100 -27.404 84.041  1.00 57.12  ? 947  HOH B O   1 
HETATM 8266 O  O   . HOH M 6 .   ? -16.273 -27.185 64.910  1.00 52.88  ? 948  HOH B O   1 
HETATM 8267 O  O   . HOH M 6 .   ? -21.647 3.193   55.516  1.00 48.58  ? 949  HOH B O   1 
HETATM 8268 O  O   . HOH M 6 .   ? -1.480  -0.664  64.934  1.00 52.84  ? 950  HOH B O   1 
HETATM 8269 O  O   . HOH M 6 .   ? -0.386  -46.913 80.944  1.00 47.62  ? 951  HOH B O   1 
HETATM 8270 O  O   . HOH M 6 .   ? 18.100  -25.097 61.481  1.00 50.55  ? 952  HOH B O   1 
HETATM 8271 O  O   . HOH M 6 .   ? -23.742 -13.352 66.613  1.00 56.24  ? 953  HOH B O   1 
HETATM 8272 O  O   . HOH M 6 .   ? -6.952  -25.584 89.106  1.00 56.20  ? 954  HOH B O   1 
HETATM 8273 O  O   . HOH M 6 .   ? -10.074 -37.235 82.806  1.00 53.87  ? 955  HOH B O   1 
HETATM 8274 O  O   . HOH M 6 .   ? 21.775  -14.669 44.093  1.00 66.72  ? 956  HOH B O   1 
HETATM 8275 O  O   . HOH M 6 .   ? -4.538  10.215  47.071  1.00 55.57  ? 957  HOH B O   1 
HETATM 8276 O  O   . HOH M 6 .   ? -7.000  -20.321 46.545  1.00 51.74  ? 958  HOH B O   1 
HETATM 8277 O  O   . HOH M 6 .   ? 7.440   -15.473 74.513  1.00 33.77  ? 959  HOH B O   1 
HETATM 8278 O  O   . HOH M 6 .   ? -20.334 -6.514  42.096  1.00 57.12  ? 960  HOH B O   1 
HETATM 8279 O  O   . HOH M 6 .   ? -8.828  -20.370 82.622  1.00 43.87  ? 961  HOH B O   1 
HETATM 8280 O  O   . HOH M 6 .   ? 0.452   -15.527 37.030  1.00 56.46  ? 962  HOH B O   1 
HETATM 8281 O  O   . HOH M 6 .   ? -17.310 1.289   40.831  1.00 48.45  ? 963  HOH B O   1 
HETATM 8282 O  O   . HOH M 6 .   ? 8.097   -5.534  68.317  1.00 57.30  ? 964  HOH B O   1 
HETATM 8283 O  O   . HOH M 6 .   ? 6.946   -12.827 90.473  1.00 57.01  ? 965  HOH B O   1 
HETATM 8284 O  O   . HOH M 6 .   ? 1.095   -12.886 36.092  1.00 45.16  ? 966  HOH B O   1 
HETATM 8285 O  O   . HOH M 6 .   ? -5.172  -23.307 54.858  1.00 43.72  ? 967  HOH B O   1 
HETATM 8286 O  O   . HOH M 6 .   ? -24.396 5.008   61.224  1.00 42.54  ? 968  HOH B O   1 
HETATM 8287 O  O   . HOH M 6 .   ? -14.991 -8.421  85.173  1.00 51.77  ? 969  HOH B O   1 
HETATM 8288 O  O   . HOH M 6 .   ? 15.752  -11.752 79.425  1.00 52.26  ? 970  HOH B O   1 
HETATM 8289 O  O   . HOH M 6 .   ? -13.613 -24.606 50.984  1.00 51.19  ? 971  HOH B O   1 
HETATM 8290 O  O   . HOH M 6 .   ? -1.645  12.373  54.135  1.00 49.65  ? 972  HOH B O   1 
HETATM 8291 O  O   . HOH M 6 .   ? 4.253   -11.749 87.426  1.00 52.73  ? 973  HOH B O   1 
HETATM 8292 O  O   . HOH M 6 .   ? 20.238  -0.959  63.253  1.00 57.70  ? 974  HOH B O   1 
HETATM 8293 O  O   . HOH M 6 .   ? -17.521 6.652   50.467  1.00 53.64  ? 975  HOH B O   1 
HETATM 8294 O  O   . HOH M 6 .   ? -13.353 -31.909 66.454  1.00 55.08  ? 976  HOH B O   1 
HETATM 8295 O  O   . HOH M 6 .   ? -12.808 -32.306 76.121  1.00 51.01  ? 977  HOH B O   1 
HETATM 8296 O  O   . HOH M 6 .   ? -8.375  -16.314 87.673  1.00 43.85  ? 978  HOH B O   1 
HETATM 8297 O  O   . HOH M 6 .   ? -2.349  -45.341 82.074  1.00 40.34  ? 979  HOH B O   1 
HETATM 8298 O  O   . HOH M 6 .   ? 17.540  -22.737 91.554  1.00 53.77  ? 980  HOH B O   1 
HETATM 8299 O  O   . HOH M 6 .   ? -17.070 -19.950 68.133  1.00 51.72  ? 981  HOH B O   1 
HETATM 8300 O  O   . HOH M 6 .   ? -15.173 -22.003 49.687  1.00 41.38  ? 982  HOH B O   1 
HETATM 8301 O  O   . HOH M 6 .   ? -11.414 -33.586 69.485  1.00 45.85  ? 983  HOH B O   1 
HETATM 8302 O  O   . HOH M 6 .   ? 13.177  -17.493 88.502  1.00 50.10  ? 984  HOH B O   1 
HETATM 8303 O  O   . HOH M 6 .   ? -22.968 3.800   63.510  1.00 41.47  ? 985  HOH B O   1 
HETATM 8304 O  O   . HOH M 6 .   ? -2.408  1.938   43.758  1.00 51.51  ? 986  HOH B O   1 
HETATM 8305 O  O   . HOH M 6 .   ? -14.591 -2.020  37.459  1.00 55.79  ? 987  HOH B O   1 
HETATM 8306 O  O   . HOH M 6 .   ? 2.028   6.661   50.005  1.00 55.39  ? 988  HOH B O   1 
HETATM 8307 O  O   . HOH M 6 .   ? -12.866 9.080   42.474  1.00 55.92  ? 989  HOH B O   1 
HETATM 8308 O  O   . HOH M 6 .   ? 6.206   2.477   47.065  1.00 49.70  ? 990  HOH B O   1 
HETATM 8309 O  O   . HOH M 6 .   ? -19.972 -26.622 58.692  1.00 53.27  ? 991  HOH B O   1 
HETATM 8310 O  O   . HOH M 6 .   ? 1.840   10.461  56.205  1.00 53.55  ? 992  HOH B O   1 
HETATM 8311 O  O   . HOH M 6 .   ? 23.019  -13.200 71.024  1.00 39.40  ? 993  HOH B O   1 
HETATM 8312 O  O   . HOH M 6 .   ? -5.543  -20.193 49.936  1.00 45.81  ? 994  HOH B O   1 
HETATM 8313 O  O   . HOH M 6 .   ? 6.403   -50.721 79.616  1.00 52.05  ? 995  HOH B O   1 
HETATM 8314 O  O   . HOH M 6 .   ? -5.419  3.335   42.780  1.00 48.69  ? 996  HOH B O   1 
HETATM 8315 O  O   . HOH M 6 .   ? -20.222 8.329   52.185  1.00 59.97  ? 997  HOH B O   1 
HETATM 8316 O  O   . HOH M 6 .   ? 17.806  -28.675 57.441  1.00 62.92  ? 998  HOH B O   1 
HETATM 8317 O  O   . HOH M 6 .   ? 9.894   -6.812  69.465  1.00 51.96  ? 999  HOH B O   1 
HETATM 8318 O  O   . HOH M 6 .   ? -13.944 -15.239 41.255  1.00 41.29  ? 1000 HOH B O   1 
HETATM 8319 O  O   . HOH M 6 .   ? -13.739 0.081   40.113  1.00 49.68  ? 1001 HOH B O   1 
HETATM 8320 O  O   . HOH M 6 .   ? -10.928 -34.685 76.374  1.00 48.36  ? 1002 HOH B O   1 
HETATM 8321 O  O   . HOH M 6 .   ? -8.662  -14.679 89.672  1.00 58.91  ? 1003 HOH B O   1 
HETATM 8322 O  O   . HOH M 6 .   ? -17.257 -28.349 79.951  1.00 60.71  ? 1004 HOH B O   1 
HETATM 8323 O  O   . HOH M 6 .   ? -2.889  -49.401 79.096  1.00 51.20  ? 1005 HOH B O   1 
HETATM 8324 O  O   . HOH M 6 .   ? 30.941  -9.786  58.909  1.00 49.56  ? 1006 HOH B O   1 
HETATM 8325 O  O   . HOH M 6 .   ? -15.387 -21.873 71.358  1.00 51.98  ? 1007 HOH B O   1 
HETATM 8326 O  O   . HOH M 6 .   ? -13.015 -31.868 71.555  1.00 44.58  ? 1008 HOH B O   1 
HETATM 8327 O  O   . HOH M 6 .   ? -5.832  -1.840  72.980  1.00 50.60  ? 1009 HOH B O   1 
HETATM 8328 O  O   . HOH M 6 .   ? -17.249 -28.852 82.271  1.00 55.61  ? 1010 HOH B O   1 
HETATM 8329 O  O   . HOH M 6 .   ? 15.084  -29.279 78.179  1.00 59.66  ? 1011 HOH B O   1 
HETATM 8330 O  O   . HOH M 6 .   ? 26.525  -12.307 69.759  1.00 45.83  ? 1012 HOH B O   1 
HETATM 8331 O  O   . HOH M 6 .   ? -7.151  -22.851 48.214  1.00 54.52  ? 1013 HOH B O   1 
HETATM 8332 O  O   . HOH M 6 .   ? -24.359 4.568   58.608  1.00 52.47  ? 1014 HOH B O   1 
HETATM 8333 O  O   . HOH M 6 .   ? -18.756 12.248  56.093  1.00 53.25  ? 1015 HOH B O   1 
HETATM 8334 O  O   . HOH M 6 .   ? -22.070 6.037   55.842  1.00 49.42  ? 1016 HOH B O   1 
HETATM 8335 O  O   . HOH M 6 .   ? 4.765   -26.010 42.634  1.00 54.36  ? 1017 HOH B O   1 
HETATM 8336 O  O   . HOH M 6 .   ? -25.573 -6.113  57.797  1.00 50.69  ? 1018 HOH B O   1 
HETATM 8337 O  O   . HOH M 6 .   ? -16.607 -22.443 67.032  1.00 49.20  ? 1019 HOH B O   1 
HETATM 8338 O  O   . HOH M 6 .   ? -10.554 -34.159 73.508  1.00 41.72  ? 1020 HOH B O   1 
HETATM 8339 O  O   . HOH M 6 .   ? 9.686   -33.770 82.252  1.00 60.10  ? 1021 HOH B O   1 
HETATM 8340 O  O   . HOH M 6 .   ? 3.606   9.233   54.806  1.00 55.87  ? 1022 HOH B O   1 
HETATM 8341 O  O   . HOH M 6 .   ? -9.424  15.375  53.557  1.00 59.50  ? 1023 HOH B O   1 
HETATM 8342 O  O   . HOH M 6 .   ? -0.663  -48.201 72.655  1.00 55.42  ? 1024 HOH B O   1 
HETATM 8343 O  O   . HOH M 6 .   ? -12.056 11.743  43.659  1.00 66.91  ? 1025 HOH B O   1 
HETATM 8344 O  O   . HOH M 6 .   ? -5.408  -23.079 49.984  1.00 53.38  ? 1026 HOH B O   1 
HETATM 8345 O  O   . HOH M 6 .   ? -21.880 6.960   53.008  1.00 65.57  ? 1027 HOH B O   1 
# 
