data_8YB3
# 
_entry.id   8YB3 
# 
_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   8YB3         pdb_00008yb3 10.2210/pdb8yb3/pdb 
WWPDB D_1300044636 ?            ?                   
# 
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                        8YB3 
_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 'OXYGEN MOLECULE'                                                              31.999    2   ?                 ? 
? ? 
6 non-polymer syn GLYCEROL                                                                       92.094    5   ?                 ? 
? ? 
7 water       nat water                                                                          18.015    827 ?                 ? 
? ? 
# 
_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 'OXYGEN MOLECULE'                                                              OXY 
6 GLYCEROL                                                                       GOL 
7 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 14581' 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Priestia megaterium NBRC 15308 = ATCC 14581' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1348623 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                        ? 'C3 H7 N O2'       
89.093  
ARG 'L-peptide linking' y ARGININE                                                                       ? 'C6 H15 N4 O2 1'   
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                     ? 'C4 H8 N2 O3'      
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                ? 'C4 H7 N O4'       
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                       ? 'C3 H7 N O2 S'     
121.158 
D0L non-polymer         . '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' ? 'C21 H32 N2 O3'    
360.490 
GLN 'L-peptide linking' y GLUTAMINE                                                                      ? 'C5 H10 N2 O3'     
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                ? 'C5 H9 N O4'       
147.129 
GLY 'peptide linking'   y GLYCINE                                                                        ? 'C2 H5 N O2'       
75.067  
GOL non-polymer         . GLYCEROL                                                                       
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                              HEME 'C34 H32 Fe N4 O4' 
616.487 
HIS 'L-peptide linking' y HISTIDINE                                                                      ? 'C6 H10 N3 O2 1'   
156.162 
HOH non-polymer         . WATER                                                                          ? 'H2 O'             
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                     ? 'C6 H13 N O2'      
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                        ? 'C6 H13 N O2'      
131.173 
LYS 'L-peptide linking' y LYSINE                                                                         ? 'C6 H15 N2 O2 1'   
147.195 
MET 'L-peptide linking' y METHIONINE                                                                     ? 'C5 H11 N O2 S'    
149.211 
OXY non-polymer         . 'OXYGEN MOLECULE'                                                              ? O2                 
31.999  
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 OXY ? ? OXY ? ? 'SUBJECT OF INVESTIGATION' ? 
3 SYN ? ? SYN ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEM 1   501  501 HEM HEM A . 
D 3 D0L 1   502  503 D0L 7PF A . 
E 4 SYN 1   503  601 SYN SYN A . 
F 5 OXY 1   504  602 OXY OXY A . 
G 6 GOL 1   505  603 GOL GOL A . 
H 2 HEM 1   501  501 HEM HEM B . 
I 3 D0L 1   502  503 D0L 7PF B . 
J 4 SYN 1   503  601 SYN SYN B . 
K 5 OXY 1   504  602 OXY OXY B . 
L 6 GOL 1   505  603 GOL GOL B . 
M 6 GOL 1   506  604 GOL GOL B . 
N 6 GOL 1   507  605 GOL GOL B . 
O 6 GOL 1   508  606 GOL GOL B . 
P 7 HOH 1   601  819 HOH HOH A . 
P 7 HOH 2   602  198 HOH HOH A . 
P 7 HOH 3   603  820 HOH HOH A . 
P 7 HOH 4   604  208 HOH HOH A . 
P 7 HOH 5   605  492 HOH HOH A . 
P 7 HOH 6   606  501 HOH HOH A . 
P 7 HOH 7   607  569 HOH HOH A . 
P 7 HOH 8   608  512 HOH HOH A . 
P 7 HOH 9   609  506 HOH HOH A . 
P 7 HOH 10  610  463 HOH HOH A . 
P 7 HOH 11  611  582 HOH HOH A . 
P 7 HOH 12  612  240 HOH HOH A . 
P 7 HOH 13  613  431 HOH HOH A . 
P 7 HOH 14  614  442 HOH HOH A . 
P 7 HOH 15  615  404 HOH HOH A . 
P 7 HOH 16  616  723 HOH HOH A . 
P 7 HOH 17  617  810 HOH HOH A . 
P 7 HOH 18  618  8   HOH HOH A . 
P 7 HOH 19  619  376 HOH HOH A . 
P 7 HOH 20  620  605 HOH HOH A . 
P 7 HOH 21  621  283 HOH HOH A . 
P 7 HOH 22  622  476 HOH HOH A . 
P 7 HOH 23  623  531 HOH HOH A . 
P 7 HOH 24  624  495 HOH HOH A . 
P 7 HOH 25  625  706 HOH HOH A . 
P 7 HOH 26  626  222 HOH HOH A . 
P 7 HOH 27  627  821 HOH HOH A . 
P 7 HOH 28  628  160 HOH HOH A . 
P 7 HOH 29  629  50  HOH HOH A . 
P 7 HOH 30  630  268 HOH HOH A . 
P 7 HOH 31  631  471 HOH HOH A . 
P 7 HOH 32  632  693 HOH HOH A . 
P 7 HOH 33  633  120 HOH HOH A . 
P 7 HOH 34  634  756 HOH HOH A . 
P 7 HOH 35  635  19  HOH HOH A . 
P 7 HOH 36  636  617 HOH HOH A . 
P 7 HOH 37  637  291 HOH HOH A . 
P 7 HOH 38  638  167 HOH HOH A . 
P 7 HOH 39  639  575 HOH HOH A . 
P 7 HOH 40  640  485 HOH HOH A . 
P 7 HOH 41  641  517 HOH HOH A . 
P 7 HOH 42  642  76  HOH HOH A . 
P 7 HOH 43  643  664 HOH HOH A . 
P 7 HOH 44  644  537 HOH HOH A . 
P 7 HOH 45  645  36  HOH HOH A . 
P 7 HOH 46  646  373 HOH HOH A . 
P 7 HOH 47  647  286 HOH HOH A . 
P 7 HOH 48  648  92  HOH HOH A . 
P 7 HOH 49  649  480 HOH HOH A . 
P 7 HOH 50  650  72  HOH HOH A . 
P 7 HOH 51  651  22  HOH HOH A . 
P 7 HOH 52  652  62  HOH HOH A . 
P 7 HOH 53  653  607 HOH HOH A . 
P 7 HOH 54  654  354 HOH HOH A . 
P 7 HOH 55  655  18  HOH HOH A . 
P 7 HOH 56  656  328 HOH HOH A . 
P 7 HOH 57  657  527 HOH HOH A . 
P 7 HOH 58  658  78  HOH HOH A . 
P 7 HOH 59  659  502 HOH HOH A . 
P 7 HOH 60  660  814 HOH HOH A . 
P 7 HOH 61  661  100 HOH HOH A . 
P 7 HOH 62  662  307 HOH HOH A . 
P 7 HOH 63  663  237 HOH HOH A . 
P 7 HOH 64  664  67  HOH HOH A . 
P 7 HOH 65  665  717 HOH HOH A . 
P 7 HOH 66  666  690 HOH HOH A . 
P 7 HOH 67  667  159 HOH HOH A . 
P 7 HOH 68  668  535 HOH HOH A . 
P 7 HOH 69  669  311 HOH HOH A . 
P 7 HOH 70  670  79  HOH HOH A . 
P 7 HOH 71  671  269 HOH HOH A . 
P 7 HOH 72  672  309 HOH HOH A . 
P 7 HOH 73  673  226 HOH HOH A . 
P 7 HOH 74  674  590 HOH HOH A . 
P 7 HOH 75  675  467 HOH HOH A . 
P 7 HOH 76  676  177 HOH HOH A . 
P 7 HOH 77  677  162 HOH HOH A . 
P 7 HOH 78  678  679 HOH HOH A . 
P 7 HOH 79  679  206 HOH HOH A . 
P 7 HOH 80  680  446 HOH HOH A . 
P 7 HOH 81  681  707 HOH HOH A . 
P 7 HOH 82  682  49  HOH HOH A . 
P 7 HOH 83  683  521 HOH HOH A . 
P 7 HOH 84  684  606 HOH HOH A . 
P 7 HOH 85  685  680 HOH HOH A . 
P 7 HOH 86  686  152 HOH HOH A . 
P 7 HOH 87  687  595 HOH HOH A . 
P 7 HOH 88  688  186 HOH HOH A . 
P 7 HOH 89  689  724 HOH HOH A . 
P 7 HOH 90  690  732 HOH HOH A . 
P 7 HOH 91  691  190 HOH HOH A . 
P 7 HOH 92  692  197 HOH HOH A . 
P 7 HOH 93  693  704 HOH HOH A . 
P 7 HOH 94  694  616 HOH HOH A . 
P 7 HOH 95  695  589 HOH HOH A . 
P 7 HOH 96  696  1   HOH HOH A . 
P 7 HOH 97  697  91  HOH HOH A . 
P 7 HOH 98  698  71  HOH HOH A . 
P 7 HOH 99  699  175 HOH HOH A . 
P 7 HOH 100 700  150 HOH HOH A . 
P 7 HOH 101 701  245 HOH HOH A . 
P 7 HOH 102 702  334 HOH HOH A . 
P 7 HOH 103 703  578 HOH HOH A . 
P 7 HOH 104 704  15  HOH HOH A . 
P 7 HOH 105 705  477 HOH HOH A . 
P 7 HOH 106 706  188 HOH HOH A . 
P 7 HOH 107 707  249 HOH HOH A . 
P 7 HOH 108 708  224 HOH HOH A . 
P 7 HOH 109 709  151 HOH HOH A . 
P 7 HOH 110 710  388 HOH HOH A . 
P 7 HOH 111 711  598 HOH HOH A . 
P 7 HOH 112 712  199 HOH HOH A . 
P 7 HOH 113 713  324 HOH HOH A . 
P 7 HOH 114 714  562 HOH HOH A . 
P 7 HOH 115 715  321 HOH HOH A . 
P 7 HOH 116 716  59  HOH HOH A . 
P 7 HOH 117 717  386 HOH HOH A . 
P 7 HOH 118 718  656 HOH HOH A . 
P 7 HOH 119 719  494 HOH HOH A . 
P 7 HOH 120 720  412 HOH HOH A . 
P 7 HOH 121 721  303 HOH HOH A . 
P 7 HOH 122 722  759 HOH HOH A . 
P 7 HOH 123 723  520 HOH HOH A . 
P 7 HOH 124 724  64  HOH HOH A . 
P 7 HOH 125 725  81  HOH HOH A . 
P 7 HOH 126 726  352 HOH HOH A . 
P 7 HOH 127 727  357 HOH HOH A . 
P 7 HOH 128 728  603 HOH HOH A . 
P 7 HOH 129 729  112 HOH HOH A . 
P 7 HOH 130 730  179 HOH HOH A . 
P 7 HOH 131 731  37  HOH HOH A . 
P 7 HOH 132 732  233 HOH HOH A . 
P 7 HOH 133 733  12  HOH HOH A . 
P 7 HOH 134 734  90  HOH HOH A . 
P 7 HOH 135 735  96  HOH HOH A . 
P 7 HOH 136 736  137 HOH HOH A . 
P 7 HOH 137 737  89  HOH HOH A . 
P 7 HOH 138 738  157 HOH HOH A . 
P 7 HOH 139 739  272 HOH HOH A . 
P 7 HOH 140 740  487 HOH HOH A . 
P 7 HOH 141 741  221 HOH HOH A . 
P 7 HOH 142 742  346 HOH HOH A . 
P 7 HOH 143 743  822 HOH HOH A . 
P 7 HOH 144 744  564 HOH HOH A . 
P 7 HOH 145 745  47  HOH HOH A . 
P 7 HOH 146 746  16  HOH HOH A . 
P 7 HOH 147 747  554 HOH HOH A . 
P 7 HOH 148 748  612 HOH HOH A . 
P 7 HOH 149 749  200 HOH HOH A . 
P 7 HOH 150 750  601 HOH HOH A . 
P 7 HOH 151 751  192 HOH HOH A . 
P 7 HOH 152 752  360 HOH HOH A . 
P 7 HOH 153 753  447 HOH HOH A . 
P 7 HOH 154 754  287 HOH HOH A . 
P 7 HOH 155 755  536 HOH HOH A . 
P 7 HOH 156 756  9   HOH HOH A . 
P 7 HOH 157 757  630 HOH HOH A . 
P 7 HOH 158 758  95  HOH HOH A . 
P 7 HOH 159 759  267 HOH HOH A . 
P 7 HOH 160 760  139 HOH HOH A . 
P 7 HOH 161 761  195 HOH HOH A . 
P 7 HOH 162 762  257 HOH HOH A . 
P 7 HOH 163 763  254 HOH HOH A . 
P 7 HOH 164 764  505 HOH HOH A . 
P 7 HOH 165 765  60  HOH HOH A . 
P 7 HOH 166 766  342 HOH HOH A . 
P 7 HOH 167 767  117 HOH HOH A . 
P 7 HOH 168 768  719 HOH HOH A . 
P 7 HOH 169 769  164 HOH HOH A . 
P 7 HOH 170 770  470 HOH HOH A . 
P 7 HOH 171 771  166 HOH HOH A . 
P 7 HOH 172 772  27  HOH HOH A . 
P 7 HOH 173 773  729 HOH HOH A . 
P 7 HOH 174 774  93  HOH HOH A . 
P 7 HOH 175 775  645 HOH HOH A . 
P 7 HOH 176 776  524 HOH HOH A . 
P 7 HOH 177 777  336 HOH HOH A . 
P 7 HOH 178 778  348 HOH HOH A . 
P 7 HOH 179 779  123 HOH HOH A . 
P 7 HOH 180 780  202 HOH HOH A . 
P 7 HOH 181 781  304 HOH HOH A . 
P 7 HOH 182 782  17  HOH HOH A . 
P 7 HOH 183 783  6   HOH HOH A . 
P 7 HOH 184 784  437 HOH HOH A . 
P 7 HOH 185 785  799 HOH HOH A . 
P 7 HOH 186 786  649 HOH HOH A . 
P 7 HOH 187 787  472 HOH HOH A . 
P 7 HOH 188 788  648 HOH HOH A . 
P 7 HOH 189 789  702 HOH HOH A . 
P 7 HOH 190 790  794 HOH HOH A . 
P 7 HOH 191 791  593 HOH HOH A . 
P 7 HOH 192 792  138 HOH HOH A . 
P 7 HOH 193 793  703 HOH HOH A . 
P 7 HOH 194 794  26  HOH HOH A . 
P 7 HOH 195 795  288 HOH HOH A . 
P 7 HOH 196 796  65  HOH HOH A . 
P 7 HOH 197 797  181 HOH HOH A . 
P 7 HOH 198 798  460 HOH HOH A . 
P 7 HOH 199 799  302 HOH HOH A . 
P 7 HOH 200 800  701 HOH HOH A . 
P 7 HOH 201 801  788 HOH HOH A . 
P 7 HOH 202 802  201 HOH HOH A . 
P 7 HOH 203 803  523 HOH HOH A . 
P 7 HOH 204 804  513 HOH HOH A . 
P 7 HOH 205 805  51  HOH HOH A . 
P 7 HOH 206 806  708 HOH HOH A . 
P 7 HOH 207 807  518 HOH HOH A . 
P 7 HOH 208 808  644 HOH HOH A . 
P 7 HOH 209 809  209 HOH HOH A . 
P 7 HOH 210 810  20  HOH HOH A . 
P 7 HOH 211 811  70  HOH HOH A . 
P 7 HOH 212 812  507 HOH HOH A . 
P 7 HOH 213 813  102 HOH HOH A . 
P 7 HOH 214 814  397 HOH HOH A . 
P 7 HOH 215 815  212 HOH HOH A . 
P 7 HOH 216 816  196 HOH HOH A . 
P 7 HOH 217 817  824 HOH HOH A . 
P 7 HOH 218 818  803 HOH HOH A . 
P 7 HOH 219 819  280 HOH HOH A . 
P 7 HOH 220 820  158 HOH HOH A . 
P 7 HOH 221 821  317 HOH HOH A . 
P 7 HOH 222 822  115 HOH HOH A . 
P 7 HOH 223 823  331 HOH HOH A . 
P 7 HOH 224 824  274 HOH HOH A . 
P 7 HOH 225 825  246 HOH HOH A . 
P 7 HOH 226 826  276 HOH HOH A . 
P 7 HOH 227 827  522 HOH HOH A . 
P 7 HOH 228 828  313 HOH HOH A . 
P 7 HOH 229 829  204 HOH HOH A . 
P 7 HOH 230 830  458 HOH HOH A . 
P 7 HOH 231 831  640 HOH HOH A . 
P 7 HOH 232 832  767 HOH HOH A . 
P 7 HOH 233 833  389 HOH HOH A . 
P 7 HOH 234 834  682 HOH HOH A . 
P 7 HOH 235 835  295 HOH HOH A . 
P 7 HOH 236 836  270 HOH HOH A . 
P 7 HOH 237 837  547 HOH HOH A . 
P 7 HOH 238 838  44  HOH HOH A . 
P 7 HOH 239 839  804 HOH HOH A . 
P 7 HOH 240 840  716 HOH HOH A . 
P 7 HOH 241 841  56  HOH HOH A . 
P 7 HOH 242 842  135 HOH HOH A . 
P 7 HOH 243 843  516 HOH HOH A . 
P 7 HOH 244 844  696 HOH HOH A . 
P 7 HOH 245 845  231 HOH HOH A . 
P 7 HOH 246 846  278 HOH HOH A . 
P 7 HOH 247 847  46  HOH HOH A . 
P 7 HOH 248 848  591 HOH HOH A . 
P 7 HOH 249 849  459 HOH HOH A . 
P 7 HOH 250 850  296 HOH HOH A . 
P 7 HOH 251 851  251 HOH HOH A . 
P 7 HOH 252 852  218 HOH HOH A . 
P 7 HOH 253 853  576 HOH HOH A . 
P 7 HOH 254 854  735 HOH HOH A . 
P 7 HOH 255 855  105 HOH HOH A . 
P 7 HOH 256 856  800 HOH HOH A . 
P 7 HOH 257 857  762 HOH HOH A . 
P 7 HOH 258 858  479 HOH HOH A . 
P 7 HOH 259 859  462 HOH HOH A . 
P 7 HOH 260 860  818 HOH HOH A . 
P 7 HOH 261 861  538 HOH HOH A . 
P 7 HOH 262 862  469 HOH HOH A . 
P 7 HOH 263 863  241 HOH HOH A . 
P 7 HOH 264 864  581 HOH HOH A . 
P 7 HOH 265 865  104 HOH HOH A . 
P 7 HOH 266 866  721 HOH HOH A . 
P 7 HOH 267 867  746 HOH HOH A . 
P 7 HOH 268 868  533 HOH HOH A . 
P 7 HOH 269 869  387 HOH HOH A . 
P 7 HOH 270 870  720 HOH HOH A . 
P 7 HOH 271 871  691 HOH HOH A . 
P 7 HOH 272 872  418 HOH HOH A . 
P 7 HOH 273 873  374 HOH HOH A . 
P 7 HOH 274 874  514 HOH HOH A . 
P 7 HOH 275 875  213 HOH HOH A . 
P 7 HOH 276 876  621 HOH HOH A . 
P 7 HOH 277 877  553 HOH HOH A . 
P 7 HOH 278 878  777 HOH HOH A . 
P 7 HOH 279 879  797 HOH HOH A . 
P 7 HOH 280 880  733 HOH HOH A . 
P 7 HOH 281 881  770 HOH HOH A . 
P 7 HOH 282 882  532 HOH HOH A . 
P 7 HOH 283 883  86  HOH HOH A . 
P 7 HOH 284 884  422 HOH HOH A . 
P 7 HOH 285 885  567 HOH HOH A . 
P 7 HOH 286 886  375 HOH HOH A . 
P 7 HOH 287 887  405 HOH HOH A . 
P 7 HOH 288 888  678 HOH HOH A . 
P 7 HOH 289 889  473 HOH HOH A . 
P 7 HOH 290 890  811 HOH HOH A . 
P 7 HOH 291 891  592 HOH HOH A . 
P 7 HOH 292 892  755 HOH HOH A . 
P 7 HOH 293 893  411 HOH HOH A . 
P 7 HOH 294 894  808 HOH HOH A . 
P 7 HOH 295 895  613 HOH HOH A . 
P 7 HOH 296 896  97  HOH HOH A . 
P 7 HOH 297 897  556 HOH HOH A . 
P 7 HOH 298 898  542 HOH HOH A . 
P 7 HOH 299 899  574 HOH HOH A . 
P 7 HOH 300 900  667 HOH HOH A . 
P 7 HOH 301 901  549 HOH HOH A . 
P 7 HOH 302 902  662 HOH HOH A . 
P 7 HOH 303 903  482 HOH HOH A . 
P 7 HOH 304 904  398 HOH HOH A . 
P 7 HOH 305 905  587 HOH HOH A . 
P 7 HOH 306 906  827 HOH HOH A . 
P 7 HOH 307 907  714 HOH HOH A . 
P 7 HOH 308 908  468 HOH HOH A . 
P 7 HOH 309 909  781 HOH HOH A . 
P 7 HOH 310 910  292 HOH HOH A . 
P 7 HOH 311 911  384 HOH HOH A . 
P 7 HOH 312 912  451 HOH HOH A . 
P 7 HOH 313 913  687 HOH HOH A . 
P 7 HOH 314 914  726 HOH HOH A . 
P 7 HOH 315 915  13  HOH HOH A . 
P 7 HOH 316 916  444 HOH HOH A . 
P 7 HOH 317 917  711 HOH HOH A . 
P 7 HOH 318 918  475 HOH HOH A . 
P 7 HOH 319 919  642 HOH HOH A . 
P 7 HOH 320 920  573 HOH HOH A . 
P 7 HOH 321 921  600 HOH HOH A . 
P 7 HOH 322 922  509 HOH HOH A . 
P 7 HOH 323 923  294 HOH HOH A . 
P 7 HOH 324 924  783 HOH HOH A . 
P 7 HOH 325 925  609 HOH HOH A . 
P 7 HOH 326 926  692 HOH HOH A . 
P 7 HOH 327 927  560 HOH HOH A . 
P 7 HOH 328 928  666 HOH HOH A . 
P 7 HOH 329 929  748 HOH HOH A . 
P 7 HOH 330 930  628 HOH HOH A . 
P 7 HOH 331 931  465 HOH HOH A . 
P 7 HOH 332 932  168 HOH HOH A . 
P 7 HOH 333 933  739 HOH HOH A . 
P 7 HOH 334 934  697 HOH HOH A . 
P 7 HOH 335 935  774 HOH HOH A . 
P 7 HOH 336 936  700 HOH HOH A . 
P 7 HOH 337 937  671 HOH HOH A . 
P 7 HOH 338 938  752 HOH HOH A . 
P 7 HOH 339 939  211 HOH HOH A . 
P 7 HOH 340 940  489 HOH HOH A . 
P 7 HOH 341 941  791 HOH HOH A . 
P 7 HOH 342 942  515 HOH HOH A . 
P 7 HOH 343 943  491 HOH HOH A . 
P 7 HOH 344 944  615 HOH HOH A . 
P 7 HOH 345 945  626 HOH HOH A . 
P 7 HOH 346 946  486 HOH HOH A . 
P 7 HOH 347 947  510 HOH HOH A . 
P 7 HOH 348 948  757 HOH HOH A . 
P 7 HOH 349 949  778 HOH HOH A . 
P 7 HOH 350 950  633 HOH HOH A . 
P 7 HOH 351 951  670 HOH HOH A . 
P 7 HOH 352 952  438 HOH HOH A . 
P 7 HOH 353 953  508 HOH HOH A . 
P 7 HOH 354 954  713 HOH HOH A . 
P 7 HOH 355 955  766 HOH HOH A . 
P 7 HOH 356 956  504 HOH HOH A . 
P 7 HOH 357 957  629 HOH HOH A . 
P 7 HOH 358 958  705 HOH HOH A . 
P 7 HOH 359 959  297 HOH HOH A . 
P 7 HOH 360 960  673 HOH HOH A . 
P 7 HOH 361 961  430 HOH HOH A . 
P 7 HOH 362 962  722 HOH HOH A . 
P 7 HOH 363 963  596 HOH HOH A . 
P 7 HOH 364 964  392 HOH HOH A . 
P 7 HOH 365 965  638 HOH HOH A . 
P 7 HOH 366 966  597 HOH HOH A . 
P 7 HOH 367 967  672 HOH HOH A . 
P 7 HOH 368 968  301 HOH HOH A . 
P 7 HOH 369 969  299 HOH HOH A . 
P 7 HOH 370 970  795 HOH HOH A . 
P 7 HOH 371 971  424 HOH HOH A . 
P 7 HOH 372 972  764 HOH HOH A . 
P 7 HOH 373 973  413 HOH HOH A . 
P 7 HOH 374 974  785 HOH HOH A . 
P 7 HOH 375 975  131 HOH HOH A . 
P 7 HOH 376 976  655 HOH HOH A . 
P 7 HOH 377 977  235 HOH HOH A . 
P 7 HOH 378 978  768 HOH HOH A . 
P 7 HOH 379 979  541 HOH HOH A . 
P 7 HOH 380 980  727 HOH HOH A . 
P 7 HOH 381 981  227 HOH HOH A . 
P 7 HOH 382 982  782 HOH HOH A . 
P 7 HOH 383 983  528 HOH HOH A . 
P 7 HOH 384 984  339 HOH HOH A . 
Q 7 HOH 1   601  394 HOH HOH B . 
Q 7 HOH 2   602  322 HOH HOH B . 
Q 7 HOH 3   603  490 HOH HOH B . 
Q 7 HOH 4   604  737 HOH HOH B . 
Q 7 HOH 5   605  815 HOH HOH B . 
Q 7 HOH 6   606  499 HOH HOH B . 
Q 7 HOH 7   607  172 HOH HOH B . 
Q 7 HOH 8   608  652 HOH HOH B . 
Q 7 HOH 9   609  483 HOH HOH B . 
Q 7 HOH 10  610  761 HOH HOH B . 
Q 7 HOH 11  611  730 HOH HOH B . 
Q 7 HOH 12  612  823 HOH HOH B . 
Q 7 HOH 13  613  367 HOH HOH B . 
Q 7 HOH 14  614  728 HOH HOH B . 
Q 7 HOH 15  615  385 HOH HOH B . 
Q 7 HOH 16  616  669 HOH HOH B . 
Q 7 HOH 17  617  353 HOH HOH B . 
Q 7 HOH 18  618  214 HOH HOH B . 
Q 7 HOH 19  619  153 HOH HOH B . 
Q 7 HOH 20  620  111 HOH HOH B . 
Q 7 HOH 21  621  809 HOH HOH B . 
Q 7 HOH 22  622  545 HOH HOH B . 
Q 7 HOH 23  623  741 HOH HOH B . 
Q 7 HOH 24  624  548 HOH HOH B . 
Q 7 HOH 25  625  362 HOH HOH B . 
Q 7 HOH 26  626  445 HOH HOH B . 
Q 7 HOH 27  627  7   HOH HOH B . 
Q 7 HOH 28  628  98  HOH HOH B . 
Q 7 HOH 29  629  393 HOH HOH B . 
Q 7 HOH 30  630  250 HOH HOH B . 
Q 7 HOH 31  631  455 HOH HOH B . 
Q 7 HOH 32  632  173 HOH HOH B . 
Q 7 HOH 33  633  332 HOH HOH B . 
Q 7 HOH 34  634  266 HOH HOH B . 
Q 7 HOH 35  635  228 HOH HOH B . 
Q 7 HOH 36  636  323 HOH HOH B . 
Q 7 HOH 37  637  585 HOH HOH B . 
Q 7 HOH 38  638  54  HOH HOH B . 
Q 7 HOH 39  639  423 HOH HOH B . 
Q 7 HOH 40  640  24  HOH HOH B . 
Q 7 HOH 41  641  315 HOH HOH B . 
Q 7 HOH 42  642  119 HOH HOH B . 
Q 7 HOH 43  643  77  HOH HOH B . 
Q 7 HOH 44  644  624 HOH HOH B . 
Q 7 HOH 45  645  28  HOH HOH B . 
Q 7 HOH 46  646  654 HOH HOH B . 
Q 7 HOH 47  647  685 HOH HOH B . 
Q 7 HOH 48  648  314 HOH HOH B . 
Q 7 HOH 49  649  148 HOH HOH B . 
Q 7 HOH 50  650  252 HOH HOH B . 
Q 7 HOH 51  651  121 HOH HOH B . 
Q 7 HOH 52  652  712 HOH HOH B . 
Q 7 HOH 53  653  457 HOH HOH B . 
Q 7 HOH 54  654  127 HOH HOH B . 
Q 7 HOH 55  655  417 HOH HOH B . 
Q 7 HOH 56  656  546 HOH HOH B . 
Q 7 HOH 57  657  48  HOH HOH B . 
Q 7 HOH 58  658  380 HOH HOH B . 
Q 7 HOH 59  659  409 HOH HOH B . 
Q 7 HOH 60  660  448 HOH HOH B . 
Q 7 HOH 61  661  87  HOH HOH B . 
Q 7 HOH 62  662  551 HOH HOH B . 
Q 7 HOH 63  663  571 HOH HOH B . 
Q 7 HOH 64  664  21  HOH HOH B . 
Q 7 HOH 65  665  279 HOH HOH B . 
Q 7 HOH 66  666  760 HOH HOH B . 
Q 7 HOH 67  667  443 HOH HOH B . 
Q 7 HOH 68  668  80  HOH HOH B . 
Q 7 HOH 69  669  180 HOH HOH B . 
Q 7 HOH 70  670  130 HOH HOH B . 
Q 7 HOH 71  671  368 HOH HOH B . 
Q 7 HOH 72  672  382 HOH HOH B . 
Q 7 HOH 73  673  661 HOH HOH B . 
Q 7 HOH 74  674  453 HOH HOH B . 
Q 7 HOH 75  675  99  HOH HOH B . 
Q 7 HOH 76  676  496 HOH HOH B . 
Q 7 HOH 77  677  259 HOH HOH B . 
Q 7 HOH 78  678  110 HOH HOH B . 
Q 7 HOH 79  679  163 HOH HOH B . 
Q 7 HOH 80  680  740 HOH HOH B . 
Q 7 HOH 81  681  68  HOH HOH B . 
Q 7 HOH 82  682  113 HOH HOH B . 
Q 7 HOH 83  683  82  HOH HOH B . 
Q 7 HOH 84  684  3   HOH HOH B . 
Q 7 HOH 85  685  289 HOH HOH B . 
Q 7 HOH 86  686  350 HOH HOH B . 
Q 7 HOH 87  687  335 HOH HOH B . 
Q 7 HOH 88  688  73  HOH HOH B . 
Q 7 HOH 89  689  238 HOH HOH B . 
Q 7 HOH 90  690  31  HOH HOH B . 
Q 7 HOH 91  691  806 HOH HOH B . 
Q 7 HOH 92  692  182 HOH HOH B . 
Q 7 HOH 93  693  33  HOH HOH B . 
Q 7 HOH 94  694  825 HOH HOH B . 
Q 7 HOH 95  695  265 HOH HOH B . 
Q 7 HOH 96  696  356 HOH HOH B . 
Q 7 HOH 97  697  236 HOH HOH B . 
Q 7 HOH 98  698  55  HOH HOH B . 
Q 7 HOH 99  699  425 HOH HOH B . 
Q 7 HOH 100 700  125 HOH HOH B . 
Q 7 HOH 101 701  634 HOH HOH B . 
Q 7 HOH 102 702  244 HOH HOH B . 
Q 7 HOH 103 703  647 HOH HOH B . 
Q 7 HOH 104 704  132 HOH HOH B . 
Q 7 HOH 105 705  38  HOH HOH B . 
Q 7 HOH 106 706  403 HOH HOH B . 
Q 7 HOH 107 707  305 HOH HOH B . 
Q 7 HOH 108 708  308 HOH HOH B . 
Q 7 HOH 109 709  156 HOH HOH B . 
Q 7 HOH 110 710  234 HOH HOH B . 
Q 7 HOH 111 711  675 HOH HOH B . 
Q 7 HOH 112 712  53  HOH HOH B . 
Q 7 HOH 113 713  215 HOH HOH B . 
Q 7 HOH 114 714  738 HOH HOH B . 
Q 7 HOH 115 715  439 HOH HOH B . 
Q 7 HOH 116 716  25  HOH HOH B . 
Q 7 HOH 117 717  63  HOH HOH B . 
Q 7 HOH 118 718  256 HOH HOH B . 
Q 7 HOH 119 719  273 HOH HOH B . 
Q 7 HOH 120 720  316 HOH HOH B . 
Q 7 HOH 121 721  718 HOH HOH B . 
Q 7 HOH 122 722  41  HOH HOH B . 
Q 7 HOH 123 723  66  HOH HOH B . 
Q 7 HOH 124 724  318 HOH HOH B . 
Q 7 HOH 125 725  372 HOH HOH B . 
Q 7 HOH 126 726  178 HOH HOH B . 
Q 7 HOH 127 727  400 HOH HOH B . 
Q 7 HOH 128 728  262 HOH HOH B . 
Q 7 HOH 129 729  484 HOH HOH B . 
Q 7 HOH 130 730  427 HOH HOH B . 
Q 7 HOH 131 731  52  HOH HOH B . 
Q 7 HOH 132 732  264 HOH HOH B . 
Q 7 HOH 133 733  5   HOH HOH B . 
Q 7 HOH 134 734  187 HOH HOH B . 
Q 7 HOH 135 735  420 HOH HOH B . 
Q 7 HOH 136 736  395 HOH HOH B . 
Q 7 HOH 137 737  452 HOH HOH B . 
Q 7 HOH 138 738  207 HOH HOH B . 
Q 7 HOH 139 739  69  HOH HOH B . 
Q 7 HOH 140 740  543 HOH HOH B . 
Q 7 HOH 141 741  275 HOH HOH B . 
Q 7 HOH 142 742  114 HOH HOH B . 
Q 7 HOH 143 743  83  HOH HOH B . 
Q 7 HOH 144 744  146 HOH HOH B . 
Q 7 HOH 145 745  154 HOH HOH B . 
Q 7 HOH 146 746  481 HOH HOH B . 
Q 7 HOH 147 747  229 HOH HOH B . 
Q 7 HOH 148 748  466 HOH HOH B . 
Q 7 HOH 149 749  124 HOH HOH B . 
Q 7 HOH 150 750  802 HOH HOH B . 
Q 7 HOH 151 751  461 HOH HOH B . 
Q 7 HOH 152 752  94  HOH HOH B . 
Q 7 HOH 153 753  30  HOH HOH B . 
Q 7 HOH 154 754  107 HOH HOH B . 
Q 7 HOH 155 755  474 HOH HOH B . 
Q 7 HOH 156 756  653 HOH HOH B . 
Q 7 HOH 157 757  88  HOH HOH B . 
Q 7 HOH 158 758  4   HOH HOH B . 
Q 7 HOH 159 759  784 HOH HOH B . 
Q 7 HOH 160 760  293 HOH HOH B . 
Q 7 HOH 161 761  263 HOH HOH B . 
Q 7 HOH 162 762  39  HOH HOH B . 
Q 7 HOH 163 763  604 HOH HOH B . 
Q 7 HOH 164 764  555 HOH HOH B . 
Q 7 HOH 165 765  109 HOH HOH B . 
Q 7 HOH 166 766  242 HOH HOH B . 
Q 7 HOH 167 767  253 HOH HOH B . 
Q 7 HOH 168 768  174 HOH HOH B . 
Q 7 HOH 169 769  165 HOH HOH B . 
Q 7 HOH 170 770  14  HOH HOH B . 
Q 7 HOH 171 771  134 HOH HOH B . 
Q 7 HOH 172 772  736 HOH HOH B . 
Q 7 HOH 173 773  184 HOH HOH B . 
Q 7 HOH 174 774  285 HOH HOH B . 
Q 7 HOH 175 775  625 HOH HOH B . 
Q 7 HOH 176 776  566 HOH HOH B . 
Q 7 HOH 177 777  128 HOH HOH B . 
Q 7 HOH 178 778  663 HOH HOH B . 
Q 7 HOH 179 779  170 HOH HOH B . 
Q 7 HOH 180 780  106 HOH HOH B . 
Q 7 HOH 181 781  665 HOH HOH B . 
Q 7 HOH 182 782  145 HOH HOH B . 
Q 7 HOH 183 783  183 HOH HOH B . 
Q 7 HOH 184 784  126 HOH HOH B . 
Q 7 HOH 185 785  45  HOH HOH B . 
Q 7 HOH 186 786  185 HOH HOH B . 
Q 7 HOH 187 787  337 HOH HOH B . 
Q 7 HOH 188 788  359 HOH HOH B . 
Q 7 HOH 189 789  383 HOH HOH B . 
Q 7 HOH 190 790  258 HOH HOH B . 
Q 7 HOH 191 791  75  HOH HOH B . 
Q 7 HOH 192 792  58  HOH HOH B . 
Q 7 HOH 193 793  2   HOH HOH B . 
Q 7 HOH 194 794  635 HOH HOH B . 
Q 7 HOH 195 795  155 HOH HOH B . 
Q 7 HOH 196 796  440 HOH HOH B . 
Q 7 HOH 197 797  370 HOH HOH B . 
Q 7 HOH 198 798  426 HOH HOH B . 
Q 7 HOH 199 799  327 HOH HOH B . 
Q 7 HOH 200 800  300 HOH HOH B . 
Q 7 HOH 201 801  349 HOH HOH B . 
Q 7 HOH 202 802  217 HOH HOH B . 
Q 7 HOH 203 803  330 HOH HOH B . 
Q 7 HOH 204 804  681 HOH HOH B . 
Q 7 HOH 205 805  149 HOH HOH B . 
Q 7 HOH 206 806  57  HOH HOH B . 
Q 7 HOH 207 807  399 HOH HOH B . 
Q 7 HOH 208 808  40  HOH HOH B . 
Q 7 HOH 209 809  749 HOH HOH B . 
Q 7 HOH 210 810  558 HOH HOH B . 
Q 7 HOH 211 811  320 HOH HOH B . 
Q 7 HOH 212 812  333 HOH HOH B . 
Q 7 HOH 213 813  223 HOH HOH B . 
Q 7 HOH 214 814  32  HOH HOH B . 
Q 7 HOH 215 815  10  HOH HOH B . 
Q 7 HOH 216 816  345 HOH HOH B . 
Q 7 HOH 217 817  659 HOH HOH B . 
Q 7 HOH 218 818  122 HOH HOH B . 
Q 7 HOH 219 819  42  HOH HOH B . 
Q 7 HOH 220 820  572 HOH HOH B . 
Q 7 HOH 221 821  35  HOH HOH B . 
Q 7 HOH 222 822  136 HOH HOH B . 
Q 7 HOH 223 823  747 HOH HOH B . 
Q 7 HOH 224 824  29  HOH HOH B . 
Q 7 HOH 225 825  710 HOH HOH B . 
Q 7 HOH 226 826  129 HOH HOH B . 
Q 7 HOH 227 827  310 HOH HOH B . 
Q 7 HOH 228 828  503 HOH HOH B . 
Q 7 HOH 229 829  261 HOH HOH B . 
Q 7 HOH 230 830  11  HOH HOH B . 
Q 7 HOH 231 831  563 HOH HOH B . 
Q 7 HOH 232 832  779 HOH HOH B . 
Q 7 HOH 233 833  519 HOH HOH B . 
Q 7 HOH 234 834  141 HOH HOH B . 
Q 7 HOH 235 835  325 HOH HOH B . 
Q 7 HOH 236 836  255 HOH HOH B . 
Q 7 HOH 237 837  544 HOH HOH B . 
Q 7 HOH 238 838  826 HOH HOH B . 
Q 7 HOH 239 839  205 HOH HOH B . 
Q 7 HOH 240 840  689 HOH HOH B . 
Q 7 HOH 241 841  216 HOH HOH B . 
Q 7 HOH 242 842  23  HOH HOH B . 
Q 7 HOH 243 843  817 HOH HOH B . 
Q 7 HOH 244 844  108 HOH HOH B . 
Q 7 HOH 245 845  419 HOH HOH B . 
Q 7 HOH 246 846  142 HOH HOH B . 
Q 7 HOH 247 847  610 HOH HOH B . 
Q 7 HOH 248 848  230 HOH HOH B . 
Q 7 HOH 249 849  432 HOH HOH B . 
Q 7 HOH 250 850  210 HOH HOH B . 
Q 7 HOH 251 851  219 HOH HOH B . 
Q 7 HOH 252 852  614 HOH HOH B . 
Q 7 HOH 253 853  379 HOH HOH B . 
Q 7 HOH 254 854  284 HOH HOH B . 
Q 7 HOH 255 855  805 HOH HOH B . 
Q 7 HOH 256 856  74  HOH HOH B . 
Q 7 HOH 257 857  651 HOH HOH B . 
Q 7 HOH 258 858  441 HOH HOH B . 
Q 7 HOH 259 859  668 HOH HOH B . 
Q 7 HOH 260 860  189 HOH HOH B . 
Q 7 HOH 261 861  161 HOH HOH B . 
Q 7 HOH 262 862  683 HOH HOH B . 
Q 7 HOH 263 863  271 HOH HOH B . 
Q 7 HOH 264 864  171 HOH HOH B . 
Q 7 HOH 265 865  260 HOH HOH B . 
Q 7 HOH 266 866  43  HOH HOH B . 
Q 7 HOH 267 867  147 HOH HOH B . 
Q 7 HOH 268 868  355 HOH HOH B . 
Q 7 HOH 269 869  103 HOH HOH B . 
Q 7 HOH 270 870  329 HOH HOH B . 
Q 7 HOH 271 871  248 HOH HOH B . 
Q 7 HOH 272 872  282 HOH HOH B . 
Q 7 HOH 273 873  84  HOH HOH B . 
Q 7 HOH 274 874  750 HOH HOH B . 
Q 7 HOH 275 875  225 HOH HOH B . 
Q 7 HOH 276 876  290 HOH HOH B . 
Q 7 HOH 277 877  176 HOH HOH B . 
Q 7 HOH 278 878  401 HOH HOH B . 
Q 7 HOH 279 879  434 HOH HOH B . 
Q 7 HOH 280 880  341 HOH HOH B . 
Q 7 HOH 281 881  798 HOH HOH B . 
Q 7 HOH 282 882  812 HOH HOH B . 
Q 7 HOH 283 883  449 HOH HOH B . 
Q 7 HOH 284 884  488 HOH HOH B . 
Q 7 HOH 285 885  365 HOH HOH B . 
Q 7 HOH 286 886  793 HOH HOH B . 
Q 7 HOH 287 887  801 HOH HOH B . 
Q 7 HOH 288 888  637 HOH HOH B . 
Q 7 HOH 289 889  646 HOH HOH B . 
Q 7 HOH 290 890  565 HOH HOH B . 
Q 7 HOH 291 891  143 HOH HOH B . 
Q 7 HOH 292 892  433 HOH HOH B . 
Q 7 HOH 293 893  478 HOH HOH B . 
Q 7 HOH 294 894  498 HOH HOH B . 
Q 7 HOH 295 895  144 HOH HOH B . 
Q 7 HOH 296 896  561 HOH HOH B . 
Q 7 HOH 297 897  61  HOH HOH B . 
Q 7 HOH 298 898  298 HOH HOH B . 
Q 7 HOH 299 899  429 HOH HOH B . 
Q 7 HOH 300 900  421 HOH HOH B . 
Q 7 HOH 301 901  620 HOH HOH B . 
Q 7 HOH 302 902  338 HOH HOH B . 
Q 7 HOH 303 903  493 HOH HOH B . 
Q 7 HOH 304 904  525 HOH HOH B . 
Q 7 HOH 305 905  366 HOH HOH B . 
Q 7 HOH 306 906  118 HOH HOH B . 
Q 7 HOH 307 907  247 HOH HOH B . 
Q 7 HOH 308 908  816 HOH HOH B . 
Q 7 HOH 309 909  306 HOH HOH B . 
Q 7 HOH 310 910  539 HOH HOH B . 
Q 7 HOH 311 911  116 HOH HOH B . 
Q 7 HOH 312 912  220 HOH HOH B . 
Q 7 HOH 313 913  731 HOH HOH B . 
Q 7 HOH 314 914  450 HOH HOH B . 
Q 7 HOH 315 915  85  HOH HOH B . 
Q 7 HOH 316 916  415 HOH HOH B . 
Q 7 HOH 317 917  281 HOH HOH B . 
Q 7 HOH 318 918  312 HOH HOH B . 
Q 7 HOH 319 919  169 HOH HOH B . 
Q 7 HOH 320 920  340 HOH HOH B . 
Q 7 HOH 321 921  780 HOH HOH B . 
Q 7 HOH 322 922  602 HOH HOH B . 
Q 7 HOH 323 923  742 HOH HOH B . 
Q 7 HOH 324 924  790 HOH HOH B . 
Q 7 HOH 325 925  586 HOH HOH B . 
Q 7 HOH 326 926  688 HOH HOH B . 
Q 7 HOH 327 927  577 HOH HOH B . 
Q 7 HOH 328 928  787 HOH HOH B . 
Q 7 HOH 329 929  381 HOH HOH B . 
Q 7 HOH 330 930  627 HOH HOH B . 
Q 7 HOH 331 931  402 HOH HOH B . 
Q 7 HOH 332 932  776 HOH HOH B . 
Q 7 HOH 333 933  772 HOH HOH B . 
Q 7 HOH 334 934  754 HOH HOH B . 
Q 7 HOH 335 935  369 HOH HOH B . 
Q 7 HOH 336 936  709 HOH HOH B . 
Q 7 HOH 337 937  686 HOH HOH B . 
Q 7 HOH 338 938  534 HOH HOH B . 
Q 7 HOH 339 939  191 HOH HOH B . 
Q 7 HOH 340 940  396 HOH HOH B . 
Q 7 HOH 341 941  319 HOH HOH B . 
Q 7 HOH 342 942  715 HOH HOH B . 
Q 7 HOH 343 943  643 HOH HOH B . 
Q 7 HOH 344 944  623 HOH HOH B . 
Q 7 HOH 345 945  371 HOH HOH B . 
Q 7 HOH 346 946  580 HOH HOH B . 
Q 7 HOH 347 947  361 HOH HOH B . 
Q 7 HOH 348 948  435 HOH HOH B . 
Q 7 HOH 349 949  744 HOH HOH B . 
Q 7 HOH 350 950  619 HOH HOH B . 
Q 7 HOH 351 951  378 HOH HOH B . 
Q 7 HOH 352 952  377 HOH HOH B . 
Q 7 HOH 353 953  699 HOH HOH B . 
Q 7 HOH 354 954  771 HOH HOH B . 
Q 7 HOH 355 955  622 HOH HOH B . 
Q 7 HOH 356 956  765 HOH HOH B . 
Q 7 HOH 357 957  497 HOH HOH B . 
Q 7 HOH 358 958  416 HOH HOH B . 
Q 7 HOH 359 959  632 HOH HOH B . 
Q 7 HOH 360 960  351 HOH HOH B . 
Q 7 HOH 361 961  358 HOH HOH B . 
Q 7 HOH 362 962  639 HOH HOH B . 
Q 7 HOH 363 963  786 HOH HOH B . 
Q 7 HOH 364 964  456 HOH HOH B . 
Q 7 HOH 365 965  390 HOH HOH B . 
Q 7 HOH 366 966  660 HOH HOH B . 
Q 7 HOH 367 967  594 HOH HOH B . 
Q 7 HOH 368 968  34  HOH HOH B . 
Q 7 HOH 369 969  758 HOH HOH B . 
Q 7 HOH 370 970  364 HOH HOH B . 
Q 7 HOH 371 971  618 HOH HOH B . 
Q 7 HOH 372 972  203 HOH HOH B . 
Q 7 HOH 373 973  583 HOH HOH B . 
Q 7 HOH 374 974  552 HOH HOH B . 
Q 7 HOH 375 975  406 HOH HOH B . 
Q 7 HOH 376 976  773 HOH HOH B . 
Q 7 HOH 377 977  807 HOH HOH B . 
Q 7 HOH 378 978  676 HOH HOH B . 
Q 7 HOH 379 979  436 HOH HOH B . 
Q 7 HOH 380 980  407 HOH HOH B . 
Q 7 HOH 381 981  347 HOH HOH B . 
Q 7 HOH 382 982  775 HOH HOH B . 
Q 7 HOH 383 983  599 HOH HOH B . 
Q 7 HOH 384 984  232 HOH HOH B . 
Q 7 HOH 385 985  464 HOH HOH B . 
Q 7 HOH 386 986  579 HOH HOH B . 
Q 7 HOH 387 987  193 HOH HOH B . 
Q 7 HOH 388 988  243 HOH HOH B . 
Q 7 HOH 389 989  530 HOH HOH B . 
Q 7 HOH 390 990  511 HOH HOH B . 
Q 7 HOH 391 991  753 HOH HOH B . 
Q 7 HOH 392 992  363 HOH HOH B . 
Q 7 HOH 393 993  734 HOH HOH B . 
Q 7 HOH 394 994  500 HOH HOH B . 
Q 7 HOH 395 995  410 HOH HOH B . 
Q 7 HOH 396 996  344 HOH HOH B . 
Q 7 HOH 397 997  559 HOH HOH B . 
Q 7 HOH 398 998  641 HOH HOH B . 
Q 7 HOH 399 999  326 HOH HOH B . 
Q 7 HOH 400 1000 557 HOH HOH B . 
Q 7 HOH 401 1001 133 HOH HOH B . 
Q 7 HOH 402 1002 796 HOH HOH B . 
Q 7 HOH 403 1003 588 HOH HOH B . 
Q 7 HOH 404 1004 813 HOH HOH B . 
Q 7 HOH 405 1005 277 HOH HOH B . 
Q 7 HOH 406 1006 529 HOH HOH B . 
Q 7 HOH 407 1007 769 HOH HOH B . 
Q 7 HOH 408 1008 454 HOH HOH B . 
Q 7 HOH 409 1009 745 HOH HOH B . 
Q 7 HOH 410 1010 550 HOH HOH B . 
Q 7 HOH 411 1011 140 HOH HOH B . 
Q 7 HOH 412 1012 608 HOH HOH B . 
Q 7 HOH 413 1013 792 HOH HOH B . 
Q 7 HOH 414 1014 657 HOH HOH B . 
Q 7 HOH 415 1015 658 HOH HOH B . 
Q 7 HOH 416 1016 540 HOH HOH B . 
Q 7 HOH 417 1017 239 HOH HOH B . 
Q 7 HOH 418 1018 343 HOH HOH B . 
Q 7 HOH 419 1019 698 HOH HOH B . 
Q 7 HOH 420 1020 570 HOH HOH B . 
Q 7 HOH 421 1021 584 HOH HOH B . 
Q 7 HOH 422 1022 611 HOH HOH B . 
Q 7 HOH 423 1023 789 HOH HOH B . 
Q 7 HOH 424 1024 725 HOH HOH B . 
Q 7 HOH 425 1025 568 HOH HOH B . 
Q 7 HOH 426 1026 631 HOH HOH B . 
Q 7 HOH 427 1027 428 HOH HOH B . 
Q 7 HOH 428 1028 414 HOH HOH B . 
Q 7 HOH 429 1029 194 HOH HOH B . 
Q 7 HOH 430 1030 695 HOH HOH B . 
Q 7 HOH 431 1031 650 HOH HOH B . 
Q 7 HOH 432 1032 763 HOH HOH B . 
Q 7 HOH 433 1033 636 HOH HOH B . 
Q 7 HOH 434 1034 684 HOH HOH B . 
Q 7 HOH 435 1035 408 HOH HOH B . 
Q 7 HOH 436 1036 677 HOH HOH B . 
Q 7 HOH 437 1037 391 HOH HOH B . 
Q 7 HOH 438 1038 674 HOH HOH B . 
Q 7 HOH 439 1039 751 HOH HOH B . 
Q 7 HOH 440 1040 526 HOH HOH B . 
Q 7 HOH 441 1041 101 HOH HOH B . 
Q 7 HOH 442 1042 694 HOH HOH B . 
Q 7 HOH 443 1043 743 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                     8YB3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.830 
_cell.length_a_esd                 ? 
_cell.length_b                     128.480 
_cell.length_b_esd                 ? 
_cell.length_c                     149.410 
_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                         8YB3 
_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                   8YB3 
_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          54.62 
_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                                       8YB3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.5 
_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                                     180719 
_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                                198.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.01 
_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                                   0.982 
_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                                    1.50 
_reflns_shell.d_res_low                                     1.51 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.70 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4434 
_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                                  0.551 
_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                                 8YB3 
_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                            1.50 
_refine.ls_d_res_low                             9.99 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     180526 
_refine.ls_number_reflns_R_free                  8995 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1798 
_refine.ls_R_factor_R_free                       0.2064 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1784 
_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                          1.33 
_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                 24.95 
_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                            0.23 
_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                       1.50 
_refine_hist.d_res_low                        9.99 
_refine_hist.number_atoms_solvent             827 
_refine_hist.number_atoms_total               8343 
_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         188 
_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 ? 7761  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.001 ? 10517 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.804 ? 1066  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055 ? 1113  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 1380  ? 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' 1.50 1.52 . . 273 5643 100.00 . . . . 0.3947 . . . . . . . . . . . 0.4174 
'X-RAY DIFFRACTION' 1.52 1.53 . . 303 5652 100.00 . . . . 0.3892 . . . . . . . . . . . 0.3938 
'X-RAY DIFFRACTION' 1.53 1.55 . . 291 5672 100.00 . . . . 0.3854 . . . . . . . . . . . 0.3796 
'X-RAY DIFFRACTION' 1.55 1.57 . . 278 5675 100.00 . . . . 0.3723 . . . . . . . . . . . 0.3825 
'X-RAY DIFFRACTION' 1.57 1.59 . . 292 5694 100.00 . . . . 0.3639 . . . . . . . . . . . 0.3465 
'X-RAY DIFFRACTION' 1.59 1.62 . . 304 5611 100.00 . . . . 0.3469 . . . . . . . . . . . 0.3457 
'X-RAY DIFFRACTION' 1.62 1.64 . . 280 5700 100.00 . . . . 0.3370 . . . . . . . . . . . 0.3298 
'X-RAY DIFFRACTION' 1.64 1.66 . . 299 5646 100.00 . . . . 0.3258 . . . . . . . . . . . 0.3431 
'X-RAY DIFFRACTION' 1.66 1.69 . . 326 5660 100.00 . . . . 0.3076 . . . . . . . . . . . 0.3350 
'X-RAY DIFFRACTION' 1.69 1.72 . . 291 5659 100.00 . . . . 0.2924 . . . . . . . . . . . 0.2911 
'X-RAY DIFFRACTION' 1.72 1.75 . . 328 5681 100.00 . . . . 0.2748 . . . . . . . . . . . 0.3219 
'X-RAY DIFFRACTION' 1.75 1.78 . . 299 5679 100.00 . . . . 0.2587 . . . . . . . . . . . 0.2727 
'X-RAY DIFFRACTION' 1.78 1.81 . . 291 5654 100.00 . . . . 0.2327 . . . . . . . . . . . 0.2759 
'X-RAY DIFFRACTION' 1.81 1.85 . . 313 5687 100.00 . . . . 0.2167 . . . . . . . . . . . 0.2414 
'X-RAY DIFFRACTION' 1.85 1.89 . . 309 5703 100.00 . . . . 0.1985 . . . . . . . . . . . 0.2343 
'X-RAY DIFFRACTION' 1.89 1.93 . . 321 5650 100.00 . . . . 0.1935 . . . . . . . . . . . 0.2381 
'X-RAY DIFFRACTION' 1.93 1.98 . . 278 5721 100.00 . . . . 0.1833 . . . . . . . . . . . 0.2345 
'X-RAY DIFFRACTION' 1.98 2.03 . . 305 5722 100.00 . . . . 0.1699 . . . . . . . . . . . 0.2120 
'X-RAY DIFFRACTION' 2.03 2.09 . . 295 5678 100.00 . . . . 0.1627 . . . . . . . . . . . 0.1791 
'X-RAY DIFFRACTION' 2.09 2.16 . . 325 5698 100.00 . . . . 0.1603 . . . . . . . . . . . 0.1915 
'X-RAY DIFFRACTION' 2.16 2.23 . . 321 5700 100.00 . . . . 0.1662 . . . . . . . . . . . 0.1959 
'X-RAY DIFFRACTION' 2.23 2.32 . . 270 5763 100.00 . . . . 0.1654 . . . . . . . . . . . 0.1984 
'X-RAY DIFFRACTION' 2.32 2.43 . . 283 5753 100.00 . . . . 0.1681 . . . . . . . . . . . 0.1973 
'X-RAY DIFFRACTION' 2.43 2.55 . . 311 5734 100.00 . . . . 0.1670 . . . . . . . . . . . 0.1892 
'X-RAY DIFFRACTION' 2.55 2.71 . . 278 5774 100.00 . . . . 0.1732 . . . . . . . . . . . 0.2030 
'X-RAY DIFFRACTION' 2.71 2.91 . . 323 5757 100.00 . . . . 0.1703 . . . . . . . . . . . 0.1935 
'X-RAY DIFFRACTION' 2.91 3.20 . . 290 5792 100.00 . . . . 0.1744 . . . . . . . . . . . 0.2105 
'X-RAY DIFFRACTION' 3.20 3.64 . . 300 5850 100.00 . . . . 0.1584 . . . . . . . . . . . 0.2094 
'X-RAY DIFFRACTION' 3.64 4.52 . . 283 5898 100.00 . . . . 0.1516 . . . . . . . . . . . 0.1724 
'X-RAY DIFFRACTION' 4.52 9.99 . . 335 6025 100.00 . . . . 0.1684 . . . . . . . . . . . 0.1811 
# 
_struct.entry_id                     8YB3 
_struct.title                        
;XFEL crystal structure of the oxygen-bound 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        8YB3 
_struct_keywords.text            'Cytochrome P450, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 6 ? 
P N N 7 ? 
Q N N 7 ? 
# 
_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 8YB3 A 1 ? 455 ? P14779 2 ? 456 ? 1 455 
2 1 8YB3 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 8YB3 ALA A 87  ? UNP P14779 PHE 88  'engineered mutation' 87  1 
1 8YB3 HIS A 393 ? UNP P14779 PHE 394 'engineered mutation' 393 2 
2 8YB3 ALA B 87  ? UNP P14779 PHE 88  'engineered mutation' 87  3 
2 8YB3 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)' 1260  ? 
1 MORE         -21   ? 
1 'SSA (A^2)'  19160 ? 
2 'ABSA (A^2)' 1260  ? 
2 MORE         -21   ? 
2 'SSA (A^2)'  19120 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,P       
2 1 B,H,I,J,K,L,M,N,O,Q 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PHE A 11  ? LYS A 15  ? PHE A 11  LYS A 15  5 ? 5  
HELX_P HELX_P2  AA2 ASN A 16  ? ASN A 21  ? ASN A 16  ASN A 21  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 24  ? GLY A 37  ? LYS A 24  GLY A 37  1 ? 14 
HELX_P HELX_P4  AA4 SER A 54  ? CYS A 62  ? SER A 54  CYS A 62  1 ? 9  
HELX_P HELX_P5  AA5 SER A 72  ? GLY A 83  ? SER A 72  GLY A 83  1 ? 12 
HELX_P HELX_P6  AA6 GLU A 93  ? LEU A 104 ? GLU A 93  LEU A 104 1 ? 12 
HELX_P HELX_P7  AA7 PRO A 105 ? PHE A 107 ? PRO A 105 PHE A 107 5 ? 3  
HELX_P HELX_P8  AA8 SER A 108 ? ARG A 132 ? SER A 108 ARG A 132 1 ? 25 
HELX_P HELX_P9  AA9 VAL A 141 ? ASN A 159 ? VAL A 141 ASN A 159 1 ? 19 
HELX_P HELX_P10 AB1 ASN A 163 ? ARG A 167 ? ASN A 163 ARG A 167 5 ? 5  
HELX_P HELX_P11 AB2 HIS A 171 ? LEU A 188 ? HIS A 171 LEU A 188 1 ? 18 
HELX_P HELX_P12 AB3 ASP A 195 ? ALA A 197 ? ASP A 195 ALA A 197 5 ? 3  
HELX_P HELX_P13 AB4 TYR A 198 ? SER A 226 ? TYR A 198 SER A 226 1 ? 29 
HELX_P HELX_P14 AB5 ASP A 232 ? GLY A 240 ? ASP A 232 GLY A 240 1 ? 9  
HELX_P HELX_P15 AB6 ASP A 250 ? GLY A 265 ? ASP A 250 GLY A 265 1 ? 16 
HELX_P HELX_P16 AB7 HIS A 266 ? ASN A 283 ? HIS A 266 ASN A 283 1 ? 18 
HELX_P HELX_P17 AB8 ASN A 283 ? LEU A 298 ? ASN A 283 LEU A 298 1 ? 16 
HELX_P HELX_P18 AB9 SER A 304 ? GLN A 310 ? SER A 304 GLN A 310 1 ? 7  
HELX_P HELX_P19 AC1 LEU A 311 ? TRP A 325 ? LEU A 311 TRP A 325 1 ? 15 
HELX_P HELX_P20 AC2 ILE A 357 ? HIS A 361 ? ILE A 357 HIS A 361 1 ? 5  
HELX_P HELX_P21 AC3 ASP A 363 ? GLY A 368 ? ASP A 363 GLY A 368 1 ? 6  
HELX_P HELX_P22 AC4 ARG A 375 ? GLU A 380 ? ARG A 375 GLU A 380 5 ? 6  
HELX_P HELX_P23 AC5 ASN A 381 ? ILE A 385 ? ASN A 381 ILE A 385 5 ? 5  
HELX_P HELX_P24 AC6 ASN A 395 ? ALA A 399 ? ASN A 395 ALA A 399 5 ? 5  
HELX_P HELX_P25 AC7 GLY A 402 ? HIS A 420 ? GLY A 402 HIS A 420 1 ? 19 
HELX_P HELX_P26 AC8 PHE B 11  ? LYS B 15  ? PHE B 11  LYS B 15  5 ? 5  
HELX_P HELX_P27 AC9 ASN B 16  ? ASN B 21  ? ASN B 16  ASN B 21  5 ? 6  
HELX_P HELX_P28 AD1 LYS B 24  ? GLY B 37  ? LYS B 24  GLY B 37  1 ? 14 
HELX_P HELX_P29 AD2 SER B 54  ? CYS B 62  ? SER B 54  CYS B 62  1 ? 9  
HELX_P HELX_P30 AD3 SER B 72  ? GLY B 83  ? SER B 72  GLY B 83  1 ? 12 
HELX_P HELX_P31 AD4 GLU B 93  ? LEU B 104 ? GLU B 93  LEU B 104 1 ? 12 
HELX_P HELX_P32 AD5 PRO B 105 ? PHE B 107 ? PRO B 105 PHE B 107 5 ? 3  
HELX_P HELX_P33 AD6 SER B 108 ? ARG B 132 ? SER B 108 ARG B 132 1 ? 25 
HELX_P HELX_P34 AD7 VAL B 141 ? ASN B 159 ? VAL B 141 ASN B 159 1 ? 19 
HELX_P HELX_P35 AD8 ASN B 163 ? ARG B 167 ? ASN B 163 ARG B 167 5 ? 5  
HELX_P HELX_P36 AD9 HIS B 171 ? LEU B 188 ? HIS B 171 LEU B 188 1 ? 18 
HELX_P HELX_P37 AE1 ASP B 195 ? ALA B 197 ? ASP B 195 ALA B 197 5 ? 3  
HELX_P HELX_P38 AE2 TYR B 198 ? ALA B 225 ? TYR B 198 ALA B 225 1 ? 28 
HELX_P HELX_P39 AE3 ASP B 232 ? GLY B 240 ? ASP B 232 GLY B 240 1 ? 9  
HELX_P HELX_P40 AE4 ASP B 250 ? GLY B 265 ? ASP B 250 GLY B 265 1 ? 16 
HELX_P HELX_P41 AE5 HIS B 266 ? ASN B 283 ? HIS B 266 ASN B 283 1 ? 18 
HELX_P HELX_P42 AE6 ASN B 283 ? LEU B 298 ? ASN B 283 LEU B 298 1 ? 16 
HELX_P HELX_P43 AE7 SER B 304 ? GLN B 310 ? SER B 304 GLN B 310 1 ? 7  
HELX_P HELX_P44 AE8 LEU B 311 ? TRP B 325 ? LEU B 311 TRP B 325 1 ? 15 
HELX_P HELX_P45 AE9 GLY B 342 ? GLU B 344 ? GLY B 342 GLU B 344 5 ? 3  
HELX_P HELX_P46 AF1 ILE B 357 ? HIS B 361 ? ILE B 357 HIS B 361 1 ? 5  
HELX_P HELX_P47 AF2 ASP B 363 ? GLY B 368 ? ASP B 363 GLY B 368 1 ? 6  
HELX_P HELX_P48 AF3 ARG B 375 ? GLU B 380 ? ARG B 375 GLU B 380 5 ? 6  
HELX_P HELX_P49 AF4 ASN B 381 ? ILE B 385 ? ASN B 381 ILE B 385 5 ? 5  
HELX_P HELX_P50 AF5 ASN B 395 ? ALA B 399 ? ASN B 395 ALA B 399 5 ? 5  
HELX_P HELX_P51 AF6 GLY B 402 ? HIS B 420 ? GLY B 402 HIS B 420 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 400 SG ? ? ? 1_555 C HEM . FE ? ? A CYS 400 A HEM 501 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc2 metalc ? ? C HEM .   FE ? ? ? 1_555 F OXY . O1 ? ? A HEM 501 A OXY 504 1_555 ? ? ? ? ? ? ? 1.923 ? ? 
metalc3 metalc ? ? B CYS 400 SG ? ? ? 1_555 H HEM . FE ? ? B CYS 400 B HEM 501 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc4 metalc ? ? H HEM .   FE ? ? ? 1_555 K OXY . O1 ? ? B HEM 501 B OXY 504 1_555 ? ? ? ? ? ? ? 1.934 ? ? 
# 
_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 97.4  ? 
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 88.1  ? 
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 83.9  ? 
5  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 176.8 ? 
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 88.0  ? 
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 93.2  ? 
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 91.3  ? 
9  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 178.6 ? 
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 91.5  ? 
11 SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O1 ? F OXY . ? A OXY 504 ? 1_555 170.8 ? 
12 NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O1 ? F OXY . ? A OXY 504 ? 1_555 88.9  ? 
13 NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O1 ? F OXY . ? A OXY 504 ? 1_555 85.3  ? 
14 NC ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O1 ? F OXY . ? A OXY 504 ? 1_555 89.5  ? 
15 ND ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O1 ? F OXY . ? A OXY 504 ? 1_555 93.4  ? 
16 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NA ? H HEM . ? B HEM 501 ? 1_555 98.0  ? 
17 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 88.4  ? 
18 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 89.2  ? 
19 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 82.9  ? 
20 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 178.2 ? 
21 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 89.3  ? 
22 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 92.9  ? 
23 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 90.9  ? 
24 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 178.6 ? 
25 NC ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 90.5  ? 
26 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O1 ? K OXY . ? B OXY 504 ? 1_555 171.0 ? 
27 NA ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O1 ? K OXY . ? B OXY 504 ? 1_555 89.9  ? 
28 NB ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O1 ? K OXY . ? B OXY 504 ? 1_555 87.4  ? 
29 NC ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O1 ? K OXY . ? B OXY 504 ? 1_555 89.1  ? 
30 ND ? H HEM .   ? B HEM 501 ? 1_555 FE ? H HEM . ? B HEM 501 ? 1_555 O1 ? K OXY . ? B OXY 504 ? 1_555 91.3  ? 
# 
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 PHE B 42  ? N PHE B 42  O THR B 49  ? O THR B 49  
AA5 2 3 N LEU B 52  ? N LEU B 52  O MET B 354 ? O MET B 354 
AA5 3 4 O VAL B 355 ? O VAL B 355 N PHE B 331 ? N PHE B 331 
AA5 4 5 O SER B 332 ? O SER B 332 N ASN B 70  ? N ASN B 70  
AA6 1 2 N ILE B 139 ? N ILE B 139 O VAL B 446 ? O VAL B 446 
AA6 2 3 O LYS B 449 ? O LYS B 449 N ASP B 422 ? N ASP B 422 
AA7 1 2 N THR B 339 ? N THR B 339 O LEU B 347 ? O LEU B 347 
AA8 1 2 N LYS B 434 ? N LYS B 434 O LYS B 440 ? O LYS B 440 
# 
_pdbx_entry_details.entry_id                   8YB3 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 15  ? ? 56.46   -125.44 
2  1 ASP A 84  ? ? -98.44  37.13   
3  1 HIS A 266 ? ? -136.44 -35.55  
4  1 LEU A 437 ? ? 70.47   -60.67  
5  1 LYS B 15  ? ? 54.46   -123.71 
6  1 ASP B 84  ? ? -97.22  36.69   
7  1 ASP B 232 ? ? -127.51 -166.69 
8  1 HIS B 266 ? ? -137.32 -34.33  
9  1 ASP B 370 ? ? -91.25  37.70   
10 1 LEU B 437 ? ? 70.91   -61.23  
# 
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 
OXY O1   O  N N 397 
OXY O2   O  N N 398 
PHE N    N  N N 399 
PHE CA   C  N S 400 
PHE C    C  N N 401 
PHE O    O  N N 402 
PHE CB   C  N N 403 
PHE CG   C  Y N 404 
PHE CD1  C  Y N 405 
PHE CD2  C  Y N 406 
PHE CE1  C  Y N 407 
PHE CE2  C  Y N 408 
PHE CZ   C  Y N 409 
PHE OXT  O  N N 410 
PHE H    H  N N 411 
PHE H2   H  N N 412 
PHE HA   H  N N 413 
PHE HB2  H  N N 414 
PHE HB3  H  N N 415 
PHE HD1  H  N N 416 
PHE HD2  H  N N 417 
PHE HE1  H  N N 418 
PHE HE2  H  N N 419 
PHE HZ   H  N N 420 
PHE HXT  H  N N 421 
PRO N    N  N N 422 
PRO CA   C  N S 423 
PRO C    C  N N 424 
PRO O    O  N N 425 
PRO CB   C  N N 426 
PRO CG   C  N N 427 
PRO CD   C  N N 428 
PRO OXT  O  N N 429 
PRO H    H  N N 430 
PRO HA   H  N N 431 
PRO HB2  H  N N 432 
PRO HB3  H  N N 433 
PRO HG2  H  N N 434 
PRO HG3  H  N N 435 
PRO HD2  H  N N 436 
PRO HD3  H  N N 437 
PRO HXT  H  N N 438 
SER N    N  N N 439 
SER CA   C  N S 440 
SER C    C  N N 441 
SER O    O  N N 442 
SER CB   C  N N 443 
SER OG   O  N N 444 
SER OXT  O  N N 445 
SER H    H  N N 446 
SER H2   H  N N 447 
SER HA   H  N N 448 
SER HB2  H  N N 449 
SER HB3  H  N N 450 
SER HG   H  N N 451 
SER HXT  H  N N 452 
SYN CAF  C  Y N 453 
SYN CAD  C  Y N 454 
SYN CAC  C  Y N 455 
SYN CAE  C  Y N 456 
SYN CAG  C  Y N 457 
SYN CAH  C  Y N 458 
SYN CAB  C  N N 459 
SYN CAA  C  N N 460 
SYN H1   H  N N 461 
SYN H2   H  N N 462 
SYN H3   H  N N 463 
SYN H4   H  N N 464 
SYN H5   H  N N 465 
SYN H6   H  N N 466 
SYN H8   H  N N 467 
SYN H9   H  N N 468 
THR N    N  N N 469 
THR CA   C  N S 470 
THR C    C  N N 471 
THR O    O  N N 472 
THR CB   C  N R 473 
THR OG1  O  N N 474 
THR CG2  C  N N 475 
THR OXT  O  N N 476 
THR H    H  N N 477 
THR H2   H  N N 478 
THR HA   H  N N 479 
THR HB   H  N N 480 
THR HG1  H  N N 481 
THR HG21 H  N N 482 
THR HG22 H  N N 483 
THR HG23 H  N N 484 
THR HXT  H  N N 485 
TRP N    N  N N 486 
TRP CA   C  N S 487 
TRP C    C  N N 488 
TRP O    O  N N 489 
TRP CB   C  N N 490 
TRP CG   C  Y N 491 
TRP CD1  C  Y N 492 
TRP CD2  C  Y N 493 
TRP NE1  N  Y N 494 
TRP CE2  C  Y N 495 
TRP CE3  C  Y N 496 
TRP CZ2  C  Y N 497 
TRP CZ3  C  Y N 498 
TRP CH2  C  Y N 499 
TRP OXT  O  N N 500 
TRP H    H  N N 501 
TRP H2   H  N N 502 
TRP HA   H  N N 503 
TRP HB2  H  N N 504 
TRP HB3  H  N N 505 
TRP HD1  H  N N 506 
TRP HE1  H  N N 507 
TRP HE3  H  N N 508 
TRP HZ2  H  N N 509 
TRP HZ3  H  N N 510 
TRP HH2  H  N N 511 
TRP HXT  H  N N 512 
TYR N    N  N N 513 
TYR CA   C  N S 514 
TYR C    C  N N 515 
TYR O    O  N N 516 
TYR CB   C  N N 517 
TYR CG   C  Y N 518 
TYR CD1  C  Y N 519 
TYR CD2  C  Y N 520 
TYR CE1  C  Y N 521 
TYR CE2  C  Y N 522 
TYR CZ   C  Y N 523 
TYR OH   O  N N 524 
TYR OXT  O  N N 525 
TYR H    H  N N 526 
TYR H2   H  N N 527 
TYR HA   H  N N 528 
TYR HB2  H  N N 529 
TYR HB3  H  N N 530 
TYR HD1  H  N N 531 
TYR HD2  H  N N 532 
TYR HE1  H  N N 533 
TYR HE2  H  N N 534 
TYR HH   H  N N 535 
TYR HXT  H  N N 536 
VAL N    N  N N 537 
VAL CA   C  N S 538 
VAL C    C  N N 539 
VAL O    O  N N 540 
VAL CB   C  N N 541 
VAL CG1  C  N N 542 
VAL CG2  C  N N 543 
VAL OXT  O  N N 544 
VAL H    H  N N 545 
VAL H2   H  N N 546 
VAL HA   H  N N 547 
VAL HB   H  N N 548 
VAL HG11 H  N N 549 
VAL HG12 H  N N 550 
VAL HG13 H  N N 551 
VAL HG21 H  N N 552 
VAL HG22 H  N N 553 
VAL HG23 H  N N 554 
VAL HXT  H  N N 555 
# 
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 
OXY O1  O2   doub N N 391 
PHE N   CA   sing N N 392 
PHE N   H    sing N N 393 
PHE N   H2   sing N N 394 
PHE CA  C    sing N N 395 
PHE CA  CB   sing N N 396 
PHE CA  HA   sing N N 397 
PHE C   O    doub N N 398 
PHE C   OXT  sing N N 399 
PHE CB  CG   sing N N 400 
PHE CB  HB2  sing N N 401 
PHE CB  HB3  sing N N 402 
PHE CG  CD1  doub Y N 403 
PHE CG  CD2  sing Y N 404 
PHE CD1 CE1  sing Y N 405 
PHE CD1 HD1  sing N N 406 
PHE CD2 CE2  doub Y N 407 
PHE CD2 HD2  sing N N 408 
PHE CE1 CZ   doub Y N 409 
PHE CE1 HE1  sing N N 410 
PHE CE2 CZ   sing Y N 411 
PHE CE2 HE2  sing N N 412 
PHE CZ  HZ   sing N N 413 
PHE OXT HXT  sing N N 414 
PRO N   CA   sing N N 415 
PRO N   CD   sing N N 416 
PRO N   H    sing N N 417 
PRO CA  C    sing N N 418 
PRO CA  CB   sing N N 419 
PRO CA  HA   sing N N 420 
PRO C   O    doub N N 421 
PRO C   OXT  sing N N 422 
PRO CB  CG   sing N N 423 
PRO CB  HB2  sing N N 424 
PRO CB  HB3  sing N N 425 
PRO CG  CD   sing N N 426 
PRO CG  HG2  sing N N 427 
PRO CG  HG3  sing N N 428 
PRO CD  HD2  sing N N 429 
PRO CD  HD3  sing N N 430 
PRO OXT HXT  sing N N 431 
SER N   CA   sing N N 432 
SER N   H    sing N N 433 
SER N   H2   sing N N 434 
SER CA  C    sing N N 435 
SER CA  CB   sing N N 436 
SER CA  HA   sing N N 437 
SER C   O    doub N N 438 
SER C   OXT  sing N N 439 
SER CB  OG   sing N N 440 
SER CB  HB2  sing N N 441 
SER CB  HB3  sing N N 442 
SER OG  HG   sing N N 443 
SER OXT HXT  sing N N 444 
SYN CAC CAE  doub Y N 445 
SYN CAC CAD  sing Y N 446 
SYN CAE CAG  sing Y N 447 
SYN CAD CAF  doub Y N 448 
SYN CAG CAH  doub Y N 449 
SYN CAF CAH  sing Y N 450 
SYN CAH CAB  sing N N 451 
SYN CAB CAA  doub N N 452 
SYN CAF H1   sing N N 453 
SYN CAD H2   sing N N 454 
SYN CAC H3   sing N N 455 
SYN CAE H4   sing N N 456 
SYN CAG H5   sing N N 457 
SYN CAB H6   sing N N 458 
SYN CAA H8   sing N N 459 
SYN CAA H9   sing N N 460 
THR N   CA   sing N N 461 
THR N   H    sing N N 462 
THR N   H2   sing N N 463 
THR CA  C    sing N N 464 
THR CA  CB   sing N N 465 
THR CA  HA   sing N N 466 
THR C   O    doub N N 467 
THR C   OXT  sing N N 468 
THR CB  OG1  sing N N 469 
THR CB  CG2  sing N N 470 
THR CB  HB   sing N N 471 
THR OG1 HG1  sing N N 472 
THR CG2 HG21 sing N N 473 
THR CG2 HG22 sing N N 474 
THR CG2 HG23 sing N N 475 
THR OXT HXT  sing N N 476 
TRP N   CA   sing N N 477 
TRP N   H    sing N N 478 
TRP N   H2   sing N N 479 
TRP CA  C    sing N N 480 
TRP CA  CB   sing N N 481 
TRP CA  HA   sing N N 482 
TRP C   O    doub N N 483 
TRP C   OXT  sing N N 484 
TRP CB  CG   sing N N 485 
TRP CB  HB2  sing N N 486 
TRP CB  HB3  sing N N 487 
TRP CG  CD1  doub Y N 488 
TRP CG  CD2  sing Y N 489 
TRP CD1 NE1  sing Y N 490 
TRP CD1 HD1  sing N N 491 
TRP CD2 CE2  doub Y N 492 
TRP CD2 CE3  sing Y N 493 
TRP NE1 CE2  sing Y N 494 
TRP NE1 HE1  sing N N 495 
TRP CE2 CZ2  sing Y N 496 
TRP CE3 CZ3  doub Y N 497 
TRP CE3 HE3  sing N N 498 
TRP CZ2 CH2  doub Y N 499 
TRP CZ2 HZ2  sing N N 500 
TRP CZ3 CH2  sing Y N 501 
TRP CZ3 HZ3  sing N N 502 
TRP CH2 HH2  sing N N 503 
TRP OXT HXT  sing N N 504 
TYR N   CA   sing N N 505 
TYR N   H    sing N N 506 
TYR N   H2   sing N N 507 
TYR CA  C    sing N N 508 
TYR CA  CB   sing N N 509 
TYR CA  HA   sing N N 510 
TYR C   O    doub N N 511 
TYR C   OXT  sing N N 512 
TYR CB  CG   sing N N 513 
TYR CB  HB2  sing N N 514 
TYR CB  HB3  sing N N 515 
TYR CG  CD1  doub Y N 516 
TYR CG  CD2  sing Y N 517 
TYR CD1 CE1  sing Y N 518 
TYR CD1 HD1  sing N N 519 
TYR CD2 CE2  doub Y N 520 
TYR CD2 HD2  sing N N 521 
TYR CE1 CZ   doub Y N 522 
TYR CE1 HE1  sing N N 523 
TYR CE2 CZ   sing Y N 524 
TYR CE2 HE2  sing N N 525 
TYR CZ  OH   sing N N 526 
TYR OH  HH   sing N N 527 
TYR OXT HXT  sing N N 528 
VAL N   CA   sing N N 529 
VAL N   H    sing N N 530 
VAL N   H2   sing N N 531 
VAL CA  C    sing N N 532 
VAL CA  CB   sing N N 533 
VAL CA  HA   sing N N 534 
VAL C   O    doub N N 535 
VAL C   OXT  sing N N 536 
VAL CB  CG1  sing N N 537 
VAL CB  CG2  sing N N 538 
VAL CB  HB   sing N N 539 
VAL CG1 HG11 sing N N 540 
VAL CG1 HG12 sing N N 541 
VAL CG1 HG13 sing N N 542 
VAL CG2 HG21 sing N N 543 
VAL CG2 HG22 sing N N 544 
VAL CG2 HG23 sing N N 545 
VAL OXT HXT  sing N N 546 
# 
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          51118 
_pdbx_serial_crystallography_data_reduction.droplet_hits          ? 
_pdbx_serial_crystallography_data_reduction.frames_failed_index   ? 
_pdbx_serial_crystallography_data_reduction.frames_indexed        34941 
_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        13.4 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   Fixed-target 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_pdbx_serial_crystallography_sample_delivery_fixed_target.diffrn_id                       1 
_pdbx_serial_crystallography_sample_delivery_fixed_target.description                     
'microcrystals were mounted on mesh loop and flash-frozen by liquid nitrogen' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_holding                  'polyimide film' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.support_base                    'SPINE magnet base' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_unit_size                36 
_pdbx_serial_crystallography_sample_delivery_fixed_target.crystals_per_unit               50 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_solvent                  
'125 mM Tris-HCl (pH 8.3), 14% w/v PEG 8000, 60 mM MgCl2, saturated styrene, and 30% glycerol' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_dehydration_prevention   none 
_pdbx_serial_crystallography_sample_delivery_fixed_target.motion_control                  ? 
_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                    8YB3 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.016998 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007783 
_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]   0.006693 
_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   ? -11.293 -23.454 -24.662 1.00 70.73  ? 1    THR A N   1 
ATOM   2    C  CA  . THR A 1 1   ? -10.039 -23.518 -23.916 1.00 71.15  ? 1    THR A CA  1 
ATOM   3    C  C   . THR A 1 1   ? -10.224 -24.237 -22.580 1.00 63.53  ? 1    THR A C   1 
ATOM   4    O  O   . THR A 1 1   ? -9.640  -23.848 -21.568 1.00 64.21  ? 1    THR A O   1 
ATOM   5    C  CB  . THR A 1 1   ? -9.460  -22.108 -23.663 1.00 71.00  ? 1    THR A CB  1 
ATOM   6    O  OG1 . THR A 1 1   ? -8.563  -22.145 -22.545 1.00 74.50  ? 1    THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 1   ? -10.577 -21.104 -23.396 1.00 68.58  ? 1    THR A CG2 1 
ATOM   8    N  N   . ILE A 1 2   ? -11.037 -25.291 -22.594 1.00 62.99  ? 2    ILE A N   1 
ATOM   9    C  CA  . ILE A 1 2   ? -11.331 -26.051 -21.382 1.00 64.08  ? 2    ILE A CA  1 
ATOM   10   C  C   . ILE A 1 2   ? -10.067 -26.765 -20.913 1.00 62.68  ? 2    ILE A C   1 
ATOM   11   O  O   . ILE A 1 2   ? -9.489  -27.581 -21.641 1.00 60.78  ? 2    ILE A O   1 
ATOM   12   C  CB  . ILE A 1 2   ? -12.471 -27.048 -21.630 1.00 62.24  ? 2    ILE A CB  1 
ATOM   13   C  CG1 . ILE A 1 2   ? -13.765 -26.300 -21.970 1.00 62.84  ? 2    ILE A CG1 1 
ATOM   14   C  CG2 . ILE A 1 2   ? -12.658 -27.960 -20.423 1.00 58.06  ? 2    ILE A CG2 1 
ATOM   15   C  CD1 . ILE A 1 2   ? -14.910 -27.204 -22.401 1.00 66.32  ? 2    ILE A CD1 1 
ATOM   16   N  N   . LYS A 1 3   ? -9.633  -26.460 -19.692 1.00 59.29  ? 3    LYS A N   1 
ATOM   17   C  CA  . LYS A 1 3   ? -8.477  -27.101 -19.078 1.00 56.94  ? 3    LYS A CA  1 
ATOM   18   C  C   . LYS A 1 3   ? -8.917  -28.187 -18.102 1.00 56.01  ? 3    LYS A C   1 
ATOM   19   O  O   . LYS A 1 3   ? -10.022 -28.145 -17.551 1.00 54.90  ? 3    LYS A O   1 
ATOM   20   C  CB  . LYS A 1 3   ? -7.614  -26.084 -18.329 1.00 52.52  ? 3    LYS A CB  1 
ATOM   21   C  CG  . LYS A 1 3   ? -6.592  -25.348 -19.161 1.00 58.15  ? 3    LYS A CG  1 
ATOM   22   C  CD  . LYS A 1 3   ? -5.494  -24.812 -18.252 1.00 54.65  ? 3    LYS A CD  1 
ATOM   23   C  CE  . LYS A 1 3   ? -4.383  -24.132 -19.037 1.00 64.25  ? 3    LYS A CE  1 
ATOM   24   N  NZ  . LYS A 1 3   ? -4.749  -22.776 -19.535 1.00 65.19  ? 3    LYS A NZ  1 
ATOM   25   N  N   . GLU A 1 4   ? -8.032  -29.161 -17.896 1.00 56.02  ? 4    GLU A N   1 
ATOM   26   C  CA  . GLU A 1 4   ? -8.192  -30.183 -16.871 1.00 56.52  ? 4    GLU A CA  1 
ATOM   27   C  C   . GLU A 1 4   ? -7.446  -29.728 -15.621 1.00 48.31  ? 4    GLU A C   1 
ATOM   28   O  O   . GLU A 1 4   ? -6.255  -29.413 -15.688 1.00 52.40  ? 4    GLU A O   1 
ATOM   29   C  CB  . GLU A 1 4   ? -7.632  -31.522 -17.359 1.00 61.26  ? 4    GLU A CB  1 
ATOM   30   C  CG  . GLU A 1 4   ? -8.215  -32.763 -16.697 1.00 62.67  ? 4    GLU A CG  1 
ATOM   31   C  CD  . GLU A 1 4   ? -9.702  -32.945 -16.960 1.00 75.48  ? 4    GLU A CD  1 
ATOM   32   O  OE1 . GLU A 1 4   ? -10.288 -32.127 -17.704 1.00 74.83  ? 4    GLU A OE1 1 
ATOM   33   O  OE2 . GLU A 1 4   ? -10.283 -33.917 -16.427 1.00 80.15  ? 4    GLU A OE2 1 
ATOM   34   N  N   . MET A 1 5   ? -8.149  -29.679 -14.479 1.00 47.89  ? 5    MET A N   1 
ATOM   35   C  CA  . MET A 1 5   ? -7.360  -29.170 -13.361 1.00 42.82  ? 5    MET A CA  1 
ATOM   36   C  C   . MET A 1 5   ? -6.632  -30.306 -12.647 1.00 37.91  ? 5    MET A C   1 
ATOM   37   O  O   . MET A 1 5   ? -7.097  -31.446 -12.642 1.00 37.90  ? 5    MET A O   1 
ATOM   38   C  CB  . MET A 1 5   ? -8.265  -28.412 -12.387 1.00 42.68  ? 5    MET A CB  1 
ATOM   39   C  CG  . MET A 1 5   ? -9.341  -29.281 -11.771 1.00 41.23  ? 5    MET A CG  1 
ATOM   40   S  SD  . MET A 1 5   ? -10.310 -28.466 -10.488 1.00 40.26  ? 5    MET A SD  1 
ATOM   41   C  CE  . MET A 1 5   ? -11.399 -27.508 -11.542 1.00 38.64  ? 5    MET A CE  1 
ATOM   42   N  N   . PRO A 1 6   ? -5.467  -30.029 -12.068 1.00 35.61  ? 6    PRO A N   1 
ATOM   43   C  CA  . PRO A 1 6   ? -4.756  -31.065 -11.313 1.00 33.90  ? 6    PRO A CA  1 
ATOM   44   C  C   . PRO A 1 6   ? -5.530  -31.495 -10.079 1.00 39.99  ? 6    PRO A C   1 
ATOM   45   O  O   . PRO A 1 6   ? -6.504  -30.870 -9.655  1.00 37.05  ? 6    PRO A O   1 
ATOM   46   C  CB  . PRO A 1 6   ? -3.443  -30.385 -10.926 1.00 37.30  ? 6    PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 6   ? -3.768  -28.942 -10.922 1.00 33.53  ? 6    PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 6   ? -4.744  -28.747 -12.046 1.00 36.14  ? 6    PRO A CD  1 
ATOM   49   N  N   . GLN A 1 7   ? -5.068  -32.598 -9.493  1.00 35.11  ? 7    GLN A N   1 
ATOM   50   C  CA  . GLN A 1 7   ? -5.672  -33.150 -8.289  1.00 34.53  ? 7    GLN A CA  1 
ATOM   51   C  C   . GLN A 1 7   ? -4.554  -33.804 -7.500  1.00 39.75  ? 7    GLN A C   1 
ATOM   52   O  O   . GLN A 1 7   ? -3.724  -34.506 -8.099  1.00 36.79  ? 7    GLN A O   1 
ATOM   53   C  CB  . GLN A 1 7   ? -6.754  -34.177 -8.615  1.00 34.73  ? 7    GLN A CB  1 
ATOM   54   C  CG  . GLN A 1 7   ? -7.378  -34.814 -7.369  1.00 35.42  ? 7    GLN A CG  1 
ATOM   55   C  CD  . GLN A 1 7   ? -8.484  -35.791 -7.727  1.00 40.09  ? 7    GLN A CD  1 
ATOM   56   O  OE1 . GLN A 1 7   ? -8.702  -36.098 -8.901  1.00 43.10  ? 7    GLN A OE1 1 
ATOM   57   N  NE2 . GLN A 1 7   ? -9.201  -36.272 -6.720  1.00 40.71  ? 7    GLN A NE2 1 
ATOM   58   N  N   . PRO A 1 8   ? -4.485  -33.586 -6.176  1.00 35.65  ? 8    PRO A N   1 
ATOM   59   C  CA  . PRO A 1 8   ? -3.423  -34.227 -5.389  1.00 31.66  ? 8    PRO A CA  1 
ATOM   60   C  C   . PRO A 1 8   ? -3.624  -35.727 -5.258  1.00 31.62  ? 8    PRO A C   1 
ATOM   61   O  O   . PRO A 1 8   ? -4.602  -36.289 -5.763  1.00 34.26  ? 8    PRO A O   1 
ATOM   62   C  CB  . PRO A 1 8   ? -3.502  -33.526 -4.023  1.00 32.01  ? 8    PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 8   ? -4.919  -33.032 -3.923  1.00 34.10  ? 8    PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 8   ? -5.308  -32.668 -5.361  1.00 34.11  ? 8    PRO A CD  1 
ATOM   65   N  N   . LYS A 1 9   ? -2.696  -36.386 -4.571  1.00 33.28  ? 9    LYS A N   1 
ATOM   66   C  CA  . LYS A 1 9   ? -2.698  -37.844 -4.544  1.00 35.14  ? 9    LYS A CA  1 
ATOM   67   C  C   . LYS A 1 9   ? -3.936  -38.384 -3.833  1.00 38.77  ? 9    LYS A C   1 
ATOM   68   O  O   . LYS A 1 9   ? -4.410  -37.811 -2.844  1.00 36.81  ? 9    LYS A O   1 
ATOM   69   C  CB  . LYS A 1 9   ? -1.426  -38.368 -3.859  1.00 34.74  ? 9    LYS A CB  1 
ATOM   70   C  CG  . LYS A 1 9   ? -1.254  -37.955 -2.394  1.00 33.35  ? 9    LYS A CG  1 
ATOM   71   C  CD  . LYS A 1 9   ? 0.179   -38.176 -1.915  1.00 34.76  ? 9    LYS A CD  1 
ATOM   72   C  CE  . LYS A 1 9   ? 0.339   -37.754 -0.461  1.00 39.75  ? 9    LYS A CE  1 
ATOM   73   N  NZ  . LYS A 1 9   ? 1.767   -37.604 -0.040  1.00 37.39  ? 9    LYS A NZ  1 
ATOM   74   N  N   . THR A 1 10  ? -4.435  -39.516 -4.330  1.00 32.54  ? 10   THR A N   1 
ATOM   75   C  CA  . THR A 1 10  ? -5.629  -40.182 -3.835  1.00 34.49  ? 10   THR A CA  1 
ATOM   76   C  C   . THR A 1 10  ? -5.295  -41.488 -3.123  1.00 35.37  ? 10   THR A C   1 
ATOM   77   O  O   . THR A 1 10  ? -4.208  -42.065 -3.272  1.00 32.56  ? 10   THR A O   1 
ATOM   78   C  CB  . THR A 1 10  ? -6.610  -40.465 -4.977  1.00 36.90  ? 10   THR A CB  1 
ATOM   79   O  OG1 . THR A 1 10  ? -5.994  -41.334 -5.953  1.00 37.78  ? 10   THR A OG1 1 
ATOM   80   C  CG2 . THR A 1 10  ? -7.048  -39.146 -5.626  1.00 34.04  ? 10   THR A CG2 1 
ATOM   81   N  N   . PHE A 1 11  ? -6.284  -41.949 -2.358  1.00 33.21  ? 11   PHE A N   1 
ATOM   82   C  CA  . PHE A 1 11  ? -6.174  -43.083 -1.449  1.00 35.65  ? 11   PHE A CA  1 
ATOM   83   C  C   . PHE A 1 11  ? -7.342  -44.045 -1.702  1.00 35.41  ? 11   PHE A C   1 
ATOM   84   O  O   . PHE A 1 11  ? -8.144  -44.338 -0.816  1.00 39.30  ? 11   PHE A O   1 
ATOM   85   C  CB  . PHE A 1 11  ? -6.175  -42.603 0.010   1.00 33.63  ? 11   PHE A CB  1 
ATOM   86   C  CG  . PHE A 1 11  ? -4.984  -41.772 0.386   1.00 33.96  ? 11   PHE A CG  1 
ATOM   87   C  CD1 . PHE A 1 11  ? -4.861  -40.457 -0.053  1.00 30.56  ? 11   PHE A CD1 1 
ATOM   88   C  CD2 . PHE A 1 11  ? -3.984  -42.293 1.188   1.00 32.70  ? 11   PHE A CD2 1 
ATOM   89   C  CE1 . PHE A 1 11  ? -3.765  -39.689 0.307   1.00 34.20  ? 11   PHE A CE1 1 
ATOM   90   C  CE2 . PHE A 1 11  ? -2.882  -41.523 1.558   1.00 32.79  ? 11   PHE A CE2 1 
ATOM   91   C  CZ  . PHE A 1 11  ? -2.772  -40.223 1.111   1.00 34.58  ? 11   PHE A CZ  1 
ATOM   92   N  N   . GLY A 1 12  ? -7.428  -44.552 -2.929  1.00 36.20  ? 12   GLY A N   1 
ATOM   93   C  CA  . GLY A 1 12  ? -8.507  -45.466 -3.273  1.00 36.76  ? 12   GLY A CA  1 
ATOM   94   C  C   . GLY A 1 12  ? -9.864  -44.840 -3.002  1.00 42.78  ? 12   GLY A C   1 
ATOM   95   O  O   . GLY A 1 12  ? -10.128 -43.692 -3.376  1.00 39.14  ? 12   GLY A O   1 
ATOM   96   N  N   . GLU A 1 13  ? -10.738 -45.596 -2.330  1.00 39.23  ? 13   GLU A N   1 
ATOM   97   C  CA  . GLU A 1 13  ? -12.111 -45.140 -2.120  1.00 46.37  ? 13   GLU A CA  1 
ATOM   98   C  C   . GLU A 1 13  ? -12.203 -43.923 -1.205  1.00 44.49  ? 13   GLU A C   1 
ATOM   99   O  O   . GLU A 1 13  ? -13.210 -43.204 -1.254  1.00 43.46  ? 13   GLU A O   1 
ATOM   100  C  CB  . GLU A 1 13  ? -12.972 -46.277 -1.554  1.00 49.13  ? 13   GLU A CB  1 
ATOM   101  C  CG  . GLU A 1 13  ? -13.260 -47.380 -2.570  1.00 56.64  ? 13   GLU A CG  1 
ATOM   102  C  CD  . GLU A 1 13  ? -13.962 -48.580 -1.961  1.00 77.18  ? 13   GLU A CD  1 
ATOM   103  O  OE1 . GLU A 1 13  ? -15.201 -48.531 -1.818  1.00 83.34  ? 13   GLU A OE1 1 
ATOM   104  O  OE2 . GLU A 1 13  ? -13.279 -49.575 -1.632  1.00 80.29  ? 13   GLU A OE2 1 
ATOM   105  N  N   . LEU A 1 14  ? -11.195 -43.683 -0.369  1.00 38.39  ? 14   LEU A N   1 
ATOM   106  C  CA  . LEU A 1 14  ? -11.158 -42.479 0.457   1.00 40.18  ? 14   LEU A CA  1 
ATOM   107  C  C   . LEU A 1 14  ? -10.789 -41.226 -0.328  1.00 39.25  ? 14   LEU A C   1 
ATOM   108  O  O   . LEU A 1 14  ? -10.846 -40.128 0.238   1.00 37.98  ? 14   LEU A O   1 
ATOM   109  C  CB  . LEU A 1 14  ? -10.175 -42.668 1.611   1.00 37.69  ? 14   LEU A CB  1 
ATOM   110  C  CG  . LEU A 1 14  ? -10.458 -43.878 2.502   1.00 42.78  ? 14   LEU A CG  1 
ATOM   111  C  CD1 . LEU A 1 14  ? -9.444  -43.972 3.630   1.00 43.40  ? 14   LEU A CD1 1 
ATOM   112  C  CD2 . LEU A 1 14  ? -11.874 -43.783 3.068   1.00 47.87  ? 14   LEU A CD2 1 
ATOM   113  N  N   . LYS A 1 15  ? -10.389 -41.369 -1.592  1.00 35.50  ? 15   LYS A N   1 
ATOM   114  C  CA  . LYS A 1 15  ? -10.076 -40.249 -2.496  1.00 35.95  ? 15   LYS A CA  1 
ATOM   115  C  C   . LYS A 1 15  ? -8.996  -39.376 -1.854  1.00 41.11  ? 15   LYS A C   1 
ATOM   116  O  O   . LYS A 1 15  ? -7.918  -39.892 -1.511  1.00 37.08  ? 15   LYS A O   1 
ATOM   117  C  CB  . LYS A 1 15  ? -11.397 -39.565 -2.817  1.00 41.16  ? 15   LYS A CB  1 
ATOM   118  C  CG  . LYS A 1 15  ? -12.411 -40.549 -3.384  1.00 45.94  ? 15   LYS A CG  1 
ATOM   119  C  CD  . LYS A 1 15  ? -13.571 -39.890 -4.100  1.00 51.84  ? 15   LYS A CD  1 
ATOM   120  C  CE  . LYS A 1 15  ? -14.656 -40.925 -4.407  1.00 58.16  ? 15   LYS A CE  1 
ATOM   121  N  NZ  . LYS A 1 15  ? -15.531 -40.505 -5.534  1.00 65.26  ? 15   LYS A NZ  1 
ATOM   122  N  N   . ASN A 1 16  ? -9.203  -38.064 -1.691  1.00 34.96  ? 16   ASN A N   1 
ATOM   123  C  CA  . ASN A 1 16  ? -8.181  -37.208 -1.100  1.00 36.08  ? 16   ASN A CA  1 
ATOM   124  C  C   . ASN A 1 16  ? -8.338  -37.047 0.408   1.00 34.62  ? 16   ASN A C   1 
ATOM   125  O  O   . ASN A 1 16  ? -7.526  -36.356 1.024   1.00 37.58  ? 16   ASN A O   1 
ATOM   126  C  CB  . ASN A 1 16  ? -8.201  -35.811 -1.740  1.00 34.73  ? 16   ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 16  ? -7.879  -35.832 -3.217  1.00 34.64  ? 16   ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 16  ? -8.710  -35.453 -4.056  1.00 34.19  ? 16   ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 16  ? -6.674  -36.301 -3.555  1.00 36.12  ? 16   ASN A ND2 1 
ATOM   130  N  N   . LEU A 1 17  ? -9.369  -37.640 1.007   1.00 37.65  ? 17   LEU A N   1 
ATOM   131  C  CA  . LEU A 1 17  ? -9.663  -37.389 2.418   1.00 37.34  ? 17   LEU A CA  1 
ATOM   132  C  C   . LEU A 1 17  ? -8.464  -37.554 3.338   1.00 39.25  ? 17   LEU A C   1 
ATOM   133  O  O   . LEU A 1 17  ? -8.277  -36.702 4.224   1.00 36.67  ? 17   LEU A O   1 
ATOM   134  C  CB  . LEU A 1 17  ? -10.809 -38.304 2.868   1.00 39.98  ? 17   LEU A CB  1 
ATOM   135  C  CG  . LEU A 1 17  ? -11.587 -37.831 4.091   1.00 45.64  ? 17   LEU A CG  1 
ATOM   136  C  CD1 . LEU A 1 17  ? -12.075 -36.398 3.883   1.00 42.68  ? 17   LEU A CD1 1 
ATOM   137  C  CD2 . LEU A 1 17  ? -12.753 -38.770 4.339   1.00 46.47  ? 17   LEU A CD2 1 
ATOM   138  N  N   . PRO A 1 18  ? -7.622  -38.581 3.192   1.00 34.13  ? 18   PRO A N   1 
ATOM   139  C  CA  . PRO A 1 18  ? -6.495  -38.745 4.128   1.00 32.72  ? 18   PRO A CA  1 
ATOM   140  C  C   . PRO A 1 18  ? -5.473  -37.628 4.085   1.00 33.18  ? 18   PRO A C   1 
ATOM   141  O  O   . PRO A 1 18  ? -4.663  -37.526 5.019   1.00 34.42  ? 18   PRO A O   1 
ATOM   142  C  CB  . PRO A 1 18  ? -5.872  -40.083 3.700   1.00 34.32  ? 18   PRO A CB  1 
ATOM   143  C  CG  . PRO A 1 18  ? -7.038  -40.834 3.119   1.00 36.08  ? 18   PRO A CG  1 
ATOM   144  C  CD  . PRO A 1 18  ? -7.825  -39.773 2.354   1.00 33.75  ? 18   PRO A CD  1 
ATOM   145  N  N   . LEU A 1 19  ? -5.482  -36.776 3.057   1.00 33.12  ? 19   LEU A N   1 
ATOM   146  C  CA  . LEU A 1 19  ? -4.596  -35.618 3.067   1.00 31.92  ? 19   LEU A CA  1 
ATOM   147  C  C   . LEU A 1 19  ? -4.926  -34.665 4.209   1.00 33.03  ? 19   LEU A C   1 
ATOM   148  O  O   . LEU A 1 19  ? -4.067  -33.878 4.616   1.00 36.22  ? 19   LEU A O   1 
ATOM   149  C  CB  . LEU A 1 19  ? -4.676  -34.896 1.722   1.00 36.54  ? 19   LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 19  ? -4.178  -35.760 0.550   1.00 34.99  ? 19   LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 19  ? -4.357  -35.023 -0.784  1.00 35.55  ? 19   LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 19  ? -2.725  -36.158 0.762   1.00 37.96  ? 19   LEU A CD2 1 
ATOM   153  N  N   . LEU A 1 20  ? -6.141  -34.732 4.738   1.00 33.69  ? 20   LEU A N   1 
ATOM   154  C  CA  . LEU A 1 20  ? -6.554  -33.926 5.884   1.00 34.49  ? 20   LEU A CA  1 
ATOM   155  C  C   . LEU A 1 20  ? -6.239  -34.585 7.219   1.00 38.18  ? 20   LEU A C   1 
ATOM   156  O  O   . LEU A 1 20  ? -6.546  -34.000 8.270   1.00 37.28  ? 20   LEU A O   1 
ATOM   157  C  CB  . LEU A 1 20  ? -8.056  -33.643 5.818   1.00 35.65  ? 20   LEU A CB  1 
ATOM   158  C  CG  . LEU A 1 20  ? -8.500  -32.929 4.544   1.00 39.91  ? 20   LEU A CG  1 
ATOM   159  C  CD1 . LEU A 1 20  ? -10.017 -32.695 4.523   1.00 36.91  ? 20   LEU A CD1 1 
ATOM   160  C  CD2 . LEU A 1 20  ? -7.724  -31.630 4.411   1.00 37.70  ? 20   LEU A CD2 1 
ATOM   161  N  N   . ASN A 1 21  ? -5.658  -35.786 7.216   1.00 38.15  ? 21   ASN A N   1 
ATOM   162  C  CA  . ASN A 1 21  ? -5.354  -36.478 8.473   1.00 38.93  ? 21   ASN A CA  1 
ATOM   163  C  C   . ASN A 1 21  ? -4.011  -35.949 8.981   1.00 40.02  ? 21   ASN A C   1 
ATOM   164  O  O   . ASN A 1 21  ? -2.960  -36.591 8.889   1.00 43.09  ? 21   ASN A O   1 
ATOM   165  C  CB  . ASN A 1 21  ? -5.319  -37.988 8.271   1.00 42.85  ? 21   ASN A CB  1 
ATOM   166  C  CG  . ASN A 1 21  ? -5.087  -38.748 9.578   1.00 51.11  ? 21   ASN A CG  1 
ATOM   167  O  OD1 . ASN A 1 21  ? -4.824  -38.148 10.624  1.00 49.73  ? 21   ASN A OD1 1 
ATOM   168  N  ND2 . ASN A 1 21  ? -5.161  -40.073 9.513   1.00 49.59  ? 21   ASN A ND2 1 
ATOM   169  N  N   . THR A 1 22  ? -4.061  -34.724 9.496   1.00 36.61  ? 22   THR A N   1 
ATOM   170  C  CA  . THR A 1 22  ? -2.900  -34.001 9.989   1.00 36.82  ? 22   THR A CA  1 
ATOM   171  C  C   . THR A 1 22  ? -3.395  -32.943 10.960  1.00 38.04  ? 22   THR A C   1 
ATOM   172  O  O   . THR A 1 22  ? -4.553  -32.540 10.914  1.00 37.91  ? 22   THR A O   1 
ATOM   173  C  CB  . THR A 1 22  ? -2.092  -33.351 8.857   1.00 37.93  ? 22   THR A CB  1 
ATOM   174  O  OG1 . THR A 1 22  ? -1.157  -32.414 9.416   1.00 41.50  ? 22   THR A OG1 1 
ATOM   175  C  CG2 . THR A 1 22  ? -3.015  -32.622 7.852   1.00 38.50  ? 22   THR A CG2 1 
ATOM   176  N  N   . ASP A 1 23  ? -2.510  -32.493 11.847  1.00 39.44  ? 23   ASP A N   1 
ATOM   177  C  CA  . ASP A 1 23  ? -2.954  -31.446 12.754  1.00 38.71  ? 23   ASP A CA  1 
ATOM   178  C  C   . ASP A 1 23  ? -2.893  -30.072 12.107  1.00 39.89  ? 23   ASP A C   1 
ATOM   179  O  O   . ASP A 1 23  ? -3.382  -29.109 12.702  1.00 35.11  ? 23   ASP A O   1 
ATOM   180  C  CB  . ASP A 1 23  ? -2.118  -31.436 14.029  1.00 44.54  ? 23   ASP A CB  1 
ATOM   181  C  CG  . ASP A 1 23  ? -0.641  -31.412 13.745  1.00 49.19  ? 23   ASP A CG  1 
ATOM   182  O  OD1 . ASP A 1 23  ? -0.248  -31.760 12.609  1.00 58.70  ? 23   ASP A OD1 1 
ATOM   183  O  OD2 . ASP A 1 23  ? 0.130   -31.061 14.667  1.00 63.69  ? 23   ASP A OD2 1 
ATOM   184  N  N   . LYS A 1 24  ? -2.313  -29.965 10.910  1.00 35.99  ? 24   LYS A N   1 
ATOM   185  C  CA  . LYS A 1 24  ? -2.177  -28.687 10.207  1.00 32.00  ? 24   LYS A CA  1 
ATOM   186  C  C   . LYS A 1 24  ? -2.729  -28.798 8.786   1.00 32.83  ? 24   LYS A C   1 
ATOM   187  O  O   . LYS A 1 24  ? -1.995  -28.651 7.804   1.00 34.28  ? 24   LYS A O   1 
ATOM   188  C  CB  . LYS A 1 24  ? -0.714  -28.245 10.206  1.00 30.79  ? 24   LYS A CB  1 
ATOM   189  C  CG  . LYS A 1 24  ? -0.176  -27.961 11.592  1.00 36.49  ? 24   LYS A CG  1 
ATOM   190  C  CD  . LYS A 1 24  ? 1.303   -27.573 11.570  1.00 36.50  ? 24   LYS A CD  1 
ATOM   191  C  CE  . LYS A 1 24  ? 1.786   -27.267 12.997  1.00 38.61  ? 24   LYS A CE  1 
ATOM   192  N  NZ  . LYS A 1 24  ? 3.195   -26.803 13.035  1.00 40.14  ? 24   LYS A NZ  1 
ATOM   193  N  N   . PRO A 1 25  ? -4.040  -29.037 8.642   1.00 34.38  ? 25   PRO A N   1 
ATOM   194  C  CA  . PRO A 1 25  ? -4.596  -29.251 7.295   1.00 33.83  ? 25   PRO A CA  1 
ATOM   195  C  C   . PRO A 1 25  ? -4.532  -28.035 6.376   1.00 35.87  ? 25   PRO A C   1 
ATOM   196  O  O   . PRO A 1 25  ? -4.274  -28.207 5.177   1.00 33.63  ? 25   PRO A O   1 
ATOM   197  C  CB  . PRO A 1 25  ? -6.045  -29.680 7.579   1.00 32.59  ? 25   PRO A CB  1 
ATOM   198  C  CG  . PRO A 1 25  ? -6.349  -29.138 8.924   1.00 32.80  ? 25   PRO A CG  1 
ATOM   199  C  CD  . PRO A 1 25  ? -5.059  -29.191 9.694   1.00 35.75  ? 25   PRO A CD  1 
ATOM   200  N  N   . VAL A 1 26  ? -4.786  -26.820 6.871   1.00 33.02  ? 26   VAL A N   1 
ATOM   201  C  CA  . VAL A 1 26  ? -4.672  -25.648 5.999   1.00 33.35  ? 26   VAL A CA  1 
ATOM   202  C  C   . VAL A 1 26  ? -3.253  -25.513 5.462   1.00 34.99  ? 26   VAL A C   1 
ATOM   203  O  O   . VAL A 1 26  ? -3.038  -25.256 4.270   1.00 34.71  ? 26   VAL A O   1 
ATOM   204  C  CB  . VAL A 1 26  ? -5.106  -24.374 6.741   1.00 31.83  ? 26   VAL A CB  1 
ATOM   205  C  CG1 . VAL A 1 26  ? -4.783  -23.157 5.883   1.00 32.48  ? 26   VAL A CG1 1 
ATOM   206  C  CG2 . VAL A 1 26  ? -6.587  -24.439 7.033   1.00 33.84  ? 26   VAL A CG2 1 
ATOM   207  N  N   . GLN A 1 27  ? -2.258  -25.664 6.336   1.00 31.46  ? 27   GLN A N   1 
ATOM   208  C  CA  . GLN A 1 27  ? -0.881  -25.554 5.872   1.00 32.94  ? 27   GLN A CA  1 
ATOM   209  C  C   . GLN A 1 27  ? -0.532  -26.685 4.903   1.00 34.91  ? 27   GLN A C   1 
ATOM   210  O  O   . GLN A 1 27  ? 0.227   -26.472 3.947   1.00 36.17  ? 27   GLN A O   1 
ATOM   211  C  CB  . GLN A 1 27  ? 0.064   -25.512 7.079   1.00 34.28  ? 27   GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 27  ? -0.094  -24.215 7.889   1.00 33.46  ? 27   GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 27  ? 0.491   -24.301 9.274   1.00 32.02  ? 27   GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 27  ? 1.678   -24.051 9.474   1.00 35.06  ? 27   GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 27  ? -0.352  -24.614 10.257  1.00 33.61  ? 27   GLN A NE2 1 
ATOM   216  N  N   . ALA A 1 28  ? -1.122  -27.864 5.085   1.00 33.50  ? 28   ALA A N   1 
ATOM   217  C  CA  . ALA A 1 28  ? -0.920  -28.939 4.111   1.00 34.00  ? 28   ALA A CA  1 
ATOM   218  C  C   . ALA A 1 28  ? -1.527  -28.576 2.763   1.00 34.38  ? 28   ALA A C   1 
ATOM   219  O  O   . ALA A 1 28  ? -0.938  -28.870 1.710   1.00 34.70  ? 28   ALA A O   1 
ATOM   220  C  CB  . ALA A 1 28  ? -1.512  -30.250 4.633   1.00 34.20  ? 28   ALA A CB  1 
ATOM   221  N  N   . LEU A 1 29  ? -2.719  -27.950 2.771   1.00 31.34  ? 29   LEU A N   1 
ATOM   222  C  CA  . LEU A 1 29  ? -3.345  -27.523 1.520   1.00 31.16  ? 29   LEU A CA  1 
ATOM   223  C  C   . LEU A 1 29  ? -2.553  -26.419 0.837   1.00 30.27  ? 29   LEU A C   1 
ATOM   224  O  O   . LEU A 1 29  ? -2.491  -26.376 -0.398  1.00 32.44  ? 29   LEU A O   1 
ATOM   225  C  CB  . LEU A 1 29  ? -4.787  -27.057 1.775   1.00 33.33  ? 29   LEU A CB  1 
ATOM   226  C  CG  . LEU A 1 29  ? -5.731  -28.219 2.104   1.00 32.89  ? 29   LEU A CG  1 
ATOM   227  C  CD1 . LEU A 1 29  ? -6.962  -27.730 2.875   1.00 34.38  ? 29   LEU A CD1 1 
ATOM   228  C  CD2 . LEU A 1 29  ? -6.145  -28.956 0.835   1.00 31.00  ? 29   LEU A CD2 1 
ATOM   229  N  N   . MET A 1 30  ? -1.947  -25.520 1.611   1.00 34.25  ? 30   MET A N   1 
ATOM   230  C  CA  . MET A 1 30  ? -1.047  -24.526 1.032   1.00 30.64  ? 30   MET A CA  1 
ATOM   231  C  C   . MET A 1 30  ? 0.125   -25.176 0.304   1.00 33.75  ? 30   MET A C   1 
ATOM   232  O  O   . MET A 1 30  ? 0.520   -24.722 -0.778  1.00 35.48  ? 30   MET A O   1 
ATOM   233  C  CB  . MET A 1 30  ? -0.550  -23.596 2.128   1.00 32.14  ? 30   MET A CB  1 
ATOM   234  C  CG  . MET A 1 30  ? -1.648  -22.674 2.659   1.00 35.51  ? 30   MET A CG  1 
ATOM   235  S  SD  . MET A 1 30  ? -1.120  -21.776 4.108   1.00 35.46  ? 30   MET A SD  1 
ATOM   236  C  CE  . MET A 1 30  ? 0.122   -20.668 3.447   1.00 36.11  ? 30   MET A CE  1 
ATOM   237  N  N   . LYS A 1 31  ? 0.707   -26.219 0.893   1.00 35.54  ? 31   LYS A N   1 
ATOM   238  C  CA  . LYS A 1 31  ? 1.805   -26.926 0.231   1.00 34.69  ? 31   LYS A CA  1 
ATOM   239  C  C   . LYS A 1 31  ? 1.343   -27.576 -1.066  1.00 38.27  ? 31   LYS A C   1 
ATOM   240  O  O   . LYS A 1 31  ? 2.066   -27.563 -2.075  1.00 36.99  ? 31   LYS A O   1 
ATOM   241  C  CB  . LYS A 1 31  ? 2.394   -27.964 1.186   1.00 39.41  ? 31   LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 31  ? 3.688   -28.601 0.706   1.00 45.83  ? 31   LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 31  ? 4.928   -27.893 1.250   1.00 57.52  ? 31   LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 31  ? 5.152   -28.177 2.727   1.00 58.64  ? 31   LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 31  ? 5.979   -27.103 3.359   1.00 67.51  ? 31   LYS A NZ  1 
ATOM   246  N  N   . ILE A 1 32  ? 0.135   -28.137 -1.070  1.00 32.52  ? 32   ILE A N   1 
ATOM   247  C  CA  . ILE A 1 32  ? -0.413  -28.709 -2.297  1.00 35.08  ? 32   ILE A CA  1 
ATOM   248  C  C   . ILE A 1 32  ? -0.587  -27.625 -3.356  1.00 36.44  ? 32   ILE A C   1 
ATOM   249  O  O   . ILE A 1 32  ? -0.217  -27.801 -4.526  1.00 33.57  ? 32   ILE A O   1 
ATOM   250  C  CB  . ILE A 1 32  ? -1.738  -29.429 -2.001  1.00 34.97  ? 32   ILE A CB  1 
ATOM   251  C  CG1 . ILE A 1 32  ? -1.482  -30.647 -1.095  1.00 35.86  ? 32   ILE A CG1 1 
ATOM   252  C  CG2 . ILE A 1 32  ? -2.434  -29.826 -3.316  1.00 35.77  ? 32   ILE A CG2 1 
ATOM   253  C  CD1 . ILE A 1 32  ? -2.756  -31.305 -0.560  1.00 32.42  ? 32   ILE A CD1 1 
ATOM   254  N  N   . ALA A 1 33  ? -1.189  -26.495 -2.970  1.00 34.95  ? 33   ALA A N   1 
ATOM   255  C  CA  . ALA A 1 33  ? -1.317  -25.382 -3.908  1.00 35.19  ? 33   ALA A CA  1 
ATOM   256  C  C   . ALA A 1 33  ? 0.044   -24.945 -4.434  1.00 36.50  ? 33   ALA A C   1 
ATOM   257  O  O   . ALA A 1 33  ? 0.177   -24.565 -5.602  1.00 37.35  ? 33   ALA A O   1 
ATOM   258  C  CB  . ALA A 1 33  ? -2.032  -24.210 -3.233  1.00 34.94  ? 33   ALA A CB  1 
ATOM   259  N  N   . ASP A 1 34  ? 1.064   -24.969 -3.579  1.00 37.19  ? 34   ASP A N   1 
ATOM   260  C  CA  . ASP A 1 34  ? 2.398   -24.611 -4.038  1.00 39.21  ? 34   ASP A CA  1 
ATOM   261  C  C   . ASP A 1 34  ? 2.803   -25.502 -5.201  1.00 38.99  ? 34   ASP A C   1 
ATOM   262  O  O   . ASP A 1 34  ? 3.448   -25.055 -6.158  1.00 43.44  ? 34   ASP A O   1 
ATOM   263  C  CB  . ASP A 1 34  ? 3.401   -24.782 -2.906  1.00 38.65  ? 34   ASP A CB  1 
ATOM   264  C  CG  . ASP A 1 34  ? 3.576   -23.530 -2.086  1.00 45.11  ? 34   ASP A CG  1 
ATOM   265  O  OD1 . ASP A 1 34  ? 3.239   -22.426 -2.566  1.00 47.53  ? 34   ASP A OD1 1 
ATOM   266  O  OD2 . ASP A 1 34  ? 4.071   -23.667 -0.947  1.00 47.65  ? 34   ASP A OD2 1 
ATOM   267  N  N   . GLU A 1 35  ? 2.438   -26.777 -5.122  1.00 36.72  ? 35   GLU A N   1 
ATOM   268  C  CA  . GLU A 1 35  ? 2.848   -27.773 -6.101  1.00 38.36  ? 35   GLU A CA  1 
ATOM   269  C  C   . GLU A 1 35  ? 1.933   -27.802 -7.320  1.00 42.19  ? 35   GLU A C   1 
ATOM   270  O  O   . GLU A 1 35  ? 2.418   -27.928 -8.451  1.00 41.48  ? 35   GLU A O   1 
ATOM   271  C  CB  . GLU A 1 35  ? 2.897   -29.155 -5.437  1.00 45.25  ? 35   GLU A CB  1 
ATOM   272  C  CG  . GLU A 1 35  ? 3.282   -30.282 -6.390  1.00 50.98  ? 35   GLU A CG  1 
ATOM   273  C  CD  . GLU A 1 35  ? 3.150   -31.668 -5.772  1.00 59.05  ? 35   GLU A CD  1 
ATOM   274  O  OE1 . GLU A 1 35  ? 3.287   -31.792 -4.537  1.00 58.99  ? 35   GLU A OE1 1 
ATOM   275  O  OE2 . GLU A 1 35  ? 2.929   -32.638 -6.537  1.00 62.98  ? 35   GLU A OE2 1 
ATOM   276  N  N   . LEU A 1 36  ? 0.620   -27.662 -7.123  1.00 33.56  ? 36   LEU A N   1 
ATOM   277  C  CA  . LEU A 1 36  ? -0.345  -27.820 -8.202  1.00 34.72  ? 36   LEU A CA  1 
ATOM   278  C  C   . LEU A 1 36  ? -0.774  -26.515 -8.863  1.00 37.96  ? 36   LEU A C   1 
ATOM   279  O  O   . LEU A 1 36  ? -1.216  -26.541 -10.021 1.00 36.71  ? 36   LEU A O   1 
ATOM   280  C  CB  . LEU A 1 36  ? -1.593  -28.547 -7.694  1.00 35.50  ? 36   LEU A CB  1 
ATOM   281  C  CG  . LEU A 1 36  ? -1.336  -29.968 -7.178  1.00 35.84  ? 36   LEU A CG  1 
ATOM   282  C  CD1 . LEU A 1 36  ? -2.661  -30.696 -6.962  1.00 37.95  ? 36   LEU A CD1 1 
ATOM   283  C  CD2 . LEU A 1 36  ? -0.421  -30.742 -8.140  1.00 40.73  ? 36   LEU A CD2 1 
ATOM   284  N  N   . GLY A 1 37  ? -0.683  -25.390 -8.171  1.00 34.91  ? 37   GLY A N   1 
ATOM   285  C  CA  . GLY A 1 37  ? -0.990  -24.102 -8.762  1.00 33.03  ? 37   GLY A CA  1 
ATOM   286  C  C   . GLY A 1 37  ? -2.310  -23.520 -8.290  1.00 37.58  ? 37   GLY A C   1 
ATOM   287  O  O   . GLY A 1 37  ? -2.828  -23.835 -7.209  1.00 35.63  ? 37   GLY A O   1 
ATOM   288  N  N   . GLU A 1 38  ? -2.874  -22.659 -9.140  1.00 31.76  ? 38   GLU A N   1 
ATOM   289  C  CA  . GLU A 1 38  ? -3.983  -21.797 -8.728  1.00 33.94  ? 38   GLU A CA  1 
ATOM   290  C  C   . GLU A 1 38  ? -5.304  -22.539 -8.513  1.00 35.02  ? 38   GLU A C   1 
ATOM   291  O  O   . GLU A 1 38  ? -6.220  -21.978 -7.901  1.00 34.11  ? 38   GLU A O   1 
ATOM   292  C  CB  . GLU A 1 38  ? -4.185  -20.696 -9.777  1.00 33.94  ? 38   GLU A CB  1 
ATOM   293  C  CG  . GLU A 1 38  ? -4.652  -21.254 -11.119 1.00 33.92  ? 38   GLU A CG  1 
ATOM   294  C  CD  . GLU A 1 38  ? -4.843  -20.178 -12.184 1.00 39.39  ? 38   GLU A CD  1 
ATOM   295  O  OE1 . GLU A 1 38  ? -4.911  -18.976 -11.831 1.00 34.67  ? 38   GLU A OE1 1 
ATOM   296  O  OE2 . GLU A 1 38  ? -4.911  -20.545 -13.378 1.00 40.28  ? 38   GLU A OE2 1 
ATOM   297  N  N   . ILE A 1 39  ? -5.451  -23.763 -9.001  1.00 31.81  ? 39   ILE A N   1 
ATOM   298  C  CA  . ILE A 1 39  ? -6.712  -24.486 -8.849  1.00 30.85  ? 39   ILE A CA  1 
ATOM   299  C  C   . ILE A 1 39  ? -6.427  -25.978 -8.790  1.00 38.34  ? 39   ILE A C   1 
ATOM   300  O  O   . ILE A 1 39  ? -5.664  -26.502 -9.605  1.00 34.37  ? 39   ILE A O   1 
ATOM   301  C  CB  . ILE A 1 39  ? -7.693  -24.151 -9.990  1.00 33.66  ? 39   ILE A CB  1 
ATOM   302  C  CG1 . ILE A 1 39  ? -9.036  -24.843 -9.768  1.00 35.04  ? 39   ILE A CG1 1 
ATOM   303  C  CG2 . ILE A 1 39  ? -7.104  -24.524 -11.360 1.00 35.28  ? 39   ILE A CG2 1 
ATOM   304  C  CD1 . ILE A 1 39  ? -10.150 -24.258 -10.608 1.00 39.45  ? 39   ILE A CD1 1 
ATOM   305  N  N   . PHE A 1 40  ? -7.021  -26.674 -7.818  1.00 31.44  ? 40   PHE A N   1 
ATOM   306  C  CA  . PHE A 1 40  ? -6.948  -28.128 -7.843  1.00 33.38  ? 40   PHE A CA  1 
ATOM   307  C  C   . PHE A 1 40  ? -8.231  -28.736 -7.304  1.00 36.29  ? 40   PHE A C   1 
ATOM   308  O  O   . PHE A 1 40  ? -8.894  -28.170 -6.429  1.00 33.50  ? 40   PHE A O   1 
ATOM   309  C  CB  . PHE A 1 40  ? -5.707  -28.671 -7.089  1.00 32.55  ? 40   PHE A CB  1 
ATOM   310  C  CG  . PHE A 1 40  ? -5.643  -28.319 -5.614  1.00 32.59  ? 40   PHE A CG  1 
ATOM   311  C  CD1 . PHE A 1 40  ? -6.238  -29.134 -4.666  1.00 33.42  ? 40   PHE A CD1 1 
ATOM   312  C  CD2 . PHE A 1 40  ? -4.924  -27.221 -5.185  1.00 33.78  ? 40   PHE A CD2 1 
ATOM   313  C  CE1 . PHE A 1 40  ? -6.149  -28.832 -3.303  1.00 30.80  ? 40   PHE A CE1 1 
ATOM   314  C  CE2 . PHE A 1 40  ? -4.828  -26.915 -3.842  1.00 34.70  ? 40   PHE A CE2 1 
ATOM   315  C  CZ  . PHE A 1 40  ? -5.451  -27.721 -2.894  1.00 31.78  ? 40   PHE A CZ  1 
ATOM   316  N  N   . LYS A 1 41  ? -8.577  -29.889 -7.873  1.00 33.93  ? 41   LYS A N   1 
ATOM   317  C  CA  . LYS A 1 41  ? -9.723  -30.675 -7.446  1.00 34.33  ? 41   LYS A CA  1 
ATOM   318  C  C   . LYS A 1 41  ? -9.405  -31.437 -6.159  1.00 33.21  ? 41   LYS A C   1 
ATOM   319  O  O   . LYS A 1 41  ? -8.293  -31.932 -5.979  1.00 35.05  ? 41   LYS A O   1 
ATOM   320  C  CB  . LYS A 1 41  ? -10.099 -31.650 -8.557  1.00 34.82  ? 41   LYS A CB  1 
ATOM   321  C  CG  . LYS A 1 41  ? -11.289 -32.522 -8.259  1.00 35.67  ? 41   LYS A CG  1 
ATOM   322  C  CD  . LYS A 1 41  ? -11.681 -33.296 -9.515  1.00 45.36  ? 41   LYS A CD  1 
ATOM   323  C  CE  . LYS A 1 41  ? -12.739 -34.336 -9.215  1.00 50.57  ? 41   LYS A CE  1 
ATOM   324  N  NZ  . LYS A 1 41  ? -13.675 -34.533 -10.355 1.00 56.12  ? 41   LYS A NZ  1 
ATOM   325  N  N   . PHE A 1 42  ? -10.379 -31.504 -5.247  1.00 32.34  ? 42   PHE A N   1 
ATOM   326  C  CA  . PHE A 1 42  ? -10.209 -32.237 -3.994  1.00 33.42  ? 42   PHE A CA  1 
ATOM   327  C  C   . PHE A 1 42  ? -11.484 -33.027 -3.760  1.00 39.56  ? 42   PHE A C   1 
ATOM   328  O  O   . PHE A 1 42  ? -12.564 -32.437 -3.654  1.00 36.21  ? 42   PHE A O   1 
ATOM   329  C  CB  . PHE A 1 42  ? -9.937  -31.288 -2.819  1.00 33.58  ? 42   PHE A CB  1 
ATOM   330  C  CG  . PHE A 1 42  ? -9.478  -31.978 -1.551  1.00 33.78  ? 42   PHE A CG  1 
ATOM   331  C  CD1 . PHE A 1 42  ? -10.388 -32.574 -0.689  1.00 39.60  ? 42   PHE A CD1 1 
ATOM   332  C  CD2 . PHE A 1 42  ? -8.135  -31.986 -1.201  1.00 34.24  ? 42   PHE A CD2 1 
ATOM   333  C  CE1 . PHE A 1 42  ? -9.957  -33.188 0.491   1.00 37.44  ? 42   PHE A CE1 1 
ATOM   334  C  CE2 . PHE A 1 42  ? -7.702  -32.602 -0.025  1.00 38.76  ? 42   PHE A CE2 1 
ATOM   335  C  CZ  . PHE A 1 42  ? -8.623  -33.202 0.815   1.00 36.29  ? 42   PHE A CZ  1 
ATOM   336  N  N   . GLU A 1 43  ? -11.357 -34.352 -3.672  1.00 37.82  ? 43   GLU A N   1 
ATOM   337  C  CA  . GLU A 1 43  ? -12.495 -35.245 -3.525  1.00 36.82  ? 43   GLU A CA  1 
ATOM   338  C  C   . GLU A 1 43  ? -12.461 -35.990 -2.199  1.00 38.92  ? 43   GLU A C   1 
ATOM   339  O  O   . GLU A 1 43  ? -11.395 -36.303 -1.657  1.00 38.52  ? 43   GLU A O   1 
ATOM   340  C  CB  . GLU A 1 43  ? -12.563 -36.285 -4.645  1.00 39.66  ? 43   GLU A CB  1 
ATOM   341  C  CG  . GLU A 1 43  ? -12.756 -35.728 -6.028  1.00 45.61  ? 43   GLU A CG  1 
ATOM   342  C  CD  . GLU A 1 43  ? -12.800 -36.828 -7.061  1.00 51.98  ? 43   GLU A CD  1 
ATOM   343  O  OE1 . GLU A 1 43  ? -11.830 -37.614 -7.127  1.00 50.48  ? 43   GLU A OE1 1 
ATOM   344  O  OE2 . GLU A 1 43  ? -13.809 -36.919 -7.784  1.00 55.94  ? 43   GLU A OE2 1 
ATOM   345  N  N   . ALA A 1 44  ? -13.657 -36.284 -1.696  1.00 39.77  ? 44   ALA A N   1 
ATOM   346  C  CA  . ALA A 1 44  ? -13.867 -37.173 -0.560  1.00 40.43  ? 44   ALA A CA  1 
ATOM   347  C  C   . ALA A 1 44  ? -15.056 -38.052 -0.914  1.00 40.77  ? 44   ALA A C   1 
ATOM   348  O  O   . ALA A 1 44  ? -15.770 -37.755 -1.875  1.00 41.44  ? 44   ALA A O   1 
ATOM   349  C  CB  . ALA A 1 44  ? -14.121 -36.393 0.730   1.00 44.42  ? 44   ALA A CB  1 
ATOM   350  N  N   . PRO A 1 45  ? -15.312 -39.132 -0.190  1.00 40.95  ? 45   PRO A N   1 
ATOM   351  C  CA  . PRO A 1 45  ? -16.513 -39.917 -0.501  1.00 44.38  ? 45   PRO A CA  1 
ATOM   352  C  C   . PRO A 1 45  ? -17.750 -39.029 -0.553  1.00 46.43  ? 45   PRO A C   1 
ATOM   353  O  O   . PRO A 1 45  ? -18.064 -38.339 0.421   1.00 43.85  ? 45   PRO A O   1 
ATOM   354  C  CB  . PRO A 1 45  ? -16.569 -40.935 0.642   1.00 46.49  ? 45   PRO A CB  1 
ATOM   355  C  CG  . PRO A 1 45  ? -15.119 -41.123 1.024   1.00 40.86  ? 45   PRO A CG  1 
ATOM   356  C  CD  . PRO A 1 45  ? -14.494 -39.754 0.866   1.00 41.81  ? 45   PRO A CD  1 
ATOM   357  N  N   . GLY A 1 46  ? -18.417 -38.998 -1.707  1.00 46.71  ? 46   GLY A N   1 
ATOM   358  C  CA  . GLY A 1 46  ? -19.650 -38.249 -1.863  1.00 51.39  ? 46   GLY A CA  1 
ATOM   359  C  C   . GLY A 1 46  ? -19.513 -36.742 -1.891  1.00 52.18  ? 46   GLY A C   1 
ATOM   360  O  O   . GLY A 1 46  ? -20.490 -36.041 -1.614  1.00 55.17  ? 46   GLY A O   1 
ATOM   361  N  N   . ARG A 1 47  ? -18.334 -36.213 -2.217  1.00 47.25  ? 47   ARG A N   1 
ATOM   362  C  CA  . ARG A 1 47  ? -18.158 -34.766 -2.227  1.00 44.30  ? 47   ARG A CA  1 
ATOM   363  C  C   . ARG A 1 47  ? -16.985 -34.390 -3.120  1.00 47.74  ? 47   ARG A C   1 
ATOM   364  O  O   . ARG A 1 47  ? -15.958 -35.077 -3.131  1.00 42.79  ? 47   ARG A O   1 
ATOM   365  C  CB  . ARG A 1 47  ? -17.923 -34.204 -0.818  1.00 43.12  ? 47   ARG A CB  1 
ATOM   366  C  CG  . ARG A 1 47  ? -17.383 -32.776 -0.868  1.00 50.67  ? 47   ARG A CG  1 
ATOM   367  C  CD  . ARG A 1 47  ? -18.023 -31.828 0.140   1.00 44.14  ? 47   ARG A CD  1 
ATOM   368  N  NE  . ARG A 1 47  ? -17.358 -30.527 0.164   1.00 45.35  ? 47   ARG A NE  1 
ATOM   369  C  CZ  . ARG A 1 47  ? -16.602 -30.066 1.155   1.00 47.13  ? 47   ARG A CZ  1 
ATOM   370  N  NH1 . ARG A 1 47  ? -16.369 -30.788 2.242   1.00 45.63  ? 47   ARG A NH1 1 
ATOM   371  N  NH2 . ARG A 1 47  ? -16.076 -28.844 1.057   1.00 40.93  ? 47   ARG A NH2 1 
ATOM   372  N  N   . VAL A 1 48  ? -17.141 -33.284 -3.846  1.00 39.00  ? 48   VAL A N   1 
ATOM   373  C  CA  . VAL A 1 48  ? -16.069 -32.700 -4.645  1.00 36.96  ? 48   VAL A CA  1 
ATOM   374  C  C   . VAL A 1 48  ? -16.003 -31.205 -4.344  1.00 37.53  ? 48   VAL A C   1 
ATOM   375  O  O   . VAL A 1 48  ? -17.040 -30.550 -4.186  1.00 36.89  ? 48   VAL A O   1 
ATOM   376  C  CB  . VAL A 1 48  ? -16.291 -32.930 -6.154  1.00 41.06  ? 48   VAL A CB  1 
ATOM   377  C  CG1 . VAL A 1 48  ? -15.239 -32.184 -6.976  1.00 39.12  ? 48   VAL A CG1 1 
ATOM   378  C  CG2 . VAL A 1 48  ? -16.296 -34.417 -6.485  1.00 48.48  ? 48   VAL A CG2 1 
ATOM   379  N  N   . THR A 1 49  ? -14.791 -30.661 -4.279  1.00 33.11  ? 49   THR A N   1 
ATOM   380  C  CA  . THR A 1 49  ? -14.619 -29.216 -4.253  1.00 35.36  ? 49   THR A CA  1 
ATOM   381  C  C   . THR A 1 49  ? -13.352 -28.870 -5.022  1.00 36.62  ? 49   THR A C   1 
ATOM   382  O  O   . THR A 1 49  ? -12.609 -29.749 -5.473  1.00 37.28  ? 49   THR A O   1 
ATOM   383  C  CB  . THR A 1 49  ? -14.607 -28.658 -2.807  1.00 31.55  ? 49   THR A CB  1 
ATOM   384  O  OG1 . THR A 1 49  ? -14.755 -27.227 -2.839  1.00 33.05  ? 49   THR A OG1 1 
ATOM   385  C  CG2 . THR A 1 49  ? -13.306 -29.015 -2.086  1.00 34.47  ? 49   THR A CG2 1 
ATOM   386  N  N   . ARG A 1 50  ? -13.136 -27.574 -5.217  1.00 35.42  ? 50   ARG A N   1 
ATOM   387  C  CA  . ARG A 1 50  ? -11.991 -27.068 -5.962  1.00 34.37  ? 50   ARG A CA  1 
ATOM   388  C  C   . ARG A 1 50  ? -11.344 -25.960 -5.151  1.00 33.12  ? 50   ARG A C   1 
ATOM   389  O  O   . ARG A 1 50  ? -12.000 -24.961 -4.833  1.00 33.01  ? 50   ARG A O   1 
ATOM   390  C  CB  . ARG A 1 50  ? -12.424 -26.545 -7.334  1.00 38.23  ? 50   ARG A CB  1 
ATOM   391  C  CG  . ARG A 1 50  ? -13.139 -27.593 -8.169  1.00 34.99  ? 50   ARG A CG  1 
ATOM   392  C  CD  . ARG A 1 50  ? -14.426 -27.066 -8.770  1.00 36.36  ? 50   ARG A CD  1 
ATOM   393  N  NE  . ARG A 1 50  ? -15.193 -28.138 -9.396  1.00 36.56  ? 50   ARG A NE  1 
ATOM   394  C  CZ  . ARG A 1 50  ? -16.172 -28.807 -8.802  1.00 38.23  ? 50   ARG A CZ  1 
ATOM   395  N  NH1 . ARG A 1 50  ? -16.577 -28.500 -7.575  1.00 36.02  ? 50   ARG A NH1 1 
ATOM   396  N  NH2 . ARG A 1 50  ? -16.758 -29.815 -9.451  1.00 35.02  ? 50   ARG A NH2 1 
ATOM   397  N  N   . TYR A 1 51  ? -10.059 -26.107 -4.850  1.00 31.47  ? 51   TYR A N   1 
ATOM   398  C  CA  . TYR A 1 51  ? -9.332  -25.119 -4.064  1.00 32.02  ? 51   TYR A CA  1 
ATOM   399  C  C   . TYR A 1 51  ? -8.754  -24.061 -4.997  1.00 34.81  ? 51   TYR A C   1 
ATOM   400  O  O   . TYR A 1 51  ? -7.986  -24.381 -5.914  1.00 32.60  ? 51   TYR A O   1 
ATOM   401  C  CB  . TYR A 1 51  ? -8.227  -25.783 -3.248  1.00 32.80  ? 51   TYR A CB  1 
ATOM   402  C  CG  . TYR A 1 51  ? -8.776  -26.478 -2.025  1.00 32.21  ? 51   TYR A CG  1 
ATOM   403  C  CD1 . TYR A 1 51  ? -9.298  -27.765 -2.112  1.00 31.15  ? 51   TYR A CD1 1 
ATOM   404  C  CD2 . TYR A 1 51  ? -8.816  -25.831 -0.801  1.00 31.03  ? 51   TYR A CD2 1 
ATOM   405  C  CE1 . TYR A 1 51  ? -9.823  -28.406 -0.976  1.00 31.50  ? 51   TYR A CE1 1 
ATOM   406  C  CE2 . TYR A 1 51  ? -9.342  -26.452 0.327   1.00 30.46  ? 51   TYR A CE2 1 
ATOM   407  C  CZ  . TYR A 1 51  ? -9.840  -27.728 0.235   1.00 35.37  ? 51   TYR A CZ  1 
ATOM   408  O  OH  . TYR A 1 51  ? -10.358 -28.324 1.364   1.00 32.28  ? 51   TYR A OH  1 
ATOM   409  N  N   . LEU A 1 52  ? -9.118  -22.805 -4.760  1.00 31.35  ? 52   LEU A N   1 
ATOM   410  C  CA  . LEU A 1 52  ? -8.632  -21.678 -5.544  1.00 31.36  ? 52   LEU A CA  1 
ATOM   411  C  C   . LEU A 1 52  ? -7.585  -20.905 -4.758  1.00 30.26  ? 52   LEU A C   1 
ATOM   412  O  O   . LEU A 1 52  ? -7.755  -20.646 -3.562  1.00 30.29  ? 52   LEU A O   1 
ATOM   413  C  CB  . LEU A 1 52  ? -9.778  -20.736 -5.916  1.00 31.29  ? 52   LEU A CB  1 
ATOM   414  C  CG  . LEU A 1 52  ? -10.938 -21.315 -6.697  1.00 32.21  ? 52   LEU A CG  1 
ATOM   415  C  CD1 . LEU A 1 52  ? -11.876 -20.168 -7.066  1.00 34.58  ? 52   LEU A CD1 1 
ATOM   416  C  CD2 . LEU A 1 52  ? -10.420 -22.024 -7.947  1.00 34.44  ? 52   LEU A CD2 1 
ATOM   417  N  N   . SER A 1 53  ? -6.503  -20.526 -5.442  1.00 30.59  ? 53   SER A N   1 
ATOM   418  C  CA  . SER A 1 53  ? -5.399  -19.838 -4.809  1.00 31.92  ? 53   SER A CA  1 
ATOM   419  C  C   . SER A 1 53  ? -4.953  -18.575 -5.529  1.00 29.77  ? 53   SER A C   1 
ATOM   420  O  O   . SER A 1 53  ? -4.097  -17.870 -4.994  1.00 32.38  ? 53   SER A O   1 
ATOM   421  C  CB  . SER A 1 53  ? -4.187  -20.786 -4.692  1.00 33.71  ? 53   SER A CB  1 
ATOM   422  O  OG  . SER A 1 53  ? -4.424  -21.741 -3.678  1.00 38.80  ? 53   SER A OG  1 
ATOM   423  N  N   . SER A 1 54  ? -5.466  -18.285 -6.730  1.00 29.85  ? 54   SER A N   1 
ATOM   424  C  CA  . SER A 1 54  ? -5.007  -17.105 -7.448  1.00 31.29  ? 54   SER A CA  1 
ATOM   425  C  C   . SER A 1 54  ? -6.065  -16.007 -7.414  1.00 31.26  ? 54   SER A C   1 
ATOM   426  O  O   . SER A 1 54  ? -7.270  -16.275 -7.431  1.00 32.55  ? 54   SER A O   1 
ATOM   427  C  CB  . SER A 1 54  ? -4.666  -17.422 -8.915  1.00 31.89  ? 54   SER A CB  1 
ATOM   428  O  OG  . SER A 1 54  ? -5.826  -17.834 -9.607  1.00 31.55  ? 54   SER A OG  1 
ATOM   429  N  N   . GLN A 1 55  ? -5.591  -14.760 -7.398  1.00 32.27  ? 55   GLN A N   1 
ATOM   430  C  CA  . GLN A 1 55  ? -6.500  -13.631 -7.545  1.00 33.83  ? 55   GLN A CA  1 
ATOM   431  C  C   . GLN A 1 55  ? -7.232  -13.684 -8.882  1.00 33.20  ? 55   GLN A C   1 
ATOM   432  O  O   . GLN A 1 55  ? -8.407  -13.305 -8.967  1.00 31.47  ? 55   GLN A O   1 
ATOM   433  C  CB  . GLN A 1 55  ? -5.718  -12.325 -7.375  1.00 31.35  ? 55   GLN A CB  1 
ATOM   434  C  CG  . GLN A 1 55  ? -6.579  -11.078 -7.412  1.00 31.98  ? 55   GLN A CG  1 
ATOM   435  C  CD  . GLN A 1 55  ? -6.694  -10.519 -8.807  1.00 34.41  ? 55   GLN A CD  1 
ATOM   436  O  OE1 . GLN A 1 55  ? -6.069  -11.018 -9.751  1.00 33.61  ? 55   GLN A OE1 1 
ATOM   437  N  NE2 . GLN A 1 55  ? -7.499  -9.483  -8.958  1.00 34.06  ? 55   GLN A NE2 1 
ATOM   438  N  N   . ARG A 1 56  ? -6.573  -14.199 -9.925  1.00 32.23  ? 56   ARG A N   1 
ATOM   439  C  CA  . ARG A 1 56  ? -7.206  -14.309 -11.238 1.00 33.83  ? 56   ARG A CA  1 
ATOM   440  C  C   . ARG A 1 56  ? -8.547  -15.026 -11.151 1.00 33.53  ? 56   ARG A C   1 
ATOM   441  O  O   . ARG A 1 56  ? -9.539  -14.594 -11.752 1.00 33.40  ? 56   ARG A O   1 
ATOM   442  C  CB  . ARG A 1 56  ? -6.261  -15.031 -12.209 1.00 35.68  ? 56   ARG A CB  1 
ATOM   443  C  CG  . ARG A 1 56  ? -6.818  -15.217 -13.624 1.00 44.05  ? 56   ARG A CG  1 
ATOM   444  C  CD  . ARG A 1 56  ? -5.847  -16.022 -14.507 1.00 42.05  ? 56   ARG A CD  1 
ATOM   445  N  NE  . ARG A 1 56  ? -6.064  -17.464 -14.417 1.00 42.57  ? 56   ARG A NE  1 
ATOM   446  C  CZ  . ARG A 1 56  ? -6.864  -18.163 -15.213 1.00 44.37  ? 56   ARG A CZ  1 
ATOM   447  N  NH1 . ARG A 1 56  ? -7.590  -17.579 -16.155 1.00 42.42  ? 56   ARG A NH1 1 
ATOM   448  N  NH2 . ARG A 1 56  ? -6.933  -19.484 -15.067 1.00 43.46  ? 56   ARG A NH2 1 
ATOM   449  N  N   . LEU A 1 57  ? -8.591  -16.143 -10.418 1.00 30.75  ? 57   LEU A N   1 
ATOM   450  C  CA  . LEU A 1 57  ? -9.813  -16.926 -10.338 1.00 32.34  ? 57   LEU A CA  1 
ATOM   451  C  C   . LEU A 1 57  ? -10.692 -16.481 -9.177  1.00 29.71  ? 57   LEU A C   1 
ATOM   452  O  O   . LEU A 1 57  ? -11.924 -16.490 -9.297  1.00 32.00  ? 57   LEU A O   1 
ATOM   453  C  CB  . LEU A 1 57  ? -9.487  -18.416 -10.199 1.00 32.93  ? 57   LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 57  ? -8.767  -19.024 -11.416 1.00 33.13  ? 57   LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 57  ? -8.373  -20.469 -11.129 1.00 34.45  ? 57   LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 57  ? -9.643  -18.940 -12.653 1.00 34.08  ? 57   LEU A CD2 1 
ATOM   457  N  N   . ILE A 1 58  ? -10.084 -16.076 -8.066  1.00 31.20  ? 58   ILE A N   1 
ATOM   458  C  CA  . ILE A 1 58  ? -10.880 -15.702 -6.902  1.00 30.95  ? 58   ILE A CA  1 
ATOM   459  C  C   . ILE A 1 58  ? -11.685 -14.427 -7.172  1.00 33.65  ? 58   ILE A C   1 
ATOM   460  O  O   . ILE A 1 58  ? -12.805 -14.276 -6.667  1.00 31.55  ? 58   ILE A O   1 
ATOM   461  C  CB  . ILE A 1 58  ? -9.943  -15.612 -5.681  1.00 27.84  ? 58   ILE A CB  1 
ATOM   462  C  CG1 . ILE A 1 58  ? -9.596  -17.050 -5.241  1.00 30.12  ? 58   ILE A CG1 1 
ATOM   463  C  CG2 . ILE A 1 58  ? -10.597 -14.828 -4.527  1.00 30.47  ? 58   ILE A CG2 1 
ATOM   464  C  CD1 . ILE A 1 58  ? -8.344  -17.175 -4.345  1.00 29.58  ? 58   ILE A CD1 1 
ATOM   465  N  N   . LYS A 1 59  ? -11.184 -13.526 -8.028  1.00 30.89  ? 59   LYS A N   1 
ATOM   466  C  CA  . LYS A 1 59  ? -11.968 -12.335 -8.341  1.00 32.37  ? 59   LYS A CA  1 
ATOM   467  C  C   . LYS A 1 59  ? -13.260 -12.698 -9.059  1.00 34.21  ? 59   LYS A C   1 
ATOM   468  O  O   . LYS A 1 59  ? -14.256 -11.978 -8.926  1.00 34.48  ? 59   LYS A O   1 
ATOM   469  C  CB  . LYS A 1 59  ? -11.145 -11.325 -9.162  1.00 31.07  ? 59   LYS A CB  1 
ATOM   470  C  CG  . LYS A 1 59  ? -10.920 -11.674 -10.627 1.00 31.01  ? 59   LYS A CG  1 
ATOM   471  C  CD  . LYS A 1 59  ? -9.851  -10.763 -11.261 1.00 32.53  ? 59   LYS A CD  1 
ATOM   472  C  CE  . LYS A 1 59  ? -9.483  -11.207 -12.668 1.00 38.60  ? 59   LYS A CE  1 
ATOM   473  N  NZ  . LYS A 1 59  ? -8.389  -10.341 -13.236 1.00 41.47  ? 59   LYS A NZ  1 
ATOM   474  N  N   . GLU A 1 60  ? -13.273 -13.802 -9.814  1.00 30.92  ? 60   GLU A N   1 
ATOM   475  C  CA  . GLU A 1 60  ? -14.527 -14.270 -10.401 1.00 31.03  ? 60   GLU A CA  1 
ATOM   476  C  C   . GLU A 1 60  ? -15.386 -14.980 -9.364  1.00 32.69  ? 60   GLU A C   1 
ATOM   477  O  O   . GLU A 1 60  ? -16.611 -14.812 -9.345  1.00 33.02  ? 60   GLU A O   1 
ATOM   478  C  CB  . GLU A 1 60  ? -14.259 -15.195 -11.601 1.00 33.29  ? 60   GLU A CB  1 
ATOM   479  C  CG  . GLU A 1 60  ? -13.464 -14.534 -12.708 1.00 32.77  ? 60   GLU A CG  1 
ATOM   480  C  CD  . GLU A 1 60  ? -13.488 -15.319 -14.008 1.00 36.84  ? 60   GLU A CD  1 
ATOM   481  O  OE1 . GLU A 1 60  ? -14.434 -16.095 -14.226 1.00 36.87  ? 60   GLU A OE1 1 
ATOM   482  O  OE2 . GLU A 1 60  ? -12.566 -15.136 -14.825 1.00 41.27  ? 60   GLU A OE2 1 
ATOM   483  N  N   . ALA A 1 61  ? -14.763 -15.763 -8.479  1.00 32.08  ? 61   ALA A N   1 
ATOM   484  C  CA  . ALA A 1 61  ? -15.534 -16.454 -7.457  1.00 29.98  ? 61   ALA A CA  1 
ATOM   485  C  C   . ALA A 1 61  ? -16.255 -15.465 -6.547  1.00 32.36  ? 61   ALA A C   1 
ATOM   486  O  O   . ALA A 1 61  ? -17.293 -15.803 -5.969  1.00 32.37  ? 61   ALA A O   1 
ATOM   487  C  CB  . ALA A 1 61  ? -14.626 -17.364 -6.621  1.00 30.83  ? 61   ALA A CB  1 
ATOM   488  N  N   . CYS A 1 62  ? -15.729 -14.245 -6.409  1.00 28.93  ? 62   CYS A N   1 
ATOM   489  C  CA  . CYS A 1 62  ? -16.351 -13.248 -5.544  1.00 29.51  ? 62   CYS A CA  1 
ATOM   490  C  C   . CYS A 1 62  ? -17.505 -12.503 -6.205  1.00 33.25  ? 62   CYS A C   1 
ATOM   491  O  O   . CYS A 1 62  ? -18.047 -11.576 -5.594  1.00 30.83  ? 62   CYS A O   1 
ATOM   492  C  CB  . CYS A 1 62  ? -15.300 -12.255 -5.057  1.00 31.61  ? 62   CYS A CB  1 
ATOM   493  S  SG  . CYS A 1 62  ? -14.177 -12.984 -3.844  1.00 31.30  ? 62   CYS A SG  1 
ATOM   494  N  N   . ASP A 1 63  ? -17.880 -12.873 -7.425  1.00 32.76  ? 63   ASP A N   1 
ATOM   495  C  CA  . ASP A 1 63  ? -19.051 -12.318 -8.099  1.00 29.56  ? 63   ASP A CA  1 
ATOM   496  C  C   . ASP A 1 63  ? -20.306 -12.917 -7.486  1.00 31.30  ? 63   ASP A C   1 
ATOM   497  O  O   . ASP A 1 63  ? -20.632 -14.078 -7.745  1.00 33.22  ? 63   ASP A O   1 
ATOM   498  C  CB  . ASP A 1 63  ? -18.969 -12.626 -9.591  1.00 31.85  ? 63   ASP A CB  1 
ATOM   499  C  CG  . ASP A 1 63  ? -20.132 -12.052 -10.388 1.00 36.70  ? 63   ASP A CG  1 
ATOM   500  O  OD1 . ASP A 1 63  ? -21.158 -11.647 -9.802  1.00 33.64  ? 63   ASP A OD1 1 
ATOM   501  O  OD2 . ASP A 1 63  ? -20.009 -12.034 -11.629 1.00 38.56  ? 63   ASP A OD2 1 
ATOM   502  N  N   . GLU A 1 64  ? -21.027 -12.119 -6.688  1.00 30.10  ? 64   GLU A N   1 
ATOM   503  C  CA  . GLU A 1 64  ? -22.186 -12.631 -5.961  1.00 30.44  ? 64   GLU A CA  1 
ATOM   504  C  C   . GLU A 1 64  ? -23.344 -12.991 -6.880  1.00 33.73  ? 64   GLU A C   1 
ATOM   505  O  O   . GLU A 1 64  ? -24.255 -13.726 -6.467  1.00 33.79  ? 64   GLU A O   1 
ATOM   506  C  CB  . GLU A 1 64  ? -22.670 -11.599 -4.939  1.00 30.64  ? 64   GLU A CB  1 
ATOM   507  C  CG  . GLU A 1 64  ? -21.658 -11.257 -3.878  1.00 30.77  ? 64   GLU A CG  1 
ATOM   508  C  CD  . GLU A 1 64  ? -22.198 -10.269 -2.861  1.00 36.38  ? 64   GLU A CD  1 
ATOM   509  O  OE1 . GLU A 1 64  ? -22.095 -9.039  -3.089  1.00 39.97  ? 64   GLU A OE1 1 
ATOM   510  O  OE2 . GLU A 1 64  ? -22.711 -10.723 -1.828  1.00 32.02  ? 64   GLU A OE2 1 
ATOM   511  N  N   . SER A 1 65  ? -23.355 -12.472 -8.103  1.00 33.27  ? 65   SER A N   1 
ATOM   512  C  CA  . SER A 1 65  ? -24.370 -12.926 -9.036  1.00 33.34  ? 65   SER A CA  1 
ATOM   513  C  C   . SER A 1 65  ? -24.101 -14.344 -9.520  1.00 33.28  ? 65   SER A C   1 
ATOM   514  O  O   . SER A 1 65  ? -25.025 -15.005 -9.999  1.00 35.60  ? 65   SER A O   1 
ATOM   515  C  CB  . SER A 1 65  ? -24.468 -11.948 -10.220 1.00 36.74  ? 65   SER A CB  1 
ATOM   516  O  OG  . SER A 1 65  ? -23.418 -12.172 -11.145 1.00 35.01  ? 65   SER A OG  1 
ATOM   517  N  N   . ARG A 1 66  ? -22.870 -14.839 -9.388  1.00 32.29  ? 66   ARG A N   1 
ATOM   518  C  CA  . ARG A 1 66  ? -22.522 -16.171 -9.860  1.00 33.76  ? 66   ARG A CA  1 
ATOM   519  C  C   . ARG A 1 66  ? -22.302 -17.179 -8.744  1.00 34.91  ? 66   ARG A C   1 
ATOM   520  O  O   . ARG A 1 66  ? -22.536 -18.367 -8.961  1.00 34.21  ? 66   ARG A O   1 
ATOM   521  C  CB  . ARG A 1 66  ? -21.254 -16.124 -10.728 1.00 35.58  ? 66   ARG A CB  1 
ATOM   522  C  CG  . ARG A 1 66  ? -21.395 -15.315 -12.017 1.00 38.40  ? 66   ARG A CG  1 
ATOM   523  C  CD  . ARG A 1 66  ? -20.018 -14.914 -12.574 1.00 40.53  ? 66   ARG A CD  1 
ATOM   524  N  NE  . ARG A 1 66  ? -19.298 -16.053 -13.133 1.00 38.68  ? 66   ARG A NE  1 
ATOM   525  C  CZ  . ARG A 1 66  ? -18.019 -16.034 -13.484 1.00 38.56  ? 66   ARG A CZ  1 
ATOM   526  N  NH1 . ARG A 1 66  ? -17.273 -14.949 -13.329 1.00 39.27  ? 66   ARG A NH1 1 
ATOM   527  N  NH2 . ARG A 1 66  ? -17.471 -17.132 -14.001 1.00 41.19  ? 66   ARG A NH2 1 
ATOM   528  N  N   . PHE A 1 67  ? -21.862 -16.736 -7.567  1.00 33.26  ? 67   PHE A N   1 
ATOM   529  C  CA  . PHE A 1 67  ? -21.511 -17.628 -6.470  1.00 29.34  ? 67   PHE A CA  1 
ATOM   530  C  C   . PHE A 1 67  ? -22.058 -17.095 -5.153  1.00 28.55  ? 67   PHE A C   1 
ATOM   531  O  O   . PHE A 1 67  ? -22.000 -15.896 -4.880  1.00 29.71  ? 67   PHE A O   1 
ATOM   532  C  CB  . PHE A 1 67  ? -19.985 -17.807 -6.354  1.00 32.36  ? 67   PHE A CB  1 
ATOM   533  C  CG  . PHE A 1 67  ? -19.344 -18.368 -7.597  1.00 33.57  ? 67   PHE A CG  1 
ATOM   534  C  CD1 . PHE A 1 67  ? -19.290 -19.741 -7.803  1.00 35.48  ? 67   PHE A CD1 1 
ATOM   535  C  CD2 . PHE A 1 67  ? -18.798 -17.526 -8.542  1.00 31.65  ? 67   PHE A CD2 1 
ATOM   536  C  CE1 . PHE A 1 67  ? -18.705 -20.261 -8.945  1.00 35.73  ? 67   PHE A CE1 1 
ATOM   537  C  CE2 . PHE A 1 67  ? -18.219 -18.040 -9.701  1.00 36.54  ? 67   PHE A CE2 1 
ATOM   538  C  CZ  . PHE A 1 67  ? -18.167 -19.404 -9.896  1.00 37.19  ? 67   PHE A CZ  1 
ATOM   539  N  N   . ASP A 1 68  ? -22.567 -18.005 -4.339  1.00 29.94  ? 68   ASP A N   1 
ATOM   540  C  CA  . ASP A 1 68  ? -23.108 -17.712 -3.019  1.00 27.85  ? 68   ASP A CA  1 
ATOM   541  C  C   . ASP A 1 68  ? -22.267 -18.452 -1.984  1.00 33.32  ? 68   ASP A C   1 
ATOM   542  O  O   . ASP A 1 68  ? -21.546 -19.397 -2.314  1.00 29.38  ? 68   ASP A O   1 
ATOM   543  C  CB  . ASP A 1 68  ? -24.586 -18.145 -2.957  1.00 30.72  ? 68   ASP A CB  1 
ATOM   544  C  CG  . ASP A 1 68  ? -25.275 -17.817 -1.627  1.00 32.26  ? 68   ASP A CG  1 
ATOM   545  O  OD1 . ASP A 1 68  ? -24.903 -16.869 -0.913  1.00 31.38  ? 68   ASP A OD1 1 
ATOM   546  O  OD2 . ASP A 1 68  ? -26.239 -18.530 -1.319  1.00 31.24  ? 68   ASP A OD2 1 
ATOM   547  N  N   . LYS A 1 69  ? -22.366 -18.020 -0.727  1.00 28.60  ? 69   LYS A N   1 
ATOM   548  C  CA  . LYS A 1 69  ? -21.689 -18.724 0.356   1.00 29.29  ? 69   LYS A CA  1 
ATOM   549  C  C   . LYS A 1 69  ? -22.167 -20.169 0.466   1.00 27.82  ? 69   LYS A C   1 
ATOM   550  O  O   . LYS A 1 69  ? -23.369 -20.443 0.490   1.00 30.67  ? 69   LYS A O   1 
ATOM   551  C  CB  . LYS A 1 69  ? -21.921 -18.011 1.692   1.00 27.53  ? 69   LYS A CB  1 
ATOM   552  C  CG  . LYS A 1 69  ? -21.558 -18.886 2.896   1.00 28.93  ? 69   LYS A CG  1 
ATOM   553  C  CD  . LYS A 1 69  ? -21.162 -18.042 4.119   1.00 28.73  ? 69   LYS A CD  1 
ATOM   554  C  CE  . LYS A 1 69  ? -21.068 -18.936 5.353   1.00 28.61  ? 69   LYS A CE  1 
ATOM   555  N  NZ  . LYS A 1 69  ? -20.336 -18.280 6.470   1.00 27.50  ? 69   LYS A NZ  1 
ATOM   556  N  N   . ASN A 1 70  ? -21.214 -21.083 0.608   1.00 27.17  ? 70   ASN A N   1 
ATOM   557  C  CA  . ASN A 1 70  ? -21.447 -22.492 0.878   1.00 31.35  ? 70   ASN A CA  1 
ATOM   558  C  C   . ASN A 1 70  ? -21.020 -22.822 2.306   1.00 29.42  ? 70   ASN A C   1 
ATOM   559  O  O   . ASN A 1 70  ? -20.107 -22.202 2.853   1.00 29.95  ? 70   ASN A O   1 
ATOM   560  C  CB  . ASN A 1 70  ? -20.670 -23.355 -0.126  1.00 29.69  ? 70   ASN A CB  1 
ATOM   561  C  CG  . ASN A 1 70  ? -20.877 -24.840 0.092   1.00 31.24  ? 70   ASN A CG  1 
ATOM   562  O  OD1 . ASN A 1 70  ? -22.011 -25.313 0.108   1.00 32.82  ? 70   ASN A OD1 1 
ATOM   563  N  ND2 . ASN A 1 70  ? -19.781 -25.580 0.267   1.00 34.91  ? 70   ASN A ND2 1 
ATOM   564  N  N   . LEU A 1 71  ? -21.698 -23.783 2.932   1.00 30.45  ? 71   LEU A N   1 
ATOM   565  C  CA  . LEU A 1 71  ? -21.227 -24.309 4.213   1.00 28.88  ? 71   LEU A CA  1 
ATOM   566  C  C   . LEU A 1 71  ? -20.228 -25.413 3.904   1.00 28.98  ? 71   LEU A C   1 
ATOM   567  O  O   . LEU A 1 71  ? -20.590 -26.462 3.361   1.00 33.46  ? 71   LEU A O   1 
ATOM   568  C  CB  . LEU A 1 71  ? -22.374 -24.821 5.076   1.00 29.83  ? 71   LEU A CB  1 
ATOM   569  C  CG  . LEU A 1 71  ? -23.500 -23.834 5.410   1.00 29.44  ? 71   LEU A CG  1 
ATOM   570  C  CD1 . LEU A 1 71  ? -24.438 -24.431 6.438   1.00 29.51  ? 71   LEU A CD1 1 
ATOM   571  C  CD2 . LEU A 1 71  ? -22.991 -22.448 5.886   1.00 31.93  ? 71   LEU A CD2 1 
ATOM   572  N  N   . SER A 1 72  ? -18.959 -25.137 4.172   1.00 28.90  ? 72   SER A N   1 
ATOM   573  C  CA  . SER A 1 72  ? -17.937 -26.163 4.156   1.00 30.02  ? 72   SER A CA  1 
ATOM   574  C  C   . SER A 1 72  ? -18.303 -27.254 5.159   1.00 32.95  ? 72   SER A C   1 
ATOM   575  O  O   . SER A 1 72  ? -19.163 -27.071 6.034   1.00 31.91  ? 72   SER A O   1 
ATOM   576  C  CB  . SER A 1 72  ? -16.592 -25.543 4.517   1.00 33.58  ? 72   SER A CB  1 
ATOM   577  O  OG  . SER A 1 72  ? -16.679 -24.942 5.805   1.00 31.20  ? 72   SER A OG  1 
ATOM   578  N  N   . GLN A 1 73  ? -17.656 -28.413 5.021   1.00 31.02  ? 73   GLN A N   1 
ATOM   579  C  CA  . GLN A 1 73  ? -17.867 -29.446 6.027   1.00 32.40  ? 73   GLN A CA  1 
ATOM   580  C  C   . GLN A 1 73  ? -17.561 -28.905 7.417   1.00 31.71  ? 73   GLN A C   1 
ATOM   581  O  O   . GLN A 1 73  ? -18.266 -29.216 8.384   1.00 33.89  ? 73   GLN A O   1 
ATOM   582  C  CB  . GLN A 1 73  ? -17.009 -30.680 5.734   1.00 36.99  ? 73   GLN A CB  1 
ATOM   583  C  CG  . GLN A 1 73  ? -17.454 -31.892 6.546   1.00 40.67  ? 73   GLN A CG  1 
ATOM   584  C  CD  . GLN A 1 73  ? -18.908 -32.240 6.288   1.00 44.60  ? 73   GLN A CD  1 
ATOM   585  O  OE1 . GLN A 1 73  ? -19.329 -32.375 5.136   1.00 44.19  ? 73   GLN A OE1 1 
ATOM   586  N  NE2 . GLN A 1 73  ? -19.693 -32.344 7.354   1.00 47.42  ? 73   GLN A NE2 1 
ATOM   587  N  N   . ALA A 1 74  ? -16.521 -28.075 7.528   1.00 31.28  ? 74   ALA A N   1 
ATOM   588  C  CA  . ALA A 1 74  ? -16.161 -27.500 8.816   1.00 31.92  ? 74   ALA A CA  1 
ATOM   589  C  C   . ALA A 1 74  ? -17.310 -26.675 9.389   1.00 30.30  ? 74   ALA A C   1 
ATOM   590  O  O   . ALA A 1 74  ? -17.668 -26.829 10.563  1.00 31.68  ? 74   ALA A O   1 
ATOM   591  C  CB  . ALA A 1 74  ? -14.893 -26.655 8.670   1.00 31.83  ? 74   ALA A CB  1 
ATOM   592  N  N   . LEU A 1 75  ? -17.913 -25.801 8.572   1.00 31.98  ? 75   LEU A N   1 
ATOM   593  C  CA  . LEU A 1 75  ? -19.046 -25.014 9.067   1.00 30.32  ? 75   LEU A CA  1 
ATOM   594  C  C   . LEU A 1 75  ? -20.248 -25.893 9.369   1.00 29.84  ? 75   LEU A C   1 
ATOM   595  O  O   . LEU A 1 75  ? -21.005 -25.596 10.297  1.00 32.53  ? 75   LEU A O   1 
ATOM   596  C  CB  . LEU A 1 75  ? -19.448 -23.922 8.066   1.00 28.30  ? 75   LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 75  ? -18.438 -22.771 7.909   1.00 31.31  ? 75   LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 75  ? -18.992 -21.670 7.006   1.00 29.78  ? 75   LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 75  ? -18.037 -22.186 9.260   1.00 32.63  ? 75   LEU A CD2 1 
ATOM   600  N  N   . LYS A 1 76  ? -20.456 -26.961 8.593   1.00 30.99  ? 76   LYS A N   1 
ATOM   601  C  CA  . LYS A 1 76  ? -21.551 -27.876 8.909   1.00 32.44  ? 76   LYS A CA  1 
ATOM   602  C  C   . LYS A 1 76  ? -21.344 -28.526 10.272  1.00 33.24  ? 76   LYS A C   1 
ATOM   603  O  O   . LYS A 1 76  ? -22.305 -28.743 11.021  1.00 32.16  ? 76   LYS A O   1 
ATOM   604  C  CB  . LYS A 1 76  ? -21.680 -28.934 7.821   1.00 33.90  ? 76   LYS A CB  1 
ATOM   605  C  CG  . LYS A 1 76  ? -22.208 -28.360 6.521   1.00 33.39  ? 76   LYS A CG  1 
ATOM   606  C  CD  . LYS A 1 76  ? -22.420 -29.449 5.479   1.00 41.06  ? 76   LYS A CD  1 
ATOM   607  C  CE  . LYS A 1 76  ? -22.769 -28.829 4.135   1.00 43.15  ? 76   LYS A CE  1 
ATOM   608  N  NZ  . LYS A 1 76  ? -22.862 -29.848 3.050   1.00 50.71  ? 76   LYS A NZ  1 
ATOM   609  N  N   . PHE A 1 77  ? -20.097 -28.838 10.620  1.00 30.50  ? 77   PHE A N   1 
ATOM   610  C  CA  . PHE A 1 77  ? -19.861 -29.400 11.948  1.00 33.47  ? 77   PHE A CA  1 
ATOM   611  C  C   . PHE A 1 77  ? -20.025 -28.341 13.032  1.00 35.53  ? 77   PHE A C   1 
ATOM   612  O  O   . PHE A 1 77  ? -20.569 -28.623 14.107  1.00 36.04  ? 77   PHE A O   1 
ATOM   613  C  CB  . PHE A 1 77  ? -18.471 -30.035 12.002  1.00 37.61  ? 77   PHE A CB  1 
ATOM   614  C  CG  . PHE A 1 77  ? -18.348 -31.310 11.204  1.00 39.08  ? 77   PHE A CG  1 
ATOM   615  C  CD1 . PHE A 1 77  ? -19.451 -32.114 10.971  1.00 44.78  ? 77   PHE A CD1 1 
ATOM   616  C  CD2 . PHE A 1 77  ? -17.114 -31.709 10.701  1.00 40.20  ? 77   PHE A CD2 1 
ATOM   617  C  CE1 . PHE A 1 77  ? -19.330 -33.293 10.241  1.00 47.81  ? 77   PHE A CE1 1 
ATOM   618  C  CE2 . PHE A 1 77  ? -16.986 -32.882 9.969   1.00 45.30  ? 77   PHE A CE2 1 
ATOM   619  C  CZ  . PHE A 1 77  ? -18.095 -33.672 9.736   1.00 44.93  ? 77   PHE A CZ  1 
ATOM   620  N  N   . VAL A 1 78  ? -19.570 -27.113 12.770  1.00 32.29  ? 78   VAL A N   1 
ATOM   621  C  CA  . VAL A 1 78  ? -19.749 -26.038 13.744  1.00 30.28  ? 78   VAL A CA  1 
ATOM   622  C  C   . VAL A 1 78  ? -21.229 -25.749 13.938  1.00 30.79  ? 78   VAL A C   1 
ATOM   623  O  O   . VAL A 1 78  ? -21.658 -25.347 15.030  1.00 33.64  ? 78   VAL A O   1 
ATOM   624  C  CB  . VAL A 1 78  ? -18.974 -24.781 13.299  1.00 30.77  ? 78   VAL A CB  1 
ATOM   625  C  CG1 . VAL A 1 78  ? -19.396 -23.558 14.138  1.00 35.43  ? 78   VAL A CG1 1 
ATOM   626  C  CG2 . VAL A 1 78  ? -17.469 -25.030 13.386  1.00 33.04  ? 78   VAL A CG2 1 
ATOM   627  N  N   . ARG A 1 79  ? -22.031 -25.971 12.894  1.00 30.93  ? 79   ARG A N   1 
ATOM   628  C  CA  . ARG A 1 79  ? -23.466 -25.744 12.993  1.00 31.91  ? 79   ARG A CA  1 
ATOM   629  C  C   . ARG A 1 79  ? -24.113 -26.645 14.032  1.00 34.72  ? 79   ARG A C   1 
ATOM   630  O  O   . ARG A 1 79  ? -25.200 -26.330 14.525  1.00 33.46  ? 79   ARG A O   1 
ATOM   631  C  CB  . ARG A 1 79  ? -24.118 -25.954 11.627  1.00 33.42  ? 79   ARG A CB  1 
ATOM   632  C  CG  . ARG A 1 79  ? -25.620 -25.762 11.641  1.00 34.64  ? 79   ARG A CG  1 
ATOM   633  C  CD  . ARG A 1 79  ? -26.161 -25.441 10.249  1.00 30.55  ? 79   ARG A CD  1 
ATOM   634  N  NE  . ARG A 1 79  ? -27.625 -25.399 10.237  1.00 37.60  ? 79   ARG A NE  1 
ATOM   635  C  CZ  . ARG A 1 79  ? -28.347 -24.543 9.525   1.00 35.96  ? 79   ARG A CZ  1 
ATOM   636  N  NH1 . ARG A 1 79  ? -27.775 -23.614 8.770   1.00 33.06  ? 79   ARG A NH1 1 
ATOM   637  N  NH2 . ARG A 1 79  ? -29.678 -24.610 9.584   1.00 37.01  ? 79   ARG A NH2 1 
ATOM   638  N  N   . ASP A 1 80  ? -23.477 -27.765 14.373  1.00 34.98  ? 80   ASP A N   1 
ATOM   639  C  CA  . ASP A 1 80  ? -24.020 -28.604 15.435  1.00 35.69  ? 80   ASP A CA  1 
ATOM   640  C  C   . ASP A 1 80  ? -24.159 -27.847 16.751  1.00 36.41  ? 80   ASP A C   1 
ATOM   641  O  O   . ASP A 1 80  ? -25.018 -28.197 17.571  1.00 40.87  ? 80   ASP A O   1 
ATOM   642  C  CB  . ASP A 1 80  ? -23.157 -29.847 15.619  1.00 38.42  ? 80   ASP A CB  1 
ATOM   643  C  CG  . ASP A 1 80  ? -23.410 -30.876 14.536  1.00 40.84  ? 80   ASP A CG  1 
ATOM   644  O  OD1 . ASP A 1 80  ? -24.480 -30.811 13.897  1.00 43.96  ? 80   ASP A OD1 1 
ATOM   645  O  OD2 . ASP A 1 80  ? -22.548 -31.750 14.330  1.00 53.12  ? 80   ASP A OD2 1 
ATOM   646  N  N   . PHE A 1 81  ? -23.343 -26.813 16.989  1.00 35.68  ? 81   PHE A N   1 
ATOM   647  C  CA  . PHE A 1 81  ? -23.599 -25.975 18.149  1.00 35.00  ? 81   PHE A CA  1 
ATOM   648  C  C   . PHE A 1 81  ? -23.925 -24.522 17.825  1.00 35.70  ? 81   PHE A C   1 
ATOM   649  O  O   . PHE A 1 81  ? -24.561 -23.869 18.655  1.00 35.63  ? 81   PHE A O   1 
ATOM   650  C  CB  . PHE A 1 81  ? -22.431 -26.031 19.161  1.00 35.19  ? 81   PHE A CB  1 
ATOM   651  C  CG  . PHE A 1 81  ? -21.061 -25.846 18.564  1.00 39.54  ? 81   PHE A CG  1 
ATOM   652  C  CD1 . PHE A 1 81  ? -20.333 -26.935 18.104  1.00 38.02  ? 81   PHE A CD1 1 
ATOM   653  C  CD2 . PHE A 1 81  ? -20.468 -24.587 18.526  1.00 35.89  ? 81   PHE A CD2 1 
ATOM   654  C  CE1 . PHE A 1 81  ? -19.048 -26.763 17.575  1.00 37.88  ? 81   PHE A CE1 1 
ATOM   655  C  CE2 . PHE A 1 81  ? -19.189 -24.407 17.997  1.00 37.84  ? 81   PHE A CE2 1 
ATOM   656  C  CZ  . PHE A 1 81  ? -18.478 -25.502 17.524  1.00 38.84  ? 81   PHE A CZ  1 
ATOM   657  N  N   . ALA A 1 82  ? -23.587 -24.017 16.634  1.00 33.34  ? 82   ALA A N   1 
ATOM   658  C  CA  . ALA A 1 82  ? -23.913 -22.637 16.275  1.00 30.40  ? 82   ALA A CA  1 
ATOM   659  C  C   . ALA A 1 82  ? -25.201 -22.510 15.470  1.00 33.77  ? 82   ALA A C   1 
ATOM   660  O  O   . ALA A 1 82  ? -25.626 -21.388 15.181  1.00 31.59  ? 82   ALA A O   1 
ATOM   661  C  CB  . ALA A 1 82  ? -22.761 -22.000 15.497  1.00 30.12  ? 82   ALA A CB  1 
ATOM   662  N  N   . GLY A 1 83  ? -25.815 -23.626 15.085  1.00 32.28  ? 83   GLY A N   1 
ATOM   663  C  CA  . GLY A 1 83  ? -27.154 -23.590 14.512  1.00 32.26  ? 83   GLY A CA  1 
ATOM   664  C  C   . GLY A 1 83  ? -27.267 -22.704 13.293  1.00 32.10  ? 83   GLY A C   1 
ATOM   665  O  O   . GLY A 1 83  ? -26.382 -22.672 12.430  1.00 33.03  ? 83   GLY A O   1 
ATOM   666  N  N   . ASP A 1 84  ? -28.387 -21.989 13.189  1.00 29.63  ? 84   ASP A N   1 
ATOM   667  C  CA  . ASP A 1 84  ? -28.563 -21.023 12.107  1.00 31.22  ? 84   ASP A CA  1 
ATOM   668  C  C   . ASP A 1 84  ? -28.252 -19.610 12.579  1.00 33.35  ? 84   ASP A C   1 
ATOM   669  O  O   . ASP A 1 84  ? -28.909 -18.646 12.189  1.00 32.61  ? 84   ASP A O   1 
ATOM   670  C  CB  . ASP A 1 84  ? -29.961 -21.120 11.479  1.00 32.46  ? 84   ASP A CB  1 
ATOM   671  C  CG  . ASP A 1 84  ? -31.101 -20.891 12.474  1.00 36.45  ? 84   ASP A CG  1 
ATOM   672  O  OD1 . ASP A 1 84  ? -30.866 -20.789 13.692  1.00 34.37  ? 84   ASP A OD1 1 
ATOM   673  O  OD2 . ASP A 1 84  ? -32.261 -20.816 12.000  1.00 34.10  ? 84   ASP A OD2 1 
ATOM   674  N  N   . GLY A 1 85  ? -27.241 -19.491 13.442  1.00 31.88  ? 85   GLY A N   1 
ATOM   675  C  CA  . GLY A 1 85  ? -26.586 -18.217 13.658  1.00 29.51  ? 85   GLY A CA  1 
ATOM   676  C  C   . GLY A 1 85  ? -25.991 -17.677 12.363  1.00 30.35  ? 85   GLY A C   1 
ATOM   677  O  O   . GLY A 1 85  ? -25.982 -18.326 11.314  1.00 29.66  ? 85   GLY A O   1 
ATOM   678  N  N   . LEU A 1 86  ? -25.504 -16.436 12.438  1.00 27.52  ? 86   LEU A N   1 
ATOM   679  C  CA  . LEU A 1 86  ? -25.136 -15.726 11.215  1.00 27.92  ? 86   LEU A CA  1 
ATOM   680  C  C   . LEU A 1 86  ? -24.074 -16.471 10.417  1.00 27.99  ? 86   LEU A C   1 
ATOM   681  O  O   . LEU A 1 86  ? -24.108 -16.462 9.183   1.00 29.08  ? 86   LEU A O   1 
ATOM   682  C  CB  . LEU A 1 86  ? -24.639 -14.313 11.538  1.00 29.17  ? 86   LEU A CB  1 
ATOM   683  C  CG  . LEU A 1 86  ? -25.750 -13.271 11.726  1.00 29.41  ? 86   LEU A CG  1 
ATOM   684  C  CD1 . LEU A 1 86  ? -25.112 -11.958 12.182  1.00 36.45  ? 86   LEU A CD1 1 
ATOM   685  C  CD2 . LEU A 1 86  ? -26.530 -13.053 10.425  1.00 28.37  ? 86   LEU A CD2 1 
ATOM   686  N  N   . ALA A 1 87  ? -23.086 -17.073 11.092  1.00 29.10  ? 87   ALA A N   1 
ATOM   687  C  CA  . ALA A 1 87  ? -21.946 -17.599 10.348  1.00 29.03  ? 87   ALA A CA  1 
ATOM   688  C  C   . ALA A 1 87  ? -22.199 -18.977 9.749   1.00 29.86  ? 87   ALA A C   1 
ATOM   689  O  O   . ALA A 1 87  ? -21.504 -19.364 8.806   1.00 29.01  ? 87   ALA A O   1 
ATOM   690  C  CB  . ALA A 1 87  ? -20.697 -17.666 11.238  1.00 27.19  ? 87   ALA A CB  1 
ATOM   691  N  N   . THR A 1 88  ? -23.180 -19.716 10.253  1.00 29.29  ? 88   THR A N   1 
ATOM   692  C  CA  . THR A 1 88  ? -23.410 -21.083 9.814   1.00 31.67  ? 88   THR A CA  1 
ATOM   693  C  C   . THR A 1 88  ? -24.771 -21.249 9.144   1.00 31.87  ? 88   THR A C   1 
ATOM   694  O  O   . THR A 1 88  ? -25.206 -22.387 8.910   1.00 32.01  ? 88   THR A O   1 
ATOM   695  C  CB  . THR A 1 88  ? -23.265 -22.053 10.995  1.00 29.98  ? 88   THR A CB  1 
ATOM   696  O  OG1 . THR A 1 88  ? -23.974 -21.557 12.139  1.00 32.01  ? 88   THR A OG1 1 
ATOM   697  C  CG2 . THR A 1 88  ? -21.798 -22.245 11.350  1.00 29.84  ? 88   THR A CG2 1 
ATOM   698  N  N   . SER A 1 89  ? -25.439 -20.157 8.808   1.00 29.71  ? 89   SER A N   1 
ATOM   699  C  CA  . SER A 1 89  ? -26.691 -20.217 8.069   1.00 29.45  ? 89   SER A CA  1 
ATOM   700  C  C   . SER A 1 89  ? -26.440 -20.037 6.570   1.00 31.48  ? 89   SER A C   1 
ATOM   701  O  O   . SER A 1 89  ? -25.472 -19.396 6.151   1.00 29.35  ? 89   SER A O   1 
ATOM   702  C  CB  . SER A 1 89  ? -27.675 -19.159 8.581   1.00 34.66  ? 89   SER A CB  1 
ATOM   703  O  OG  . SER A 1 89  ? -27.069 -17.884 8.627   1.00 38.18  ? 89   SER A OG  1 
ATOM   704  N  N   . TRP A 1 90  ? -27.306 -20.640 5.760   1.00 31.87  ? 90   TRP A N   1 
ATOM   705  C  CA  . TRP A 1 90  ? -27.301 -20.362 4.329   1.00 30.77  ? 90   TRP A CA  1 
ATOM   706  C  C   . TRP A 1 90  ? -27.937 -18.998 4.061   1.00 30.42  ? 90   TRP A C   1 
ATOM   707  O  O   . TRP A 1 90  ? -28.821 -18.550 4.792   1.00 31.16  ? 90   TRP A O   1 
ATOM   708  C  CB  . TRP A 1 90  ? -28.076 -21.435 3.554   1.00 32.66  ? 90   TRP A CB  1 
ATOM   709  C  CG  . TRP A 1 90  ? -27.567 -22.830 3.766   1.00 31.04  ? 90   TRP A CG  1 
ATOM   710  C  CD1 . TRP A 1 90  ? -27.964 -23.701 4.740   1.00 31.63  ? 90   TRP A CD1 1 
ATOM   711  C  CD2 . TRP A 1 90  ? -26.583 -23.518 2.990   1.00 32.11  ? 90   TRP A CD2 1 
ATOM   712  N  NE1 . TRP A 1 90  ? -27.289 -24.889 4.619   1.00 30.82  ? 90   TRP A NE1 1 
ATOM   713  C  CE2 . TRP A 1 90  ? -26.432 -24.807 3.553   1.00 30.51  ? 90   TRP A CE2 1 
ATOM   714  C  CE3 . TRP A 1 90  ? -25.814 -23.172 1.880   1.00 29.86  ? 90   TRP A CE3 1 
ATOM   715  C  CZ2 . TRP A 1 90  ? -25.535 -25.755 3.039   1.00 33.68  ? 90   TRP A CZ2 1 
ATOM   716  C  CZ3 . TRP A 1 90  ? -24.915 -24.116 1.362   1.00 33.29  ? 90   TRP A CZ3 1 
ATOM   717  C  CH2 . TRP A 1 90  ? -24.787 -25.393 1.945   1.00 33.90  ? 90   TRP A CH2 1 
ATOM   718  N  N   . THR A 1 91  ? -27.497 -18.350 2.979   1.00 31.02  ? 91   THR A N   1 
ATOM   719  C  CA  . THR A 1 91  ? -28.010 -17.018 2.662   1.00 28.74  ? 91   THR A CA  1 
ATOM   720  C  C   . THR A 1 91  ? -29.516 -17.033 2.459   1.00 30.75  ? 91   THR A C   1 
ATOM   721  O  O   . THR A 1 91  ? -30.186 -16.024 2.711   1.00 31.43  ? 91   THR A O   1 
ATOM   722  C  CB  . THR A 1 91  ? -27.303 -16.481 1.415   1.00 28.81  ? 91   THR A CB  1 
ATOM   723  O  OG1 . THR A 1 91  ? -25.895 -16.576 1.609   1.00 29.31  ? 91   THR A OG1 1 
ATOM   724  C  CG2 . THR A 1 91  ? -27.682 -15.022 1.117   1.00 31.65  ? 91   THR A CG2 1 
ATOM   725  N  N   . HIS A 1 92  ? -30.058 -18.155 1.994   1.00 31.00  ? 92   HIS A N   1 
ATOM   726  C  CA  . HIS A 1 92  ? -31.484 -18.276 1.708   1.00 30.76  ? 92   HIS A CA  1 
ATOM   727  C  C   . HIS A 1 92  ? -32.312 -18.722 2.906   1.00 33.10  ? 92   HIS A C   1 
ATOM   728  O  O   . HIS A 1 92  ? -33.545 -18.771 2.800   1.00 31.93  ? 92   HIS A O   1 
ATOM   729  C  CB  . HIS A 1 92  ? -31.700 -19.246 0.540   1.00 33.35  ? 92   HIS A CB  1 
ATOM   730  C  CG  . HIS A 1 92  ? -30.984 -20.553 0.696   1.00 33.77  ? 92   HIS A CG  1 
ATOM   731  N  ND1 . HIS A 1 92  ? -31.421 -21.548 1.549   1.00 32.71  ? 92   HIS A ND1 1 
ATOM   732  C  CD2 . HIS A 1 92  ? -29.864 -21.028 0.104   1.00 33.02  ? 92   HIS A CD2 1 
ATOM   733  C  CE1 . HIS A 1 92  ? -30.601 -22.583 1.466   1.00 31.35  ? 92   HIS A CE1 1 
ATOM   734  N  NE2 . HIS A 1 92  ? -29.651 -22.293 0.600   1.00 33.60  ? 92   HIS A NE2 1 
ATOM   735  N  N   . GLU A 1 93  ? -31.696 -19.039 4.040   1.00 31.31  ? 93   GLU A N   1 
ATOM   736  C  CA  . GLU A 1 93  ? -32.498 -19.310 5.224   1.00 30.59  ? 93   GLU A CA  1 
ATOM   737  C  C   . GLU A 1 93  ? -33.045 -18.006 5.772   1.00 31.75  ? 93   GLU A C   1 
ATOM   738  O  O   . GLU A 1 93  ? -32.326 -17.006 5.861   1.00 32.27  ? 93   GLU A O   1 
ATOM   739  C  CB  . GLU A 1 93  ? -31.678 -20.014 6.304   1.00 33.31  ? 93   GLU A CB  1 
ATOM   740  C  CG  . GLU A 1 93  ? -31.403 -21.497 6.029   1.00 31.76  ? 93   GLU A CG  1 
ATOM   741  C  CD  . GLU A 1 93  ? -30.552 -22.119 7.116   1.00 38.38  ? 93   GLU A CD  1 
ATOM   742  O  OE1 . GLU A 1 93  ? -29.324 -21.868 7.114   1.00 33.45  ? 93   GLU A OE1 1 
ATOM   743  O  OE2 . GLU A 1 93  ? -31.106 -22.863 7.969   1.00 35.93  ? 93   GLU A OE2 1 
ATOM   744  N  N   . LYS A 1 94  ? -34.328 -18.016 6.148   1.00 32.58  ? 94   LYS A N   1 
ATOM   745  C  CA  . LYS A 1 94  ? -34.958 -16.789 6.615   1.00 31.98  ? 94   LYS A CA  1 
ATOM   746  C  C   . LYS A 1 94  ? -34.132 -16.130 7.713   1.00 30.67  ? 94   LYS A C   1 
ATOM   747  O  O   . LYS A 1 94  ? -33.976 -14.904 7.730   1.00 33.52  ? 94   LYS A O   1 
ATOM   748  C  CB  . LYS A 1 94  ? -36.380 -17.091 7.102   1.00 37.56  ? 94   LYS A CB  1 
ATOM   749  C  CG  . LYS A 1 94  ? -37.075 -15.937 7.806   1.00 36.20  ? 94   LYS A CG  1 
ATOM   750  C  CD  . LYS A 1 94  ? -38.489 -16.351 8.211   1.00 38.65  ? 94   LYS A CD  1 
ATOM   751  C  CE  . LYS A 1 94  ? -39.157 -15.298 9.052   1.00 41.63  ? 94   LYS A CE  1 
ATOM   752  N  NZ  . LYS A 1 94  ? -40.493 -15.785 9.499   1.00 49.79  ? 94   LYS A NZ  1 
ATOM   753  N  N   . ASN A 1 95  ? -33.553 -16.930 8.613   1.00 30.03  ? 95   ASN A N   1 
ATOM   754  C  CA  . ASN A 1 95  ? -32.892 -16.336 9.762   1.00 31.62  ? 95   ASN A CA  1 
ATOM   755  C  C   . ASN A 1 95  ? -31.567 -15.664 9.413   1.00 31.79  ? 95   ASN A C   1 
ATOM   756  O  O   . ASN A 1 95  ? -31.059 -14.912 10.255  1.00 30.72  ? 95   ASN A O   1 
ATOM   757  C  CB  . ASN A 1 95  ? -32.690 -17.387 10.861  1.00 32.04  ? 95   ASN A CB  1 
ATOM   758  C  CG  . ASN A 1 95  ? -33.885 -17.495 11.782  1.00 34.32  ? 95   ASN A CG  1 
ATOM   759  O  OD1 . ASN A 1 95  ? -34.688 -16.562 11.881  1.00 36.75  ? 95   ASN A OD1 1 
ATOM   760  N  ND2 . ASN A 1 95  ? -34.015 -18.632 12.458  1.00 33.28  ? 95   ASN A ND2 1 
ATOM   761  N  N   . TRP A 1 96  ? -31.010 -15.867 8.210   1.00 31.10  ? 96   TRP A N   1 
ATOM   762  C  CA  . TRP A 1 96  ? -29.773 -15.155 7.893   1.00 30.47  ? 96   TRP A CA  1 
ATOM   763  C  C   . TRP A 1 96  ? -30.050 -13.666 7.692   1.00 29.98  ? 96   TRP A C   1 
ATOM   764  O  O   . TRP A 1 96  ? -29.542 -12.824 8.443   1.00 31.93  ? 96   TRP A O   1 
ATOM   765  C  CB  . TRP A 1 96  ? -29.025 -15.742 6.677   1.00 29.24  ? 96   TRP A CB  1 
ATOM   766  C  CG  . TRP A 1 96  ? -27.842 -14.829 6.475   1.00 29.72  ? 96   TRP A CG  1 
ATOM   767  C  CD1 . TRP A 1 96  ? -26.749 -14.732 7.297   1.00 29.59  ? 96   TRP A CD1 1 
ATOM   768  C  CD2 . TRP A 1 96  ? -27.735 -13.751 5.541   1.00 30.86  ? 96   TRP A CD2 1 
ATOM   769  N  NE1 . TRP A 1 96  ? -25.947 -13.691 6.894   1.00 29.46  ? 96   TRP A NE1 1 
ATOM   770  C  CE2 . TRP A 1 96  ? -26.522 -13.076 5.816   1.00 29.57  ? 96   TRP A CE2 1 
ATOM   771  C  CE3 . TRP A 1 96  ? -28.524 -13.310 4.471   1.00 30.75  ? 96   TRP A CE3 1 
ATOM   772  C  CZ2 . TRP A 1 96  ? -26.079 -11.986 5.057   1.00 35.06  ? 96   TRP A CZ2 1 
ATOM   773  C  CZ3 . TRP A 1 96  ? -28.085 -12.207 3.724   1.00 31.79  ? 96   TRP A CZ3 1 
ATOM   774  C  CH2 . TRP A 1 96  ? -26.866 -11.570 4.018   1.00 33.71  ? 96   TRP A CH2 1 
ATOM   775  N  N   . LYS A 1 97  ? -30.880 -13.313 6.701   1.00 30.94  ? 97   LYS A N   1 
ATOM   776  C  CA  . LYS A 1 97  ? -31.081 -11.893 6.440   1.00 31.98  ? 97   LYS A CA  1 
ATOM   777  C  C   . LYS A 1 97  ? -31.796 -11.227 7.611   1.00 32.08  ? 97   LYS A C   1 
ATOM   778  O  O   . LYS A 1 97  ? -31.552 -10.051 7.904   1.00 31.07  ? 97   LYS A O   1 
ATOM   779  C  CB  . LYS A 1 97  ? -31.870 -11.696 5.140   1.00 33.66  ? 97   LYS A CB  1 
ATOM   780  C  CG  . LYS A 1 97  ? -32.067 -10.226 4.732   1.00 35.93  ? 97   LYS A CG  1 
ATOM   781  C  CD  . LYS A 1 97  ? -30.743 -9.474  4.642   1.00 38.98  ? 97   LYS A CD  1 
ATOM   782  C  CE  . LYS A 1 97  ? -30.906 -8.176  3.870   1.00 45.12  ? 97   LYS A CE  1 
ATOM   783  N  NZ  . LYS A 1 97  ? -30.514 -8.304  2.449   1.00 55.06  ? 97   LYS A NZ  1 
ATOM   784  N  N   . LYS A 1 98  ? -32.677 -11.956 8.294   1.00 33.36  ? 98   LYS A N   1 
ATOM   785  C  CA  . LYS A 1 98  ? -33.388 -11.360 9.421   1.00 33.84  ? 98   LYS A CA  1 
ATOM   786  C  C   . LYS A 1 98  ? -32.416 -10.939 10.526  1.00 34.02  ? 98   LYS A C   1 
ATOM   787  O  O   . LYS A 1 98  ? -32.446 -9.793  10.999  1.00 32.71  ? 98   LYS A O   1 
ATOM   788  C  CB  . LYS A 1 98  ? -34.435 -12.348 9.944   1.00 38.85  ? 98   LYS A CB  1 
ATOM   789  C  CG  . LYS A 1 98  ? -35.245 -11.873 11.133  1.00 34.80  ? 98   LYS A CG  1 
ATOM   790  C  CD  . LYS A 1 98  ? -36.310 -12.955 11.453  1.00 39.13  ? 98   LYS A CD  1 
ATOM   791  C  CE  . LYS A 1 98  ? -36.872 -12.837 12.856  1.00 39.91  ? 98   LYS A CE  1 
ATOM   792  N  NZ  . LYS A 1 98  ? -37.890 -13.922 13.071  1.00 37.90  ? 98   LYS A NZ  1 
ATOM   793  N  N   . ALA A 1 99  ? -31.531 -11.854 10.940  1.00 30.66  ? 99   ALA A N   1 
ATOM   794  C  CA  . ALA A 1 99  ? -30.538 -11.520 11.962  1.00 30.60  ? 99   ALA A CA  1 
ATOM   795  C  C   . ALA A 1 99  ? -29.523 -10.519 11.437  1.00 31.21  ? 99   ALA A C   1 
ATOM   796  O  O   . ALA A 1 99  ? -29.032 -9.671  12.187  1.00 30.81  ? 99   ALA A O   1 
ATOM   797  C  CB  . ALA A 1 99  ? -29.828 -12.779 12.437  1.00 30.60  ? 99   ALA A CB  1 
ATOM   798  N  N   . HIS A 1 100 ? -29.175 -10.617 10.155  1.00 31.36  ? 100  HIS A N   1 
ATOM   799  C  CA  . HIS A 1 100 ? -28.278 -9.628  9.569   1.00 31.16  ? 100  HIS A CA  1 
ATOM   800  C  C   . HIS A 1 100 ? -28.851 -8.221  9.695   1.00 33.61  ? 100  HIS A C   1 
ATOM   801  O  O   . HIS A 1 100 ? -28.168 -7.296  10.145  1.00 31.97  ? 100  HIS A O   1 
ATOM   802  C  CB  . HIS A 1 100 ? -28.020 -9.981  8.105   1.00 31.67  ? 100  HIS A CB  1 
ATOM   803  C  CG  . HIS A 1 100 ? -27.176 -8.983  7.377   1.00 35.92  ? 100  HIS A CG  1 
ATOM   804  N  ND1 . HIS A 1 100 ? -25.799 -8.994  7.430   1.00 39.86  ? 100  HIS A ND1 1 
ATOM   805  C  CD2 . HIS A 1 100 ? -27.514 -7.964  6.550   1.00 43.94  ? 100  HIS A CD2 1 
ATOM   806  C  CE1 . HIS A 1 100 ? -25.324 -8.016  6.679   1.00 45.92  ? 100  HIS A CE1 1 
ATOM   807  N  NE2 . HIS A 1 100 ? -26.343 -7.375  6.135   1.00 50.79  ? 100  HIS A NE2 1 
ATOM   808  N  N   . ASN A 1 101 ? -30.114 -8.039  9.297   1.00 32.66  ? 101  ASN A N   1 
ATOM   809  C  CA  . ASN A 1 101 ? -30.724 -6.719  9.387   1.00 31.82  ? 101  ASN A CA  1 
ATOM   810  C  C   . ASN A 1 101 ? -30.796 -6.244  10.831  1.00 31.40  ? 101  ASN A C   1 
ATOM   811  O  O   . ASN A 1 101 ? -30.605 -5.055  11.113  1.00 34.92  ? 101  ASN A O   1 
ATOM   812  C  CB  . ASN A 1 101 ? -32.132 -6.751  8.787   1.00 32.09  ? 101  ASN A CB  1 
ATOM   813  C  CG  . ASN A 1 101 ? -32.122 -6.838  7.275   1.00 33.47  ? 101  ASN A CG  1 
ATOM   814  O  OD1 . ASN A 1 101 ? -31.126 -6.528  6.628   1.00 35.50  ? 101  ASN A OD1 1 
ATOM   815  N  ND2 . ASN A 1 101 ? -33.250 -7.265  6.700   1.00 36.00  ? 101  ASN A ND2 1 
ATOM   816  N  N   . ILE A 1 102 ? -31.107 -7.155  11.757  1.00 32.18  ? 102  ILE A N   1 
ATOM   817  C  CA  . ILE A 1 102 ? -31.277 -6.775  13.153  1.00 34.22  ? 102  ILE A CA  1 
ATOM   818  C  C   . ILE A 1 102 ? -29.937 -6.430  13.788  1.00 34.46  ? 102  ILE A C   1 
ATOM   819  O  O   . ILE A 1 102 ? -29.845 -5.507  14.604  1.00 32.54  ? 102  ILE A O   1 
ATOM   820  C  CB  . ILE A 1 102 ? -31.994 -7.901  13.919  1.00 32.41  ? 102  ILE A CB  1 
ATOM   821  C  CG1 . ILE A 1 102 ? -33.468 -7.978  13.500  1.00 35.17  ? 102  ILE A CG1 1 
ATOM   822  C  CG2 . ILE A 1 102 ? -31.832 -7.737  15.427  1.00 37.53  ? 102  ILE A CG2 1 
ATOM   823  C  CD1 . ILE A 1 102 ? -34.146 -9.266  13.940  1.00 32.45  ? 102  ILE A CD1 1 
ATOM   824  N  N   . LEU A 1 103 ? -28.873 -7.144  13.410  1.00 30.58  ? 103  LEU A N   1 
ATOM   825  C  CA  . LEU A 1 103 ? -27.593 -6.996  14.105  1.00 32.34  ? 103  LEU A CA  1 
ATOM   826  C  C   . LEU A 1 103 ? -26.609 -6.052  13.416  1.00 32.75  ? 103  LEU A C   1 
ATOM   827  O  O   . LEU A 1 103 ? -25.671 -5.574  14.072  1.00 31.72  ? 103  LEU A O   1 
ATOM   828  C  CB  . LEU A 1 103 ? -26.947 -8.380  14.307  1.00 31.72  ? 103  LEU A CB  1 
ATOM   829  C  CG  . LEU A 1 103 ? -27.786 -9.308  15.200  1.00 31.86  ? 103  LEU A CG  1 
ATOM   830  C  CD1 . LEU A 1 103 ? -27.166 -10.704 15.335  1.00 32.44  ? 103  LEU A CD1 1 
ATOM   831  C  CD2 . LEU A 1 103 ? -28.029 -8.684  16.585  1.00 36.54  ? 103  LEU A CD2 1 
ATOM   832  N  N   . LEU A 1 104 ? -26.797 -5.731  12.140  1.00 31.69  ? 104  LEU A N   1 
ATOM   833  C  CA  . LEU A 1 104 ? -25.886 -4.787  11.487  1.00 32.22  ? 104  LEU A CA  1 
ATOM   834  C  C   . LEU A 1 104 ? -25.733 -3.467  12.249  1.00 35.48  ? 104  LEU A C   1 
ATOM   835  O  O   . LEU A 1 104 ? -24.597 -2.971  12.349  1.00 33.99  ? 104  LEU A O   1 
ATOM   836  C  CB  . LEU A 1 104 ? -26.347 -4.547  10.037  1.00 34.76  ? 104  LEU A CB  1 
ATOM   837  C  CG  . LEU A 1 104 ? -25.334 -3.979  9.040   1.00 44.64  ? 104  LEU A CG  1 
ATOM   838  C  CD1 . LEU A 1 104 ? -24.130 -4.907  8.911   1.00 40.53  ? 104  LEU A CD1 1 
ATOM   839  C  CD2 . LEU A 1 104 ? -25.987 -3.779  7.678   1.00 43.12  ? 104  LEU A CD2 1 
ATOM   840  N  N   . PRO A 1 105 ? -26.783 -2.861  12.811  1.00 32.70  ? 105  PRO A N   1 
ATOM   841  C  CA  . PRO A 1 105 ? -26.589 -1.604  13.557  1.00 37.32  ? 105  PRO A CA  1 
ATOM   842  C  C   . PRO A 1 105 ? -25.704 -1.756  14.781  1.00 34.96  ? 105  PRO A C   1 
ATOM   843  O  O   . PRO A 1 105 ? -25.138 -0.756  15.243  1.00 37.14  ? 105  PRO A O   1 
ATOM   844  C  CB  . PRO A 1 105 ? -28.017 -1.200  13.951  1.00 37.22  ? 105  PRO A CB  1 
ATOM   845  C  CG  . PRO A 1 105 ? -28.882 -1.830  12.896  1.00 37.55  ? 105  PRO A CG  1 
ATOM   846  C  CD  . PRO A 1 105 ? -28.206 -3.153  12.573  1.00 33.83  ? 105  PRO A CD  1 
ATOM   847  N  N   . SER A 1 106 ? -25.574 -2.964  15.325  1.00 31.34  ? 106  SER A N   1 
ATOM   848  C  CA  . SER A 1 106 ? -24.681 -3.191  16.459  1.00 31.99  ? 106  SER A CA  1 
ATOM   849  C  C   . SER A 1 106 ? -23.211 -3.091  16.075  1.00 35.00  ? 106  SER A C   1 
ATOM   850  O  O   . SER A 1 106 ? -22.346 -3.196  16.958  1.00 34.71  ? 106  SER A O   1 
ATOM   851  C  CB  . SER A 1 106 ? -24.953 -4.568  17.071  1.00 35.60  ? 106  SER A CB  1 
ATOM   852  O  OG  . SER A 1 106 ? -26.241 -4.595  17.655  1.00 42.03  ? 106  SER A OG  1 
ATOM   853  N  N   . PHE A 1 107 ? -22.914 -2.897  14.790  1.00 34.18  ? 107  PHE A N   1 
ATOM   854  C  CA  . PHE A 1 107 ? -21.552 -2.651  14.325  1.00 36.64  ? 107  PHE A CA  1 
ATOM   855  C  C   . PHE A 1 107 ? -21.436 -1.348  13.531  1.00 35.33  ? 107  PHE A C   1 
ATOM   856  O  O   . PHE A 1 107 ? -20.482 -1.169  12.774  1.00 44.10  ? 107  PHE A O   1 
ATOM   857  C  CB  . PHE A 1 107 ? -21.069 -3.861  13.528  1.00 37.23  ? 107  PHE A CB  1 
ATOM   858  C  CG  . PHE A 1 107 ? -21.087 -5.126  14.338  1.00 36.42  ? 107  PHE A CG  1 
ATOM   859  C  CD1 . PHE A 1 107 ? -20.041 -5.422  15.206  1.00 36.32  ? 107  PHE A CD1 1 
ATOM   860  C  CD2 . PHE A 1 107 ? -22.176 -5.970  14.305  1.00 35.12  ? 107  PHE A CD2 1 
ATOM   861  C  CE1 . PHE A 1 107 ? -20.076 -6.570  15.992  1.00 38.95  ? 107  PHE A CE1 1 
ATOM   862  C  CE2 . PHE A 1 107 ? -22.233 -7.103  15.095  1.00 34.91  ? 107  PHE A CE2 1 
ATOM   863  C  CZ  . PHE A 1 107 ? -21.165 -7.414  15.943  1.00 38.25  ? 107  PHE A CZ  1 
ATOM   864  N  N   . SER A 1 108 ? -22.349 -0.406  13.740  1.00 46.34  ? 108  SER A N   1 
ATOM   865  C  CA  . SER A 1 108 ? -22.208 0.922   13.158  1.00 40.81  ? 108  SER A CA  1 
ATOM   866  C  C   . SER A 1 108 ? -21.081 1.694   13.847  1.00 49.41  ? 108  SER A C   1 
ATOM   867  O  O   . SER A 1 108 ? -20.576 1.301   14.908  1.00 42.21  ? 108  SER A O   1 
ATOM   868  C  CB  . SER A 1 108 ? -23.501 1.707   13.300  1.00 44.78  ? 108  SER A CB  1 
ATOM   869  O  OG  . SER A 1 108 ? -23.762 1.983   14.669  1.00 49.34  ? 108  SER A OG  1 
ATOM   870  N  N   . GLN A 1 109 ? -20.692 2.823   13.239  1.00 45.68  ? 109  GLN A N   1 
ATOM   871  C  CA  . GLN A 1 109 ? -19.751 3.719   13.906  1.00 44.82  ? 109  GLN A CA  1 
ATOM   872  C  C   . GLN A 1 109 ? -20.256 4.080   15.295  1.00 45.50  ? 109  GLN A C   1 
ATOM   873  O  O   . GLN A 1 109 ? -19.508 4.031   16.280  1.00 48.11  ? 109  GLN A O   1 
ATOM   874  C  CB  . GLN A 1 109 ? -19.521 5.007   13.094  1.00 50.81  ? 109  GLN A CB  1 
ATOM   875  C  CG  . GLN A 1 109 ? -18.949 4.855   11.680  1.00 56.14  ? 109  GLN A CG  1 
ATOM   876  C  CD  . GLN A 1 109 ? -19.229 6.074   10.790  1.00 58.07  ? 109  GLN A CD  1 
ATOM   877  O  OE1 . GLN A 1 109 ? -19.858 7.042   11.221  1.00 58.38  ? 109  GLN A OE1 1 
ATOM   878  N  NE2 . GLN A 1 109 ? -18.752 6.027   9.545   1.00 57.95  ? 109  GLN A NE2 1 
ATOM   879  N  N   . GLN A 1 110 ? -21.530 4.452   15.392  1.00 44.78  ? 110  GLN A N   1 
ATOM   880  C  CA  . GLN A 1 110 ? -22.049 4.909   16.671  1.00 46.70  ? 110  GLN A CA  1 
ATOM   881  C  C   . GLN A 1 110 ? -22.052 3.787   17.698  1.00 45.31  ? 110  GLN A C   1 
ATOM   882  O  O   . GLN A 1 110 ? -21.915 4.040   18.906  1.00 43.30  ? 110  GLN A O   1 
ATOM   883  C  CB  . GLN A 1 110 ? -23.452 5.482   16.493  1.00 54.93  ? 110  GLN A CB  1 
ATOM   884  C  CG  . GLN A 1 110 ? -24.087 5.838   17.802  1.00 57.34  ? 110  GLN A CG  1 
ATOM   885  C  CD  . GLN A 1 110 ? -23.532 7.148   18.327  1.00 63.56  ? 110  GLN A CD  1 
ATOM   886  O  OE1 . GLN A 1 110 ? -23.414 7.349   19.538  1.00 70.37  ? 110  GLN A OE1 1 
ATOM   887  N  NE2 . GLN A 1 110 ? -23.152 8.037   17.409  1.00 61.40  ? 110  GLN A NE2 1 
ATOM   888  N  N   . ALA A 1 111 ? -22.235 2.547   17.239  1.00 45.17  ? 111  ALA A N   1 
ATOM   889  C  CA  . ALA A 1 111 ? -22.097 1.395   18.121  1.00 43.21  ? 111  ALA A CA  1 
ATOM   890  C  C   . ALA A 1 111 ? -20.660 1.227   18.585  1.00 36.79  ? 111  ALA A C   1 
ATOM   891  O  O   . ALA A 1 111 ? -20.420 0.894   19.748  1.00 39.79  ? 111  ALA A O   1 
ATOM   892  C  CB  . ALA A 1 111 ? -22.560 0.126   17.408  1.00 37.79  ? 111  ALA A CB  1 
ATOM   893  N  N   . MET A 1 112 ? -19.694 1.410   17.679  1.00 34.62  ? 112  MET A N   1 
ATOM   894  C  CA  . MET A 1 112 ? -18.295 1.210   18.043  1.00 36.50  ? 112  MET A CA  1 
ATOM   895  C  C   . MET A 1 112 ? -17.867 2.238   19.086  1.00 37.10  ? 112  MET A C   1 
ATOM   896  O  O   . MET A 1 112 ? -17.114 1.929   20.018  1.00 33.66  ? 112  MET A O   1 
ATOM   897  C  CB  . MET A 1 112 ? -17.412 1.317   16.804  1.00 42.41  ? 112  MET A CB  1 
ATOM   898  C  CG  . MET A 1 112 ? -17.410 0.066   15.916  1.00 47.47  ? 112  MET A CG  1 
ATOM   899  S  SD  . MET A 1 112 ? -17.011 -1.473  16.767  1.00 39.83  ? 112  MET A SD  1 
ATOM   900  C  CE  . MET A 1 112 ? -15.384 -1.118  17.367  1.00 45.06  ? 112  MET A CE  1 
ATOM   901  N  N   . LYS A 1 113 ? -18.339 3.478   18.934  1.00 36.19  ? 113  LYS A N   1 
ATOM   902  C  CA  . LYS A 1 113 ? -18.085 4.490   19.952  1.00 35.61  ? 113  LYS A CA  1 
ATOM   903  C  C   . LYS A 1 113 ? -18.646 4.074   21.303  1.00 34.28  ? 113  LYS A C   1 
ATOM   904  O  O   . LYS A 1 113 ? -18.049 4.384   22.343  1.00 39.13  ? 113  LYS A O   1 
ATOM   905  C  CB  . LYS A 1 113 ? -18.678 5.830   19.508  1.00 33.93  ? 113  LYS A CB  1 
ATOM   906  C  CG  . LYS A 1 113 ? -18.039 6.386   18.228  1.00 37.25  ? 113  LYS A CG  1 
ATOM   907  C  CD  . LYS A 1 113 ? -18.744 7.669   17.754  1.00 42.15  ? 113  LYS A CD  1 
ATOM   908  C  CE  . LYS A 1 113 ? -18.106 8.225   16.481  1.00 45.56  ? 113  LYS A CE  1 
ATOM   909  N  NZ  . LYS A 1 113 ? -19.004 9.210   15.794  1.00 47.61  ? 113  LYS A NZ  1 
ATOM   910  N  N   . GLY A 1 114 ? -19.774 3.359   21.311  1.00 32.72  ? 114  GLY A N   1 
ATOM   911  C  CA  . GLY A 1 114 ? -20.353 2.891   22.562  1.00 36.62  ? 114  GLY A CA  1 
ATOM   912  C  C   . GLY A 1 114 ? -19.619 1.723   23.196  1.00 37.52  ? 114  GLY A C   1 
ATOM   913  O  O   . GLY A 1 114 ? -19.653 1.566   24.423  1.00 39.06  ? 114  GLY A O   1 
ATOM   914  N  N   . TYR A 1 115 ? -18.962 0.881   22.382  1.00 35.63  ? 115  TYR A N   1 
ATOM   915  C  CA  . TYR A 1 115 ? -18.158 -0.225  22.896  1.00 33.76  ? 115  TYR A CA  1 
ATOM   916  C  C   . TYR A 1 115 ? -16.802 0.219   23.410  1.00 34.96  ? 115  TYR A C   1 
ATOM   917  O  O   . TYR A 1 115 ? -16.172 -0.525  24.166  1.00 32.17  ? 115  TYR A O   1 
ATOM   918  C  CB  . TYR A 1 115 ? -17.881 -1.277  21.811  1.00 30.48  ? 115  TYR A CB  1 
ATOM   919  C  CG  . TYR A 1 115 ? -19.097 -1.945  21.235  1.00 32.52  ? 115  TYR A CG  1 
ATOM   920  C  CD1 . TYR A 1 115 ? -20.093 -2.455  22.056  1.00 35.11  ? 115  TYR A CD1 1 
ATOM   921  C  CD2 . TYR A 1 115 ? -19.241 -2.081  19.852  1.00 31.91  ? 115  TYR A CD2 1 
ATOM   922  C  CE1 . TYR A 1 115 ? -21.207 -3.080  21.514  1.00 36.13  ? 115  TYR A CE1 1 
ATOM   923  C  CE2 . TYR A 1 115 ? -20.335 -2.703  19.309  1.00 34.79  ? 115  TYR A CE2 1 
ATOM   924  C  CZ  . TYR A 1 115 ? -21.316 -3.198  20.135  1.00 35.31  ? 115  TYR A CZ  1 
ATOM   925  O  OH  . TYR A 1 115 ? -22.410 -3.812  19.567  1.00 37.24  ? 115  TYR A OH  1 
ATOM   926  N  N   . HIS A 1 116 ? -16.321 1.382   22.972  1.00 33.38  ? 116  HIS A N   1 
ATOM   927  C  CA  . HIS A 1 116 ? -14.921 1.737   23.163  1.00 33.12  ? 116  HIS A CA  1 
ATOM   928  C  C   . HIS A 1 116 ? -14.507 1.674   24.634  1.00 32.33  ? 116  HIS A C   1 
ATOM   929  O  O   . HIS A 1 116 ? -13.440 1.144   24.969  1.00 33.20  ? 116  HIS A O   1 
ATOM   930  C  CB  . HIS A 1 116 ? -14.667 3.134   22.591  1.00 31.68  ? 116  HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 116 ? -13.257 3.591   22.757  1.00 34.45  ? 116  HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 116 ? -12.269 3.315   21.835  1.00 34.31  ? 116  HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 116 ? -12.659 4.281   23.758  1.00 34.67  ? 116  HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 116 ? -11.122 3.813   22.263  1.00 36.24  ? 116  HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 116 ? -11.335 4.413   23.422  1.00 33.37  ? 116  HIS A NE2 1 
ATOM   936  N  N   . ALA A 1 117 ? -15.324 2.238   25.532  1.00 33.87  ? 117  ALA A N   1 
ATOM   937  C  CA  . ALA A 1 117 ? -14.903 2.326   26.932  1.00 35.27  ? 117  ALA A CA  1 
ATOM   938  C  C   . ALA A 1 117 ? -14.690 0.944   27.534  1.00 34.18  ? 117  ALA A C   1 
ATOM   939  O  O   . ALA A 1 117 ? -13.779 0.744   28.350  1.00 33.61  ? 117  ALA A O   1 
ATOM   940  C  CB  . ALA A 1 117 ? -15.924 3.115   27.757  1.00 36.06  ? 117  ALA A CB  1 
ATOM   941  N  N   A MET A 1 118 ? -15.531 -0.021  27.150  0.60 32.52  ? 118  MET A N   1 
ATOM   942  N  N   B MET A 1 118 ? -15.522 -0.026  27.153  0.40 32.54  ? 118  MET A N   1 
ATOM   943  C  CA  A MET A 1 118 ? -15.388 -1.371  27.678  0.60 32.14  ? 118  MET A CA  1 
ATOM   944  C  CA  B MET A 1 118 ? -15.380 -1.367  27.705  0.40 32.16  ? 118  MET A CA  1 
ATOM   945  C  C   A MET A 1 118 ? -14.186 -2.077  27.058  0.60 30.82  ? 118  MET A C   1 
ATOM   946  C  C   B MET A 1 118 ? -14.284 -2.175  27.011  0.40 30.92  ? 118  MET A C   1 
ATOM   947  O  O   A MET A 1 118 ? -13.503 -2.852  27.736  0.60 30.28  ? 118  MET A O   1 
ATOM   948  O  O   B MET A 1 118 ? -13.769 -3.126  27.609  0.40 31.23  ? 118  MET A O   1 
ATOM   949  C  CB  A MET A 1 118 ? -16.674 -2.162  27.448  0.60 33.75  ? 118  MET A CB  1 
ATOM   950  C  CB  B MET A 1 118 ? -16.724 -2.097  27.652  0.40 33.71  ? 118  MET A CB  1 
ATOM   951  C  CG  A MET A 1 118 ? -17.743 -1.892  28.492  0.60 34.79  ? 118  MET A CG  1 
ATOM   952  C  CG  B MET A 1 118 ? -17.681 -1.735  28.805  0.40 34.62  ? 118  MET A CG  1 
ATOM   953  S  SD  A MET A 1 118 ? -19.348 -2.544  28.007  0.60 38.14  ? 118  MET A SD  1 
ATOM   954  S  SD  B MET A 1 118 ? -16.903 -1.534  30.431  0.40 40.47  ? 118  MET A SD  1 
ATOM   955  C  CE  A MET A 1 118 ? -20.157 -2.621  29.609  0.60 39.64  ? 118  MET A CE  1 
ATOM   956  C  CE  B MET A 1 118 ? -16.852 0.247   30.607  0.40 39.77  ? 118  MET A CE  1 
ATOM   957  N  N   . MET A 1 119 ? -13.883 -1.817  25.781  1.00 32.02  ? 119  MET A N   1 
ATOM   958  C  CA  . MET A 1 119 ? -12.657 -2.418  25.272  1.00 28.87  ? 119  MET A CA  1 
ATOM   959  C  C   . MET A 1 119 ? -11.455 -1.840  25.993  1.00 31.24  ? 119  MET A C   1 
ATOM   960  O  O   . MET A 1 119 ? -10.494 -2.567  26.239  1.00 31.35  ? 119  MET A O   1 
ATOM   961  C  CB  . MET A 1 119 ? -12.452 -2.385  23.739  1.00 33.53  ? 119  MET A CB  1 
ATOM   962  C  CG  . MET A 1 119 ? -13.650 -2.523  22.820  1.00 30.92  ? 119  MET A CG  1 
ATOM   963  S  SD  . MET A 1 119 ? -13.089 -2.225  21.112  1.00 33.07  ? 119  MET A SD  1 
ATOM   964  C  CE  . MET A 1 119 ? -14.290 -3.292  20.282  1.00 31.84  ? 119  MET A CE  1 
ATOM   965  N  N   . VAL A 1 120 ? -11.516 -0.569  26.398  1.00 29.95  ? 120  VAL A N   1 
ATOM   966  C  CA  . VAL A 1 120 ? -10.409 0.009   27.158  1.00 31.12  ? 120  VAL A CA  1 
ATOM   967  C  C   . VAL A 1 120 ? -10.271 -0.689  28.506  1.00 31.19  ? 120  VAL A C   1 
ATOM   968  O  O   . VAL A 1 120 ? -9.159  -0.991  28.960  1.00 32.14  ? 120  VAL A O   1 
ATOM   969  C  CB  . VAL A 1 120 ? -10.603 1.531   27.327  1.00 34.21  ? 120  VAL A CB  1 
ATOM   970  C  CG1 . VAL A 1 120 ? -9.616  2.078   28.339  1.00 34.04  ? 120  VAL A CG1 1 
ATOM   971  C  CG2 . VAL A 1 120 ? -10.433 2.253   25.980  1.00 31.77  ? 120  VAL A CG2 1 
ATOM   972  N  N   . ASP A 1 121 ? -11.403 -0.957  29.160  1.00 31.58  ? 121  ASP A N   1 
ATOM   973  C  CA  . ASP A 1 121 ? -11.405 -1.699  30.415  1.00 32.91  ? 121  ASP A CA  1 
ATOM   974  C  C   . ASP A 1 121 ? -10.554 -2.965  30.308  1.00 33.19  ? 121  ASP A C   1 
ATOM   975  O  O   . ASP A 1 121 ? -9.650  -3.191  31.126  1.00 31.26  ? 121  ASP A O   1 
ATOM   976  C  CB  . ASP A 1 121 ? -12.856 -2.030  30.796  1.00 31.45  ? 121  ASP A CB  1 
ATOM   977  C  CG  . ASP A 1 121 ? -12.975 -2.717  32.142  1.00 34.02  ? 121  ASP A CG  1 
ATOM   978  O  OD1 . ASP A 1 121 ? -12.404 -3.804  32.321  1.00 32.14  ? 121  ASP A OD1 1 
ATOM   979  O  OD2 . ASP A 1 121 ? -13.682 -2.184  33.016  1.00 34.25  ? 121  ASP A OD2 1 
ATOM   980  N  N   . ILE A 1 122 ? -10.802 -3.789  29.280  1.00 30.73  ? 122  ILE A N   1 
ATOM   981  C  CA  . ILE A 1 122 ? -10.064 -5.043  29.152  1.00 31.27  ? 122  ILE A CA  1 
ATOM   982  C  C   . ILE A 1 122 ? -8.619  -4.779  28.735  1.00 31.38  ? 122  ILE A C   1 
ATOM   983  O  O   . ILE A 1 122 ? -7.686  -5.443  29.213  1.00 29.36  ? 122  ILE A O   1 
ATOM   984  C  CB  . ILE A 1 122 ? -10.772 -5.989  28.162  1.00 29.11  ? 122  ILE A CB  1 
ATOM   985  C  CG1 . ILE A 1 122 ? -12.234 -6.178  28.575  1.00 29.40  ? 122  ILE A CG1 1 
ATOM   986  C  CG2 . ILE A 1 122 ? -10.048 -7.350  28.084  1.00 31.25  ? 122  ILE A CG2 1 
ATOM   987  C  CD1 . ILE A 1 122 ? -12.415 -6.617  30.037  1.00 30.77  ? 122  ILE A CD1 1 
ATOM   988  N  N   . ALA A 1 123 ? -8.408  -3.805  27.850  1.00 31.10  ? 123  ALA A N   1 
ATOM   989  C  CA  . ALA A 1 123 ? -7.052  -3.500  27.400  1.00 32.03  ? 123  ALA A CA  1 
ATOM   990  C  C   . ALA A 1 123 ? -6.184  -3.048  28.565  1.00 31.98  ? 123  ALA A C   1 
ATOM   991  O  O   . ALA A 1 123 ? -5.001  -3.412  28.664  1.00 31.40  ? 123  ALA A O   1 
ATOM   992  C  CB  . ALA A 1 123 ? -7.088  -2.408  26.327  1.00 30.33  ? 123  ALA A CB  1 
ATOM   993  N  N   . VAL A 1 124 ? -6.750  -2.230  29.445  1.00 30.54  ? 124  VAL A N   1 
ATOM   994  C  CA  . VAL A 1 124 ? -5.998  -1.793  30.617  1.00 31.59  ? 124  VAL A CA  1 
ATOM   995  C  C   . VAL A 1 124 ? -5.650  -2.989  31.500  1.00 31.97  ? 124  VAL A C   1 
ATOM   996  O  O   . VAL A 1 124 ? -4.552  -3.062  32.061  1.00 32.94  ? 124  VAL A O   1 
ATOM   997  C  CB  . VAL A 1 124 ? -6.786  -0.711  31.379  1.00 34.18  ? 124  VAL A CB  1 
ATOM   998  C  CG1 . VAL A 1 124 ? -6.218  -0.540  32.791  1.00 33.86  ? 124  VAL A CG1 1 
ATOM   999  C  CG2 . VAL A 1 124 ? -6.736  0.627   30.619  1.00 31.35  ? 124  VAL A CG2 1 
ATOM   1000 N  N   . GLN A 1 125 ? -6.571  -3.947  31.648  1.00 30.12  ? 125  GLN A N   1 
ATOM   1001 C  CA  . GLN A 1 125 ? -6.231  -5.154  32.401  1.00 30.61  ? 125  GLN A CA  1 
ATOM   1002 C  C   . GLN A 1 125 ? -5.031  -5.876  31.787  1.00 32.24  ? 125  GLN A C   1 
ATOM   1003 O  O   . GLN A 1 125 ? -4.159  -6.383  32.508  1.00 29.46  ? 125  GLN A O   1 
ATOM   1004 C  CB  . GLN A 1 125 ? -7.441  -6.087  32.476  1.00 30.39  ? 125  GLN A CB  1 
ATOM   1005 C  CG  . GLN A 1 125 ? -8.604  -5.527  33.321  1.00 31.58  ? 125  GLN A CG  1 
ATOM   1006 C  CD  . GLN A 1 125 ? -9.651  -6.582  33.620  1.00 30.78  ? 125  GLN A CD  1 
ATOM   1007 O  OE1 . GLN A 1 125 ? -9.325  -7.672  34.082  1.00 30.27  ? 125  GLN A OE1 1 
ATOM   1008 N  NE2 . GLN A 1 125 ? -10.928 -6.259  33.363  1.00 30.55  ? 125  GLN A NE2 1 
ATOM   1009 N  N   . LEU A 1 126 ? -4.966  -5.942  30.456  1.00 28.56  ? 126  LEU A N   1 
ATOM   1010 C  CA  . LEU A 1 126 ? -3.821  -6.568  29.804  1.00 27.86  ? 126  LEU A CA  1 
ATOM   1011 C  C   . LEU A 1 126 ? -2.530  -5.817  30.114  1.00 31.62  ? 126  LEU A C   1 
ATOM   1012 O  O   . LEU A 1 126 ? -1.518  -6.423  30.503  1.00 30.89  ? 126  LEU A O   1 
ATOM   1013 C  CB  . LEU A 1 126 ? -4.039  -6.632  28.290  1.00 30.50  ? 126  LEU A CB  1 
ATOM   1014 C  CG  . LEU A 1 126 ? -2.832  -7.157  27.514  1.00 32.04  ? 126  LEU A CG  1 
ATOM   1015 C  CD1 . LEU A 1 126 ? -2.653  -8.657  27.732  1.00 30.12  ? 126  LEU A CD1 1 
ATOM   1016 C  CD2 . LEU A 1 126 ? -2.994  -6.887  26.013  1.00 40.57  ? 126  LEU A CD2 1 
ATOM   1017 N  N   . VAL A 1 127 ? -2.536  -4.498  29.914  1.00 31.19  ? 127  VAL A N   1 
ATOM   1018 C  CA  . VAL A 1 127 ? -1.338  -3.708  30.185  1.00 32.33  ? 127  VAL A CA  1 
ATOM   1019 C  C   . VAL A 1 127 ? -0.928  -3.867  31.643  1.00 32.48  ? 127  VAL A C   1 
ATOM   1020 O  O   . VAL A 1 127 ? 0.258   -4.027  31.954  1.00 32.11  ? 127  VAL A O   1 
ATOM   1021 C  CB  . VAL A 1 127 ? -1.582  -2.233  29.822  1.00 32.13  ? 127  VAL A CB  1 
ATOM   1022 C  CG1 . VAL A 1 127 ? -0.415  -1.362  30.291  1.00 34.01  ? 127  VAL A CG1 1 
ATOM   1023 C  CG2 . VAL A 1 127 ? -1.823  -2.085  28.297  1.00 31.39  ? 127  VAL A CG2 1 
ATOM   1024 N  N   . GLN A 1 128 ? -1.895  -3.829  32.561  1.00 29.62  ? 128  GLN A N   1 
ATOM   1025 C  CA  . GLN A 1 128 ? -1.543  -3.956  33.976  1.00 32.92  ? 128  GLN A CA  1 
ATOM   1026 C  C   . GLN A 1 128 ? -0.944  -5.328  34.272  1.00 33.74  ? 128  GLN A C   1 
ATOM   1027 O  O   . GLN A 1 128 ? 0.026   -5.437  35.034  1.00 32.36  ? 128  GLN A O   1 
ATOM   1028 C  CB  . GLN A 1 128 ? -2.771  -3.688  34.843  1.00 32.95  ? 128  GLN A CB  1 
ATOM   1029 C  CG  . GLN A 1 128 ? -2.965  -2.217  35.092  1.00 37.00  ? 128  GLN A CG  1 
ATOM   1030 C  CD  . GLN A 1 128 ? -4.234  -1.904  35.845  1.00 46.49  ? 128  GLN A CD  1 
ATOM   1031 O  OE1 . GLN A 1 128 ? -5.182  -2.692  35.852  1.00 47.96  ? 128  GLN A OE1 1 
ATOM   1032 N  NE2 . GLN A 1 128 ? -4.254  -0.750  36.502  1.00 45.91  ? 128  GLN A NE2 1 
ATOM   1033 N  N   . LYS A 1 129 ? -1.484  -6.392  33.667  1.00 30.95  ? 129  LYS A N   1 
ATOM   1034 C  CA  . LYS A 1 129 ? -0.876  -7.704  33.865  1.00 28.68  ? 129  LYS A CA  1 
ATOM   1035 C  C   . LYS A 1 129 ? 0.598   -7.669  33.482  1.00 30.75  ? 129  LYS A C   1 
ATOM   1036 O  O   . LYS A 1 129 ? 1.461   -8.176  34.207  1.00 30.98  ? 129  LYS A O   1 
ATOM   1037 C  CB  . LYS A 1 129 ? -1.590  -8.780  33.046  1.00 31.23  ? 129  LYS A CB  1 
ATOM   1038 C  CG  . LYS A 1 129 ? -0.910  -10.157 33.188  1.00 32.94  ? 129  LYS A CG  1 
ATOM   1039 C  CD  . LYS A 1 129 ? -1.641  -11.276 32.467  1.00 33.14  ? 129  LYS A CD  1 
ATOM   1040 C  CE  . LYS A 1 129 ? -0.876  -12.615 32.610  1.00 33.92  ? 129  LYS A CE  1 
ATOM   1041 N  NZ  . LYS A 1 129 ? -1.614  -13.796 32.055  1.00 33.98  ? 129  LYS A NZ  1 
ATOM   1042 N  N   . TRP A 1 130 ? 0.903   -7.069  32.335  1.00 27.98  ? 130  TRP A N   1 
ATOM   1043 C  CA  . TRP A 1 130 ? 2.283   -7.096  31.869  1.00 30.77  ? 130  TRP A CA  1 
ATOM   1044 C  C   . TRP A 1 130 ? 3.188   -6.194  32.708  1.00 32.25  ? 130  TRP A C   1 
ATOM   1045 O  O   . TRP A 1 130 ? 4.356   -6.552  32.959  1.00 32.37  ? 130  TRP A O   1 
ATOM   1046 C  CB  . TRP A 1 130 ? 2.323   -6.734  30.385  1.00 28.65  ? 130  TRP A CB  1 
ATOM   1047 C  CG  . TRP A 1 130 ? 1.719   -7.809  29.507  1.00 29.99  ? 130  TRP A CG  1 
ATOM   1048 C  CD1 . TRP A 1 130 ? 1.195   -9.027  29.897  1.00 31.27  ? 130  TRP A CD1 1 
ATOM   1049 C  CD2 . TRP A 1 130 ? 1.585   -7.757  28.087  1.00 29.44  ? 130  TRP A CD2 1 
ATOM   1050 N  NE1 . TRP A 1 130 ? 0.742   -9.721  28.798  1.00 28.81  ? 130  TRP A NE1 1 
ATOM   1051 C  CE2 . TRP A 1 130 ? 0.974   -8.964  27.675  1.00 28.04  ? 130  TRP A CE2 1 
ATOM   1052 C  CE3 . TRP A 1 130 ? 1.930   -6.807  27.123  1.00 29.93  ? 130  TRP A CE3 1 
ATOM   1053 C  CZ2 . TRP A 1 130 ? 0.708   -9.246  26.342  1.00 31.11  ? 130  TRP A CZ2 1 
ATOM   1054 C  CZ3 . TRP A 1 130 ? 1.669   -7.091  25.785  1.00 30.24  ? 130  TRP A CZ3 1 
ATOM   1055 C  CH2 . TRP A 1 130 ? 1.060   -8.297  25.410  1.00 32.43  ? 130  TRP A CH2 1 
ATOM   1056 N  N   . GLU A 1 131 ? 2.694   -5.017  33.131  1.00 31.05  ? 131  GLU A N   1 
ATOM   1057 C  CA  . GLU A 1 131 ? 3.461   -4.189  34.069  1.00 30.92  ? 131  GLU A CA  1 
ATOM   1058 C  C   . GLU A 1 131 ? 3.794   -4.903  35.365  1.00 34.94  ? 131  GLU A C   1 
ATOM   1059 O  O   . GLU A 1 131 ? 4.791   -4.551  36.011  1.00 33.44  ? 131  GLU A O   1 
ATOM   1060 C  CB  . GLU A 1 131 ? 2.744   -2.876  34.396  1.00 31.89  ? 131  GLU A CB  1 
ATOM   1061 C  CG  . GLU A 1 131 ? 2.396   -2.105  33.147  1.00 34.32  ? 131  GLU A CG  1 
ATOM   1062 C  CD  . GLU A 1 131 ? 3.472   -1.078  32.818  1.00 38.67  ? 131  GLU A CD  1 
ATOM   1063 O  OE1 . GLU A 1 131 ? 4.669   -1.414  32.988  1.00 41.49  ? 131  GLU A OE1 1 
ATOM   1064 O  OE2 . GLU A 1 131 ? 3.153   0.013   32.299  1.00 42.87  ? 131  GLU A OE2 1 
ATOM   1065 N  N   . ARG A 1 132 ? 3.012   -5.901  35.745  1.00 31.83  ? 132  ARG A N   1 
ATOM   1066 C  CA  . ARG A 1 132 ? 3.188   -6.565  37.027  1.00 30.65  ? 132  ARG A CA  1 
ATOM   1067 C  C   . ARG A 1 132 ? 4.022   -7.840  36.957  1.00 33.67  ? 132  ARG A C   1 
ATOM   1068 O  O   . ARG A 1 132 ? 4.181   -8.515  37.984  1.00 31.14  ? 132  ARG A O   1 
ATOM   1069 C  CB  . ARG A 1 132 ? 1.813   -6.869  37.637  1.00 31.28  ? 132  ARG A CB  1 
ATOM   1070 C  CG  . ARG A 1 132 ? 1.126   -5.617  38.104  1.00 32.92  ? 132  ARG A CG  1 
ATOM   1071 C  CD  . ARG A 1 132 ? -0.372  -5.797  38.361  1.00 32.38  ? 132  ARG A CD  1 
ATOM   1072 N  NE  . ARG A 1 132 ? -0.942  -4.531  38.808  1.00 32.48  ? 132  ARG A NE  1 
ATOM   1073 C  CZ  . ARG A 1 132 ? -2.239  -4.298  38.954  1.00 33.29  ? 132  ARG A CZ  1 
ATOM   1074 N  NH1 . ARG A 1 132 ? -3.146  -5.210  38.643  1.00 31.07  ? 132  ARG A NH1 1 
ATOM   1075 N  NH2 . ARG A 1 132 ? -2.634  -3.126  39.438  1.00 38.97  ? 132  ARG A NH2 1 
ATOM   1076 N  N   . LEU A 1 133 ? 4.550   -8.190  35.782  1.00 34.26  ? 133  LEU A N   1 
ATOM   1077 C  CA  . LEU A 1 133 ? 5.434   -9.337  35.660  1.00 30.30  ? 133  LEU A CA  1 
ATOM   1078 C  C   . LEU A 1 133 ? 6.776   -9.049  36.322  1.00 34.78  ? 133  LEU A C   1 
ATOM   1079 O  O   . LEU A 1 133 ? 7.254   -7.912  36.336  1.00 35.68  ? 133  LEU A O   1 
ATOM   1080 C  CB  . LEU A 1 133 ? 5.661   -9.690  34.189  1.00 34.04  ? 133  LEU A CB  1 
ATOM   1081 C  CG  . LEU A 1 133 ? 4.409   -10.219 33.487  1.00 31.98  ? 133  LEU A CG  1 
ATOM   1082 C  CD1 . LEU A 1 133 ? 4.709   -10.633 32.024  1.00 34.41  ? 133  LEU A CD1 1 
ATOM   1083 C  CD2 . LEU A 1 133 ? 3.841   -11.392 34.261  1.00 34.65  ? 133  LEU A CD2 1 
ATOM   1084 N  N   . ASN A 1 134 ? 7.387   -10.094 36.864  1.00 31.97  ? 134  ASN A N   1 
ATOM   1085 C  CA  . ASN A 1 134 ? 8.705   -9.895  37.439  1.00 37.25  ? 134  ASN A CA  1 
ATOM   1086 C  C   . ASN A 1 134 ? 9.758   -9.933  36.339  1.00 39.65  ? 134  ASN A C   1 
ATOM   1087 O  O   . ASN A 1 134 ? 9.486   -10.297 35.192  1.00 36.79  ? 134  ASN A O   1 
ATOM   1088 C  CB  . ASN A 1 134 ? 9.000   -10.952 38.502  1.00 35.30  ? 134  ASN A CB  1 
ATOM   1089 C  CG  . ASN A 1 134 ? 7.987   -10.926 39.626  1.00 34.36  ? 134  ASN A CG  1 
ATOM   1090 O  OD1 . ASN A 1 134 ? 7.909   -9.957  40.379  1.00 33.98  ? 134  ASN A OD1 1 
ATOM   1091 N  ND2 . ASN A 1 134 ? 7.199   -11.984 39.734  1.00 37.17  ? 134  ASN A ND2 1 
ATOM   1092 N  N   . ALA A 1 135 ? 10.976  -9.545  36.710  1.00 40.99  ? 135  ALA A N   1 
ATOM   1093 C  CA  . ALA A 1 135 ? 12.084  -9.550  35.763  1.00 48.37  ? 135  ALA A CA  1 
ATOM   1094 C  C   . ALA A 1 135 ? 12.279  -10.941 35.173  1.00 44.93  ? 135  ALA A C   1 
ATOM   1095 O  O   . ALA A 1 135 ? 12.237  -11.952 35.877  1.00 45.64  ? 135  ALA A O   1 
ATOM   1096 C  CB  . ALA A 1 135 ? 13.369  -9.083  36.451  1.00 48.97  ? 135  ALA A CB  1 
ATOM   1097 N  N   . ASP A 1 136 ? 12.480  -10.999 33.864  1.00 47.34  ? 136  ASP A N   1 
ATOM   1098 C  CA  . ASP A 1 136 ? 12.787  -12.255 33.189  1.00 51.87  ? 136  ASP A CA  1 
ATOM   1099 C  C   . ASP A 1 136 ? 11.652  -13.279 33.265  1.00 52.08  ? 136  ASP A C   1 
ATOM   1100 O  O   . ASP A 1 136 ? 11.831  -14.423 32.824  1.00 55.07  ? 136  ASP A O   1 
ATOM   1101 C  CB  . ASP A 1 136 ? 14.089  -12.866 33.730  1.00 57.69  ? 136  ASP A CB  1 
ATOM   1102 C  CG  . ASP A 1 136 ? 15.301  -11.979 33.474  1.00 63.24  ? 136  ASP A CG  1 
ATOM   1103 O  OD1 . ASP A 1 136 ? 15.282  -11.207 32.486  1.00 66.61  ? 136  ASP A OD1 1 
ATOM   1104 O  OD2 . ASP A 1 136 ? 16.264  -12.037 34.269  1.00 69.59  ? 136  ASP A OD2 1 
ATOM   1105 N  N   . GLU A 1 137 ? 10.489  -12.920 33.812  1.00 45.00  ? 137  GLU A N   1 
ATOM   1106 C  CA  . GLU A 1 137 ? 9.297   -13.651 33.410  1.00 37.64  ? 137  GLU A CA  1 
ATOM   1107 C  C   . GLU A 1 137 ? 8.966   -13.263 31.973  1.00 36.06  ? 137  GLU A C   1 
ATOM   1108 O  O   . GLU A 1 137 ? 9.461   -12.266 31.450  1.00 41.53  ? 137  GLU A O   1 
ATOM   1109 C  CB  . GLU A 1 137 ? 8.115   -13.359 34.341  1.00 37.03  ? 137  GLU A CB  1 
ATOM   1110 C  CG  . GLU A 1 137 ? 8.296   -13.978 35.723  1.00 40.88  ? 137  GLU A CG  1 
ATOM   1111 C  CD  . GLU A 1 137 ? 7.215   -13.615 36.724  1.00 44.68  ? 137  GLU A CD  1 
ATOM   1112 O  OE1 . GLU A 1 137 ? 6.351   -12.761 36.430  1.00 37.71  ? 137  GLU A OE1 1 
ATOM   1113 O  OE2 . GLU A 1 137 ? 7.243   -14.194 37.831  1.00 48.77  ? 137  GLU A OE2 1 
ATOM   1114 N  N   . HIS A 1 138 ? 8.131   -14.059 31.324  1.00 35.08  ? 138  HIS A N   1 
ATOM   1115 C  CA  . HIS A 1 138 ? 7.775   -13.763 29.939  1.00 36.50  ? 138  HIS A CA  1 
ATOM   1116 C  C   . HIS A 1 138 ? 6.263   -13.758 29.771  1.00 34.30  ? 138  HIS A C   1 
ATOM   1117 O  O   . HIS A 1 138 ? 5.503   -14.119 30.670  1.00 33.64  ? 138  HIS A O   1 
ATOM   1118 C  CB  . HIS A 1 138 ? 8.401   -14.768 28.962  1.00 34.21  ? 138  HIS A CB  1 
ATOM   1119 C  CG  . HIS A 1 138 ? 7.982   -16.181 29.209  1.00 35.97  ? 138  HIS A CG  1 
ATOM   1120 N  ND1 . HIS A 1 138 ? 8.744   -17.060 29.947  1.00 43.14  ? 138  HIS A ND1 1 
ATOM   1121 C  CD2 . HIS A 1 138 ? 6.873   -16.861 28.841  1.00 34.91  ? 138  HIS A CD2 1 
ATOM   1122 C  CE1 . HIS A 1 138 ? 8.128   -18.227 30.009  1.00 44.23  ? 138  HIS A CE1 1 
ATOM   1123 N  NE2 . HIS A 1 138 ? 6.989   -18.133 29.345  1.00 40.36  ? 138  HIS A NE2 1 
ATOM   1124 N  N   . ILE A 1 139 ? 5.848   -13.334 28.582  1.00 31.18  ? 139  ILE A N   1 
ATOM   1125 C  CA  . ILE A 1 139 ? 4.444   -13.274 28.188  1.00 33.31  ? 139  ILE A CA  1 
ATOM   1126 C  C   . ILE A 1 139 ? 4.144   -14.461 27.287  1.00 32.10  ? 139  ILE A C   1 
ATOM   1127 O  O   . ILE A 1 139 ? 4.878   -14.716 26.315  1.00 32.84  ? 139  ILE A O   1 
ATOM   1128 C  CB  . ILE A 1 139 ? 4.138   -11.956 27.459  1.00 32.50  ? 139  ILE A CB  1 
ATOM   1129 C  CG1 . ILE A 1 139 ? 4.171   -10.783 28.432  1.00 33.33  ? 139  ILE A CG1 1 
ATOM   1130 C  CG2 . ILE A 1 139 ? 2.811   -12.042 26.687  1.00 30.15  ? 139  ILE A CG2 1 
ATOM   1131 C  CD1 . ILE A 1 139 ? 4.562   -9.480  27.760  1.00 33.31  ? 139  ILE A CD1 1 
ATOM   1132 N  N   . GLU A 1 140 ? 3.054   -15.176 27.596  1.00 30.56  ? 140  GLU A N   1 
ATOM   1133 C  CA  . GLU A 1 140 ? 2.494   -16.209 26.724  1.00 32.35  ? 140  GLU A CA  1 
ATOM   1134 C  C   . GLU A 1 140 ? 1.504   -15.511 25.798  1.00 33.85  ? 140  GLU A C   1 
ATOM   1135 O  O   . GLU A 1 140 ? 0.377   -15.206 26.194  1.00 30.74  ? 140  GLU A O   1 
ATOM   1136 C  CB  . GLU A 1 140 ? 1.818   -17.301 27.545  1.00 32.39  ? 140  GLU A CB  1 
ATOM   1137 C  CG  . GLU A 1 140 ? 2.814   -18.118 28.371  1.00 35.80  ? 140  GLU A CG  1 
ATOM   1138 C  CD  . GLU A 1 140 ? 2.150   -19.174 29.232  1.00 43.91  ? 140  GLU A CD  1 
ATOM   1139 O  OE1 . GLU A 1 140 ? 0.972   -18.993 29.620  1.00 42.52  ? 140  GLU A OE1 1 
ATOM   1140 O  OE2 . GLU A 1 140 ? 2.818   -20.180 29.535  1.00 48.00  ? 140  GLU A OE2 1 
ATOM   1141 N  N   . VAL A 1 141 ? 1.924   -15.243 24.565  1.00 31.62  ? 141  VAL A N   1 
ATOM   1142 C  CA  . VAL A 1 141 ? 1.239   -14.254 23.725  1.00 28.91  ? 141  VAL A CA  1 
ATOM   1143 C  C   . VAL A 1 141 ? -0.160  -14.714 23.307  1.00 30.22  ? 141  VAL A C   1 
ATOM   1144 O  O   . VAL A 1 141 ? -1.141  -14.020 23.630  1.00 30.96  ? 141  VAL A O   1 
ATOM   1145 C  CB  . VAL A 1 141 ? 2.094   -13.897 22.503  1.00 28.82  ? 141  VAL A CB  1 
ATOM   1146 C  CG1 . VAL A 1 141 ? 1.295   -13.026 21.519  1.00 31.40  ? 141  VAL A CG1 1 
ATOM   1147 C  CG2 . VAL A 1 141 ? 3.378   -13.176 22.944  1.00 31.08  ? 141  VAL A CG2 1 
ATOM   1148 N  N   . PRO A 1 142 ? -0.331  -15.831 22.585  1.00 31.21  ? 142  PRO A N   1 
ATOM   1149 C  CA  . PRO A 1 142 ? -1.704  -16.210 22.198  1.00 33.06  ? 142  PRO A CA  1 
ATOM   1150 C  C   . PRO A 1 142 ? -2.610  -16.415 23.401  1.00 30.80  ? 142  PRO A C   1 
ATOM   1151 O  O   . PRO A 1 142 ? -3.808  -16.097 23.356  1.00 29.70  ? 142  PRO A O   1 
ATOM   1152 C  CB  . PRO A 1 142 ? -1.508  -17.505 21.391  1.00 32.23  ? 142  PRO A CB  1 
ATOM   1153 C  CG  . PRO A 1 142 ? -0.079  -17.973 21.734  1.00 32.29  ? 142  PRO A CG  1 
ATOM   1154 C  CD  . PRO A 1 142 ? 0.672   -16.701 21.943  1.00 29.40  ? 142  PRO A CD  1 
ATOM   1155 N  N   . GLU A 1 143 ? -2.053  -16.927 24.494  1.00 28.27  ? 143  GLU A N   1 
ATOM   1156 C  CA  . GLU A 1 143 ? -2.844  -17.114 25.705  1.00 29.12  ? 143  GLU A CA  1 
ATOM   1157 C  C   . GLU A 1 143 ? -3.415  -15.788 26.196  1.00 32.07  ? 143  GLU A C   1 
ATOM   1158 O  O   . GLU A 1 143 ? -4.612  -15.685 26.491  1.00 29.88  ? 143  GLU A O   1 
ATOM   1159 C  CB  . GLU A 1 143 ? -1.980  -17.773 26.788  1.00 29.94  ? 143  GLU A CB  1 
ATOM   1160 C  CG  . GLU A 1 143 ? -1.605  -19.248 26.549  1.00 33.39  ? 143  GLU A CG  1 
ATOM   1161 C  CD  . GLU A 1 143 ? -0.529  -19.495 25.478  1.00 36.27  ? 143  GLU A CD  1 
ATOM   1162 O  OE1 . GLU A 1 143 ? 0.150   -18.557 24.997  1.00 32.15  ? 143  GLU A OE1 1 
ATOM   1163 O  OE2 . GLU A 1 143 ? -0.371  -20.675 25.126  1.00 40.41  ? 143  GLU A OE2 1 
ATOM   1164 N  N   . ASP A 1 144 ? -2.565  -14.765 26.334  1.00 28.73  ? 144  ASP A N   1 
ATOM   1165 C  CA  . ASP A 1 144 ? -3.049  -13.471 26.803  1.00 28.01  ? 144  ASP A CA  1 
ATOM   1166 C  C   . ASP A 1 144 ? -3.902  -12.753 25.755  1.00 27.68  ? 144  ASP A C   1 
ATOM   1167 O  O   . ASP A 1 144 ? -4.827  -12.018 26.116  1.00 29.72  ? 144  ASP A O   1 
ATOM   1168 C  CB  . ASP A 1 144 ? -1.871  -12.583 27.224  1.00 30.78  ? 144  ASP A CB  1 
ATOM   1169 C  CG  . ASP A 1 144 ? -1.425  -12.848 28.663  1.00 34.01  ? 144  ASP A CG  1 
ATOM   1170 O  OD1 . ASP A 1 144 ? -2.186  -13.518 29.409  1.00 30.54  ? 144  ASP A OD1 1 
ATOM   1171 O  OD2 . ASP A 1 144 ? -0.319  -12.387 29.045  1.00 32.57  ? 144  ASP A OD2 1 
ATOM   1172 N  N   . MET A 1 145 ? -3.595  -12.906 24.463  1.00 29.08  ? 145  MET A N   1 
ATOM   1173 C  CA  . MET A 1 145 ? -4.489  -12.314 23.465  1.00 31.03  ? 145  MET A CA  1 
ATOM   1174 C  C   . MET A 1 145 ? -5.875  -12.947 23.512  1.00 29.58  ? 145  MET A C   1 
ATOM   1175 O  O   . MET A 1 145 ? -6.880  -12.259 23.291  1.00 28.84  ? 145  MET A O   1 
ATOM   1176 C  CB  . MET A 1 145 ? -3.869  -12.440 22.074  1.00 28.31  ? 145  MET A CB  1 
ATOM   1177 C  CG  . MET A 1 145 ? -2.552  -11.651 21.885  1.00 29.11  ? 145  MET A CG  1 
ATOM   1178 S  SD  . MET A 1 145 ? -2.641  -9.901  22.375  1.00 32.51  ? 145  MET A SD  1 
ATOM   1179 C  CE  . MET A 1 145 ? -1.926  -9.886  24.021  1.00 34.96  ? 145  MET A CE  1 
ATOM   1180 N  N   . THR A 1 146 ? -5.950  -14.243 23.807  1.00 28.45  ? 146  THR A N   1 
ATOM   1181 C  CA  . THR A 1 146 ? -7.246  -14.906 23.908  1.00 29.51  ? 146  THR A CA  1 
ATOM   1182 C  C   . THR A 1 146 ? -7.990  -14.469 25.164  1.00 30.61  ? 146  THR A C   1 
ATOM   1183 O  O   . THR A 1 146 ? -9.214  -14.276 25.131  1.00 30.18  ? 146  THR A O   1 
ATOM   1184 C  CB  . THR A 1 146 ? -7.046  -16.420 23.870  1.00 31.00  ? 146  THR A CB  1 
ATOM   1185 O  OG1 . THR A 1 146 ? -6.452  -16.779 22.608  1.00 34.37  ? 146  THR A OG1 1 
ATOM   1186 C  CG2 . THR A 1 146 ? -8.378  -17.161 24.049  1.00 34.38  ? 146  THR A CG2 1 
ATOM   1187 N  N   . ARG A 1 147 ? -7.270  -14.288 26.285  1.00 26.74  ? 147  ARG A N   1 
ATOM   1188 C  CA  . ARG A 1 147 ? -7.878  -13.667 27.460  1.00 29.20  ? 147  ARG A CA  1 
ATOM   1189 C  C   . ARG A 1 147 ? -8.515  -12.337 27.097  1.00 30.04  ? 147  ARG A C   1 
ATOM   1190 O  O   . ARG A 1 147 ? -9.677  -12.067 27.433  1.00 29.75  ? 147  ARG A O   1 
ATOM   1191 C  CB  . ARG A 1 147 ? -6.822  -13.463 28.553  1.00 30.33  ? 147  ARG A CB  1 
ATOM   1192 C  CG  . ARG A 1 147 ? -6.382  -14.744 29.224  1.00 31.78  ? 147  ARG A CG  1 
ATOM   1193 C  CD  . ARG A 1 147 ? -5.419  -14.426 30.381  1.00 31.76  ? 147  ARG A CD  1 
ATOM   1194 N  NE  . ARG A 1 147 ? -5.155  -15.603 31.196  1.00 32.94  ? 147  ARG A NE  1 
ATOM   1195 C  CZ  . ARG A 1 147 ? -4.121  -16.414 31.026  1.00 37.51  ? 147  ARG A CZ  1 
ATOM   1196 N  NH1 . ARG A 1 147 ? -3.212  -16.194 30.084  1.00 33.11  ? 147  ARG A NH1 1 
ATOM   1197 N  NH2 . ARG A 1 147 ? -3.987  -17.464 31.831  1.00 39.79  ? 147  ARG A NH2 1 
ATOM   1198 N  N   . LEU A 1 148 ? -7.757  -11.494 26.400  1.00 30.09  ? 148  LEU A N   1 
ATOM   1199 C  CA  . LEU A 1 148 ? -8.229  -10.155 26.072  1.00 28.18  ? 148  LEU A CA  1 
ATOM   1200 C  C   . LEU A 1 148 ? -9.440  -10.206 25.151  1.00 28.88  ? 148  LEU A C   1 
ATOM   1201 O  O   . LEU A 1 148 ? -10.459 -9.544  25.408  1.00 31.15  ? 148  LEU A O   1 
ATOM   1202 C  CB  . LEU A 1 148 ? -7.097  -9.356  25.426  1.00 32.59  ? 148  LEU A CB  1 
ATOM   1203 C  CG  . LEU A 1 148 ? -7.641  -8.017  24.925  1.00 30.40  ? 148  LEU A CG  1 
ATOM   1204 C  CD1 . LEU A 1 148 ? -7.022  -6.848  25.640  1.00 34.61  ? 148  LEU A CD1 1 
ATOM   1205 C  CD2 . LEU A 1 148 ? -7.453  -7.910  23.425  1.00 36.83  ? 148  LEU A CD2 1 
ATOM   1206 N  N   . THR A 1 149 ? -9.356  -10.970 24.057  1.00 27.33  ? 149  THR A N   1 
ATOM   1207 C  CA  . THR A 1 149 ? -10.436 -10.859 23.076  1.00 26.02  ? 149  THR A CA  1 
ATOM   1208 C  C   . THR A 1 149 ? -11.712 -11.527 23.574  1.00 28.16  ? 149  THR A C   1 
ATOM   1209 O  O   . THR A 1 149 ? -12.811 -11.044 23.288  1.00 28.42  ? 149  THR A O   1 
ATOM   1210 C  CB  . THR A 1 149 ? -10.031 -11.430 21.714  1.00 27.61  ? 149  THR A CB  1 
ATOM   1211 O  OG1 . THR A 1 149 ? -9.713  -12.819 21.832  1.00 28.55  ? 149  THR A OG1 1 
ATOM   1212 C  CG2 . THR A 1 149 ? -8.870  -10.625 21.103  1.00 27.67  ? 149  THR A CG2 1 
ATOM   1213 N  N   . LEU A 1 150 ? -11.597 -12.645 24.302  1.00 29.45  ? 150  LEU A N   1 
ATOM   1214 C  CA  . LEU A 1 150 ? -12.788 -13.242 24.907  1.00 30.98  ? 150  LEU A CA  1 
ATOM   1215 C  C   . LEU A 1 150 ? -13.439 -12.261 25.875  1.00 29.51  ? 150  LEU A C   1 
ATOM   1216 O  O   . LEU A 1 150 ? -14.660 -12.051 25.852  1.00 29.82  ? 150  LEU A O   1 
ATOM   1217 C  CB  . LEU A 1 150 ? -12.429 -14.541 25.645  1.00 30.82  ? 150  LEU A CB  1 
ATOM   1218 C  CG  . LEU A 1 150 ? -13.627 -15.135 26.400  1.00 32.04  ? 150  LEU A CG  1 
ATOM   1219 C  CD1 . LEU A 1 150 ? -14.609 -15.709 25.401  1.00 33.10  ? 150  LEU A CD1 1 
ATOM   1220 C  CD2 . LEU A 1 150 ? -13.193 -16.226 27.429  1.00 31.88  ? 150  LEU A CD2 1 
ATOM   1221 N  N   . ASP A 1 151 ? -12.633 -11.647 26.744  1.00 28.16  ? 151  ASP A N   1 
ATOM   1222 C  CA  . ASP A 1 151 ? -13.213 -10.723 27.712  1.00 28.21  ? 151  ASP A CA  1 
ATOM   1223 C  C   . ASP A 1 151 ? -13.849 -9.531  27.020  1.00 28.51  ? 151  ASP A C   1 
ATOM   1224 O  O   . ASP A 1 151 ? -14.874 -9.015  27.487  1.00 30.56  ? 151  ASP A O   1 
ATOM   1225 C  CB  . ASP A 1 151 ? -12.148 -10.275 28.717  1.00 28.78  ? 151  ASP A CB  1 
ATOM   1226 C  CG  . ASP A 1 151 ? -11.989 -11.264 29.863  1.00 30.86  ? 151  ASP A CG  1 
ATOM   1227 O  OD1 . ASP A 1 151 ? -12.233 -12.466 29.658  1.00 33.88  ? 151  ASP A OD1 1 
ATOM   1228 O  OD2 . ASP A 1 151 ? -11.652 -10.823 30.960  1.00 33.10  ? 151  ASP A OD2 1 
ATOM   1229 N  N   . THR A 1 152 ? -13.275 -9.090  25.905  1.00 29.66  ? 152  THR A N   1 
ATOM   1230 C  CA  . THR A 1 152 ? -13.811 -7.920  25.229  1.00 29.90  ? 152  THR A CA  1 
ATOM   1231 C  C   . THR A 1 152 ? -15.176 -8.224  24.611  1.00 29.98  ? 152  THR A C   1 
ATOM   1232 O  O   . THR A 1 152 ? -16.126 -7.451  24.782  1.00 30.69  ? 152  THR A O   1 
ATOM   1233 C  CB  . THR A 1 152 ? -12.802 -7.406  24.197  1.00 28.32  ? 152  THR A CB  1 
ATOM   1234 O  OG1 . THR A 1 152 ? -11.610 -6.987  24.883  1.00 30.41  ? 152  THR A OG1 1 
ATOM   1235 C  CG2 . THR A 1 152 ? -13.353 -6.222  23.424  1.00 30.03  ? 152  THR A CG2 1 
ATOM   1236 N  N   . ILE A 1 153 ? -15.317 -9.360  23.923  1.00 29.61  ? 153  ILE A N   1 
ATOM   1237 C  CA  . ILE A 1 153 ? -16.636 -9.621  23.349  1.00 26.93  ? 153  ILE A CA  1 
ATOM   1238 C  C   . ILE A 1 153 ? -17.646 -9.917  24.457  1.00 29.96  ? 153  ILE A C   1 
ATOM   1239 O  O   . ILE A 1 153 ? -18.817 -9.525  24.361  1.00 29.45  ? 153  ILE A O   1 
ATOM   1240 C  CB  . ILE A 1 153 ? -16.578 -10.734 22.284  1.00 28.37  ? 153  ILE A CB  1 
ATOM   1241 C  CG1 . ILE A 1 153 ? -17.948 -10.870 21.577  1.00 31.26  ? 153  ILE A CG1 1 
ATOM   1242 C  CG2 . ILE A 1 153 ? -16.203 -12.063 22.900  1.00 31.61  ? 153  ILE A CG2 1 
ATOM   1243 C  CD1 . ILE A 1 153 ? -18.363 -9.636  20.797  1.00 35.03  ? 153  ILE A CD1 1 
ATOM   1244 N  N   . GLY A 1 154 ? -17.221 -10.566 25.544  1.00 29.87  ? 154  GLY A N   1 
ATOM   1245 C  CA  . GLY A 1 154 ? -18.144 -10.807 26.647  1.00 32.05  ? 154  GLY A CA  1 
ATOM   1246 C  C   . GLY A 1 154 ? -18.687 -9.515  27.236  1.00 31.21  ? 154  GLY A C   1 
ATOM   1247 O  O   . GLY A 1 154 ? -19.897 -9.362  27.434  1.00 32.27  ? 154  GLY A O   1 
ATOM   1248 N  N   . LEU A 1 155 ? -17.795 -8.567  27.524  1.00 29.95  ? 155  LEU A N   1 
ATOM   1249 C  CA  . LEU A 1 155 ? -18.199 -7.328  28.193  1.00 29.49  ? 155  LEU A CA  1 
ATOM   1250 C  C   . LEU A 1 155 ? -18.899 -6.388  27.224  1.00 31.67  ? 155  LEU A C   1 
ATOM   1251 O  O   . LEU A 1 155 ? -19.991 -5.888  27.507  1.00 34.41  ? 155  LEU A O   1 
ATOM   1252 C  CB  . LEU A 1 155 ? -16.974 -6.641  28.787  1.00 33.93  ? 155  LEU A CB  1 
ATOM   1253 C  CG  . LEU A 1 155 ? -17.190 -5.365  29.603  1.00 31.76  ? 155  LEU A CG  1 
ATOM   1254 C  CD1 . LEU A 1 155 ? -18.135 -5.639  30.752  1.00 33.59  ? 155  LEU A CD1 1 
ATOM   1255 C  CD2 . LEU A 1 155 ? -15.843 -4.849  30.123  1.00 32.27  ? 155  LEU A CD2 1 
ATOM   1256 N  N   . CYS A 1 156 ? -18.286 -6.159  26.062  1.00 33.20  ? 156  CYS A N   1 
ATOM   1257 C  CA  . CYS A 1 156 ? -18.808 -5.207  25.094  1.00 33.05  ? 156  CYS A CA  1 
ATOM   1258 C  C   . CYS A 1 156 ? -20.154 -5.696  24.568  1.00 32.09  ? 156  CYS A C   1 
ATOM   1259 O  O   . CYS A 1 156 ? -21.096 -4.915  24.418  1.00 35.82  ? 156  CYS A O   1 
ATOM   1260 C  CB  . CYS A 1 156 ? -17.815 -5.119  23.940  1.00 29.02  ? 156  CYS A CB  1 
ATOM   1261 S  SG  . CYS A 1 156 ? -16.432 -4.038  24.338  1.00 35.11  ? 156  CYS A SG  1 
ATOM   1262 N  N   . GLY A 1 157 ? -20.258 -6.986  24.253  1.00 33.42  ? 157  GLY A N   1 
ATOM   1263 C  CA  . GLY A 1 157 ? -21.441 -7.474  23.582  1.00 33.29  ? 157  GLY A CA  1 
ATOM   1264 C  C   . GLY A 1 157 ? -22.535 -7.898  24.538  1.00 36.05  ? 157  GLY A C   1 
ATOM   1265 O  O   . GLY A 1 157 ? -23.715 -7.757  24.213  1.00 34.12  ? 157  GLY A O   1 
ATOM   1266 N  N   . PHE A 1 158 ? -22.179 -8.370  25.746  1.00 32.69  ? 158  PHE A N   1 
ATOM   1267 C  CA  . PHE A 1 158 ? -23.160 -9.012  26.620  1.00 33.14  ? 158  PHE A CA  1 
ATOM   1268 C  C   . PHE A 1 158 ? -23.119 -8.535  28.064  1.00 35.65  ? 158  PHE A C   1 
ATOM   1269 O  O   . PHE A 1 158 ? -23.862 -9.073  28.898  1.00 35.59  ? 158  PHE A O   1 
ATOM   1270 C  CB  . PHE A 1 158 ? -22.974 -10.535 26.567  1.00 36.25  ? 158  PHE A CB  1 
ATOM   1271 C  CG  . PHE A 1 158 ? -22.991 -11.063 25.166  1.00 32.91  ? 158  PHE A CG  1 
ATOM   1272 C  CD1 . PHE A 1 158 ? -24.201 -11.339 24.547  1.00 32.80  ? 158  PHE A CD1 1 
ATOM   1273 C  CD2 . PHE A 1 158 ? -21.821 -11.182 24.440  1.00 34.55  ? 158  PHE A CD2 1 
ATOM   1274 C  CE1 . PHE A 1 158 ? -24.239 -11.778 23.238  1.00 32.76  ? 158  PHE A CE1 1 
ATOM   1275 C  CE2 . PHE A 1 158 ? -21.849 -11.630 23.116  1.00 33.61  ? 158  PHE A CE2 1 
ATOM   1276 C  CZ  . PHE A 1 158 ? -23.071 -11.920 22.521  1.00 34.39  ? 158  PHE A CZ  1 
ATOM   1277 N  N   . ASN A 1 159 ? -22.290 -7.546  28.374  1.00 33.44  ? 159  ASN A N   1 
ATOM   1278 C  CA  . ASN A 1 159 ? -22.133 -7.063  29.742  1.00 33.92  ? 159  ASN A CA  1 
ATOM   1279 C  C   . ASN A 1 159 ? -21.831 -8.203  30.706  1.00 37.18  ? 159  ASN A C   1 
ATOM   1280 O  O   . ASN A 1 159 ? -22.304 -8.224  31.845  1.00 34.96  ? 159  ASN A O   1 
ATOM   1281 C  CB  . ASN A 1 159 ? -23.374 -6.287  30.201  1.00 39.28  ? 159  ASN A CB  1 
ATOM   1282 C  CG  . ASN A 1 159 ? -23.052 -5.295  31.297  1.00 47.17  ? 159  ASN A CG  1 
ATOM   1283 O  OD1 . ASN A 1 159 ? -21.904 -4.872  31.435  1.00 37.62  ? 159  ASN A OD1 1 
ATOM   1284 N  ND2 . ASN A 1 159 ? -24.056 -4.936  32.098  1.00 46.84  ? 159  ASN A ND2 1 
ATOM   1285 N  N   . TYR A 1 160 ? -21.016 -9.158  30.261  1.00 32.82  ? 160  TYR A N   1 
ATOM   1286 C  CA  . TYR A 1 160 ? -20.636 -10.294 31.086  1.00 30.41  ? 160  TYR A CA  1 
ATOM   1287 C  C   . TYR A 1 160 ? -19.119 -10.296 31.211  1.00 29.17  ? 160  TYR A C   1 
ATOM   1288 O  O   . TYR A 1 160 ? -18.418 -10.085 30.217  1.00 31.64  ? 160  TYR A O   1 
ATOM   1289 C  CB  . TYR A 1 160 ? -21.125 -11.618 30.487  1.00 31.88  ? 160  TYR A CB  1 
ATOM   1290 C  CG  . TYR A 1 160 ? -20.860 -12.814 31.375  1.00 33.99  ? 160  TYR A CG  1 
ATOM   1291 C  CD1 . TYR A 1 160 ? -21.728 -13.143 32.409  1.00 36.57  ? 160  TYR A CD1 1 
ATOM   1292 C  CD2 . TYR A 1 160 ? -19.734 -13.616 31.181  1.00 34.27  ? 160  TYR A CD2 1 
ATOM   1293 C  CE1 . TYR A 1 160 ? -21.480 -14.242 33.238  1.00 37.21  ? 160  TYR A CE1 1 
ATOM   1294 C  CE2 . TYR A 1 160 ? -19.483 -14.710 31.999  1.00 38.13  ? 160  TYR A CE2 1 
ATOM   1295 C  CZ  . TYR A 1 160 ? -20.360 -15.016 33.029  1.00 40.04  ? 160  TYR A CZ  1 
ATOM   1296 O  OH  . TYR A 1 160 ? -20.107 -16.096 33.845  1.00 42.77  ? 160  TYR A OH  1 
ATOM   1297 N  N   . ARG A 1 161 ? -18.613 -10.492 32.432  1.00 30.72  ? 161  ARG A N   1 
ATOM   1298 C  CA  . ARG A 1 161 ? -17.168 -10.501 32.673  1.00 30.79  ? 161  ARG A CA  1 
ATOM   1299 C  C   . ARG A 1 161 ? -16.684 -11.943 32.805  1.00 28.26  ? 161  ARG A C   1 
ATOM   1300 O  O   . ARG A 1 161 ? -16.958 -12.616 33.800  1.00 33.44  ? 161  ARG A O   1 
ATOM   1301 C  CB  . ARG A 1 161 ? -16.807 -9.678  33.908  1.00 31.01  ? 161  ARG A CB  1 
ATOM   1302 C  CG  . ARG A 1 161 ? -17.024 -8.194  33.674  1.00 33.05  ? 161  ARG A CG  1 
ATOM   1303 C  CD  . ARG A 1 161 ? -16.480 -7.334  34.773  1.00 33.20  ? 161  ARG A CD  1 
ATOM   1304 N  NE  . ARG A 1 161 ? -16.675 -5.935  34.440  1.00 32.44  ? 161  ARG A NE  1 
ATOM   1305 C  CZ  . ARG A 1 161 ? -15.744 -5.139  33.938  1.00 30.29  ? 161  ARG A CZ  1 
ATOM   1306 N  NH1 . ARG A 1 161 ? -14.518 -5.572  33.688  1.00 30.87  ? 161  ARG A NH1 1 
ATOM   1307 N  NH2 . ARG A 1 161 ? -16.049 -3.873  33.685  1.00 30.19  ? 161  ARG A NH2 1 
ATOM   1308 N  N   . PHE A 1 162 ? -15.952 -12.420 31.791  1.00 27.79  ? 162  PHE A N   1 
ATOM   1309 C  CA  . PHE A 1 162 ? -15.314 -13.724 31.901  1.00 30.68  ? 162  PHE A CA  1 
ATOM   1310 C  C   . PHE A 1 162 ? -14.143 -13.701 32.883  1.00 31.60  ? 162  PHE A C   1 
ATOM   1311 O  O   . PHE A 1 162 ? -13.738 -14.761 33.373  1.00 31.08  ? 162  PHE A O   1 
ATOM   1312 C  CB  . PHE A 1 162 ? -14.815 -14.185 30.524  1.00 32.68  ? 162  PHE A CB  1 
ATOM   1313 C  CG  . PHE A 1 162 ? -15.907 -14.626 29.595  1.00 30.13  ? 162  PHE A CG  1 
ATOM   1314 C  CD1 . PHE A 1 162 ? -16.466 -15.880 29.718  1.00 38.39  ? 162  PHE A CD1 1 
ATOM   1315 C  CD2 . PHE A 1 162 ? -16.338 -13.789 28.579  1.00 32.26  ? 162  PHE A CD2 1 
ATOM   1316 C  CE1 . PHE A 1 162 ? -17.471 -16.295 28.856  1.00 42.41  ? 162  PHE A CE1 1 
ATOM   1317 C  CE2 . PHE A 1 162 ? -17.344 -14.194 27.709  1.00 34.86  ? 162  PHE A CE2 1 
ATOM   1318 C  CZ  . PHE A 1 162 ? -17.906 -15.452 27.850  1.00 37.48  ? 162  PHE A CZ  1 
ATOM   1319 N  N   . ASN A 1 163 ? -13.595 -12.520 33.157  1.00 30.69  ? 163  ASN A N   1 
ATOM   1320 C  CA  . ASN A 1 163 ? -12.515 -12.335 34.131  1.00 30.50  ? 163  ASN A CA  1 
ATOM   1321 C  C   . ASN A 1 163 ? -11.338 -13.249 33.820  1.00 30.49  ? 163  ASN A C   1 
ATOM   1322 O  O   . ASN A 1 163 ? -10.774 -13.917 34.691  1.00 31.13  ? 163  ASN A O   1 
ATOM   1323 C  CB  . ASN A 1 163 ? -13.041 -12.524 35.553  1.00 31.05  ? 163  ASN A CB  1 
ATOM   1324 C  CG  . ASN A 1 163 ? -13.859 -11.341 35.996  1.00 29.20  ? 163  ASN A CG  1 
ATOM   1325 O  OD1 . ASN A 1 163 ? -13.454 -10.198 35.797  1.00 30.81  ? 163  ASN A OD1 1 
ATOM   1326 N  ND2 . ASN A 1 163 ? -15.046 -11.603 36.554  1.00 31.23  ? 163  ASN A ND2 1 
ATOM   1327 N  N   . SER A 1 164 ? -10.981 -13.273 32.530  1.00 29.00  ? 164  SER A N   1 
ATOM   1328 C  CA  . SER A 1 164 ? -9.948  -14.181 32.064  1.00 30.89  ? 164  SER A CA  1 
ATOM   1329 C  C   . SER A 1 164 ? -8.602  -13.855 32.672  1.00 30.34  ? 164  SER A C   1 
ATOM   1330 O  O   . SER A 1 164 ? -7.780  -14.761 32.841  1.00 31.35  ? 164  SER A O   1 
ATOM   1331 C  CB  . SER A 1 164 ? -9.855  -14.142 30.537  1.00 32.00  ? 164  SER A CB  1 
ATOM   1332 O  OG  . SER A 1 164 ? -11.030 -14.698 29.971  1.00 31.09  ? 164  SER A OG  1 
ATOM   1333 N  N   . PHE A 1 165 ? -8.348  -12.587 32.985  1.00 30.59  ? 165  PHE A N   1 
ATOM   1334 C  CA  . PHE A 1 165 ? -7.073  -12.232 33.602  1.00 31.11  ? 165  PHE A CA  1 
ATOM   1335 C  C   . PHE A 1 165 ? -7.025  -12.557 35.083  1.00 36.11  ? 165  PHE A C   1 
ATOM   1336 O  O   . PHE A 1 165 ? -5.993  -12.316 35.715  1.00 34.07  ? 165  PHE A O   1 
ATOM   1337 C  CB  . PHE A 1 165 ? -6.768  -10.751 33.384  1.00 31.78  ? 165  PHE A CB  1 
ATOM   1338 C  CG  . PHE A 1 165 ? -6.447  -10.422 31.952  1.00 33.34  ? 165  PHE A CG  1 
ATOM   1339 C  CD1 . PHE A 1 165 ? -5.268  -10.888 31.362  1.00 32.63  ? 165  PHE A CD1 1 
ATOM   1340 C  CD2 . PHE A 1 165 ? -7.350  -9.714  31.175  1.00 30.99  ? 165  PHE A CD2 1 
ATOM   1341 C  CE1 . PHE A 1 165 ? -4.980  -10.608 30.033  1.00 30.64  ? 165  PHE A CE1 1 
ATOM   1342 C  CE2 . PHE A 1 165 ? -7.068  -9.430  29.840  1.00 32.34  ? 165  PHE A CE2 1 
ATOM   1343 C  CZ  . PHE A 1 165 ? -5.888  -9.880  29.268  1.00 29.78  ? 165  PHE A CZ  1 
ATOM   1344 N  N   . TYR A 1 166 ? -8.106  -13.084 35.650  1.00 31.85  ? 166  TYR A N   1 
ATOM   1345 C  CA  . TYR A 1 166 ? -8.094  -13.616 37.006  1.00 35.02  ? 166  TYR A CA  1 
ATOM   1346 C  C   . TYR A 1 166 ? -7.910  -15.126 37.026  1.00 35.94  ? 166  TYR A C   1 
ATOM   1347 O  O   . TYR A 1 166 ? -8.072  -15.748 38.080  1.00 37.56  ? 166  TYR A O   1 
ATOM   1348 C  CB  . TYR A 1 166 ? -9.376  -13.207 37.736  1.00 31.97  ? 166  TYR A CB  1 
ATOM   1349 C  CG  . TYR A 1 166 ? -9.442  -11.716 37.960  1.00 30.04  ? 166  TYR A CG  1 
ATOM   1350 C  CD1 . TYR A 1 166 ? -9.959  -10.862 36.980  1.00 28.24  ? 166  TYR A CD1 1 
ATOM   1351 C  CD2 . TYR A 1 166 ? -8.938  -11.149 39.135  1.00 30.38  ? 166  TYR A CD2 1 
ATOM   1352 C  CE1 . TYR A 1 166 ? -10.000 -9.496  37.166  1.00 30.34  ? 166  TYR A CE1 1 
ATOM   1353 C  CE2 . TYR A 1 166 ? -8.966  -9.786  39.334  1.00 28.74  ? 166  TYR A CE2 1 
ATOM   1354 C  CZ  . TYR A 1 166 ? -9.503  -8.961  38.351  1.00 27.37  ? 166  TYR A CZ  1 
ATOM   1355 O  OH  . TYR A 1 166 ? -9.528  -7.609  38.535  1.00 29.34  ? 166  TYR A OH  1 
ATOM   1356 N  N   . ARG A 1 167 ? -7.555  -15.726 35.886  1.00 35.28  ? 167  ARG A N   1 
ATOM   1357 C  CA  . ARG A 1 167 ? -7.420  -17.169 35.761  1.00 38.48  ? 167  ARG A CA  1 
ATOM   1358 C  C   . ARG A 1 167 ? -6.059  -17.498 35.170  1.00 44.49  ? 167  ARG A C   1 
ATOM   1359 O  O   . ARG A 1 167 ? -5.657  -16.904 34.166  1.00 42.41  ? 167  ARG A O   1 
ATOM   1360 C  CB  . ARG A 1 167 ? -8.520  -17.761 34.873  1.00 39.39  ? 167  ARG A CB  1 
ATOM   1361 C  CG  . ARG A 1 167 ? -9.928  -17.429 35.330  1.00 38.97  ? 167  ARG A CG  1 
ATOM   1362 C  CD  . ARG A 1 167 ? -10.927 -17.638 34.188  1.00 42.70  ? 167  ARG A CD  1 
ATOM   1363 N  NE  . ARG A 1 167 ? -12.245 -17.129 34.539  1.00 45.28  ? 167  ARG A NE  1 
ATOM   1364 C  CZ  . ARG A 1 167 ? -13.184 -17.832 35.156  1.00 48.27  ? 167  ARG A CZ  1 
ATOM   1365 N  NH1 . ARG A 1 167 ? -13.018 -19.118 35.431  1.00 50.17  ? 167  ARG A NH1 1 
ATOM   1366 N  NH2 . ARG A 1 167 ? -14.321 -17.231 35.499  1.00 47.76  ? 167  ARG A NH2 1 
ATOM   1367 N  N   . ASP A 1 168 ? -5.355  -18.446 35.788  1.00 45.56  ? 168  ASP A N   1 
ATOM   1368 C  CA  . ASP A 1 168 ? -4.120  -18.931 35.190  1.00 45.96  ? 168  ASP A CA  1 
ATOM   1369 C  C   . ASP A 1 168 ? -4.374  -20.033 34.174  1.00 47.32  ? 168  ASP A C   1 
ATOM   1370 O  O   . ASP A 1 168 ? -3.484  -20.335 33.373  1.00 52.34  ? 168  ASP A O   1 
ATOM   1371 C  CB  . ASP A 1 168 ? -3.133  -19.398 36.278  1.00 49.39  ? 168  ASP A CB  1 
ATOM   1372 C  CG  . ASP A 1 168 ? -3.756  -20.345 37.292  1.00 54.84  ? 168  ASP A CG  1 
ATOM   1373 O  OD1 . ASP A 1 168 ? -4.690  -19.941 38.022  1.00 56.99  ? 168  ASP A OD1 1 
ATOM   1374 O  OD2 . ASP A 1 168 ? -3.306  -21.506 37.370  1.00 66.70  ? 168  ASP A OD2 1 
ATOM   1375 N  N   . GLN A 1 169 ? -5.572  -20.597 34.171  1.00 48.80  ? 169  GLN A N   1 
ATOM   1376 C  CA  . GLN A 1 169 ? -6.055  -21.573 33.218  1.00 54.35  ? 169  GLN A CA  1 
ATOM   1377 C  C   . GLN A 1 169 ? -7.159  -20.962 32.363  1.00 55.23  ? 169  GLN A C   1 
ATOM   1378 O  O   . GLN A 1 169 ? -7.812  -19.996 32.772  1.00 52.69  ? 169  GLN A O   1 
ATOM   1379 C  CB  . GLN A 1 169 ? -6.585  -22.805 33.963  1.00 57.93  ? 169  GLN A CB  1 
ATOM   1380 C  CG  . GLN A 1 169 ? -5.492  -23.591 34.687  1.00 64.50  ? 169  GLN A CG  1 
ATOM   1381 C  CD  . GLN A 1 169 ? -6.012  -24.863 35.328  1.00 73.24  ? 169  GLN A CD  1 
ATOM   1382 O  OE1 . GLN A 1 169 ? -6.744  -24.815 36.319  1.00 75.58  ? 169  GLN A OE1 1 
ATOM   1383 N  NE2 . GLN A 1 169 ? -5.652  -26.007 34.756  1.00 77.63  ? 169  GLN A NE2 1 
ATOM   1384 N  N   . PRO A 1 170 ? -7.394  -21.495 31.165  1.00 54.97  ? 170  PRO A N   1 
ATOM   1385 C  CA  . PRO A 1 170 ? -8.443  -20.926 30.307  1.00 53.53  ? 170  PRO A CA  1 
ATOM   1386 C  C   . PRO A 1 170 ? -9.813  -21.012 30.969  1.00 55.44  ? 170  PRO A C   1 
ATOM   1387 O  O   . PRO A 1 170 ? -10.091 -21.914 31.767  1.00 51.93  ? 170  PRO A O   1 
ATOM   1388 C  CB  . PRO A 1 170 ? -8.377  -21.791 29.041  1.00 57.33  ? 170  PRO A CB  1 
ATOM   1389 C  CG  . PRO A 1 170 ? -6.992  -22.379 29.049  1.00 56.73  ? 170  PRO A CG  1 
ATOM   1390 C  CD  . PRO A 1 170 ? -6.654  -22.581 30.499  1.00 54.75  ? 170  PRO A CD  1 
ATOM   1391 N  N   . HIS A 1 171 ? -10.668 -20.043 30.640  1.00 50.88  ? 171  HIS A N   1 
ATOM   1392 C  CA  . HIS A 1 171 ? -12.045 -20.102 31.096  1.00 53.95  ? 171  HIS A CA  1 
ATOM   1393 C  C   . HIS A 1 171 ? -12.659 -21.428 30.646  1.00 55.74  ? 171  HIS A C   1 
ATOM   1394 O  O   . HIS A 1 171 ? -12.290 -21.960 29.593  1.00 51.09  ? 171  HIS A O   1 
ATOM   1395 C  CB  . HIS A 1 171 ? -12.856 -18.924 30.544  1.00 46.87  ? 171  HIS A CB  1 
ATOM   1396 C  CG  . HIS A 1 171 ? -14.202 -18.761 31.181  1.00 48.76  ? 171  HIS A CG  1 
ATOM   1397 N  ND1 . HIS A 1 171 ? -15.274 -19.571 30.876  1.00 54.08  ? 171  HIS A ND1 1 
ATOM   1398 C  CD2 . HIS A 1 171 ? -14.653 -17.872 32.099  1.00 44.51  ? 171  HIS A CD2 1 
ATOM   1399 C  CE1 . HIS A 1 171 ? -16.323 -19.203 31.592  1.00 49.69  ? 171  HIS A CE1 1 
ATOM   1400 N  NE2 . HIS A 1 171 ? -15.974 -18.171 32.338  1.00 46.32  ? 171  HIS A NE2 1 
ATOM   1401 N  N   . PRO A 1 172 ? -13.574 -21.997 31.438  1.00 54.83  ? 172  PRO A N   1 
ATOM   1402 C  CA  . PRO A 1 172 ? -14.265 -23.221 30.996  1.00 50.67  ? 172  PRO A CA  1 
ATOM   1403 C  C   . PRO A 1 172 ? -14.772 -23.134 29.565  1.00 55.78  ? 172  PRO A C   1 
ATOM   1404 O  O   . PRO A 1 172 ? -14.644 -24.095 28.789  1.00 47.69  ? 172  PRO A O   1 
ATOM   1405 C  CB  . PRO A 1 172 ? -15.419 -23.340 32.004  1.00 57.46  ? 172  PRO A CB  1 
ATOM   1406 C  CG  . PRO A 1 172 ? -14.885 -22.701 33.246  1.00 57.11  ? 172  PRO A CG  1 
ATOM   1407 C  CD  . PRO A 1 172 ? -13.962 -21.593 32.802  1.00 53.01  ? 172  PRO A CD  1 
ATOM   1408 N  N   . PHE A 1 173 ? -15.343 -21.990 29.190  1.00 51.47  ? 173  PHE A N   1 
ATOM   1409 C  CA  . PHE A 1 173 ? -15.807 -21.807 27.822  1.00 47.64  ? 173  PHE A CA  1 
ATOM   1410 C  C   . PHE A 1 173 ? -14.693 -22.110 26.829  1.00 50.26  ? 173  PHE A C   1 
ATOM   1411 O  O   . PHE A 1 173 ? -14.844 -22.959 25.944  1.00 55.03  ? 173  PHE A O   1 
ATOM   1412 C  CB  . PHE A 1 173 ? -16.331 -20.383 27.641  1.00 50.73  ? 173  PHE A CB  1 
ATOM   1413 C  CG  . PHE A 1 173 ? -17.260 -20.225 26.473  1.00 52.38  ? 173  PHE A CG  1 
ATOM   1414 C  CD1 . PHE A 1 173 ? -18.612 -20.506 26.601  1.00 48.31  ? 173  PHE A CD1 1 
ATOM   1415 C  CD2 . PHE A 1 173 ? -16.779 -19.789 25.246  1.00 54.23  ? 173  PHE A CD2 1 
ATOM   1416 C  CE1 . PHE A 1 173 ? -19.468 -20.355 25.526  1.00 51.88  ? 173  PHE A CE1 1 
ATOM   1417 C  CE2 . PHE A 1 173 ? -17.635 -19.639 24.164  1.00 46.41  ? 173  PHE A CE2 1 
ATOM   1418 C  CZ  . PHE A 1 173 ? -18.981 -19.923 24.310  1.00 52.26  ? 173  PHE A CZ  1 
ATOM   1419 N  N   . ILE A 1 174 ? -13.549 -21.438 26.983  1.00 47.90  ? 174  ILE A N   1 
ATOM   1420 C  CA  . ILE A 1 174 ? -12.445 -21.607 26.038  1.00 47.48  ? 174  ILE A CA  1 
ATOM   1421 C  C   . ILE A 1 174 ? -12.044 -23.076 25.922  1.00 51.23  ? 174  ILE A C   1 
ATOM   1422 O  O   . ILE A 1 174 ? -11.798 -23.587 24.819  1.00 46.63  ? 174  ILE A O   1 
ATOM   1423 C  CB  . ILE A 1 174 ? -11.248 -20.728 26.452  1.00 51.21  ? 174  ILE A CB  1 
ATOM   1424 C  CG1 . ILE A 1 174 ? -11.571 -19.238 26.267  1.00 45.20  ? 174  ILE A CG1 1 
ATOM   1425 C  CG2 . ILE A 1 174 ? -9.988  -21.144 25.686  1.00 48.86  ? 174  ILE A CG2 1 
ATOM   1426 C  CD1 . ILE A 1 174 ? -11.845 -18.815 24.803  1.00 40.77  ? 174  ILE A CD1 1 
ATOM   1427 N  N   . THR A 1 175 ? -11.961 -23.776 27.057  1.00 49.00  ? 175  THR A N   1 
ATOM   1428 C  CA  . THR A 1 175 ? -11.535 -25.172 27.031  1.00 48.69  ? 175  THR A CA  1 
ATOM   1429 C  C   . THR A 1 175 ? -12.494 -26.017 26.202  1.00 51.16  ? 175  THR A C   1 
ATOM   1430 O  O   . THR A 1 175 ? -12.070 -26.787 25.333  1.00 48.45  ? 175  THR A O   1 
ATOM   1431 C  CB  . THR A 1 175 ? -11.435 -25.719 28.453  1.00 50.52  ? 175  THR A CB  1 
ATOM   1432 O  OG1 . THR A 1 175 ? -10.437 -24.986 29.171  1.00 54.00  ? 175  THR A OG1 1 
ATOM   1433 C  CG2 . THR A 1 175 ? -11.047 -27.191 28.421  1.00 54.33  ? 175  THR A CG2 1 
ATOM   1434 N  N   . SER A 1 176 ? -13.796 -25.884 26.462  1.00 46.34  ? 176  SER A N   1 
ATOM   1435 C  CA  . SER A 1 176 ? -14.790 -26.614 25.685  1.00 53.04  ? 176  SER A CA  1 
ATOM   1436 C  C   . SER A 1 176 ? -14.785 -26.169 24.224  1.00 50.26  ? 176  SER A C   1 
ATOM   1437 O  O   . SER A 1 176 ? -14.808 -27.002 23.312  1.00 48.66  ? 176  SER A O   1 
ATOM   1438 C  CB  . SER A 1 176 ? -16.171 -26.424 26.311  1.00 52.80  ? 176  SER A CB  1 
ATOM   1439 O  OG  . SER A 1 176 ? -16.261 -27.145 27.519  1.00 52.30  ? 176  SER A OG  1 
ATOM   1440 N  N   . MET A 1 177 ? -14.743 -24.855 23.982  1.00 44.46  ? 177  MET A N   1 
ATOM   1441 C  CA  . MET A 1 177 ? -14.793 -24.361 22.609  1.00 43.53  ? 177  MET A CA  1 
ATOM   1442 C  C   . MET A 1 177 ? -13.604 -24.872 21.806  1.00 46.70  ? 177  MET A C   1 
ATOM   1443 O  O   . MET A 1 177 ? -13.760 -25.351 20.674  1.00 45.95  ? 177  MET A O   1 
ATOM   1444 C  CB  . MET A 1 177 ? -14.842 -22.828 22.584  1.00 49.37  ? 177  MET A CB  1 
ATOM   1445 C  CG  . MET A 1 177 ? -14.880 -22.226 21.164  1.00 46.15  ? 177  MET A CG  1 
ATOM   1446 S  SD  . MET A 1 177 ? -14.047 -20.628 20.922  1.00 42.97  ? 177  MET A SD  1 
ATOM   1447 C  CE  . MET A 1 177 ? -12.326 -21.013 21.292  1.00 43.52  ? 177  MET A CE  1 
ATOM   1448 N  N   . VAL A 1 178 ? -12.402 -24.783 22.375  1.00 43.85  ? 178  VAL A N   1 
ATOM   1449 C  CA  . VAL A 1 178 ? -11.238 -25.272 21.645  1.00 49.03  ? 178  VAL A CA  1 
ATOM   1450 C  C   . VAL A 1 178 ? -11.393 -26.760 21.361  1.00 51.98  ? 178  VAL A C   1 
ATOM   1451 O  O   . VAL A 1 178 ? -10.972 -27.252 20.304  1.00 50.65  ? 178  VAL A O   1 
ATOM   1452 C  CB  . VAL A 1 178 ? -9.941  -24.977 22.423  1.00 47.42  ? 178  VAL A CB  1 
ATOM   1453 C  CG1 . VAL A 1 178 ? -8.788  -25.817 21.862  1.00 49.38  ? 178  VAL A CG1 1 
ATOM   1454 C  CG2 . VAL A 1 178 ? -9.629  -23.485 22.402  1.00 48.14  ? 178  VAL A CG2 1 
ATOM   1455 N  N   . ARG A 1 179 ? -12.022 -27.491 22.284  1.00 52.12  ? 179  ARG A N   1 
ATOM   1456 C  CA  . ARG A 1 179 ? -12.202 -28.931 22.122  1.00 51.19  ? 179  ARG A CA  1 
ATOM   1457 C  C   . ARG A 1 179 ? -13.238 -29.243 21.050  1.00 50.86  ? 179  ARG A C   1 
ATOM   1458 O  O   . ARG A 1 179 ? -13.060 -30.178 20.262  1.00 50.51  ? 179  ARG A O   1 
ATOM   1459 C  CB  . ARG A 1 179 ? -12.609 -29.552 23.458  1.00 55.19  ? 179  ARG A CB  1 
ATOM   1460 C  CG  . ARG A 1 179 ? -11.939 -30.873 23.760  1.00 61.76  ? 179  ARG A CG  1 
ATOM   1461 C  CD  . ARG A 1 179 ? -11.658 -31.006 25.255  1.00 65.78  ? 179  ARG A CD  1 
ATOM   1462 N  NE  . ARG A 1 179 ? -12.850 -30.844 26.082  1.00 63.89  ? 179  ARG A NE  1 
ATOM   1463 C  CZ  . ARG A 1 179 ? -12.825 -30.714 27.402  1.00 65.95  ? 179  ARG A CZ  1 
ATOM   1464 N  NH1 . ARG A 1 179 ? -11.682 -30.673 28.072  1.00 66.74  ? 179  ARG A NH1 1 
ATOM   1465 N  NH2 . ARG A 1 179 ? -13.974 -30.616 28.067  1.00 63.54  ? 179  ARG A NH2 1 
ATOM   1466 N  N   . ALA A 1 180 ? -14.333 -28.479 21.018  1.00 49.19  ? 180  ALA A N   1 
ATOM   1467 C  CA  . ALA A 1 180 ? -15.319 -28.640 19.957  1.00 48.37  ? 180  ALA A CA  1 
ATOM   1468 C  C   . ALA A 1 180 ? -14.705 -28.344 18.596  1.00 48.88  ? 180  ALA A C   1 
ATOM   1469 O  O   . ALA A 1 180 ? -14.954 -29.068 17.624  1.00 46.89  ? 180  ALA A O   1 
ATOM   1470 C  CB  . ALA A 1 180 ? -16.520 -27.736 20.219  1.00 46.58  ? 180  ALA A CB  1 
ATOM   1471 N  N   . LEU A 1 181 ? -13.881 -27.294 18.513  1.00 44.09  ? 181  LEU A N   1 
ATOM   1472 C  CA  . LEU A 1 181 ? -13.220 -26.965 17.255  1.00 45.68  ? 181  LEU A CA  1 
ATOM   1473 C  C   . LEU A 1 181 ? -12.228 -28.053 16.869  1.00 46.59  ? 181  LEU A C   1 
ATOM   1474 O  O   . LEU A 1 181 ? -12.151 -28.439 15.697  1.00 45.87  ? 181  LEU A O   1 
ATOM   1475 C  CB  . LEU A 1 181 ? -12.517 -25.607 17.359  1.00 41.65  ? 181  LEU A CB  1 
ATOM   1476 C  CG  . LEU A 1 181 ? -13.411 -24.375 17.533  1.00 41.37  ? 181  LEU A CG  1 
ATOM   1477 C  CD1 . LEU A 1 181 ? -12.574 -23.100 17.691  1.00 44.62  ? 181  LEU A CD1 1 
ATOM   1478 C  CD2 . LEU A 1 181 ? -14.375 -24.246 16.352  1.00 44.65  ? 181  LEU A CD2 1 
ATOM   1479 N  N   A ASP A 1 182 ? -11.453 -28.547 17.840  0.57 46.11  ? 182  ASP A N   1 
ATOM   1480 N  N   B ASP A 1 182 ? -11.460 -28.560 17.838  0.43 46.17  ? 182  ASP A N   1 
ATOM   1481 C  CA  A ASP A 1 182 ? -10.588 -29.697 17.595  0.57 50.31  ? 182  ASP A CA  1 
ATOM   1482 C  CA  B ASP A 1 182 ? -10.582 -29.694 17.565  0.43 50.29  ? 182  ASP A CA  1 
ATOM   1483 C  C   A ASP A 1 182 ? -11.383 -30.847 16.997  0.57 48.62  ? 182  ASP A C   1 
ATOM   1484 C  C   B ASP A 1 182 ? -11.372 -30.869 17.004  0.43 48.63  ? 182  ASP A C   1 
ATOM   1485 O  O   A ASP A 1 182 ? -10.993 -31.435 15.980  0.57 50.17  ? 182  ASP A O   1 
ATOM   1486 O  O   B ASP A 1 182 ? -10.968 -31.494 16.016  0.43 50.15  ? 182  ASP A O   1 
ATOM   1487 C  CB  A ASP A 1 182 ? -9.921  -30.152 18.896  0.57 50.55  ? 182  ASP A CB  1 
ATOM   1488 C  CB  B ASP A 1 182 ? -9.840  -30.115 18.835  0.43 50.57  ? 182  ASP A CB  1 
ATOM   1489 C  CG  A ASP A 1 182 ? -8.817  -29.222 19.345  0.57 55.07  ? 182  ASP A CG  1 
ATOM   1490 C  CG  B ASP A 1 182 ? -8.705  -29.179 19.182  0.43 54.92  ? 182  ASP A CG  1 
ATOM   1491 O  OD1 A ASP A 1 182 ? -8.237  -28.523 18.488  0.57 55.11  ? 182  ASP A OD1 1 
ATOM   1492 O  OD1 B ASP A 1 182 ? -8.192  -28.506 18.264  0.43 55.10  ? 182  ASP A OD1 1 
ATOM   1493 O  OD2 A ASP A 1 182 ? -8.520  -29.201 20.560  0.57 58.13  ? 182  ASP A OD2 1 
ATOM   1494 O  OD2 B ASP A 1 182 ? -8.317  -29.126 20.369  0.43 57.65  ? 182  ASP A OD2 1 
ATOM   1495 N  N   . GLU A 1 183 ? -12.505 -31.187 17.633  1.00 46.59  ? 183  GLU A N   1 
ATOM   1496 C  CA  . GLU A 1 183 ? -13.326 -32.293 17.162  1.00 50.04  ? 183  GLU A CA  1 
ATOM   1497 C  C   . GLU A 1 183 ? -13.824 -32.026 15.746  1.00 48.58  ? 183  GLU A C   1 
ATOM   1498 O  O   . GLU A 1 183 ? -13.849 -32.934 14.902  1.00 46.22  ? 183  GLU A O   1 
ATOM   1499 C  CB  . GLU A 1 183 ? -14.489 -32.512 18.137  1.00 48.03  ? 183  GLU A CB  1 
ATOM   1500 C  CG  . GLU A 1 183 ? -15.614 -33.416 17.638  1.00 54.63  ? 183  GLU A CG  1 
ATOM   1501 C  CD  . GLU A 1 183 ? -15.231 -34.889 17.597  1.00 55.63  ? 183  GLU A CD  1 
ATOM   1502 O  OE1 . GLU A 1 183 ? -14.074 -35.221 17.927  1.00 54.04  ? 183  GLU A OE1 1 
ATOM   1503 O  OE2 . GLU A 1 183 ? -16.085 -35.714 17.205  1.00 52.20  ? 183  GLU A OE2 1 
ATOM   1504 N  N   . ALA A 1 184 ? -14.184 -30.772 15.456  1.00 46.68  ? 184  ALA A N   1 
ATOM   1505 C  CA  . ALA A 1 184 ? -14.676 -30.435 14.126  1.00 43.37  ? 184  ALA A CA  1 
ATOM   1506 C  C   . ALA A 1 184 ? -13.585 -30.619 13.076  1.00 46.10  ? 184  ALA A C   1 
ATOM   1507 O  O   . ALA A 1 184 ? -13.819 -31.246 12.037  1.00 45.12  ? 184  ALA A O   1 
ATOM   1508 C  CB  . ALA A 1 184 ? -15.219 -29.004 14.108  1.00 45.37  ? 184  ALA A CB  1 
ATOM   1509 N  N   . MET A 1 185 ? -12.384 -30.070 13.322  1.00 41.19  ? 185  MET A N   1 
ATOM   1510 C  CA  . MET A 1 185 ? -11.262 -30.312 12.412  1.00 42.95  ? 185  MET A CA  1 
ATOM   1511 C  C   . MET A 1 185 ? -11.014 -31.795 12.208  1.00 46.41  ? 185  MET A C   1 
ATOM   1512 O  O   . MET A 1 185 ? -10.887 -32.266 11.072  1.00 44.14  ? 185  MET A O   1 
ATOM   1513 C  CB  . MET A 1 185 ? -9.953  -29.717 12.925  1.00 44.23  ? 185  MET A CB  1 
ATOM   1514 C  CG  . MET A 1 185 ? -9.023  -29.286 11.782  1.00 38.61  ? 185  MET A CG  1 
ATOM   1515 S  SD  . MET A 1 185 ? -7.661  -28.266 12.345  1.00 43.83  ? 185  MET A SD  1 
ATOM   1516 C  CE  . MET A 1 185 ? -6.785  -29.391 13.436  1.00 48.35  ? 185  MET A CE  1 
ATOM   1517 N  N   . ASN A 1 186 ? -10.826 -32.526 13.310  1.00 46.42  ? 186  ASN A N   1 
ATOM   1518 C  CA  . ASN A 1 186 ? -10.450 -33.929 13.200  1.00 46.03  ? 186  ASN A CA  1 
ATOM   1519 C  C   . ASN A 1 186 ? -11.540 -34.735 12.519  1.00 43.89  ? 186  ASN A C   1 
ATOM   1520 O  O   . ASN A 1 186 ? -11.243 -35.689 11.796  1.00 48.57  ? 186  ASN A O   1 
ATOM   1521 C  CB  . ASN A 1 186 ? -10.150 -34.513 14.584  1.00 48.65  ? 186  ASN A CB  1 
ATOM   1522 C  CG  . ASN A 1 186 ? -9.583  -35.926 14.505  1.00 55.27  ? 186  ASN A CG  1 
ATOM   1523 O  OD1 . ASN A 1 186 ? -10.296 -36.911 14.718  1.00 56.74  ? 186  ASN A OD1 1 
ATOM   1524 N  ND2 . ASN A 1 186 ? -8.290  -36.026 14.201  1.00 51.39  ? 186  ASN A ND2 1 
ATOM   1525 N  N   . LYS A 1 187 ? -12.805 -34.365 12.729  1.00 45.47  ? 187  LYS A N   1 
ATOM   1526 C  CA  . LYS A 1 187 ? -13.904 -35.055 12.067  1.00 46.65  ? 187  LYS A CA  1 
ATOM   1527 C  C   . LYS A 1 187 ? -13.869 -34.881 10.552  1.00 46.57  ? 187  LYS A C   1 
ATOM   1528 O  O   . LYS A 1 187 ? -14.480 -35.682 9.837   1.00 48.73  ? 187  LYS A O   1 
ATOM   1529 C  CB  . LYS A 1 187 ? -15.238 -34.544 12.616  1.00 48.36  ? 187  LYS A CB  1 
ATOM   1530 C  CG  . LYS A 1 187 ? -16.263 -35.615 12.953  1.00 56.49  ? 187  LYS A CG  1 
ATOM   1531 C  CD  . LYS A 1 187 ? -17.659 -35.004 13.036  1.00 55.16  ? 187  LYS A CD  1 
ATOM   1532 C  CE  . LYS A 1 187 ? -17.965 -34.492 14.433  1.00 58.61  ? 187  LYS A CE  1 
ATOM   1533 N  NZ  . LYS A 1 187 ? -19.434 -34.387 14.695  1.00 63.10  ? 187  LYS A NZ  1 
ATOM   1534 N  N   . LEU A 1 188 ? -13.177 -33.851 10.052  1.00 45.10  ? 188  LEU A N   1 
ATOM   1535 C  CA  . LEU A 1 188 ? -13.123 -33.611 8.612   1.00 43.46  ? 188  LEU A CA  1 
ATOM   1536 C  C   . LEU A 1 188 ? -12.602 -34.830 7.858   1.00 45.10  ? 188  LEU A C   1 
ATOM   1537 O  O   . LEU A 1 188 ? -13.049 -35.112 6.742   1.00 46.51  ? 188  LEU A O   1 
ATOM   1538 C  CB  . LEU A 1 188 ? -12.247 -32.389 8.308   1.00 42.45  ? 188  LEU A CB  1 
ATOM   1539 C  CG  . LEU A 1 188 ? -12.770 -31.028 8.786   1.00 44.81  ? 188  LEU A CG  1 
ATOM   1540 C  CD1 . LEU A 1 188 ? -11.755 -29.910 8.512   1.00 44.70  ? 188  LEU A CD1 1 
ATOM   1541 C  CD2 . LEU A 1 188 ? -14.118 -30.721 8.142   1.00 42.04  ? 188  LEU A CD2 1 
ATOM   1542 N  N   . GLN A 1 189 ? -11.651 -35.558 8.437   1.00 52.68  ? 189  GLN A N   1 
ATOM   1543 C  CA  . GLN A 1 189 ? -11.031 -36.681 7.743   1.00 51.93  ? 189  GLN A CA  1 
ATOM   1544 C  C   . GLN A 1 189 ? -11.603 -38.038 8.146   1.00 54.98  ? 189  GLN A C   1 
ATOM   1545 O  O   . GLN A 1 189 ? -11.182 -39.057 7.589   1.00 55.81  ? 189  GLN A O   1 
ATOM   1546 C  CB  . GLN A 1 189 ? -9.510  -36.662 7.964   1.00 50.84  ? 189  GLN A CB  1 
ATOM   1547 C  CG  . GLN A 1 189 ? -9.085  -36.599 9.422   1.00 49.33  ? 189  GLN A CG  1 
ATOM   1548 C  CD  . GLN A 1 189 ? -9.160  -37.943 10.120  1.00 57.84  ? 189  GLN A CD  1 
ATOM   1549 O  OE1 . GLN A 1 189 ? -8.503  -38.903 9.714   1.00 62.01  ? 189  GLN A OE1 1 
ATOM   1550 N  NE2 . GLN A 1 189 ? -9.958  -38.018 11.182  1.00 59.28  ? 189  GLN A NE2 1 
ATOM   1551 N  N   . ARG A 1 190 ? -12.549 -38.085 9.084   1.00 52.68  ? 190  ARG A N   1 
ATOM   1552 C  CA  . ARG A 1 190 ? -13.130 -39.362 9.494   1.00 57.46  ? 190  ARG A CA  1 
ATOM   1553 C  C   . ARG A 1 190 ? -13.995 -39.936 8.381   1.00 60.58  ? 190  ARG A C   1 
ATOM   1554 O  O   . ARG A 1 190 ? -15.008 -39.339 8.003   1.00 62.80  ? 190  ARG A O   1 
ATOM   1555 C  CB  . ARG A 1 190 ? -13.957 -39.195 10.762  1.00 57.98  ? 190  ARG A CB  1 
ATOM   1556 C  CG  . ARG A 1 190 ? -13.183 -39.392 12.027  1.00 60.24  ? 190  ARG A CG  1 
ATOM   1557 C  CD  . ARG A 1 190 ? -14.063 -39.105 13.217  1.00 55.80  ? 190  ARG A CD  1 
ATOM   1558 N  NE  . ARG A 1 190 ? -13.338 -38.369 14.241  1.00 52.42  ? 190  ARG A NE  1 
ATOM   1559 C  CZ  . ARG A 1 190 ? -13.918 -37.758 15.262  1.00 53.32  ? 190  ARG A CZ  1 
ATOM   1560 N  NH1 . ARG A 1 190 ? -15.232 -37.780 15.424  1.00 51.81  ? 190  ARG A NH1 1 
ATOM   1561 N  NH2 . ARG A 1 190 ? -13.164 -37.103 16.137  1.00 55.90  ? 190  ARG A NH2 1 
ATOM   1562 N  N   . ALA A 1 191 ? -13.607 -41.106 7.868   1.00 65.33  ? 191  ALA A N   1 
ATOM   1563 C  CA  . ALA A 1 191 ? -14.390 -41.746 6.817   1.00 67.77  ? 191  ALA A CA  1 
ATOM   1564 C  C   . ALA A 1 191 ? -15.642 -42.427 7.363   1.00 66.32  ? 191  ALA A C   1 
ATOM   1565 O  O   . ALA A 1 191 ? -16.664 -42.479 6.668   1.00 67.53  ? 191  ALA A O   1 
ATOM   1566 C  CB  . ALA A 1 191 ? -13.526 -42.755 6.057   1.00 64.94  ? 191  ALA A CB  1 
ATOM   1567 N  N   . ASN A 1 192 ? -15.590 -42.950 8.593   1.00 66.06  ? 192  ASN A N   1 
ATOM   1568 C  CA  . ASN A 1 192 ? -16.729 -43.607 9.235   1.00 69.34  ? 192  ASN A CA  1 
ATOM   1569 C  C   . ASN A 1 192 ? -17.002 -42.907 10.562  1.00 65.88  ? 192  ASN A C   1 
ATOM   1570 O  O   . ASN A 1 192 ? -16.673 -43.437 11.635  1.00 65.26  ? 192  ASN A O   1 
ATOM   1571 C  CB  . ASN A 1 192 ? -16.476 -45.099 9.451   1.00 69.49  ? 192  ASN A CB  1 
ATOM   1572 C  CG  . ASN A 1 192 ? -15.524 -45.683 8.428   1.00 75.58  ? 192  ASN A CG  1 
ATOM   1573 O  OD1 . ASN A 1 192 ? -14.323 -45.808 8.682   1.00 79.49  ? 192  ASN A OD1 1 
ATOM   1574 N  ND2 . ASN A 1 192 ? -16.050 -46.029 7.256   1.00 70.37  ? 192  ASN A ND2 1 
ATOM   1575 N  N   . PRO A 1 193 ? -17.624 -41.726 10.531  1.00 66.94  ? 193  PRO A N   1 
ATOM   1576 C  CA  . PRO A 1 193 ? -17.850 -40.991 11.786  1.00 66.13  ? 193  PRO A CA  1 
ATOM   1577 C  C   . PRO A 1 193 ? -18.780 -41.704 12.749  1.00 67.36  ? 193  PRO A C   1 
ATOM   1578 O  O   . PRO A 1 193 ? -18.763 -41.389 13.945  1.00 65.77  ? 193  PRO A O   1 
ATOM   1579 C  CB  . PRO A 1 193 ? -18.443 -39.656 11.318  1.00 62.66  ? 193  PRO A CB  1 
ATOM   1580 C  CG  . PRO A 1 193 ? -19.003 -39.917 9.954   1.00 66.78  ? 193  PRO A CG  1 
ATOM   1581 C  CD  . PRO A 1 193 ? -18.428 -41.201 9.414   1.00 63.87  ? 193  PRO A CD  1 
ATOM   1582 N  N   . ASP A 1 194 ? -19.592 -42.647 12.273  1.00 69.20  ? 194  ASP A N   1 
ATOM   1583 C  CA  . ASP A 1 194 ? -20.481 -43.417 13.133  1.00 71.09  ? 194  ASP A CA  1 
ATOM   1584 C  C   . ASP A 1 194 ? -19.854 -44.719 13.616  1.00 70.92  ? 194  ASP A C   1 
ATOM   1585 O  O   . ASP A 1 194 ? -20.547 -45.531 14.238  1.00 73.11  ? 194  ASP A O   1 
ATOM   1586 C  CB  . ASP A 1 194 ? -21.800 -43.708 12.410  1.00 71.93  ? 194  ASP A CB  1 
ATOM   1587 C  CG  . ASP A 1 194 ? -22.651 -42.468 12.229  1.00 75.17  ? 194  ASP A CG  1 
ATOM   1588 O  OD1 . ASP A 1 194 ? -22.528 -41.531 13.049  1.00 77.35  ? 194  ASP A OD1 1 
ATOM   1589 O  OD2 . ASP A 1 194 ? -23.441 -42.427 11.263  1.00 80.92  ? 194  ASP A OD2 1 
ATOM   1590 N  N   . ASP A 1 195 ? -18.572 -44.937 13.346  1.00 69.16  ? 195  ASP A N   1 
ATOM   1591 C  CA  . ASP A 1 195 ? -17.885 -46.094 13.900  1.00 71.35  ? 195  ASP A CA  1 
ATOM   1592 C  C   . ASP A 1 195 ? -17.833 -45.976 15.421  1.00 72.18  ? 195  ASP A C   1 
ATOM   1593 O  O   . ASP A 1 195 ? -17.440 -44.922 15.942  1.00 67.58  ? 195  ASP A O   1 
ATOM   1594 C  CB  . ASP A 1 195 ? -16.467 -46.202 13.339  1.00 70.37  ? 195  ASP A CB  1 
ATOM   1595 C  CG  . ASP A 1 195 ? -15.750 -47.456 13.804  1.00 74.04  ? 195  ASP A CG  1 
ATOM   1596 O  OD1 . ASP A 1 195 ? -16.211 -48.563 13.458  1.00 78.30  ? 195  ASP A OD1 1 
ATOM   1597 O  OD2 . ASP A 1 195 ? -14.732 -47.341 14.518  1.00 74.15  ? 195  ASP A OD2 1 
ATOM   1598 N  N   . PRO A 1 196 ? -18.197 -47.023 16.164  1.00 73.91  ? 196  PRO A N   1 
ATOM   1599 C  CA  . PRO A 1 196 ? -18.215 -46.924 17.633  1.00 71.33  ? 196  PRO A CA  1 
ATOM   1600 C  C   . PRO A 1 196 ? -16.887 -46.494 18.247  1.00 66.73  ? 196  PRO A C   1 
ATOM   1601 O  O   . PRO A 1 196 ? -16.835 -46.160 19.435  1.00 67.50  ? 196  PRO A O   1 
ATOM   1602 C  CB  . PRO A 1 196 ? -18.599 -48.344 18.071  1.00 74.84  ? 196  PRO A CB  1 
ATOM   1603 C  CG  . PRO A 1 196 ? -19.344 -48.908 16.909  1.00 73.85  ? 196  PRO A CG  1 
ATOM   1604 C  CD  . PRO A 1 196 ? -18.685 -48.328 15.688  1.00 75.20  ? 196  PRO A CD  1 
ATOM   1605 N  N   . ALA A 1 197 ? -15.805 -46.499 17.463  1.00 67.28  ? 197  ALA A N   1 
ATOM   1606 C  CA  . ALA A 1 197 ? -14.539 -45.966 17.958  1.00 67.27  ? 197  ALA A CA  1 
ATOM   1607 C  C   . ALA A 1 197 ? -14.650 -44.501 18.365  1.00 63.76  ? 197  ALA A C   1 
ATOM   1608 O  O   . ALA A 1 197 ? -13.850 -44.028 19.180  1.00 62.38  ? 197  ALA A O   1 
ATOM   1609 C  CB  . ALA A 1 197 ? -13.445 -46.128 16.900  1.00 67.00  ? 197  ALA A CB  1 
ATOM   1610 N  N   . TYR A 1 198 ? -15.621 -43.771 17.820  1.00 64.28  ? 198  TYR A N   1 
ATOM   1611 C  CA  . TYR A 1 198 ? -15.793 -42.357 18.122  1.00 62.88  ? 198  TYR A CA  1 
ATOM   1612 C  C   . TYR A 1 198 ? -16.951 -42.107 19.079  1.00 60.82  ? 198  TYR A C   1 
ATOM   1613 O  O   . TYR A 1 198 ? -17.473 -40.989 19.137  1.00 56.13  ? 198  TYR A O   1 
ATOM   1614 C  CB  . TYR A 1 198 ? -15.984 -41.568 16.828  1.00 59.74  ? 198  TYR A CB  1 
ATOM   1615 C  CG  . TYR A 1 198 ? -14.876 -41.800 15.834  1.00 60.91  ? 198  TYR A CG  1 
ATOM   1616 C  CD1 . TYR A 1 198 ? -15.125 -42.433 14.624  1.00 62.24  ? 198  TYR A CD1 1 
ATOM   1617 C  CD2 . TYR A 1 198 ? -13.571 -41.411 16.117  1.00 59.90  ? 198  TYR A CD2 1 
ATOM   1618 C  CE1 . TYR A 1 198 ? -14.109 -42.656 13.712  1.00 63.74  ? 198  TYR A CE1 1 
ATOM   1619 C  CE2 . TYR A 1 198 ? -12.546 -41.632 15.210  1.00 64.32  ? 198  TYR A CE2 1 
ATOM   1620 C  CZ  . TYR A 1 198 ? -12.822 -42.256 14.011  1.00 60.76  ? 198  TYR A CZ  1 
ATOM   1621 O  OH  . TYR A 1 198 ? -11.810 -42.474 13.107  1.00 72.56  ? 198  TYR A OH  1 
ATOM   1622 N  N   . ASP A 1 199 ? -17.369 -43.132 19.823  1.00 59.97  ? 199  ASP A N   1 
ATOM   1623 C  CA  . ASP A 1 199 ? -18.438 -42.939 20.794  1.00 60.40  ? 199  ASP A CA  1 
ATOM   1624 C  C   . ASP A 1 199 ? -18.039 -41.914 21.845  1.00 60.12  ? 199  ASP A C   1 
ATOM   1625 O  O   . ASP A 1 199 ? -18.837 -41.042 22.205  1.00 59.06  ? 199  ASP A O   1 
ATOM   1626 C  CB  . ASP A 1 199 ? -18.801 -44.270 21.452  1.00 65.27  ? 199  ASP A CB  1 
ATOM   1627 C  CG  . ASP A 1 199 ? -19.615 -45.170 20.544  1.00 67.11  ? 199  ASP A CG  1 
ATOM   1628 O  OD1 . ASP A 1 199 ? -20.201 -44.665 19.564  1.00 67.94  ? 199  ASP A OD1 1 
ATOM   1629 O  OD2 . ASP A 1 199 ? -19.677 -46.385 20.820  1.00 70.31  ? 199  ASP A OD2 1 
ATOM   1630 N  N   . GLU A 1 200 ? -16.803 -42.000 22.344  1.00 61.62  ? 200  GLU A N   1 
ATOM   1631 C  CA  . GLU A 1 200 ? -16.348 -41.059 23.363  1.00 62.66  ? 200  GLU A CA  1 
ATOM   1632 C  C   . GLU A 1 200 ? -16.185 -39.658 22.784  1.00 60.01  ? 200  GLU A C   1 
ATOM   1633 O  O   . GLU A 1 200 ? -16.544 -38.670 23.434  1.00 57.67  ? 200  GLU A O   1 
ATOM   1634 C  CB  . GLU A 1 200 ? -15.040 -41.552 23.987  1.00 62.71  ? 200  GLU A CB  1 
ATOM   1635 C  CG  . GLU A 1 200 ? -14.408 -40.609 25.009  1.00 62.23  ? 200  GLU A CG  1 
ATOM   1636 C  CD  . GLU A 1 200 ? -15.322 -40.292 26.187  1.00 68.24  ? 200  GLU A CD  1 
ATOM   1637 O  OE1 . GLU A 1 200 ? -16.326 -41.010 26.391  1.00 69.59  ? 200  GLU A OE1 1 
ATOM   1638 O  OE2 . GLU A 1 200 ? -15.030 -39.322 26.918  1.00 70.98  ? 200  GLU A OE2 1 
ATOM   1639 N  N   . ASN A 1 201 ? -15.640 -39.549 21.569  1.00 59.63  ? 201  ASN A N   1 
ATOM   1640 C  CA  . ASN A 1 201 ? -15.631 -38.258 20.889  1.00 57.89  ? 201  ASN A CA  1 
ATOM   1641 C  C   . ASN A 1 201 ? -17.033 -37.665 20.877  1.00 59.30  ? 201  ASN A C   1 
ATOM   1642 O  O   . ASN A 1 201 ? -17.230 -36.487 21.201  1.00 59.50  ? 201  ASN A O   1 
ATOM   1643 C  CB  . ASN A 1 201 ? -15.104 -38.408 19.459  1.00 61.02  ? 201  ASN A CB  1 
ATOM   1644 C  CG  . ASN A 1 201 ? -13.680 -38.921 19.409  1.00 64.22  ? 201  ASN A CG  1 
ATOM   1645 O  OD1 . ASN A 1 201 ? -13.448 -40.127 19.329  1.00 64.53  ? 201  ASN A OD1 1 
ATOM   1646 N  ND2 . ASN A 1 201 ? -12.715 -38.005 19.450  1.00 62.13  ? 201  ASN A ND2 1 
ATOM   1647 N  N   . LYS A 1 202 ? -18.026 -38.492 20.536  1.00 56.59  ? 202  LYS A N   1 
ATOM   1648 C  CA  . LYS A 1 202 ? -19.409 -38.034 20.482  1.00 57.04  ? 202  LYS A CA  1 
ATOM   1649 C  C   . LYS A 1 202 ? -19.885 -37.557 21.851  1.00 58.54  ? 202  LYS A C   1 
ATOM   1650 O  O   . LYS A 1 202 ? -20.534 -36.510 21.964  1.00 52.11  ? 202  LYS A O   1 
ATOM   1651 C  CB  . LYS A 1 202 ? -20.301 -39.164 19.968  1.00 61.43  ? 202  LYS A CB  1 
ATOM   1652 C  CG  . LYS A 1 202 ? -21.068 -38.849 18.697  1.00 66.33  ? 202  LYS A CG  1 
ATOM   1653 C  CD  . LYS A 1 202 ? -20.123 -38.775 17.506  1.00 72.00  ? 202  LYS A CD  1 
ATOM   1654 C  CE  . LYS A 1 202 ? -20.883 -38.654 16.185  1.00 82.02  ? 202  LYS A CE  1 
ATOM   1655 N  NZ  . LYS A 1 202 ? -20.195 -37.755 15.203  1.00 77.79  ? 202  LYS A NZ  1 
ATOM   1656 N  N   . ARG A 1 203 ? -19.574 -38.317 22.904  1.00 57.28  ? 203  ARG A N   1 
ATOM   1657 C  CA  . ARG A 1 203 ? -19.966 -37.912 24.250  1.00 55.14  ? 203  ARG A CA  1 
ATOM   1658 C  C   . ARG A 1 203 ? -19.256 -36.626 24.663  1.00 57.00  ? 203  ARG A C   1 
ATOM   1659 O  O   . ARG A 1 203 ? -19.885 -35.689 25.168  1.00 58.68  ? 203  ARG A O   1 
ATOM   1660 C  CB  . ARG A 1 203 ? -19.666 -39.036 25.244  1.00 62.92  ? 203  ARG A CB  1 
ATOM   1661 C  CG  . ARG A 1 203 ? -20.320 -38.857 26.613  1.00 66.20  ? 203  ARG A CG  1 
ATOM   1662 C  CD  . ARG A 1 203 ? -19.469 -39.439 27.737  1.00 67.07  ? 203  ARG A CD  1 
ATOM   1663 N  NE  . ARG A 1 203 ? -18.147 -38.825 27.805  1.00 72.29  ? 203  ARG A NE  1 
ATOM   1664 C  CZ  . ARG A 1 203 ? -17.884 -37.677 28.417  1.00 72.97  ? 203  ARG A CZ  1 
ATOM   1665 N  NH1 . ARG A 1 203 ? -18.829 -36.996 29.047  1.00 71.94  ? 203  ARG A NH1 1 
ATOM   1666 N  NH2 . ARG A 1 203 ? -16.641 -37.202 28.399  1.00 72.90  ? 203  ARG A NH2 1 
ATOM   1667 N  N   . GLN A 1 204 ? -17.936 -36.570 24.466  1.00 56.09  ? 204  GLN A N   1 
ATOM   1668 C  CA  . GLN A 1 204 ? -17.184 -35.377 24.841  1.00 59.97  ? 204  GLN A CA  1 
ATOM   1669 C  C   . GLN A 1 204 ? -17.680 -34.156 24.072  1.00 60.94  ? 204  GLN A C   1 
ATOM   1670 O  O   . GLN A 1 204 ? -17.817 -33.065 24.639  1.00 58.83  ? 204  GLN A O   1 
ATOM   1671 C  CB  . GLN A 1 204 ? -15.691 -35.601 24.594  1.00 61.92  ? 204  GLN A CB  1 
ATOM   1672 C  CG  . GLN A 1 204 ? -14.834 -34.373 24.820  1.00 64.08  ? 204  GLN A CG  1 
ATOM   1673 C  CD  . GLN A 1 204 ? -14.824 -33.936 26.276  1.00 67.61  ? 204  GLN A CD  1 
ATOM   1674 O  OE1 . GLN A 1 204 ? -15.460 -32.948 26.652  1.00 65.64  ? 204  GLN A OE1 1 
ATOM   1675 N  NE2 . GLN A 1 204 ? -14.092 -34.673 27.104  1.00 68.42  ? 204  GLN A NE2 1 
ATOM   1676 N  N   . PHE A 1 205 ? -17.957 -34.325 22.776  1.00 59.18  ? 205  PHE A N   1 
ATOM   1677 C  CA  . PHE A 1 205 ? -18.538 -33.249 21.976  1.00 59.47  ? 205  PHE A CA  1 
ATOM   1678 C  C   . PHE A 1 205 ? -19.811 -32.707 22.616  1.00 57.56  ? 205  PHE A C   1 
ATOM   1679 O  O   . PHE A 1 205 ? -19.970 -31.492 22.785  1.00 56.57  ? 205  PHE A O   1 
ATOM   1680 C  CB  . PHE A 1 205 ? -18.819 -33.756 20.560  1.00 55.25  ? 205  PHE A CB  1 
ATOM   1681 C  CG  . PHE A 1 205 ? -19.107 -32.667 19.561  1.00 57.22  ? 205  PHE A CG  1 
ATOM   1682 C  CD1 . PHE A 1 205 ? -18.155 -31.705 19.264  1.00 52.80  ? 205  PHE A CD1 1 
ATOM   1683 C  CD2 . PHE A 1 205 ? -20.325 -32.628 18.896  1.00 55.19  ? 205  PHE A CD2 1 
ATOM   1684 C  CE1 . PHE A 1 205 ? -18.418 -30.712 18.330  1.00 53.17  ? 205  PHE A CE1 1 
ATOM   1685 C  CE2 . PHE A 1 205 ? -20.597 -31.639 17.958  1.00 53.24  ? 205  PHE A CE2 1 
ATOM   1686 C  CZ  . PHE A 1 205 ? -19.646 -30.680 17.676  1.00 51.70  ? 205  PHE A CZ  1 
ATOM   1687 N  N   . GLN A 1 206 ? -20.735 -33.598 22.978  1.00 55.42  ? 206  GLN A N   1 
ATOM   1688 C  CA  . GLN A 1 206 ? -21.970 -33.149 23.612  1.00 58.32  ? 206  GLN A CA  1 
ATOM   1689 C  C   . GLN A 1 206 ? -21.680 -32.449 24.934  1.00 60.11  ? 206  GLN A C   1 
ATOM   1690 O  O   . GLN A 1 206 ? -22.332 -31.457 25.282  1.00 55.30  ? 206  GLN A O   1 
ATOM   1691 C  CB  . GLN A 1 206 ? -22.905 -34.337 23.821  1.00 59.32  ? 206  GLN A CB  1 
ATOM   1692 C  CG  . GLN A 1 206 ? -23.390 -34.933 22.521  1.00 68.58  ? 206  GLN A CG  1 
ATOM   1693 C  CD  . GLN A 1 206 ? -24.031 -33.895 21.621  1.00 70.18  ? 206  GLN A CD  1 
ATOM   1694 O  OE1 . GLN A 1 206 ? -23.891 -33.946 20.397  1.00 70.10  ? 206  GLN A OE1 1 
ATOM   1695 N  NE2 . GLN A 1 206 ? -24.733 -32.939 22.226  1.00 67.59  ? 206  GLN A NE2 1 
ATOM   1696 N  N   . GLU A 1 207 ? -20.690 -32.943 25.677  1.00 62.50  ? 207  GLU A N   1 
ATOM   1697 C  CA  . GLU A 1 207 ? -20.338 -32.331 26.953  1.00 63.16  ? 207  GLU A CA  1 
ATOM   1698 C  C   . GLU A 1 207 ? -19.820 -30.909 26.752  1.00 61.09  ? 207  GLU A C   1 
ATOM   1699 O  O   . GLU A 1 207 ? -20.256 -29.975 27.436  1.00 55.40  ? 207  GLU A O   1 
ATOM   1700 C  CB  . GLU A 1 207 ? -19.312 -33.214 27.671  1.00 66.14  ? 207  GLU A CB  1 
ATOM   1701 C  CG  . GLU A 1 207 ? -18.754 -32.664 28.974  1.00 71.99  ? 207  GLU A CG  1 
ATOM   1702 C  CD  . GLU A 1 207 ? -17.787 -33.638 29.637  1.00 78.44  ? 207  GLU A CD  1 
ATOM   1703 O  OE1 . GLU A 1 207 ? -18.121 -34.842 29.729  1.00 79.37  ? 207  GLU A OE1 1 
ATOM   1704 O  OE2 . GLU A 1 207 ? -16.692 -33.202 30.056  1.00 80.10  ? 207  GLU A OE2 1 
ATOM   1705 N  N   . ASP A 1 208 ? -18.899 -30.720 25.801  1.00 58.42  ? 208  ASP A N   1 
ATOM   1706 C  CA  . ASP A 1 208 ? -18.423 -29.373 25.500  1.00 55.30  ? 208  ASP A CA  1 
ATOM   1707 C  C   . ASP A 1 208 ? -19.534 -28.485 24.956  1.00 56.16  ? 208  ASP A C   1 
ATOM   1708 O  O   . ASP A 1 208 ? -19.496 -27.262 25.149  1.00 52.23  ? 208  ASP A O   1 
ATOM   1709 C  CB  . ASP A 1 208 ? -17.249 -29.425 24.520  1.00 59.31  ? 208  ASP A CB  1 
ATOM   1710 C  CG  . ASP A 1 208 ? -16.081 -30.216 25.058  1.00 59.87  ? 208  ASP A CG  1 
ATOM   1711 O  OD1 . ASP A 1 208 ? -15.995 -30.353 26.295  1.00 63.89  ? 208  ASP A OD1 1 
ATOM   1712 O  OD2 . ASP A 1 208 ? -15.254 -30.700 24.256  1.00 56.33  ? 208  ASP A OD2 1 
ATOM   1713 N  N   . ILE A 1 209 ? -20.527 -29.069 24.280  1.00 56.81  ? 209  ILE A N   1 
ATOM   1714 C  CA  . ILE A 1 209 ? -21.641 -28.264 23.791  1.00 55.02  ? 209  ILE A CA  1 
ATOM   1715 C  C   . ILE A 1 209 ? -22.514 -27.800 24.949  1.00 55.89  ? 209  ILE A C   1 
ATOM   1716 O  O   . ILE A 1 209 ? -23.046 -26.683 24.926  1.00 51.97  ? 209  ILE A O   1 
ATOM   1717 C  CB  . ILE A 1 209 ? -22.451 -29.042 22.736  1.00 56.58  ? 209  ILE A CB  1 
ATOM   1718 C  CG1 . ILE A 1 209 ? -21.671 -29.109 21.411  1.00 49.00  ? 209  ILE A CG1 1 
ATOM   1719 C  CG2 . ILE A 1 209 ? -23.801 -28.393 22.524  1.00 54.05  ? 209  ILE A CG2 1 
ATOM   1720 C  CD1 . ILE A 1 209 ? -22.307 -30.002 20.348  1.00 47.07  ? 209  ILE A CD1 1 
ATOM   1721 N  N   . LYS A 1 210 ? -22.661 -28.623 25.988  1.00 56.08  ? 210  LYS A N   1 
ATOM   1722 C  CA  . LYS A 1 210 ? -23.476 -28.205 27.123  1.00 55.32  ? 210  LYS A CA  1 
ATOM   1723 C  C   . LYS A 1 210 ? -22.766 -27.136 27.951  1.00 54.42  ? 210  LYS A C   1 
ATOM   1724 O  O   . LYS A 1 210 ? -23.411 -26.215 28.463  1.00 52.10  ? 210  LYS A O   1 
ATOM   1725 C  CB  . LYS A 1 210 ? -23.841 -29.413 27.986  1.00 57.62  ? 210  LYS A CB  1 
ATOM   1726 C  CG  . LYS A 1 210 ? -24.472 -29.046 29.326  1.00 64.10  ? 210  LYS A CG  1 
ATOM   1727 C  CD  . LYS A 1 210 ? -24.243 -30.114 30.385  1.00 68.41  ? 210  LYS A CD  1 
ATOM   1728 C  CE  . LYS A 1 210 ? -24.714 -29.632 31.754  1.00 66.49  ? 210  LYS A CE  1 
ATOM   1729 N  NZ  . LYS A 1 210 ? -26.026 -28.924 31.669  1.00 67.53  ? 210  LYS A NZ  1 
ATOM   1730 N  N   . VAL A 1 211 ? -21.439 -27.236 28.085  1.00 50.23  ? 211  VAL A N   1 
ATOM   1731 C  CA  . VAL A 1 211 ? -20.681 -26.202 28.790  1.00 53.65  ? 211  VAL A CA  1 
ATOM   1732 C  C   . VAL A 1 211 ? -20.943 -24.840 28.156  1.00 53.53  ? 211  VAL A C   1 
ATOM   1733 O  O   . VAL A 1 211 ? -21.277 -23.865 28.840  1.00 51.78  ? 211  VAL A O   1 
ATOM   1734 C  CB  . VAL A 1 211 ? -19.177 -26.543 28.794  1.00 54.66  ? 211  VAL A CB  1 
ATOM   1735 C  CG1 . VAL A 1 211 ? -18.338 -25.313 29.152  1.00 52.13  ? 211  VAL A CG1 1 
ATOM   1736 C  CG2 . VAL A 1 211 ? -18.883 -27.678 29.763  1.00 52.58  ? 211  VAL A CG2 1 
ATOM   1737 N  N   . MET A 1 212 ? -20.816 -24.762 26.827  1.00 53.37  ? 212  MET A N   1 
ATOM   1738 C  CA  . MET A 1 212 ? -21.012 -23.491 26.137  1.00 52.81  ? 212  MET A CA  1 
ATOM   1739 C  C   . MET A 1 212 ? -22.451 -23.001 26.273  1.00 51.83  ? 212  MET A C   1 
ATOM   1740 O  O   . MET A 1 212 ? -22.689 -21.797 26.429  1.00 51.88  ? 212  MET A O   1 
ATOM   1741 C  CB  . MET A 1 212 ? -20.607 -23.621 24.663  1.00 54.07  ? 212  MET A CB  1 
ATOM   1742 C  CG  . MET A 1 212 ? -19.090 -23.536 24.435  1.00 52.52  ? 212  MET A CG  1 
ATOM   1743 S  SD  . MET A 1 212 ? -18.575 -23.878 22.732  1.00 55.60  ? 212  MET A SD  1 
ATOM   1744 C  CE  . MET A 1 212 ? -20.106 -24.578 22.116  1.00 54.80  ? 212  MET A CE  1 
ATOM   1745 N  N   . ASN A 1 213 ? -23.424 -23.917 26.232  1.00 46.94  ? 213  ASN A N   1 
ATOM   1746 C  CA  . ASN A 1 213 ? -24.830 -23.523 26.336  1.00 50.13  ? 213  ASN A CA  1 
ATOM   1747 C  C   . ASN A 1 213 ? -25.201 -23.099 27.752  1.00 56.04  ? 213  ASN A C   1 
ATOM   1748 O  O   . ASN A 1 213 ? -26.145 -22.318 27.940  1.00 54.08  ? 213  ASN A O   1 
ATOM   1749 C  CB  . ASN A 1 213 ? -25.733 -24.668 25.884  1.00 48.96  ? 213  ASN A CB  1 
ATOM   1750 C  CG  . ASN A 1 213 ? -26.175 -24.528 24.447  1.00 60.71  ? 213  ASN A CG  1 
ATOM   1751 O  OD1 . ASN A 1 213 ? -27.292 -24.090 24.173  1.00 63.30  ? 213  ASN A OD1 1 
ATOM   1752 N  ND2 . ASN A 1 213 ? -25.302 -24.901 23.516  1.00 55.59  ? 213  ASN A ND2 1 
ATOM   1753 N  N   . ASP A 1 214 ? -24.488 -23.612 28.757  1.00 54.43  ? 214  ASP A N   1 
ATOM   1754 C  CA  . ASP A 1 214 ? -24.752 -23.205 30.133  1.00 55.20  ? 214  ASP A CA  1 
ATOM   1755 C  C   . ASP A 1 214 ? -24.347 -21.756 30.366  1.00 51.19  ? 214  ASP A C   1 
ATOM   1756 O  O   . ASP A 1 214 ? -25.049 -21.015 31.060  1.00 50.31  ? 214  ASP A O   1 
ATOM   1757 C  CB  . ASP A 1 214 ? -24.023 -24.134 31.103  1.00 54.38  ? 214  ASP A CB  1 
ATOM   1758 C  CG  . ASP A 1 214 ? -24.663 -25.507 31.183  1.00 53.32  ? 214  ASP A CG  1 
ATOM   1759 O  OD1 . ASP A 1 214 ? -25.774 -25.670 30.637  1.00 56.86  ? 214  ASP A OD1 1 
ATOM   1760 O  OD2 . ASP A 1 214 ? -24.059 -26.419 31.787  1.00 59.50  ? 214  ASP A OD2 1 
ATOM   1761 N  N   . LEU A 1 215 ? -23.217 -21.332 29.795  1.00 53.97  ? 215  LEU A N   1 
ATOM   1762 C  CA  . LEU A 1 215 ? -22.829 -19.932 29.909  1.00 52.13  ? 215  LEU A CA  1 
ATOM   1763 C  C   . LEU A 1 215 ? -23.826 -19.036 29.190  1.00 49.16  ? 215  LEU A C   1 
ATOM   1764 O  O   . LEU A 1 215 ? -24.140 -17.937 29.663  1.00 50.51  ? 215  LEU A O   1 
ATOM   1765 C  CB  . LEU A 1 215 ? -21.425 -19.716 29.350  1.00 54.59  ? 215  LEU A CB  1 
ATOM   1766 C  CG  . LEU A 1 215 ? -21.064 -18.230 29.320  1.00 51.76  ? 215  LEU A CG  1 
ATOM   1767 C  CD1 . LEU A 1 215 ? -20.204 -17.895 30.530  1.00 53.16  ? 215  LEU A CD1 1 
ATOM   1768 C  CD2 . LEU A 1 215 ? -20.352 -17.860 28.039  1.00 51.54  ? 215  LEU A CD2 1 
ATOM   1769 N  N   . VAL A 1 216 ? -24.333 -19.493 28.040  1.00 51.95  ? 216  VAL A N   1 
ATOM   1770 C  CA  . VAL A 1 216 ? -25.352 -18.739 27.313  1.00 51.55  ? 216  VAL A CA  1 
ATOM   1771 C  C   . VAL A 1 216 ? -26.589 -18.541 28.177  1.00 54.33  ? 216  VAL A C   1 
ATOM   1772 O  O   . VAL A 1 216 ? -27.181 -17.454 28.199  1.00 52.18  ? 216  VAL A O   1 
ATOM   1773 C  CB  . VAL A 1 216 ? -25.691 -19.447 25.989  1.00 50.25  ? 216  VAL A CB  1 
ATOM   1774 C  CG1 . VAL A 1 216 ? -26.953 -18.870 25.390  1.00 44.51  ? 216  VAL A CG1 1 
ATOM   1775 C  CG2 . VAL A 1 216 ? -24.526 -19.316 25.032  1.00 46.08  ? 216  VAL A CG2 1 
ATOM   1776 N  N   . ASP A 1 217 ? -27.008 -19.588 28.895  1.00 56.12  ? 217  ASP A N   1 
ATOM   1777 C  CA  . ASP A 1 217 ? -28.116 -19.447 29.838  1.00 54.28  ? 217  ASP A CA  1 
ATOM   1778 C  C   . ASP A 1 217 ? -27.868 -18.294 30.804  1.00 54.03  ? 217  ASP A C   1 
ATOM   1779 O  O   . ASP A 1 217 ? -28.722 -17.415 30.982  1.00 49.96  ? 217  ASP A O   1 
ATOM   1780 C  CB  . ASP A 1 217 ? -28.312 -20.751 30.620  1.00 58.20  ? 217  ASP A CB  1 
ATOM   1781 C  CG  . ASP A 1 217 ? -28.538 -21.951 29.722  1.00 60.56  ? 217  ASP A CG  1 
ATOM   1782 O  OD1 . ASP A 1 217 ? -28.910 -21.752 28.547  1.00 62.40  ? 217  ASP A OD1 1 
ATOM   1783 O  OD2 . ASP A 1 217 ? -28.321 -23.092 30.192  1.00 61.30  ? 217  ASP A OD2 1 
ATOM   1784 N  N   . LYS A 1 218 ? -26.693 -18.294 31.441  1.00 55.67  ? 218  LYS A N   1 
ATOM   1785 C  CA  . LYS A 1 218 ? -26.373 -17.300 32.463  1.00 54.93  ? 218  LYS A CA  1 
ATOM   1786 C  C   . LYS A 1 218 ? -26.340 -15.898 31.874  1.00 54.66  ? 218  LYS A C   1 
ATOM   1787 O  O   . LYS A 1 218 ? -26.874 -14.951 32.467  1.00 53.14  ? 218  LYS A O   1 
ATOM   1788 C  CB  . LYS A 1 218 ? -25.033 -17.650 33.117  1.00 54.99  ? 218  LYS A CB  1 
ATOM   1789 C  CG  . LYS A 1 218 ? -24.491 -16.619 34.121  1.00 54.60  ? 218  LYS A CG  1 
ATOM   1790 C  CD  . LYS A 1 218 ? -25.423 -16.435 35.314  1.00 60.42  ? 218  LYS A CD  1 
ATOM   1791 C  CE  . LYS A 1 218 ? -24.656 -16.001 36.571  1.00 60.92  ? 218  LYS A CE  1 
ATOM   1792 N  NZ  . LYS A 1 218 ? -23.922 -14.707 36.397  1.00 48.99  ? 218  LYS A NZ  1 
ATOM   1793 N  N   . ILE A 1 219 ? -25.724 -15.739 30.703  1.00 45.23  ? 219  ILE A N   1 
ATOM   1794 C  CA  . ILE A 1 219 ? -25.732 -14.429 30.068  1.00 44.99  ? 219  ILE A CA  1 
ATOM   1795 C  C   . ILE A 1 219 ? -27.163 -13.958 29.849  1.00 48.10  ? 219  ILE A C   1 
ATOM   1796 O  O   . ILE A 1 219 ? -27.492 -12.790 30.095  1.00 50.59  ? 219  ILE A O   1 
ATOM   1797 C  CB  . ILE A 1 219 ? -24.931 -14.459 28.754  1.00 45.19  ? 219  ILE A CB  1 
ATOM   1798 C  CG1 . ILE A 1 219 ? -23.435 -14.595 29.056  1.00 41.65  ? 219  ILE A CG1 1 
ATOM   1799 C  CG2 . ILE A 1 219 ? -25.231 -13.212 27.939  1.00 46.20  ? 219  ILE A CG2 1 
ATOM   1800 C  CD1 . ILE A 1 219 ? -22.579 -14.937 27.833  1.00 38.71  ? 219  ILE A CD1 1 
ATOM   1801 N  N   . ILE A 1 220 ? -28.045 -14.859 29.409  1.00 50.03  ? 220  ILE A N   1 
ATOM   1802 C  CA  . ILE A 1 220 ? -29.424 -14.453 29.151  1.00 47.44  ? 220  ILE A CA  1 
ATOM   1803 C  C   . ILE A 1 220 ? -30.155 -14.163 30.454  1.00 53.79  ? 220  ILE A C   1 
ATOM   1804 O  O   . ILE A 1 220 ? -30.872 -13.159 30.566  1.00 54.08  ? 220  ILE A O   1 
ATOM   1805 C  CB  . ILE A 1 220 ? -30.159 -15.513 28.316  1.00 49.56  ? 220  ILE A CB  1 
ATOM   1806 C  CG1 . ILE A 1 220 ? -29.674 -15.456 26.861  1.00 50.27  ? 220  ILE A CG1 1 
ATOM   1807 C  CG2 . ILE A 1 220 ? -31.662 -15.280 28.399  1.00 54.62  ? 220  ILE A CG2 1 
ATOM   1808 C  CD1 . ILE A 1 220 ? -30.313 -16.483 25.945  1.00 51.60  ? 220  ILE A CD1 1 
ATOM   1809 N  N   . ALA A 1 221 ? -29.995 -15.033 31.455  1.00 55.95  ? 221  ALA A N   1 
ATOM   1810 C  CA  . ALA A 1 221 ? -30.660 -14.825 32.741  1.00 60.12  ? 221  ALA A CA  1 
ATOM   1811 C  C   . ALA A 1 221 ? -30.292 -13.474 33.348  1.00 60.19  ? 221  ALA A C   1 
ATOM   1812 O  O   . ALA A 1 221 ? -31.173 -12.690 33.722  1.00 60.91  ? 221  ALA A O   1 
ATOM   1813 C  CB  . ALA A 1 221 ? -30.309 -15.958 33.708  1.00 57.42  ? 221  ALA A CB  1 
ATOM   1814 N  N   . ASP A 1 222 ? -28.989 -13.187 33.461  1.00 57.11  ? 222  ASP A N   1 
ATOM   1815 C  CA  . ASP A 1 222 ? -28.560 -11.941 34.093  1.00 58.00  ? 222  ASP A CA  1 
ATOM   1816 C  C   . ASP A 1 222 ? -29.094 -10.717 33.360  1.00 60.02  ? 222  ASP A C   1 
ATOM   1817 O  O   . ASP A 1 222 ? -29.457 -9.717  33.993  1.00 56.22  ? 222  ASP A O   1 
ATOM   1818 C  CB  . ASP A 1 222 ? -27.034 -11.881 34.196  1.00 57.05  ? 222  ASP A CB  1 
ATOM   1819 C  CG  . ASP A 1 222 ? -26.441 -13.104 34.875  1.00 59.46  ? 222  ASP A CG  1 
ATOM   1820 O  OD1 . ASP A 1 222 ? -27.206 -13.854 35.522  1.00 56.02  ? 222  ASP A OD1 1 
ATOM   1821 O  OD2 . ASP A 1 222 ? -25.206 -13.295 34.792  1.00 55.28  ? 222  ASP A OD2 1 
ATOM   1822 N  N   . ARG A 1 223 ? -29.152 -10.766 32.028  1.00 55.63  ? 223  ARG A N   1 
ATOM   1823 C  CA  . ARG A 1 223 ? -29.646 -9.608  31.290  1.00 55.23  ? 223  ARG A CA  1 
ATOM   1824 C  C   . ARG A 1 223 ? -31.124 -9.361  31.571  1.00 57.86  ? 223  ARG A C   1 
ATOM   1825 O  O   . ARG A 1 223 ? -31.522 -8.236  31.891  1.00 60.55  ? 223  ARG A O   1 
ATOM   1826 C  CB  . ARG A 1 223 ? -29.417 -9.784  29.791  1.00 52.30  ? 223  ARG A CB  1 
ATOM   1827 C  CG  . ARG A 1 223 ? -30.033 -8.666  28.975  1.00 49.31  ? 223  ARG A CG  1 
ATOM   1828 C  CD  . ARG A 1 223 ? -29.442 -7.326  29.384  1.00 51.52  ? 223  ARG A CD  1 
ATOM   1829 N  NE  . ARG A 1 223 ? -27.999 -7.272  29.173  1.00 46.37  ? 223  ARG A NE  1 
ATOM   1830 C  CZ  . ARG A 1 223 ? -27.410 -6.688  28.136  1.00 49.74  ? 223  ARG A CZ  1 
ATOM   1831 N  NH1 . ARG A 1 223 ? -28.112 -6.091  27.183  1.00 40.54  ? 223  ARG A NH1 1 
ATOM   1832 N  NH2 . ARG A 1 223 ? -26.078 -6.695  28.056  1.00 41.57  ? 223  ARG A NH2 1 
ATOM   1833 N  N   . LYS A 1 224 ? -31.960 -10.398 31.447  1.00 52.16  ? 224  LYS A N   1 
ATOM   1834 C  CA  . LYS A 1 224 ? -33.400 -10.189 31.587  1.00 64.73  ? 224  LYS A CA  1 
ATOM   1835 C  C   . LYS A 1 224 ? -33.806 -9.884  33.026  1.00 69.34  ? 224  LYS A C   1 
ATOM   1836 O  O   . LYS A 1 224 ? -34.874 -9.301  33.247  1.00 73.46  ? 224  LYS A O   1 
ATOM   1837 C  CB  . LYS A 1 224 ? -34.170 -11.405 31.064  1.00 63.63  ? 224  LYS A CB  1 
ATOM   1838 C  CG  . LYS A 1 224 ? -33.785 -12.725 31.711  1.00 65.38  ? 224  LYS A CG  1 
ATOM   1839 C  CD  . LYS A 1 224 ? -34.584 -13.868 31.105  1.00 65.24  ? 224  LYS A CD  1 
ATOM   1840 C  CE  . LYS A 1 224 ? -33.829 -15.184 31.177  1.00 61.12  ? 224  LYS A CE  1 
ATOM   1841 N  NZ  . LYS A 1 224 ? -34.223 -16.084 30.055  1.00 66.65  ? 224  LYS A NZ  1 
ATOM   1842 N  N   . ALA A 1 225 ? -32.983 -10.259 34.003  1.00 66.99  ? 225  ALA A N   1 
ATOM   1843 C  CA  . ALA A 1 225 ? -33.226 -9.901  35.393  1.00 70.34  ? 225  ALA A CA  1 
ATOM   1844 C  C   . ALA A 1 225 ? -32.515 -8.618  35.806  1.00 75.84  ? 225  ALA A C   1 
ATOM   1845 O  O   . ALA A 1 225 ? -32.846 -8.055  36.854  1.00 81.23  ? 225  ALA A O   1 
ATOM   1846 C  CB  . ALA A 1 225 ? -32.796 -11.047 36.318  1.00 65.71  ? 225  ALA A CB  1 
ATOM   1847 N  N   . SER A 1 226 ? -31.557 -8.147  35.010  1.00 77.14  ? 226  SER A N   1 
ATOM   1848 C  CA  . SER A 1 226 ? -30.786 -6.960  35.351  1.00 81.29  ? 226  SER A CA  1 
ATOM   1849 C  C   . SER A 1 226 ? -31.694 -5.748  35.531  1.00 89.27  ? 226  SER A C   1 
ATOM   1850 O  O   . SER A 1 226 ? -32.810 -5.685  35.006  1.00 87.30  ? 226  SER A O   1 
ATOM   1851 C  CB  . SER A 1 226 ? -29.746 -6.670  34.266  1.00 77.73  ? 226  SER A CB  1 
ATOM   1852 O  OG  . SER A 1 226 ? -29.122 -5.414  34.473  1.00 86.06  ? 226  SER A OG  1 
ATOM   1853 N  N   . GLY A 1 227 ? -31.189 -4.772  36.285  1.00 94.82  ? 227  GLY A N   1 
ATOM   1854 C  CA  . GLY A 1 227 ? -31.868 -3.506  36.478  1.00 97.20  ? 227  GLY A CA  1 
ATOM   1855 C  C   . GLY A 1 227 ? -31.117 -2.358  35.835  1.00 101.87 ? 227  GLY A C   1 
ATOM   1856 O  O   . GLY A 1 227 ? -31.537 -1.199  35.922  1.00 103.16 ? 227  GLY A O   1 
ATOM   1857 N  N   . GLU A 1 228 ? -29.994 -2.674  35.194  1.00 101.88 ? 228  GLU A N   1 
ATOM   1858 C  CA  . GLU A 1 228 ? -29.220 -1.700  34.438  1.00 102.36 ? 228  GLU A CA  1 
ATOM   1859 C  C   . GLU A 1 228 ? -29.750 -1.606  33.012  1.00 98.66  ? 228  GLU A C   1 
ATOM   1860 O  O   . GLU A 1 228 ? -30.213 -2.592  32.433  1.00 97.43  ? 228  GLU A O   1 
ATOM   1861 C  CB  . GLU A 1 228 ? -27.735 -2.076  34.415  1.00 102.30 ? 228  GLU A CB  1 
ATOM   1862 C  CG  . GLU A 1 228 ? -27.146 -2.483  35.767  1.00 105.70 ? 228  GLU A CG  1 
ATOM   1863 C  CD  . GLU A 1 228 ? -27.101 -1.340  36.768  1.00 105.76 ? 228  GLU A CD  1 
ATOM   1864 O  OE1 . GLU A 1 228 ? -26.831 -0.193  36.354  1.00 101.79 ? 228  GLU A OE1 1 
ATOM   1865 O  OE2 . GLU A 1 228 ? -27.328 -1.592  37.971  1.00 108.59 ? 228  GLU A OE2 1 
ATOM   1866 N  N   . GLN A 1 229 ? -29.674 -0.404  32.446  1.00 97.50  ? 229  GLN A N   1 
ATOM   1867 C  CA  . GLN A 1 229 ? -30.166 -0.140  31.095  1.00 93.70  ? 229  GLN A CA  1 
ATOM   1868 C  C   . GLN A 1 229 ? -28.995 -0.259  30.126  1.00 89.72  ? 229  GLN A C   1 
ATOM   1869 O  O   . GLN A 1 229 ? -28.147 0.635   30.044  1.00 86.42  ? 229  GLN A O   1 
ATOM   1870 C  CB  . GLN A 1 229 ? -30.826 1.232   31.018  1.00 94.34  ? 229  GLN A CB  1 
ATOM   1871 C  CG  . GLN A 1 229 ? -32.084 1.341   31.861  1.00 100.58 ? 229  GLN A CG  1 
ATOM   1872 C  CD  . GLN A 1 229 ? -33.303 0.779   31.157  1.00 102.37 ? 229  GLN A CD  1 
ATOM   1873 O  OE1 . GLN A 1 229 ? -33.804 -0.287  31.515  1.00 102.80 ? 229  GLN A OE1 1 
ATOM   1874 N  NE2 . GLN A 1 229 ? -33.787 1.494   30.147  1.00 105.57 ? 229  GLN A NE2 1 
ATOM   1875 N  N   . SER A 1 230 ? -28.956 -1.365  29.387  1.00 82.63  ? 230  SER A N   1 
ATOM   1876 C  CA  . SER A 1 230 ? -27.875 -1.654  28.458  1.00 70.47  ? 230  SER A CA  1 
ATOM   1877 C  C   . SER A 1 230 ? -28.294 -1.328  27.030  1.00 64.04  ? 230  SER A C   1 
ATOM   1878 O  O   . SER A 1 230 ? -29.480 -1.339  26.688  1.00 62.13  ? 230  SER A O   1 
ATOM   1879 C  CB  . SER A 1 230 ? -27.452 -3.125  28.551  1.00 66.21  ? 230  SER A CB  1 
ATOM   1880 O  OG  . SER A 1 230 ? -26.761 -3.394  29.761  1.00 64.96  ? 230  SER A OG  1 
ATOM   1881 N  N   . ASP A 1 231 ? -27.294 -1.021  26.193  1.00 58.82  ? 231  ASP A N   1 
ATOM   1882 C  CA  . ASP A 1 231 ? -27.492 -0.812  24.759  1.00 56.80  ? 231  ASP A CA  1 
ATOM   1883 C  C   . ASP A 1 231 ? -26.308 -1.474  24.058  1.00 58.56  ? 231  ASP A C   1 
ATOM   1884 O  O   . ASP A 1 231 ? -25.373 -0.811  23.601  1.00 62.28  ? 231  ASP A O   1 
ATOM   1885 C  CB  . ASP A 1 231 ? -27.603 0.665   24.398  1.00 60.87  ? 231  ASP A CB  1 
ATOM   1886 C  CG  . ASP A 1 231 ? -27.955 0.880   22.934  1.00 68.61  ? 231  ASP A CG  1 
ATOM   1887 O  OD1 . ASP A 1 231 ? -28.433 -0.077  22.288  1.00 66.93  ? 231  ASP A OD1 1 
ATOM   1888 O  OD2 . ASP A 1 231 ? -27.747 2.002   22.425  1.00 76.13  ? 231  ASP A OD2 1 
ATOM   1889 N  N   . ASP A 1 232 ? -26.345 -2.803  23.984  1.00 50.01  ? 232  ASP A N   1 
ATOM   1890 C  CA  . ASP A 1 232 ? -25.246 -3.536  23.372  1.00 45.97  ? 232  ASP A CA  1 
ATOM   1891 C  C   . ASP A 1 232 ? -25.756 -4.601  22.411  1.00 48.21  ? 232  ASP A C   1 
ATOM   1892 O  O   . ASP A 1 232 ? -26.929 -4.590  22.018  1.00 43.44  ? 232  ASP A O   1 
ATOM   1893 C  CB  . ASP A 1 232 ? -24.351 -4.148  24.453  1.00 43.17  ? 232  ASP A CB  1 
ATOM   1894 C  CG  . ASP A 1 232 ? -25.093 -5.122  25.371  1.00 41.13  ? 232  ASP A CG  1 
ATOM   1895 O  OD1 . ASP A 1 232 ? -26.218 -5.564  25.047  1.00 42.31  ? 232  ASP A OD1 1 
ATOM   1896 O  OD2 . ASP A 1 232 ? -24.535 -5.453  26.436  1.00 41.64  ? 232  ASP A OD2 1 
ATOM   1897 N  N   . LEU A 1 233 ? -24.868 -5.515  22.015  1.00 43.68  ? 233  LEU A N   1 
ATOM   1898 C  CA  . LEU A 1 233 ? -25.239 -6.547  21.054  1.00 37.20  ? 233  LEU A CA  1 
ATOM   1899 C  C   . LEU A 1 233 ? -26.426 -7.362  21.561  1.00 39.94  ? 233  LEU A C   1 
ATOM   1900 O  O   . LEU A 1 233 ? -27.398 -7.595  20.829  1.00 38.03  ? 233  LEU A O   1 
ATOM   1901 C  CB  . LEU A 1 233 ? -24.014 -7.430  20.785  1.00 37.39  ? 233  LEU A CB  1 
ATOM   1902 C  CG  . LEU A 1 233 ? -24.017 -8.538  19.751  1.00 41.15  ? 233  LEU A CG  1 
ATOM   1903 C  CD1 . LEU A 1 233 ? -24.396 -8.029  18.357  1.00 41.93  ? 233  LEU A CD1 1 
ATOM   1904 C  CD2 . LEU A 1 233 ? -22.625 -9.165  19.733  1.00 39.26  ? 233  LEU A CD2 1 
ATOM   1905 N  N   . LEU A 1 234 ? -26.384 -7.770  22.827  1.00 38.72  ? 234  LEU A N   1 
ATOM   1906 C  CA  . LEU A 1 234 ? -27.474 -8.560  23.388  1.00 33.51  ? 234  LEU A CA  1 
ATOM   1907 C  C   . LEU A 1 234 ? -28.787 -7.783  23.380  1.00 42.32  ? 234  LEU A C   1 
ATOM   1908 O  O   . LEU A 1 234 ? -29.861 -8.358  23.148  1.00 41.42  ? 234  LEU A O   1 
ATOM   1909 C  CB  . LEU A 1 234 ? -27.123 -8.981  24.812  1.00 39.98  ? 234  LEU A CB  1 
ATOM   1910 C  CG  . LEU A 1 234 ? -28.132 -9.916  25.469  1.00 39.83  ? 234  LEU A CG  1 
ATOM   1911 C  CD1 . LEU A 1 234 ? -28.392 -11.114 24.594  1.00 40.29  ? 234  LEU A CD1 1 
ATOM   1912 C  CD2 . LEU A 1 234 ? -27.637 -10.338 26.857  1.00 45.62  ? 234  LEU A CD2 1 
ATOM   1913 N  N   . THR A 1 235 ? -28.725 -6.476  23.661  1.00 40.62  ? 235  THR A N   1 
ATOM   1914 C  CA  . THR A 1 235 ? -29.930 -5.651  23.594  1.00 42.52  ? 235  THR A CA  1 
ATOM   1915 C  C   . THR A 1 235 ? -30.575 -5.750  22.226  1.00 42.58  ? 235  THR A C   1 
ATOM   1916 O  O   . THR A 1 235 ? -31.802 -5.864  22.113  1.00 43.12  ? 235  THR A O   1 
ATOM   1917 C  CB  . THR A 1 235 ? -29.599 -4.191  23.888  1.00 43.20  ? 235  THR A CB  1 
ATOM   1918 O  OG1 . THR A 1 235 ? -28.929 -4.095  25.148  1.00 42.32  ? 235  THR A OG1 1 
ATOM   1919 C  CG2 . THR A 1 235 ? -30.882 -3.366  23.932  1.00 41.84  ? 235  THR A CG2 1 
ATOM   1920 N  N   . HIS A 1 236 ? -29.759 -5.696  21.173  1.00 40.20  ? 236  HIS A N   1 
ATOM   1921 C  CA  . HIS A 1 236 ? -30.282 -5.785  19.818  1.00 42.55  ? 236  HIS A CA  1 
ATOM   1922 C  C   . HIS A 1 236 ? -30.865 -7.172  19.556  1.00 43.10  ? 236  HIS A C   1 
ATOM   1923 O  O   . HIS A 1 236 ? -31.901 -7.298  18.896  1.00 41.67  ? 236  HIS A O   1 
ATOM   1924 C  CB  . HIS A 1 236 ? -29.164 -5.481  18.821  1.00 38.94  ? 236  HIS A CB  1 
ATOM   1925 C  CG  . HIS A 1 236 ? -28.985 -4.021  18.544  1.00 44.91  ? 236  HIS A CG  1 
ATOM   1926 N  ND1 . HIS A 1 236 ? -28.283 -3.195  19.399  1.00 48.91  ? 236  HIS A ND1 1 
ATOM   1927 C  CD2 . HIS A 1 236 ? -29.412 -3.234  17.527  1.00 52.21  ? 236  HIS A CD2 1 
ATOM   1928 C  CE1 . HIS A 1 236 ? -28.284 -1.964  18.918  1.00 46.31  ? 236  HIS A CE1 1 
ATOM   1929 N  NE2 . HIS A 1 236 ? -28.959 -1.960  17.782  1.00 45.68  ? 236  HIS A NE2 1 
ATOM   1930 N  N   . MET A 1 237 ? -30.217 -8.232  20.063  1.00 40.10  ? 237  MET A N   1 
ATOM   1931 C  CA  . MET A 1 237 ? -30.757 -9.577  19.857  1.00 39.10  ? 237  MET A CA  1 
ATOM   1932 C  C   . MET A 1 237 ? -32.154 -9.691  20.467  1.00 42.06  ? 237  MET A C   1 
ATOM   1933 O  O   . MET A 1 237 ? -33.068 -10.256 19.853  1.00 43.54  ? 237  MET A O   1 
ATOM   1934 C  CB  . MET A 1 237 ? -29.859 -10.676 20.461  1.00 34.05  ? 237  MET A CB  1 
ATOM   1935 C  CG  . MET A 1 237 ? -28.735 -11.317 19.549  1.00 38.32  ? 237  MET A CG  1 
ATOM   1936 S  SD  . MET A 1 237 ? -27.339 -11.883 20.576  1.00 39.33  ? 237  MET A SD  1 
ATOM   1937 C  CE  . MET A 1 237 ? -25.897 -11.822 19.500  1.00 35.95  ? 237  MET A CE  1 
ATOM   1938 N  N   . LEU A 1 238 ? -32.342 -9.137  21.673  1.00 41.07  ? 238  LEU A N   1 
ATOM   1939 C  CA  . LEU A 1 238 ? -33.577 -9.328  22.426  1.00 41.51  ? 238  LEU A CA  1 
ATOM   1940 C  C   . LEU A 1 238 ? -34.681 -8.363  22.015  1.00 43.40  ? 238  LEU A C   1 
ATOM   1941 O  O   . LEU A 1 238 ? -35.862 -8.679  22.194  1.00 47.03  ? 238  LEU A O   1 
ATOM   1942 C  CB  . LEU A 1 238 ? -33.303 -9.194  23.935  1.00 42.05  ? 238  LEU A CB  1 
ATOM   1943 C  CG  . LEU A 1 238 ? -32.275 -10.168 24.532  1.00 44.94  ? 238  LEU A CG  1 
ATOM   1944 C  CD1 . LEU A 1 238 ? -31.809 -9.771  25.946  1.00 40.15  ? 238  LEU A CD1 1 
ATOM   1945 C  CD2 . LEU A 1 238 ? -32.847 -11.577 24.548  1.00 46.87  ? 238  LEU A CD2 1 
ATOM   1946 N  N   . ASN A 1 239 ? -34.339 -7.209  21.454  1.00 41.21  ? 239  ASN A N   1 
ATOM   1947 C  CA  . ASN A 1 239 ? -35.328 -6.179  21.175  1.00 42.26  ? 239  ASN A CA  1 
ATOM   1948 C  C   . ASN A 1 239 ? -35.423 -5.754  19.719  1.00 44.07  ? 239  ASN A C   1 
ATOM   1949 O  O   . ASN A 1 239 ? -36.461 -5.210  19.328  1.00 47.14  ? 239  ASN A O   1 
ATOM   1950 C  CB  . ASN A 1 239 ? -35.043 -4.944  22.040  1.00 46.13  ? 239  ASN A CB  1 
ATOM   1951 C  CG  . ASN A 1 239 ? -35.027 -5.283  23.519  1.00 49.86  ? 239  ASN A CG  1 
ATOM   1952 O  OD1 . ASN A 1 239 ? -36.078 -5.492  24.125  1.00 57.38  ? 239  ASN A OD1 1 
ATOM   1953 N  ND2 . ASN A 1 239 ? -33.835 -5.401  24.092  1.00 50.69  ? 239  ASN A ND2 1 
ATOM   1954 N  N   . GLY A 1 240 ? -34.398 -5.991  18.905  1.00 40.35  ? 240  GLY A N   1 
ATOM   1955 C  CA  . GLY A 1 240 ? -34.414 -5.479  17.550  1.00 39.44  ? 240  GLY A CA  1 
ATOM   1956 C  C   . GLY A 1 240 ? -35.466 -6.152  16.690  1.00 38.34  ? 240  GLY A C   1 
ATOM   1957 O  O   . GLY A 1 240 ? -35.772 -7.334  16.839  1.00 41.51  ? 240  GLY A O   1 
ATOM   1958 N  N   . LYS A 1 241 ? -36.022 -5.383  15.761  1.00 39.17  ? 241  LYS A N   1 
ATOM   1959 C  CA  . LYS A 1 241 ? -37.000 -5.903  14.816  1.00 42.41  ? 241  LYS A CA  1 
ATOM   1960 C  C   . LYS A 1 241 ? -36.442 -5.793  13.409  1.00 39.15  ? 241  LYS A C   1 
ATOM   1961 O  O   . LYS A 1 241 ? -35.890 -4.748  13.037  1.00 41.76  ? 241  LYS A O   1 
ATOM   1962 C  CB  . LYS A 1 241 ? -38.327 -5.150  14.914  1.00 46.60  ? 241  LYS A CB  1 
ATOM   1963 C  CG  . LYS A 1 241 ? -39.375 -5.873  15.739  1.00 48.36  ? 241  LYS A CG  1 
ATOM   1964 C  CD  . LYS A 1 241 ? -39.012 -5.850  17.204  1.00 47.28  ? 241  LYS A CD  1 
ATOM   1965 C  CE  . LYS A 1 241 ? -40.144 -6.381  18.075  1.00 58.46  ? 241  LYS A CE  1 
ATOM   1966 N  NZ  . LYS A 1 241 ? -39.724 -6.520  19.503  1.00 59.89  ? 241  LYS A NZ  1 
ATOM   1967 N  N   . ASP A 1 242 ? -36.588 -6.867  12.636  1.00 38.80  ? 242  ASP A N   1 
ATOM   1968 C  CA  . ASP A 1 242 ? -36.127 -6.886  11.246  1.00 41.27  ? 242  ASP A CA  1 
ATOM   1969 C  C   . ASP A 1 242 ? -37.039 -6.027  10.383  1.00 46.10  ? 242  ASP A C   1 
ATOM   1970 O  O   . ASP A 1 242 ? -38.232 -6.335  10.265  1.00 47.56  ? 242  ASP A O   1 
ATOM   1971 C  CB  . ASP A 1 242 ? -36.085 -8.323  10.712  1.00 36.84  ? 242  ASP A CB  1 
ATOM   1972 C  CG  . ASP A 1 242 ? -35.938 -8.387  9.191   1.00 38.51  ? 242  ASP A CG  1 
ATOM   1973 O  OD1 . ASP A 1 242 ? -35.431 -7.415  8.596   1.00 38.56  ? 242  ASP A OD1 1 
ATOM   1974 O  OD2 . ASP A 1 242 ? -36.308 -9.418  8.585   1.00 36.93  ? 242  ASP A OD2 1 
ATOM   1975 N  N   . PRO A 1 243 ? -36.532 -4.963  9.756   1.00 44.18  ? 243  PRO A N   1 
ATOM   1976 C  CA  . PRO A 1 243 ? -37.393 -4.153  8.871   1.00 51.14  ? 243  PRO A CA  1 
ATOM   1977 C  C   . PRO A 1 243 ? -38.155 -4.960  7.827   1.00 49.17  ? 243  PRO A C   1 
ATOM   1978 O  O   . PRO A 1 243 ? -39.307 -4.629  7.523   1.00 57.58  ? 243  PRO A O   1 
ATOM   1979 C  CB  . PRO A 1 243 ? -36.392 -3.183  8.216   1.00 49.01  ? 243  PRO A CB  1 
ATOM   1980 C  CG  . PRO A 1 243 ? -35.229 -3.131  9.170   1.00 48.75  ? 243  PRO A CG  1 
ATOM   1981 C  CD  . PRO A 1 243 ? -35.130 -4.504  9.752   1.00 43.17  ? 243  PRO A CD  1 
ATOM   1982 N  N   . GLU A 1 244 ? -37.553 -6.010  7.263   1.00 52.45  ? 244  GLU A N   1 
ATOM   1983 C  CA  . GLU A 1 244 ? -38.173 -6.737  6.158   1.00 43.08  ? 244  GLU A CA  1 
ATOM   1984 C  C   . GLU A 1 244 ? -39.317 -7.626  6.638   1.00 53.24  ? 244  GLU A C   1 
ATOM   1985 O  O   . GLU A 1 244 ? -40.478 -7.408  6.268   1.00 51.94  ? 244  GLU A O   1 
ATOM   1986 C  CB  . GLU A 1 244 ? -37.128 -7.571  5.410   1.00 46.13  ? 244  GLU A CB  1 
ATOM   1987 C  CG  . GLU A 1 244 ? -37.728 -8.585  4.440   1.00 50.36  ? 244  GLU A CG  1 
ATOM   1988 C  CD  . GLU A 1 244 ? -36.679 -9.288  3.599   1.00 58.19  ? 244  GLU A CD  1 
ATOM   1989 O  OE1 . GLU A 1 244 ? -35.498 -9.296  4.005   1.00 50.40  ? 244  GLU A OE1 1 
ATOM   1990 O  OE2 . GLU A 1 244 ? -37.034 -9.841  2.534   1.00 65.62  ? 244  GLU A OE2 1 
ATOM   1991 N  N   . THR A 1 245 ? -39.001 -8.638  7.451   1.00 50.43  ? 245  THR A N   1 
ATOM   1992 C  CA  . THR A 1 245 ? -40.032 -9.512  8.002   1.00 48.55  ? 245  THR A CA  1 
ATOM   1993 C  C   . THR A 1 245 ? -40.849 -8.847  9.105   1.00 47.89  ? 245  THR A C   1 
ATOM   1994 O  O   . THR A 1 245 ? -41.946 -9.325  9.413   1.00 51.15  ? 245  THR A O   1 
ATOM   1995 C  CB  . THR A 1 245 ? -39.395 -10.800 8.541   1.00 47.75  ? 245  THR A CB  1 
ATOM   1996 O  OG1 . THR A 1 245 ? -38.591 -10.487 9.690   1.00 42.96  ? 245  THR A OG1 1 
ATOM   1997 C  CG2 . THR A 1 245 ? -38.548 -11.493 7.471   1.00 48.22  ? 245  THR A CG2 1 
ATOM   1998 N  N   . GLY A 1 246 ? -40.339 -7.779  9.718   1.00 45.78  ? 246  GLY A N   1 
ATOM   1999 C  CA  . GLY A 1 246 ? -41.016 -7.119  10.821  1.00 46.90  ? 246  GLY A CA  1 
ATOM   2000 C  C   . GLY A 1 246 ? -40.865 -7.794  12.168  1.00 51.41  ? 246  GLY A C   1 
ATOM   2001 O  O   . GLY A 1 246 ? -41.254 -7.202  13.186  1.00 48.90  ? 246  GLY A O   1 
ATOM   2002 N  N   . GLU A 1 247 ? -40.280 -9.042  12.215  1.00 44.86  ? 247  GLU A N   1 
ATOM   2003 C  CA  . GLU A 1 247 ? -40.142 -9.958  13.333  1.00 36.65  ? 247  GLU A CA  1 
ATOM   2004 C  C   . GLU A 1 247 ? -38.835 -9.713  14.086  1.00 43.66  ? 247  GLU A C   1 
ATOM   2005 O  O   . GLU A 1 247 ? -37.843 -9.271  13.497  1.00 39.47  ? 247  GLU A O   1 
ATOM   2006 C  CB  . GLU A 1 247 ? -40.163 -11.405 12.839  1.00 43.49  ? 247  GLU A CB  1 
ATOM   2007 C  CG  . GLU A 1 247 ? -41.306 -11.741 11.869  1.00 41.23  ? 247  GLU A CG  1 
ATOM   2008 C  CD  . GLU A 1 247 ? -41.221 -13.158 11.324  1.00 51.31  ? 247  GLU A CD  1 
ATOM   2009 O  OE1 . GLU A 1 247 ? -40.210 -13.840 11.586  1.00 44.71  ? 247  GLU A OE1 1 
ATOM   2010 O  OE2 . GLU A 1 247 ? -42.171 -13.595 10.635  1.00 45.73  ? 247  GLU A OE2 1 
ATOM   2011 N  N   . PRO A 1 248 ? -38.823 -9.982  15.385  1.00 40.09  ? 248  PRO A N   1 
ATOM   2012 C  CA  . PRO A 1 248 ? -37.563 -10.074 16.124  1.00 38.25  ? 248  PRO A CA  1 
ATOM   2013 C  C   . PRO A 1 248 ? -37.058 -11.509 16.050  1.00 36.87  ? 248  PRO A C   1 
ATOM   2014 O  O   . PRO A 1 248 ? -37.761 -12.417 15.606  1.00 35.17  ? 248  PRO A O   1 
ATOM   2015 C  CB  . PRO A 1 248 ? -37.978 -9.701  17.548  1.00 42.14  ? 248  PRO A CB  1 
ATOM   2016 C  CG  . PRO A 1 248 ? -39.357 -10.302 17.661  1.00 44.60  ? 248  PRO A CG  1 
ATOM   2017 C  CD  . PRO A 1 248 ? -39.990 -10.144 16.273  1.00 42.94  ? 248  PRO A CD  1 
ATOM   2018 N  N   . LEU A 1 249 ? -35.807 -11.698 16.470  1.00 34.89  ? 249  LEU A N   1 
ATOM   2019 C  CA  . LEU A 1 249 ? -35.273 -13.051 16.580  1.00 36.41  ? 249  LEU A CA  1 
ATOM   2020 C  C   . LEU A 1 249 ? -36.012 -13.820 17.662  1.00 35.16  ? 249  LEU A C   1 
ATOM   2021 O  O   . LEU A 1 249 ? -36.384 -13.256 18.690  1.00 37.53  ? 249  LEU A O   1 
ATOM   2022 C  CB  . LEU A 1 249 ? -33.786 -13.025 16.924  1.00 33.83  ? 249  LEU A CB  1 
ATOM   2023 C  CG  . LEU A 1 249 ? -32.918 -12.248 15.944  1.00 34.43  ? 249  LEU A CG  1 
ATOM   2024 C  CD1 . LEU A 1 249 ? -31.469 -12.308 16.418  1.00 35.31  ? 249  LEU A CD1 1 
ATOM   2025 C  CD2 . LEU A 1 249 ? -33.061 -12.828 14.550  1.00 34.58  ? 249  LEU A CD2 1 
ATOM   2026 N  N   . ASP A 1 250 ? -36.211 -15.117 17.443  1.00 38.00  ? 250  ASP A N   1 
ATOM   2027 C  CA  . ASP A 1 250 ? -36.808 -15.914 18.508  1.00 39.73  ? 250  ASP A CA  1 
ATOM   2028 C  C   . ASP A 1 250 ? -35.729 -16.477 19.433  1.00 41.23  ? 250  ASP A C   1 
ATOM   2029 O  O   . ASP A 1 250 ? -34.525 -16.341 19.195  1.00 38.22  ? 250  ASP A O   1 
ATOM   2030 C  CB  . ASP A 1 250 ? -37.707 -17.018 17.931  1.00 43.90  ? 250  ASP A CB  1 
ATOM   2031 C  CG  . ASP A 1 250 ? -36.952 -18.072 17.134  1.00 45.72  ? 250  ASP A CG  1 
ATOM   2032 O  OD1 . ASP A 1 250 ? -35.718 -18.211 17.257  1.00 42.80  ? 250  ASP A OD1 1 
ATOM   2033 O  OD2 . ASP A 1 250 ? -37.620 -18.773 16.354  1.00 57.50  ? 250  ASP A OD2 1 
ATOM   2034 N  N   . ASP A 1 251 ? -36.178 -17.098 20.525  1.00 40.06  ? 251  ASP A N   1 
ATOM   2035 C  CA  . ASP A 1 251 ? -35.253 -17.491 21.581  1.00 43.01  ? 251  ASP A CA  1 
ATOM   2036 C  C   . ASP A 1 251 ? -34.222 -18.491 21.079  1.00 36.20  ? 251  ASP A C   1 
ATOM   2037 O  O   . ASP A 1 251 ? -33.045 -18.399 21.431  1.00 39.28  ? 251  ASP A O   1 
ATOM   2038 C  CB  . ASP A 1 251 ? -36.016 -18.077 22.767  1.00 45.59  ? 251  ASP A CB  1 
ATOM   2039 C  CG  . ASP A 1 251 ? -36.624 -17.008 23.650  1.00 55.40  ? 251  ASP A CG  1 
ATOM   2040 O  OD1 . ASP A 1 251 ? -36.332 -15.814 23.424  1.00 51.85  ? 251  ASP A OD1 1 
ATOM   2041 O  OD2 . ASP A 1 251 ? -37.389 -17.364 24.569  1.00 59.53  ? 251  ASP A OD2 1 
ATOM   2042 N  N   . GLU A 1 252 ? -34.642 -19.459 20.260  1.00 39.62  ? 252  GLU A N   1 
ATOM   2043 C  CA  . GLU A 1 252 ? -33.688 -20.450 19.770  1.00 39.80  ? 252  GLU A CA  1 
ATOM   2044 C  C   . GLU A 1 252 ? -32.583 -19.783 18.958  1.00 35.58  ? 252  GLU A C   1 
ATOM   2045 O  O   . GLU A 1 252 ? -31.392 -20.058 19.164  1.00 35.97  ? 252  GLU A O   1 
ATOM   2046 C  CB  . GLU A 1 252 ? -34.391 -21.524 18.942  1.00 41.72  ? 252  GLU A CB  1 
ATOM   2047 C  CG  . GLU A 1 252 ? -33.449 -22.677 18.565  1.00 41.47  ? 252  GLU A CG  1 
ATOM   2048 C  CD  . GLU A 1 252 ? -34.059 -23.666 17.594  1.00 50.66  ? 252  GLU A CD  1 
ATOM   2049 O  OE1 . GLU A 1 252 ? -34.757 -24.591 18.057  1.00 61.26  ? 252  GLU A OE1 1 
ATOM   2050 O  OE2 . GLU A 1 252 ? -33.818 -23.543 16.372  1.00 55.43  ? 252  GLU A OE2 1 
ATOM   2051 N  N   . ASN A 1 253 ? -32.955 -18.878 18.048  1.00 34.31  ? 253  ASN A N   1 
ATOM   2052 C  CA  . ASN A 1 253 ? -31.931 -18.241 17.225  1.00 32.11  ? 253  ASN A CA  1 
ATOM   2053 C  C   . ASN A 1 253 ? -31.042 -17.313 18.050  1.00 34.62  ? 253  ASN A C   1 
ATOM   2054 O  O   . ASN A 1 253 ? -29.830 -17.239 17.816  1.00 32.46  ? 253  ASN A O   1 
ATOM   2055 C  CB  . ASN A 1 253 ? -32.563 -17.486 16.064  1.00 33.35  ? 253  ASN A CB  1 
ATOM   2056 C  CG  . ASN A 1 253 ? -31.521 -16.967 15.084  1.00 29.13  ? 253  ASN A CG  1 
ATOM   2057 O  OD1 . ASN A 1 253 ? -31.201 -15.782 15.084  1.00 33.08  ? 253  ASN A OD1 1 
ATOM   2058 N  ND2 . ASN A 1 253 ? -30.951 -17.874 14.278  1.00 29.98  ? 253  ASN A ND2 1 
ATOM   2059 N  N   . ILE A 1 254 ? -31.620 -16.573 18.997  1.00 33.29  ? 254  ILE A N   1 
ATOM   2060 C  CA  . ILE A 1 254 ? -30.800 -15.749 19.892  1.00 32.83  ? 254  ILE A CA  1 
ATOM   2061 C  C   . ILE A 1 254 ? -29.684 -16.577 20.525  1.00 33.01  ? 254  ILE A C   1 
ATOM   2062 O  O   . ILE A 1 254 ? -28.516 -16.161 20.554  1.00 32.31  ? 254  ILE A O   1 
ATOM   2063 C  CB  . ILE A 1 254 ? -31.681 -15.079 20.963  1.00 34.84  ? 254  ILE A CB  1 
ATOM   2064 C  CG1 . ILE A 1 254 ? -32.555 -14.007 20.311  1.00 35.08  ? 254  ILE A CG1 1 
ATOM   2065 C  CG2 . ILE A 1 254 ? -30.799 -14.507 22.093  1.00 33.80  ? 254  ILE A CG2 1 
ATOM   2066 C  CD1 . ILE A 1 254 ? -33.642 -13.449 21.213  1.00 41.25  ? 254  ILE A CD1 1 
ATOM   2067 N  N   . ARG A 1 255 ? -30.023 -17.759 21.050  1.00 32.92  ? 255  ARG A N   1 
ATOM   2068 C  CA  . ARG A 1 255 ? -29.004 -18.602 21.676  1.00 32.58  ? 255  ARG A CA  1 
ATOM   2069 C  C   . ARG A 1 255 ? -27.899 -18.944 20.687  1.00 32.71  ? 255  ARG A C   1 
ATOM   2070 O  O   . ARG A 1 255 ? -26.710 -18.923 21.035  1.00 32.64  ? 255  ARG A O   1 
ATOM   2071 C  CB  . ARG A 1 255 ? -29.628 -19.881 22.227  1.00 36.22  ? 255  ARG A CB  1 
ATOM   2072 C  CG  . ARG A 1 255 ? -30.431 -19.671 23.492  1.00 44.21  ? 255  ARG A CG  1 
ATOM   2073 C  CD  . ARG A 1 255 ? -31.111 -20.959 23.933  1.00 52.57  ? 255  ARG A CD  1 
ATOM   2074 N  NE  . ARG A 1 255 ? -30.144 -21.803 24.624  1.00 56.82  ? 255  ARG A NE  1 
ATOM   2075 C  CZ  . ARG A 1 255 ? -29.840 -21.706 25.911  1.00 62.54  ? 255  ARG A CZ  1 
ATOM   2076 N  NH1 . ARG A 1 255 ? -30.452 -20.839 26.704  1.00 58.50  ? 255  ARG A NH1 1 
ATOM   2077 N  NH2 . ARG A 1 255 ? -28.881 -22.482 26.411  1.00 62.40  ? 255  ARG A NH2 1 
ATOM   2078 N  N   . TYR A 1 256 ? -28.276 -19.272 19.452  1.00 32.64  ? 256  TYR A N   1 
ATOM   2079 C  CA  . TYR A 1 256 ? -27.275 -19.555 18.429  1.00 30.88  ? 256  TYR A CA  1 
ATOM   2080 C  C   . TYR A 1 256 ? -26.405 -18.338 18.150  1.00 30.85  ? 256  TYR A C   1 
ATOM   2081 O  O   . TYR A 1 256 ? -25.193 -18.477 17.934  1.00 31.49  ? 256  TYR A O   1 
ATOM   2082 C  CB  . TYR A 1 256 ? -27.954 -20.026 17.144  1.00 32.70  ? 256  TYR A CB  1 
ATOM   2083 C  CG  . TYR A 1 256 ? -28.473 -21.450 17.231  1.00 36.09  ? 256  TYR A CG  1 
ATOM   2084 C  CD1 . TYR A 1 256 ? -27.706 -22.462 17.802  1.00 36.07  ? 256  TYR A CD1 1 
ATOM   2085 C  CD2 . TYR A 1 256 ? -29.728 -21.782 16.725  1.00 37.57  ? 256  TYR A CD2 1 
ATOM   2086 C  CE1 . TYR A 1 256 ? -28.183 -23.771 17.882  1.00 41.88  ? 256  TYR A CE1 1 
ATOM   2087 C  CE2 . TYR A 1 256 ? -30.206 -23.079 16.799  1.00 38.87  ? 256  TYR A CE2 1 
ATOM   2088 C  CZ  . TYR A 1 256 ? -29.435 -24.062 17.373  1.00 38.00  ? 256  TYR A CZ  1 
ATOM   2089 O  OH  . TYR A 1 256 ? -29.929 -25.345 17.435  1.00 46.74  ? 256  TYR A OH  1 
ATOM   2090 N  N   . GLN A 1 257 ? -27.001 -17.139 18.104  1.00 30.39  ? 257  GLN A N   1 
ATOM   2091 C  CA  . GLN A 1 257 ? -26.195 -15.947 17.835  1.00 28.57  ? 257  GLN A CA  1 
ATOM   2092 C  C   . GLN A 1 257 ? -25.201 -15.675 18.963  1.00 30.44  ? 257  GLN A C   1 
ATOM   2093 O  O   . GLN A 1 257 ? -24.073 -15.240 18.703  1.00 30.77  ? 257  GLN A O   1 
ATOM   2094 C  CB  . GLN A 1 257 ? -27.069 -14.709 17.607  1.00 29.74  ? 257  GLN A CB  1 
ATOM   2095 C  CG  . GLN A 1 257 ? -28.145 -14.840 16.522  1.00 29.53  ? 257  GLN A CG  1 
ATOM   2096 C  CD  . GLN A 1 257 ? -27.599 -15.010 15.101  1.00 31.17  ? 257  GLN A CD  1 
ATOM   2097 O  OE1 . GLN A 1 257 ? -26.379 -14.960 14.861  1.00 29.55  ? 257  GLN A OE1 1 
ATOM   2098 N  NE2 . GLN A 1 257 ? -28.506 -15.200 14.148  1.00 27.24  ? 257  GLN A NE2 1 
ATOM   2099 N  N   . ILE A 1 258 ? -25.607 -15.883 20.226  1.00 30.88  ? 258  ILE A N   1 
ATOM   2100 C  CA  . ILE A 1 258 ? -24.682 -15.653 21.338  1.00 32.53  ? 258  ILE A CA  1 
ATOM   2101 C  C   . ILE A 1 258 ? -23.497 -16.600 21.235  1.00 29.83  ? 258  ILE A C   1 
ATOM   2102 O  O   . ILE A 1 258 ? -22.340 -16.193 21.377  1.00 30.85  ? 258  ILE A O   1 
ATOM   2103 C  CB  . ILE A 1 258 ? -25.404 -15.806 22.691  1.00 31.13  ? 258  ILE A CB  1 
ATOM   2104 C  CG1 . ILE A 1 258 ? -26.484 -14.732 22.817  1.00 34.35  ? 258  ILE A CG1 1 
ATOM   2105 C  CG2 . ILE A 1 258 ? -24.402 -15.677 23.854  1.00 30.81  ? 258  ILE A CG2 1 
ATOM   2106 C  CD1 . ILE A 1 258 ? -27.392 -14.899 24.058  1.00 34.38  ? 258  ILE A CD1 1 
ATOM   2107 N  N   . ILE A 1 259 ? -23.774 -17.885 20.990  1.00 29.47  ? 259  ILE A N   1 
ATOM   2108 C  CA  . ILE A 1 259 ? -22.696 -18.850 20.788  1.00 28.33  ? 259  ILE A CA  1 
ATOM   2109 C  C   . ILE A 1 259 ? -21.802 -18.397 19.645  1.00 29.74  ? 259  ILE A C   1 
ATOM   2110 O  O   . ILE A 1 259 ? -20.569 -18.391 19.756  1.00 28.76  ? 259  ILE A O   1 
ATOM   2111 C  CB  . ILE A 1 259 ? -23.275 -20.249 20.518  1.00 33.12  ? 259  ILE A CB  1 
ATOM   2112 C  CG1 . ILE A 1 259 ? -23.901 -20.803 21.802  1.00 35.53  ? 259  ILE A CG1 1 
ATOM   2113 C  CG2 . ILE A 1 259 ? -22.207 -21.177 19.948  1.00 36.37  ? 259  ILE A CG2 1 
ATOM   2114 C  CD1 . ILE A 1 259 ? -24.659 -22.083 21.598  1.00 41.10  ? 259  ILE A CD1 1 
ATOM   2115 N  N   . THR A 1 260 ? -22.420 -18.025 18.525  1.00 28.58  ? 260  THR A N   1 
ATOM   2116 C  CA  . THR A 1 260 ? -21.671 -17.570 17.354  1.00 29.00  ? 260  THR A CA  1 
ATOM   2117 C  C   . THR A 1 260 ? -20.777 -16.379 17.680  1.00 31.23  ? 260  THR A C   1 
ATOM   2118 O  O   . THR A 1 260 ? -19.594 -16.356 17.314  1.00 29.91  ? 260  THR A O   1 
ATOM   2119 C  CB  . THR A 1 260 ? -22.650 -17.202 16.242  1.00 28.67  ? 260  THR A CB  1 
ATOM   2120 O  OG1 . THR A 1 260 ? -23.387 -18.373 15.871  1.00 29.49  ? 260  THR A OG1 1 
ATOM   2121 C  CG2 . THR A 1 260 ? -21.900 -16.641 15.043  1.00 29.84  ? 260  THR A CG2 1 
ATOM   2122 N  N   . PHE A 1 261 ? -21.331 -15.355 18.326  1.00 29.44  ? 261  PHE A N   1 
ATOM   2123 C  CA  . PHE A 1 261 ? -20.522 -14.161 18.544  1.00 29.99  ? 261  PHE A CA  1 
ATOM   2124 C  C   . PHE A 1 261 ? -19.474 -14.384 19.625  1.00 31.78  ? 261  PHE A C   1 
ATOM   2125 O  O   . PHE A 1 261 ? -18.390 -13.789 19.560  1.00 32.59  ? 261  PHE A O   1 
ATOM   2126 C  CB  . PHE A 1 261 ? -21.447 -12.969 18.841  1.00 33.00  ? 261  PHE A CB  1 
ATOM   2127 C  CG  . PHE A 1 261 ? -22.011 -12.343 17.586  1.00 30.47  ? 261  PHE A CG  1 
ATOM   2128 C  CD1 . PHE A 1 261 ? -21.327 -11.329 16.938  1.00 34.43  ? 261  PHE A CD1 1 
ATOM   2129 C  CD2 . PHE A 1 261 ? -23.216 -12.776 17.046  1.00 34.53  ? 261  PHE A CD2 1 
ATOM   2130 C  CE1 . PHE A 1 261 ? -21.825 -10.750 15.795  1.00 31.87  ? 261  PHE A CE1 1 
ATOM   2131 C  CE2 . PHE A 1 261 ? -23.718 -12.201 15.894  1.00 35.16  ? 261  PHE A CE2 1 
ATOM   2132 C  CZ  . PHE A 1 261 ? -23.023 -11.187 15.262  1.00 36.26  ? 261  PHE A CZ  1 
ATOM   2133 N  N   . LEU A 1 262 ? -19.749 -15.239 20.619  1.00 30.81  ? 262  LEU A N   1 
ATOM   2134 C  CA  . LEU A 1 262 ? -18.702 -15.513 21.605  1.00 31.84  ? 262  LEU A CA  1 
ATOM   2135 C  C   . LEU A 1 262 ? -17.515 -16.211 20.966  1.00 34.43  ? 262  LEU A C   1 
ATOM   2136 O  O   . LEU A 1 262 ? -16.367 -15.959 21.352  1.00 35.09  ? 262  LEU A O   1 
ATOM   2137 C  CB  . LEU A 1 262 ? -19.235 -16.354 22.767  1.00 32.53  ? 262  LEU A CB  1 
ATOM   2138 C  CG  . LEU A 1 262 ? -20.171 -15.636 23.729  1.00 34.38  ? 262  LEU A CG  1 
ATOM   2139 C  CD1 . LEU A 1 262 ? -20.701 -16.634 24.760  1.00 34.22  ? 262  LEU A CD1 1 
ATOM   2140 C  CD2 . LEU A 1 262 ? -19.466 -14.454 24.407  1.00 33.32  ? 262  LEU A CD2 1 
ATOM   2141 N  N   . ILE A 1 263 ? -17.766 -17.067 19.978  1.00 31.74  ? 263  ILE A N   1 
ATOM   2142 C  CA  . ILE A 1 263 ? -16.683 -17.780 19.305  1.00 31.57  ? 263  ILE A CA  1 
ATOM   2143 C  C   . ILE A 1 263 ? -16.059 -16.909 18.221  1.00 30.49  ? 263  ILE A C   1 
ATOM   2144 O  O   . ILE A 1 263 ? -14.856 -16.616 18.249  1.00 36.53  ? 263  ILE A O   1 
ATOM   2145 C  CB  . ILE A 1 263 ? -17.209 -19.105 18.737  1.00 32.52  ? 263  ILE A CB  1 
ATOM   2146 C  CG1 . ILE A 1 263 ? -17.630 -20.006 19.897  1.00 38.58  ? 263  ILE A CG1 1 
ATOM   2147 C  CG2 . ILE A 1 263 ? -16.182 -19.779 17.790  1.00 34.21  ? 263  ILE A CG2 1 
ATOM   2148 C  CD1 . ILE A 1 263 ? -18.265 -21.293 19.458  1.00 38.12  ? 263  ILE A CD1 1 
ATOM   2149 N  N   . ALA A 1 264 ? -16.872 -16.472 17.259  1.00 30.66  ? 264  ALA A N   1 
ATOM   2150 C  CA  . ALA A 1 264 ? -16.353 -15.664 16.155  1.00 33.57  ? 264  ALA A CA  1 
ATOM   2151 C  C   . ALA A 1 264 ? -15.893 -14.295 16.621  1.00 32.75  ? 264  ALA A C   1 
ATOM   2152 O  O   . ALA A 1 264 ? -14.972 -13.720 16.028  1.00 33.12  ? 264  ALA A O   1 
ATOM   2153 C  CB  . ALA A 1 264 ? -17.410 -15.504 15.056  1.00 33.03  ? 264  ALA A CB  1 
ATOM   2154 N  N   . GLY A 1 265 ? -16.518 -13.751 17.661  1.00 33.66  ? 265  GLY A N   1 
ATOM   2155 C  CA  . GLY A 1 265 ? -16.177 -12.427 18.143  1.00 33.70  ? 265  GLY A CA  1 
ATOM   2156 C  C   . GLY A 1 265 ? -14.888 -12.329 18.935  1.00 36.07  ? 265  GLY A C   1 
ATOM   2157 O  O   . GLY A 1 265 ? -14.535 -11.216 19.339  1.00 35.07  ? 265  GLY A O   1 
ATOM   2158 N  N   . HIS A 1 266 ? -14.178 -13.439 19.166  1.00 37.09  ? 266  HIS A N   1 
ATOM   2159 C  CA  . HIS A 1 266 ? -12.892 -13.363 19.864  1.00 33.91  ? 266  HIS A CA  1 
ATOM   2160 C  C   . HIS A 1 266 ? -11.780 -14.213 19.255  1.00 35.89  ? 266  HIS A C   1 
ATOM   2161 O  O   . HIS A 1 266 ? -10.613 -13.803 19.276  1.00 33.11  ? 266  HIS A O   1 
ATOM   2162 C  CB  . HIS A 1 266 ? -13.047 -13.758 21.336  1.00 34.28  ? 266  HIS A CB  1 
ATOM   2163 C  CG  . HIS A 1 266 ? -12.763 -15.203 21.605  1.00 33.33  ? 266  HIS A CG  1 
ATOM   2164 N  ND1 . HIS A 1 266 ? -13.722 -16.182 21.480  1.00 34.97  ? 266  HIS A ND1 1 
ATOM   2165 C  CD2 . HIS A 1 266 ? -11.628 -15.837 21.991  1.00 34.50  ? 266  HIS A CD2 1 
ATOM   2166 C  CE1 . HIS A 1 266 ? -13.194 -17.356 21.782  1.00 34.65  ? 266  HIS A CE1 1 
ATOM   2167 N  NE2 . HIS A 1 266 ? -11.922 -17.174 22.089  1.00 33.88  ? 266  HIS A NE2 1 
ATOM   2168 N  N   . GLU A 1 267 ? -12.098 -15.392 18.719  1.00 33.97  ? 267  GLU A N   1 
ATOM   2169 C  CA  . GLU A 1 267 ? -11.026 -16.341 18.419  1.00 32.59  ? 267  GLU A CA  1 
ATOM   2170 C  C   . GLU A 1 267 ? -10.130 -15.824 17.293  1.00 32.74  ? 267  GLU A C   1 
ATOM   2171 O  O   . GLU A 1 267 ? -8.893  -15.858 17.393  1.00 34.71  ? 267  GLU A O   1 
ATOM   2172 C  CB  . GLU A 1 267 ? -11.611 -17.707 18.083  1.00 34.50  ? 267  GLU A CB  1 
ATOM   2173 C  CG  . GLU A 1 267 ? -10.729 -18.553 17.201  1.00 35.56  ? 267  GLU A CG  1 
ATOM   2174 C  CD  . GLU A 1 267 ? -9.499  -19.037 17.935  1.00 39.07  ? 267  GLU A CD  1 
ATOM   2175 O  OE1 . GLU A 1 267 ? -9.574  -19.199 19.169  1.00 40.03  ? 267  GLU A OE1 1 
ATOM   2176 O  OE2 . GLU A 1 267 ? -8.455  -19.255 17.277  1.00 40.71  ? 267  GLU A OE2 1 
ATOM   2177 N  N   . THR A 1 268 ? -10.726 -15.304 16.232  1.00 29.62  ? 268  THR A N   1 
ATOM   2178 C  CA  . THR A 1 268 ? -9.897  -14.821 15.137  1.00 30.91  ? 268  THR A CA  1 
ATOM   2179 C  C   . THR A 1 268 ? -9.149  -13.548 15.508  1.00 29.50  ? 268  THR A C   1 
ATOM   2180 O  O   . THR A 1 268 ? -8.056  -13.311 14.980  1.00 32.22  ? 268  THR A O   1 
ATOM   2181 C  CB  . THR A 1 268 ? -10.756 -14.618 13.901  1.00 32.96  ? 268  THR A CB  1 
ATOM   2182 O  OG1 . THR A 1 268 ? -11.982 -13.983 14.286  1.00 32.33  ? 268  THR A OG1 1 
ATOM   2183 C  CG2 . THR A 1 268 ? -11.074 -15.989 13.273  1.00 29.47  ? 268  THR A CG2 1 
ATOM   2184 N  N   . THR A 1 269 ? -9.700  -12.717 16.398  1.00 28.27  ? 269  THR A N   1 
ATOM   2185 C  CA  . THR A 1 269 ? -8.996  -11.484 16.749  1.00 28.94  ? 269  THR A CA  1 
ATOM   2186 C  C   . THR A 1 269 ? -7.791  -11.782 17.632  1.00 27.82  ? 269  THR A C   1 
ATOM   2187 O  O   . THR A 1 269 ? -6.772  -11.076 17.553  1.00 29.65  ? 269  THR A O   1 
ATOM   2188 C  CB  . THR A 1 269 ? -9.951  -10.497 17.429  1.00 28.09  ? 269  THR A CB  1 
ATOM   2189 O  OG1 . THR A 1 269 ? -11.053 -10.260 16.536  1.00 28.82  ? 269  THR A OG1 1 
ATOM   2190 C  CG2 . THR A 1 269 ? -9.267  -9.163  17.713  1.00 28.40  ? 269  THR A CG2 1 
ATOM   2191 N  N   A SER A 1 270 ? -7.871  -12.818 18.463  0.66 27.94  ? 270  SER A N   1 
ATOM   2192 N  N   B SER A 1 270 ? -7.885  -12.806 18.483  0.34 27.98  ? 270  SER A N   1 
ATOM   2193 C  CA  A SER A 1 270 ? -6.695  -13.192 19.244  0.66 27.81  ? 270  SER A CA  1 
ATOM   2194 C  CA  B SER A 1 270 ? -6.716  -13.230 19.249  0.34 27.89  ? 270  SER A CA  1 
ATOM   2195 C  C   A SER A 1 270 ? -5.587  -13.723 18.338  0.66 30.45  ? 270  SER A C   1 
ATOM   2196 C  C   B SER A 1 270 ? -5.601  -13.694 18.320  0.34 30.40  ? 270  SER A C   1 
ATOM   2197 O  O   A SER A 1 270 ? -4.400  -13.453 18.570  0.66 30.03  ? 270  SER A O   1 
ATOM   2198 O  O   B SER A 1 270 ? -4.428  -13.355 18.521  0.34 29.99  ? 270  SER A O   1 
ATOM   2199 C  CB  A SER A 1 270 ? -7.081  -14.218 20.318  0.66 29.55  ? 270  SER A CB  1 
ATOM   2200 C  CB  B SER A 1 270 ? -7.108  -14.341 20.231  0.34 29.56  ? 270  SER A CB  1 
ATOM   2201 O  OG  A SER A 1 270 ? -7.507  -15.445 19.751  0.66 29.28  ? 270  SER A OG  1 
ATOM   2202 O  OG  B SER A 1 270 ? -5.971  -15.037 20.726  0.34 29.93  ? 270  SER A OG  1 
ATOM   2203 N  N   . GLY A 1 271 ? -5.952  -14.467 17.292  1.00 30.15  ? 271  GLY A N   1 
ATOM   2204 C  CA  . GLY A 1 271 ? -4.955  -14.889 16.325  1.00 28.59  ? 271  GLY A CA  1 
ATOM   2205 C  C   . GLY A 1 271 ? -4.315  -13.710 15.625  1.00 30.08  ? 271  GLY A C   1 
ATOM   2206 O  O   . GLY A 1 271 ? -3.088  -13.663 15.452  1.00 30.00  ? 271  GLY A O   1 
ATOM   2207 N  N   . LEU A 1 272 ? -5.129  -12.734 15.216  1.00 28.34  ? 272  LEU A N   1 
ATOM   2208 C  CA  . LEU A 1 272 ? -4.570  -11.560 14.545  1.00 28.29  ? 272  LEU A CA  1 
ATOM   2209 C  C   . LEU A 1 272 ? -3.559  -10.844 15.432  1.00 28.74  ? 272  LEU A C   1 
ATOM   2210 O  O   . LEU A 1 272 ? -2.444  -10.520 14.999  1.00 28.40  ? 272  LEU A O   1 
ATOM   2211 C  CB  . LEU A 1 272 ? -5.690  -10.606 14.139  1.00 27.54  ? 272  LEU A CB  1 
ATOM   2212 C  CG  . LEU A 1 272 ? -5.237  -9.221  13.662  1.00 28.82  ? 272  LEU A CG  1 
ATOM   2213 C  CD1 . LEU A 1 272 ? -4.276  -9.320  12.432  1.00 28.72  ? 272  LEU A CD1 1 
ATOM   2214 C  CD2 . LEU A 1 272 ? -6.448  -8.341  13.344  1.00 29.95  ? 272  LEU A CD2 1 
ATOM   2215 N  N   . LEU A 1 273 ? -3.938  -10.567 16.676  1.00 27.86  ? 273  LEU A N   1 
ATOM   2216 C  CA  . LEU A 1 273 ? -3.032  -9.853  17.568  1.00 29.61  ? 273  LEU A CA  1 
ATOM   2217 C  C   . LEU A 1 273 ? -1.758  -10.650 17.798  1.00 29.80  ? 273  LEU A C   1 
ATOM   2218 O  O   . LEU A 1 273 ? -0.664  -10.075 17.859  1.00 30.42  ? 273  LEU A O   1 
ATOM   2219 C  CB  . LEU A 1 273 ? -3.731  -9.552  18.893  1.00 27.14  ? 273  LEU A CB  1 
ATOM   2220 C  CG  . LEU A 1 273 ? -4.660  -8.342  18.824  1.00 27.23  ? 273  LEU A CG  1 
ATOM   2221 C  CD1 . LEU A 1 273 ? -5.628  -8.379  20.010  1.00 29.34  ? 273  LEU A CD1 1 
ATOM   2222 C  CD2 . LEU A 1 273 ? -3.837  -7.037  18.851  1.00 31.16  ? 273  LEU A CD2 1 
ATOM   2223 N  N   . SER A 1 274 ? -1.878  -11.975 17.896  1.00 28.01  ? 274  SER A N   1 
ATOM   2224 C  CA  . SER A 1 274 ? -0.699  -12.825 18.089  1.00 29.82  ? 274  SER A CA  1 
ATOM   2225 C  C   . SER A 1 274 ? 0.236   -12.753 16.886  1.00 31.80  ? 274  SER A C   1 
ATOM   2226 O  O   . SER A 1 274 ? 1.451   -12.540 17.035  1.00 29.57  ? 274  SER A O   1 
ATOM   2227 C  CB  . SER A 1 274 ? -1.144  -14.260 18.357  1.00 30.43  ? 274  SER A CB  1 
ATOM   2228 O  OG  . SER A 1 274 ? -1.969  -14.294 19.533  1.00 29.29  ? 274  SER A OG  1 
ATOM   2229 N  N   . PHE A 1 275 ? -0.311  -12.942 15.680  1.00 29.96  ? 275  PHE A N   1 
ATOM   2230 C  CA  . PHE A 1 275 ? 0.514   -12.830 14.477  1.00 29.25  ? 275  PHE A CA  1 
ATOM   2231 C  C   . PHE A 1 275 ? 1.103   -11.432 14.332  1.00 32.67  ? 275  PHE A C   1 
ATOM   2232 O  O   . PHE A 1 275 ? 2.248   -11.286 13.885  1.00 33.17  ? 275  PHE A O   1 
ATOM   2233 C  CB  . PHE A 1 275 ? -0.307  -13.179 13.233  1.00 27.72  ? 275  PHE A CB  1 
ATOM   2234 C  CG  . PHE A 1 275 ? -0.483  -14.642 13.013  1.00 28.38  ? 275  PHE A CG  1 
ATOM   2235 C  CD1 . PHE A 1 275 ? 0.612   -15.468 12.743  1.00 30.72  ? 275  PHE A CD1 1 
ATOM   2236 C  CD2 . PHE A 1 275 ? -1.748  -15.202 13.046  1.00 28.00  ? 275  PHE A CD2 1 
ATOM   2237 C  CE1 . PHE A 1 275 ? 0.435   -16.825 12.501  1.00 30.24  ? 275  PHE A CE1 1 
ATOM   2238 C  CE2 . PHE A 1 275 ? -1.929  -16.545 12.829  1.00 31.04  ? 275  PHE A CE2 1 
ATOM   2239 C  CZ  . PHE A 1 275 ? -0.843  -17.367 12.561  1.00 33.11  ? 275  PHE A CZ  1 
ATOM   2240 N  N   . ALA A 1 276 ? 0.334   -10.390 14.674  1.00 30.38  ? 276  ALA A N   1 
ATOM   2241 C  CA  . ALA A 1 276 ? 0.832   -9.027  14.516  1.00 30.20  ? 276  ALA A CA  1 
ATOM   2242 C  C   . ALA A 1 276 ? 2.040   -8.783  15.413  1.00 30.62  ? 276  ALA A C   1 
ATOM   2243 O  O   . ALA A 1 276 ? 3.063   -8.253  14.966  1.00 32.06  ? 276  ALA A O   1 
ATOM   2244 C  CB  . ALA A 1 276 ? -0.266  -8.006  14.813  1.00 34.46  ? 276  ALA A CB  1 
ATOM   2245 N  N   . LEU A 1 277 ? 1.954   -9.195  16.675  1.00 31.29  ? 277  LEU A N   1 
ATOM   2246 C  CA  . LEU A 1 277 ? 3.102   -9.021  17.563  1.00 29.50  ? 277  LEU A CA  1 
ATOM   2247 C  C   . LEU A 1 277 ? 4.280   -9.864  17.091  1.00 33.75  ? 277  LEU A C   1 
ATOM   2248 O  O   . LEU A 1 277 ? 5.434   -9.413  17.137  1.00 32.42  ? 277  LEU A O   1 
ATOM   2249 C  CB  . LEU A 1 277 ? 2.715   -9.381  18.998  1.00 31.38  ? 277  LEU A CB  1 
ATOM   2250 C  CG  . LEU A 1 277 ? 3.825   -9.184  20.042  1.00 35.13  ? 277  LEU A CG  1 
ATOM   2251 C  CD1 . LEU A 1 277 ? 4.291   -7.736  20.060  1.00 34.11  ? 277  LEU A CD1 1 
ATOM   2252 C  CD2 . LEU A 1 277 ? 3.386   -9.612  21.445  1.00 34.38  ? 277  LEU A CD2 1 
ATOM   2253 N  N   . TYR A 1 278 ? 4.008   -11.080 16.610  1.00 30.69  ? 278  TYR A N   1 
ATOM   2254 C  CA  . TYR A 1 278 ? 5.067   -11.904 16.033  1.00 30.32  ? 278  TYR A CA  1 
ATOM   2255 C  C   . TYR A 1 278 ? 5.792   -11.138 14.936  1.00 33.86  ? 278  TYR A C   1 
ATOM   2256 O  O   . TYR A 1 278 ? 7.022   -11.000 14.955  1.00 32.74  ? 278  TYR A O   1 
ATOM   2257 C  CB  . TYR A 1 278 ? 4.492   -13.215 15.477  1.00 31.23  ? 278  TYR A CB  1 
ATOM   2258 C  CG  . TYR A 1 278 ? 5.467   -13.959 14.578  1.00 34.99  ? 278  TYR A CG  1 
ATOM   2259 C  CD1 . TYR A 1 278 ? 6.432   -14.801 15.122  1.00 35.93  ? 278  TYR A CD1 1 
ATOM   2260 C  CD2 . TYR A 1 278 ? 5.441   -13.793 13.202  1.00 33.58  ? 278  TYR A CD2 1 
ATOM   2261 C  CE1 . TYR A 1 278 ? 7.337   -15.477 14.318  1.00 35.50  ? 278  TYR A CE1 1 
ATOM   2262 C  CE2 . TYR A 1 278 ? 6.351   -14.466 12.385  1.00 35.58  ? 278  TYR A CE2 1 
ATOM   2263 C  CZ  . TYR A 1 278 ? 7.289   -15.305 12.950  1.00 37.49  ? 278  TYR A CZ  1 
ATOM   2264 O  OH  . TYR A 1 278 ? 8.195   -15.967 12.139  1.00 37.57  ? 278  TYR A OH  1 
ATOM   2265 N  N   . PHE A 1 279 ? 5.046   -10.621 13.967  1.00 31.77  ? 279  PHE A N   1 
ATOM   2266 C  CA  . PHE A 1 279 ? 5.713   -9.922  12.874  1.00 31.95  ? 279  PHE A CA  1 
ATOM   2267 C  C   . PHE A 1 279 ? 6.422   -8.666  13.355  1.00 32.47  ? 279  PHE A C   1 
ATOM   2268 O  O   . PHE A 1 279 ? 7.473   -8.310  12.813  1.00 35.44  ? 279  PHE A O   1 
ATOM   2269 C  CB  . PHE A 1 279 ? 4.711   -9.596  11.765  1.00 30.53  ? 279  PHE A CB  1 
ATOM   2270 C  CG  . PHE A 1 279 ? 4.370   -10.780 10.916  1.00 32.58  ? 279  PHE A CG  1 
ATOM   2271 C  CD1 . PHE A 1 279 ? 5.340   -11.406 10.140  1.00 34.05  ? 279  PHE A CD1 1 
ATOM   2272 C  CD2 . PHE A 1 279 ? 3.073   -11.272 10.882  1.00 36.71  ? 279  PHE A CD2 1 
ATOM   2273 C  CE1 . PHE A 1 279 ? 5.028   -12.503 9.367   1.00 35.69  ? 279  PHE A CE1 1 
ATOM   2274 C  CE2 . PHE A 1 279 ? 2.753   -12.373 10.112  1.00 32.76  ? 279  PHE A CE2 1 
ATOM   2275 C  CZ  . PHE A 1 279 ? 3.727   -12.984 9.337   1.00 37.10  ? 279  PHE A CZ  1 
ATOM   2276 N  N   . LEU A 1 280 ? 5.891   -7.993  14.375  1.00 30.88  ? 280  LEU A N   1 
ATOM   2277 C  CA  . LEU A 1 280 ? 6.534   -6.769  14.841  1.00 32.10  ? 280  LEU A CA  1 
ATOM   2278 C  C   . LEU A 1 280 ? 7.880   -7.063  15.505  1.00 34.50  ? 280  LEU A C   1 
ATOM   2279 O  O   . LEU A 1 280 ? 8.864   -6.353  15.247  1.00 34.26  ? 280  LEU A O   1 
ATOM   2280 C  CB  . LEU A 1 280 ? 5.608   -6.007  15.787  1.00 33.71  ? 280  LEU A CB  1 
ATOM   2281 C  CG  . LEU A 1 280 ? 4.427   -5.274  15.116  1.00 32.87  ? 280  LEU A CG  1 
ATOM   2282 C  CD1 . LEU A 1 280 ? 3.590   -4.498  16.145  1.00 36.44  ? 280  LEU A CD1 1 
ATOM   2283 C  CD2 . LEU A 1 280 ? 4.905   -4.327  14.011  1.00 32.81  ? 280  LEU A CD2 1 
ATOM   2284 N  N   . VAL A 1 281 ? 7.961   -8.104  16.343  1.00 32.75  ? 281  VAL A N   1 
ATOM   2285 C  CA  . VAL A 1 281 ? 9.262   -8.402  16.969  1.00 32.51  ? 281  VAL A CA  1 
ATOM   2286 C  C   . VAL A 1 281 ? 10.239  -9.000  15.964  1.00 37.93  ? 281  VAL A C   1 
ATOM   2287 O  O   . VAL A 1 281 ? 11.460  -8.880  16.146  1.00 36.25  ? 281  VAL A O   1 
ATOM   2288 C  CB  . VAL A 1 281 ? 9.134   -9.320  18.206  1.00 32.71  ? 281  VAL A CB  1 
ATOM   2289 C  CG1 . VAL A 1 281 ? 8.322   -8.631  19.285  1.00 37.89  ? 281  VAL A CG1 1 
ATOM   2290 C  CG2 . VAL A 1 281 ? 8.560   -10.712 17.832  1.00 33.09  ? 281  VAL A CG2 1 
ATOM   2291 N  N   . LYS A 1 282 ? 9.749   -9.626  14.893  1.00 33.32  ? 282  LYS A N   1 
ATOM   2292 C  CA  . LYS A 1 282 ? 10.636  -10.082 13.827  1.00 37.43  ? 282  LYS A CA  1 
ATOM   2293 C  C   . LYS A 1 282 ? 11.049  -8.961  12.873  1.00 35.82  ? 282  LYS A C   1 
ATOM   2294 O  O   . LYS A 1 282 ? 11.954  -9.174  12.052  1.00 40.17  ? 282  LYS A O   1 
ATOM   2295 C  CB  . LYS A 1 282 ? 9.970   -11.205 13.028  1.00 38.93  ? 282  LYS A CB  1 
ATOM   2296 C  CG  . LYS A 1 282 ? 9.724   -12.510 13.817  1.00 35.09  ? 282  LYS A CG  1 
ATOM   2297 C  CD  . LYS A 1 282 ? 11.019  -13.068 14.455  1.00 36.14  ? 282  LYS A CD  1 
ATOM   2298 C  CE  . LYS A 1 282 ? 10.835  -14.539 14.838  1.00 37.69  ? 282  LYS A CE  1 
ATOM   2299 N  NZ  . LYS A 1 282 ? 12.003  -15.070 15.628  1.00 36.12  ? 282  LYS A NZ  1 
ATOM   2300 N  N   . ASN A 1 283 ? 10.419  -7.787  12.957  1.00 35.84  ? 283  ASN A N   1 
ATOM   2301 C  CA  . ASN A 1 283 ? 10.674  -6.667  12.044  1.00 35.52  ? 283  ASN A CA  1 
ATOM   2302 C  C   . ASN A 1 283 ? 10.783  -5.382  12.847  1.00 39.40  ? 283  ASN A C   1 
ATOM   2303 O  O   . ASN A 1 283 ? 9.894   -4.522  12.812  1.00 35.78  ? 283  ASN A O   1 
ATOM   2304 C  CB  . ASN A 1 283 ? 9.573   -6.577  10.984  1.00 36.72  ? 283  ASN A CB  1 
ATOM   2305 C  CG  . ASN A 1 283 ? 9.616   -7.734  10.023  1.00 34.05  ? 283  ASN A CG  1 
ATOM   2306 O  OD1 . ASN A 1 283 ? 10.386  -7.716  9.054   1.00 37.54  ? 283  ASN A OD1 1 
ATOM   2307 N  ND2 . ASN A 1 283 ? 8.823   -8.770  10.290  1.00 32.38  ? 283  ASN A ND2 1 
ATOM   2308 N  N   . PRO A 1 284 ? 11.891  -5.209  13.574  1.00 41.85  ? 284  PRO A N   1 
ATOM   2309 C  CA  . PRO A 1 284 ? 11.975  -4.109  14.550  1.00 43.06  ? 284  PRO A CA  1 
ATOM   2310 C  C   . PRO A 1 284 ? 11.797  -2.732  13.948  1.00 36.33  ? 284  PRO A C   1 
ATOM   2311 O  O   . PRO A 1 284 ? 11.354  -1.820  14.656  1.00 40.89  ? 284  PRO A O   1 
ATOM   2312 C  CB  . PRO A 1 284 ? 13.389  -4.263  15.134  1.00 44.99  ? 284  PRO A CB  1 
ATOM   2313 C  CG  . PRO A 1 284 ? 13.805  -5.650  14.800  1.00 41.56  ? 284  PRO A CG  1 
ATOM   2314 C  CD  . PRO A 1 284 ? 13.115  -6.025  13.534  1.00 44.30  ? 284  PRO A CD  1 
ATOM   2315 N  N   . HIS A 1 285 ? 12.182  -2.542  12.680  1.00 38.85  ? 285  HIS A N   1 
ATOM   2316 C  CA  . HIS A 1 285 ? 12.001  -1.248  12.025  1.00 41.43  ? 285  HIS A CA  1 
ATOM   2317 C  C   . HIS A 1 285 ? 10.521  -0.927  11.881  1.00 34.67  ? 285  HIS A C   1 
ATOM   2318 O  O   . HIS A 1 285 ? 10.095  0.226   12.060  1.00 36.57  ? 285  HIS A O   1 
ATOM   2319 C  CB  . HIS A 1 285 ? 12.679  -1.268  10.653  1.00 43.76  ? 285  HIS A CB  1 
ATOM   2320 C  CG  . HIS A 1 285 ? 14.170  -1.429  10.713  1.00 54.57  ? 285  HIS A CG  1 
ATOM   2321 N  ND1 . HIS A 1 285 ? 14.877  -2.165  9.784   1.00 57.22  ? 285  HIS A ND1 1 
ATOM   2322 C  CD2 . HIS A 1 285 ? 15.087  -0.949  11.588  1.00 57.75  ? 285  HIS A CD2 1 
ATOM   2323 C  CE1 . HIS A 1 285 ? 16.163  -2.136  10.086  1.00 57.68  ? 285  HIS A CE1 1 
ATOM   2324 N  NE2 . HIS A 1 285 ? 16.317  -1.406  11.177  1.00 60.93  ? 285  HIS A NE2 1 
ATOM   2325 N  N   . VAL A 1 286 ? 9.718   -1.949  11.584  1.00 39.32  ? 286  VAL A N   1 
ATOM   2326 C  CA  . VAL A 1 286 ? 8.269   -1.780  11.551  1.00 38.04  ? 286  VAL A CA  1 
ATOM   2327 C  C   . VAL A 1 286 ? 7.736   -1.493  12.950  1.00 35.44  ? 286  VAL A C   1 
ATOM   2328 O  O   . VAL A 1 286 ? 6.946   -0.559  13.156  1.00 35.54  ? 286  VAL A O   1 
ATOM   2329 C  CB  . VAL A 1 286 ? 7.604   -3.021  10.925  1.00 34.50  ? 286  VAL A CB  1 
ATOM   2330 C  CG1 . VAL A 1 286 ? 6.086   -2.844  10.888  1.00 33.67  ? 286  VAL A CG1 1 
ATOM   2331 C  CG2 . VAL A 1 286 ? 8.153   -3.285  9.500   1.00 37.48  ? 286  VAL A CG2 1 
ATOM   2332 N  N   . LEU A 1 287 ? 8.182   -2.272  13.946  1.00 36.70  ? 287  LEU A N   1 
ATOM   2333 C  CA  . LEU A 1 287 ? 7.788   -2.006  15.326  1.00 34.81  ? 287  LEU A CA  1 
ATOM   2334 C  C   . LEU A 1 287 ? 8.073   -0.559  15.712  1.00 33.13  ? 287  LEU A C   1 
ATOM   2335 O  O   . LEU A 1 287 ? 7.208   0.136   16.264  1.00 34.97  ? 287  LEU A O   1 
ATOM   2336 C  CB  . LEU A 1 287 ? 8.501   -2.973  16.275  1.00 35.64  ? 287  LEU A CB  1 
ATOM   2337 C  CG  . LEU A 1 287 ? 7.898   -3.117  17.684  1.00 37.08  ? 287  LEU A CG  1 
ATOM   2338 C  CD1 . LEU A 1 287 ? 8.363   -4.407  18.334  1.00 42.85  ? 287  LEU A CD1 1 
ATOM   2339 C  CD2 . LEU A 1 287 ? 8.251   -1.921  18.562  1.00 39.68  ? 287  LEU A CD2 1 
ATOM   2340 N  N   . GLN A 1 288 ? 9.279   -0.074  15.389  1.00 37.83  ? 288  GLN A N   1 
ATOM   2341 C  CA  . GLN A 1 288 ? 9.629   1.303   15.716  1.00 39.36  ? 288  GLN A CA  1 
ATOM   2342 C  C   . GLN A 1 288 ? 8.656   2.292   15.097  1.00 38.42  ? 288  GLN A C   1 
ATOM   2343 O  O   . GLN A 1 288 ? 8.200   3.228   15.765  1.00 37.67  ? 288  GLN A O   1 
ATOM   2344 C  CB  . GLN A 1 288 ? 11.051  1.622   15.254  1.00 48.04  ? 288  GLN A CB  1 
ATOM   2345 C  CG  . GLN A 1 288 ? 11.558  2.898   15.875  1.00 47.61  ? 288  GLN A CG  1 
ATOM   2346 C  CD  . GLN A 1 288 ? 12.894  3.330   15.329  1.00 59.20  ? 288  GLN A CD  1 
ATOM   2347 O  OE1 . GLN A 1 288 ? 13.626  2.539   14.729  1.00 61.35  ? 288  GLN A OE1 1 
ATOM   2348 N  NE2 . GLN A 1 288 ? 13.220  4.603   15.524  1.00 64.31  ? 288  GLN A NE2 1 
ATOM   2349 N  N   . LYS A 1 289 ? 8.346   2.120   13.805  1.00 38.26  ? 289  LYS A N   1 
ATOM   2350 C  CA  . LYS A 1 289 ? 7.430   3.040   13.138  1.00 37.34  ? 289  LYS A CA  1 
ATOM   2351 C  C   . LYS A 1 289 ? 6.055   3.022   13.791  1.00 33.59  ? 289  LYS A C   1 
ATOM   2352 O  O   . LYS A 1 289 ? 5.444   4.075   14.007  1.00 34.88  ? 289  LYS A O   1 
ATOM   2353 C  CB  . LYS A 1 289 ? 7.333   2.692   11.651  1.00 34.73  ? 289  LYS A CB  1 
ATOM   2354 C  CG  . LYS A 1 289 ? 6.656   3.751   10.785  1.00 39.18  ? 289  LYS A CG  1 
ATOM   2355 C  CD  . LYS A 1 289 ? 6.875   3.449   9.289   1.00 39.16  ? 289  LYS A CD  1 
ATOM   2356 C  CE  . LYS A 1 289 ? 5.955   4.272   8.399   1.00 40.80  ? 289  LYS A CE  1 
ATOM   2357 N  NZ  . LYS A 1 289 ? 6.138   3.935   6.940   1.00 46.30  ? 289  LYS A NZ  1 
ATOM   2358 N  N   . ALA A 1 290 ? 5.545   1.837   14.117  1.00 37.17  ? 290  ALA A N   1 
ATOM   2359 C  CA  . ALA A 1 290 ? 4.237   1.787   14.764  1.00 35.01  ? 290  ALA A CA  1 
ATOM   2360 C  C   . ALA A 1 290 ? 4.307   2.333   16.182  1.00 31.07  ? 290  ALA A C   1 
ATOM   2361 O  O   . ALA A 1 290 ? 3.369   2.996   16.647  1.00 35.27  ? 290  ALA A O   1 
ATOM   2362 C  CB  . ALA A 1 290 ? 3.693   0.359   14.745  1.00 36.53  ? 290  ALA A CB  1 
ATOM   2363 N  N   . ALA A 1 291 ? 5.413   2.077   16.886  1.00 33.82  ? 291  ALA A N   1 
ATOM   2364 C  CA  . ALA A 1 291 ? 5.580   2.637   18.225  1.00 38.39  ? 291  ALA A CA  1 
ATOM   2365 C  C   . ALA A 1 291 ? 5.616   4.161   18.191  1.00 35.88  ? 291  ALA A C   1 
ATOM   2366 O  O   . ALA A 1 291 ? 5.057   4.824   19.074  1.00 38.39  ? 291  ALA A O   1 
ATOM   2367 C  CB  . ALA A 1 291 ? 6.860   2.088   18.862  1.00 38.29  ? 291  ALA A CB  1 
ATOM   2368 N  N   . GLU A 1 292 ? 6.277   4.737   17.177  1.00 36.28  ? 292  GLU A N   1 
ATOM   2369 C  CA  . GLU A 1 292 ? 6.309   6.192   17.059  1.00 37.82  ? 292  GLU A CA  1 
ATOM   2370 C  C   . GLU A 1 292 ? 4.913   6.757   16.862  1.00 38.42  ? 292  GLU A C   1 
ATOM   2371 O  O   . GLU A 1 292 ? 4.551   7.769   17.477  1.00 39.37  ? 292  GLU A O   1 
ATOM   2372 C  CB  . GLU A 1 292 ? 7.233   6.605   15.911  1.00 42.27  ? 292  GLU A CB  1 
ATOM   2373 C  CG  . GLU A 1 292 ? 8.699   6.535   16.319  1.00 47.39  ? 292  GLU A CG  1 
ATOM   2374 C  CD  . GLU A 1 292 ? 9.666   6.510   15.148  1.00 52.81  ? 292  GLU A CD  1 
ATOM   2375 O  OE1 . GLU A 1 292 ? 9.220   6.475   13.983  1.00 54.29  ? 292  GLU A OE1 1 
ATOM   2376 O  OE2 . GLU A 1 292 ? 10.886  6.510   15.405  1.00 52.02  ? 292  GLU A OE2 1 
ATOM   2377 N  N   . GLU A 1 293 ? 4.105   6.111   16.015  1.00 38.66  ? 293  GLU A N   1 
ATOM   2378 C  CA  . GLU A 1 293 ? 2.716   6.528   15.869  1.00 39.49  ? 293  GLU A CA  1 
ATOM   2379 C  C   . GLU A 1 293 ? 1.977   6.453   17.197  1.00 35.65  ? 293  GLU A C   1 
ATOM   2380 O  O   . GLU A 1 293 ? 1.284   7.395   17.594  1.00 37.56  ? 293  GLU A O   1 
ATOM   2381 C  CB  . GLU A 1 293 ? 2.015   5.662   14.826  1.00 35.83  ? 293  GLU A CB  1 
ATOM   2382 C  CG  . GLU A 1 293 ? 0.583   6.109   14.578  1.00 36.85  ? 293  GLU A CG  1 
ATOM   2383 C  CD  . GLU A 1 293 ? -0.079  5.302   13.488  1.00 38.98  ? 293  GLU A CD  1 
ATOM   2384 O  OE1 . GLU A 1 293 ? -0.443  4.136   13.760  1.00 35.90  ? 293  GLU A OE1 1 
ATOM   2385 O  OE2 . GLU A 1 293 ? -0.228  5.831   12.366  1.00 35.87  ? 293  GLU A OE2 1 
ATOM   2386 N  N   . ALA A 1 294 ? 2.094   5.321   17.889  1.00 38.15  ? 294  ALA A N   1 
ATOM   2387 C  CA  . ALA A 1 294 ? 1.400   5.146   19.157  1.00 37.56  ? 294  ALA A CA  1 
ATOM   2388 C  C   . ALA A 1 294 ? 1.743   6.267   20.136  1.00 34.38  ? 294  ALA A C   1 
ATOM   2389 O  O   . ALA A 1 294 ? 0.856   6.858   20.763  1.00 37.88  ? 294  ALA A O   1 
ATOM   2390 C  CB  . ALA A 1 294 ? 1.758   3.778   19.743  1.00 35.81  ? 294  ALA A CB  1 
ATOM   2391 N  N   . ALA A 1 295 ? 3.030   6.601   20.241  1.00 40.17  ? 295  ALA A N   1 
ATOM   2392 C  CA  . ALA A 1 295 ? 3.451   7.645   21.173  1.00 38.28  ? 295  ALA A CA  1 
ATOM   2393 C  C   . ALA A 1 295 ? 2.906   9.010   20.767  1.00 39.30  ? 295  ALA A C   1 
ATOM   2394 O  O   . ALA A 1 295 ? 2.482   9.798   21.620  1.00 39.77  ? 295  ALA A O   1 
ATOM   2395 C  CB  . ALA A 1 295 ? 4.979   7.670   21.262  1.00 41.78  ? 295  ALA A CB  1 
ATOM   2396 N  N   . ARG A 1 296 ? 2.891   9.303   19.466  1.00 43.48  ? 296  ARG A N   1 
ATOM   2397 C  CA  . ARG A 1 296 ? 2.411   10.602  19.002  1.00 41.07  ? 296  ARG A CA  1 
ATOM   2398 C  C   . ARG A 1 296 ? 0.899   10.728  19.151  1.00 40.69  ? 296  ARG A C   1 
ATOM   2399 O  O   . ARG A 1 296 ? 0.385   11.806  19.477  1.00 41.42  ? 296  ARG A O   1 
ATOM   2400 C  CB  . ARG A 1 296 ? 2.835   10.806  17.550  1.00 45.57  ? 296  ARG A CB  1 
ATOM   2401 C  CG  . ARG A 1 296 ? 2.002   11.803  16.795  1.00 42.55  ? 296  ARG A CG  1 
ATOM   2402 C  CD  . ARG A 1 296 ? 2.748   12.267  15.575  1.00 56.28  ? 296  ARG A CD  1 
ATOM   2403 N  NE  . ARG A 1 296 ? 3.315   11.115  14.888  1.00 54.07  ? 296  ARG A NE  1 
ATOM   2404 C  CZ  . ARG A 1 296 ? 2.637   10.317  14.077  1.00 53.05  ? 296  ARG A CZ  1 
ATOM   2405 N  NH1 . ARG A 1 296 ? 1.332   10.471  13.887  1.00 51.72  ? 296  ARG A NH1 1 
ATOM   2406 N  NH2 . ARG A 1 296 ? 3.281   9.331   13.452  1.00 54.99  ? 296  ARG A NH2 1 
ATOM   2407 N  N   . VAL A 1 297 ? 0.168   9.638   18.944  1.00 37.52  ? 297  VAL A N   1 
ATOM   2408 C  CA  . VAL A 1 297 ? -1.293  9.720   18.927  1.00 37.38  ? 297  VAL A CA  1 
ATOM   2409 C  C   . VAL A 1 297 ? -1.892  9.530   20.314  1.00 37.82  ? 297  VAL A C   1 
ATOM   2410 O  O   . VAL A 1 297 ? -2.839  10.228  20.688  1.00 38.90  ? 297  VAL A O   1 
ATOM   2411 C  CB  . VAL A 1 297 ? -1.865  8.694   17.932  1.00 36.07  ? 297  VAL A CB  1 
ATOM   2412 C  CG1 . VAL A 1 297 ? -3.377  8.565   18.133  1.00 36.36  ? 297  VAL A CG1 1 
ATOM   2413 C  CG2 . VAL A 1 297 ? -1.543  9.112   16.503  1.00 35.75  ? 297  VAL A CG2 1 
ATOM   2414 N  N   . LEU A 1 298 ? -1.396  8.563   21.084  1.00 39.81  ? 298  LEU A N   1 
ATOM   2415 C  CA  . LEU A 1 298 ? -2.040  8.195   22.343  1.00 37.88  ? 298  LEU A CA  1 
ATOM   2416 C  C   . LEU A 1 298 ? -1.473  9.050   23.480  1.00 42.72  ? 298  LEU A C   1 
ATOM   2417 O  O   . LEU A 1 298 ? -0.721  8.596   24.347  1.00 42.18  ? 298  LEU A O   1 
ATOM   2418 C  CB  . LEU A 1 298 ? -1.876  6.703   22.603  1.00 36.19  ? 298  LEU A CB  1 
ATOM   2419 C  CG  . LEU A 1 298 ? -2.437  5.785   21.509  1.00 34.84  ? 298  LEU A CG  1 
ATOM   2420 C  CD1 . LEU A 1 298 ? -2.172  4.313   21.852  1.00 34.21  ? 298  LEU A CD1 1 
ATOM   2421 C  CD2 . LEU A 1 298 ? -3.928  6.042   21.320  1.00 39.87  ? 298  LEU A CD2 1 
ATOM   2422 N  N   . VAL A 1 299 ? -1.874  10.327  23.462  1.00 40.16  ? 299  VAL A N   1 
ATOM   2423 C  CA  . VAL A 1 299 ? -1.322  11.324  24.377  1.00 44.99  ? 299  VAL A CA  1 
ATOM   2424 C  C   . VAL A 1 299 ? -2.043  11.364  25.715  1.00 46.87  ? 299  VAL A C   1 
ATOM   2425 O  O   . VAL A 1 299 ? -1.632  12.126  26.603  1.00 44.85  ? 299  VAL A O   1 
ATOM   2426 C  CB  . VAL A 1 299 ? -1.347  12.727  23.733  1.00 40.15  ? 299  VAL A CB  1 
ATOM   2427 C  CG1 . VAL A 1 299 ? -0.522  12.730  22.446  1.00 43.99  ? 299  VAL A CG1 1 
ATOM   2428 C  CG2 . VAL A 1 299 ? -2.790  13.161  23.470  1.00 40.80  ? 299  VAL A CG2 1 
ATOM   2429 N  N   . ASP A 1 300 ? -3.099  10.581  25.896  1.00 40.96  ? 300  ASP A N   1 
ATOM   2430 C  CA  . ASP A 1 300 ? -3.811  10.548  27.160  1.00 43.18  ? 300  ASP A CA  1 
ATOM   2431 C  C   . ASP A 1 300 ? -3.590  9.210   27.864  1.00 43.92  ? 300  ASP A C   1 
ATOM   2432 O  O   . ASP A 1 300 ? -3.183  8.224   27.240  1.00 41.98  ? 300  ASP A O   1 
ATOM   2433 C  CB  . ASP A 1 300 ? -5.312  10.801  26.939  1.00 44.01  ? 300  ASP A CB  1 
ATOM   2434 C  CG  . ASP A 1 300 ? -5.592  12.190  26.372  1.00 49.55  ? 300  ASP A CG  1 
ATOM   2435 O  OD1 . ASP A 1 300 ? -4.942  13.160  26.820  1.00 43.99  ? 300  ASP A OD1 1 
ATOM   2436 O  OD2 . ASP A 1 300 ? -6.449  12.316  25.468  1.00 50.50  ? 300  ASP A OD2 1 
ATOM   2437 N  N   . PRO A 1 301 ? -3.815  9.151   29.177  1.00 44.30  ? 301  PRO A N   1 
ATOM   2438 C  CA  . PRO A 1 301 ? -3.681  7.862   29.886  1.00 45.71  ? 301  PRO A CA  1 
ATOM   2439 C  C   . PRO A 1 301 ? -4.624  6.791   29.359  1.00 40.28  ? 301  PRO A C   1 
ATOM   2440 O  O   . PRO A 1 301 ? -4.273  5.604   29.363  1.00 43.43  ? 301  PRO A O   1 
ATOM   2441 C  CB  . PRO A 1 301 ? -3.996  8.211   31.350  1.00 48.65  ? 301  PRO A CB  1 
ATOM   2442 C  CG  . PRO A 1 301 ? -4.067  9.706   31.434  1.00 48.60  ? 301  PRO A CG  1 
ATOM   2443 C  CD  . PRO A 1 301 ? -4.141  10.286  30.056  1.00 47.52  ? 301  PRO A CD  1 
ATOM   2444 N  N   . VAL A 1 302 ? -5.810  7.185   28.921  1.00 41.18  ? 302  VAL A N   1 
ATOM   2445 C  CA  . VAL A 1 302 ? -6.813  6.294   28.342  1.00 43.33  ? 302  VAL A CA  1 
ATOM   2446 C  C   . VAL A 1 302 ? -6.947  6.656   26.867  1.00 43.66  ? 302  VAL A C   1 
ATOM   2447 O  O   . VAL A 1 302 ? -7.141  7.836   26.552  1.00 43.11  ? 302  VAL A O   1 
ATOM   2448 C  CB  . VAL A 1 302 ? -8.172  6.444   29.061  1.00 44.26  ? 302  VAL A CB  1 
ATOM   2449 C  CG1 . VAL A 1 302 ? -9.241  5.622   28.395  1.00 50.24  ? 302  VAL A CG1 1 
ATOM   2450 C  CG2 . VAL A 1 302 ? -8.051  6.088   30.553  1.00 50.84  ? 302  VAL A CG2 1 
ATOM   2451 N  N   . PRO A 1 303 ? -6.824  5.709   25.933  1.00 41.37  ? 303  PRO A N   1 
ATOM   2452 C  CA  . PRO A 1 303 ? -7.086  6.055   24.527  1.00 37.82  ? 303  PRO A CA  1 
ATOM   2453 C  C   . PRO A 1 303 ? -8.551  6.384   24.302  1.00 39.11  ? 303  PRO A C   1 
ATOM   2454 O  O   . PRO A 1 303 ? -9.447  5.779   24.899  1.00 36.81  ? 303  PRO A O   1 
ATOM   2455 C  CB  . PRO A 1 303 ? -6.674  4.793   23.758  1.00 42.52  ? 303  PRO A CB  1 
ATOM   2456 C  CG  . PRO A 1 303 ? -5.707  4.109   24.666  1.00 42.44  ? 303  PRO A CG  1 
ATOM   2457 C  CD  . PRO A 1 303 ? -6.208  4.376   26.052  1.00 41.39  ? 303  PRO A CD  1 
ATOM   2458 N  N   . SER A 1 304 ? -8.791  7.360   23.425  1.00 36.52  ? 304  SER A N   1 
ATOM   2459 C  CA  . SER A 1 304 ? -10.142 7.694   23.000  1.00 37.09  ? 304  SER A CA  1 
ATOM   2460 C  C   . SER A 1 304 ? -10.465 7.026   21.660  1.00 34.11  ? 304  SER A C   1 
ATOM   2461 O  O   . SER A 1 304 ? -9.576  6.609   20.918  1.00 35.32  ? 304  SER A O   1 
ATOM   2462 C  CB  . SER A 1 304 ? -10.303 9.211   22.881  1.00 38.69  ? 304  SER A CB  1 
ATOM   2463 O  OG  . SER A 1 304 ? -9.637  9.674   21.726  1.00 36.37  ? 304  SER A OG  1 
ATOM   2464 N  N   . TYR A 1 305 ? -11.767 6.938   21.365  1.00 36.79  ? 305  TYR A N   1 
ATOM   2465 C  CA  . TYR A 1 305 ? -12.203 6.429   20.066  1.00 36.03  ? 305  TYR A CA  1 
ATOM   2466 C  C   . TYR A 1 305 ? -11.542 7.201   18.933  1.00 38.25  ? 305  TYR A C   1 
ATOM   2467 O  O   . TYR A 1 305 ? -11.008 6.609   17.989  1.00 36.86  ? 305  TYR A O   1 
ATOM   2468 C  CB  . TYR A 1 305 ? -13.723 6.519   19.954  1.00 37.45  ? 305  TYR A CB  1 
ATOM   2469 C  CG  . TYR A 1 305 ? -14.257 6.127   18.597  1.00 38.92  ? 305  TYR A CG  1 
ATOM   2470 C  CD1 . TYR A 1 305 ? -14.517 4.797   18.296  1.00 38.82  ? 305  TYR A CD1 1 
ATOM   2471 C  CD2 . TYR A 1 305 ? -14.480 7.084   17.612  1.00 39.77  ? 305  TYR A CD2 1 
ATOM   2472 C  CE1 . TYR A 1 305 ? -15.004 4.429   17.043  1.00 41.14  ? 305  TYR A CE1 1 
ATOM   2473 C  CE2 . TYR A 1 305 ? -14.960 6.724   16.358  1.00 40.91  ? 305  TYR A CE2 1 
ATOM   2474 C  CZ  . TYR A 1 305 ? -15.215 5.396   16.086  1.00 40.82  ? 305  TYR A CZ  1 
ATOM   2475 O  OH  . TYR A 1 305 ? -15.695 5.027   14.852  1.00 48.62  ? 305  TYR A OH  1 
ATOM   2476 N  N   . LYS A 1 306 ? -11.573 8.538   19.013  1.00 39.76  ? 306  LYS A N   1 
ATOM   2477 C  CA  . LYS A 1 306 ? -10.983 9.358   17.960  1.00 38.37  ? 306  LYS A CA  1 
ATOM   2478 C  C   . LYS A 1 306 ? -9.502  9.068   17.795  1.00 37.76  ? 306  LYS A C   1 
ATOM   2479 O  O   . LYS A 1 306 ? -8.991  9.043   16.670  1.00 38.51  ? 306  LYS A O   1 
ATOM   2480 C  CB  . LYS A 1 306 ? -11.195 10.842  18.264  1.00 44.20  ? 306  LYS A CB  1 
ATOM   2481 C  CG  . LYS A 1 306 ? -12.643 11.268  18.259  1.00 46.56  ? 306  LYS A CG  1 
ATOM   2482 C  CD  . LYS A 1 306 ? -12.771 12.744  17.915  1.00 50.23  ? 306  LYS A CD  1 
ATOM   2483 C  CE  . LYS A 1 306 ? -13.975 13.354  18.607  1.00 58.23  ? 306  LYS A CE  1 
ATOM   2484 N  NZ  . LYS A 1 306 ? -13.619 14.623  19.312  1.00 67.03  ? 306  LYS A NZ  1 
ATOM   2485 N  N   . GLN A 1 307 ? -8.788  8.861   18.906  1.00 34.65  ? 307  GLN A N   1 
ATOM   2486 C  CA  . GLN A 1 307 ? -7.358  8.584   18.800  1.00 35.18  ? 307  GLN A CA  1 
ATOM   2487 C  C   . GLN A 1 307 ? -7.102  7.249   18.113  1.00 35.74  ? 307  GLN A C   1 
ATOM   2488 O  O   . GLN A 1 307 ? -6.186  7.136   17.296  1.00 36.03  ? 307  GLN A O   1 
ATOM   2489 C  CB  . GLN A 1 307 ? -6.704  8.606   20.185  1.00 34.45  ? 307  GLN A CB  1 
ATOM   2490 C  CG  . GLN A 1 307 ? -6.503  10.023  20.712  1.00 38.86  ? 307  GLN A CG  1 
ATOM   2491 C  CD  . GLN A 1 307 ? -6.339  10.089  22.222  1.00 42.21  ? 307  GLN A CD  1 
ATOM   2492 O  OE1 . GLN A 1 307 ? -6.545  9.102   22.927  1.00 40.80  ? 307  GLN A OE1 1 
ATOM   2493 N  NE2 . GLN A 1 307 ? -5.991  11.274  22.729  1.00 41.72  ? 307  GLN A NE2 1 
ATOM   2494 N  N   . VAL A 1 308 ? -7.882  6.218   18.448  1.00 37.36  ? 308  VAL A N   1 
ATOM   2495 C  CA  . VAL A 1 308 ? -7.678  4.924   17.801  1.00 34.03  ? 308  VAL A CA  1 
ATOM   2496 C  C   . VAL A 1 308 ? -7.876  5.046   16.290  1.00 33.87  ? 308  VAL A C   1 
ATOM   2497 O  O   . VAL A 1 308 ? -7.158  4.422   15.502  1.00 33.85  ? 308  VAL A O   1 
ATOM   2498 C  CB  . VAL A 1 308 ? -8.609  3.866   18.420  1.00 34.35  ? 308  VAL A CB  1 
ATOM   2499 C  CG1 . VAL A 1 308 ? -8.562  2.566   17.595  1.00 34.48  ? 308  VAL A CG1 1 
ATOM   2500 C  CG2 . VAL A 1 308 ? -8.216  3.615   19.885  1.00 35.77  ? 308  VAL A CG2 1 
ATOM   2501 N  N   . LYS A 1 309 ? -8.838  5.869   15.864  1.00 37.76  ? 309  LYS A N   1 
ATOM   2502 C  CA  . LYS A 1 309 ? -9.045  6.083   14.434  1.00 37.29  ? 309  LYS A CA  1 
ATOM   2503 C  C   . LYS A 1 309 ? -7.834  6.708   13.760  1.00 38.40  ? 309  LYS A C   1 
ATOM   2504 O  O   . LYS A 1 309 ? -7.683  6.588   12.539  1.00 36.75  ? 309  LYS A O   1 
ATOM   2505 C  CB  . LYS A 1 309 ? -10.276 6.959   14.208  1.00 36.51  ? 309  LYS A CB  1 
ATOM   2506 C  CG  . LYS A 1 309 ? -11.572 6.278   14.577  1.00 40.64  ? 309  LYS A CG  1 
ATOM   2507 C  CD  . LYS A 1 309 ? -11.615 4.892   13.943  1.00 42.30  ? 309  LYS A CD  1 
ATOM   2508 C  CE  . LYS A 1 309 ? -12.985 4.259   14.040  1.00 51.66  ? 309  LYS A CE  1 
ATOM   2509 N  NZ  . LYS A 1 309 ? -12.972 2.888   13.453  1.00 57.09  ? 309  LYS A NZ  1 
ATOM   2510 N  N   . GLN A 1 310 ? -6.966  7.368   14.516  1.00 36.39  ? 310  GLN A N   1 
ATOM   2511 C  CA  . GLN A 1 310 ? -5.793  8.002   13.942  1.00 37.91  ? 310  GLN A CA  1 
ATOM   2512 C  C   . GLN A 1 310 ? -4.567  7.107   13.963  1.00 37.69  ? 310  GLN A C   1 
ATOM   2513 O  O   . GLN A 1 310 ? -3.501  7.528   13.503  1.00 35.73  ? 310  GLN A O   1 
ATOM   2514 C  CB  . GLN A 1 310 ? -5.512  9.329   14.663  1.00 36.33  ? 310  GLN A CB  1 
ATOM   2515 C  CG  . GLN A 1 310 ? -6.572  10.396  14.366  1.00 40.95  ? 310  GLN A CG  1 
ATOM   2516 C  CD  . GLN A 1 310 ? -6.783  10.604  12.859  1.00 46.32  ? 310  GLN A CD  1 
ATOM   2517 O  OE1 . GLN A 1 310 ? -5.821  10.765  12.111  1.00 49.86  ? 310  GLN A OE1 1 
ATOM   2518 N  NE2 . GLN A 1 310 ? -8.040  10.601  12.418  1.00 48.12  ? 310  GLN A NE2 1 
ATOM   2519 N  N   . LEU A 1 311 ? -4.690  5.874   14.460  1.00 32.32  ? 311  LEU A N   1 
ATOM   2520 C  CA  . LEU A 1 311 ? -3.575  4.923   14.446  1.00 32.32  ? 311  LEU A CA  1 
ATOM   2521 C  C   . LEU A 1 311 ? -3.516  4.214   13.088  1.00 35.25  ? 311  LEU A C   1 
ATOM   2522 O  O   . LEU A 1 311 ? -3.700  3.001   12.957  1.00 35.19  ? 311  LEU A O   1 
ATOM   2523 C  CB  . LEU A 1 311 ? -3.714  3.934   15.595  1.00 32.20  ? 311  LEU A CB  1 
ATOM   2524 C  CG  . LEU A 1 311 ? -3.597  4.522   17.016  1.00 32.64  ? 311  LEU A CG  1 
ATOM   2525 C  CD1 . LEU A 1 311 ? -3.888  3.468   18.088  1.00 32.53  ? 311  LEU A CD1 1 
ATOM   2526 C  CD2 . LEU A 1 311 ? -2.215  5.137   17.226  1.00 37.63  ? 311  LEU A CD2 1 
ATOM   2527 N  N   . LYS A 1 312 ? -3.212  5.002   12.057  1.00 35.01  ? 312  LYS A N   1 
ATOM   2528 C  CA  . LYS A 1 312 ? -3.371  4.505   10.698  1.00 34.20  ? 312  LYS A CA  1 
ATOM   2529 C  C   . LYS A 1 312 ? -2.296  3.478   10.355  1.00 32.73  ? 312  LYS A C   1 
ATOM   2530 O  O   . LYS A 1 312 ? -2.581  2.482   9.685   1.00 33.47  ? 312  LYS A O   1 
ATOM   2531 C  CB  . LYS A 1 312 ? -3.371  5.684   9.724   1.00 39.81  ? 312  LYS A CB  1 
ATOM   2532 C  CG  . LYS A 1 312 ? -4.679  6.472   9.813   1.00 46.09  ? 312  LYS A CG  1 
ATOM   2533 C  CD  . LYS A 1 312 ? -4.555  7.895   9.282   1.00 50.06  ? 312  LYS A CD  1 
ATOM   2534 C  CE  . LYS A 1 312 ? -5.907  8.614   9.302   1.00 58.41  ? 312  LYS A CE  1 
ATOM   2535 N  NZ  . LYS A 1 312 ? -7.044  7.710   8.989   1.00 60.83  ? 312  LYS A NZ  1 
ATOM   2536 N  N   . TYR A 1 313 ? -1.057  3.690   10.825  1.00 34.71  ? 313  TYR A N   1 
ATOM   2537 C  CA  . TYR A 1 313 ? -0.000  2.726   10.540  1.00 32.65  ? 313  TYR A CA  1 
ATOM   2538 C  C   . TYR A 1 313 ? -0.214  1.431   11.315  1.00 31.89  ? 313  TYR A C   1 
ATOM   2539 O  O   . TYR A 1 313 ? 0.039   0.343   10.787  1.00 32.71  ? 313  TYR A O   1 
ATOM   2540 C  CB  . TYR A 1 313 ? 1.381   3.305   10.865  1.00 36.92  ? 313  TYR A CB  1 
ATOM   2541 C  CG  . TYR A 1 313 ? 2.494   2.425   10.343  1.00 35.32  ? 313  TYR A CG  1 
ATOM   2542 C  CD1 . TYR A 1 313 ? 2.761   2.361   8.978   1.00 36.80  ? 313  TYR A CD1 1 
ATOM   2543 C  CD2 . TYR A 1 313 ? 3.271   1.649   11.196  1.00 35.21  ? 313  TYR A CD2 1 
ATOM   2544 C  CE1 . TYR A 1 313 ? 3.769   1.563   8.477   1.00 35.40  ? 313  TYR A CE1 1 
ATOM   2545 C  CE2 . TYR A 1 313 ? 4.272   0.827   10.700  1.00 33.90  ? 313  TYR A CE2 1 
ATOM   2546 C  CZ  . TYR A 1 313 ? 4.523   0.800   9.339   1.00 37.58  ? 313  TYR A CZ  1 
ATOM   2547 O  OH  . TYR A 1 313 ? 5.511   -0.002  8.838   1.00 34.76  ? 313  TYR A OH  1 
ATOM   2548 N  N   . VAL A 1 314 ? -0.661  1.531   12.572  1.00 31.98  ? 314  VAL A N   1 
ATOM   2549 C  CA  . VAL A 1 314 ? -1.049  0.331   13.299  1.00 31.42  ? 314  VAL A CA  1 
ATOM   2550 C  C   . VAL A 1 314 ? -2.101  -0.431  12.499  1.00 32.50  ? 314  VAL A C   1 
ATOM   2551 O  O   . VAL A 1 314 ? -2.063  -1.661  12.406  1.00 32.16  ? 314  VAL A O   1 
ATOM   2552 C  CB  . VAL A 1 314 ? -1.555  0.701   14.705  1.00 33.03  ? 314  VAL A CB  1 
ATOM   2553 C  CG1 . VAL A 1 314 ? -2.080  -0.538  15.444  1.00 33.96  ? 314  VAL A CG1 1 
ATOM   2554 C  CG2 . VAL A 1 314 ? -0.450  1.379   15.524  1.00 36.33  ? 314  VAL A CG2 1 
ATOM   2555 N  N   . GLY A 1 315 ? -3.040  0.293   11.893  1.00 31.41  ? 315  GLY A N   1 
ATOM   2556 C  CA  . GLY A 1 315 ? -4.033  -0.365  11.057  1.00 33.68  ? 315  GLY A CA  1 
ATOM   2557 C  C   . GLY A 1 315 ? -3.418  -1.099  9.875   1.00 33.27  ? 315  GLY A C   1 
ATOM   2558 O  O   . GLY A 1 315 ? -3.869  -2.192  9.503   1.00 31.01  ? 315  GLY A O   1 
ATOM   2559 N  N   . MET A 1 316 ? -2.390  -0.502  9.255   1.00 31.73  ? 316  MET A N   1 
ATOM   2560 C  CA  . MET A 1 316 ? -1.708  -1.157  8.143   1.00 31.72  ? 316  MET A CA  1 
ATOM   2561 C  C   . MET A 1 316 ? -0.941  -2.387  8.618   1.00 29.81  ? 316  MET A C   1 
ATOM   2562 O  O   . MET A 1 316 ? -0.854  -3.396  7.905   1.00 30.74  ? 316  MET A O   1 
ATOM   2563 C  CB  . MET A 1 316 ? -0.749  -0.165  7.466   1.00 36.44  ? 316  MET A CB  1 
ATOM   2564 C  CG  . MET A 1 316 ? -1.326  0.568   6.277   1.00 43.81  ? 316  MET A CG  1 
ATOM   2565 S  SD  . MET A 1 316 ? -0.540  2.189   6.051   1.00 47.55  ? 316  MET A SD  1 
ATOM   2566 C  CE  . MET A 1 316 ? 1.118   1.679   5.647   1.00 43.74  ? 316  MET A CE  1 
ATOM   2567 N  N   . VAL A 1 317 ? -0.365  -2.314  9.821   1.00 30.65  ? 317  VAL A N   1 
ATOM   2568 C  CA  . VAL A 1 317 ? 0.317   -3.465  10.407  1.00 31.12  ? 317  VAL A CA  1 
ATOM   2569 C  C   . VAL A 1 317 ? -0.644  -4.638  10.545  1.00 29.85  ? 317  VAL A C   1 
ATOM   2570 O  O   . VAL A 1 317 ? -0.322  -5.779  10.194  1.00 32.22  ? 317  VAL A O   1 
ATOM   2571 C  CB  . VAL A 1 317 ? 0.925   -3.087  11.770  1.00 30.15  ? 317  VAL A CB  1 
ATOM   2572 C  CG1 . VAL A 1 317 ? 1.283   -4.331  12.557  1.00 28.89  ? 317  VAL A CG1 1 
ATOM   2573 C  CG2 . VAL A 1 317 ? 2.164   -2.181  11.575  1.00 33.23  ? 317  VAL A CG2 1 
ATOM   2574 N  N   . LEU A 1 318 ? -1.847  -4.365  11.049  1.00 31.11  ? 318  LEU A N   1 
ATOM   2575 C  CA  . LEU A 1 318 ? -2.831  -5.428  11.210  1.00 29.81  ? 318  LEU A CA  1 
ATOM   2576 C  C   . LEU A 1 318 ? -3.257  -5.993  9.861   1.00 29.54  ? 318  LEU A C   1 
ATOM   2577 O  O   . LEU A 1 318 ? -3.405  -7.206  9.711   1.00 29.42  ? 318  LEU A O   1 
ATOM   2578 C  CB  . LEU A 1 318 ? -4.039  -4.904  11.992  1.00 31.24  ? 318  LEU A CB  1 
ATOM   2579 C  CG  . LEU A 1 318 ? -3.735  -4.548  13.455  1.00 29.58  ? 318  LEU A CG  1 
ATOM   2580 C  CD1 . LEU A 1 318 ? -4.847  -3.685  14.041  1.00 31.10  ? 318  LEU A CD1 1 
ATOM   2581 C  CD2 . LEU A 1 318 ? -3.524  -5.828  14.266  1.00 29.98  ? 318  LEU A CD2 1 
ATOM   2582 N  N   . ASN A 1 319 ? -3.456  -5.135  8.860   1.00 29.25  ? 319  ASN A N   1 
ATOM   2583 C  CA  . ASN A 1 319 ? -3.831  -5.659  7.554   1.00 31.64  ? 319  ASN A CA  1 
ATOM   2584 C  C   . ASN A 1 319 ? -2.727  -6.531  6.983   1.00 31.88  ? 319  ASN A C   1 
ATOM   2585 O  O   . ASN A 1 319 ? -2.999  -7.560  6.362   1.00 29.92  ? 319  ASN A O   1 
ATOM   2586 C  CB  . ASN A 1 319 ? -4.171  -4.517  6.601   1.00 32.12  ? 319  ASN A CB  1 
ATOM   2587 C  CG  . ASN A 1 319 ? -5.593  -4.045  6.780   1.00 36.88  ? 319  ASN A CG  1 
ATOM   2588 O  OD1 . ASN A 1 319 ? -6.468  -4.831  7.137   1.00 36.67  ? 319  ASN A OD1 1 
ATOM   2589 N  ND2 . ASN A 1 319 ? -5.833  -2.754  6.553   1.00 39.85  ? 319  ASN A ND2 1 
ATOM   2590 N  N   . GLU A 1 320 ? -1.466  -6.144  7.198   1.00 30.94  ? 320  GLU A N   1 
ATOM   2591 C  CA  . GLU A 1 320 ? -0.379  -6.943  6.657   1.00 27.57  ? 320  GLU A CA  1 
ATOM   2592 C  C   . GLU A 1 320 ? -0.254  -8.273  7.399   1.00 28.12  ? 320  GLU A C   1 
ATOM   2593 O  O   . GLU A 1 320 ? 0.069   -9.292  6.782   1.00 30.14  ? 320  GLU A O   1 
ATOM   2594 C  CB  . GLU A 1 320 ? 0.932   -6.142  6.706   1.00 30.42  ? 320  GLU A CB  1 
ATOM   2595 C  CG  . GLU A 1 320 ? 2.168   -6.894  6.205   1.00 31.01  ? 320  GLU A CG  1 
ATOM   2596 C  CD  . GLU A 1 320 ? 2.236   -7.024  4.696   1.00 34.74  ? 320  GLU A CD  1 
ATOM   2597 O  OE1 . GLU A 1 320 ? 1.185   -6.925  4.012   1.00 32.74  ? 320  GLU A OE1 1 
ATOM   2598 O  OE2 . GLU A 1 320 ? 3.346   -7.271  4.175   1.00 32.46  ? 320  GLU A OE2 1 
ATOM   2599 N  N   . ALA A 1 321 ? -0.559  -8.300  8.710   1.00 29.28  ? 321  ALA A N   1 
ATOM   2600 C  CA  . ALA A 1 321 ? -0.620  -9.579  9.420   1.00 30.01  ? 321  ALA A CA  1 
ATOM   2601 C  C   . ALA A 1 321 ? -1.767  -10.448 8.902   1.00 28.68  ? 321  ALA A C   1 
ATOM   2602 O  O   . ALA A 1 321 ? -1.620  -11.665 8.774   1.00 29.62  ? 321  ALA A O   1 
ATOM   2603 C  CB  . ALA A 1 321 ? -0.762  -9.338  10.933  1.00 28.58  ? 321  ALA A CB  1 
ATOM   2604 N  N   . LEU A 1 322 ? -2.920  -9.844  8.594   1.00 29.20  ? 322  LEU A N   1 
ATOM   2605 C  CA  . LEU A 1 322 ? -4.004  -10.624 7.990   1.00 27.61  ? 322  LEU A CA  1 
ATOM   2606 C  C   . LEU A 1 322 ? -3.663  -11.092 6.577   1.00 28.40  ? 322  LEU A C   1 
ATOM   2607 O  O   . LEU A 1 322 ? -4.238  -12.080 6.092   1.00 29.73  ? 322  LEU A O   1 
ATOM   2608 C  CB  . LEU A 1 322 ? -5.296  -9.800  7.942   1.00 30.16  ? 322  LEU A CB  1 
ATOM   2609 C  CG  . LEU A 1 322 ? -5.992  -9.595  9.283   1.00 30.73  ? 322  LEU A CG  1 
ATOM   2610 C  CD1 . LEU A 1 322 ? -7.130  -8.599  9.111   1.00 31.30  ? 322  LEU A CD1 1 
ATOM   2611 C  CD2 . LEU A 1 322 ? -6.490  -10.933 9.831   1.00 29.66  ? 322  LEU A CD2 1 
ATOM   2612 N  N   . ARG A 1 323 ? -2.782  -10.376 5.875   1.00 27.48  ? 323  ARG A N   1 
ATOM   2613 C  CA  . ARG A 1 323 ? -2.388  -10.840 4.555   1.00 27.48  ? 323  ARG A CA  1 
ATOM   2614 C  C   . ARG A 1 323 ? -1.599  -12.133 4.673   1.00 27.44  ? 323  ARG A C   1 
ATOM   2615 O  O   . ARG A 1 323 ? -1.928  -13.137 4.043   1.00 29.29  ? 323  ARG A O   1 
ATOM   2616 C  CB  . ARG A 1 323 ? -1.566  -9.773  3.814   1.00 28.86  ? 323  ARG A CB  1 
ATOM   2617 C  CG  . ARG A 1 323 ? -1.256  -10.202 2.383   1.00 30.07  ? 323  ARG A CG  1 
ATOM   2618 C  CD  . ARG A 1 323 ? -0.353  -9.201  1.648   1.00 30.78  ? 323  ARG A CD  1 
ATOM   2619 N  NE  . ARG A 1 323 ? 0.969   -9.123  2.267   1.00 32.28  ? 323  ARG A NE  1 
ATOM   2620 C  CZ  . ARG A 1 323 ? 1.972   -9.948  1.989   1.00 33.99  ? 323  ARG A CZ  1 
ATOM   2621 N  NH1 . ARG A 1 323 ? 1.827   -10.943 1.141   1.00 33.00  ? 323  ARG A NH1 1 
ATOM   2622 N  NH2 . ARG A 1 323 ? 3.145   -9.783  2.600   1.00 32.90  ? 323  ARG A NH2 1 
ATOM   2623 N  N   . LEU A 1 324 ? -0.574  -12.142 5.521   1.00 31.13  ? 324  LEU A N   1 
ATOM   2624 C  CA  . LEU A 1 324 ? 0.287   -13.314 5.581   1.00 31.53  ? 324  LEU A CA  1 
ATOM   2625 C  C   . LEU A 1 324 ? -0.391  -14.490 6.285   1.00 32.46  ? 324  LEU A C   1 
ATOM   2626 O  O   . LEU A 1 324 ? -0.242  -15.643 5.864   1.00 32.01  ? 324  LEU A O   1 
ATOM   2627 C  CB  . LEU A 1 324 ? 1.598   -12.924 6.255   1.00 33.41  ? 324  LEU A CB  1 
ATOM   2628 C  CG  . LEU A 1 324 ? 2.493   -12.194 5.253   1.00 37.04  ? 324  LEU A CG  1 
ATOM   2629 C  CD1 . LEU A 1 324 ? 3.656   -11.494 5.964   1.00 37.88  ? 324  LEU A CD1 1 
ATOM   2630 C  CD2 . LEU A 1 324 ? 2.990   -13.170 4.183   1.00 38.33  ? 324  LEU A CD2 1 
ATOM   2631 N  N   . TRP A 1 325 ? -1.147  -14.239 7.352   1.00 30.22  ? 325  TRP A N   1 
ATOM   2632 C  CA  . TRP A 1 325 ? -1.797  -15.320 8.098   1.00 28.72  ? 325  TRP A CA  1 
ATOM   2633 C  C   . TRP A 1 325 ? -3.225  -14.937 8.453   1.00 29.08  ? 325  TRP A C   1 
ATOM   2634 O  O   . TRP A 1 325 ? -3.536  -14.633 9.610   1.00 30.08  ? 325  TRP A O   1 
ATOM   2635 C  CB  . TRP A 1 325 ? -0.973  -15.686 9.338   1.00 29.78  ? 325  TRP A CB  1 
ATOM   2636 C  CG  . TRP A 1 325 ? 0.240   -16.410 8.916   1.00 30.75  ? 325  TRP A CG  1 
ATOM   2637 C  CD1 . TRP A 1 325 ? 1.534   -15.980 9.025   1.00 32.21  ? 325  TRP A CD1 1 
ATOM   2638 C  CD2 . TRP A 1 325 ? 0.285   -17.672 8.244   1.00 29.83  ? 325  TRP A CD2 1 
ATOM   2639 N  NE1 . TRP A 1 325 ? 2.384   -16.912 8.465   1.00 34.04  ? 325  TRP A NE1 1 
ATOM   2640 C  CE2 . TRP A 1 325 ? 1.640   -17.963 7.990   1.00 32.81  ? 325  TRP A CE2 1 
ATOM   2641 C  CE3 . TRP A 1 325 ? -0.688  -18.604 7.853   1.00 31.22  ? 325  TRP A CE3 1 
ATOM   2642 C  CZ2 . TRP A 1 325 ? 2.045   -19.140 7.348   1.00 36.20  ? 325  TRP A CZ2 1 
ATOM   2643 C  CZ3 . TRP A 1 325 ? -0.287  -19.765 7.207   1.00 36.99  ? 325  TRP A CZ3 1 
ATOM   2644 C  CH2 . TRP A 1 325 ? 1.078   -20.024 6.969   1.00 35.22  ? 325  TRP A CH2 1 
ATOM   2645 N  N   . PRO A 1 326 ? -4.132  -14.975 7.477   1.00 28.47  ? 326  PRO A N   1 
ATOM   2646 C  CA  . PRO A 1 326 ? -5.560  -14.733 7.768   1.00 28.97  ? 326  PRO A CA  1 
ATOM   2647 C  C   . PRO A 1 326 ? -6.116  -15.815 8.684   1.00 28.31  ? 326  PRO A C   1 
ATOM   2648 O  O   . PRO A 1 326 ? -6.077  -17.004 8.353   1.00 30.41  ? 326  PRO A O   1 
ATOM   2649 C  CB  . PRO A 1 326 ? -6.211  -14.771 6.380   1.00 30.31  ? 326  PRO A CB  1 
ATOM   2650 C  CG  . PRO A 1 326 ? -5.292  -15.649 5.558   1.00 29.25  ? 326  PRO A CG  1 
ATOM   2651 C  CD  . PRO A 1 326 ? -3.906  -15.311 6.056   1.00 29.80  ? 326  PRO A CD  1 
ATOM   2652 N  N   . THR A 1 327 ? -6.669  -15.399 9.838   1.00 30.89  ? 327  THR A N   1 
ATOM   2653 C  CA  . THR A 1 327 ? -6.908  -16.338 10.938  1.00 28.97  ? 327  THR A CA  1 
ATOM   2654 C  C   . THR A 1 327 ? -8.166  -17.179 10.752  1.00 31.98  ? 327  THR A C   1 
ATOM   2655 O  O   . THR A 1 327 ? -8.277  -18.241 11.379  1.00 31.53  ? 327  THR A O   1 
ATOM   2656 C  CB  . THR A 1 327 ? -6.951  -15.574 12.272  1.00 30.66  ? 327  THR A CB  1 
ATOM   2657 O  OG1 . THR A 1 327 ? -7.781  -14.412 12.145  1.00 28.58  ? 327  THR A OG1 1 
ATOM   2658 C  CG2 . THR A 1 327 ? -5.545  -15.087 12.623  1.00 30.07  ? 327  THR A CG2 1 
ATOM   2659 N  N   . ALA A 1 328 ? -9.116  -16.741 9.907   1.00 29.58  ? 328  ALA A N   1 
ATOM   2660 C  CA  . ALA A 1 328 ? -10.112 -17.658 9.379   1.00 29.31  ? 328  ALA A CA  1 
ATOM   2661 C  C   . ALA A 1 328 ? -9.709  -17.994 7.949   1.00 30.79  ? 328  ALA A C   1 
ATOM   2662 O  O   . ALA A 1 328 ? -10.047 -17.255 7.020   1.00 34.19  ? 328  ALA A O   1 
ATOM   2663 C  CB  . ALA A 1 328 ? -11.510 -17.043 9.421   1.00 32.15  ? 328  ALA A CB  1 
ATOM   2664 N  N   . PRO A 1 329 ? -8.977  -19.093 7.738   1.00 28.21  ? 329  PRO A N   1 
ATOM   2665 C  CA  . PRO A 1 329 ? -8.132  -19.207 6.543   1.00 29.77  ? 329  PRO A CA  1 
ATOM   2666 C  C   . PRO A 1 329 ? -8.844  -19.639 5.273   1.00 30.69  ? 329  PRO A C   1 
ATOM   2667 O  O   . PRO A 1 329 ? -8.196  -19.730 4.224   1.00 29.54  ? 329  PRO A O   1 
ATOM   2668 C  CB  . PRO A 1 329 ? -7.089  -20.254 6.977   1.00 31.37  ? 329  PRO A CB  1 
ATOM   2669 C  CG  . PRO A 1 329 ? -7.847  -21.151 7.920   1.00 29.33  ? 329  PRO A CG  1 
ATOM   2670 C  CD  . PRO A 1 329 ? -8.722  -20.170 8.718   1.00 28.31  ? 329  PRO A CD  1 
ATOM   2671 N  N   . ALA A 1 330 ? -10.147 -19.885 5.295   1.00 29.18  ? 330  ALA A N   1 
ATOM   2672 C  CA  . ALA A 1 330 ? -10.820 -20.286 4.068   1.00 28.43  ? 330  ALA A CA  1 
ATOM   2673 C  C   . ALA A 1 330 ? -12.287 -19.935 4.185   1.00 30.06  ? 330  ALA A C   1 
ATOM   2674 O  O   . ALA A 1 330 ? -12.829 -19.794 5.284   1.00 31.64  ? 330  ALA A O   1 
ATOM   2675 C  CB  . ALA A 1 330 ? -10.661 -21.785 3.788   1.00 31.24  ? 330  ALA A CB  1 
ATOM   2676 N  N   . PHE A 1 331 ? -12.911 -19.764 3.028   1.00 27.52  ? 331  PHE A N   1 
ATOM   2677 C  CA  . PHE A 1 331 ? -14.358 -19.765 2.950   1.00 30.16  ? 331  PHE A CA  1 
ATOM   2678 C  C   . PHE A 1 331 ? -14.743 -20.520 1.691   1.00 32.26  ? 331  PHE A C   1 
ATOM   2679 O  O   . PHE A 1 331 ? -13.917 -20.748 0.804   1.00 32.03  ? 331  PHE A O   1 
ATOM   2680 C  CB  . PHE A 1 331 ? -14.965 -18.353 2.990   1.00 29.45  ? 331  PHE A CB  1 
ATOM   2681 C  CG  . PHE A 1 331 ? -14.444 -17.400 1.956   1.00 30.09  ? 331  PHE A CG  1 
ATOM   2682 C  CD1 . PHE A 1 331 ? -13.320 -16.633 2.207   1.00 31.61  ? 331  PHE A CD1 1 
ATOM   2683 C  CD2 . PHE A 1 331 ? -15.131 -17.203 0.764   1.00 29.47  ? 331  PHE A CD2 1 
ATOM   2684 C  CE1 . PHE A 1 331 ? -12.859 -15.719 1.271   1.00 31.89  ? 331  PHE A CE1 1 
ATOM   2685 C  CE2 . PHE A 1 331 ? -14.670 -16.268 -0.184  1.00 32.00  ? 331  PHE A CE2 1 
ATOM   2686 C  CZ  . PHE A 1 331 ? -13.547 -15.533 0.075   1.00 31.11  ? 331  PHE A CZ  1 
ATOM   2687 N  N   . SER A 1 332 ? -16.009 -20.915 1.632   1.00 31.82  ? 332  SER A N   1 
ATOM   2688 C  CA  . SER A 1 332 ? -16.508 -21.815 0.608   1.00 29.91  ? 332  SER A CA  1 
ATOM   2689 C  C   . SER A 1 332 ? -17.658 -21.162 -0.148  1.00 31.30  ? 332  SER A C   1 
ATOM   2690 O  O   . SER A 1 332 ? -18.418 -20.372 0.416   1.00 30.30  ? 332  SER A O   1 
ATOM   2691 C  CB  . SER A 1 332 ? -16.979 -23.128 1.244   1.00 29.74  ? 332  SER A CB  1 
ATOM   2692 O  OG  . SER A 1 332 ? -17.334 -24.079 0.273   1.00 33.33  ? 332  SER A OG  1 
ATOM   2693 N  N   . LEU A 1 333 ? -17.764 -21.491 -1.433  1.00 29.29  ? 333  LEU A N   1 
ATOM   2694 C  CA  . LEU A 1 333 ? -18.778 -20.934 -2.319  1.00 30.25  ? 333  LEU A CA  1 
ATOM   2695 C  C   . LEU A 1 333 ? -19.404 -22.053 -3.144  1.00 31.73  ? 333  LEU A C   1 
ATOM   2696 O  O   . LEU A 1 333 ? -18.810 -23.119 -3.330  1.00 33.28  ? 333  LEU A O   1 
ATOM   2697 C  CB  . LEU A 1 333 ? -18.168 -19.893 -3.268  1.00 27.51  ? 333  LEU A CB  1 
ATOM   2698 C  CG  . LEU A 1 333 ? -17.439 -18.749 -2.565  1.00 30.40  ? 333  LEU A CG  1 
ATOM   2699 C  CD1 . LEU A 1 333 ? -16.444 -18.072 -3.504  1.00 34.47  ? 333  LEU A CD1 1 
ATOM   2700 C  CD2 . LEU A 1 333 ? -18.436 -17.738 -1.972  1.00 31.83  ? 333  LEU A CD2 1 
ATOM   2701 N  N   . TYR A 1 334 ? -20.607 -21.807 -3.653  1.00 29.44  ? 334  TYR A N   1 
ATOM   2702 C  CA  . TYR A 1 334 ? -21.183 -22.710 -4.646  1.00 30.26  ? 334  TYR A CA  1 
ATOM   2703 C  C   . TYR A 1 334 ? -21.699 -21.909 -5.832  1.00 33.38  ? 334  TYR A C   1 
ATOM   2704 O  O   . TYR A 1 334 ? -22.119 -20.758 -5.698  1.00 32.79  ? 334  TYR A O   1 
ATOM   2705 C  CB  . TYR A 1 334 ? -22.310 -23.588 -4.054  1.00 31.80  ? 334  TYR A CB  1 
ATOM   2706 C  CG  . TYR A 1 334 ? -23.567 -22.810 -3.702  1.00 29.02  ? 334  TYR A CG  1 
ATOM   2707 C  CD1 . TYR A 1 334 ? -23.728 -22.238 -2.443  1.00 29.03  ? 334  TYR A CD1 1 
ATOM   2708 C  CD2 . TYR A 1 334 ? -24.581 -22.621 -4.645  1.00 31.03  ? 334  TYR A CD2 1 
ATOM   2709 C  CE1 . TYR A 1 334 ? -24.875 -21.517 -2.126  1.00 29.78  ? 334  TYR A CE1 1 
ATOM   2710 C  CE2 . TYR A 1 334 ? -25.709 -21.892 -4.344  1.00 32.98  ? 334  TYR A CE2 1 
ATOM   2711 C  CZ  . TYR A 1 334 ? -25.863 -21.353 -3.082  1.00 33.30  ? 334  TYR A CZ  1 
ATOM   2712 O  OH  . TYR A 1 334 ? -26.996 -20.618 -2.793  1.00 34.45  ? 334  TYR A OH  1 
ATOM   2713 N  N   . ALA A 1 335 ? -21.665 -22.535 -7.000  1.00 32.68  ? 335  ALA A N   1 
ATOM   2714 C  CA  . ALA A 1 335 ? -22.126 -21.870 -8.216  1.00 33.24  ? 335  ALA A CA  1 
ATOM   2715 C  C   . ALA A 1 335 ? -23.646 -21.766 -8.229  1.00 33.73  ? 335  ALA A C   1 
ATOM   2716 O  O   . ALA A 1 335 ? -24.350 -22.777 -8.128  1.00 34.68  ? 335  ALA A O   1 
ATOM   2717 C  CB  . ALA A 1 335 ? -21.628 -22.631 -9.447  1.00 34.51  ? 335  ALA A CB  1 
ATOM   2718 N  N   . LYS A 1 336 ? -24.154 -20.539 -8.376  1.00 32.09  ? 336  LYS A N   1 
ATOM   2719 C  CA  . LYS A 1 336 ? -25.596 -20.327 -8.436  1.00 35.94  ? 336  LYS A CA  1 
ATOM   2720 C  C   . LYS A 1 336 ? -26.195 -20.856 -9.733  1.00 38.56  ? 336  LYS A C   1 
ATOM   2721 O  O   . LYS A 1 336 ? -27.374 -21.229 -9.759  1.00 40.44  ? 336  LYS A O   1 
ATOM   2722 C  CB  . LYS A 1 336 ? -25.907 -18.841 -8.289  1.00 36.95  ? 336  LYS A CB  1 
ATOM   2723 C  CG  . LYS A 1 336 ? -25.710 -18.324 -6.865  1.00 35.52  ? 336  LYS A CG  1 
ATOM   2724 C  CD  . LYS A 1 336 ? -25.584 -16.794 -6.806  1.00 38.25  ? 336  LYS A CD  1 
ATOM   2725 C  CE  . LYS A 1 336 ? -26.856 -16.107 -7.286  1.00 42.07  ? 336  LYS A CE  1 
ATOM   2726 N  NZ  . LYS A 1 336 ? -28.046 -16.534 -6.489  1.00 40.46  ? 336  LYS A NZ  1 
ATOM   2727 N  N   . GLU A 1 337 ? -25.404 -20.888 -10.804 1.00 35.13  ? 337  GLU A N   1 
ATOM   2728 C  CA  . GLU A 1 337 ? -25.834 -21.366 -12.112 1.00 40.80  ? 337  GLU A CA  1 
ATOM   2729 C  C   . GLU A 1 337 ? -24.612 -21.945 -12.812 1.00 39.24  ? 337  GLU A C   1 
ATOM   2730 O  O   . GLU A 1 337 ? -23.479 -21.725 -12.383 1.00 37.33  ? 337  GLU A O   1 
ATOM   2731 C  CB  . GLU A 1 337 ? -26.426 -20.225 -12.948 1.00 41.26  ? 337  GLU A CB  1 
ATOM   2732 C  CG  . GLU A 1 337 ? -27.782 -19.741 -12.464 1.00 48.67  ? 337  GLU A CG  1 
ATOM   2733 C  CD  . GLU A 1 337 ? -28.861 -20.798 -12.540 1.00 52.57  ? 337  GLU A CD  1 
ATOM   2734 O  OE1 . GLU A 1 337 ? -28.716 -21.755 -13.329 1.00 55.05  ? 337  GLU A OE1 1 
ATOM   2735 O  OE2 . GLU A 1 337 ? -29.844 -20.682 -11.776 1.00 59.83  ? 337  GLU A OE2 1 
ATOM   2736 N  N   . ASP A 1 338 ? -24.835 -22.677 -13.908 1.00 41.14  ? 338  ASP A N   1 
ATOM   2737 C  CA  . ASP A 1 338 ? -23.711 -23.059 -14.756 1.00 38.86  ? 338  ASP A CA  1 
ATOM   2738 C  C   . ASP A 1 338 ? -22.880 -21.830 -15.094 1.00 42.20  ? 338  ASP A C   1 
ATOM   2739 O  O   . ASP A 1 338 ? -23.419 -20.759 -15.379 1.00 40.47  ? 338  ASP A O   1 
ATOM   2740 C  CB  . ASP A 1 338 ? -24.188 -23.716 -16.060 1.00 42.76  ? 338  ASP A CB  1 
ATOM   2741 C  CG  . ASP A 1 338 ? -24.909 -25.035 -15.842 1.00 45.21  ? 338  ASP A CG  1 
ATOM   2742 O  OD1 . ASP A 1 338 ? -24.901 -25.573 -14.717 1.00 43.65  ? 338  ASP A OD1 1 
ATOM   2743 O  OD2 . ASP A 1 338 ? -25.495 -25.546 -16.823 1.00 44.60  ? 338  ASP A OD2 1 
ATOM   2744 N  N   . THR A 1 339 ? -21.560 -21.984 -15.085 1.00 37.17  ? 339  THR A N   1 
ATOM   2745 C  CA  . THR A 1 339 ? -20.693 -20.856 -15.391 1.00 40.46  ? 339  THR A CA  1 
ATOM   2746 C  C   . THR A 1 339 ? -19.286 -21.388 -15.619 1.00 42.24  ? 339  THR A C   1 
ATOM   2747 O  O   . THR A 1 339 ? -18.965 -22.515 -15.234 1.00 45.75  ? 339  THR A O   1 
ATOM   2748 C  CB  . THR A 1 339 ? -20.730 -19.812 -14.260 1.00 42.96  ? 339  THR A CB  1 
ATOM   2749 O  OG1 . THR A 1 339 ? -20.217 -18.556 -14.724 1.00 42.03  ? 339  THR A OG1 1 
ATOM   2750 C  CG2 . THR A 1 339 ? -19.929 -20.301 -13.040 1.00 38.61  ? 339  THR A CG2 1 
ATOM   2751 N  N   . VAL A 1 340 ? -18.456 -20.574 -16.264 1.00 38.99  ? 340  VAL A N   1 
ATOM   2752 C  CA  . VAL A 1 340 ? -17.091 -20.955 -16.597 1.00 38.69  ? 340  VAL A CA  1 
ATOM   2753 C  C   . VAL A 1 340 ? -16.133 -20.047 -15.844 1.00 42.18  ? 340  VAL A C   1 
ATOM   2754 O  O   . VAL A 1 340 ? -16.209 -18.818 -15.958 1.00 38.93  ? 340  VAL A O   1 
ATOM   2755 C  CB  . VAL A 1 340 ? -16.830 -20.887 -18.114 1.00 40.07  ? 340  VAL A CB  1 
ATOM   2756 C  CG1 . VAL A 1 340 ? -15.360 -21.127 -18.403 1.00 40.78  ? 340  VAL A CG1 1 
ATOM   2757 C  CG2 . VAL A 1 340 ? -17.690 -21.914 -18.828 1.00 41.42  ? 340  VAL A CG2 1 
ATOM   2758 N  N   . LEU A 1 341 ? -15.224 -20.653 -15.092 1.00 39.00  ? 341  LEU A N   1 
ATOM   2759 C  CA  . LEU A 1 341 ? -14.251 -19.911 -14.307 1.00 40.77  ? 341  LEU A CA  1 
ATOM   2760 C  C   . LEU A 1 341 ? -12.996 -19.674 -15.133 1.00 40.60  ? 341  LEU A C   1 
ATOM   2761 O  O   . LEU A 1 341 ? -12.433 -20.618 -15.691 1.00 41.68  ? 341  LEU A O   1 
ATOM   2762 C  CB  . LEU A 1 341 ? -13.906 -20.689 -13.039 1.00 43.82  ? 341  LEU A CB  1 
ATOM   2763 C  CG  . LEU A 1 341 ? -13.489 -19.885 -11.825 1.00 46.69  ? 341  LEU A CG  1 
ATOM   2764 C  CD1 . LEU A 1 341 ? -14.589 -18.891 -11.461 1.00 42.28  ? 341  LEU A CD1 1 
ATOM   2765 C  CD2 . LEU A 1 341 ? -13.199 -20.855 -10.678 1.00 40.98  ? 341  LEU A CD2 1 
ATOM   2766 N  N   . GLY A 1 342 ? -12.554 -18.421 -15.192 1.00 41.30  ? 342  GLY A N   1 
ATOM   2767 C  CA  . GLY A 1 342 ? -11.310 -18.084 -15.858 1.00 39.95  ? 342  GLY A CA  1 
ATOM   2768 C  C   . GLY A 1 342 ? -11.252 -18.438 -17.326 1.00 46.47  ? 342  GLY A C   1 
ATOM   2769 O  O   . GLY A 1 342 ? -10.156 -18.599 -17.873 1.00 43.71  ? 342  GLY A O   1 
ATOM   2770 N  N   . GLY A 1 343 ? -12.401 -18.558 -17.984 1.00 41.76  ? 343  GLY A N   1 
ATOM   2771 C  CA  . GLY A 1 343 ? -12.430 -18.988 -19.369 1.00 43.27  ? 343  GLY A CA  1 
ATOM   2772 C  C   . GLY A 1 343 ? -11.940 -20.396 -19.607 1.00 49.53  ? 343  GLY A C   1 
ATOM   2773 O  O   . GLY A 1 343 ? -11.809 -20.800 -20.768 1.00 44.32  ? 343  GLY A O   1 
ATOM   2774 N  N   . GLU A 1 344 ? -11.681 -21.165 -18.546 1.00 43.17  ? 344  GLU A N   1 
ATOM   2775 C  CA  . GLU A 1 344 ? -11.010 -22.454 -18.687 1.00 47.53  ? 344  GLU A CA  1 
ATOM   2776 C  C   . GLU A 1 344 ? -11.682 -23.584 -17.915 1.00 45.18  ? 344  GLU A C   1 
ATOM   2777 O  O   . GLU A 1 344 ? -11.553 -24.751 -18.290 1.00 42.20  ? 344  GLU A O   1 
ATOM   2778 C  CB  . GLU A 1 344 ? -9.544  -22.334 -18.243 1.00 50.40  ? 344  GLU A CB  1 
ATOM   2779 C  CG  . GLU A 1 344 ? -8.715  -21.386 -19.107 1.00 52.36  ? 344  GLU A CG  1 
ATOM   2780 C  CD  . GLU A 1 344 ? -7.276  -21.217 -18.638 1.00 55.97  ? 344  GLU A CD  1 
ATOM   2781 O  OE1 . GLU A 1 344 ? -7.029  -21.181 -17.415 1.00 54.02  ? 344  GLU A OE1 1 
ATOM   2782 O  OE2 . GLU A 1 344 ? -6.382  -21.120 -19.508 1.00 62.33  ? 344  GLU A OE2 1 
ATOM   2783 N  N   . TYR A 1 345 ? -12.376 -23.270 -16.825 1.00 42.54  ? 345  TYR A N   1 
ATOM   2784 C  CA  . TYR A 1 345 ? -12.909 -24.310 -15.945 1.00 44.06  ? 345  TYR A CA  1 
ATOM   2785 C  C   . TYR A 1 345 ? -14.418 -24.222 -15.860 1.00 42.04  ? 345  TYR A C   1 
ATOM   2786 O  O   . TYR A 1 345 ? -14.955 -23.436 -15.057 1.00 40.65  ? 345  TYR A O   1 
ATOM   2787 C  CB  . TYR A 1 345 ? -12.286 -24.213 -14.554 1.00 40.97  ? 345  TYR A CB  1 
ATOM   2788 C  CG  . TYR A 1 345 ? -10.794 -24.301 -14.626 1.00 39.28  ? 345  TYR A CG  1 
ATOM   2789 C  CD1 . TYR A 1 345 ? -10.170 -25.519 -14.846 1.00 41.35  ? 345  TYR A CD1 1 
ATOM   2790 C  CD2 . TYR A 1 345 ? -10.007 -23.171 -14.503 1.00 36.54  ? 345  TYR A CD2 1 
ATOM   2791 C  CE1 . TYR A 1 345 ? -8.797  -25.611 -14.935 1.00 41.62  ? 345  TYR A CE1 1 
ATOM   2792 C  CE2 . TYR A 1 345 ? -8.630  -23.249 -14.589 1.00 41.59  ? 345  TYR A CE2 1 
ATOM   2793 C  CZ  . TYR A 1 345 ? -8.029  -24.478 -14.803 1.00 42.79  ? 345  TYR A CZ  1 
ATOM   2794 O  OH  . TYR A 1 345 ? -6.656  -24.569 -14.892 1.00 43.02  ? 345  TYR A OH  1 
ATOM   2795 N  N   . PRO A 1 346 ? -15.142 -25.013 -16.645 1.00 41.37  ? 346  PRO A N   1 
ATOM   2796 C  CA  . PRO A 1 346 ? -16.600 -24.984 -16.566 1.00 40.39  ? 346  PRO A CA  1 
ATOM   2797 C  C   . PRO A 1 346 ? -17.100 -25.626 -15.280 1.00 43.92  ? 346  PRO A C   1 
ATOM   2798 O  O   . PRO A 1 346 ? -16.595 -26.662 -14.833 1.00 39.95  ? 346  PRO A O   1 
ATOM   2799 C  CB  . PRO A 1 346 ? -17.038 -25.778 -17.802 1.00 46.25  ? 346  PRO A CB  1 
ATOM   2800 C  CG  . PRO A 1 346 ? -15.899 -26.726 -18.033 1.00 48.17  ? 346  PRO A CG  1 
ATOM   2801 C  CD  . PRO A 1 346 ? -14.659 -25.951 -17.673 1.00 45.67  ? 346  PRO A CD  1 
ATOM   2802 N  N   . LEU A 1 347 ? -18.106 -24.986 -14.693 1.00 39.48  ? 347  LEU A N   1 
ATOM   2803 C  CA  . LEU A 1 347 ? -18.768 -25.446 -13.485 1.00 40.51  ? 347  LEU A CA  1 
ATOM   2804 C  C   . LEU A 1 347 ? -20.260 -25.578 -13.746 1.00 38.02  ? 347  LEU A C   1 
ATOM   2805 O  O   . LEU A 1 347 ? -20.850 -24.794 -14.496 1.00 42.14  ? 347  LEU A O   1 
ATOM   2806 C  CB  . LEU A 1 347 ? -18.538 -24.475 -12.324 1.00 37.10  ? 347  LEU A CB  1 
ATOM   2807 C  CG  . LEU A 1 347 ? -17.075 -24.188 -11.983 1.00 37.77  ? 347  LEU A CG  1 
ATOM   2808 C  CD1 . LEU A 1 347 ? -16.953 -23.021 -10.995 1.00 40.95  ? 347  LEU A CD1 1 
ATOM   2809 C  CD2 . LEU A 1 347 ? -16.420 -25.444 -11.440 1.00 36.90  ? 347  LEU A CD2 1 
ATOM   2810 N  N   . GLU A 1 348 ? -20.863 -26.575 -13.117 1.00 36.96  ? 348  GLU A N   1 
ATOM   2811 C  CA  . GLU A 1 348 ? -22.305 -26.750 -13.128 1.00 39.58  ? 348  GLU A CA  1 
ATOM   2812 C  C   . GLU A 1 348 ? -22.917 -26.126 -11.882 1.00 39.51  ? 348  GLU A C   1 
ATOM   2813 O  O   . GLU A 1 348 ? -22.290 -26.064 -10.818 1.00 38.73  ? 348  GLU A O   1 
ATOM   2814 C  CB  . GLU A 1 348 ? -22.666 -28.234 -13.194 1.00 42.94  ? 348  GLU A CB  1 
ATOM   2815 C  CG  . GLU A 1 348 ? -22.041 -28.944 -14.376 1.00 40.97  ? 348  GLU A CG  1 
ATOM   2816 C  CD  . GLU A 1 348 ? -22.555 -30.362 -14.524 1.00 56.50  ? 348  GLU A CD  1 
ATOM   2817 O  OE1 . GLU A 1 348 ? -22.052 -31.083 -15.407 1.00 68.28  ? 348  GLU A OE1 1 
ATOM   2818 O  OE2 . GLU A 1 348 ? -23.460 -30.753 -13.759 1.00 59.78  ? 348  GLU A OE2 1 
ATOM   2819 N  N   . LYS A 1 349 ? -24.161 -25.678 -12.019 1.00 38.53  ? 349  LYS A N   1 
ATOM   2820 C  CA  . LYS A 1 349 ? -24.911 -25.183 -10.874 1.00 39.20  ? 349  LYS A CA  1 
ATOM   2821 C  C   . LYS A 1 349 ? -24.734 -26.107 -9.676  1.00 42.52  ? 349  LYS A C   1 
ATOM   2822 O  O   . LYS A 1 349 ? -24.874 -27.332 -9.787  1.00 39.61  ? 349  LYS A O   1 
ATOM   2823 C  CB  . LYS A 1 349 ? -26.390 -25.067 -11.236 1.00 37.52  ? 349  LYS A CB  1 
ATOM   2824 C  CG  . LYS A 1 349 ? -27.305 -24.639 -10.094 1.00 42.76  ? 349  LYS A CG  1 
ATOM   2825 C  CD  . LYS A 1 349 ? -28.758 -24.621 -10.578 1.00 46.59  ? 349  LYS A CD  1 
ATOM   2826 C  CE  . LYS A 1 349 ? -29.726 -24.174 -9.489  1.00 53.38  ? 349  LYS A CE  1 
ATOM   2827 N  NZ  . LYS A 1 349 ? -30.835 -23.333 -10.045 1.00 58.52  ? 349  LYS A NZ  1 
ATOM   2828 N  N   . GLY A 1 350 ? -24.411 -25.515 -8.527  1.00 36.05  ? 350  GLY A N   1 
ATOM   2829 C  CA  . GLY A 1 350 ? -24.204 -26.274 -7.317  1.00 35.31  ? 350  GLY A CA  1 
ATOM   2830 C  C   . GLY A 1 350 ? -22.770 -26.668 -7.045  1.00 38.26  ? 350  GLY A C   1 
ATOM   2831 O  O   . GLY A 1 350 ? -22.450 -27.034 -5.905  1.00 35.66  ? 350  GLY A O   1 
ATOM   2832 N  N   . ASP A 1 351 ? -21.896 -26.599 -8.048  1.00 36.71  ? 351  ASP A N   1 
ATOM   2833 C  CA  . ASP A 1 351 ? -20.501 -26.958 -7.841  1.00 37.08  ? 351  ASP A CA  1 
ATOM   2834 C  C   . ASP A 1 351 ? -19.876 -26.038 -6.801  1.00 34.65  ? 351  ASP A C   1 
ATOM   2835 O  O   . ASP A 1 351 ? -20.126 -24.829 -6.788  1.00 33.98  ? 351  ASP A O   1 
ATOM   2836 C  CB  . ASP A 1 351 ? -19.711 -26.864 -9.147  1.00 37.32  ? 351  ASP A CB  1 
ATOM   2837 C  CG  . ASP A 1 351 ? -19.900 -28.087 -10.058 1.00 39.70  ? 351  ASP A CG  1 
ATOM   2838 O  OD1 . ASP A 1 351 ? -20.624 -29.033 -9.683  1.00 36.98  ? 351  ASP A OD1 1 
ATOM   2839 O  OD2 . ASP A 1 351 ? -19.310 -28.083 -11.158 1.00 39.38  ? 351  ASP A OD2 1 
ATOM   2840 N  N   . GLU A 1 352 ? -19.020 -26.620 -5.959  1.00 35.13  ? 352  GLU A N   1 
ATOM   2841 C  CA  . GLU A 1 352 ? -18.419 -25.949 -4.813  1.00 35.00  ? 352  GLU A CA  1 
ATOM   2842 C  C   . GLU A 1 352 ? -16.987 -25.503 -5.087  1.00 37.94  ? 352  GLU A C   1 
ATOM   2843 O  O   . GLU A 1 352 ? -16.249 -26.133 -5.852  1.00 35.28  ? 352  GLU A O   1 
ATOM   2844 C  CB  . GLU A 1 352 ? -18.422 -26.887 -3.606  1.00 35.94  ? 352  GLU A CB  1 
ATOM   2845 C  CG  . GLU A 1 352 ? -19.782 -27.141 -3.019  1.00 43.20  ? 352  GLU A CG  1 
ATOM   2846 C  CD  . GLU A 1 352 ? -19.723 -28.161 -1.903  1.00 47.63  ? 352  GLU A CD  1 
ATOM   2847 O  OE1 . GLU A 1 352 ? -18.700 -28.171 -1.174  1.00 41.75  ? 352  GLU A OE1 1 
ATOM   2848 O  OE2 . GLU A 1 352 ? -20.706 -28.916 -1.744  1.00 51.19  ? 352  GLU A OE2 1 
ATOM   2849 N  N   . LEU A 1 353 ? -16.589 -24.428 -4.403  1.00 31.32  ? 353  LEU A N   1 
ATOM   2850 C  CA  . LEU A 1 353 ? -15.241 -23.885 -4.441  1.00 31.52  ? 353  LEU A CA  1 
ATOM   2851 C  C   . LEU A 1 353 ? -14.750 -23.660 -3.021  1.00 34.59  ? 353  LEU A C   1 
ATOM   2852 O  O   . LEU A 1 353 ? -15.537 -23.367 -2.123  1.00 33.82  ? 353  LEU A O   1 
ATOM   2853 C  CB  . LEU A 1 353 ? -15.169 -22.548 -5.181  1.00 31.71  ? 353  LEU A CB  1 
ATOM   2854 C  CG  . LEU A 1 353 ? -15.713 -22.512 -6.602  1.00 37.16  ? 353  LEU A CG  1 
ATOM   2855 C  CD1 . LEU A 1 353 ? -15.865 -21.078 -7.064  1.00 32.45  ? 353  LEU A CD1 1 
ATOM   2856 C  CD2 . LEU A 1 353 ? -14.720 -23.258 -7.479  1.00 36.17  ? 353  LEU A CD2 1 
ATOM   2857 N  N   . MET A 1 354 ? -13.439 -23.717 -2.834  1.00 32.02  ? 354  MET A N   1 
ATOM   2858 C  CA  . MET A 1 354 ? -12.852 -23.430 -1.541  1.00 31.72  ? 354  MET A CA  1 
ATOM   2859 C  C   . MET A 1 354 ? -11.863 -22.303 -1.830  1.00 31.57  ? 354  MET A C   1 
ATOM   2860 O  O   . MET A 1 354 ? -11.004 -22.456 -2.703  1.00 35.10  ? 354  MET A O   1 
ATOM   2861 C  CB  . MET A 1 354 ? -12.113 -24.683 -1.064  1.00 35.00  ? 354  MET A CB  1 
ATOM   2862 C  CG  . MET A 1 354 ? -12.888 -25.615 -0.145  1.00 33.74  ? 354  MET A CG  1 
ATOM   2863 S  SD  . MET A 1 354 ? -14.143 -25.133 1.052   1.00 34.50  ? 354  MET A SD  1 
ATOM   2864 C  CE  . MET A 1 354 ? -13.144 -24.346 2.290   1.00 34.23  ? 354  MET A CE  1 
ATOM   2865 N  N   . VAL A 1 355 ? -11.972 -21.174 -1.141  1.00 30.67  ? 355  VAL A N   1 
ATOM   2866 C  CA  . VAL A 1 355 ? -11.002 -20.094 -1.314  1.00 28.25  ? 355  VAL A CA  1 
ATOM   2867 C  C   . VAL A 1 355 ? -9.910  -20.223 -0.254  1.00 29.70  ? 355  VAL A C   1 
ATOM   2868 O  O   . VAL A 1 355 ? -10.174 -20.082 0.943   1.00 30.12  ? 355  VAL A O   1 
ATOM   2869 C  CB  . VAL A 1 355 ? -11.675 -18.714 -1.237  1.00 30.88  ? 355  VAL A CB  1 
ATOM   2870 C  CG1 . VAL A 1 355 ? -10.623 -17.618 -1.335  1.00 30.18  ? 355  VAL A CG1 1 
ATOM   2871 C  CG2 . VAL A 1 355 ? -12.712 -18.565 -2.353  1.00 30.12  ? 355  VAL A CG2 1 
ATOM   2872 N  N   . LEU A 1 356 ? -8.670  -20.487 -0.690  1.00 29.44  ? 356  LEU A N   1 
ATOM   2873 C  CA  . LEU A 1 356 ? -7.565  -20.739 0.247   1.00 29.97  ? 356  LEU A CA  1 
ATOM   2874 C  C   . LEU A 1 356 ? -6.856  -19.415 0.494   1.00 28.78  ? 356  LEU A C   1 
ATOM   2875 O  O   . LEU A 1 356 ? -5.958  -19.019 -0.246  1.00 31.11  ? 356  LEU A O   1 
ATOM   2876 C  CB  . LEU A 1 356 ? -6.632  -21.812 -0.312  1.00 29.07  ? 356  LEU A CB  1 
ATOM   2877 C  CG  . LEU A 1 356 ? -5.514  -22.396 0.568   1.00 33.72  ? 356  LEU A CG  1 
ATOM   2878 C  CD1 . LEU A 1 356 ? -6.106  -23.021 1.834   1.00 33.43  ? 356  LEU A CD1 1 
ATOM   2879 C  CD2 . LEU A 1 356 ? -4.734  -23.472 -0.189  1.00 30.60  ? 356  LEU A CD2 1 
ATOM   2880 N  N   . ILE A 1 357 ? -7.262  -18.716 1.553   1.00 28.22  ? 357  ILE A N   1 
ATOM   2881 C  CA  . ILE A 1 357 ? -6.927  -17.297 1.680   1.00 30.31  ? 357  ILE A CA  1 
ATOM   2882 C  C   . ILE A 1 357 ? -5.426  -17.080 1.877   1.00 29.09  ? 357  ILE A C   1 
ATOM   2883 O  O   . ILE A 1 357 ? -4.866  -16.141 1.284   1.00 30.23  ? 357  ILE A O   1 
ATOM   2884 C  CB  . ILE A 1 357 ? -7.719  -16.618 2.813   1.00 28.76  ? 357  ILE A CB  1 
ATOM   2885 C  CG1 . ILE A 1 357 ? -9.228  -16.871 2.661   1.00 28.66  ? 357  ILE A CG1 1 
ATOM   2886 C  CG2 . ILE A 1 357 ? -7.468  -15.125 2.731   1.00 29.81  ? 357  ILE A CG2 1 
ATOM   2887 C  CD1 . ILE A 1 357 ? -10.061 -16.373 3.874   1.00 27.10  ? 357  ILE A CD1 1 
ATOM   2888 N  N   . PRO A 1 358 ? -4.721  -17.873 2.696   1.00 30.58  ? 358  PRO A N   1 
ATOM   2889 C  CA  . PRO A 1 358 ? -3.278  -17.600 2.849   1.00 31.28  ? 358  PRO A CA  1 
ATOM   2890 C  C   . PRO A 1 358 ? -2.522  -17.742 1.538   1.00 31.95  ? 358  PRO A C   1 
ATOM   2891 O  O   . PRO A 1 358 ? -1.522  -17.046 1.306   1.00 31.00  ? 358  PRO A O   1 
ATOM   2892 C  CB  . PRO A 1 358 ? -2.817  -18.631 3.893   1.00 33.57  ? 358  PRO A CB  1 
ATOM   2893 C  CG  . PRO A 1 358 ? -4.101  -19.087 4.593   1.00 31.91  ? 358  PRO A CG  1 
ATOM   2894 C  CD  . PRO A 1 358 ? -5.149  -19.036 3.503   1.00 30.55  ? 358  PRO A CD  1 
ATOM   2895 N  N   . GLN A 1 359 ? -2.991  -18.611 0.659   1.00 32.25  ? 359  GLN A N   1 
ATOM   2896 C  CA  . GLN A 1 359 ? -2.337  -18.772 -0.633  1.00 32.94  ? 359  GLN A CA  1 
ATOM   2897 C  C   . GLN A 1 359 ? -2.709  -17.640 -1.597  1.00 34.36  ? 359  GLN A C   1 
ATOM   2898 O  O   . GLN A 1 359 ? -1.850  -17.125 -2.326  1.00 34.22  ? 359  GLN A O   1 
ATOM   2899 C  CB  . GLN A 1 359 ? -2.698  -20.143 -1.200  1.00 35.81  ? 359  GLN A CB  1 
ATOM   2900 C  CG  . GLN A 1 359 ? -1.708  -20.659 -2.218  1.00 37.62  ? 359  GLN A CG  1 
ATOM   2901 C  CD  . GLN A 1 359 ? -0.349  -21.011 -1.628  1.00 36.60  ? 359  GLN A CD  1 
ATOM   2902 O  OE1 . GLN A 1 359 ? -0.172  -21.136 -0.401  1.00 37.90  ? 359  GLN A OE1 1 
ATOM   2903 N  NE2 . GLN A 1 359 ? 0.636   -21.159 -2.516  1.00 39.97  ? 359  GLN A NE2 1 
ATOM   2904 N  N   . LEU A 1 360 ? -3.971  -17.209 -1.599  1.00 31.81  ? 360  LEU A N   1 
ATOM   2905 C  CA  . LEU A 1 360 ? -4.332  -16.018 -2.365  1.00 28.71  ? 360  LEU A CA  1 
ATOM   2906 C  C   . LEU A 1 360 ? -3.448  -14.833 -2.006  1.00 30.80  ? 360  LEU A C   1 
ATOM   2907 O  O   . LEU A 1 360 ? -2.991  -14.089 -2.883  1.00 31.87  ? 360  LEU A O   1 
ATOM   2908 C  CB  . LEU A 1 360 ? -5.806  -15.665 -2.108  1.00 28.35  ? 360  LEU A CB  1 
ATOM   2909 C  CG  . LEU A 1 360 ? -6.234  -14.235 -2.507  1.00 29.37  ? 360  LEU A CG  1 
ATOM   2910 C  CD1 . LEU A 1 360 ? -6.302  -14.064 -4.033  1.00 29.74  ? 360  LEU A CD1 1 
ATOM   2911 C  CD2 . LEU A 1 360 ? -7.584  -13.890 -1.889  1.00 32.70  ? 360  LEU A CD2 1 
ATOM   2912 N  N   . HIS A 1 361 ? -3.215  -14.630 -0.718  1.00 29.18  ? 361  HIS A N   1 
ATOM   2913 C  CA  . HIS A 1 361 ? -2.446  -13.499 -0.238  1.00 29.33  ? 361  HIS A CA  1 
ATOM   2914 C  C   . HIS A 1 361 ? -0.960  -13.630 -0.527  1.00 28.84  ? 361  HIS A C   1 
ATOM   2915 O  O   . HIS A 1 361 ? -0.196  -12.745 -0.141  1.00 31.72  ? 361  HIS A O   1 
ATOM   2916 C  CB  . HIS A 1 361 ? -2.691  -13.343 1.262   1.00 31.78  ? 361  HIS A CB  1 
ATOM   2917 C  CG  . HIS A 1 361 ? -4.085  -12.892 1.589   1.00 28.80  ? 361  HIS A CG  1 
ATOM   2918 N  ND1 . HIS A 1 361 ? -4.564  -12.839 2.878   1.00 30.62  ? 361  HIS A ND1 1 
ATOM   2919 C  CD2 . HIS A 1 361 ? -5.088  -12.448 0.794   1.00 29.88  ? 361  HIS A CD2 1 
ATOM   2920 C  CE1 . HIS A 1 361 ? -5.807  -12.384 2.868   1.00 30.14  ? 361  HIS A CE1 1 
ATOM   2921 N  NE2 . HIS A 1 361 ? -6.148  -12.137 1.616   1.00 28.70  ? 361  HIS A NE2 1 
ATOM   2922 N  N   . ARG A 1 362 ? -0.552  -14.732 -1.143  1.00 30.87  ? 362  ARG A N   1 
ATOM   2923 C  CA  . ARG A 1 362 ? 0.828   -14.934 -1.572  1.00 31.31  ? 362  ARG A CA  1 
ATOM   2924 C  C   . ARG A 1 362 ? 0.954   -14.938 -3.090  1.00 36.52  ? 362  ARG A C   1 
ATOM   2925 O  O   . ARG A 1 362 ? 1.993   -15.344 -3.621  1.00 34.94  ? 362  ARG A O   1 
ATOM   2926 C  CB  . ARG A 1 362 ? 1.385   -16.230 -0.975  1.00 32.06  ? 362  ARG A CB  1 
ATOM   2927 C  CG  . ARG A 1 362 ? 1.768   -16.112 0.507   1.00 31.32  ? 362  ARG A CG  1 
ATOM   2928 C  CD  . ARG A 1 362 ? 1.899   -17.498 1.176   1.00 34.06  ? 362  ARG A CD  1 
ATOM   2929 N  NE  . ARG A 1 362 ? 2.409   -17.394 2.543   1.00 32.25  ? 362  ARG A NE  1 
ATOM   2930 C  CZ  . ARG A 1 362 ? 1.696   -16.956 3.575   1.00 36.09  ? 362  ARG A CZ  1 
ATOM   2931 N  NH1 . ARG A 1 362 ? 0.418   -16.630 3.443   1.00 32.97  ? 362  ARG A NH1 1 
ATOM   2932 N  NH2 . ARG A 1 362 ? 2.287   -16.814 4.759   1.00 33.70  ? 362  ARG A NH2 1 
ATOM   2933 N  N   . ASP A 1 363 ? -0.075  -14.485 -3.797  1.00 31.91  ? 363  ASP A N   1 
ATOM   2934 C  CA  . ASP A 1 363 ? -0.042  -14.376 -5.252  1.00 35.44  ? 363  ASP A CA  1 
ATOM   2935 C  C   . ASP A 1 363 ? 1.013   -13.371 -5.708  1.00 33.61  ? 363  ASP A C   1 
ATOM   2936 O  O   . ASP A 1 363 ? 0.838   -12.148 -5.578  1.00 34.03  ? 363  ASP A O   1 
ATOM   2937 C  CB  . ASP A 1 363 ? -1.435  -13.987 -5.756  1.00 33.32  ? 363  ASP A CB  1 
ATOM   2938 C  CG  . ASP A 1 363 ? -1.568  -14.081 -7.260  1.00 36.50  ? 363  ASP A CG  1 
ATOM   2939 O  OD1 . ASP A 1 363 ? -0.534  -13.960 -7.961  1.00 34.69  ? 363  ASP A OD1 1 
ATOM   2940 O  OD2 . ASP A 1 363 ? -2.710  -14.271 -7.739  1.00 33.88  ? 363  ASP A OD2 1 
ATOM   2941 N  N   . LYS A 1 364 ? 2.127   -13.875 -6.250  1.00 38.75  ? 364  LYS A N   1 
ATOM   2942 C  CA  . LYS A 1 364 ? 3.195   -12.960 -6.638  1.00 38.94  ? 364  LYS A CA  1 
ATOM   2943 C  C   . LYS A 1 364 ? 2.794   -12.027 -7.770  1.00 35.56  ? 364  LYS A C   1 
ATOM   2944 O  O   . LYS A 1 364 ? 3.395   -10.953 -7.904  1.00 36.78  ? 364  LYS A O   1 
ATOM   2945 C  CB  . LYS A 1 364 ? 4.469   -13.712 -7.043  1.00 40.49  ? 364  LYS A CB  1 
ATOM   2946 C  CG  . LYS A 1 364 ? 5.315   -14.193 -5.876  1.00 42.76  ? 364  LYS A CG  1 
ATOM   2947 C  CD  . LYS A 1 364 ? 6.384   -15.184 -6.352  1.00 47.72  ? 364  LYS A CD  1 
ATOM   2948 C  CE  . LYS A 1 364 ? 7.081   -15.857 -5.173  1.00 53.10  ? 364  LYS A CE  1 
ATOM   2949 N  NZ  . LYS A 1 364 ? 7.812   -17.086 -5.602  1.00 57.37  ? 364  LYS A NZ  1 
ATOM   2950 N  N   . THR A 1 365 ? 1.803   -12.392 -8.581  1.00 32.84  ? 365  THR A N   1 
ATOM   2951 C  CA  . THR A 1 365 ? 1.396   -11.464 -9.631  1.00 35.51  ? 365  THR A CA  1 
ATOM   2952 C  C   . THR A 1 365 ? 0.744   -10.223 -9.056  1.00 39.27  ? 365  THR A C   1 
ATOM   2953 O  O   . THR A 1 365 ? 0.710   -9.188  -9.727  1.00 34.91  ? 365  THR A O   1 
ATOM   2954 C  CB  . THR A 1 365 ? 0.471   -12.143 -10.648 1.00 37.21  ? 365  THR A CB  1 
ATOM   2955 O  OG1 . THR A 1 365 ? -0.831  -12.360 -10.081 1.00 37.20  ? 365  THR A OG1 1 
ATOM   2956 C  CG2 . THR A 1 365 ? 1.074   -13.478 -11.121 1.00 38.56  ? 365  THR A CG2 1 
ATOM   2957 N  N   . ILE A 1 366 ? 0.271   -10.288 -7.815  1.00 30.71  ? 366  ILE A N   1 
ATOM   2958 C  CA  . ILE A 1 366 ? -0.358  -9.155  -7.153  1.00 32.21  ? 366  ILE A CA  1 
ATOM   2959 C  C   . ILE A 1 366 ? 0.639   -8.385  -6.308  1.00 34.65  ? 366  ILE A C   1 
ATOM   2960 O  O   . ILE A 1 366 ? 0.775   -7.168  -6.438  1.00 38.27  ? 366  ILE A O   1 
ATOM   2961 C  CB  . ILE A 1 366 ? -1.543  -9.634  -6.285  1.00 32.59  ? 366  ILE A CB  1 
ATOM   2962 C  CG1 . ILE A 1 366 ? -2.632  -10.258 -7.149  1.00 34.98  ? 366  ILE A CG1 1 
ATOM   2963 C  CG2 . ILE A 1 366 ? -2.040  -8.474  -5.411  1.00 33.80  ? 366  ILE A CG2 1 
ATOM   2964 C  CD1 . ILE A 1 366 ? -3.299  -9.309  -8.104  1.00 35.48  ? 366  ILE A CD1 1 
ATOM   2965 N  N   . TRP A 1 367 ? 1.345   -9.087  -5.425  1.00 33.41  ? 367  TRP A N   1 
ATOM   2966 C  CA  . TRP A 1 367 ? 2.115   -8.430  -4.383  1.00 37.63  ? 367  TRP A CA  1 
ATOM   2967 C  C   . TRP A 1 367 ? 3.573   -8.230  -4.761  1.00 37.85  ? 367  TRP A C   1 
ATOM   2968 O  O   . TRP A 1 367 ? 4.253   -7.396  -4.147  1.00 45.06  ? 367  TRP A O   1 
ATOM   2969 C  CB  . TRP A 1 367 ? 1.994   -9.232  -3.078  1.00 39.60  ? 367  TRP A CB  1 
ATOM   2970 C  CG  . TRP A 1 367 ? 0.538   -9.438  -2.692  1.00 34.26  ? 367  TRP A CG  1 
ATOM   2971 C  CD1 . TRP A 1 367 ? -0.206  -10.557 -2.887  1.00 33.12  ? 367  TRP A CD1 1 
ATOM   2972 C  CD2 . TRP A 1 367 ? -0.336  -8.471  -2.080  1.00 35.41  ? 367  TRP A CD2 1 
ATOM   2973 N  NE1 . TRP A 1 367 ? -1.500  -10.350 -2.436  1.00 32.20  ? 367  TRP A NE1 1 
ATOM   2974 C  CE2 . TRP A 1 367 ? -1.595  -9.080  -1.933  1.00 33.08  ? 367  TRP A CE2 1 
ATOM   2975 C  CE3 . TRP A 1 367 ? -0.173  -7.150  -1.651  1.00 32.06  ? 367  TRP A CE3 1 
ATOM   2976 C  CZ2 . TRP A 1 367 ? -2.689  -8.417  -1.352  1.00 31.70  ? 367  TRP A CZ2 1 
ATOM   2977 C  CZ3 . TRP A 1 367 ? -1.254  -6.495  -1.076  1.00 37.36  ? 367  TRP A CZ3 1 
ATOM   2978 C  CH2 . TRP A 1 367 ? -2.496  -7.130  -0.936  1.00 32.30  ? 367  TRP A CH2 1 
ATOM   2979 N  N   . GLY A 1 368 ? 4.058   -8.948  -5.756  1.00 38.13  ? 368  GLY A N   1 
ATOM   2980 C  CA  . GLY A 1 368 ? 5.444   -8.825  -6.155  1.00 38.68  ? 368  GLY A CA  1 
ATOM   2981 C  C   . GLY A 1 368 ? 6.295   -9.929  -5.568  1.00 49.90  ? 368  GLY A C   1 
ATOM   2982 O  O   . GLY A 1 368 ? 5.817   -10.870 -4.923  1.00 43.98  ? 368  GLY A O   1 
ATOM   2983 N  N   . ASP A 1 369 ? 7.601   -9.799  -5.808  1.00 45.88  ? 369  ASP A N   1 
ATOM   2984 C  CA  . ASP A 1 369 ? 8.524   -10.843 -5.383  1.00 55.51  ? 369  ASP A CA  1 
ATOM   2985 C  C   . ASP A 1 369 ? 8.736   -10.838 -3.870  1.00 48.53  ? 369  ASP A C   1 
ATOM   2986 O  O   . ASP A 1 369 ? 9.049   -11.883 -3.293  1.00 56.43  ? 369  ASP A O   1 
ATOM   2987 C  CB  . ASP A 1 369 ? 9.851   -10.683 -6.129  1.00 55.58  ? 369  ASP A CB  1 
ATOM   2988 C  CG  . ASP A 1 369 ? 9.752   -11.098 -7.598  1.00 65.34  ? 369  ASP A CG  1 
ATOM   2989 O  OD1 . ASP A 1 369 ? 8.870   -11.926 -7.943  1.00 56.11  ? 369  ASP A OD1 1 
ATOM   2990 O  OD2 . ASP A 1 369 ? 10.546  -10.579 -8.412  1.00 65.84  ? 369  ASP A OD2 1 
ATOM   2991 N  N   . ASP A 1 370 ? 8.564   -9.691  -3.210  1.00 50.04  ? 370  ASP A N   1 
ATOM   2992 C  CA  . ASP A 1 370 ? 8.797   -9.593  -1.771  1.00 48.14  ? 370  ASP A CA  1 
ATOM   2993 C  C   . ASP A 1 370 ? 7.594   -10.078 -0.959  1.00 46.19  ? 370  ASP A C   1 
ATOM   2994 O  O   . ASP A 1 370 ? 7.401   -9.643  0.181   1.00 44.50  ? 370  ASP A O   1 
ATOM   2995 C  CB  . ASP A 1 370 ? 9.142   -8.148  -1.384  1.00 47.16  ? 370  ASP A CB  1 
ATOM   2996 C  CG  . ASP A 1 370 ? 7.949   -7.207  -1.495  1.00 50.05  ? 370  ASP A CG  1 
ATOM   2997 O  OD1 . ASP A 1 370 ? 6.932   -7.601  -2.099  1.00 51.78  ? 370  ASP A OD1 1 
ATOM   2998 O  OD2 . ASP A 1 370 ? 8.027   -6.065  -0.992  1.00 53.35  ? 370  ASP A OD2 1 
ATOM   2999 N  N   . VAL A 1 371 ? 6.823   -11.017 -1.515  1.00 46.30  ? 371  VAL A N   1 
ATOM   3000 C  CA  . VAL A 1 371 ? 5.503   -11.350 -0.969  1.00 44.97  ? 371  VAL A CA  1 
ATOM   3001 C  C   . VAL A 1 371 ? 5.581   -11.925 0.445   1.00 43.97  ? 371  VAL A C   1 
ATOM   3002 O  O   . VAL A 1 371 ? 4.629   -11.791 1.235   1.00 39.78  ? 371  VAL A O   1 
ATOM   3003 C  CB  . VAL A 1 371 ? 4.774   -12.310 -1.930  1.00 46.15  ? 371  VAL A CB  1 
ATOM   3004 C  CG1 . VAL A 1 371 ? 5.425   -13.687 -1.926  1.00 47.30  ? 371  VAL A CG1 1 
ATOM   3005 C  CG2 . VAL A 1 371 ? 3.307   -12.403 -1.562  1.00 42.10  ? 371  VAL A CG2 1 
ATOM   3006 N  N   . GLU A 1 372 ? 6.688   -12.582 0.795   1.00 40.30  ? 372  GLU A N   1 
ATOM   3007 C  CA  . GLU A 1 372 ? 6.821   -13.130 2.139   1.00 42.20  ? 372  GLU A CA  1 
ATOM   3008 C  C   . GLU A 1 372 ? 7.302   -12.095 3.153   1.00 40.29  ? 372  GLU A C   1 
ATOM   3009 O  O   . GLU A 1 372 ? 7.257   -12.365 4.355   1.00 41.49  ? 372  GLU A O   1 
ATOM   3010 C  CB  . GLU A 1 372 ? 7.760   -14.346 2.126   1.00 44.65  ? 372  GLU A CB  1 
ATOM   3011 C  CG  . GLU A 1 372 ? 7.157   -15.569 1.440   1.00 43.15  ? 372  GLU A CG  1 
ATOM   3012 C  CD  . GLU A 1 372 ? 6.172   -16.331 2.332   1.00 47.26  ? 372  GLU A CD  1 
ATOM   3013 O  OE1 . GLU A 1 372 ? 6.272   -16.227 3.578   1.00 48.72  ? 372  GLU A OE1 1 
ATOM   3014 O  OE2 . GLU A 1 372 ? 5.282   -17.018 1.783   1.00 48.03  ? 372  GLU A OE2 1 
ATOM   3015 N  N   . GLU A 1 373 ? 7.732   -10.920 2.705   1.00 36.07  ? 373  GLU A N   1 
ATOM   3016 C  CA  . GLU A 1 373 ? 8.177   -9.859  3.599   1.00 40.27  ? 373  GLU A CA  1 
ATOM   3017 C  C   . GLU A 1 373 ? 6.992   -9.195  4.287   1.00 41.63  ? 373  GLU A C   1 
ATOM   3018 O  O   . GLU A 1 373 ? 5.901   -9.093  3.721   1.00 36.53  ? 373  GLU A O   1 
ATOM   3019 C  CB  . GLU A 1 373 ? 8.945   -8.800  2.815   1.00 43.28  ? 373  GLU A CB  1 
ATOM   3020 C  CG  . GLU A 1 373 ? 10.273  -9.279  2.290   1.00 47.68  ? 373  GLU A CG  1 
ATOM   3021 C  CD  . GLU A 1 373 ? 11.197  -8.128  1.969   1.00 58.57  ? 373  GLU A CD  1 
ATOM   3022 O  OE1 . GLU A 1 373 ? 11.048  -7.051  2.589   1.00 67.42  ? 373  GLU A OE1 1 
ATOM   3023 O  OE2 . GLU A 1 373 ? 12.044  -8.292  1.066   1.00 68.14  ? 373  GLU A OE2 1 
ATOM   3024 N  N   . PHE A 1 374 ? 7.232   -8.698  5.499   1.00 36.13  ? 374  PHE A N   1 
ATOM   3025 C  CA  . PHE A 1 374 ? 6.233   -7.959  6.267   1.00 35.84  ? 374  PHE A CA  1 
ATOM   3026 C  C   . PHE A 1 374 ? 6.428   -6.471  6.000   1.00 35.86  ? 374  PHE A C   1 
ATOM   3027 O  O   . PHE A 1 374 ? 7.292   -5.823  6.606   1.00 37.24  ? 374  PHE A O   1 
ATOM   3028 C  CB  . PHE A 1 374 ? 6.354   -8.281  7.755   1.00 33.57  ? 374  PHE A CB  1 
ATOM   3029 C  CG  . PHE A 1 374 ? 5.199   -7.788  8.572   1.00 30.45  ? 374  PHE A CG  1 
ATOM   3030 C  CD1 . PHE A 1 374 ? 3.991   -8.477  8.560   1.00 33.91  ? 374  PHE A CD1 1 
ATOM   3031 C  CD2 . PHE A 1 374 ? 5.301   -6.632  9.324   1.00 32.36  ? 374  PHE A CD2 1 
ATOM   3032 C  CE1 . PHE A 1 374 ? 2.916   -8.030  9.303   1.00 27.56  ? 374  PHE A CE1 1 
ATOM   3033 C  CE2 . PHE A 1 374 ? 4.219   -6.173  10.073  1.00 37.08  ? 374  PHE A CE2 1 
ATOM   3034 C  CZ  . PHE A 1 374 ? 3.022   -6.883  10.054  1.00 34.36  ? 374  PHE A CZ  1 
ATOM   3035 N  N   . ARG A 1 375 ? 5.612   -5.916  5.101   1.00 32.73  ? 375  ARG A N   1 
ATOM   3036 C  CA  . ARG A 1 375 ? 5.715   -4.514  4.697   1.00 34.29  ? 375  ARG A CA  1 
ATOM   3037 C  C   . ARG A 1 375 ? 4.341   -3.871  4.762   1.00 35.35  ? 375  ARG A C   1 
ATOM   3038 O  O   . ARG A 1 375 ? 3.599   -3.866  3.770   1.00 35.33  ? 375  ARG A O   1 
ATOM   3039 C  CB  . ARG A 1 375 ? 6.303   -4.390  3.290   1.00 40.29  ? 375  ARG A CB  1 
ATOM   3040 C  CG  . ARG A 1 375 ? 6.723   -2.977  2.942   1.00 47.13  ? 375  ARG A CG  1 
ATOM   3041 C  CD  . ARG A 1 375 ? 7.702   -2.948  1.769   1.00 50.87  ? 375  ARG A CD  1 
ATOM   3042 N  NE  . ARG A 1 375 ? 7.155   -3.624  0.600   1.00 49.69  ? 375  ARG A NE  1 
ATOM   3043 C  CZ  . ARG A 1 375 ? 6.290   -3.076  -0.243  1.00 54.22  ? 375  ARG A CZ  1 
ATOM   3044 N  NH1 . ARG A 1 375 ? 5.789   -1.867  -0.029  1.00 52.31  ? 375  ARG A NH1 1 
ATOM   3045 N  NH2 . ARG A 1 375 ? 5.905   -3.763  -1.319  1.00 51.92  ? 375  ARG A NH2 1 
ATOM   3046 N  N   . PRO A 1 376 ? 3.967   -3.313  5.909   1.00 33.12  ? 376  PRO A N   1 
ATOM   3047 C  CA  . PRO A 1 376 ? 2.632   -2.701  6.024   1.00 32.92  ? 376  PRO A CA  1 
ATOM   3048 C  C   . PRO A 1 376 ? 2.353   -1.661  4.962   1.00 34.37  ? 376  PRO A C   1 
ATOM   3049 O  O   . PRO A 1 376 ? 1.186   -1.444  4.594   1.00 33.97  ? 376  PRO A O   1 
ATOM   3050 C  CB  . PRO A 1 376 ? 2.667   -2.072  7.416   1.00 33.59  ? 376  PRO A CB  1 
ATOM   3051 C  CG  . PRO A 1 376 ? 3.617   -2.956  8.193   1.00 34.71  ? 376  PRO A CG  1 
ATOM   3052 C  CD  . PRO A 1 376 ? 4.705   -3.276  7.185   1.00 32.39  ? 376  PRO A CD  1 
ATOM   3053 N  N   . GLU A 1 377 ? 3.400   -1.001  4.460   1.00 35.74  ? 377  GLU A N   1 
ATOM   3054 C  CA  . GLU A 1 377 ? 3.223   0.040   3.457   1.00 38.82  ? 377  GLU A CA  1 
ATOM   3055 C  C   . GLU A 1 377 ? 2.553   -0.469  2.181   1.00 36.08  ? 377  GLU A C   1 
ATOM   3056 O  O   . GLU A 1 377 ? 2.110   0.356   1.369   1.00 37.91  ? 377  GLU A O   1 
ATOM   3057 C  CB  . GLU A 1 377 ? 4.583   0.696   3.161   1.00 40.62  ? 377  GLU A CB  1 
ATOM   3058 C  CG  . GLU A 1 377 ? 5.148   1.508   4.358   1.00 42.81  ? 377  GLU A CG  1 
ATOM   3059 C  CD  . GLU A 1 377 ? 5.902   0.671   5.411   1.00 40.84  ? 377  GLU A CD  1 
ATOM   3060 O  OE1 . GLU A 1 377 ? 6.084   -0.556  5.215   1.00 36.15  ? 377  GLU A OE1 1 
ATOM   3061 O  OE2 . GLU A 1 377 ? 6.249   1.244   6.470   1.00 39.57  ? 377  GLU A OE2 1 
ATOM   3062 N  N   . ARG A 1 378 ? 2.469   -1.790  1.980   1.00 35.32  ? 378  ARG A N   1 
ATOM   3063 C  CA  . ARG A 1 378 ? 1.672   -2.330  0.877   1.00 38.38  ? 378  ARG A CA  1 
ATOM   3064 C  C   . ARG A 1 378 ? 0.259   -1.784  0.869   1.00 36.15  ? 378  ARG A C   1 
ATOM   3065 O  O   . ARG A 1 378 ? -0.386  -1.765  -0.187  1.00 37.25  ? 378  ARG A O   1 
ATOM   3066 C  CB  . ARG A 1 378 ? 1.556   -3.858  0.960   1.00 39.77  ? 378  ARG A CB  1 
ATOM   3067 C  CG  . ARG A 1 378 ? 2.778   -4.636  0.711   1.00 44.34  ? 378  ARG A CG  1 
ATOM   3068 C  CD  . ARG A 1 378 ? 2.483   -6.073  1.059   1.00 36.28  ? 378  ARG A CD  1 
ATOM   3069 N  NE  . ARG A 1 378 ? 3.707   -6.769  1.417   1.00 38.36  ? 378  ARG A NE  1 
ATOM   3070 C  CZ  . ARG A 1 378 ? 4.577   -7.235  0.535   1.00 42.67  ? 378  ARG A CZ  1 
ATOM   3071 N  NH1 . ARG A 1 378 ? 4.415   -7.037  -0.763  1.00 38.59  ? 378  ARG A NH1 1 
ATOM   3072 N  NH2 . ARG A 1 378 ? 5.628   -7.927  0.963   1.00 44.49  ? 378  ARG A NH2 1 
ATOM   3073 N  N   . PHE A 1 379 ? -0.265  -1.399  2.032   1.00 32.69  ? 379  PHE A N   1 
ATOM   3074 C  CA  . PHE A 1 379 ? -1.663  -1.018  2.163   1.00 32.31  ? 379  PHE A CA  1 
ATOM   3075 C  C   . PHE A 1 379 ? -1.854  0.484   2.143   1.00 33.67  ? 379  PHE A C   1 
ATOM   3076 O  O   . PHE A 1 379 ? -2.941  0.969   2.460   1.00 35.77  ? 379  PHE A O   1 
ATOM   3077 C  CB  . PHE A 1 379 ? -2.262  -1.650  3.435   1.00 32.44  ? 379  PHE A CB  1 
ATOM   3078 C  CG  . PHE A 1 379 ? -2.454  -3.133  3.293   1.00 34.00  ? 379  PHE A CG  1 
ATOM   3079 C  CD1 . PHE A 1 379 ? -3.612  -3.647  2.702   1.00 32.13  ? 379  PHE A CD1 1 
ATOM   3080 C  CD2 . PHE A 1 379 ? -1.448  -4.013  3.647   1.00 34.64  ? 379  PHE A CD2 1 
ATOM   3081 C  CE1 . PHE A 1 379 ? -3.767  -5.024  2.512   1.00 34.14  ? 379  PHE A CE1 1 
ATOM   3082 C  CE2 . PHE A 1 379 ? -1.599  -5.390  3.457   1.00 32.15  ? 379  PHE A CE2 1 
ATOM   3083 C  CZ  . PHE A 1 379 ? -2.760  -5.895  2.893   1.00 33.49  ? 379  PHE A CZ  1 
ATOM   3084 N  N   . GLU A 1 380 ? -0.834  1.229   1.723   1.00 33.51  ? 380  GLU A N   1 
ATOM   3085 C  CA  . GLU A 1 380 ? -0.928  2.678   1.772   1.00 38.22  ? 380  GLU A CA  1 
ATOM   3086 C  C   . GLU A 1 380 ? -2.033  3.195   0.863   1.00 34.44  ? 380  GLU A C   1 
ATOM   3087 O  O   . GLU A 1 380 ? -2.667  4.207   1.174   1.00 36.17  ? 380  GLU A O   1 
ATOM   3088 C  CB  . GLU A 1 380 ? 0.423   3.274   1.392   1.00 40.69  ? 380  GLU A CB  1 
ATOM   3089 C  CG  . GLU A 1 380 ? 1.085   3.966   2.580   1.00 49.73  ? 380  GLU A CG  1 
ATOM   3090 C  CD  . GLU A 1 380 ? 2.555   4.196   2.347   1.00 54.91  ? 380  GLU A CD  1 
ATOM   3091 O  OE1 . GLU A 1 380 ? 3.306   4.281   3.341   1.00 53.20  ? 380  GLU A OE1 1 
ATOM   3092 O  OE2 . GLU A 1 380 ? 2.954   4.294   1.164   1.00 54.85  ? 380  GLU A OE2 1 
ATOM   3093 N  N   . ASN A 1 381 ? -2.296  2.507   -0.244  1.00 37.05  ? 381  ASN A N   1 
ATOM   3094 C  CA  . ASN A 1 381 ? -3.268  2.957   -1.238  1.00 34.58  ? 381  ASN A CA  1 
ATOM   3095 C  C   . ASN A 1 381 ? -4.165  1.811   -1.683  1.00 31.82  ? 381  ASN A C   1 
ATOM   3096 O  O   . ASN A 1 381 ? -3.800  1.065   -2.610  1.00 31.97  ? 381  ASN A O   1 
ATOM   3097 C  CB  . ASN A 1 381 ? -2.575  3.558   -2.452  1.00 37.89  ? 381  ASN A CB  1 
ATOM   3098 C  CG  . ASN A 1 381 ? -3.558  4.169   -3.420  1.00 38.72  ? 381  ASN A CG  1 
ATOM   3099 O  OD1 . ASN A 1 381 ? -4.770  4.177   -3.162  1.00 37.47  ? 381  ASN A OD1 1 
ATOM   3100 N  ND2 . ASN A 1 381 ? -3.054  4.684   -4.538  1.00 38.21  ? 381  ASN A ND2 1 
ATOM   3101 N  N   . PRO A 1 382 ? -5.353  1.662   -1.080  1.00 34.90  ? 382  PRO A N   1 
ATOM   3102 C  CA  . PRO A 1 382 ? -6.262  0.579   -1.493  1.00 34.14  ? 382  PRO A CA  1 
ATOM   3103 C  C   . PRO A 1 382 ? -6.639  0.619   -2.966  1.00 32.69  ? 382  PRO A C   1 
ATOM   3104 O  O   . PRO A 1 382 ? -6.994  -0.429  -3.520  1.00 32.58  ? 382  PRO A O   1 
ATOM   3105 C  CB  . PRO A 1 382 ? -7.487  0.784   -0.591  1.00 35.58  ? 382  PRO A CB  1 
ATOM   3106 C  CG  . PRO A 1 382 ? -6.928  1.502   0.637   1.00 40.10  ? 382  PRO A CG  1 
ATOM   3107 C  CD  . PRO A 1 382 ? -5.858  2.413   0.080   1.00 35.05  ? 382  PRO A CD  1 
ATOM   3108 N  N   . SER A 1 383 ? -6.552  1.782   -3.622  1.00 31.02  ? 383  SER A N   1 
ATOM   3109 C  CA  . SER A 1 383 ? -6.850  1.852   -5.049  1.00 30.50  ? 383  SER A CA  1 
ATOM   3110 C  C   . SER A 1 383 ? -5.763  1.199   -5.902  1.00 32.24  ? 383  SER A C   1 
ATOM   3111 O  O   . SER A 1 383 ? -5.998  0.903   -7.078  1.00 33.83  ? 383  SER A O   1 
ATOM   3112 C  CB  . SER A 1 383 ? -7.041  3.315   -5.475  1.00 33.03  ? 383  SER A CB  1 
ATOM   3113 O  OG  . SER A 1 383 ? -8.091  3.924   -4.717  1.00 32.32  ? 383  SER A OG  1 
ATOM   3114 N  N   . ALA A 1 384 ? -4.580  0.989   -5.347  1.00 33.37  ? 384  ALA A N   1 
ATOM   3115 C  CA  . ALA A 1 384 ? -3.511  0.324   -6.073  1.00 35.56  ? 384  ALA A CA  1 
ATOM   3116 C  C   . ALA A 1 384 ? -3.530  -1.188  -5.901  1.00 36.73  ? 384  ALA A C   1 
ATOM   3117 O  O   . ALA A 1 384 ? -2.675  -1.870  -6.479  1.00 35.74  ? 384  ALA A O   1 
ATOM   3118 C  CB  . ALA A 1 384 ? -2.151  0.878   -5.629  1.00 36.53  ? 384  ALA A CB  1 
ATOM   3119 N  N   . ILE A 1 385 ? -4.459  -1.726  -5.120  1.00 31.42  ? 385  ILE A N   1 
ATOM   3120 C  CA  . ILE A 1 385 ? -4.596  -3.168  -4.924  1.00 33.64  ? 385  ILE A CA  1 
ATOM   3121 C  C   . ILE A 1 385 ? -5.699  -3.665  -5.851  1.00 32.68  ? 385  ILE A C   1 
ATOM   3122 O  O   . ILE A 1 385 ? -6.835  -3.174  -5.752  1.00 32.15  ? 385  ILE A O   1 
ATOM   3123 C  CB  . ILE A 1 385 ? -4.918  -3.507  -3.462  1.00 33.23  ? 385  ILE A CB  1 
ATOM   3124 C  CG1 . ILE A 1 385 ? -3.814  -2.953  -2.538  1.00 39.06  ? 385  ILE A CG1 1 
ATOM   3125 C  CG2 . ILE A 1 385 ? -5.106  -5.027  -3.292  1.00 30.62  ? 385  ILE A CG2 1 
ATOM   3126 C  CD1 . ILE A 1 385 ? -4.103  -3.133  -1.063  1.00 37.85  ? 385  ILE A CD1 1 
ATOM   3127 N  N   . PRO A 1 386 ? -5.430  -4.627  -6.736  1.00 32.37  ? 386  PRO A N   1 
ATOM   3128 C  CA  . PRO A 1 386 ? -6.491  -5.165  -7.599  1.00 29.81  ? 386  PRO A CA  1 
ATOM   3129 C  C   . PRO A 1 386 ? -7.663  -5.729  -6.806  1.00 30.44  ? 386  PRO A C   1 
ATOM   3130 O  O   . PRO A 1 386 ? -7.550  -6.103  -5.635  1.00 30.49  ? 386  PRO A O   1 
ATOM   3131 C  CB  . PRO A 1 386 ? -5.782  -6.269  -8.395  1.00 32.99  ? 386  PRO A CB  1 
ATOM   3132 C  CG  . PRO A 1 386 ? -4.340  -5.842  -8.389  1.00 33.91  ? 386  PRO A CG  1 
ATOM   3133 C  CD  . PRO A 1 386 ? -4.119  -5.225  -7.040  1.00 33.50  ? 386  PRO A CD  1 
ATOM   3134 N  N   . GLN A 1 387 ? -8.813  -5.806  -7.480  1.00 32.09  ? 387  GLN A N   1 
ATOM   3135 C  CA  . GLN A 1 387 ? -10.019 -6.288  -6.825  1.00 31.07  ? 387  GLN A CA  1 
ATOM   3136 C  C   . GLN A 1 387 ? -9.830  -7.705  -6.306  1.00 29.95  ? 387  GLN A C   1 
ATOM   3137 O  O   . GLN A 1 387 ? -9.259  -8.565  -6.985  1.00 29.79  ? 387  GLN A O   1 
ATOM   3138 C  CB  . GLN A 1 387 ? -11.205 -6.269  -7.794  1.00 30.59  ? 387  GLN A CB  1 
ATOM   3139 C  CG  . GLN A 1 387 ? -11.687 -4.887  -8.162  1.00 33.24  ? 387  GLN A CG  1 
ATOM   3140 C  CD  . GLN A 1 387 ? -13.099 -4.915  -8.679  1.00 30.21  ? 387  GLN A CD  1 
ATOM   3141 O  OE1 . GLN A 1 387 ? -14.055 -4.904  -7.898  1.00 31.39  ? 387  GLN A OE1 1 
ATOM   3142 N  NE2 . GLN A 1 387 ? -13.241 -4.974  -10.000 1.00 32.55  ? 387  GLN A NE2 1 
ATOM   3143 N  N   . HIS A 1 388 ? -10.355 -7.945  -5.105  1.00 29.28  ? 388  HIS A N   1 
ATOM   3144 C  CA  . HIS A 1 388 ? -10.452 -9.266  -4.482  1.00 29.61  ? 388  HIS A CA  1 
ATOM   3145 C  C   . HIS A 1 388 ? -9.094  -9.918  -4.270  1.00 30.72  ? 388  HIS A C   1 
ATOM   3146 O  O   . HIS A 1 388 ? -8.996  -11.135 -4.099  1.00 30.82  ? 388  HIS A O   1 
ATOM   3147 C  CB  . HIS A 1 388 ? -11.389 -10.168 -5.280  1.00 32.73  ? 388  HIS A CB  1 
ATOM   3148 C  CG  . HIS A 1 388 ? -12.738 -9.547  -5.454  1.00 28.68  ? 388  HIS A CG  1 
ATOM   3149 N  ND1 . HIS A 1 388 ? -13.537 -9.226  -4.376  1.00 30.18  ? 388  HIS A ND1 1 
ATOM   3150 C  CD2 . HIS A 1 388 ? -13.398 -9.124  -6.558  1.00 31.84  ? 388  HIS A CD2 1 
ATOM   3151 C  CE1 . HIS A 1 388 ? -14.648 -8.656  -4.814  1.00 33.90  ? 388  HIS A CE1 1 
ATOM   3152 N  NE2 . HIS A 1 388 ? -14.592 -8.589  -6.134  1.00 30.92  ? 388  HIS A NE2 1 
ATOM   3153 N  N   . ALA A 1 389 ? -8.042  -9.114  -4.237  1.00 29.73  ? 389  ALA A N   1 
ATOM   3154 C  CA  . ALA A 1 389 ? -6.726  -9.646  -3.897  1.00 27.93  ? 389  ALA A CA  1 
ATOM   3155 C  C   . ALA A 1 389 ? -6.579  -9.952  -2.409  1.00 29.70  ? 389  ALA A C   1 
ATOM   3156 O  O   . ALA A 1 389 ? -5.692  -10.733 -2.031  1.00 30.99  ? 389  ALA A O   1 
ATOM   3157 C  CB  . ALA A 1 389 ? -5.654  -8.641  -4.298  1.00 28.84  ? 389  ALA A CB  1 
ATOM   3158 N  N   . PHE A 1 390 ? -7.405  -9.341  -1.564  1.00 28.45  ? 390  PHE A N   1 
ATOM   3159 C  CA  . PHE A 1 390 ? -7.201  -9.324  -0.113  1.00 26.69  ? 390  PHE A CA  1 
ATOM   3160 C  C   . PHE A 1 390 ? -8.546  -9.606  0.545   1.00 30.29  ? 390  PHE A C   1 
ATOM   3161 O  O   . PHE A 1 390 ? -9.423  -8.736  0.551   1.00 30.45  ? 390  PHE A O   1 
ATOM   3162 C  CB  . PHE A 1 390 ? -6.631  -7.966  0.307   1.00 29.19  ? 390  PHE A CB  1 
ATOM   3163 C  CG  . PHE A 1 390 ? -6.387  -7.806  1.790   1.00 32.58  ? 390  PHE A CG  1 
ATOM   3164 C  CD1 . PHE A 1 390 ? -5.445  -8.580  2.454   1.00 28.93  ? 390  PHE A CD1 1 
ATOM   3165 C  CD2 . PHE A 1 390 ? -7.083  -6.840  2.505   1.00 30.82  ? 390  PHE A CD2 1 
ATOM   3166 C  CE1 . PHE A 1 390 ? -5.219  -8.399  3.825   1.00 29.00  ? 390  PHE A CE1 1 
ATOM   3167 C  CE2 . PHE A 1 390 ? -6.874  -6.659  3.867   1.00 30.68  ? 390  PHE A CE2 1 
ATOM   3168 C  CZ  . PHE A 1 390 ? -5.924  -7.421  4.528   1.00 29.33  ? 390  PHE A CZ  1 
ATOM   3169 N  N   . LYS A 1 391 ? -8.723  -10.833 1.084   1.00 28.23  ? 391  LYS A N   1 
ATOM   3170 C  CA  . LYS A 1 391 ? -10.050 -11.299 1.497   1.00 28.51  ? 391  LYS A CA  1 
ATOM   3171 C  C   . LYS A 1 391 ? -10.058 -11.902 2.900   1.00 26.10  ? 391  LYS A C   1 
ATOM   3172 O  O   . LYS A 1 391 ? -10.687 -12.945 3.120   1.00 29.52  ? 391  LYS A O   1 
ATOM   3173 C  CB  . LYS A 1 391 ? -10.582 -12.355 0.520   1.00 30.71  ? 391  LYS A CB  1 
ATOM   3174 C  CG  . LYS A 1 391 ? -10.578 -11.994 -0.972  1.00 30.85  ? 391  LYS A CG  1 
ATOM   3175 C  CD  . LYS A 1 391 ? -11.464 -10.781 -1.290  1.00 30.68  ? 391  LYS A CD  1 
ATOM   3176 C  CE  . LYS A 1 391 ? -12.925 -11.049 -0.954  1.00 31.71  ? 391  LYS A CE  1 
ATOM   3177 N  NZ  . LYS A 1 391 ? -13.794 -10.006 -1.593  1.00 33.49  ? 391  LYS A NZ  1 
ATOM   3178 N  N   . PRO A 1 392 ? -9.400  -11.283 3.880   1.00 27.58  ? 392  PRO A N   1 
ATOM   3179 C  CA  . PRO A 1 392 ? -9.360  -11.889 5.219   1.00 28.25  ? 392  PRO A CA  1 
ATOM   3180 C  C   . PRO A 1 392 ? -10.689 -11.855 5.936   1.00 30.41  ? 392  PRO A C   1 
ATOM   3181 O  O   . PRO A 1 392 ? -10.836 -12.562 6.942   1.00 28.75  ? 392  PRO A O   1 
ATOM   3182 C  CB  . PRO A 1 392 ? -8.323  -11.038 5.956   1.00 30.08  ? 392  PRO A CB  1 
ATOM   3183 C  CG  . PRO A 1 392 ? -8.492  -9.692  5.336   1.00 29.90  ? 392  PRO A CG  1 
ATOM   3184 C  CD  . PRO A 1 392 ? -8.690  -9.991  3.852   1.00 28.32  ? 392  PRO A CD  1 
ATOM   3185 N  N   A HIS A 1 393 ? -11.656 -11.068 5.476   0.52 29.07  ? 393  HIS A N   1 
ATOM   3186 N  N   B HIS A 1 393 ? -11.643 -11.048 5.457   0.48 29.05  ? 393  HIS A N   1 
ATOM   3187 C  CA  A HIS A 1 393 ? -12.969 -11.047 6.110   0.52 28.70  ? 393  HIS A CA  1 
ATOM   3188 C  CA  B HIS A 1 393 ? -12.973 -10.921 6.043   0.48 28.69  ? 393  HIS A CA  1 
ATOM   3189 C  C   A HIS A 1 393 ? -14.049 -11.546 5.156   0.52 28.96  ? 393  HIS A C   1 
ATOM   3190 C  C   B HIS A 1 393 ? -14.052 -11.644 5.240   0.48 28.95  ? 393  HIS A C   1 
ATOM   3191 O  O   A HIS A 1 393 ? -15.218 -11.161 5.261   0.52 28.74  ? 393  HIS A O   1 
ATOM   3192 O  O   B HIS A 1 393 ? -15.243 -11.482 5.536   0.48 28.62  ? 393  HIS A O   1 
ATOM   3193 C  CB  A HIS A 1 393 ? -13.285 -9.651  6.649   0.52 29.94  ? 393  HIS A CB  1 
ATOM   3194 C  CB  B HIS A 1 393 ? -13.362 -9.441  6.182   0.48 29.27  ? 393  HIS A CB  1 
ATOM   3195 C  CG  A HIS A 1 393 ? -12.504 -9.302  7.881   0.52 29.30  ? 393  HIS A CG  1 
ATOM   3196 C  CG  B HIS A 1 393 ? -12.249 -8.547  6.638   0.48 31.95  ? 393  HIS A CG  1 
ATOM   3197 N  ND1 A HIS A 1 393 ? -11.408 -8.469  7.853   0.52 33.18  ? 393  HIS A ND1 1 
ATOM   3198 N  ND1 B HIS A 1 393 ? -11.762 -8.563  7.927   0.48 32.63  ? 393  HIS A ND1 1 
ATOM   3199 C  CD2 A HIS A 1 393 ? -12.637 -9.704  9.170   0.52 31.16  ? 393  HIS A CD2 1 
ATOM   3200 C  CD2 B HIS A 1 393 ? -11.549 -7.589  5.984   0.48 34.46  ? 393  HIS A CD2 1 
ATOM   3201 C  CE1 A HIS A 1 393 ? -10.911 -8.355  9.073   0.52 31.00  ? 393  HIS A CE1 1 
ATOM   3202 C  CE1 B HIS A 1 393 ? -10.801 -7.663  8.043   0.48 30.72  ? 393  HIS A CE1 1 
ATOM   3203 N  NE2 A HIS A 1 393 ? -11.631 -9.103  9.889   0.52 34.64  ? 393  HIS A NE2 1 
ATOM   3204 N  NE2 B HIS A 1 393 ? -10.651 -7.059  6.878   0.48 32.46  ? 393  HIS A NE2 1 
ATOM   3205 N  N   . GLY A 1 394 ? -13.676 -12.425 4.228   1.00 28.34  ? 394  GLY A N   1 
ATOM   3206 C  CA  . GLY A 1 394 ? -14.674 -13.046 3.385   1.00 27.66  ? 394  GLY A CA  1 
ATOM   3207 C  C   . GLY A 1 394 ? -15.145 -12.102 2.291   1.00 28.73  ? 394  GLY A C   1 
ATOM   3208 O  O   . GLY A 1 394 ? -14.431 -11.174 1.890   1.00 30.40  ? 394  GLY A O   1 
ATOM   3209 N  N   . ASN A 1 395 ? -16.369 -12.347 1.790   1.00 26.99  ? 395  ASN A N   1 
ATOM   3210 C  CA  . ASN A 1 395 ? -16.819 -11.667 0.580   1.00 28.33  ? 395  ASN A CA  1 
ATOM   3211 C  C   . ASN A 1 395 ? -18.282 -11.242 0.619   1.00 30.64  ? 395  ASN A C   1 
ATOM   3212 O  O   . ASN A 1 395 ? -19.143 -11.997 1.064   1.00 29.62  ? 395  ASN A O   1 
ATOM   3213 C  CB  . ASN A 1 395 ? -16.656 -12.553 -0.657  1.00 26.11  ? 395  ASN A CB  1 
ATOM   3214 C  CG  . ASN A 1 395 ? -16.969 -11.795 -1.936  1.00 29.58  ? 395  ASN A CG  1 
ATOM   3215 O  OD1 . ASN A 1 395 ? -16.305 -10.809 -2.247  1.00 30.80  ? 395  ASN A OD1 1 
ATOM   3216 N  ND2 . ASN A 1 395 ? -17.987 -12.237 -2.673  1.00 30.35  ? 395  ASN A ND2 1 
ATOM   3217 N  N   . GLY A 1 396 ? -18.555 -10.043 0.089   1.00 30.52  ? 396  GLY A N   1 
ATOM   3218 C  CA  . GLY A 1 396 ? -19.918 -9.655  -0.237  1.00 31.92  ? 396  GLY A CA  1 
ATOM   3219 C  C   . GLY A 1 396 ? -20.809 -9.520  0.987   1.00 28.95  ? 396  GLY A C   1 
ATOM   3220 O  O   . GLY A 1 396 ? -20.357 -9.184  2.076   1.00 29.62  ? 396  GLY A O   1 
ATOM   3221 N  N   . GLN A 1 397 ? -22.106 -9.788  0.787   1.00 27.78  ? 397  GLN A N   1 
ATOM   3222 C  CA  . GLN A 1 397 ? -23.058 -9.694  1.887   1.00 30.57  ? 397  GLN A CA  1 
ATOM   3223 C  C   . GLN A 1 397 ? -22.783 -10.727 2.968   1.00 31.65  ? 397  GLN A C   1 
ATOM   3224 O  O   . GLN A 1 397 ? -23.246 -10.566 4.104   1.00 30.57  ? 397  GLN A O   1 
ATOM   3225 C  CB  . GLN A 1 397 ? -24.494 -9.843  1.365   1.00 28.99  ? 397  GLN A CB  1 
ATOM   3226 C  CG  . GLN A 1 397 ? -24.857 -11.223 0.835   1.00 32.78  ? 397  GLN A CG  1 
ATOM   3227 C  CD  . GLN A 1 397 ? -26.263 -11.266 0.255   1.00 34.84  ? 397  GLN A CD  1 
ATOM   3228 O  OE1 . GLN A 1 397 ? -27.097 -10.417 0.572   1.00 35.21  ? 397  GLN A OE1 1 
ATOM   3229 N  NE2 . GLN A 1 397 ? -26.522 -12.239 -0.621  1.00 34.99  ? 397  GLN A NE2 1 
ATOM   3230 N  N   . ARG A 1 398 ? -22.035 -11.780 2.650   1.00 29.75  ? 398  ARG A N   1 
ATOM   3231 C  CA  . ARG A 1 398 ? -21.645 -12.761 3.653   1.00 27.97  ? 398  ARG A CA  1 
ATOM   3232 C  C   . ARG A 1 398 ? -20.252 -12.476 4.217   1.00 29.03  ? 398  ARG A C   1 
ATOM   3233 O  O   . ARG A 1 398 ? -19.644 -13.357 4.824   1.00 28.88  ? 398  ARG A O   1 
ATOM   3234 C  CB  . ARG A 1 398 ? -21.713 -14.180 3.073   1.00 30.88  ? 398  ARG A CB  1 
ATOM   3235 C  CG  . ARG A 1 398 ? -23.106 -14.612 2.595   1.00 28.59  ? 398  ARG A CG  1 
ATOM   3236 C  CD  . ARG A 1 398 ? -24.176 -14.430 3.681   1.00 28.84  ? 398  ARG A CD  1 
ATOM   3237 N  NE  . ARG A 1 398 ? -23.875 -15.147 4.918   1.00 26.82  ? 398  ARG A NE  1 
ATOM   3238 C  CZ  . ARG A 1 398 ? -24.230 -16.405 5.179   1.00 28.36  ? 398  ARG A CZ  1 
ATOM   3239 N  NH1 . ARG A 1 398 ? -24.897 -17.134 4.297   1.00 29.59  ? 398  ARG A NH1 1 
ATOM   3240 N  NH2 . ARG A 1 398 ? -23.910 -16.940 6.358   1.00 28.81  ? 398  ARG A NH2 1 
ATOM   3241 N  N   . ALA A 1 399 ? -19.727 -11.271 4.004   1.00 27.82  ? 399  ALA A N   1 
ATOM   3242 C  CA  . ALA A 1 399 ? -18.484 -10.903 4.655   1.00 29.14  ? 399  ALA A CA  1 
ATOM   3243 C  C   . ALA A 1 399 ? -18.684 -10.792 6.165   1.00 29.54  ? 399  ALA A C   1 
ATOM   3244 O  O   . ALA A 1 399 ? -19.804 -10.746 6.680   1.00 30.79  ? 399  ALA A O   1 
ATOM   3245 C  CB  . ALA A 1 399 ? -17.943 -9.585  4.093   1.00 30.28  ? 399  ALA A CB  1 
ATOM   3246 N  N   . CYS A 1 400 ? -17.560 -10.694 6.869   1.00 28.03  ? 400  CYS A N   1 
ATOM   3247 C  CA  . CYS A 1 400 ? -17.547 -10.676 8.325   1.00 28.52  ? 400  CYS A CA  1 
ATOM   3248 C  C   . CYS A 1 400 ? -18.306 -9.474  8.873   1.00 32.37  ? 400  CYS A C   1 
ATOM   3249 O  O   . CYS A 1 400 ? -17.920 -8.329  8.638   1.00 32.12  ? 400  CYS A O   1 
ATOM   3250 C  CB  . CYS A 1 400 ? -16.100 -10.643 8.804   1.00 28.22  ? 400  CYS A CB  1 
ATOM   3251 S  SG  . CYS A 1 400 ? -15.967 -10.551 10.602  1.00 30.08  ? 400  CYS A SG  1 
ATOM   3252 N  N   . ILE A 1 401 ? -19.379 -9.719  9.632   1.00 30.52  ? 401  ILE A N   1 
ATOM   3253 C  CA  . ILE A 1 401 ? -20.101 -8.594  10.211  1.00 29.01  ? 401  ILE A CA  1 
ATOM   3254 C  C   . ILE A 1 401 ? -19.291 -7.909  11.311  1.00 31.07  ? 401  ILE A C   1 
ATOM   3255 O  O   . ILE A 1 401 ? -19.543 -6.739  11.628  1.00 31.26  ? 401  ILE A O   1 
ATOM   3256 C  CB  . ILE A 1 401 ? -21.460 -9.068  10.746  1.00 27.63  ? 401  ILE A CB  1 
ATOM   3257 C  CG1 . ILE A 1 401 ? -22.386 -7.872  10.973  1.00 32.11  ? 401  ILE A CG1 1 
ATOM   3258 C  CG2 . ILE A 1 401 ? -21.287 -9.845  12.020  1.00 30.26  ? 401  ILE A CG2 1 
ATOM   3259 C  CD1 . ILE A 1 401 ? -23.773 -8.275  11.430  1.00 34.12  ? 401  ILE A CD1 1 
ATOM   3260 N  N   . GLY A 1 402 ? -18.302 -8.594  11.882  1.00 26.51  ? 402  GLY A N   1 
ATOM   3261 C  CA  . GLY A 1 402 ? -17.519 -8.076  12.994  1.00 30.68  ? 402  GLY A CA  1 
ATOM   3262 C  C   . GLY A 1 402 ? -16.226 -7.392  12.603  1.00 28.96  ? 402  GLY A C   1 
ATOM   3263 O  O   . GLY A 1 402 ? -15.432 -7.051  13.484  1.00 32.01  ? 402  GLY A O   1 
ATOM   3264 N  N   . GLN A 1 403 ? -16.013 -7.140  11.315  1.00 29.47  ? 403  GLN A N   1 
ATOM   3265 C  CA  . GLN A 1 403 ? -14.730 -6.613  10.846  1.00 30.87  ? 403  GLN A CA  1 
ATOM   3266 C  C   . GLN A 1 403 ? -14.323 -5.333  11.577  1.00 32.06  ? 403  GLN A C   1 
ATOM   3267 O  O   . GLN A 1 403 ? -13.171 -5.197  12.012  1.00 32.63  ? 403  GLN A O   1 
ATOM   3268 C  CB  . GLN A 1 403 ? -14.787 -6.382  9.330   1.00 30.93  ? 403  GLN A CB  1 
ATOM   3269 C  CG  . GLN A 1 403 ? -13.650 -5.506  8.814   1.00 35.57  ? 403  GLN A CG  1 
ATOM   3270 C  CD  . GLN A 1 403 ? -13.780 -5.165  7.343   1.00 44.60  ? 403  GLN A CD  1 
ATOM   3271 O  OE1 . GLN A 1 403 ? -14.627 -5.712  6.636   1.00 41.01  ? 403  GLN A OE1 1 
ATOM   3272 N  NE2 . GLN A 1 403 ? -12.955 -4.233  6.881   1.00 48.25  ? 403  GLN A NE2 1 
ATOM   3273 N  N   . GLN A 1 404 ? -15.244 -4.378  11.719  1.00 33.21  ? 404  GLN A N   1 
ATOM   3274 C  CA  . GLN A 1 404 ? -14.879 -3.118  12.373  1.00 35.11  ? 404  GLN A CA  1 
ATOM   3275 C  C   . GLN A 1 404 ? -14.643 -3.310  13.863  1.00 34.94  ? 404  GLN A C   1 
ATOM   3276 O  O   . GLN A 1 404 ? -13.755 -2.671  14.443  1.00 36.30  ? 404  GLN A O   1 
ATOM   3277 C  CB  . GLN A 1 404 ? -15.958 -2.058  12.139  1.00 36.89  ? 404  GLN A CB  1 
ATOM   3278 C  CG  . GLN A 1 404 ? -16.208 -1.810  10.668  1.00 48.91  ? 404  GLN A CG  1 
ATOM   3279 C  CD  . GLN A 1 404 ? -15.128 -0.939  10.070  1.00 56.12  ? 404  GLN A CD  1 
ATOM   3280 O  OE1 . GLN A 1 404 ? -14.286 -1.416  9.305   1.00 59.44  ? 404  GLN A OE1 1 
ATOM   3281 N  NE2 . GLN A 1 404 ? -15.133 0.344   10.426  1.00 68.67  ? 404  GLN A NE2 1 
ATOM   3282 N  N   . PHE A 1 405 ? -15.444 -4.160  14.504  1.00 32.32  ? 405  PHE A N   1 
ATOM   3283 C  CA  . PHE A 1 405 ? -15.217 -4.483  15.915  1.00 30.61  ? 405  PHE A CA  1 
ATOM   3284 C  C   . PHE A 1 405 ? -13.809 -5.036  16.110  1.00 33.00  ? 405  PHE A C   1 
ATOM   3285 O  O   . PHE A 1 405 ? -13.042 -4.559  16.961  1.00 31.63  ? 405  PHE A O   1 
ATOM   3286 C  CB  . PHE A 1 405 ? -16.280 -5.489  16.376  1.00 31.36  ? 405  PHE A CB  1 
ATOM   3287 C  CG  . PHE A 1 405 ? -16.308 -5.733  17.869  1.00 31.02  ? 405  PHE A CG  1 
ATOM   3288 C  CD1 . PHE A 1 405 ? -15.436 -6.642  18.447  1.00 29.02  ? 405  PHE A CD1 1 
ATOM   3289 C  CD2 . PHE A 1 405 ? -17.225 -5.084  18.684  1.00 31.32  ? 405  PHE A CD2 1 
ATOM   3290 C  CE1 . PHE A 1 405 ? -15.448 -6.889  19.804  1.00 31.85  ? 405  PHE A CE1 1 
ATOM   3291 C  CE2 . PHE A 1 405 ? -17.245 -5.322  20.062  1.00 33.36  ? 405  PHE A CE2 1 
ATOM   3292 C  CZ  . PHE A 1 405 ? -16.347 -6.240  20.618  1.00 34.17  ? 405  PHE A CZ  1 
ATOM   3293 N  N   . ALA A 1 406 ? -13.456 -6.052  15.318  1.00 30.43  ? 406  ALA A N   1 
ATOM   3294 C  CA  . ALA A 1 406 ? -12.139 -6.681  15.418  1.00 30.83  ? 406  ALA A CA  1 
ATOM   3295 C  C   . ALA A 1 406 ? -11.017 -5.673  15.192  1.00 31.72  ? 406  ALA A C   1 
ATOM   3296 O  O   . ALA A 1 406 ? -10.022 -5.657  15.929  1.00 30.26  ? 406  ALA A O   1 
ATOM   3297 C  CB  . ALA A 1 406 ? -12.026 -7.826  14.404  1.00 29.52  ? 406  ALA A CB  1 
ATOM   3298 N  N   . LEU A 1 407 ? -11.137 -4.846  14.154  1.00 29.22  ? 407  LEU A N   1 
ATOM   3299 C  CA  . LEU A 1 407 ? -10.040 -3.937  13.840  1.00 31.56  ? 407  LEU A CA  1 
ATOM   3300 C  C   . LEU A 1 407 ? -9.953  -2.796  14.845  1.00 31.36  ? 407  LEU A C   1 
ATOM   3301 O  O   . LEU A 1 407 ? -8.849  -2.331  15.161  1.00 31.66  ? 407  LEU A O   1 
ATOM   3302 C  CB  . LEU A 1 407 ? -10.188 -3.424  12.413  1.00 31.98  ? 407  LEU A CB  1 
ATOM   3303 C  CG  . LEU A 1 407 ? -9.947  -4.527  11.374  1.00 35.17  ? 407  LEU A CG  1 
ATOM   3304 C  CD1 . LEU A 1 407 ? -10.203 -3.991  9.945   1.00 40.18  ? 407  LEU A CD1 1 
ATOM   3305 C  CD2 . LEU A 1 407 ? -8.562  -5.098  11.484  1.00 36.30  ? 407  LEU A CD2 1 
ATOM   3306 N  N   . HIS A 1 408 ? -11.079 -2.349  15.394  1.00 32.45  ? 408  HIS A N   1 
ATOM   3307 C  CA  . HIS A 1 408 ? -10.990 -1.324  16.421  1.00 32.00  ? 408  HIS A CA  1 
ATOM   3308 C  C   . HIS A 1 408 ? -10.329 -1.886  17.671  1.00 31.66  ? 408  HIS A C   1 
ATOM   3309 O  O   . HIS A 1 408 ? -9.420  -1.268  18.236  1.00 32.08  ? 408  HIS A O   1 
ATOM   3310 C  CB  . HIS A 1 408 ? -12.368 -0.760  16.755  1.00 34.19  ? 408  HIS A CB  1 
ATOM   3311 C  CG  . HIS A 1 408 ? -12.306 0.481   17.598  1.00 33.68  ? 408  HIS A CG  1 
ATOM   3312 N  ND1 . HIS A 1 408 ? -12.069 1.727   17.060  1.00 34.91  ? 408  HIS A ND1 1 
ATOM   3313 C  CD2 . HIS A 1 408 ? -12.456 0.668   18.934  1.00 35.64  ? 408  HIS A CD2 1 
ATOM   3314 C  CE1 . HIS A 1 408 ? -12.074 2.629   18.027  1.00 34.45  ? 408  HIS A CE1 1 
ATOM   3315 N  NE2 . HIS A 1 408 ? -12.293 2.012   19.175  1.00 34.95  ? 408  HIS A NE2 1 
ATOM   3316 N  N   . GLU A 1 409 ? -10.771 -3.069  18.105  1.00 28.83  ? 409  GLU A N   1 
ATOM   3317 C  CA  . GLU A 1 409 ? -10.183 -3.699  19.282  1.00 29.49  ? 409  GLU A CA  1 
ATOM   3318 C  C   . GLU A 1 409 ? -8.689  -3.909  19.088  1.00 31.24  ? 409  GLU A C   1 
ATOM   3319 O  O   . GLU A 1 409 ? -7.878  -3.571  19.960  1.00 32.17  ? 409  GLU A O   1 
ATOM   3320 C  CB  . GLU A 1 409 ? -10.874 -5.033  19.558  1.00 31.77  ? 409  GLU A CB  1 
ATOM   3321 C  CG  . GLU A 1 409 ? -10.205 -5.821  20.696  1.00 30.81  ? 409  GLU A CG  1 
ATOM   3322 C  CD  . GLU A 1 409 ? -10.918 -7.130  20.991  1.00 32.12  ? 409  GLU A CD  1 
ATOM   3323 O  OE1 . GLU A 1 409 ? -11.845 -7.503  20.233  1.00 31.60  ? 409  GLU A OE1 1 
ATOM   3324 O  OE2 . GLU A 1 409 ? -10.559 -7.773  21.987  1.00 32.48  ? 409  GLU A OE2 1 
ATOM   3325 N  N   . ALA A 1 410 ? -8.310  -4.497  17.954  1.00 29.37  ? 410  ALA A N   1 
ATOM   3326 C  CA  . ALA A 1 410 ? -6.908  -4.836  17.753  1.00 27.75  ? 410  ALA A CA  1 
ATOM   3327 C  C   . ALA A 1 410 ? -6.059  -3.583  17.606  1.00 31.35  ? 410  ALA A C   1 
ATOM   3328 O  O   . ALA A 1 410 ? -4.916  -3.542  18.083  1.00 31.77  ? 410  ALA A O   1 
ATOM   3329 C  CB  . ALA A 1 410 ? -6.766  -5.752  16.537  1.00 31.00  ? 410  ALA A CB  1 
ATOM   3330 N  N   . THR A 1 411 ? -6.590  -2.547  16.955  1.00 31.25  ? 411  THR A N   1 
ATOM   3331 C  CA  . THR A 1 411 ? -5.815  -1.317  16.826  1.00 31.09  ? 411  THR A CA  1 
ATOM   3332 C  C   . THR A 1 411 ? -5.607  -0.664  18.194  1.00 31.33  ? 411  THR A C   1 
ATOM   3333 O  O   . THR A 1 411 ? -4.487  -0.258  18.543  1.00 33.20  ? 411  THR A O   1 
ATOM   3334 C  CB  . THR A 1 411 ? -6.513  -0.361  15.856  1.00 33.45  ? 411  THR A CB  1 
ATOM   3335 O  OG1 . THR A 1 411 ? -6.686  -1.014  14.587  1.00 30.89  ? 411  THR A OG1 1 
ATOM   3336 C  CG2 . THR A 1 411 ? -5.659  0.920   15.662  1.00 32.94  ? 411  THR A CG2 1 
ATOM   3337 N  N   . LEU A 1 412 ? -6.676  -0.576  18.988  1.00 31.44  ? 412  LEU A N   1 
ATOM   3338 C  CA  . LEU A 1 412 ? -6.580  -0.030  20.342  1.00 30.56  ? 412  LEU A CA  1 
ATOM   3339 C  C   . LEU A 1 412 ? -5.533  -0.773  21.163  1.00 33.99  ? 412  LEU A C   1 
ATOM   3340 O  O   . LEU A 1 412 ? -4.659  -0.161  21.793  1.00 32.45  ? 412  LEU A O   1 
ATOM   3341 C  CB  . LEU A 1 412 ? -7.948  -0.116  21.020  1.00 31.56  ? 412  LEU A CB  1 
ATOM   3342 C  CG  . LEU A 1 412 ? -7.922  0.005   22.546  1.00 37.24  ? 412  LEU A CG  1 
ATOM   3343 C  CD1 . LEU A 1 412 ? -7.518  1.426   22.945  1.00 38.46  ? 412  LEU A CD1 1 
ATOM   3344 C  CD2 . LEU A 1 412 ? -9.268  -0.393  23.156  1.00 36.12  ? 412  LEU A CD2 1 
ATOM   3345 N  N   . VAL A 1 413 ? -5.610  -2.101  21.167  1.00 31.43  ? 413  VAL A N   1 
ATOM   3346 C  CA  . VAL A 1 413 ? -4.777  -2.910  22.056  1.00 31.90  ? 413  VAL A CA  1 
ATOM   3347 C  C   . VAL A 1 413 ? -3.323  -2.884  21.596  1.00 29.65  ? 413  VAL A C   1 
ATOM   3348 O  O   . VAL A 1 413 ? -2.398  -2.706  22.401  1.00 32.21  ? 413  VAL A O   1 
ATOM   3349 C  CB  . VAL A 1 413 ? -5.335  -4.343  22.134  1.00 33.79  ? 413  VAL A CB  1 
ATOM   3350 C  CG1 . VAL A 1 413 ? -4.391  -5.251  22.879  1.00 38.45  ? 413  VAL A CG1 1 
ATOM   3351 C  CG2 . VAL A 1 413 ? -6.710  -4.326  22.817  1.00 32.01  ? 413  VAL A CG2 1 
ATOM   3352 N  N   . LEU A 1 414 ? -3.093  -3.042  20.290  1.00 30.00  ? 414  LEU A N   1 
ATOM   3353 C  CA  . LEU A 1 414 ? -1.717  -2.995  19.816  1.00 30.80  ? 414  LEU A CA  1 
ATOM   3354 C  C   . LEU A 1 414 ? -1.130  -1.600  20.008  1.00 33.94  ? 414  LEU A C   1 
ATOM   3355 O  O   . LEU A 1 414 ? 0.055   -1.459  20.343  1.00 32.69  ? 414  LEU A O   1 
ATOM   3356 C  CB  . LEU A 1 414 ? -1.652  -3.428  18.344  1.00 32.60  ? 414  LEU A CB  1 
ATOM   3357 C  CG  . LEU A 1 414 ? -0.285  -3.651  17.691  1.00 34.38  ? 414  LEU A CG  1 
ATOM   3358 C  CD1 . LEU A 1 414 ? 0.539   -4.706  18.443  1.00 38.03  ? 414  LEU A CD1 1 
ATOM   3359 C  CD2 . LEU A 1 414 ? -0.447  -4.045  16.214  1.00 34.36  ? 414  LEU A CD2 1 
ATOM   3360 N  N   . GLY A 1 415 ? -1.943  -0.557  19.803  1.00 32.08  ? 415  GLY A N   1 
ATOM   3361 C  CA  . GLY A 1 415 ? -1.467  0.792   20.081  1.00 30.31  ? 415  GLY A CA  1 
ATOM   3362 C  C   . GLY A 1 415 ? -1.029  0.946   21.524  1.00 36.38  ? 415  GLY A C   1 
ATOM   3363 O  O   . GLY A 1 415 ? 0.038   1.493   21.813  1.00 33.45  ? 415  GLY A O   1 
ATOM   3364 N  N   . MET A 1 416 ? -1.844  0.449   22.455  1.00 30.95  ? 416  MET A N   1 
ATOM   3365 C  CA  . MET A 1 416 ? -1.447  0.519   23.856  1.00 33.46  ? 416  MET A CA  1 
ATOM   3366 C  C   . MET A 1 416 ? -0.232  -0.355  24.146  1.00 32.06  ? 416  MET A C   1 
ATOM   3367 O  O   . MET A 1 416 ? 0.642   0.063   24.914  1.00 34.51  ? 416  MET A O   1 
ATOM   3368 C  CB  . MET A 1 416 ? -2.607  0.174   24.792  1.00 34.28  ? 416  MET A CB  1 
ATOM   3369 C  CG  . MET A 1 416 ? -3.809  1.074   24.660  1.00 33.18  ? 416  MET A CG  1 
ATOM   3370 S  SD  . MET A 1 416 ? -5.112  0.718   25.867  1.00 37.21  ? 416  MET A SD  1 
ATOM   3371 C  CE  . MET A 1 416 ? -4.238  1.045   27.393  1.00 40.53  ? 416  MET A CE  1 
ATOM   3372 N  N   . MET A 1 417 ? -0.129  -1.560  23.562  1.00 33.47  ? 417  MET A N   1 
ATOM   3373 C  CA  . MET A 1 417 ? 1.081   -2.316  23.857  1.00 33.79  ? 417  MET A CA  1 
ATOM   3374 C  C   . MET A 1 417 ? 2.314   -1.574  23.381  1.00 34.53  ? 417  MET A C   1 
ATOM   3375 O  O   . MET A 1 417 ? 3.348   -1.587  24.057  1.00 33.80  ? 417  MET A O   1 
ATOM   3376 C  CB  . MET A 1 417 ? 1.124   -3.753  23.301  1.00 35.63  ? 417  MET A CB  1 
ATOM   3377 C  CG  . MET A 1 417 ? 0.104   -4.835  23.721  1.00 35.69  ? 417  MET A CG  1 
ATOM   3378 S  SD  . MET A 1 417 ? -0.651  -5.835  22.434  1.00 34.28  ? 417  MET A SD  1 
ATOM   3379 C  CE  . MET A 1 417 ? 0.783   -6.865  22.080  1.00 37.85  ? 417  MET A CE  1 
ATOM   3380 N  N   . LEU A 1 418 ? 2.235   -0.942  22.212  1.00 33.08  ? 418  LEU A N   1 
ATOM   3381 C  CA  . LEU A 1 418 ? 3.411   -0.252  21.689  1.00 33.29  ? 418  LEU A CA  1 
ATOM   3382 C  C   . LEU A 1 418 ? 3.689   1.048   22.431  1.00 33.47  ? 418  LEU A C   1 
ATOM   3383 O  O   . LEU A 1 418 ? 4.830   1.526   22.440  1.00 36.58  ? 418  LEU A O   1 
ATOM   3384 C  CB  . LEU A 1 418 ? 3.220   0.020   20.201  1.00 32.43  ? 418  LEU A CB  1 
ATOM   3385 C  CG  . LEU A 1 418 ? 3.153   -1.269  19.372  1.00 34.73  ? 418  LEU A CG  1 
ATOM   3386 C  CD1 . LEU A 1 418 ? 2.765   -0.980  17.919  1.00 36.28  ? 418  LEU A CD1 1 
ATOM   3387 C  CD2 . LEU A 1 418 ? 4.447   -2.052  19.412  1.00 40.12  ? 418  LEU A CD2 1 
ATOM   3388 N  N   . LYS A 1 419 ? 2.664   1.656   23.018  1.00 33.85  ? 419  LYS A N   1 
ATOM   3389 C  CA  . LYS A 1 419 ? 2.885   2.853   23.825  1.00 33.39  ? 419  LYS A CA  1 
ATOM   3390 C  C   . LYS A 1 419 ? 3.624   2.513   25.111  1.00 39.52  ? 419  LYS A C   1 
ATOM   3391 O  O   . LYS A 1 419 ? 4.527   3.251   25.531  1.00 37.52  ? 419  LYS A O   1 
ATOM   3392 C  CB  . LYS A 1 419 ? 1.551   3.527   24.151  1.00 36.24  ? 419  LYS A CB  1 
ATOM   3393 C  CG  . LYS A 1 419 ? 1.679   4.684   25.171  1.00 37.77  ? 419  LYS A CG  1 
ATOM   3394 C  CD  . LYS A 1 419 ? 0.335   5.346   25.442  1.00 37.87  ? 419  LYS A CD  1 
ATOM   3395 C  CE  . LYS A 1 419 ? 0.426   6.426   26.517  1.00 41.25  ? 419  LYS A CE  1 
ATOM   3396 N  NZ  . LYS A 1 419 ? -0.877  7.129   26.684  1.00 41.42  ? 419  LYS A NZ  1 
ATOM   3397 N  N   . HIS A 1 420 ? 3.279   1.385   25.731  1.00 35.16  ? 420  HIS A N   1 
ATOM   3398 C  CA  . HIS A 1 420 ? 3.684   1.131   27.110  1.00 34.97  ? 420  HIS A CA  1 
ATOM   3399 C  C   . HIS A 1 420 ? 4.885   0.201   27.265  1.00 36.15  ? 420  HIS A C   1 
ATOM   3400 O  O   . HIS A 1 420 ? 5.462   0.166   28.355  1.00 37.49  ? 420  HIS A O   1 
ATOM   3401 C  CB  . HIS A 1 420 ? 2.493   0.576   27.901  1.00 34.75  ? 420  HIS A CB  1 
ATOM   3402 C  CG  . HIS A 1 420 ? 1.472   1.619   28.232  1.00 37.75  ? 420  HIS A CG  1 
ATOM   3403 N  ND1 . HIS A 1 420 ? 1.606   2.473   29.304  1.00 35.92  ? 420  HIS A ND1 1 
ATOM   3404 C  CD2 . HIS A 1 420 ? 0.313   1.960   27.621  1.00 36.43  ? 420  HIS A CD2 1 
ATOM   3405 C  CE1 . HIS A 1 420 ? 0.571   3.293   29.342  1.00 38.63  ? 420  HIS A CE1 1 
ATOM   3406 N  NE2 . HIS A 1 420 ? -0.230  3.003   28.331  1.00 37.34  ? 420  HIS A NE2 1 
ATOM   3407 N  N   . PHE A 1 421 ? 5.295   -0.533  26.229  1.00 35.12  ? 421  PHE A N   1 
ATOM   3408 C  CA  . PHE A 1 421 ? 6.339   -1.543  26.365  1.00 36.09  ? 421  PHE A CA  1 
ATOM   3409 C  C   . PHE A 1 421 ? 7.234   -1.597  25.138  1.00 38.62  ? 421  PHE A C   1 
ATOM   3410 O  O   . PHE A 1 421 ? 6.781   -1.414  24.004  1.00 36.65  ? 421  PHE A O   1 
ATOM   3411 C  CB  . PHE A 1 421 ? 5.770   -2.967  26.551  1.00 36.51  ? 421  PHE A CB  1 
ATOM   3412 C  CG  . PHE A 1 421 ? 4.788   -3.091  27.677  1.00 34.38  ? 421  PHE A CG  1 
ATOM   3413 C  CD1 . PHE A 1 421 ? 5.218   -3.309  28.973  1.00 33.83  ? 421  PHE A CD1 1 
ATOM   3414 C  CD2 . PHE A 1 421 ? 3.427   -2.991  27.431  1.00 36.54  ? 421  PHE A CD2 1 
ATOM   3415 C  CE1 . PHE A 1 421 ? 4.316   -3.426  30.007  1.00 35.64  ? 421  PHE A CE1 1 
ATOM   3416 C  CE2 . PHE A 1 421 ? 2.511   -3.102  28.453  1.00 33.38  ? 421  PHE A CE2 1 
ATOM   3417 C  CZ  . PHE A 1 421 ? 2.952   -3.319  29.753  1.00 34.86  ? 421  PHE A CZ  1 
ATOM   3418 N  N   . ASP A 1 422 ? 8.511   -1.879  25.387  1.00 40.34  ? 422  ASP A N   1 
ATOM   3419 C  CA  . ASP A 1 422 ? 9.395   -2.467  24.396  1.00 39.45  ? 422  ASP A CA  1 
ATOM   3420 C  C   . ASP A 1 422 ? 9.274   -3.982  24.484  1.00 41.63  ? 422  ASP A C   1 
ATOM   3421 O  O   . ASP A 1 422 ? 8.966   -4.528  25.545  1.00 41.47  ? 422  ASP A O   1 
ATOM   3422 C  CB  . ASP A 1 422 ? 10.845  -2.048  24.639  1.00 39.65  ? 422  ASP A CB  1 
ATOM   3423 C  CG  . ASP A 1 422 ? 11.055  -0.576  24.406  1.00 45.45  ? 422  ASP A CG  1 
ATOM   3424 O  OD1 . ASP A 1 422 ? 10.736  -0.109  23.289  1.00 49.73  ? 422  ASP A OD1 1 
ATOM   3425 O  OD2 . ASP A 1 422 ? 11.520  0.108   25.337  1.00 49.88  ? 422  ASP A OD2 1 
ATOM   3426 N  N   . PHE A 1 423 ? 9.512   -4.662  23.364  1.00 35.51  ? 423  PHE A N   1 
ATOM   3427 C  CA  . PHE A 1 423 ? 9.344   -6.110  23.306  1.00 36.41  ? 423  PHE A CA  1 
ATOM   3428 C  C   . PHE A 1 423 ? 10.608  -6.793  22.820  1.00 40.60  ? 423  PHE A C   1 
ATOM   3429 O  O   . PHE A 1 423 ? 11.319  -6.281  21.947  1.00 42.30  ? 423  PHE A O   1 
ATOM   3430 C  CB  . PHE A 1 423 ? 8.173   -6.518  22.399  1.00 34.74  ? 423  PHE A CB  1 
ATOM   3431 C  CG  . PHE A 1 423 ? 6.842   -6.066  22.913  1.00 33.81  ? 423  PHE A CG  1 
ATOM   3432 C  CD1 . PHE A 1 423 ? 6.119   -6.864  23.785  1.00 36.36  ? 423  PHE A CD1 1 
ATOM   3433 C  CD2 . PHE A 1 423 ? 6.334   -4.824  22.556  1.00 36.49  ? 423  PHE A CD2 1 
ATOM   3434 C  CE1 . PHE A 1 423 ? 4.889   -6.449  24.272  1.00 35.12  ? 423  PHE A CE1 1 
ATOM   3435 C  CE2 . PHE A 1 423 ? 5.116   -4.394  23.039  1.00 32.01  ? 423  PHE A CE2 1 
ATOM   3436 C  CZ  . PHE A 1 423 ? 4.390   -5.204  23.910  1.00 35.97  ? 423  PHE A CZ  1 
ATOM   3437 N  N   . GLU A 1 424 ? 10.866  -7.970  23.373  1.00 37.26  ? 424  GLU A N   1 
ATOM   3438 C  CA  . GLU A 1 424 ? 12.060  -8.734  23.045  1.00 37.75  ? 424  GLU A CA  1 
ATOM   3439 C  C   . GLU A 1 424 ? 11.661  -10.150 22.670  1.00 35.92  ? 424  GLU A C   1 
ATOM   3440 O  O   . GLU A 1 424 ? 10.969  -10.829 23.439  1.00 35.53  ? 424  GLU A O   1 
ATOM   3441 C  CB  . GLU A 1 424 ? 13.040  -8.755  24.225  1.00 36.20  ? 424  GLU A CB  1 
ATOM   3442 C  CG  . GLU A 1 424 ? 14.345  -9.444  23.905  1.00 40.90  ? 424  GLU A CG  1 
ATOM   3443 C  CD  . GLU A 1 424 ? 15.162  -9.747  25.150  1.00 48.49  ? 424  GLU A CD  1 
ATOM   3444 O  OE1 . GLU A 1 424 ? 14.707  -9.427  26.271  1.00 45.76  ? 424  GLU A OE1 1 
ATOM   3445 O  OE2 . GLU A 1 424 ? 16.274  -10.280 24.999  1.00 50.82  ? 424  GLU A OE2 1 
ATOM   3446 N  N   . ASP A 1 425 ? 12.108  -10.592 21.495  1.00 36.87  ? 425  ASP A N   1 
ATOM   3447 C  CA  . ASP A 1 425 ? 11.953  -11.978 21.051  1.00 33.04  ? 425  ASP A CA  1 
ATOM   3448 C  C   . ASP A 1 425 ? 13.110  -12.770 21.661  1.00 37.16  ? 425  ASP A C   1 
ATOM   3449 O  O   . ASP A 1 425 ? 14.070  -13.170 20.995  1.00 36.83  ? 425  ASP A O   1 
ATOM   3450 C  CB  . ASP A 1 425 ? 11.924  -12.028 19.526  1.00 34.98  ? 425  ASP A CB  1 
ATOM   3451 C  CG  . ASP A 1 425 ? 11.917  -13.429 18.957  1.00 33.39  ? 425  ASP A CG  1 
ATOM   3452 O  OD1 . ASP A 1 425 ? 11.458  -14.381 19.619  1.00 35.58  ? 425  ASP A OD1 1 
ATOM   3453 O  OD2 . ASP A 1 425 ? 12.362  -13.556 17.789  1.00 36.58  ? 425  ASP A OD2 1 
ATOM   3454 N  N   . HIS A 1 426 ? 13.008  -12.976 22.979  1.00 36.81  ? 426  HIS A N   1 
ATOM   3455 C  CA  . HIS A 1 426 ? 14.157  -13.461 23.744  1.00 38.40  ? 426  HIS A CA  1 
ATOM   3456 C  C   . HIS A 1 426 ? 14.505  -14.911 23.439  1.00 39.54  ? 426  HIS A C   1 
ATOM   3457 O  O   . HIS A 1 426 ? 15.635  -15.327 23.719  1.00 41.49  ? 426  HIS A O   1 
ATOM   3458 C  CB  . HIS A 1 426 ? 13.906  -13.301 25.240  1.00 37.11  ? 426  HIS A CB  1 
ATOM   3459 C  CG  . HIS A 1 426 ? 12.769  -14.126 25.750  1.00 39.80  ? 426  HIS A CG  1 
ATOM   3460 N  ND1 . HIS A 1 426 ? 11.461  -13.900 25.372  1.00 34.87  ? 426  HIS A ND1 1 
ATOM   3461 C  CD2 . HIS A 1 426 ? 12.739  -15.171 26.613  1.00 40.20  ? 426  HIS A CD2 1 
ATOM   3462 C  CE1 . HIS A 1 426 ? 10.676  -14.775 25.977  1.00 36.83  ? 426  HIS A CE1 1 
ATOM   3463 N  NE2 . HIS A 1 426 ? 11.424  -15.551 26.743  1.00 41.97  ? 426  HIS A NE2 1 
ATOM   3464 N  N   . THR A 1 427 ? 13.578  -15.689 22.876  1.00 37.51  ? 427  THR A N   1 
ATOM   3465 C  CA  . THR A 1 427 ? 13.850  -17.074 22.508  1.00 34.55  ? 427  THR A CA  1 
ATOM   3466 C  C   . THR A 1 427 ? 14.129  -17.266 21.022  1.00 36.64  ? 427  THR A C   1 
ATOM   3467 O  O   . THR A 1 427 ? 14.301  -18.406 20.586  1.00 35.28  ? 427  THR A O   1 
ATOM   3468 C  CB  . THR A 1 427 ? 12.682  -17.987 22.916  1.00 39.88  ? 427  THR A CB  1 
ATOM   3469 O  OG1 . THR A 1 427 ? 11.575  -17.814 22.010  1.00 38.58  ? 427  THR A OG1 1 
ATOM   3470 C  CG2 . THR A 1 427 ? 12.231  -17.668 24.339  1.00 37.67  ? 427  THR A CG2 1 
ATOM   3471 N  N   . ASN A 1 428 ? 14.172  -16.197 20.234  1.00 35.58  ? 428  ASN A N   1 
ATOM   3472 C  CA  . ASN A 1 428 ? 14.239  -16.323 18.782  1.00 36.77  ? 428  ASN A CA  1 
ATOM   3473 C  C   . ASN A 1 428 ? 13.194  -17.325 18.293  1.00 37.39  ? 428  ASN A C   1 
ATOM   3474 O  O   . ASN A 1 428 ? 13.492  -18.360 17.689  1.00 38.99  ? 428  ASN A O   1 
ATOM   3475 C  CB  . ASN A 1 428 ? 15.645  -16.715 18.324  1.00 36.66  ? 428  ASN A CB  1 
ATOM   3476 C  CG  . ASN A 1 428 ? 15.829  -16.514 16.839  1.00 45.68  ? 428  ASN A CG  1 
ATOM   3477 O  OD1 . ASN A 1 428 ? 15.119  -15.709 16.228  1.00 43.23  ? 428  ASN A OD1 1 
ATOM   3478 N  ND2 . ASN A 1 428 ? 16.767  -17.248 16.241  1.00 45.66  ? 428  ASN A ND2 1 
ATOM   3479 N  N   . TYR A 1 429 ? 11.937  -16.983 18.563  1.00 36.07  ? 429  TYR A N   1 
ATOM   3480 C  CA  . TYR A 1 429 ? 10.852  -17.940 18.410  1.00 34.97  ? 429  TYR A CA  1 
ATOM   3481 C  C   . TYR A 1 429 ? 10.692  -18.380 16.959  1.00 35.64  ? 429  TYR A C   1 
ATOM   3482 O  O   . TYR A 1 429 ? 10.710  -17.558 16.038  1.00 35.37  ? 429  TYR A O   1 
ATOM   3483 C  CB  . TYR A 1 429 ? 9.562   -17.307 18.934  1.00 35.91  ? 429  TYR A CB  1 
ATOM   3484 C  CG  . TYR A 1 429 ? 8.300   -18.017 18.533  1.00 36.04  ? 429  TYR A CG  1 
ATOM   3485 C  CD1 . TYR A 1 429 ? 7.938   -19.226 19.121  1.00 32.68  ? 429  TYR A CD1 1 
ATOM   3486 C  CD2 . TYR A 1 429 ? 7.452   -17.464 17.565  1.00 36.99  ? 429  TYR A CD2 1 
ATOM   3487 C  CE1 . TYR A 1 429 ? 6.740   -19.875 18.753  1.00 34.56  ? 429  TYR A CE1 1 
ATOM   3488 C  CE2 . TYR A 1 429 ? 6.274   -18.099 17.197  1.00 33.87  ? 429  TYR A CE2 1 
ATOM   3489 C  CZ  . TYR A 1 429 ? 5.930   -19.296 17.774  1.00 36.05  ? 429  TYR A CZ  1 
ATOM   3490 O  OH  . TYR A 1 429 ? 4.756   -19.907 17.383  1.00 31.50  ? 429  TYR A OH  1 
ATOM   3491 N  N   . GLU A 1 430 ? 10.544  -19.686 16.767  1.00 34.59  ? 430  GLU A N   1 
ATOM   3492 C  CA  . GLU A 1 430 ? 10.252  -20.274 15.466  1.00 42.20  ? 430  GLU A CA  1 
ATOM   3493 C  C   . GLU A 1 430 ? 8.742   -20.380 15.302  1.00 36.98  ? 430  GLU A C   1 
ATOM   3494 O  O   . GLU A 1 430 ? 8.084   -21.101 16.060  1.00 38.16  ? 430  GLU A O   1 
ATOM   3495 C  CB  . GLU A 1 430 ? 10.879  -21.660 15.330  1.00 44.35  ? 430  GLU A CB  1 
ATOM   3496 C  CG  . GLU A 1 430 ? 10.949  -22.158 13.899  1.00 47.14  ? 430  GLU A CG  1 
ATOM   3497 C  CD  . GLU A 1 430 ? 11.677  -23.489 13.768  1.00 62.95  ? 430  GLU A CD  1 
ATOM   3498 O  OE1 . GLU A 1 430 ? 12.742  -23.662 14.397  1.00 67.67  ? 430  GLU A OE1 1 
ATOM   3499 O  OE2 . GLU A 1 430 ? 11.172  -24.368 13.039  1.00 70.93  ? 430  GLU A OE2 1 
ATOM   3500 N  N   . LEU A 1 431 ? 8.200   -19.696 14.296  1.00 34.08  ? 431  LEU A N   1 
ATOM   3501 C  CA  . LEU A 1 431 ? 6.749   -19.675 14.125  1.00 33.85  ? 431  LEU A CA  1 
ATOM   3502 C  C   . LEU A 1 431 ? 6.198   -21.090 13.983  1.00 37.26  ? 431  LEU A C   1 
ATOM   3503 O  O   . LEU A 1 431 ? 6.669   -21.878 13.157  1.00 36.62  ? 431  LEU A O   1 
ATOM   3504 C  CB  . LEU A 1 431 ? 6.375   -18.823 12.912  1.00 36.09  ? 431  LEU A CB  1 
ATOM   3505 C  CG  . LEU A 1 431 ? 4.868   -18.727 12.643  1.00 34.04  ? 431  LEU A CG  1 
ATOM   3506 C  CD1 . LEU A 1 431 ? 4.161   -18.091 13.833  1.00 35.54  ? 431  LEU A CD1 1 
ATOM   3507 C  CD2 . LEU A 1 431 ? 4.618   -17.951 11.364  1.00 37.75  ? 431  LEU A CD2 1 
ATOM   3508 N  N   . ASP A 1 432 ? 5.188   -21.400 14.799  1.00 33.29  ? 432  ASP A N   1 
ATOM   3509 C  CA  . ASP A 1 432 ? 4.533   -22.703 14.837  1.00 32.00  ? 432  ASP A CA  1 
ATOM   3510 C  C   . ASP A 1 432 ? 3.033   -22.428 14.886  1.00 33.13  ? 432  ASP A C   1 
ATOM   3511 O  O   . ASP A 1 432 ? 2.538   -21.889 15.883  1.00 35.89  ? 432  ASP A O   1 
ATOM   3512 C  CB  . ASP A 1 432 ? 5.000   -23.494 16.069  1.00 38.64  ? 432  ASP A CB  1 
ATOM   3513 C  CG  . ASP A 1 432 ? 4.370   -24.873 16.175  1.00 43.58  ? 432  ASP A CG  1 
ATOM   3514 O  OD1 . ASP A 1 432 ? 3.582   -25.262 15.296  1.00 41.09  ? 432  ASP A OD1 1 
ATOM   3515 O  OD2 . ASP A 1 432 ? 4.664   -25.578 17.167  1.00 50.93  ? 432  ASP A OD2 1 
ATOM   3516 N  N   . ILE A 1 433 ? 2.319   -22.764 13.821  1.00 32.64  ? 433  ILE A N   1 
ATOM   3517 C  CA  . ILE A 1 433 ? 0.932   -22.332 13.658  1.00 32.48  ? 433  ILE A CA  1 
ATOM   3518 C  C   . ILE A 1 433 ? 0.016   -23.499 14.000  1.00 32.40  ? 433  ILE A C   1 
ATOM   3519 O  O   . ILE A 1 433 ? -0.042  -24.503 13.278  1.00 32.17  ? 433  ILE A O   1 
ATOM   3520 C  CB  . ILE A 1 433 ? 0.677   -21.803 12.239  1.00 31.21  ? 433  ILE A CB  1 
ATOM   3521 C  CG1 . ILE A 1 433 ? 1.533   -20.562 12.005  1.00 33.02  ? 433  ILE A CG1 1 
ATOM   3522 C  CG2 . ILE A 1 433 ? -0.829  -21.446 12.046  1.00 30.75  ? 433  ILE A CG2 1 
ATOM   3523 C  CD1 . ILE A 1 433 ? 1.536   -20.077 10.565  1.00 35.38  ? 433  ILE A CD1 1 
ATOM   3524 N  N   . LYS A 1 434 ? -0.737  -23.344 15.088  1.00 31.87  ? 434  LYS A N   1 
ATOM   3525 C  CA  . LYS A 1 434 ? -1.705  -24.343 15.501  1.00 32.66  ? 434  LYS A CA  1 
ATOM   3526 C  C   . LYS A 1 434 ? -3.013  -24.115 14.763  1.00 31.45  ? 434  LYS A C   1 
ATOM   3527 O  O   . LYS A 1 434 ? -3.437  -22.971 14.571  1.00 33.97  ? 434  LYS A O   1 
ATOM   3528 C  CB  . LYS A 1 434 ? -1.946  -24.260 17.009  1.00 36.31  ? 434  LYS A CB  1 
ATOM   3529 C  CG  . LYS A 1 434 ? -3.006  -25.206 17.543  1.00 34.30  ? 434  LYS A CG  1 
ATOM   3530 C  CD  . LYS A 1 434 ? -3.016  -25.138 19.078  1.00 37.21  ? 434  LYS A CD  1 
ATOM   3531 C  CE  . LYS A 1 434 ? -4.122  -25.985 19.690  1.00 41.81  ? 434  LYS A CE  1 
ATOM   3532 N  NZ  . LYS A 1 434 ? -3.908  -27.431 19.414  1.00 45.10  ? 434  LYS A NZ  1 
ATOM   3533 N  N   . GLU A 1 435 ? -3.656  -25.203 14.365  1.00 30.29  ? 435  GLU A N   1 
ATOM   3534 C  CA  . GLU A 1 435 ? -4.911  -25.126 13.631  1.00 32.73  ? 435  GLU A CA  1 
ATOM   3535 C  C   . GLU A 1 435 ? -6.066  -25.657 14.470  1.00 33.09  ? 435  GLU A C   1 
ATOM   3536 O  O   . GLU A 1 435 ? -6.023  -26.788 14.975  1.00 33.08  ? 435  GLU A O   1 
ATOM   3537 C  CB  . GLU A 1 435 ? -4.802  -25.881 12.305  1.00 31.72  ? 435  GLU A CB  1 
ATOM   3538 C  CG  . GLU A 1 435 ? -3.691  -25.308 11.446  1.00 32.36  ? 435  GLU A CG  1 
ATOM   3539 C  CD  . GLU A 1 435 ? -3.828  -25.676 9.975   1.00 35.09  ? 435  GLU A CD  1 
ATOM   3540 O  OE1 . GLU A 1 435 ? -4.944  -26.079 9.567   1.00 32.62  ? 435  GLU A OE1 1 
ATOM   3541 O  OE2 . GLU A 1 435 ? -2.820  -25.558 9.236   1.00 33.99  ? 435  GLU A OE2 1 
ATOM   3542 N  N   . THR A 1 436 ? -7.095  -24.834 14.608  1.00 33.76  ? 436  THR A N   1 
ATOM   3543 C  CA  . THR A 1 436 ? -8.369  -25.208 15.207  1.00 34.77  ? 436  THR A CA  1 
ATOM   3544 C  C   . THR A 1 436 ? -9.503  -24.747 14.297  1.00 34.28  ? 436  THR A C   1 
ATOM   3545 O  O   . THR A 1 436 ? -10.441 -24.076 14.724  1.00 35.11  ? 436  THR A O   1 
ATOM   3546 C  CB  . THR A 1 436 ? -8.508  -24.613 16.606  1.00 34.27  ? 436  THR A CB  1 
ATOM   3547 O  OG1 . THR A 1 436 ? -8.387  -23.183 16.543  1.00 34.49  ? 436  THR A OG1 1 
ATOM   3548 C  CG2 . THR A 1 436 ? -7.421  -25.168 17.534  1.00 37.14  ? 436  THR A CG2 1 
ATOM   3549 N  N   . LEU A 1 437 ? -9.417  -25.133 13.021  1.00 31.74  ? 437  LEU A N   1 
ATOM   3550 C  CA  . LEU A 1 437 ? -10.135 -24.501 11.917  1.00 33.35  ? 437  LEU A CA  1 
ATOM   3551 C  C   . LEU A 1 437 ? -9.506  -23.123 11.696  1.00 36.21  ? 437  LEU A C   1 
ATOM   3552 O  O   . LEU A 1 437 ? -8.934  -22.877 10.625  1.00 35.64  ? 437  LEU A O   1 
ATOM   3553 C  CB  . LEU A 1 437 ? -11.656 -24.435 12.166  1.00 34.76  ? 437  LEU A CB  1 
ATOM   3554 C  CG  . LEU A 1 437 ? -12.436 -25.754 12.441  1.00 39.47  ? 437  LEU A CG  1 
ATOM   3555 C  CD1 . LEU A 1 437 ? -13.945 -25.512 12.491  1.00 37.93  ? 437  LEU A CD1 1 
ATOM   3556 C  CD2 . LEU A 1 437 ? -12.119 -26.822 11.408  1.00 35.70  ? 437  LEU A CD2 1 
ATOM   3557 N  N   . THR A 1 438 ? -9.545  -22.248 12.711  1.00 34.78  ? 438  THR A N   1 
ATOM   3558 C  CA  . THR A 1 438 ? -8.778  -21.006 12.726  1.00 34.39  ? 438  THR A CA  1 
ATOM   3559 C  C   . THR A 1 438 ? -7.279  -21.262 12.976  1.00 34.42  ? 438  THR A C   1 
ATOM   3560 O  O   . THR A 1 438 ? -6.862  -22.360 13.370  1.00 33.00  ? 438  THR A O   1 
ATOM   3561 C  CB  . THR A 1 438 ? -9.317  -20.058 13.791  1.00 35.74  ? 438  THR A CB  1 
ATOM   3562 O  OG1 . THR A 1 438 ? -9.295  -20.718 15.066  1.00 37.61  ? 438  THR A OG1 1 
ATOM   3563 C  CG2 . THR A 1 438 ? -10.760 -19.644 13.465  1.00 32.81  ? 438  THR A CG2 1 
ATOM   3564 N  N   . LEU A 1 439 ? -6.474  -20.216 12.756  1.00 31.17  ? 439  LEU A N   1 
ATOM   3565 C  CA  . LEU A 1 439 ? -5.013  -20.270 12.856  1.00 28.60  ? 439  LEU A CA  1 
ATOM   3566 C  C   . LEU A 1 439 ? -4.486  -19.349 13.954  1.00 30.86  ? 439  LEU A C   1 
ATOM   3567 O  O   . LEU A 1 439 ? -4.919  -18.198 14.080  1.00 29.83  ? 439  LEU A O   1 
ATOM   3568 C  CB  . LEU A 1 439 ? -4.376  -19.869 11.532  1.00 29.37  ? 439  LEU A CB  1 
ATOM   3569 C  CG  . LEU A 1 439 ? -4.825  -20.588 10.260  1.00 29.77  ? 439  LEU A CG  1 
ATOM   3570 C  CD1 . LEU A 1 439 ? -3.989  -20.041 9.093   1.00 32.19  ? 439  LEU A CD1 1 
ATOM   3571 C  CD2 . LEU A 1 439 ? -4.686  -22.120 10.355  1.00 29.70  ? 439  LEU A CD2 1 
ATOM   3572 N  N   . LYS A 1 440 ? -3.511  -19.840 14.733  1.00 29.83  ? 440  LYS A N   1 
ATOM   3573 C  CA  . LYS A 1 440 ? -2.922  -19.042 15.800  1.00 28.93  ? 440  LYS A CA  1 
ATOM   3574 C  C   . LYS A 1 440 ? -1.505  -19.541 16.044  1.00 32.02  ? 440  LYS A C   1 
ATOM   3575 O  O   . LYS A 1 440 ? -1.278  -20.758 15.976  1.00 34.67  ? 440  LYS A O   1 
ATOM   3576 C  CB  . LYS A 1 440 ? -3.757  -19.149 17.094  1.00 33.63  ? 440  LYS A CB  1 
ATOM   3577 C  CG  . LYS A 1 440 ? -3.569  -18.003 18.069  1.00 37.53  ? 440  LYS A CG  1 
ATOM   3578 C  CD  . LYS A 1 440 ? -4.443  -18.158 19.334  1.00 38.52  ? 440  LYS A CD  1 
ATOM   3579 C  CE  . LYS A 1 440 ? -5.896  -18.460 19.034  1.00 40.82  ? 440  LYS A CE  1 
ATOM   3580 N  NZ  . LYS A 1 440 ? -6.746  -18.342 20.286  1.00 39.34  ? 440  LYS A NZ  1 
ATOM   3581 N  N   . PRO A 1 441 ? -0.538  -18.656 16.309  1.00 32.70  ? 441  PRO A N   1 
ATOM   3582 C  CA  . PRO A 1 441 ? 0.776   -19.135 16.763  1.00 32.04  ? 441  PRO A CA  1 
ATOM   3583 C  C   . PRO A 1 441 ? 0.611   -19.972 18.023  1.00 35.39  ? 441  PRO A C   1 
ATOM   3584 O  O   . PRO A 1 441 ? -0.278  -19.729 18.841  1.00 33.62  ? 441  PRO A O   1 
ATOM   3585 C  CB  . PRO A 1 441 ? 1.555   -17.845 17.056  1.00 31.82  ? 441  PRO A CB  1 
ATOM   3586 C  CG  . PRO A 1 441 ? 0.840   -16.761 16.313  1.00 33.59  ? 441  PRO A CG  1 
ATOM   3587 C  CD  . PRO A 1 441 ? -0.614  -17.184 16.301  1.00 29.57  ? 441  PRO A CD  1 
ATOM   3588 N  N   . GLU A 1 442 ? 1.479   -20.965 18.177  1.00 33.32  ? 442  GLU A N   1 
ATOM   3589 C  CA  . GLU A 1 442 ? 1.530   -21.763 19.392  1.00 35.64  ? 442  GLU A CA  1 
ATOM   3590 C  C   . GLU A 1 442 ? 2.910   -21.602 20.009  1.00 35.88  ? 442  GLU A C   1 
ATOM   3591 O  O   . GLU A 1 442 ? 3.921   -21.604 19.295  1.00 33.18  ? 442  GLU A O   1 
ATOM   3592 C  CB  . GLU A 1 442 ? 1.244   -23.247 19.127  1.00 38.47  ? 442  GLU A CB  1 
ATOM   3593 C  CG  . GLU A 1 442 ? 1.279   -24.074 20.419  1.00 40.33  ? 442  GLU A CG  1 
ATOM   3594 C  CD  . GLU A 1 442 ? 0.840   -25.524 20.236  1.00 44.94  ? 442  GLU A CD  1 
ATOM   3595 O  OE1 . GLU A 1 442 ? 0.932   -26.058 19.112  1.00 45.24  ? 442  GLU A OE1 1 
ATOM   3596 O  OE2 . GLU A 1 442 ? 0.381   -26.122 21.233  1.00 52.72  ? 442  GLU A OE2 1 
ATOM   3597 N  N   . GLY A 1 443 ? 2.945   -21.428 21.327  1.00 34.88  ? 443  GLY A N   1 
ATOM   3598 C  CA  . GLY A 1 443 ? 4.214   -21.334 22.028  1.00 33.95  ? 443  GLY A CA  1 
ATOM   3599 C  C   . GLY A 1 443 ? 4.976   -20.050 21.815  1.00 33.49  ? 443  GLY A C   1 
ATOM   3600 O  O   . GLY A 1 443 ? 6.156   -19.987 22.167  1.00 36.71  ? 443  GLY A O   1 
ATOM   3601 N  N   . PHE A 1 444 ? 4.341   -19.023 21.248  1.00 33.34  ? 444  PHE A N   1 
ATOM   3602 C  CA  . PHE A 1 444 ? 4.975   -17.728 21.035  1.00 33.62  ? 444  PHE A CA  1 
ATOM   3603 C  C   . PHE A 1 444 ? 5.073   -16.987 22.365  1.00 34.24  ? 444  PHE A C   1 
ATOM   3604 O  O   . PHE A 1 444 ? 4.053   -16.693 23.001  1.00 32.06  ? 444  PHE A O   1 
ATOM   3605 C  CB  . PHE A 1 444 ? 4.171   -16.932 20.000  1.00 32.22  ? 444  PHE A CB  1 
ATOM   3606 C  CG  . PHE A 1 444 ? 4.670   -15.534 19.753  1.00 34.32  ? 444  PHE A CG  1 
ATOM   3607 C  CD1 . PHE A 1 444 ? 6.022   -15.239 19.741  1.00 34.66  ? 444  PHE A CD1 1 
ATOM   3608 C  CD2 . PHE A 1 444 ? 3.769   -14.512 19.462  1.00 33.09  ? 444  PHE A CD2 1 
ATOM   3609 C  CE1 . PHE A 1 444 ? 6.464   -13.943 19.507  1.00 33.26  ? 444  PHE A CE1 1 
ATOM   3610 C  CE2 . PHE A 1 444 ? 4.200   -13.218 19.215  1.00 34.16  ? 444  PHE A CE2 1 
ATOM   3611 C  CZ  . PHE A 1 444 ? 5.554   -12.926 19.234  1.00 34.28  ? 444  PHE A CZ  1 
ATOM   3612 N  N   . VAL A 1 445 ? 6.304   -16.713 22.802  1.00 31.01  ? 445  VAL A N   1 
ATOM   3613 C  CA  . VAL A 1 445 ? 6.564   -15.986 24.035  1.00 34.53  ? 445  VAL A CA  1 
ATOM   3614 C  C   . VAL A 1 445 ? 7.485   -14.819 23.715  1.00 31.46  ? 445  VAL A C   1 
ATOM   3615 O  O   . VAL A 1 445 ? 8.283   -14.875 22.772  1.00 34.27  ? 445  VAL A O   1 
ATOM   3616 C  CB  . VAL A 1 445 ? 7.189   -16.892 25.125  1.00 34.09  ? 445  VAL A CB  1 
ATOM   3617 C  CG1 . VAL A 1 445 ? 6.234   -18.019 25.496  1.00 34.36  ? 445  VAL A CG1 1 
ATOM   3618 C  CG2 . VAL A 1 445 ? 8.523   -17.473 24.634  1.00 37.45  ? 445  VAL A CG2 1 
ATOM   3619 N  N   . VAL A 1 446 ? 7.352   -13.745 24.485  1.00 32.25  ? 446  VAL A N   1 
ATOM   3620 C  CA  . VAL A 1 446 ? 8.240   -12.586 24.403  1.00 33.77  ? 446  VAL A CA  1 
ATOM   3621 C  C   . VAL A 1 446 ? 8.450   -12.048 25.814  1.00 36.12  ? 446  VAL A C   1 
ATOM   3622 O  O   . VAL A 1 446 ? 7.768   -12.441 26.765  1.00 34.95  ? 446  VAL A O   1 
ATOM   3623 C  CB  . VAL A 1 446 ? 7.685   -11.464 23.487  1.00 34.02  ? 446  VAL A CB  1 
ATOM   3624 C  CG1 . VAL A 1 446 ? 7.372   -11.992 22.092  1.00 33.39  ? 446  VAL A CG1 1 
ATOM   3625 C  CG2 . VAL A 1 446 ? 6.448   -10.786 24.119  1.00 34.39  ? 446  VAL A CG2 1 
ATOM   3626 N  N   . LYS A 1 447 ? 9.411   -11.136 25.946  1.00 36.23  ? 447  LYS A N   1 
ATOM   3627 C  CA  . LYS A 1 447 ? 9.569   -10.343 27.151  1.00 33.50  ? 447  LYS A CA  1 
ATOM   3628 C  C   . LYS A 1 447 ? 9.217   -8.899  26.838  1.00 39.29  ? 447  LYS A C   1 
ATOM   3629 O  O   . LYS A 1 447 ? 9.536   -8.390  25.760  1.00 40.49  ? 447  LYS A O   1 
ATOM   3630 C  CB  . LYS A 1 447 ? 10.997  -10.417 27.704  1.00 38.78  ? 447  LYS A CB  1 
ATOM   3631 C  CG  . LYS A 1 447 ? 11.352  -11.744 28.319  1.00 38.55  ? 447  LYS A CG  1 
ATOM   3632 C  CD  . LYS A 1 447 ? 12.853  -11.777 28.660  1.00 44.92  ? 447  LYS A CD  1 
ATOM   3633 C  CE  . LYS A 1 447 ? 13.099  -12.399 30.012  1.00 54.02  ? 447  LYS A CE  1 
ATOM   3634 N  NZ  . LYS A 1 447 ? 13.344  -13.856 29.842  1.00 57.80  ? 447  LYS A NZ  1 
ATOM   3635 N  N   . ALA A 1 448 ? 8.544   -8.244  27.771  1.00 34.93  ? 448  ALA A N   1 
ATOM   3636 C  CA  . ALA A 1 448 ? 8.259   -6.827  27.641  1.00 37.83  ? 448  ALA A CA  1 
ATOM   3637 C  C   . ALA A 1 448 ? 9.120   -6.058  28.626  1.00 44.05  ? 448  ALA A C   1 
ATOM   3638 O  O   . ALA A 1 448 ? 9.384   -6.526  29.739  1.00 47.44  ? 448  ALA A O   1 
ATOM   3639 C  CB  . ALA A 1 448 ? 6.776   -6.525  27.881  1.00 36.82  ? 448  ALA A CB  1 
ATOM   3640 N  N   . LYS A 1 449 ? 9.571   -4.894  28.205  1.00 37.90  ? 449  LYS A N   1 
ATOM   3641 C  CA  . LYS A 1 449 ? 10.268  -3.961  29.079  1.00 39.35  ? 449  LYS A CA  1 
ATOM   3642 C  C   . LYS A 1 449 ? 9.390   -2.728  29.194  1.00 41.04  ? 449  LYS A C   1 
ATOM   3643 O  O   . LYS A 1 449 ? 9.196   -2.012  28.210  1.00 39.44  ? 449  LYS A O   1 
ATOM   3644 C  CB  . LYS A 1 449 ? 11.647  -3.613  28.517  1.00 47.69  ? 449  LYS A CB  1 
ATOM   3645 C  CG  . LYS A 1 449 ? 12.649  -3.142  29.560  1.00 52.43  ? 449  LYS A CG  1 
ATOM   3646 C  CD  . LYS A 1 449 ? 13.409  -4.302  30.192  1.00 61.86  ? 449  LYS A CD  1 
ATOM   3647 C  CE  . LYS A 1 449 ? 14.912  -4.038  30.171  1.00 72.10  ? 449  LYS A CE  1 
ATOM   3648 N  NZ  . LYS A 1 449 ? 15.635  -4.731  31.277  1.00 79.51  ? 449  LYS A NZ  1 
ATOM   3649 N  N   . SER A 1 450 ? 8.849   -2.486  30.383  1.00 37.62  ? 450  SER A N   1 
ATOM   3650 C  CA  . SER A 1 450 ? 7.974   -1.341  30.568  1.00 40.36  ? 450  SER A CA  1 
ATOM   3651 C  C   . SER A 1 450 ? 8.677   -0.034  30.216  1.00 40.31  ? 450  SER A C   1 
ATOM   3652 O  O   . SER A 1 450 ? 9.844   0.178   30.556  1.00 41.05  ? 450  SER A O   1 
ATOM   3653 C  CB  . SER A 1 450 ? 7.480   -1.284  32.008  1.00 35.03  ? 450  SER A CB  1 
ATOM   3654 O  OG  . SER A 1 450 ? 6.575   -0.205  32.175  1.00 40.40  ? 450  SER A OG  1 
ATOM   3655 N  N   . LYS A 1 451 ? 7.949   0.850   29.530  1.00 38.42  ? 451  LYS A N   1 
ATOM   3656 C  CA  . LYS A 1 451 ? 8.362   2.240   29.366  1.00 41.12  ? 451  LYS A CA  1 
ATOM   3657 C  C   . LYS A 1 451 ? 7.968   3.095   30.559  1.00 45.05  ? 451  LYS A C   1 
ATOM   3658 O  O   . LYS A 1 451 ? 8.192   4.309   30.536  1.00 51.45  ? 451  LYS A O   1 
ATOM   3659 C  CB  . LYS A 1 451 ? 7.769   2.821   28.076  1.00 41.58  ? 451  LYS A CB  1 
ATOM   3660 C  CG  . LYS A 1 451 ? 8.354   2.186   26.819  1.00 43.12  ? 451  LYS A CG  1 
ATOM   3661 C  CD  . LYS A 1 451 ? 7.699   2.720   25.554  1.00 45.70  ? 451  LYS A CD  1 
ATOM   3662 C  CE  . LYS A 1 451 ? 8.362   2.171   24.309  1.00 44.21  ? 451  LYS A CE  1 
ATOM   3663 N  NZ  . LYS A 1 451 ? 9.731   2.719   24.119  1.00 51.25  ? 451  LYS A NZ  1 
ATOM   3664 N  N   . LYS A 1 452 ? 7.381   2.478   31.585  1.00 40.37  ? 452  LYS A N   1 
ATOM   3665 C  CA  . LYS A 1 452 ? 6.951   3.144   32.811  1.00 46.16  ? 452  LYS A CA  1 
ATOM   3666 C  C   . LYS A 1 452 ? 6.133   4.402   32.521  1.00 46.15  ? 452  LYS A C   1 
ATOM   3667 O  O   . LYS A 1 452 ? 6.390   5.484   33.054  1.00 47.63  ? 452  LYS A O   1 
ATOM   3668 C  CB  . LYS A 1 452 ? 8.151   3.450   33.717  1.00 49.00  ? 452  LYS A CB  1 
ATOM   3669 C  CG  . LYS A 1 452 ? 8.839   2.206   34.291  1.00 50.60  ? 452  LYS A CG  1 
ATOM   3670 C  CD  . LYS A 1 452 ? 10.265  2.519   34.759  1.00 56.82  ? 452  LYS A CD  1 
ATOM   3671 C  CE  . LYS A 1 452 ? 10.909  1.340   35.490  1.00 66.47  ? 452  LYS A CE  1 
ATOM   3672 N  NZ  . LYS A 1 452 ? 12.013  0.707   34.712  1.00 70.52  ? 452  LYS A NZ  1 
ATOM   3673 N  N   . ILE A 1 453 ? 5.104   4.248   31.698  1.00 41.44  ? 453  ILE A N   1 
ATOM   3674 C  CA  . ILE A 1 453 ? 4.187   5.337   31.383  1.00 42.29  ? 453  ILE A CA  1 
ATOM   3675 C  C   . ILE A 1 453 ? 2.875   5.077   32.113  1.00 46.12  ? 453  ILE A C   1 
ATOM   3676 O  O   . ILE A 1 453 ? 2.220   4.059   31.852  1.00 40.90  ? 453  ILE A O   1 
ATOM   3677 C  CB  . ILE A 1 453 ? 3.966   5.464   29.871  1.00 42.94  ? 453  ILE A CB  1 
ATOM   3678 C  CG1 . ILE A 1 453 ? 5.308   5.751   29.190  1.00 45.49  ? 453  ILE A CG1 1 
ATOM   3679 C  CG2 . ILE A 1 453 ? 2.945   6.546   29.589  1.00 45.13  ? 453  ILE A CG2 1 
ATOM   3680 C  CD1 . ILE A 1 453 ? 5.258   5.658   27.678  1.00 43.04  ? 453  ILE A CD1 1 
ATOM   3681 N  N   . PRO A 1 454 ? 2.461   5.954   33.027  1.00 47.62  ? 454  PRO A N   1 
ATOM   3682 C  CA  . PRO A 1 454 ? 1.294   5.660   33.867  1.00 49.46  ? 454  PRO A CA  1 
ATOM   3683 C  C   . PRO A 1 454 ? 0.015   5.512   33.060  1.00 47.79  ? 454  PRO A C   1 
ATOM   3684 O  O   . PRO A 1 454 ? -0.149  6.112   31.994  1.00 47.94  ? 454  PRO A O   1 
ATOM   3685 C  CB  . PRO A 1 454 ? 1.203   6.875   34.802  1.00 51.46  ? 454  PRO A CB  1 
ATOM   3686 C  CG  . PRO A 1 454 ? 2.492   7.613   34.681  1.00 53.77  ? 454  PRO A CG  1 
ATOM   3687 C  CD  . PRO A 1 454 ? 3.302   7.042   33.558  1.00 49.78  ? 454  PRO A CD  1 
ATOM   3688 N  N   . LEU A 1 455 ? -0.909  4.722   33.605  1.00 45.58  ? 455  LEU A N   1 
ATOM   3689 C  CA  . LEU A 1 455 ? -2.264  4.608   33.064  1.00 46.91  ? 455  LEU A CA  1 
ATOM   3690 C  C   . LEU A 1 455 ? -3.240  5.541   33.793  1.00 53.63  ? 455  LEU A C   1 
ATOM   3691 O  O   . LEU A 1 455 ? -2.860  6.276   34.710  1.00 55.63  ? 455  LEU A O   1 
ATOM   3692 C  CB  . LEU A 1 455 ? -2.766  3.166   33.162  1.00 48.29  ? 455  LEU A CB  1 
ATOM   3693 C  CG  . LEU A 1 455 ? -2.066  2.130   32.289  1.00 43.93  ? 455  LEU A CG  1 
ATOM   3694 C  CD1 . LEU A 1 455 ? -2.286  0.741   32.871  1.00 46.62  ? 455  LEU A CD1 1 
ATOM   3695 C  CD2 . LEU A 1 455 ? -2.599  2.217   30.873  1.00 41.70  ? 455  LEU A CD2 1 
ATOM   3696 O  OXT . LEU A 1 455 ? -4.437  5.583   33.482  1.00 51.10  ? 455  LEU A OXT 1 
ATOM   3697 N  N   . THR B 1 1   ? -1.388  -25.278 99.890  1.00 76.25  ? 1    THR B N   1 
ATOM   3698 C  CA  . THR B 1 1   ? -0.368  -24.456 99.246  1.00 73.97  ? 1    THR B CA  1 
ATOM   3699 C  C   . THR B 1 1   ? -0.033  -25.007 97.859  1.00 65.46  ? 1    THR B C   1 
ATOM   3700 O  O   . THR B 1 1   ? -0.525  -24.498 96.848  1.00 63.47  ? 1    THR B O   1 
ATOM   3701 C  CB  . THR B 1 1   ? 0.913   -24.367 100.111 1.00 75.59  ? 1    THR B CB  1 
ATOM   3702 O  OG1 . THR B 1 1   ? 2.001   -23.863 99.323  1.00 74.00  ? 1    THR B OG1 1 
ATOM   3703 C  CG2 . THR B 1 1   ? 1.277   -25.732 100.693 1.00 70.68  ? 1    THR B CG2 1 
ATOM   3704 N  N   . ILE B 1 2   ? 0.798   -26.049 97.821  1.00 67.41  ? 2    ILE B N   1 
ATOM   3705 C  CA  . ILE B 1 2   ? 1.126   -26.722 96.568  1.00 61.68  ? 2    ILE B CA  1 
ATOM   3706 C  C   . ILE B 1 2   ? -0.080  -27.542 96.123  1.00 64.95  ? 2    ILE B C   1 
ATOM   3707 O  O   . ILE B 1 2   ? -0.557  -28.419 96.855  1.00 61.93  ? 2    ILE B O   1 
ATOM   3708 C  CB  . ILE B 1 2   ? 2.371   -27.604 96.732  1.00 64.62  ? 2    ILE B CB  1 
ATOM   3709 C  CG1 . ILE B 1 2   ? 3.553   -26.780 97.259  1.00 65.96  ? 2    ILE B CG1 1 
ATOM   3710 C  CG2 . ILE B 1 2   ? 2.724   -28.289 95.409  1.00 58.22  ? 2    ILE B CG2 1 
ATOM   3711 C  CD1 . ILE B 1 2   ? 3.892   -25.555 96.422  1.00 62.11  ? 2    ILE B CD1 1 
ATOM   3712 N  N   . LYS B 1 3   ? -0.587  -27.250 94.925  1.00 55.80  ? 3    LYS B N   1 
ATOM   3713 C  CA  . LYS B 1 3   ? -1.753  -27.922 94.371  1.00 58.12  ? 3    LYS B CA  1 
ATOM   3714 C  C   . LYS B 1 3   ? -1.332  -28.951 93.330  1.00 56.40  ? 3    LYS B C   1 
ATOM   3715 O  O   . LYS B 1 3   ? -0.300  -28.811 92.665  1.00 56.91  ? 3    LYS B O   1 
ATOM   3716 C  CB  . LYS B 1 3   ? -2.726  -26.922 93.728  1.00 56.96  ? 3    LYS B CB  1 
ATOM   3717 C  CG  . LYS B 1 3   ? -3.098  -25.739 94.608  1.00 60.08  ? 3    LYS B CG  1 
ATOM   3718 C  CD  . LYS B 1 3   ? -4.608  -25.526 94.654  1.00 63.78  ? 3    LYS B CD  1 
ATOM   3719 C  CE  . LYS B 1 3   ? -5.195  -25.265 93.276  1.00 62.49  ? 3    LYS B CE  1 
ATOM   3720 N  NZ  . LYS B 1 3   ? -6.648  -24.936 93.366  1.00 64.44  ? 3    LYS B NZ  1 
ATOM   3721 N  N   . GLU B 1 4   ? -2.152  -29.986 93.192  1.00 57.53  ? 4    GLU B N   1 
ATOM   3722 C  CA  . GLU B 1 4   ? -1.971  -30.979 92.147  1.00 56.42  ? 4    GLU B CA  1 
ATOM   3723 C  C   . GLU B 1 4   ? -2.741  -30.544 90.903  1.00 49.40  ? 4    GLU B C   1 
ATOM   3724 O  O   . GLU B 1 4   ? -3.924  -30.204 90.980  1.00 46.22  ? 4    GLU B O   1 
ATOM   3725 C  CB  . GLU B 1 4   ? -2.433  -32.355 92.628  1.00 59.85  ? 4    GLU B CB  1 
ATOM   3726 C  CG  . GLU B 1 4   ? -1.832  -33.521 91.859  1.00 63.87  ? 4    GLU B CG  1 
ATOM   3727 C  CD  . GLU B 1 4   ? -2.824  -34.651 91.626  1.00 73.16  ? 4    GLU B CD  1 
ATOM   3728 O  OE1 . GLU B 1 4   ? -4.018  -34.483 91.963  1.00 76.87  ? 4    GLU B OE1 1 
ATOM   3729 O  OE2 . GLU B 1 4   ? -2.407  -35.708 91.101  1.00 72.34  ? 4    GLU B OE2 1 
ATOM   3730 N  N   . MET B 1 5   ? -2.061  -30.533 89.782  1.00 49.11  ? 5    MET B N   1 
ATOM   3731 C  CA  . MET B 1 5   ? -2.572  -30.109 88.489  1.00 47.15  ? 5    MET B CA  1 
ATOM   3732 C  C   . MET B 1 5   ? -3.508  -31.162 87.904  1.00 38.88  ? 5    MET B C   1 
ATOM   3733 O  O   . MET B 1 5   ? -3.173  -32.343 87.906  1.00 37.04  ? 5    MET B O   1 
ATOM   3734 C  CB  . MET B 1 5   ? -1.411  -29.914 87.536  1.00 44.03  ? 5    MET B CB  1 
ATOM   3735 C  CG  . MET B 1 5   ? -1.543  -28.780 86.630  1.00 46.77  ? 5    MET B CG  1 
ATOM   3736 S  SD  . MET B 1 5   ? -0.071  -28.931 85.630  1.00 39.27  ? 5    MET B SD  1 
ATOM   3737 C  CE  . MET B 1 5   ? 1.094   -28.169 86.757  1.00 42.26  ? 5    MET B CE  1 
ATOM   3738 N  N   . PRO B 1 6   ? -4.661  -30.771 87.361  1.00 34.31  ? 6    PRO B N   1 
ATOM   3739 C  CA  . PRO B 1 6   ? -5.501  -31.749 86.664  1.00 36.11  ? 6    PRO B CA  1 
ATOM   3740 C  C   . PRO B 1 6   ? -4.860  -32.165 85.347  1.00 36.83  ? 6    PRO B C   1 
ATOM   3741 O  O   . PRO B 1 6   ? -3.950  -31.510 84.834  1.00 33.84  ? 6    PRO B O   1 
ATOM   3742 C  CB  . PRO B 1 6   ? -6.820  -31.002 86.431  1.00 38.79  ? 6    PRO B CB  1 
ATOM   3743 C  CG  . PRO B 1 6   ? -6.470  -29.581 86.504  1.00 38.71  ? 6    PRO B CG  1 
ATOM   3744 C  CD  . PRO B 1 6   ? -5.311  -29.453 87.454  1.00 40.08  ? 6    PRO B CD  1 
ATOM   3745 N  N   . GLN B 1 7   ? -5.358  -33.275 84.801  1.00 33.30  ? 7    GLN B N   1 
ATOM   3746 C  CA  . GLN B 1 7   ? -4.833  -33.836 83.567  1.00 33.80  ? 7    GLN B CA  1 
ATOM   3747 C  C   . GLN B 1 7   ? -5.989  -34.453 82.796  1.00 35.08  ? 7    GLN B C   1 
ATOM   3748 O  O   . GLN B 1 7   ? -6.831  -35.130 83.409  1.00 36.40  ? 7    GLN B O   1 
ATOM   3749 C  CB  . GLN B 1 7   ? -3.767  -34.893 83.866  1.00 35.46  ? 7    GLN B CB  1 
ATOM   3750 C  CG  . GLN B 1 7   ? -3.173  -35.558 82.637  1.00 31.55  ? 7    GLN B CG  1 
ATOM   3751 C  CD  . GLN B 1 7   ? -2.078  -36.551 82.991  1.00 39.44  ? 7    GLN B CD  1 
ATOM   3752 O  OE1 . GLN B 1 7   ? -1.882  -36.890 84.165  1.00 42.88  ? 7    GLN B OE1 1 
ATOM   3753 N  NE2 . GLN B 1 7   ? -1.348  -37.013 81.976  1.00 34.97  ? 7    GLN B NE2 1 
ATOM   3754 N  N   . PRO B 1 8   ? -6.074  -34.235 81.480  1.00 32.49  ? 8    PRO B N   1 
ATOM   3755 C  CA  . PRO B 1 8   ? -7.160  -34.848 80.703  1.00 31.36  ? 8    PRO B CA  1 
ATOM   3756 C  C   . PRO B 1 8   ? -6.981  -36.346 80.533  1.00 32.00  ? 8    PRO B C   1 
ATOM   3757 O  O   . PRO B 1 8   ? -5.988  -36.914 80.989  1.00 33.43  ? 8    PRO B O   1 
ATOM   3758 C  CB  . PRO B 1 8   ? -7.090  -34.114 79.358  1.00 31.39  ? 8    PRO B CB  1 
ATOM   3759 C  CG  . PRO B 1 8   ? -5.628  -33.682 79.244  1.00 31.21  ? 8    PRO B CG  1 
ATOM   3760 C  CD  . PRO B 1 8   ? -5.226  -33.343 80.658  1.00 33.53  ? 8    PRO B CD  1 
ATOM   3761 N  N   . LYS B 1 9   ? -7.941  -36.989 79.874  1.00 32.37  ? 9    LYS B N   1 
ATOM   3762 C  CA  . LYS B 1 9   ? -7.997  -38.443 79.828  1.00 30.95  ? 9    LYS B CA  1 
ATOM   3763 C  C   . LYS B 1 9   ? -6.799  -39.034 79.097  1.00 32.72  ? 9    LYS B C   1 
ATOM   3764 O  O   . LYS B 1 9   ? -6.262  -38.448 78.149  1.00 32.14  ? 9    LYS B O   1 
ATOM   3765 C  CB  . LYS B 1 9   ? -9.288  -38.903 79.152  1.00 30.94  ? 9    LYS B CB  1 
ATOM   3766 C  CG  . LYS B 1 9   ? -9.415  -38.504 77.691  1.00 32.54  ? 9    LYS B CG  1 
ATOM   3767 C  CD  . LYS B 1 9   ? -10.811 -38.824 77.153  1.00 34.94  ? 9    LYS B CD  1 
ATOM   3768 C  CE  . LYS B 1 9   ? -11.000 -38.229 75.759  1.00 41.47  ? 9    LYS B CE  1 
ATOM   3769 N  NZ  . LYS B 1 9   ? -12.405 -38.371 75.276  1.00 41.28  ? 9    LYS B NZ  1 
ATOM   3770 N  N   . THR B 1 10  ? -6.413  -40.238 79.521  1.00 34.33  ? 10   THR B N   1 
ATOM   3771 C  CA  . THR B 1 10  ? -5.211  -40.911 79.056  1.00 30.34  ? 10   THR B CA  1 
ATOM   3772 C  C   . THR B 1 10  ? -5.549  -42.163 78.256  1.00 33.81  ? 10   THR B C   1 
ATOM   3773 O  O   . THR B 1 10  ? -6.659  -42.694 78.327  1.00 31.49  ? 10   THR B O   1 
ATOM   3774 C  CB  . THR B 1 10  ? -4.314  -41.299 80.239  1.00 35.88  ? 10   THR B CB  1 
ATOM   3775 O  OG1 . THR B 1 10  ? -5.074  -42.076 81.183  1.00 34.08  ? 10   THR B OG1 1 
ATOM   3776 C  CG2 . THR B 1 10  ? -3.778  -40.053 80.927  1.00 35.81  ? 10   THR B CG2 1 
ATOM   3777 N  N   . PHE B 1 11  ? -4.537  -42.639 77.524  1.00 30.55  ? 11   PHE B N   1 
ATOM   3778 C  CA  . PHE B 1 11  ? -4.636  -43.721 76.551  1.00 32.27  ? 11   PHE B CA  1 
ATOM   3779 C  C   . PHE B 1 11  ? -3.493  -44.716 76.792  1.00 35.09  ? 11   PHE B C   1 
ATOM   3780 O  O   . PHE B 1 11  ? -2.681  -44.988 75.912  1.00 35.46  ? 11   PHE B O   1 
ATOM   3781 C  CB  . PHE B 1 11  ? -4.575  -43.180 75.118  1.00 34.06  ? 11   PHE B CB  1 
ATOM   3782 C  CG  . PHE B 1 11  ? -5.719  -42.277 74.746  1.00 31.10  ? 11   PHE B CG  1 
ATOM   3783 C  CD1 . PHE B 1 11  ? -5.768  -40.964 75.208  1.00 29.08  ? 11   PHE B CD1 1 
ATOM   3784 C  CD2 . PHE B 1 11  ? -6.748  -42.734 73.923  1.00 31.64  ? 11   PHE B CD2 1 
ATOM   3785 C  CE1 . PHE B 1 11  ? -6.832  -40.126 74.865  1.00 31.82  ? 11   PHE B CE1 1 
ATOM   3786 C  CE2 . PHE B 1 11  ? -7.802  -41.906 73.577  1.00 33.27  ? 11   PHE B CE2 1 
ATOM   3787 C  CZ  . PHE B 1 11  ? -7.841  -40.594 74.047  1.00 30.51  ? 11   PHE B CZ  1 
ATOM   3788 N  N   . GLY B 1 12  ? -3.420  -45.242 78.009  1.00 33.08  ? 12   GLY B N   1 
ATOM   3789 C  CA  . GLY B 1 12  ? -2.361  -46.190 78.320  1.00 36.11  ? 12   GLY B CA  1 
ATOM   3790 C  C   . GLY B 1 12  ? -0.989  -45.566 78.145  1.00 37.90  ? 12   GLY B C   1 
ATOM   3791 O  O   . GLY B 1 12  ? -0.741  -44.414 78.527  1.00 34.48  ? 12   GLY B O   1 
ATOM   3792 N  N   . GLU B 1 13  ? -0.082  -46.335 77.544  1.00 36.42  ? 13   GLU B N   1 
ATOM   3793 C  CA  . GLU B 1 13  ? 1.284   -45.852 77.364  1.00 40.29  ? 13   GLU B CA  1 
ATOM   3794 C  C   . GLU B 1 13  ? 1.373   -44.648 76.427  1.00 40.38  ? 13   GLU B C   1 
ATOM   3795 O  O   . GLU B 1 13  ? 2.402   -43.962 76.427  1.00 41.29  ? 13   GLU B O   1 
ATOM   3796 C  CB  . GLU B 1 13  ? 2.166   -46.994 76.861  1.00 43.41  ? 13   GLU B CB  1 
ATOM   3797 C  CG  . GLU B 1 13  ? 2.433   -48.066 77.926  1.00 50.74  ? 13   GLU B CG  1 
ATOM   3798 C  CD  . GLU B 1 13  ? 2.759   -47.473 79.290  1.00 58.87  ? 13   GLU B CD  1 
ATOM   3799 O  OE1 . GLU B 1 13  ? 3.932   -47.096 79.510  1.00 64.19  ? 13   GLU B OE1 1 
ATOM   3800 O  OE2 . GLU B 1 13  ? 1.849   -47.392 80.147  1.00 63.13  ? 13   GLU B OE2 1 
ATOM   3801 N  N   . LEU B 1 14  ? 0.335   -44.366 75.637  1.00 37.30  ? 14   LEU B N   1 
ATOM   3802 C  CA  . LEU B 1 14  ? 0.351   -43.153 74.820  1.00 33.96  ? 14   LEU B CA  1 
ATOM   3803 C  C   . LEU B 1 14  ? 0.008   -41.899 75.621  1.00 37.79  ? 14   LEU B C   1 
ATOM   3804 O  O   . LEU B 1 14  ? 0.125   -40.792 75.085  1.00 36.15  ? 14   LEU B O   1 
ATOM   3805 C  CB  . LEU B 1 14  ? -0.600  -43.298 73.630  1.00 36.14  ? 14   LEU B CB  1 
ATOM   3806 C  CG  . LEU B 1 14  ? -0.222  -44.408 72.649  1.00 42.97  ? 14   LEU B CG  1 
ATOM   3807 C  CD1 . LEU B 1 14  ? -1.266  -44.580 71.549  1.00 41.50  ? 14   LEU B CD1 1 
ATOM   3808 C  CD2 . LEU B 1 14  ? 1.153   -44.140 72.056  1.00 45.69  ? 14   LEU B CD2 1 
ATOM   3809 N  N   . LYS B 1 15  ? -0.379  -42.051 76.887  1.00 34.90  ? 15   LYS B N   1 
ATOM   3810 C  CA  . LYS B 1 15  ? -0.684  -40.944 77.785  1.00 33.87  ? 15   LYS B CA  1 
ATOM   3811 C  C   . LYS B 1 15  ? -1.736  -40.041 77.140  1.00 34.86  ? 15   LYS B C   1 
ATOM   3812 O  O   . LYS B 1 15  ? -2.805  -40.533 76.768  1.00 33.60  ? 15   LYS B O   1 
ATOM   3813 C  CB  . LYS B 1 15  ? 0.610   -40.222 78.167  1.00 35.18  ? 15   LYS B CB  1 
ATOM   3814 C  CG  . LYS B 1 15  ? 1.581   -41.242 78.819  1.00 39.99  ? 15   LYS B CG  1 
ATOM   3815 C  CD  . LYS B 1 15  ? 2.910   -40.657 79.235  1.00 45.82  ? 15   LYS B CD  1 
ATOM   3816 C  CE  . LYS B 1 15  ? 3.724   -41.702 79.991  1.00 48.18  ? 15   LYS B CE  1 
ATOM   3817 N  NZ  . LYS B 1 15  ? 5.054   -41.198 80.422  1.00 52.58  ? 15   LYS B NZ  1 
ATOM   3818 N  N   . ASN B 1 16  ? -1.470  -38.745 76.973  1.00 31.48  ? 16   ASN B N   1 
ATOM   3819 C  CA  . ASN B 1 16  ? -2.479  -37.872 76.370  1.00 31.66  ? 16   ASN B CA  1 
ATOM   3820 C  C   . ASN B 1 16  ? -2.320  -37.689 74.865  1.00 34.35  ? 16   ASN B C   1 
ATOM   3821 O  O   . ASN B 1 16  ? -3.127  -36.975 74.261  1.00 32.47  ? 16   ASN B O   1 
ATOM   3822 C  CB  . ASN B 1 16  ? -2.473  -36.490 77.034  1.00 30.93  ? 16   ASN B CB  1 
ATOM   3823 C  CG  . ASN B 1 16  ? -2.754  -36.551 78.531  1.00 34.18  ? 16   ASN B CG  1 
ATOM   3824 O  OD1 . ASN B 1 16  ? -1.908  -36.187 79.346  1.00 33.19  ? 16   ASN B OD1 1 
ATOM   3825 N  ND2 . ASN B 1 16  ? -3.957  -37.008 78.894  1.00 31.87  ? 16   ASN B ND2 1 
ATOM   3826 N  N   . LEU B 1 17  ? -1.309  -38.286 74.239  1.00 34.05  ? 17   LEU B N   1 
ATOM   3827 C  CA  . LEU B 1 17  ? -1.035  -37.964 72.840  1.00 33.33  ? 17   LEU B CA  1 
ATOM   3828 C  C   . LEU B 1 17  ? -2.238  -38.133 71.917  1.00 35.91  ? 17   LEU B C   1 
ATOM   3829 O  O   . LEU B 1 17  ? -2.420  -37.286 71.025  1.00 35.07  ? 17   LEU B O   1 
ATOM   3830 C  CB  . LEU B 1 17  ? 0.145   -38.809 72.342  1.00 36.50  ? 17   LEU B CB  1 
ATOM   3831 C  CG  . LEU B 1 17  ? 0.640   -38.458 70.939  1.00 39.18  ? 17   LEU B CG  1 
ATOM   3832 C  CD1 . LEU B 1 17  ? 1.155   -37.040 70.918  1.00 40.69  ? 17   LEU B CD1 1 
ATOM   3833 C  CD2 . LEU B 1 17  ? 1.747   -39.421 70.554  1.00 39.25  ? 17   LEU B CD2 1 
ATOM   3834 N  N   . PRO B 1 18  ? -3.075  -39.164 72.051  1.00 33.35  ? 18   PRO B N   1 
ATOM   3835 C  CA  . PRO B 1 18  ? -4.193  -39.319 71.110  1.00 31.46  ? 18   PRO B CA  1 
ATOM   3836 C  C   . PRO B 1 18  ? -5.213  -38.186 71.159  1.00 31.07  ? 18   PRO B C   1 
ATOM   3837 O  O   . PRO B 1 18  ? -6.038  -38.086 70.244  1.00 31.71  ? 18   PRO B O   1 
ATOM   3838 C  CB  . PRO B 1 18  ? -4.817  -40.654 71.527  1.00 32.78  ? 18   PRO B CB  1 
ATOM   3839 C  CG  . PRO B 1 18  ? -3.633  -41.413 72.130  1.00 36.92  ? 18   PRO B CG  1 
ATOM   3840 C  CD  . PRO B 1 18  ? -2.900  -40.360 72.898  1.00 35.26  ? 18   PRO B CD  1 
ATOM   3841 N  N   . LEU B 1 19  ? -5.195  -37.355 72.197  1.00 31.56  ? 19   LEU B N   1 
ATOM   3842 C  CA  . LEU B 1 19  ? -6.070  -36.188 72.214  1.00 32.34  ? 19   LEU B CA  1 
ATOM   3843 C  C   . LEU B 1 19  ? -5.754  -35.237 71.076  1.00 34.66  ? 19   LEU B C   1 
ATOM   3844 O  O   . LEU B 1 19  ? -6.613  -34.438 70.690  1.00 33.85  ? 19   LEU B O   1 
ATOM   3845 C  CB  . LEU B 1 19  ? -5.944  -35.458 73.550  1.00 32.60  ? 19   LEU B CB  1 
ATOM   3846 C  CG  . LEU B 1 19  ? -6.447  -36.278 74.734  1.00 30.74  ? 19   LEU B CG  1 
ATOM   3847 C  CD1 . LEU B 1 19  ? -6.232  -35.563 76.029  1.00 32.78  ? 19   LEU B CD1 1 
ATOM   3848 C  CD2 . LEU B 1 19  ? -7.921  -36.599 74.527  1.00 31.58  ? 19   LEU B CD2 1 
ATOM   3849 N  N   . LEU B 1 20  ? -4.540  -35.304 70.538  1.00 33.42  ? 20   LEU B N   1 
ATOM   3850 C  CA  . LEU B 1 20  ? -4.150  -34.481 69.400  1.00 33.20  ? 20   LEU B CA  1 
ATOM   3851 C  C   . LEU B 1 20  ? -4.444  -35.142 68.069  1.00 32.82  ? 20   LEU B C   1 
ATOM   3852 O  O   . LEU B 1 20  ? -4.153  -34.549 67.024  1.00 33.70  ? 20   LEU B O   1 
ATOM   3853 C  CB  . LEU B 1 20  ? -2.655  -34.155 69.482  1.00 31.91  ? 20   LEU B CB  1 
ATOM   3854 C  CG  . LEU B 1 20  ? -2.203  -33.472 70.761  1.00 34.90  ? 20   LEU B CG  1 
ATOM   3855 C  CD1 . LEU B 1 20  ? -0.683  -33.276 70.724  1.00 38.67  ? 20   LEU B CD1 1 
ATOM   3856 C  CD2 . LEU B 1 20  ? -2.929  -32.164 70.959  1.00 39.03  ? 20   LEU B CD2 1 
ATOM   3857 N  N   . ASN B 1 21  ? -4.989  -36.363 68.071  1.00 33.90  ? 21   ASN B N   1 
ATOM   3858 C  CA  . ASN B 1 21  ? -5.302  -37.056 66.822  1.00 32.46  ? 21   ASN B CA  1 
ATOM   3859 C  C   . ASN B 1 21  ? -6.657  -36.567 66.316  1.00 38.30  ? 21   ASN B C   1 
ATOM   3860 O  O   . ASN B 1 21  ? -7.685  -37.242 66.405  1.00 35.30  ? 21   ASN B O   1 
ATOM   3861 C  CB  . ASN B 1 21  ? -5.290  -38.566 67.015  1.00 34.99  ? 21   ASN B CB  1 
ATOM   3862 C  CG  . ASN B 1 21  ? -5.500  -39.323 65.708  1.00 45.87  ? 21   ASN B CG  1 
ATOM   3863 O  OD1 . ASN B 1 21  ? -5.565  -38.729 64.625  1.00 43.38  ? 21   ASN B OD1 1 
ATOM   3864 N  ND2 . ASN B 1 21  ? -5.589  -40.638 65.803  1.00 46.85  ? 21   ASN B ND2 1 
ATOM   3865 N  N   . THR B 1 22  ? -6.635  -35.344 65.794  1.00 32.79  ? 22   THR B N   1 
ATOM   3866 C  CA  . THR B 1 22  ? -7.826  -34.666 65.314  1.00 35.47  ? 22   THR B CA  1 
ATOM   3867 C  C   . THR B 1 22  ? -7.378  -33.585 64.347  1.00 33.41  ? 22   THR B C   1 
ATOM   3868 O  O   . THR B 1 22  ? -6.245  -33.106 64.429  1.00 33.50  ? 22   THR B O   1 
ATOM   3869 C  CB  . THR B 1 22  ? -8.630  -34.043 66.459  1.00 39.08  ? 22   THR B CB  1 
ATOM   3870 O  OG1 . THR B 1 22  ? -9.621  -33.163 65.909  1.00 40.90  ? 22   THR B OG1 1 
ATOM   3871 C  CG2 . THR B 1 22  ? -7.713  -33.233 67.422  1.00 34.13  ? 22   THR B CG2 1 
ATOM   3872 N  N   . ASP B 1 23  ? -8.265  -33.206 63.423  1.00 34.62  ? 23   ASP B N   1 
ATOM   3873 C  CA  . ASP B 1 23  ? -7.883  -32.113 62.540  1.00 39.78  ? 23   ASP B CA  1 
ATOM   3874 C  C   . ASP B 1 23  ? -7.979  -30.757 63.222  1.00 33.46  ? 23   ASP B C   1 
ATOM   3875 O  O   . ASP B 1 23  ? -7.578  -29.758 62.614  1.00 31.63  ? 23   ASP B O   1 
ATOM   3876 C  CB  . ASP B 1 23  ? -8.740  -32.085 61.268  1.00 39.49  ? 23   ASP B CB  1 
ATOM   3877 C  CG  . ASP B 1 23  ? -10.224 -32.106 61.559  1.00 43.15  ? 23   ASP B CG  1 
ATOM   3878 O  OD1 . ASP B 1 23  ? -10.610 -32.124 62.746  1.00 46.99  ? 23   ASP B OD1 1 
ATOM   3879 O  OD2 . ASP B 1 23  ? -11.014 -32.088 60.589  1.00 58.38  ? 23   ASP B OD2 1 
ATOM   3880 N  N   . LYS B 1 24  ? -8.491  -30.700 64.452  1.00 33.54  ? 24   LYS B N   1 
ATOM   3881 C  CA  . LYS B 1 24  ? -8.714  -29.437 65.160  1.00 30.98  ? 24   LYS B CA  1 
ATOM   3882 C  C   . LYS B 1 24  ? -8.149  -29.522 66.571  1.00 29.56  ? 24   LYS B C   1 
ATOM   3883 O  O   . LYS B 1 24  ? -8.884  -29.439 67.564  1.00 32.71  ? 24   LYS B O   1 
ATOM   3884 C  CB  . LYS B 1 24  ? -10.206 -29.097 65.172  1.00 32.11  ? 24   LYS B CB  1 
ATOM   3885 C  CG  . LYS B 1 24  ? -10.723 -28.756 63.764  1.00 31.10  ? 24   LYS B CG  1 
ATOM   3886 C  CD  . LYS B 1 24  ? -12.249 -28.604 63.719  1.00 35.72  ? 24   LYS B CD  1 
ATOM   3887 C  CE  . LYS B 1 24  ? -12.715 -28.119 62.343  1.00 35.88  ? 24   LYS B CE  1 
ATOM   3888 N  NZ  . LYS B 1 24  ? -14.190 -27.849 62.323  1.00 37.47  ? 24   LYS B NZ  1 
ATOM   3889 N  N   . PRO B 1 25  ? -6.823  -29.660 66.693  1.00 28.65  ? 25   PRO B N   1 
ATOM   3890 C  CA  . PRO B 1 25  ? -6.235  -29.890 68.021  1.00 28.66  ? 25   PRO B CA  1 
ATOM   3891 C  C   . PRO B 1 25  ? -6.284  -28.686 68.948  1.00 30.71  ? 25   PRO B C   1 
ATOM   3892 O  O   . PRO B 1 25  ? -6.479  -28.856 70.155  1.00 28.85  ? 25   PRO B O   1 
ATOM   3893 C  CB  . PRO B 1 25  ? -4.792  -30.296 67.695  1.00 27.81  ? 25   PRO B CB  1 
ATOM   3894 C  CG  . PRO B 1 25  ? -4.525  -29.687 66.333  1.00 31.21  ? 25   PRO B CG  1 
ATOM   3895 C  CD  . PRO B 1 25  ? -5.836  -29.798 65.604  1.00 30.88  ? 25   PRO B CD  1 
ATOM   3896 N  N   . VAL B 1 26  ? -6.100  -27.467 68.438  1.00 29.53  ? 26   VAL B N   1 
ATOM   3897 C  CA  . VAL B 1 26  ? -6.181  -26.316 69.335  1.00 27.44  ? 26   VAL B CA  1 
ATOM   3898 C  C   . VAL B 1 26  ? -7.584  -26.202 69.895  1.00 28.40  ? 26   VAL B C   1 
ATOM   3899 O  O   . VAL B 1 26  ? -7.771  -25.971 71.090  1.00 29.61  ? 26   VAL B O   1 
ATOM   3900 C  CB  . VAL B 1 26  ? -5.755  -25.019 68.619  1.00 29.44  ? 26   VAL B CB  1 
ATOM   3901 C  CG1 . VAL B 1 26  ? -6.092  -23.820 69.512  1.00 30.17  ? 26   VAL B CG1 1 
ATOM   3902 C  CG2 . VAL B 1 26  ? -4.248  -25.084 68.284  1.00 31.72  ? 26   VAL B CG2 1 
ATOM   3903 N  N   . GLN B 1 27  ? -8.593  -26.404 69.050  1.00 30.59  ? 27   GLN B N   1 
ATOM   3904 C  CA  . GLN B 1 27  ? -9.963  -26.326 69.543  1.00 30.50  ? 27   GLN B CA  1 
ATOM   3905 C  C   . GLN B 1 27  ? -10.263 -27.430 70.542  1.00 31.66  ? 27   GLN B C   1 
ATOM   3906 O  O   . GLN B 1 27  ? -11.019 -27.210 71.500  1.00 29.03  ? 27   GLN B O   1 
ATOM   3907 C  CB  . GLN B 1 27  ? -10.936 -26.359 68.369  1.00 30.64  ? 27   GLN B CB  1 
ATOM   3908 C  CG  . GLN B 1 27  ? -10.868 -25.057 67.562  1.00 31.67  ? 27   GLN B CG  1 
ATOM   3909 C  CD  . GLN B 1 27  ? -11.466 -25.172 66.164  1.00 29.20  ? 27   GLN B CD  1 
ATOM   3910 O  OE1 . GLN B 1 27  ? -12.675 -24.966 65.967  1.00 32.09  ? 27   GLN B OE1 1 
ATOM   3911 N  NE2 . GLN B 1 27  ? -10.623 -25.481 65.185  1.00 30.39  ? 27   GLN B NE2 1 
ATOM   3912 N  N   . ALA B 1 28  ? -9.672  -28.615 70.346  1.00 33.77  ? 28   ALA B N   1 
ATOM   3913 C  CA  . ALA B 1 28  ? -9.788  -29.673 71.348  1.00 31.57  ? 28   ALA B CA  1 
ATOM   3914 C  C   . ALA B 1 28  ? -9.169  -29.245 72.673  1.00 34.16  ? 28   ALA B C   1 
ATOM   3915 O  O   . ALA B 1 28  ? -9.755  -29.459 73.742  1.00 32.37  ? 28   ALA B O   1 
ATOM   3916 C  CB  . ALA B 1 28  ? -9.126  -30.956 70.825  1.00 30.36  ? 28   ALA B CB  1 
ATOM   3917 N  N   . LEU B 1 29  ? -7.983  -28.626 72.627  1.00 30.35  ? 29   LEU B N   1 
ATOM   3918 C  CA  . LEU B 1 29  ? -7.343  -28.180 73.858  1.00 27.28  ? 29   LEU B CA  1 
ATOM   3919 C  C   . LEU B 1 29  ? -8.145  -27.076 74.543  1.00 31.29  ? 29   LEU B C   1 
ATOM   3920 O  O   . LEU B 1 29  ? -8.162  -27.000 75.775  1.00 31.12  ? 29   LEU B O   1 
ATOM   3921 C  CB  . LEU B 1 29  ? -5.922  -27.714 73.545  1.00 30.43  ? 29   LEU B CB  1 
ATOM   3922 C  CG  . LEU B 1 29  ? -4.955  -28.833 73.157  1.00 31.78  ? 29   LEU B CG  1 
ATOM   3923 C  CD1 . LEU B 1 29  ? -3.722  -28.276 72.417  1.00 31.37  ? 29   LEU B CD1 1 
ATOM   3924 C  CD2 . LEU B 1 29  ? -4.511  -29.598 74.391  1.00 31.94  ? 29   LEU B CD2 1 
ATOM   3925 N  N   . MET B 1 30  ? -8.790  -26.203 73.762  1.00 29.87  ? 30   MET B N   1 
ATOM   3926 C  CA  . MET B 1 30  ? -9.696  -25.209 74.339  1.00 30.90  ? 30   MET B CA  1 
ATOM   3927 C  C   . MET B 1 30  ? -10.820 -25.863 75.127  1.00 32.40  ? 30   MET B C   1 
ATOM   3928 O  O   . MET B 1 30  ? -11.125 -25.435 76.240  1.00 33.44  ? 30   MET B O   1 
ATOM   3929 C  CB  . MET B 1 30  ? -10.248 -24.321 73.229  1.00 30.57  ? 30   MET B CB  1 
ATOM   3930 C  CG  . MET B 1 30  ? -9.156  -23.541 72.503  1.00 31.39  ? 30   MET B CG  1 
ATOM   3931 S  SD  . MET B 1 30  ? -9.821  -22.497 71.193  1.00 33.32  ? 30   MET B SD  1 
ATOM   3932 C  CE  . MET B 1 30  ? -11.092 -21.541 72.033  1.00 31.22  ? 30   MET B CE  1 
ATOM   3933 N  N   . LYS B 1 31  ? -11.449 -26.902 74.561  1.00 34.56  ? 31   LYS B N   1 
ATOM   3934 C  CA  . LYS B 1 31  ? -12.509 -27.605 75.288  1.00 32.05  ? 31   LYS B CA  1 
ATOM   3935 C  C   . LYS B 1 31  ? -11.966 -28.269 76.548  1.00 31.76  ? 31   LYS B C   1 
ATOM   3936 O  O   . LYS B 1 31  ? -12.623 -28.269 77.596  1.00 31.41  ? 31   LYS B O   1 
ATOM   3937 C  CB  . LYS B 1 31  ? -13.168 -28.638 74.375  1.00 34.21  ? 31   LYS B CB  1 
ATOM   3938 C  CG  . LYS B 1 31  ? -14.282 -28.044 73.529  1.00 47.23  ? 31   LYS B CG  1 
ATOM   3939 C  CD  . LYS B 1 31  ? -14.703 -28.978 72.400  1.00 52.08  ? 31   LYS B CD  1 
ATOM   3940 C  CE  . LYS B 1 31  ? -15.046 -28.193 71.137  1.00 55.03  ? 31   LYS B CE  1 
ATOM   3941 N  NZ  . LYS B 1 31  ? -16.396 -27.560 71.249  1.00 67.39  ? 31   LYS B NZ  1 
ATOM   3942 N  N   . ILE B 1 32  ? -10.753 -28.823 76.481  1.00 32.73  ? 32   ILE B N   1 
ATOM   3943 C  CA  . ILE B 1 32  ? -10.168 -29.405 77.682  1.00 29.67  ? 32   ILE B CA  1 
ATOM   3944 C  C   . ILE B 1 32  ? -9.948  -28.325 78.735  1.00 31.61  ? 32   ILE B C   1 
ATOM   3945 O  O   . ILE B 1 32  ? -10.263 -28.514 79.916  1.00 33.21  ? 32   ILE B O   1 
ATOM   3946 C  CB  . ILE B 1 32  ? -8.862  -30.149 77.337  1.00 31.71  ? 32   ILE B CB  1 
ATOM   3947 C  CG1 . ILE B 1 32  ? -9.177  -31.362 76.463  1.00 33.36  ? 32   ILE B CG1 1 
ATOM   3948 C  CG2 . ILE B 1 32  ? -8.092  -30.544 78.613  1.00 28.91  ? 32   ILE B CG2 1 
ATOM   3949 C  CD1 . ILE B 1 32  ? -7.950  -31.941 75.779  1.00 35.22  ? 32   ILE B CD1 1 
ATOM   3950 N  N   . ALA B 1 33  ? -9.439  -27.161 78.319  1.00 30.67  ? 33   ALA B N   1 
ATOM   3951 C  CA  . ALA B 1 33  ? -9.232  -26.064 79.261  1.00 31.09  ? 33   ALA B CA  1 
ATOM   3952 C  C   . ALA B 1 33  ? -10.556 -25.621 79.876  1.00 31.60  ? 33   ALA B C   1 
ATOM   3953 O  O   . ALA B 1 33  ? -10.621 -25.283 81.066  1.00 32.61  ? 33   ALA B O   1 
ATOM   3954 C  CB  . ALA B 1 33  ? -8.546  -24.886 78.558  1.00 31.95  ? 33   ALA B CB  1 
ATOM   3955 N  N   . ASP B 1 34  ? -11.620 -25.612 79.081  1.00 32.63  ? 34   ASP B N   1 
ATOM   3956 C  CA  . ASP B 1 34  ? -12.920 -25.252 79.636  1.00 34.53  ? 34   ASP B CA  1 
ATOM   3957 C  C   . ASP B 1 34  ? -13.332 -26.228 80.728  1.00 37.75  ? 34   ASP B C   1 
ATOM   3958 O  O   . ASP B 1 34  ? -13.930 -25.827 81.734  1.00 38.71  ? 34   ASP B O   1 
ATOM   3959 C  CB  . ASP B 1 34  ? -13.969 -25.207 78.530  1.00 36.61  ? 34   ASP B CB  1 
ATOM   3960 C  CG  . ASP B 1 34  ? -13.949 -23.900 77.772  1.00 40.97  ? 34   ASP B CG  1 
ATOM   3961 O  OD1 . ASP B 1 34  ? -13.350 -22.930 78.279  1.00 42.57  ? 34   ASP B OD1 1 
ATOM   3962 O  OD2 . ASP B 1 34  ? -14.550 -23.839 76.684  1.00 44.62  ? 34   ASP B OD2 1 
ATOM   3963 N  N   . GLU B 1 35  ? -13.000 -27.507 80.560  1.00 34.70  ? 35   GLU B N   1 
ATOM   3964 C  CA  . GLU B 1 35  ? -13.339 -28.522 81.556  1.00 33.54  ? 35   GLU B CA  1 
ATOM   3965 C  C   . GLU B 1 35  ? -12.439 -28.445 82.780  1.00 36.03  ? 35   GLU B C   1 
ATOM   3966 O  O   . GLU B 1 35  ? -12.915 -28.563 83.914  1.00 38.29  ? 35   GLU B O   1 
ATOM   3967 C  CB  . GLU B 1 35  ? -13.235 -29.921 80.942  1.00 37.40  ? 35   GLU B CB  1 
ATOM   3968 C  CG  . GLU B 1 35  ? -14.315 -30.255 79.925  1.00 45.74  ? 35   GLU B CG  1 
ATOM   3969 C  CD  . GLU B 1 35  ? -14.429 -31.754 79.639  1.00 54.45  ? 35   GLU B CD  1 
ATOM   3970 O  OE1 . GLU B 1 35  ? -15.489 -32.179 79.125  1.00 56.23  ? 35   GLU B OE1 1 
ATOM   3971 O  OE2 . GLU B 1 35  ? -13.464 -32.499 79.926  1.00 50.31  ? 35   GLU B OE2 1 
ATOM   3972 N  N   . LEU B 1 36  ? -11.135 -28.264 82.573  1.00 33.45  ? 36   LEU B N   1 
ATOM   3973 C  CA  . LEU B 1 36  ? -10.171 -28.471 83.638  1.00 33.35  ? 36   LEU B CA  1 
ATOM   3974 C  C   . LEU B 1 36  ? -9.721  -27.190 84.316  1.00 31.50  ? 36   LEU B C   1 
ATOM   3975 O  O   . LEU B 1 36  ? -9.231  -27.255 85.450  1.00 34.12  ? 36   LEU B O   1 
ATOM   3976 C  CB  . LEU B 1 36  ? -8.935  -29.202 83.098  1.00 31.55  ? 36   LEU B CB  1 
ATOM   3977 C  CG  . LEU B 1 36  ? -9.231  -30.609 82.596  1.00 32.72  ? 36   LEU B CG  1 
ATOM   3978 C  CD1 . LEU B 1 36  ? -7.921  -31.340 82.231  1.00 32.82  ? 36   LEU B CD1 1 
ATOM   3979 C  CD2 . LEU B 1 36  ? -9.995  -31.398 83.650  1.00 37.11  ? 36   LEU B CD2 1 
ATOM   3980 N  N   . GLY B 1 37  ? -9.833  -26.050 83.655  1.00 30.39  ? 37   GLY B N   1 
ATOM   3981 C  CA  . GLY B 1 37  ? -9.503  -24.779 84.287  1.00 33.07  ? 37   GLY B CA  1 
ATOM   3982 C  C   . GLY B 1 37  ? -8.190  -24.188 83.795  1.00 33.00  ? 37   GLY B C   1 
ATOM   3983 O  O   . GLY B 1 37  ? -7.716  -24.466 82.693  1.00 32.92  ? 37   GLY B O   1 
ATOM   3984 N  N   . GLU B 1 38  ? -7.595  -23.350 84.650  1.00 31.86  ? 38   GLU B N   1 
ATOM   3985 C  CA  . GLU B 1 38  ? -6.525  -22.451 84.226  1.00 33.74  ? 38   GLU B CA  1 
ATOM   3986 C  C   . GLU B 1 38  ? -5.214  -23.157 83.929  1.00 34.82  ? 38   GLU B C   1 
ATOM   3987 O  O   . GLU B 1 38  ? -4.331  -22.534 83.321  1.00 30.76  ? 38   GLU B O   1 
ATOM   3988 C  CB  . GLU B 1 38  ? -6.293  -21.377 85.291  1.00 33.77  ? 38   GLU B CB  1 
ATOM   3989 C  CG  . GLU B 1 38  ? -5.767  -21.942 86.584  1.00 35.50  ? 38   GLU B CG  1 
ATOM   3990 C  CD  . GLU B 1 38  ? -5.530  -20.892 87.657  1.00 41.35  ? 38   GLU B CD  1 
ATOM   3991 O  OE1 . GLU B 1 38  ? -5.445  -19.682 87.338  1.00 35.24  ? 38   GLU B OE1 1 
ATOM   3992 O  OE2 . GLU B 1 38  ? -5.426  -21.296 88.836  1.00 39.57  ? 38   GLU B OE2 1 
ATOM   3993 N  N   . ILE B 1 39  ? -5.049  -24.412 84.338  1.00 33.59  ? 39   ILE B N   1 
ATOM   3994 C  CA  . ILE B 1 39  ? -3.792  -25.128 84.123  1.00 30.30  ? 39   ILE B CA  1 
ATOM   3995 C  C   . ILE B 1 39  ? -4.085  -26.621 84.072  1.00 34.49  ? 39   ILE B C   1 
ATOM   3996 O  O   . ILE B 1 39  ? -4.840  -27.144 84.895  1.00 34.35  ? 39   ILE B O   1 
ATOM   3997 C  CB  . ILE B 1 39  ? -2.750  -24.805 85.215  1.00 32.47  ? 39   ILE B CB  1 
ATOM   3998 C  CG1 . ILE B 1 39  ? -1.402  -25.475 84.901  1.00 32.31  ? 39   ILE B CG1 1 
ATOM   3999 C  CG2 . ILE B 1 39  ? -3.261  -25.187 86.620  1.00 31.49  ? 39   ILE B CG2 1 
ATOM   4000 C  CD1 . ILE B 1 39  ? -0.240  -24.921 85.750  1.00 36.32  ? 39   ILE B CD1 1 
ATOM   4001 N  N   . PHE B 1 40  ? -3.514  -27.311 83.092  1.00 31.57  ? 40   PHE B N   1 
ATOM   4002 C  CA  . PHE B 1 40  ? -3.576  -28.767 83.107  1.00 31.24  ? 40   PHE B CA  1 
ATOM   4003 C  C   . PHE B 1 40  ? -2.282  -29.334 82.550  1.00 33.74  ? 40   PHE B C   1 
ATOM   4004 O  O   . PHE B 1 40  ? -1.612  -28.716 81.721  1.00 32.99  ? 40   PHE B O   1 
ATOM   4005 C  CB  . PHE B 1 40  ? -4.809  -29.335 82.361  1.00 32.58  ? 40   PHE B CB  1 
ATOM   4006 C  CG  . PHE B 1 40  ? -4.879  -29.001 80.889  1.00 31.80  ? 40   PHE B CG  1 
ATOM   4007 C  CD1 . PHE B 1 40  ? -4.288  -29.819 79.934  1.00 29.78  ? 40   PHE B CD1 1 
ATOM   4008 C  CD2 . PHE B 1 40  ? -5.609  -27.891 80.458  1.00 31.92  ? 40   PHE B CD2 1 
ATOM   4009 C  CE1 . PHE B 1 40  ? -4.388  -29.505 78.574  1.00 30.39  ? 40   PHE B CE1 1 
ATOM   4010 C  CE2 . PHE B 1 40  ? -5.714  -27.584 79.115  1.00 31.23  ? 40   PHE B CE2 1 
ATOM   4011 C  CZ  . PHE B 1 40  ? -5.109  -28.391 78.167  1.00 30.44  ? 40   PHE B CZ  1 
ATOM   4012 N  N   . LYS B 1 41  ? -1.922  -30.503 83.056  1.00 31.74  ? 41   LYS B N   1 
ATOM   4013 C  CA  . LYS B 1 41  ? -0.747  -31.219 82.589  1.00 31.96  ? 41   LYS B CA  1 
ATOM   4014 C  C   . LYS B 1 41  ? -1.108  -32.022 81.353  1.00 33.54  ? 41   LYS B C   1 
ATOM   4015 O  O   . LYS B 1 41  ? -2.209  -32.569 81.255  1.00 32.13  ? 41   LYS B O   1 
ATOM   4016 C  CB  . LYS B 1 41  ? -0.236  -32.142 83.696  1.00 35.75  ? 41   LYS B CB  1 
ATOM   4017 C  CG  . LYS B 1 41  ? 0.837   -33.125 83.283  1.00 38.65  ? 41   LYS B CG  1 
ATOM   4018 C  CD  . LYS B 1 41  ? 1.460   -33.691 84.544  1.00 45.04  ? 41   LYS B CD  1 
ATOM   4019 C  CE  . LYS B 1 41  ? 1.860   -35.132 84.384  1.00 51.24  ? 41   LYS B CE  1 
ATOM   4020 N  NZ  . LYS B 1 41  ? 2.810   -35.520 85.467  1.00 53.78  ? 41   LYS B NZ  1 
ATOM   4021 N  N   . PHE B 1 42  ? -0.187  -32.077 80.395  1.00 31.43  ? 42   PHE B N   1 
ATOM   4022 C  CA  . PHE B 1 42  ? -0.383  -32.849 79.179  1.00 30.79  ? 42   PHE B CA  1 
ATOM   4023 C  C   . PHE B 1 42  ? 0.874   -33.666 78.949  1.00 32.74  ? 42   PHE B C   1 
ATOM   4024 O  O   . PHE B 1 42  ? 1.974   -33.109 78.839  1.00 34.56  ? 42   PHE B O   1 
ATOM   4025 C  CB  . PHE B 1 42  ? -0.686  -31.930 77.986  1.00 30.68  ? 42   PHE B CB  1 
ATOM   4026 C  CG  . PHE B 1 42  ? -1.095  -32.658 76.741  1.00 31.59  ? 42   PHE B CG  1 
ATOM   4027 C  CD1 . PHE B 1 42  ? -0.145  -33.271 75.936  1.00 36.73  ? 42   PHE B CD1 1 
ATOM   4028 C  CD2 . PHE B 1 42  ? -2.432  -32.712 76.356  1.00 34.12  ? 42   PHE B CD2 1 
ATOM   4029 C  CE1 . PHE B 1 42  ? -0.513  -33.951 74.767  1.00 36.95  ? 42   PHE B CE1 1 
ATOM   4030 C  CE2 . PHE B 1 42  ? -2.811  -33.369 75.188  1.00 33.85  ? 42   PHE B CE2 1 
ATOM   4031 C  CZ  . PHE B 1 42  ? -1.855  -33.988 74.388  1.00 35.91  ? 42   PHE B CZ  1 
ATOM   4032 N  N   . GLU B 1 43  ? 0.716   -34.979 78.892  1.00 32.83  ? 43   GLU B N   1 
ATOM   4033 C  CA  . GLU B 1 43  ? 1.843   -35.889 78.774  1.00 35.75  ? 43   GLU B CA  1 
ATOM   4034 C  C   . GLU B 1 43  ? 1.781   -36.636 77.456  1.00 33.60  ? 43   GLU B C   1 
ATOM   4035 O  O   . GLU B 1 43  ? 0.702   -37.016 76.988  1.00 33.76  ? 43   GLU B O   1 
ATOM   4036 C  CB  . GLU B 1 43  ? 1.858   -36.907 79.904  1.00 35.71  ? 43   GLU B CB  1 
ATOM   4037 C  CG  . GLU B 1 43  ? 2.195   -36.337 81.231  1.00 38.00  ? 43   GLU B CG  1 
ATOM   4038 C  CD  . GLU B 1 43  ? 2.323   -37.430 82.272  1.00 46.46  ? 43   GLU B CD  1 
ATOM   4039 O  OE1 . GLU B 1 43  ? 1.380   -38.234 82.391  1.00 49.58  ? 43   GLU B OE1 1 
ATOM   4040 O  OE2 . GLU B 1 43  ? 3.356   -37.481 82.961  1.00 53.84  ? 43   GLU B OE2 1 
ATOM   4041 N  N   . ALA B 1 44  ? 2.944   -36.847 76.867  1.00 36.06  ? 44   ALA B N   1 
ATOM   4042 C  CA  . ALA B 1 44  ? 3.129   -37.747 75.745  1.00 34.89  ? 44   ALA B CA  1 
ATOM   4043 C  C   . ALA B 1 44  ? 4.333   -38.608 76.077  1.00 33.28  ? 44   ALA B C   1 
ATOM   4044 O  O   . ALA B 1 44  ? 5.098   -38.286 76.995  1.00 34.36  ? 44   ALA B O   1 
ATOM   4045 C  CB  . ALA B 1 44  ? 3.364   -36.981 74.437  1.00 37.20  ? 44   ALA B CB  1 
ATOM   4046 N  N   . PRO B 1 45  ? 4.516   -39.718 75.382  1.00 35.43  ? 45   PRO B N   1 
ATOM   4047 C  CA  . PRO B 1 45  ? 5.711   -40.525 75.644  1.00 36.33  ? 45   PRO B CA  1 
ATOM   4048 C  C   . PRO B 1 45  ? 6.947   -39.647 75.547  1.00 39.24  ? 45   PRO B C   1 
ATOM   4049 O  O   . PRO B 1 45  ? 7.213   -39.054 74.496  1.00 42.58  ? 45   PRO B O   1 
ATOM   4050 C  CB  . PRO B 1 45  ? 5.676   -41.590 74.544  1.00 38.05  ? 45   PRO B CB  1 
ATOM   4051 C  CG  . PRO B 1 45  ? 4.205   -41.677 74.142  1.00 38.10  ? 45   PRO B CG  1 
ATOM   4052 C  CD  . PRO B 1 45  ? 3.705   -40.262 74.274  1.00 35.83  ? 45   PRO B CD  1 
ATOM   4053 N  N   . GLY B 1 46  ? 7.672   -39.526 76.653  1.00 43.72  ? 46   GLY B N   1 
ATOM   4054 C  CA  . GLY B 1 46  ? 8.904   -38.763 76.685  1.00 47.00  ? 46   GLY B CA  1 
ATOM   4055 C  C   . GLY B 1 46  ? 8.757   -37.262 76.799  1.00 45.12  ? 46   GLY B C   1 
ATOM   4056 O  O   . GLY B 1 46  ? 9.759   -36.552 76.659  1.00 45.78  ? 46   GLY B O   1 
ATOM   4057 N  N   . ARG B 1 47  ? 7.556   -36.742 77.046  1.00 38.99  ? 47   ARG B N   1 
ATOM   4058 C  CA  . ARG B 1 47  ? 7.404   -35.296 77.132  1.00 39.17  ? 47   ARG B CA  1 
ATOM   4059 C  C   . ARG B 1 47  ? 6.266   -34.929 78.069  1.00 35.97  ? 47   ARG B C   1 
ATOM   4060 O  O   . ARG B 1 47  ? 5.260   -35.637 78.156  1.00 37.49  ? 47   ARG B O   1 
ATOM   4061 C  CB  . ARG B 1 47  ? 7.154   -34.660 75.760  1.00 41.80  ? 47   ARG B CB  1 
ATOM   4062 C  CG  . ARG B 1 47  ? 6.802   -33.179 75.876  1.00 48.19  ? 47   ARG B CG  1 
ATOM   4063 C  CD  . ARG B 1 47  ? 7.008   -32.415 74.580  1.00 47.29  ? 47   ARG B CD  1 
ATOM   4064 N  NE  . ARG B 1 47  ? 6.510   -31.044 74.656  1.00 42.05  ? 47   ARG B NE  1 
ATOM   4065 C  CZ  . ARG B 1 47  ? 5.864   -30.443 73.667  1.00 40.99  ? 47   ARG B CZ  1 
ATOM   4066 N  NH1 . ARG B 1 47  ? 5.635   -31.064 72.519  1.00 44.89  ? 47   ARG B NH1 1 
ATOM   4067 N  NH2 . ARG B 1 47  ? 5.438   -29.188 73.830  1.00 36.27  ? 47   ARG B NH2 1 
ATOM   4068 N  N   . VAL B 1 48  ? 6.438   -33.810 78.768  1.00 34.02  ? 48   VAL B N   1 
ATOM   4069 C  CA  . VAL B 1 48  ? 5.371   -33.213 79.569  1.00 31.16  ? 48   VAL B CA  1 
ATOM   4070 C  C   . VAL B 1 48  ? 5.355   -31.714 79.293  1.00 36.71  ? 48   VAL B C   1 
ATOM   4071 O  O   . VAL B 1 48  ? 6.411   -31.080 79.160  1.00 37.18  ? 48   VAL B O   1 
ATOM   4072 C  CB  . VAL B 1 48  ? 5.544   -33.495 81.075  1.00 39.69  ? 48   VAL B CB  1 
ATOM   4073 C  CG1 . VAL B 1 48  ? 6.908   -33.039 81.544  1.00 43.18  ? 48   VAL B CG1 1 
ATOM   4074 C  CG2 . VAL B 1 48  ? 4.444   -32.812 81.882  1.00 40.62  ? 48   VAL B CG2 1 
ATOM   4075 N  N   . THR B 1 49  ? 4.156   -31.148 79.194  1.00 31.93  ? 49   THR B N   1 
ATOM   4076 C  CA  . THR B 1 49  ? 3.992   -29.701 79.194  1.00 32.43  ? 49   THR B CA  1 
ATOM   4077 C  C   . THR B 1 49  ? 2.761   -29.364 80.023  1.00 33.37  ? 49   THR B C   1 
ATOM   4078 O  O   . THR B 1 49  ? 2.041   -30.251 80.493  1.00 33.80  ? 49   THR B O   1 
ATOM   4079 C  CB  . THR B 1 49  ? 3.915   -29.129 77.762  1.00 34.49  ? 49   THR B CB  1 
ATOM   4080 O  OG1 . THR B 1 49  ? 4.077   -27.698 77.805  1.00 32.86  ? 49   THR B OG1 1 
ATOM   4081 C  CG2 . THR B 1 49  ? 2.571   -29.461 77.102  1.00 34.02  ? 49   THR B CG2 1 
ATOM   4082 N  N   . ARG B 1 50  ? 2.577   -28.073 80.278  1.00 30.97  ? 50   ARG B N   1 
ATOM   4083 C  CA  . ARG B 1 50  ? 1.463   -27.568 81.080  1.00 31.43  ? 50   ARG B CA  1 
ATOM   4084 C  C   . ARG B 1 50  ? 0.767   -26.465 80.296  1.00 32.88  ? 50   ARG B C   1 
ATOM   4085 O  O   . ARG B 1 50  ? 1.403   -25.476 79.916  1.00 33.08  ? 50   ARG B O   1 
ATOM   4086 C  CB  . ARG B 1 50  ? 1.953   -27.036 82.433  1.00 34.86  ? 50   ARG B CB  1 
ATOM   4087 C  CG  . ARG B 1 50  ? 2.702   -28.081 83.236  1.00 35.66  ? 50   ARG B CG  1 
ATOM   4088 C  CD  . ARG B 1 50  ? 3.983   -27.504 83.809  1.00 37.07  ? 50   ARG B CD  1 
ATOM   4089 N  NE  . ARG B 1 50  ? 4.821   -28.563 84.359  1.00 40.50  ? 50   ARG B NE  1 
ATOM   4090 C  CZ  . ARG B 1 50  ? 5.785   -29.184 83.692  1.00 39.87  ? 50   ARG B CZ  1 
ATOM   4091 N  NH1 . ARG B 1 50  ? 6.127   -28.820 82.455  1.00 35.17  ? 50   ARG B NH1 1 
ATOM   4092 N  NH2 . ARG B 1 50  ? 6.417   -30.204 84.271  1.00 39.69  ? 50   ARG B NH2 1 
ATOM   4093 N  N   . TYR B 1 51  ? -0.529  -26.625 80.060  1.00 29.03  ? 51   TYR B N   1 
ATOM   4094 C  CA  . TYR B 1 51  ? -1.307  -25.652 79.293  1.00 29.93  ? 51   TYR B CA  1 
ATOM   4095 C  C   . TYR B 1 51  ? -1.934  -24.630 80.225  1.00 30.74  ? 51   TYR B C   1 
ATOM   4096 O  O   . TYR B 1 51  ? -2.658  -25.000 81.154  1.00 31.57  ? 51   TYR B O   1 
ATOM   4097 C  CB  . TYR B 1 51  ? -2.408  -26.345 78.489  1.00 29.81  ? 51   TYR B CB  1 
ATOM   4098 C  CG  . TYR B 1 51  ? -1.872  -27.034 77.269  1.00 28.64  ? 51   TYR B CG  1 
ATOM   4099 C  CD1 . TYR B 1 51  ? -1.356  -28.323 77.350  1.00 30.71  ? 51   TYR B CD1 1 
ATOM   4100 C  CD2 . TYR B 1 51  ? -1.865  -26.388 76.035  1.00 30.76  ? 51   TYR B CD2 1 
ATOM   4101 C  CE1 . TYR B 1 51  ? -0.843  -28.958 76.215  1.00 29.88  ? 51   TYR B CE1 1 
ATOM   4102 C  CE2 . TYR B 1 51  ? -1.350  -27.009 74.904  1.00 31.60  ? 51   TYR B CE2 1 
ATOM   4103 C  CZ  . TYR B 1 51  ? -0.843  -28.298 75.003  1.00 27.95  ? 51   TYR B CZ  1 
ATOM   4104 O  OH  . TYR B 1 51  ? -0.334  -28.929 73.878  1.00 30.48  ? 51   TYR B OH  1 
ATOM   4105 N  N   . LEU B 1 52  ? -1.670  -23.352 79.961  1.00 30.08  ? 52   LEU B N   1 
ATOM   4106 C  CA  . LEU B 1 52  ? -2.120  -22.251 80.800  1.00 28.72  ? 52   LEU B CA  1 
ATOM   4107 C  C   . LEU B 1 52  ? -3.213  -21.469 80.085  1.00 30.55  ? 52   LEU B C   1 
ATOM   4108 O  O   . LEU B 1 52  ? -3.097  -21.175 78.890  1.00 30.34  ? 52   LEU B O   1 
ATOM   4109 C  CB  . LEU B 1 52  ? -0.972  -21.303 81.138  1.00 31.97  ? 52   LEU B CB  1 
ATOM   4110 C  CG  . LEU B 1 52  ? 0.261   -21.907 81.793  1.00 33.31  ? 52   LEU B CG  1 
ATOM   4111 C  CD1 . LEU B 1 52  ? 1.224   -20.793 82.149  1.00 35.69  ? 52   LEU B CD1 1 
ATOM   4112 C  CD2 . LEU B 1 52  ? -0.145  -22.695 83.024  1.00 34.11  ? 52   LEU B CD2 1 
ATOM   4113 N  N   . SER B 1 53  ? -4.255  -21.082 80.836  1.00 29.86  ? 53   SER B N   1 
ATOM   4114 C  CA  . SER B 1 53  ? -5.411  -20.407 80.247  1.00 26.28  ? 53   SER B CA  1 
ATOM   4115 C  C   . SER B 1 53  ? -5.847  -19.147 80.979  1.00 30.10  ? 53   SER B C   1 
ATOM   4116 O  O   . SER B 1 53  ? -6.695  -18.427 80.443  1.00 30.46  ? 53   SER B O   1 
ATOM   4117 C  CB  . SER B 1 53  ? -6.617  -21.366 80.181  1.00 30.68  ? 53   SER B CB  1 
ATOM   4118 O  OG  . SER B 1 53  ? -6.338  -22.420 79.279  1.00 33.45  ? 53   SER B OG  1 
ATOM   4119 N  N   . SER B 1 54  ? -5.343  -18.872 82.185  1.00 30.42  ? 54   SER B N   1 
ATOM   4120 C  CA  . SER B 1 54  ? -5.774  -17.701 82.947  1.00 29.25  ? 54   SER B CA  1 
ATOM   4121 C  C   . SER B 1 54  ? -4.754  -16.580 82.841  1.00 30.12  ? 54   SER B C   1 
ATOM   4122 O  O   . SER B 1 54  ? -3.545  -16.814 82.751  1.00 33.08  ? 54   SER B O   1 
ATOM   4123 C  CB  . SER B 1 54  ? -5.994  -18.042 84.426  1.00 32.26  ? 54   SER B CB  1 
ATOM   4124 O  OG  . SER B 1 54  ? -4.764  -18.386 85.038  1.00 31.21  ? 54   SER B OG  1 
ATOM   4125 N  N   . GLN B 1 55  ? -5.257  -15.347 82.877  1.00 31.62  ? 55   GLN B N   1 
ATOM   4126 C  CA  . GLN B 1 55  ? -4.358  -14.203 82.947  1.00 31.83  ? 55   GLN B CA  1 
ATOM   4127 C  C   . GLN B 1 55  ? -3.512  -14.263 84.208  1.00 30.35  ? 55   GLN B C   1 
ATOM   4128 O  O   . GLN B 1 55  ? -2.344  -13.860 84.201  1.00 31.25  ? 55   GLN B O   1 
ATOM   4129 C  CB  . GLN B 1 55  ? -5.180  -12.910 82.883  1.00 31.23  ? 55   GLN B CB  1 
ATOM   4130 C  CG  . GLN B 1 55  ? -4.361  -11.647 82.698  1.00 35.41  ? 55   GLN B CG  1 
ATOM   4131 C  CD  . GLN B 1 55  ? -3.893  -11.045 84.021  1.00 33.67  ? 55   GLN B CD  1 
ATOM   4132 O  OE1 . GLN B 1 55  ? -4.308  -11.468 85.100  1.00 35.08  ? 55   GLN B OE1 1 
ATOM   4133 N  NE2 . GLN B 1 55  ? -3.013  -10.050 83.933  1.00 37.77  ? 55   GLN B NE2 1 
ATOM   4134 N  N   . ARG B 1 56  ? -4.077  -14.796 85.291  1.00 31.32  ? 56   ARG B N   1 
ATOM   4135 C  CA  . ARG B 1 56  ? -3.340  -14.888 86.548  1.00 32.39  ? 56   ARG B CA  1 
ATOM   4136 C  C   . ARG B 1 56  ? -2.020  -15.622 86.365  1.00 33.45  ? 56   ARG B C   1 
ATOM   4137 O  O   . ARG B 1 56  ? -0.968  -15.166 86.830  1.00 36.34  ? 56   ARG B O   1 
ATOM   4138 C  CB  . ARG B 1 56  ? -4.202  -15.604 87.597  1.00 35.59  ? 56   ARG B CB  1 
ATOM   4139 C  CG  . ARG B 1 56  ? -3.493  -15.841 88.922  1.00 43.15  ? 56   ARG B CG  1 
ATOM   4140 C  CD  . ARG B 1 56  ? -4.384  -16.629 89.894  1.00 43.63  ? 56   ARG B CD  1 
ATOM   4141 N  NE  . ARG B 1 56  ? -4.218  -18.076 89.796  1.00 43.33  ? 56   ARG B NE  1 
ATOM   4142 C  CZ  . ARG B 1 56  ? -3.381  -18.783 90.544  1.00 42.48  ? 56   ARG B CZ  1 
ATOM   4143 N  NH1 . ARG B 1 56  ? -2.573  -18.199 91.416  1.00 40.44  ? 56   ARG B NH1 1 
ATOM   4144 N  NH2 . ARG B 1 56  ? -3.369  -20.112 90.433  1.00 40.99  ? 56   ARG B NH2 1 
ATOM   4145 N  N   . LEU B 1 57  ? -2.061  -16.778 85.703  1.00 31.51  ? 57   LEU B N   1 
ATOM   4146 C  CA  . LEU B 1 57  ? -0.853  -17.561 85.491  1.00 28.27  ? 57   LEU B CA  1 
ATOM   4147 C  C   . LEU B 1 57  ? -0.065  -17.096 84.276  1.00 31.59  ? 57   LEU B C   1 
ATOM   4148 O  O   . LEU B 1 57  ? 1.167   -17.114 84.306  1.00 30.25  ? 57   LEU B O   1 
ATOM   4149 C  CB  . LEU B 1 57  ? -1.198  -19.041 85.339  1.00 30.37  ? 57   LEU B CB  1 
ATOM   4150 C  CG  . LEU B 1 57  ? -1.808  -19.650 86.609  1.00 32.04  ? 57   LEU B CG  1 
ATOM   4151 C  CD1 . LEU B 1 57  ? -2.088  -21.129 86.396  1.00 33.27  ? 57   LEU B CD1 1 
ATOM   4152 C  CD2 . LEU B 1 57  ? -0.904  -19.405 87.820  1.00 34.22  ? 57   LEU B CD2 1 
ATOM   4153 N  N   . ILE B 1 58  ? -0.745  -16.651 83.219  1.00 29.66  ? 58   ILE B N   1 
ATOM   4154 C  CA  . ILE B 1 58  ? -0.011  -16.262 82.017  1.00 31.49  ? 58   ILE B CA  1 
ATOM   4155 C  C   . ILE B 1 58  ? 0.816   -15.001 82.255  1.00 32.02  ? 58   ILE B C   1 
ATOM   4156 O  O   . ILE B 1 58  ? 1.901   -14.851 81.675  1.00 32.29  ? 58   ILE B O   1 
ATOM   4157 C  CB  . ILE B 1 58  ? -1.001  -16.137 80.839  1.00 30.75  ? 58   ILE B CB  1 
ATOM   4158 C  CG1 . ILE B 1 58  ? -1.461  -17.547 80.441  1.00 29.63  ? 58   ILE B CG1 1 
ATOM   4159 C  CG2 . ILE B 1 58  ? -0.377  -15.444 79.643  1.00 28.60  ? 58   ILE B CG2 1 
ATOM   4160 C  CD1 . ILE B 1 58  ? -2.651  -17.577 79.502  1.00 28.03  ? 58   ILE B CD1 1 
ATOM   4161 N  N   . LYS B 1 59  ? 0.362   -14.090 83.126  1.00 31.33  ? 59   LYS B N   1 
ATOM   4162 C  CA  . LYS B 1 59  ? 1.179   -12.909 83.399  1.00 33.48  ? 59   LYS B CA  1 
ATOM   4163 C  C   . LYS B 1 59  ? 2.512   -13.299 84.034  1.00 32.75  ? 59   LYS B C   1 
ATOM   4164 O  O   . LYS B 1 59  ? 3.536   -12.656 83.782  1.00 33.36  ? 59   LYS B O   1 
ATOM   4165 C  CB  . LYS B 1 59  ? 0.427   -11.920 84.294  1.00 32.67  ? 59   LYS B CB  1 
ATOM   4166 C  CG  . LYS B 1 59  ? 0.283   -12.336 85.733  1.00 34.92  ? 59   LYS B CG  1 
ATOM   4167 C  CD  . LYS B 1 59  ? -0.470  -11.273 86.519  1.00 40.26  ? 59   LYS B CD  1 
ATOM   4168 C  CE  . LYS B 1 59  ? -0.631  -11.666 87.979  1.00 42.91  ? 59   LYS B CE  1 
ATOM   4169 N  NZ  . LYS B 1 59  ? -1.347  -10.570 88.711  1.00 48.88  ? 59   LYS B NZ  1 
ATOM   4170 N  N   . GLU B 1 60  ? 2.519   -14.338 84.879  1.00 32.51  ? 60   GLU B N   1 
ATOM   4171 C  CA  . GLU B 1 60  ? 3.791   -14.830 85.415  1.00 36.20  ? 60   GLU B CA  1 
ATOM   4172 C  C   . GLU B 1 60  ? 4.639   -15.484 84.328  1.00 34.22  ? 60   GLU B C   1 
ATOM   4173 O  O   . GLU B 1 60  ? 5.851   -15.254 84.252  1.00 34.79  ? 60   GLU B O   1 
ATOM   4174 C  CB  . GLU B 1 60  ? 3.542   -15.817 86.556  1.00 33.84  ? 60   GLU B CB  1 
ATOM   4175 C  CG  . GLU B 1 60  ? 3.062   -15.150 87.830  1.00 36.93  ? 60   GLU B CG  1 
ATOM   4176 C  CD  . GLU B 1 60  ? 3.023   -16.109 89.006  1.00 39.71  ? 60   GLU B CD  1 
ATOM   4177 O  OE1 . GLU B 1 60  ? 3.915   -16.985 89.110  1.00 36.40  ? 60   GLU B OE1 1 
ATOM   4178 O  OE2 . GLU B 1 60  ? 2.097   -15.976 89.834  1.00 42.32  ? 60   GLU B OE2 1 
ATOM   4179 N  N   . ALA B 1 61  ? 4.026   -16.318 83.490  1.00 31.57  ? 61   ALA B N   1 
ATOM   4180 C  CA  . ALA B 1 61  ? 4.763   -16.941 82.399  1.00 34.04  ? 61   ALA B CA  1 
ATOM   4181 C  C   . ALA B 1 61  ? 5.417   -15.905 81.495  1.00 33.83  ? 61   ALA B C   1 
ATOM   4182 O  O   . ALA B 1 61  ? 6.450   -16.192 80.870  1.00 31.83  ? 61   ALA B O   1 
ATOM   4183 C  CB  . ALA B 1 61  ? 3.827   -17.831 81.579  1.00 33.40  ? 61   ALA B CB  1 
ATOM   4184 N  N   . CYS B 1 62  ? 4.832   -14.708 81.399  1.00 32.99  ? 62   CYS B N   1 
ATOM   4185 C  CA  . CYS B 1 62  ? 5.334   -13.640 80.538  1.00 30.54  ? 62   CYS B CA  1 
ATOM   4186 C  C   . CYS B 1 62  ? 6.427   -12.810 81.206  1.00 33.28  ? 62   CYS B C   1 
ATOM   4187 O  O   . CYS B 1 62  ? 6.900   -11.828 80.617  1.00 32.38  ? 62   CYS B O   1 
ATOM   4188 C  CB  . CYS B 1 62  ? 4.183   -12.731 80.101  1.00 31.71  ? 62   CYS B CB  1 
ATOM   4189 S  SG  . CYS B 1 62  ? 3.099   -13.492 78.862  1.00 33.65  ? 62   CYS B SG  1 
ATOM   4190 N  N   . ASP B 1 63  ? 6.840   -13.178 82.415  1.00 32.28  ? 63   ASP B N   1 
ATOM   4191 C  CA  . ASP B 1 63  ? 7.965   -12.527 83.077  1.00 31.90  ? 63   ASP B CA  1 
ATOM   4192 C  C   . ASP B 1 63  ? 9.258   -13.068 82.479  1.00 31.45  ? 63   ASP B C   1 
ATOM   4193 O  O   . ASP B 1 63  ? 9.618   -14.225 82.714  1.00 33.01  ? 63   ASP B O   1 
ATOM   4194 C  CB  . ASP B 1 63  ? 7.881   -12.785 84.581  1.00 34.41  ? 63   ASP B CB  1 
ATOM   4195 C  CG  . ASP B 1 63  ? 9.053   -12.207 85.355  1.00 39.80  ? 63   ASP B CG  1 
ATOM   4196 O  OD1 . ASP B 1 63  ? 10.068  -11.785 84.754  1.00 34.23  ? 63   ASP B OD1 1 
ATOM   4197 O  OD2 . ASP B 1 63  ? 8.949   -12.198 86.597  1.00 38.73  ? 63   ASP B OD2 1 
ATOM   4198 N  N   . GLU B 1 64  ? 9.959   -12.238 81.695  1.00 32.33  ? 64   GLU B N   1 
ATOM   4199 C  CA  . GLU B 1 64  ? 11.121  -12.714 80.951  1.00 33.25  ? 64   GLU B CA  1 
ATOM   4200 C  C   . GLU B 1 64  ? 12.322  -12.993 81.841  1.00 32.36  ? 64   GLU B C   1 
ATOM   4201 O  O   . GLU B 1 64  ? 13.288  -13.612 81.375  1.00 33.09  ? 64   GLU B O   1 
ATOM   4202 C  CB  . GLU B 1 64  ? 11.510  -11.690 79.890  1.00 35.82  ? 64   GLU B CB  1 
ATOM   4203 C  CG  . GLU B 1 64  ? 10.474  -11.505 78.798  1.00 33.96  ? 64   GLU B CG  1 
ATOM   4204 C  CD  . GLU B 1 64  ? 10.869  -10.398 77.851  1.00 39.27  ? 64   GLU B CD  1 
ATOM   4205 O  OE1 . GLU B 1 64  ? 10.779  -9.220  78.248  1.00 42.77  ? 64   GLU B OE1 1 
ATOM   4206 O  OE2 . GLU B 1 64  ? 11.262  -10.703 76.717  1.00 32.46  ? 64   GLU B OE2 1 
ATOM   4207 N  N   . SER B 1 65  ? 12.298  -12.535 83.094  1.00 33.74  ? 65   SER B N   1 
ATOM   4208 C  CA  . SER B 1 65  ? 13.360  -12.923 84.009  1.00 34.58  ? 65   SER B CA  1 
ATOM   4209 C  C   . SER B 1 65  ? 13.189  -14.359 84.463  1.00 35.28  ? 65   SER B C   1 
ATOM   4210 O  O   . SER B 1 65  ? 14.153  -14.962 84.943  1.00 35.45  ? 65   SER B O   1 
ATOM   4211 C  CB  . SER B 1 65  ? 13.406  -11.985 85.227  1.00 37.86  ? 65   SER B CB  1 
ATOM   4212 O  OG  . SER B 1 65  ? 12.351  -12.269 86.136  1.00 40.71  ? 65   SER B OG  1 
ATOM   4213 N  N   . ARG B 1 66  ? 11.992  -14.924 84.305  1.00 32.33  ? 66   ARG B N   1 
ATOM   4214 C  CA  . ARG B 1 66  ? 11.704  -16.267 84.778  1.00 34.12  ? 66   ARG B CA  1 
ATOM   4215 C  C   . ARG B 1 66  ? 11.507  -17.282 83.666  1.00 31.86  ? 66   ARG B C   1 
ATOM   4216 O  O   . ARG B 1 66  ? 11.826  -18.459 83.861  1.00 32.83  ? 66   ARG B O   1 
ATOM   4217 C  CB  . ARG B 1 66  ? 10.457  -16.257 85.672  1.00 33.98  ? 66   ARG B CB  1 
ATOM   4218 C  CG  . ARG B 1 66  ? 10.598  -15.410 86.935  1.00 36.37  ? 66   ARG B CG  1 
ATOM   4219 C  CD  . ARG B 1 66  ? 9.233   -15.212 87.619  1.00 38.43  ? 66   ARG B CD  1 
ATOM   4220 N  NE  . ARG B 1 66  ? 8.764   -16.462 88.202  1.00 37.72  ? 66   ARG B NE  1 
ATOM   4221 C  CZ  . ARG B 1 66  ? 7.512   -16.718 88.564  1.00 36.53  ? 66   ARG B CZ  1 
ATOM   4222 N  NH1 . ARG B 1 66  ? 6.545   -15.828 88.407  1.00 35.55  ? 66   ARG B NH1 1 
ATOM   4223 N  NH2 . ARG B 1 66  ? 7.221   -17.909 89.081  1.00 40.14  ? 66   ARG B NH2 1 
ATOM   4224 N  N   . PHE B 1 67  ? 10.999  -16.860 82.509  1.00 31.34  ? 67   PHE B N   1 
ATOM   4225 C  CA  . PHE B 1 67  ? 10.692  -17.773 81.417  1.00 29.64  ? 67   PHE B CA  1 
ATOM   4226 C  C   . PHE B 1 67  ? 11.175  -17.183 80.107  1.00 31.84  ? 67   PHE B C   1 
ATOM   4227 O  O   . PHE B 1 67  ? 11.067  -15.974 79.892  1.00 33.20  ? 67   PHE B O   1 
ATOM   4228 C  CB  . PHE B 1 67  ? 9.180   -18.042 81.328  1.00 33.15  ? 67   PHE B CB  1 
ATOM   4229 C  CG  . PHE B 1 67  ? 8.599   -18.617 82.591  1.00 31.53  ? 67   PHE B CG  1 
ATOM   4230 C  CD1 . PHE B 1 67  ? 8.587   -19.985 82.800  1.00 32.38  ? 67   PHE B CD1 1 
ATOM   4231 C  CD2 . PHE B 1 67  ? 8.060   -17.784 83.559  1.00 31.37  ? 67   PHE B CD2 1 
ATOM   4232 C  CE1 . PHE B 1 67  ? 8.059   -20.525 83.964  1.00 30.97  ? 67   PHE B CE1 1 
ATOM   4233 C  CE2 . PHE B 1 67  ? 7.542   -18.319 84.752  1.00 33.06  ? 67   PHE B CE2 1 
ATOM   4234 C  CZ  . PHE B 1 67  ? 7.535   -19.689 84.939  1.00 32.74  ? 67   PHE B CZ  1 
ATOM   4235 N  N   . ASP B 1 68  ? 11.701  -18.046 79.234  1.00 29.70  ? 68   ASP B N   1 
ATOM   4236 C  CA  . ASP B 1 68  ? 12.129  -17.676 77.892  1.00 27.53  ? 68   ASP B CA  1 
ATOM   4237 C  C   . ASP B 1 68  ? 11.282  -18.437 76.876  1.00 28.96  ? 68   ASP B C   1 
ATOM   4238 O  O   . ASP B 1 68  ? 10.614  -19.425 77.207  1.00 29.47  ? 68   ASP B O   1 
ATOM   4239 C  CB  . ASP B 1 68  ? 13.636  -17.996 77.738  1.00 29.91  ? 68   ASP B CB  1 
ATOM   4240 C  CG  . ASP B 1 68  ? 14.208  -17.636 76.382  1.00 34.11  ? 68   ASP B CG  1 
ATOM   4241 O  OD1 . ASP B 1 68  ? 13.709  -16.714 75.696  1.00 30.62  ? 68   ASP B OD1 1 
ATOM   4242 O  OD2 . ASP B 1 68  ? 15.206  -18.296 76.022  1.00 32.48  ? 68   ASP B OD2 1 
ATOM   4243 N  N   . LYS B 1 69  ? 11.312  -17.972 75.629  1.00 29.23  ? 69   LYS B N   1 
ATOM   4244 C  CA  . LYS B 1 69  ? 10.609  -18.677 74.560  1.00 30.06  ? 69   LYS B CA  1 
ATOM   4245 C  C   . LYS B 1 69  ? 11.153  -20.093 74.381  1.00 31.05  ? 69   LYS B C   1 
ATOM   4246 O  O   . LYS B 1 69  ? 12.366  -20.303 74.297  1.00 31.38  ? 69   LYS B O   1 
ATOM   4247 C  CB  . LYS B 1 69  ? 10.738  -17.905 73.241  1.00 29.13  ? 69   LYS B CB  1 
ATOM   4248 C  CG  . LYS B 1 69  ? 10.390  -18.756 72.014  1.00 30.54  ? 69   LYS B CG  1 
ATOM   4249 C  CD  . LYS B 1 69  ? 9.983   -17.892 70.801  1.00 26.99  ? 69   LYS B CD  1 
ATOM   4250 C  CE  . LYS B 1 69  ? 9.862   -18.784 69.564  1.00 26.86  ? 69   LYS B CE  1 
ATOM   4251 N  NZ  . LYS B 1 69  ? 8.946   -18.223 68.480  1.00 26.95  ? 69   LYS B NZ  1 
ATOM   4252 N  N   . ASN B 1 70  ? 10.242  -21.066 74.300  1.00 29.45  ? 70   ASN B N   1 
ATOM   4253 C  CA  . ASN B 1 70  ? 10.539  -22.445 73.965  1.00 29.73  ? 70   ASN B CA  1 
ATOM   4254 C  C   . ASN B 1 70  ? 10.067  -22.724 72.542  1.00 28.97  ? 70   ASN B C   1 
ATOM   4255 O  O   . ASN B 1 70  ? 9.094   -22.128 72.070  1.00 31.33  ? 70   ASN B O   1 
ATOM   4256 C  CB  . ASN B 1 70  ? 9.831   -23.401 74.937  1.00 30.84  ? 70   ASN B CB  1 
ATOM   4257 C  CG  . ASN B 1 70  ? 10.143  -24.848 74.661  1.00 33.76  ? 70   ASN B CG  1 
ATOM   4258 O  OD1 . ASN B 1 70  ? 11.309  -25.248 74.589  1.00 32.70  ? 70   ASN B OD1 1 
ATOM   4259 N  ND2 . ASN B 1 70  ? 9.101   -25.651 74.502  1.00 32.80  ? 70   ASN B ND2 1 
ATOM   4260 N  N   . LEU B 1 71  ? 10.748  -23.634 71.857  1.00 29.13  ? 71   LEU B N   1 
ATOM   4261 C  CA  . LEU B 1 71  ? 10.247  -24.147 70.586  1.00 28.68  ? 71   LEU B CA  1 
ATOM   4262 C  C   . LEU B 1 71  ? 9.330   -25.316 70.908  1.00 30.76  ? 71   LEU B C   1 
ATOM   4263 O  O   . LEU B 1 71  ? 9.785   -26.371 71.367  1.00 31.85  ? 71   LEU B O   1 
ATOM   4264 C  CB  . LEU B 1 71  ? 11.384  -24.568 69.656  1.00 31.34  ? 71   LEU B CB  1 
ATOM   4265 C  CG  . LEU B 1 71  ? 12.418  -23.493 69.313  1.00 32.47  ? 71   LEU B CG  1 
ATOM   4266 C  CD1 . LEU B 1 71  ? 13.359  -24.049 68.253  1.00 31.52  ? 71   LEU B CD1 1 
ATOM   4267 C  CD2 . LEU B 1 71  ? 11.765  -22.193 68.820  1.00 31.66  ? 71   LEU B CD2 1 
ATOM   4268 N  N   . SER B 1 72  ? 8.031   -25.114 70.695  1.00 29.62  ? 72   SER B N   1 
ATOM   4269 C  CA  . SER B 1 72  ? 7.072   -26.203 70.728  1.00 32.03  ? 72   SER B CA  1 
ATOM   4270 C  C   . SER B 1 72  ? 7.460   -27.266 69.702  1.00 31.66  ? 72   SER B C   1 
ATOM   4271 O  O   . SER B 1 72  ? 8.276   -27.033 68.812  1.00 31.29  ? 72   SER B O   1 
ATOM   4272 C  CB  . SER B 1 72  ? 5.679   -25.656 70.417  1.00 27.94  ? 72   SER B CB  1 
ATOM   4273 O  OG  . SER B 1 72  ? 5.722   -25.003 69.157  1.00 30.91  ? 72   SER B OG  1 
ATOM   4274 N  N   . GLN B 1 73  ? 6.889   -28.463 69.840  1.00 31.91  ? 73   GLN B N   1 
ATOM   4275 C  CA  . GLN B 1 73  ? 7.101   -29.454 68.791  1.00 33.19  ? 73   GLN B CA  1 
ATOM   4276 C  C   . GLN B 1 73  ? 6.700   -28.885 67.440  1.00 32.94  ? 73   GLN B C   1 
ATOM   4277 O  O   . GLN B 1 73  ? 7.383   -29.097 66.429  1.00 32.29  ? 73   GLN B O   1 
ATOM   4278 C  CB  . GLN B 1 73  ? 6.323   -30.736 69.083  1.00 34.43  ? 73   GLN B CB  1 
ATOM   4279 C  CG  . GLN B 1 73  ? 6.761   -31.864 68.170  1.00 39.17  ? 73   GLN B CG  1 
ATOM   4280 C  CD  . GLN B 1 73  ? 8.214   -32.234 68.403  1.00 44.71  ? 73   GLN B CD  1 
ATOM   4281 O  OE1 . GLN B 1 73  ? 9.085   -31.985 67.556  1.00 43.69  ? 73   GLN B OE1 1 
ATOM   4282 N  NE2 . GLN B 1 73  ? 8.490   -32.806 69.570  1.00 41.46  ? 73   GLN B NE2 1 
ATOM   4283 N  N   . ALA B 1 74  ? 5.602   -28.132 67.410  1.00 32.11  ? 74   ALA B N   1 
ATOM   4284 C  CA  . ALA B 1 74  ? 5.159   -27.528 66.160  1.00 31.73  ? 74   ALA B CA  1 
ATOM   4285 C  C   . ALA B 1 74  ? 6.262   -26.665 65.550  1.00 32.04  ? 74   ALA B C   1 
ATOM   4286 O  O   . ALA B 1 74  ? 6.572   -26.783 64.357  1.00 31.41  ? 74   ALA B O   1 
ATOM   4287 C  CB  . ALA B 1 74  ? 3.888   -26.715 66.416  1.00 30.56  ? 74   ALA B CB  1 
ATOM   4288 N  N   . LEU B 1 75  ? 6.864   -25.784 66.356  1.00 29.78  ? 75   LEU B N   1 
ATOM   4289 C  CA  . LEU B 1 75  ? 7.926   -24.932 65.828  1.00 28.84  ? 75   LEU B CA  1 
ATOM   4290 C  C   . LEU B 1 75  ? 9.169   -25.737 65.484  1.00 29.32  ? 75   LEU B C   1 
ATOM   4291 O  O   . LEU B 1 75  ? 9.874   -25.396 64.524  1.00 31.06  ? 75   LEU B O   1 
ATOM   4292 C  CB  . LEU B 1 75  ? 8.273   -23.812 66.813  1.00 28.99  ? 75   LEU B CB  1 
ATOM   4293 C  CG  . LEU B 1 75  ? 7.211   -22.710 66.970  1.00 30.54  ? 75   LEU B CG  1 
ATOM   4294 C  CD1 . LEU B 1 75  ? 7.719   -21.595 67.892  1.00 29.34  ? 75   LEU B CD1 1 
ATOM   4295 C  CD2 . LEU B 1 75  ? 6.751   -22.139 65.622  1.00 32.46  ? 75   LEU B CD2 1 
ATOM   4296 N  N   . LYS B 1 76  ? 9.457   -26.808 66.233  1.00 31.26  ? 76   LYS B N   1 
ATOM   4297 C  CA  . LYS B 1 76  ? 10.591  -27.649 65.849  1.00 31.98  ? 76   LYS B CA  1 
ATOM   4298 C  C   . LYS B 1 76  ? 10.385  -28.234 64.455  1.00 32.67  ? 76   LYS B C   1 
ATOM   4299 O  O   . LYS B 1 76  ? 11.327  -28.318 63.647  1.00 31.08  ? 76   LYS B O   1 
ATOM   4300 C  CB  . LYS B 1 76  ? 10.812  -28.749 66.892  1.00 31.21  ? 76   LYS B CB  1 
ATOM   4301 C  CG  . LYS B 1 76  ? 11.411  -28.215 68.204  1.00 35.39  ? 76   LYS B CG  1 
ATOM   4302 C  CD  . LYS B 1 76  ? 11.754  -29.353 69.160  1.00 35.71  ? 76   LYS B CD  1 
ATOM   4303 C  CE  . LYS B 1 76  ? 12.280  -28.805 70.478  1.00 43.92  ? 76   LYS B CE  1 
ATOM   4304 N  NZ  . LYS B 1 76  ? 12.296  -29.861 71.523  1.00 48.55  ? 76   LYS B NZ  1 
ATOM   4305 N  N   . PHE B 1 77  ? 9.149   -28.609 64.132  1.00 32.88  ? 77   PHE B N   1 
ATOM   4306 C  CA  . PHE B 1 77  ? 8.882   -29.142 62.801  1.00 33.51  ? 77   PHE B CA  1 
ATOM   4307 C  C   . PHE B 1 77  ? 8.912   -28.047 61.739  1.00 33.55  ? 77   PHE B C   1 
ATOM   4308 O  O   . PHE B 1 77  ? 9.365   -28.285 60.615  1.00 33.75  ? 77   PHE B O   1 
ATOM   4309 C  CB  . PHE B 1 77  ? 7.538   -29.862 62.788  1.00 33.09  ? 77   PHE B CB  1 
ATOM   4310 C  CG  . PHE B 1 77  ? 7.541   -31.152 63.545  1.00 35.51  ? 77   PHE B CG  1 
ATOM   4311 C  CD1 . PHE B 1 77  ? 8.718   -31.866 63.719  1.00 38.25  ? 77   PHE B CD1 1 
ATOM   4312 C  CD2 . PHE B 1 77  ? 6.376   -31.650 64.084  1.00 33.71  ? 77   PHE B CD2 1 
ATOM   4313 C  CE1 . PHE B 1 77  ? 8.721   -33.068 64.414  1.00 42.47  ? 77   PHE B CE1 1 
ATOM   4314 C  CE2 . PHE B 1 77  ? 6.370   -32.852 64.776  1.00 39.65  ? 77   PHE B CE2 1 
ATOM   4315 C  CZ  . PHE B 1 77  ? 7.545   -33.558 64.937  1.00 41.35  ? 77   PHE B CZ  1 
ATOM   4316 N  N   . VAL B 1 78  ? 8.415   -26.849 62.058  1.00 31.73  ? 78   VAL B N   1 
ATOM   4317 C  CA  . VAL B 1 78  ? 8.535   -25.751 61.103  1.00 29.66  ? 78   VAL B CA  1 
ATOM   4318 C  C   . VAL B 1 78  ? 10.001  -25.411 60.884  1.00 32.30  ? 78   VAL B C   1 
ATOM   4319 O  O   . VAL B 1 78  ? 10.402  -25.037 59.779  1.00 31.34  ? 78   VAL B O   1 
ATOM   4320 C  CB  . VAL B 1 78  ? 7.723   -24.534 61.593  1.00 31.88  ? 78   VAL B CB  1 
ATOM   4321 C  CG1 . VAL B 1 78  ? 8.003   -23.302 60.761  1.00 33.88  ? 78   VAL B CG1 1 
ATOM   4322 C  CG2 . VAL B 1 78  ? 6.224   -24.872 61.574  1.00 31.77  ? 78   VAL B CG2 1 
ATOM   4323 N  N   . ARG B 1 79  ? 10.824  -25.562 61.920  1.00 33.28  ? 79   ARG B N   1 
ATOM   4324 C  CA  . ARG B 1 79  ? 12.254  -25.287 61.786  1.00 32.09  ? 79   ARG B CA  1 
ATOM   4325 C  C   . ARG B 1 79  ? 12.919  -26.137 60.705  1.00 35.87  ? 79   ARG B C   1 
ATOM   4326 O  O   . ARG B 1 79  ? 13.975  -25.747 60.184  1.00 33.07  ? 79   ARG B O   1 
ATOM   4327 C  CB  . ARG B 1 79  ? 12.947  -25.497 63.139  1.00 29.96  ? 79   ARG B CB  1 
ATOM   4328 C  CG  . ARG B 1 79  ? 14.449  -25.271 63.075  1.00 33.23  ? 79   ARG B CG  1 
ATOM   4329 C  CD  . ARG B 1 79  ? 15.005  -24.951 64.450  1.00 31.21  ? 79   ARG B CD  1 
ATOM   4330 N  NE  . ARG B 1 79  ? 16.468  -24.907 64.412  1.00 36.79  ? 79   ARG B NE  1 
ATOM   4331 C  CZ  . ARG B 1 79  ? 17.206  -24.033 65.083  1.00 38.04  ? 79   ARG B CZ  1 
ATOM   4332 N  NH1 . ARG B 1 79  ? 16.654  -23.081 65.813  1.00 30.50  ? 79   ARG B NH1 1 
ATOM   4333 N  NH2 . ARG B 1 79  ? 18.535  -24.109 65.006  1.00 35.67  ? 79   ARG B NH2 1 
ATOM   4334 N  N   . ASP B 1 80  ? 12.344  -27.292 60.358  1.00 34.29  ? 80   ASP B N   1 
ATOM   4335 C  CA  . ASP B 1 80  ? 12.907  -28.081 59.266  1.00 35.08  ? 80   ASP B CA  1 
ATOM   4336 C  C   . ASP B 1 80  ? 12.963  -27.294 57.963  1.00 37.56  ? 80   ASP B C   1 
ATOM   4337 O  O   . ASP B 1 80  ? 13.802  -27.588 57.102  1.00 37.15  ? 80   ASP B O   1 
ATOM   4338 C  CB  . ASP B 1 80  ? 12.111  -29.372 59.061  1.00 37.09  ? 80   ASP B CB  1 
ATOM   4339 C  CG  . ASP B 1 80  ? 12.382  -30.394 60.146  1.00 43.65  ? 80   ASP B CG  1 
ATOM   4340 O  OD1 . ASP B 1 80  ? 13.434  -30.288 60.798  1.00 43.59  ? 80   ASP B OD1 1 
ATOM   4341 O  OD2 . ASP B 1 80  ? 11.544  -31.291 60.357  1.00 47.70  ? 80   ASP B OD2 1 
ATOM   4342 N  N   . PHE B 1 81  ? 12.096  -26.294 57.780  1.00 32.00  ? 81   PHE B N   1 
ATOM   4343 C  CA  . PHE B 1 81  ? 12.255  -25.429 56.622  1.00 34.10  ? 81   PHE B CA  1 
ATOM   4344 C  C   . PHE B 1 81  ? 12.493  -23.958 56.954  1.00 31.72  ? 81   PHE B C   1 
ATOM   4345 O  O   . PHE B 1 81  ? 13.025  -23.240 56.103  1.00 31.41  ? 81   PHE B O   1 
ATOM   4346 C  CB  . PHE B 1 81  ? 11.058  -25.568 55.657  1.00 34.93  ? 81   PHE B CB  1 
ATOM   4347 C  CG  . PHE B 1 81  ? 9.707   -25.438 56.299  1.00 35.14  ? 81   PHE B CG  1 
ATOM   4348 C  CD1 . PHE B 1 81  ? 9.024   -26.556 56.752  1.00 36.61  ? 81   PHE B CD1 1 
ATOM   4349 C  CD2 . PHE B 1 81  ? 9.087   -24.204 56.386  1.00 30.35  ? 81   PHE B CD2 1 
ATOM   4350 C  CE1 . PHE B 1 81  ? 7.765   -26.443 57.321  1.00 35.02  ? 81   PHE B CE1 1 
ATOM   4351 C  CE2 . PHE B 1 81  ? 7.820   -24.080 56.962  1.00 34.11  ? 81   PHE B CE2 1 
ATOM   4352 C  CZ  . PHE B 1 81  ? 7.158   -25.205 57.430  1.00 35.03  ? 81   PHE B CZ  1 
ATOM   4353 N  N   . ALA B 1 82  ? 12.177  -23.502 58.169  1.00 30.83  ? 82   ALA B N   1 
ATOM   4354 C  CA  . ALA B 1 82  ? 12.447  -22.128 58.562  1.00 30.77  ? 82   ALA B CA  1 
ATOM   4355 C  C   . ALA B 1 82  ? 13.752  -21.955 59.340  1.00 31.38  ? 82   ALA B C   1 
ATOM   4356 O  O   . ALA B 1 82  ? 14.133  -20.814 59.616  1.00 32.99  ? 82   ALA B O   1 
ATOM   4357 C  CB  . ALA B 1 82  ? 11.267  -21.572 59.388  1.00 29.13  ? 82   ALA B CB  1 
ATOM   4358 N  N   . GLY B 1 83  ? 14.433  -23.043 59.702  1.00 31.43  ? 83   GLY B N   1 
ATOM   4359 C  CA  . GLY B 1 83  ? 15.804  -22.938 60.193  1.00 32.19  ? 83   GLY B CA  1 
ATOM   4360 C  C   . GLY B 1 83  ? 15.934  -22.051 61.420  1.00 33.98  ? 83   GLY B C   1 
ATOM   4361 O  O   . GLY B 1 83  ? 15.077  -22.046 62.318  1.00 31.05  ? 83   GLY B O   1 
ATOM   4362 N  N   . ASP B 1 84  ? 17.030  -21.288 61.477  1.00 30.05  ? 84   ASP B N   1 
ATOM   4363 C  CA  . ASP B 1 84  ? 17.213  -20.333 62.570  1.00 31.47  ? 84   ASP B CA  1 
ATOM   4364 C  C   . ASP B 1 84  ? 16.789  -18.932 62.159  1.00 28.45  ? 84   ASP B C   1 
ATOM   4365 O  O   . ASP B 1 84  ? 17.397  -17.937 62.575  1.00 30.46  ? 84   ASP B O   1 
ATOM   4366 C  CB  . ASP B 1 84  ? 18.648  -20.346 63.118  1.00 31.12  ? 84   ASP B CB  1 
ATOM   4367 C  CG  . ASP B 1 84  ? 19.718  -20.037 62.067  1.00 32.88  ? 84   ASP B CG  1 
ATOM   4368 O  OD1 . ASP B 1 84  ? 19.412  -19.889 60.863  1.00 32.37  ? 84   ASP B OD1 1 
ATOM   4369 O  OD2 . ASP B 1 84  ? 20.913  -19.958 62.476  1.00 33.08  ? 84   ASP B OD2 1 
ATOM   4370 N  N   . GLY B 1 85  ? 15.720  -18.842 61.351  1.00 30.23  ? 85   GLY B N   1 
ATOM   4371 C  CA  . GLY B 1 85  ? 15.023  -17.585 61.152  1.00 28.69  ? 85   GLY B CA  1 
ATOM   4372 C  C   . GLY B 1 85  ? 14.424  -17.099 62.462  1.00 32.24  ? 85   GLY B C   1 
ATOM   4373 O  O   . GLY B 1 85  ? 14.443  -17.783 63.483  1.00 30.12  ? 85   GLY B O   1 
ATOM   4374 N  N   . LEU B 1 86  ? 13.866  -15.884 62.424  1.00 28.02  ? 86   LEU B N   1 
ATOM   4375 C  CA  . LEU B 1 86  ? 13.510  -15.213 63.678  1.00 28.68  ? 86   LEU B CA  1 
ATOM   4376 C  C   . LEU B 1 86  ? 12.501  -16.011 64.493  1.00 29.75  ? 86   LEU B C   1 
ATOM   4377 O  O   . LEU B 1 86  ? 12.545  -16.003 65.732  1.00 29.96  ? 86   LEU B O   1 
ATOM   4378 C  CB  . LEU B 1 86  ? 12.953  -13.817 63.393  1.00 29.08  ? 86   LEU B CB  1 
ATOM   4379 C  CG  . LEU B 1 86  ? 13.976  -12.682 63.232  1.00 29.98  ? 86   LEU B CG  1 
ATOM   4380 C  CD1 . LEU B 1 86  ? 13.204  -11.427 62.878  1.00 32.22  ? 86   LEU B CD1 1 
ATOM   4381 C  CD2 . LEU B 1 86  ? 14.820  -12.486 64.509  1.00 30.33  ? 86   LEU B CD2 1 
ATOM   4382 N  N   . ALA B 1 87  ? 11.552  -16.665 63.832  1.00 28.23  ? 87   ALA B N   1 
ATOM   4383 C  CA  . ALA B 1 87  ? 10.461  -17.291 64.583  1.00 27.52  ? 87   ALA B CA  1 
ATOM   4384 C  C   . ALA B 1 87  ? 10.814  -18.667 65.145  1.00 27.97  ? 87   ALA B C   1 
ATOM   4385 O  O   . ALA B 1 87  ? 10.143  -19.141 66.073  1.00 27.95  ? 87   ALA B O   1 
ATOM   4386 C  CB  . ALA B 1 87  ? 9.222   -17.400 63.681  1.00 30.49  ? 87   ALA B CB  1 
ATOM   4387 N  N   . THR B 1 88  ? 11.831  -19.335 64.603  1.00 29.38  ? 88   THR B N   1 
ATOM   4388 C  CA  . THR B 1 88  ? 12.163  -20.692 65.015  1.00 26.73  ? 88   THR B CA  1 
ATOM   4389 C  C   . THR B 1 88  ? 13.573  -20.796 65.584  1.00 27.94  ? 88   THR B C   1 
ATOM   4390 O  O   . THR B 1 88  ? 14.103  -21.907 65.730  1.00 31.38  ? 88   THR B O   1 
ATOM   4391 C  CB  . THR B 1 88  ? 11.986  -21.661 63.840  1.00 27.50  ? 88   THR B CB  1 
ATOM   4392 O  OG1 . THR B 1 88  ? 12.637  -21.134 62.668  1.00 29.39  ? 88   THR B OG1 1 
ATOM   4393 C  CG2 . THR B 1 88  ? 10.505  -21.848 63.547  1.00 30.14  ? 88   THR B CG2 1 
ATOM   4394 N  N   . SER B 1 89  ? 14.183  -19.670 65.911  1.00 29.90  ? 89   SER B N   1 
ATOM   4395 C  CA  . SER B 1 89  ? 15.458  -19.655 66.617  1.00 30.56  ? 89   SER B CA  1 
ATOM   4396 C  C   . SER B 1 89  ? 15.249  -19.566 68.123  1.00 30.26  ? 89   SER B C   1 
ATOM   4397 O  O   . SER B 1 89  ? 14.263  -19.006 68.609  1.00 29.16  ? 89   SER B O   1 
ATOM   4398 C  CB  . SER B 1 89  ? 16.319  -18.488 66.126  1.00 32.61  ? 89   SER B CB  1 
ATOM   4399 O  OG  . SER B 1 89  ? 15.578  -17.281 66.091  1.00 38.92  ? 89   SER B OG  1 
ATOM   4400 N  N   . TRP B 1 90  ? 16.191  -20.145 68.867  1.00 29.60  ? 90   TRP B N   1 
ATOM   4401 C  CA  . TRP B 1 90  ? 16.220  -19.954 70.306  1.00 29.82  ? 90   TRP B CA  1 
ATOM   4402 C  C   . TRP B 1 90  ? 16.805  -18.587 70.614  1.00 31.29  ? 90   TRP B C   1 
ATOM   4403 O  O   . TRP B 1 90  ? 17.642  -18.070 69.866  1.00 29.95  ? 90   TRP B O   1 
ATOM   4404 C  CB  . TRP B 1 90  ? 17.069  -21.030 70.991  1.00 30.23  ? 90   TRP B CB  1 
ATOM   4405 C  CG  . TRP B 1 90  ? 16.609  -22.427 70.747  1.00 31.22  ? 90   TRP B CG  1 
ATOM   4406 C  CD1 . TRP B 1 90  ? 16.982  -23.246 69.729  1.00 31.12  ? 90   TRP B CD1 1 
ATOM   4407 C  CD2 . TRP B 1 90  ? 15.681  -23.174 71.546  1.00 29.92  ? 90   TRP B CD2 1 
ATOM   4408 N  NE1 . TRP B 1 90  ? 16.356  -24.461 69.842  1.00 30.57  ? 90   TRP B NE1 1 
ATOM   4409 C  CE2 . TRP B 1 90  ? 15.550  -24.443 70.950  1.00 32.84  ? 90   TRP B CE2 1 
ATOM   4410 C  CE3 . TRP B 1 90  ? 14.956  -22.891 72.707  1.00 31.89  ? 90   TRP B CE3 1 
ATOM   4411 C  CZ2 . TRP B 1 90  ? 14.712  -25.440 71.472  1.00 35.56  ? 90   TRP B CZ2 1 
ATOM   4412 C  CZ3 . TRP B 1 90  ? 14.123  -23.885 73.238  1.00 33.59  ? 90   TRP B CZ3 1 
ATOM   4413 C  CH2 . TRP B 1 90  ? 14.012  -25.146 72.612  1.00 33.93  ? 90   TRP B CH2 1 
ATOM   4414 N  N   . THR B 1 91  ? 16.356  -18.002 71.722  1.00 28.42  ? 91   THR B N   1 
ATOM   4415 C  CA  . THR B 1 91  ? 16.827  -16.666 72.067  1.00 26.93  ? 91   THR B CA  1 
ATOM   4416 C  C   . THR B 1 91  ? 18.343  -16.629 72.222  1.00 34.16  ? 91   THR B C   1 
ATOM   4417 O  O   . THR B 1 91  ? 18.968  -15.590 71.970  1.00 31.59  ? 91   THR B O   1 
ATOM   4418 C  CB  . THR B 1 91  ? 16.155  -16.193 73.349  1.00 31.48  ? 91   THR B CB  1 
ATOM   4419 O  OG1 . THR B 1 91  ? 14.736  -16.282 73.189  1.00 30.28  ? 91   THR B OG1 1 
ATOM   4420 C  CG2 . THR B 1 91  ? 16.551  -14.756 73.665  1.00 32.92  ? 91   THR B CG2 1 
ATOM   4421 N  N   . HIS B 1 92  ? 18.950  -17.748 72.627  1.00 29.72  ? 92   HIS B N   1 
ATOM   4422 C  CA  . HIS B 1 92  ? 20.383  -17.783 72.872  1.00 28.04  ? 92   HIS B CA  1 
ATOM   4423 C  C   . HIS B 1 92  ? 21.207  -18.096 71.630  1.00 31.58  ? 92   HIS B C   1 
ATOM   4424 O  O   . HIS B 1 92  ? 22.440  -18.017 71.692  1.00 30.83  ? 92   HIS B O   1 
ATOM   4425 C  CB  . HIS B 1 92  ? 20.687  -18.814 73.978  1.00 31.98  ? 92   HIS B CB  1 
ATOM   4426 C  CG  . HIS B 1 92  ? 20.079  -20.162 73.728  1.00 31.59  ? 92   HIS B CG  1 
ATOM   4427 N  ND1 . HIS B 1 92  ? 20.582  -21.043 72.793  1.00 32.43  ? 92   HIS B ND1 1 
ATOM   4428 C  CD2 . HIS B 1 92  ? 19.023  -20.789 74.306  1.00 33.61  ? 92   HIS B CD2 1 
ATOM   4429 C  CE1 . HIS B 1 92  ? 19.852  -22.145 72.792  1.00 33.59  ? 92   HIS B CE1 1 
ATOM   4430 N  NE2 . HIS B 1 92  ? 18.909  -22.022 73.710  1.00 33.04  ? 92   HIS B NE2 1 
ATOM   4431 N  N   . GLU B 1 93  ? 20.579  -18.439 70.505  1.00 30.65  ? 93   GLU B N   1 
ATOM   4432 C  CA  . GLU B 1 93  ? 21.345  -18.634 69.283  1.00 28.69  ? 93   GLU B CA  1 
ATOM   4433 C  C   . GLU B 1 93  ? 21.803  -17.285 68.746  1.00 29.95  ? 93   GLU B C   1 
ATOM   4434 O  O   . GLU B 1 93  ? 21.037  -16.323 68.712  1.00 30.91  ? 93   GLU B O   1 
ATOM   4435 C  CB  . GLU B 1 93  ? 20.519  -19.351 68.221  1.00 30.97  ? 93   GLU B CB  1 
ATOM   4436 C  CG  . GLU B 1 93  ? 20.296  -20.834 68.512  1.00 30.04  ? 93   GLU B CG  1 
ATOM   4437 C  CD  . GLU B 1 93  ? 19.489  -21.487 67.423  1.00 32.47  ? 93   GLU B CD  1 
ATOM   4438 O  OE1 . GLU B 1 93  ? 18.251  -21.307 67.407  1.00 33.40  ? 93   GLU B OE1 1 
ATOM   4439 O  OE2 . GLU B 1 93  ? 20.093  -22.181 66.579  1.00 32.82  ? 93   GLU B OE2 1 
ATOM   4440 N  N   . LYS B 1 94  ? 23.071  -17.217 68.328  1.00 30.44  ? 94   LYS B N   1 
ATOM   4441 C  CA  . LYS B 1 94  ? 23.625  -15.947 67.854  1.00 31.27  ? 94   LYS B CA  1 
ATOM   4442 C  C   . LYS B 1 94  ? 22.727  -15.289 66.804  1.00 28.60  ? 94   LYS B C   1 
ATOM   4443 O  O   . LYS B 1 94  ? 22.536  -14.066 66.815  1.00 31.60  ? 94   LYS B O   1 
ATOM   4444 C  CB  . LYS B 1 94  ? 25.028  -16.185 67.292  1.00 30.70  ? 94   LYS B CB  1 
ATOM   4445 C  CG  . LYS B 1 94  ? 25.658  -14.936 66.634  1.00 31.99  ? 94   LYS B CG  1 
ATOM   4446 C  CD  . LYS B 1 94  ? 27.121  -15.219 66.243  1.00 32.99  ? 94   LYS B CD  1 
ATOM   4447 C  CE  . LYS B 1 94  ? 27.777  -14.033 65.579  1.00 37.28  ? 94   LYS B CE  1 
ATOM   4448 N  NZ  . LYS B 1 94  ? 29.215  -14.350 65.224  1.00 37.43  ? 94   LYS B NZ  1 
ATOM   4449 N  N   . ASN B 1 95  ? 22.148  -16.084 65.898  1.00 30.40  ? 95   ASN B N   1 
ATOM   4450 C  CA  . ASN B 1 95  ? 21.406  -15.475 64.799  1.00 30.80  ? 95   ASN B CA  1 
ATOM   4451 C  C   . ASN B 1 95  ? 20.065  -14.888 65.231  1.00 31.19  ? 95   ASN B C   1 
ATOM   4452 O  O   . ASN B 1 95  ? 19.483  -14.126 64.449  1.00 29.87  ? 95   ASN B O   1 
ATOM   4453 C  CB  . ASN B 1 95  ? 21.172  -16.482 63.673  1.00 29.93  ? 95   ASN B CB  1 
ATOM   4454 C  CG  . ASN B 1 95  ? 22.342  -16.560 62.693  1.00 32.35  ? 95   ASN B CG  1 
ATOM   4455 O  OD1 . ASN B 1 95  ? 23.091  -15.594 62.523  1.00 36.42  ? 95   ASN B OD1 1 
ATOM   4456 N  ND2 . ASN B 1 95  ? 22.503  -17.718 62.045  1.00 30.54  ? 95   ASN B ND2 1 
ATOM   4457 N  N   . TRP B 1 96  ? 19.554  -15.189 66.432  1.00 30.63  ? 96   TRP B N   1 
ATOM   4458 C  CA  . TRP B 1 96  ? 18.299  -14.544 66.825  1.00 30.21  ? 96   TRP B CA  1 
ATOM   4459 C  C   . TRP B 1 96  ? 18.504  -13.046 67.066  1.00 29.56  ? 96   TRP B C   1 
ATOM   4460 O  O   . TRP B 1 96  ? 17.934  -12.203 66.360  1.00 30.13  ? 96   TRP B O   1 
ATOM   4461 C  CB  . TRP B 1 96  ? 17.646  -15.193 68.055  1.00 28.25  ? 96   TRP B CB  1 
ATOM   4462 C  CG  . TRP B 1 96  ? 16.419  -14.359 68.303  1.00 29.84  ? 96   TRP B CG  1 
ATOM   4463 C  CD1 . TRP B 1 96  ? 15.286  -14.328 67.520  1.00 31.29  ? 96   TRP B CD1 1 
ATOM   4464 C  CD2 . TRP B 1 96  ? 16.271  -13.311 69.265  1.00 29.32  ? 96   TRP B CD2 1 
ATOM   4465 N  NE1 . TRP B 1 96  ? 14.428  -13.363 67.978  1.00 29.23  ? 96   TRP B NE1 1 
ATOM   4466 C  CE2 . TRP B 1 96  ? 15.005  -12.717 69.044  1.00 28.36  ? 96   TRP B CE2 1 
ATOM   4467 C  CE3 . TRP B 1 96  ? 17.071  -12.832 70.317  1.00 31.55  ? 96   TRP B CE3 1 
ATOM   4468 C  CZ2 . TRP B 1 96  ? 14.517  -11.660 69.835  1.00 31.28  ? 96   TRP B CZ2 1 
ATOM   4469 C  CZ3 . TRP B 1 96  ? 16.586  -11.786 71.104  1.00 30.76  ? 96   TRP B CZ3 1 
ATOM   4470 C  CH2 . TRP B 1 96  ? 15.306  -11.215 70.856  1.00 30.83  ? 96   TRP B CH2 1 
ATOM   4471 N  N   . LYS B 1 97  ? 19.336  -12.683 68.044  1.00 29.93  ? 97   LYS B N   1 
ATOM   4472 C  CA  . LYS B 1 97  ? 19.484  -11.260 68.339  1.00 30.74  ? 97   LYS B CA  1 
ATOM   4473 C  C   . LYS B 1 97  ? 20.096  -10.519 67.164  1.00 28.57  ? 97   LYS B C   1 
ATOM   4474 O  O   . LYS B 1 97  ? 19.767  -9.349  66.914  1.00 31.52  ? 97   LYS B O   1 
ATOM   4475 C  CB  . LYS B 1 97  ? 20.341  -11.050 69.584  1.00 30.95  ? 97   LYS B CB  1 
ATOM   4476 C  CG  . LYS B 1 97  ? 20.326  -9.598  70.109  1.00 33.29  ? 97   LYS B CG  1 
ATOM   4477 C  CD  . LYS B 1 97  ? 18.914  -9.148  70.519  1.00 37.01  ? 97   LYS B CD  1 
ATOM   4478 C  CE  . LYS B 1 97  ? 18.930  -7.756  71.154  1.00 43.85  ? 97   LYS B CE  1 
ATOM   4479 N  NZ  . LYS B 1 97  ? 19.701  -7.760  72.422  1.00 48.78  ? 97   LYS B NZ  1 
ATOM   4480 N  N   . LYS B 1 98  ? 20.991  -11.177 66.434  1.00 30.20  ? 98   LYS B N   1 
ATOM   4481 C  CA  . LYS B 1 98  ? 21.611  -10.536 65.280  1.00 29.02  ? 98   LYS B CA  1 
ATOM   4482 C  C   . LYS B 1 98  ? 20.568  -10.148 64.241  1.00 33.53  ? 98   LYS B C   1 
ATOM   4483 O  O   . LYS B 1 98  ? 20.509  -8.989  63.801  1.00 30.54  ? 98   LYS B O   1 
ATOM   4484 C  CB  . LYS B 1 98  ? 22.662  -11.475 64.691  1.00 35.08  ? 98   LYS B CB  1 
ATOM   4485 C  CG  . LYS B 1 98  ? 23.354  -10.963 63.481  1.00 36.91  ? 98   LYS B CG  1 
ATOM   4486 C  CD  . LYS B 1 98  ? 24.455  -11.941 63.109  1.00 34.81  ? 98   LYS B CD  1 
ATOM   4487 C  CE  . LYS B 1 98  ? 24.979  -11.675 61.734  1.00 33.62  ? 98   LYS B CE  1 
ATOM   4488 N  NZ  . LYS B 1 98  ? 26.043  -12.661 61.451  1.00 32.77  ? 98   LYS B NZ  1 
ATOM   4489 N  N   . ALA B 1 99  ? 19.733  -11.111 63.828  1.00 31.69  ? 99   ALA B N   1 
ATOM   4490 C  CA  . ALA B 1 99  ? 18.691  -10.809 62.852  1.00 31.46  ? 99   ALA B CA  1 
ATOM   4491 C  C   . ALA B 1 99  ? 17.665  -9.836  63.422  1.00 29.54  ? 99   ALA B C   1 
ATOM   4492 O  O   . ALA B 1 99  ? 17.151  -8.968  62.694  1.00 30.97  ? 99   ALA B O   1 
ATOM   4493 C  CB  . ALA B 1 99  ? 18.002  -12.102 62.395  1.00 29.41  ? 99   ALA B CB  1 
ATOM   4494 N  N   . HIS B 1 100 ? 17.342  -9.974  64.712  1.00 28.93  ? 100  HIS B N   1 
ATOM   4495 C  CA  . HIS B 1 100 ? 16.419  -9.051  65.359  1.00 32.74  ? 100  HIS B CA  1 
ATOM   4496 C  C   . HIS B 1 100 ? 16.932  -7.622  65.260  1.00 34.39  ? 100  HIS B C   1 
ATOM   4497 O  O   . HIS B 1 100 ? 16.202  -6.719  64.852  1.00 32.60  ? 100  HIS B O   1 
ATOM   4498 C  CB  . HIS B 1 100 ? 16.201  -9.475  66.819  1.00 30.03  ? 100  HIS B CB  1 
ATOM   4499 C  CG  . HIS B 1 100 ? 15.404  -8.504  67.632  1.00 37.84  ? 100  HIS B CG  1 
ATOM   4500 N  ND1 . HIS B 1 100 ? 14.023  -8.484  67.624  1.00 37.46  ? 100  HIS B ND1 1 
ATOM   4501 C  CD2 . HIS B 1 100 ? 15.790  -7.549  68.514  1.00 37.82  ? 100  HIS B CD2 1 
ATOM   4502 C  CE1 . HIS B 1 100 ? 13.595  -7.550  68.456  1.00 38.89  ? 100  HIS B CE1 1 
ATOM   4503 N  NE2 . HIS B 1 100 ? 14.646  -6.964  69.005  1.00 41.48  ? 100  HIS B NE2 1 
ATOM   4504 N  N   . ASN B 1 101 ? 18.206  -7.397  65.604  1.00 30.29  ? 101  ASN B N   1 
ATOM   4505 C  CA  . ASN B 1 101 ? 18.745  -6.043  65.523  1.00 33.20  ? 101  ASN B CA  1 
ATOM   4506 C  C   . ASN B 1 101 ? 18.741  -5.528  64.089  1.00 30.74  ? 101  ASN B C   1 
ATOM   4507 O  O   . ASN B 1 101 ? 18.510  -4.338  63.842  1.00 35.19  ? 101  ASN B O   1 
ATOM   4508 C  CB  . ASN B 1 101 ? 20.166  -6.018  66.100  1.00 30.73  ? 101  ASN B CB  1 
ATOM   4509 C  CG  . ASN B 1 101 ? 20.182  -6.144  67.617  1.00 33.02  ? 101  ASN B CG  1 
ATOM   4510 O  OD1 . ASN B 1 101 ? 19.179  -5.903  68.287  1.00 35.63  ? 101  ASN B OD1 1 
ATOM   4511 N  ND2 . ASN B 1 101 ? 21.345  -6.495  68.176  1.00 33.46  ? 101  ASN B ND2 1 
ATOM   4512 N  N   . ILE B 1 102 ? 19.007  -6.410  63.136  1.00 30.84  ? 102  ILE B N   1 
ATOM   4513 C  CA  . ILE B 1 102 ? 19.131  -5.996  61.748  1.00 30.38  ? 102  ILE B CA  1 
ATOM   4514 C  C   . ILE B 1 102 ? 17.769  -5.663  61.159  1.00 35.21  ? 102  ILE B C   1 
ATOM   4515 O  O   . ILE B 1 102 ? 17.638  -4.729  60.358  1.00 35.35  ? 102  ILE B O   1 
ATOM   4516 C  CB  . ILE B 1 102 ? 19.849  -7.084  60.928  1.00 30.78  ? 102  ILE B CB  1 
ATOM   4517 C  CG1 . ILE B 1 102 ? 21.342  -7.144  61.319  1.00 32.96  ? 102  ILE B CG1 1 
ATOM   4518 C  CG2 . ILE B 1 102 ? 19.677  -6.845  59.438  1.00 36.03  ? 102  ILE B CG2 1 
ATOM   4519 C  CD1 . ILE B 1 102 ? 22.088  -8.303  60.732  1.00 33.62  ? 102  ILE B CD1 1 
ATOM   4520 N  N   . LEU B 1 103 ? 16.736  -6.414  61.538  1.00 32.11  ? 103  LEU B N   1 
ATOM   4521 C  CA  . LEU B 1 103 ? 15.446  -6.290  60.870  1.00 32.24  ? 103  LEU B CA  1 
ATOM   4522 C  C   . LEU B 1 103 ? 14.438  -5.434  61.623  1.00 35.45  ? 103  LEU B C   1 
ATOM   4523 O  O   . LEU B 1 103 ? 13.467  -4.981  61.004  1.00 35.05  ? 103  LEU B O   1 
ATOM   4524 C  CB  . LEU B 1 103 ? 14.846  -7.684  60.620  1.00 30.07  ? 103  LEU B CB  1 
ATOM   4525 C  CG  . LEU B 1 103 ? 15.703  -8.548  59.686  1.00 35.04  ? 103  LEU B CG  1 
ATOM   4526 C  CD1 . LEU B 1 103 ? 15.203  -9.985  59.615  1.00 33.71  ? 103  LEU B CD1 1 
ATOM   4527 C  CD2 . LEU B 1 103 ? 15.767  -7.957  58.268  1.00 37.81  ? 103  LEU B CD2 1 
ATOM   4528 N  N   . LEU B 1 104 ? 14.637  -5.175  62.917  1.00 31.71  ? 104  LEU B N   1 
ATOM   4529 C  CA  . LEU B 1 104 ? 13.646  -4.392  63.659  1.00 34.99  ? 104  LEU B CA  1 
ATOM   4530 C  C   . LEU B 1 104 ? 13.382  -3.038  63.008  1.00 40.63  ? 104  LEU B C   1 
ATOM   4531 O  O   . LEU B 1 104 ? 12.209  -2.619  62.964  1.00 37.44  ? 104  LEU B O   1 
ATOM   4532 C  CB  . LEU B 1 104 ? 14.093  -4.214  65.120  1.00 37.92  ? 104  LEU B CB  1 
ATOM   4533 C  CG  . LEU B 1 104 ? 13.077  -3.635  66.108  1.00 39.86  ? 104  LEU B CG  1 
ATOM   4534 C  CD1 . LEU B 1 104 ? 11.839  -4.535  66.221  1.00 41.64  ? 104  LEU B CD1 1 
ATOM   4535 C  CD2 . LEU B 1 104 ? 13.701  -3.368  67.497  1.00 42.32  ? 104  LEU B CD2 1 
ATOM   4536 N  N   . PRO B 1 105 ? 14.388  -2.325  62.492  1.00 40.33  ? 105  PRO B N   1 
ATOM   4537 C  CA  . PRO B 1 105 ? 14.112  -1.053  61.803  1.00 43.20  ? 105  PRO B CA  1 
ATOM   4538 C  C   . PRO B 1 105 ? 13.187  -1.183  60.607  1.00 44.01  ? 105  PRO B C   1 
ATOM   4539 O  O   . PRO B 1 105 ? 12.531  -0.196  60.253  1.00 47.85  ? 105  PRO B O   1 
ATOM   4540 C  CB  . PRO B 1 105 ? 15.507  -0.584  61.369  1.00 46.04  ? 105  PRO B CB  1 
ATOM   4541 C  CG  . PRO B 1 105 ? 16.425  -1.163  62.420  1.00 41.92  ? 105  PRO B CG  1 
ATOM   4542 C  CD  . PRO B 1 105 ? 15.836  -2.530  62.718  1.00 37.75  ? 105  PRO B CD  1 
ATOM   4543 N  N   . SER B 1 106 ? 13.126  -2.352  59.961  1.00 35.62  ? 106  SER B N   1 
ATOM   4544 C  CA  . SER B 1 106 ? 12.250  -2.532  58.809  1.00 37.41  ? 106  SER B CA  1 
ATOM   4545 C  C   . SER B 1 106 ? 10.794  -2.498  59.190  1.00 36.01  ? 106  SER B C   1 
ATOM   4546 O  O   . SER B 1 106 ? 9.930   -2.580  58.307  1.00 35.73  ? 106  SER B O   1 
ATOM   4547 C  CB  . SER B 1 106 ? 12.553  -3.853  58.106  1.00 39.68  ? 106  SER B CB  1 
ATOM   4548 O  OG  . SER B 1 106 ? 13.855  -3.823  57.561  1.00 48.65  ? 106  SER B OG  1 
ATOM   4549 N  N   . PHE B 1 107 ? 10.512  -2.391  60.478  1.00 35.42  ? 107  PHE B N   1 
ATOM   4550 C  CA  . PHE B 1 107 ? 9.150   -2.312  60.971  1.00 41.62  ? 107  PHE B CA  1 
ATOM   4551 C  C   . PHE B 1 107 ? 8.961   -1.053  61.817  1.00 39.10  ? 107  PHE B C   1 
ATOM   4552 O  O   . PHE B 1 107 ? 8.146   -1.031  62.735  1.00 50.68  ? 107  PHE B O   1 
ATOM   4553 C  CB  . PHE B 1 107 ? 8.807   -3.596  61.722  1.00 41.30  ? 107  PHE B CB  1 
ATOM   4554 C  CG  . PHE B 1 107 ? 8.878   -4.815  60.848  1.00 38.37  ? 107  PHE B CG  1 
ATOM   4555 C  CD1 . PHE B 1 107 ? 7.795   -5.166  60.040  1.00 38.02  ? 107  PHE B CD1 1 
ATOM   4556 C  CD2 . PHE B 1 107 ? 10.037  -5.564  60.753  1.00 37.72  ? 107  PHE B CD2 1 
ATOM   4557 C  CE1 . PHE B 1 107 ? 7.866   -6.266  59.200  1.00 39.00  ? 107  PHE B CE1 1 
ATOM   4558 C  CE2 . PHE B 1 107 ? 10.120  -6.653  59.902  1.00 37.32  ? 107  PHE B CE2 1 
ATOM   4559 C  CZ  . PHE B 1 107 ? 9.025   -7.016  59.132  1.00 42.44  ? 107  PHE B CZ  1 
ATOM   4560 N  N   . SER B 1 108 ? 9.689   0.013   61.484  1.00 45.56  ? 108  SER B N   1 
ATOM   4561 C  CA  . SER B 1 108 ? 9.520   1.328   62.097  1.00 46.39  ? 108  SER B CA  1 
ATOM   4562 C  C   . SER B 1 108 ? 8.463   2.138   61.344  1.00 52.19  ? 108  SER B C   1 
ATOM   4563 O  O   . SER B 1 108 ? 8.153   1.872   60.178  1.00 47.59  ? 108  SER B O   1 
ATOM   4564 C  CB  . SER B 1 108 ? 10.837  2.101   62.101  1.00 49.08  ? 108  SER B CB  1 
ATOM   4565 O  OG  . SER B 1 108 ? 11.195  2.500   60.786  1.00 52.83  ? 108  SER B OG  1 
ATOM   4566 N  N   . GLN B 1 109 ? 7.923   3.160   62.018  1.00 52.91  ? 109  GLN B N   1 
ATOM   4567 C  CA  . GLN B 1 109 ? 6.896   3.975   61.378  1.00 51.01  ? 109  GLN B CA  1 
ATOM   4568 C  C   . GLN B 1 109 ? 7.389   4.511   60.036  1.00 48.27  ? 109  GLN B C   1 
ATOM   4569 O  O   . GLN B 1 109 ? 6.668   4.469   59.032  1.00 48.35  ? 109  GLN B O   1 
ATOM   4570 C  CB  . GLN B 1 109 ? 6.459   5.130   62.284  1.00 63.17  ? 109  GLN B CB  1 
ATOM   4571 C  CG  . GLN B 1 109 ? 7.483   6.245   62.428  1.00 64.58  ? 109  GLN B CG  1 
ATOM   4572 C  CD  . GLN B 1 109 ? 6.831   7.610   62.623  1.00 68.74  ? 109  GLN B CD  1 
ATOM   4573 O  OE1 . GLN B 1 109 ? 5.819   7.740   63.317  1.00 70.68  ? 109  GLN B OE1 1 
ATOM   4574 N  NE2 . GLN B 1 109 ? 7.397   8.630   61.986  1.00 71.51  ? 109  GLN B NE2 1 
ATOM   4575 N  N   . GLN B 1 110 ? 8.618   5.029   59.994  1.00 51.89  ? 110  GLN B N   1 
ATOM   4576 C  CA  . GLN B 1 110 ? 9.151   5.484   58.714  1.00 52.89  ? 110  GLN B CA  1 
ATOM   4577 C  C   . GLN B 1 110 ? 9.070   4.368   57.677  1.00 54.81  ? 110  GLN B C   1 
ATOM   4578 O  O   . GLN B 1 110 ? 8.787   4.617   56.496  1.00 45.47  ? 110  GLN B O   1 
ATOM   4579 C  CB  . GLN B 1 110 ? 10.593  5.975   58.874  1.00 59.15  ? 110  GLN B CB  1 
ATOM   4580 C  CG  . GLN B 1 110 ? 11.290  6.251   57.539  1.00 63.63  ? 110  GLN B CG  1 
ATOM   4581 C  CD  . GLN B 1 110 ? 12.232  7.441   57.592  1.00 76.82  ? 110  GLN B CD  1 
ATOM   4582 O  OE1 . GLN B 1 110 ? 11.973  8.429   58.284  1.00 83.99  ? 110  GLN B OE1 1 
ATOM   4583 N  NE2 . GLN B 1 110 ? 13.335  7.353   56.856  1.00 79.70  ? 110  GLN B NE2 1 
ATOM   4584 N  N   . ALA B 1 111 ? 9.294   3.123   58.115  1.00 51.08  ? 111  ALA B N   1 
ATOM   4585 C  CA  . ALA B 1 111 ? 9.187   1.975   57.223  1.00 49.25  ? 111  ALA B CA  1 
ATOM   4586 C  C   . ALA B 1 111 ? 7.738   1.712   56.811  1.00 36.30  ? 111  ALA B C   1 
ATOM   4587 O  O   . ALA B 1 111 ? 7.478   1.422   55.641  1.00 42.09  ? 111  ALA B O   1 
ATOM   4588 C  CB  . ALA B 1 111 ? 9.791   0.738   57.892  1.00 43.76  ? 111  ALA B CB  1 
ATOM   4589 N  N   . MET B 1 112 ? 6.789   1.783   57.747  1.00 41.26  ? 112  MET B N   1 
ATOM   4590 C  CA  . MET B 1 112 ? 5.397   1.538   57.364  1.00 43.66  ? 112  MET B CA  1 
ATOM   4591 C  C   . MET B 1 112 ? 4.838   2.629   56.465  1.00 38.71  ? 112  MET B C   1 
ATOM   4592 O  O   . MET B 1 112 ? 4.026   2.342   55.572  1.00 35.80  ? 112  MET B O   1 
ATOM   4593 C  CB  . MET B 1 112 ? 4.504   1.339   58.582  1.00 46.71  ? 112  MET B CB  1 
ATOM   4594 C  CG  . MET B 1 112 ? 5.036   0.297   59.517  1.00 54.01  ? 112  MET B CG  1 
ATOM   4595 S  SD  . MET B 1 112 ? 4.388   -1.278  58.885  1.00 40.76  ? 112  MET B SD  1 
ATOM   4596 C  CE  . MET B 1 112 ? 2.842   -0.778  58.148  1.00 46.47  ? 112  MET B CE  1 
ATOM   4597 N  N   . LYS B 1 113 ? 5.230   3.886   56.682  1.00 37.99  ? 113  LYS B N   1 
ATOM   4598 C  CA  . LYS B 1 113 ? 4.884   4.896   55.693  1.00 35.30  ? 113  LYS B CA  1 
ATOM   4599 C  C   . LYS B 1 113 ? 5.426   4.514   54.333  1.00 37.55  ? 113  LYS B C   1 
ATOM   4600 O  O   . LYS B 1 113 ? 4.785   4.777   53.310  1.00 37.79  ? 113  LYS B O   1 
ATOM   4601 C  CB  . LYS B 1 113 ? 5.416   6.268   56.110  1.00 36.58  ? 113  LYS B CB  1 
ATOM   4602 C  CG  . LYS B 1 113 ? 4.832   6.727   57.418  1.00 39.41  ? 113  LYS B CG  1 
ATOM   4603 C  CD  . LYS B 1 113 ? 5.561   7.929   57.983  1.00 43.95  ? 113  LYS B CD  1 
ATOM   4604 C  CE  . LYS B 1 113 ? 4.851   8.440   59.240  1.00 50.23  ? 113  LYS B CE  1 
ATOM   4605 N  NZ  . LYS B 1 113 ? 5.267   9.820   59.620  1.00 56.24  ? 113  LYS B NZ  1 
ATOM   4606 N  N   . GLY B 1 114 ? 6.593   3.866   54.306  1.00 35.19  ? 114  GLY B N   1 
ATOM   4607 C  CA  . GLY B 1 114 ? 7.193   3.475   53.047  1.00 36.32  ? 114  GLY B CA  1 
ATOM   4608 C  C   . GLY B 1 114 ? 6.559   2.250   52.418  1.00 39.02  ? 114  GLY B C   1 
ATOM   4609 O  O   . GLY B 1 114 ? 6.595   2.101   51.194  1.00 39.07  ? 114  GLY B O   1 
ATOM   4610 N  N   . TYR B 1 115 ? 5.973   1.359   53.231  1.00 35.51  ? 115  TYR B N   1 
ATOM   4611 C  CA  . TYR B 1 115 ? 5.282   0.193   52.676  1.00 33.88  ? 115  TYR B CA  1 
ATOM   4612 C  C   . TYR B 1 115 ? 3.886   0.528   52.189  1.00 32.82  ? 115  TYR B C   1 
ATOM   4613 O  O   . TYR B 1 115 ? 3.299   -0.259  51.435  1.00 32.28  ? 115  TYR B O   1 
ATOM   4614 C  CB  . TYR B 1 115 ? 5.133   -0.919  53.724  1.00 31.98  ? 115  TYR B CB  1 
ATOM   4615 C  CG  . TYR B 1 115 ? 6.410   -1.509  54.247  1.00 33.05  ? 115  TYR B CG  1 
ATOM   4616 C  CD1 . TYR B 1 115 ? 7.451   -1.827  53.392  1.00 36.07  ? 115  TYR B CD1 1 
ATOM   4617 C  CD2 . TYR B 1 115 ? 6.576   -1.738  55.604  1.00 33.56  ? 115  TYR B CD2 1 
ATOM   4618 C  CE1 . TYR B 1 115 ? 8.628   -2.367  53.874  1.00 39.47  ? 115  TYR B CE1 1 
ATOM   4619 C  CE2 . TYR B 1 115 ? 7.741   -2.275  56.099  1.00 34.43  ? 115  TYR B CE2 1 
ATOM   4620 C  CZ  . TYR B 1 115 ? 8.766   -2.593  55.228  1.00 37.12  ? 115  TYR B CZ  1 
ATOM   4621 O  OH  . TYR B 1 115 ? 9.943   -3.130  55.727  1.00 39.31  ? 115  TYR B OH  1 
ATOM   4622 N  N   . HIS B 1 116 ? 3.343   1.657   52.637  1.00 30.74  ? 116  HIS B N   1 
ATOM   4623 C  CA  . HIS B 1 116 ? 1.922   1.935   52.459  1.00 30.32  ? 116  HIS B CA  1 
ATOM   4624 C  C   . HIS B 1 116 ? 1.493   1.871   50.995  1.00 32.29  ? 116  HIS B C   1 
ATOM   4625 O  O   . HIS B 1 116 ? 0.465   1.263   50.666  1.00 32.27  ? 116  HIS B O   1 
ATOM   4626 C  CB  . HIS B 1 116 ? 1.603   3.300   53.053  1.00 31.72  ? 116  HIS B CB  1 
ATOM   4627 C  CG  . HIS B 1 116 ? 0.173   3.671   52.905  1.00 31.34  ? 116  HIS B CG  1 
ATOM   4628 N  ND1 . HIS B 1 116 ? -0.778  3.326   53.837  1.00 29.78  ? 116  HIS B ND1 1 
ATOM   4629 C  CD2 . HIS B 1 116 ? -0.483  4.297   51.903  1.00 30.60  ? 116  HIS B CD2 1 
ATOM   4630 C  CE1 . HIS B 1 116 ? -1.960  3.747   53.426  1.00 31.73  ? 116  HIS B CE1 1 
ATOM   4631 N  NE2 . HIS B 1 116 ? -1.807  4.343   52.258  1.00 29.80  ? 116  HIS B NE2 1 
ATOM   4632 N  N   . ALA B 1 117 ? 2.224   2.545   50.103  1.00 31.32  ? 117  ALA B N   1 
ATOM   4633 C  CA  . ALA B 1 117 ? 1.783   2.599   48.708  1.00 34.06  ? 117  ALA B CA  1 
ATOM   4634 C  C   . ALA B 1 117 ? 1.668   1.202   48.107  1.00 33.52  ? 117  ALA B C   1 
ATOM   4635 O  O   . ALA B 1 117 ? 0.765   0.931   47.302  1.00 31.62  ? 117  ALA B O   1 
ATOM   4636 C  CB  . ALA B 1 117 ? 2.746   3.453   47.877  1.00 34.99  ? 117  ALA B CB  1 
ATOM   4637 N  N   . MET B 1 118 ? 2.598   0.308   48.453  1.00 30.09  ? 118  MET B N   1 
ATOM   4638 C  CA  . MET B 1 118 ? 2.545   -1.035  47.894  1.00 34.25  ? 118  MET B CA  1 
ATOM   4639 C  C   . MET B 1 118 ? 1.418   -1.848  48.526  1.00 29.54  ? 118  MET B C   1 
ATOM   4640 O  O   . MET B 1 118 ? 0.846   -2.729  47.878  1.00 31.64  ? 118  MET B O   1 
ATOM   4641 C  CB  . MET B 1 118 ? 3.888   -1.741  48.080  1.00 36.05  ? 118  MET B CB  1 
ATOM   4642 C  CG  . MET B 1 118 ? 4.895   -1.445  46.980  1.00 38.61  ? 118  MET B CG  1 
ATOM   4643 S  SD  . MET B 1 118 ? 6.585   -1.825  47.467  1.00 48.20  ? 118  MET B SD  1 
ATOM   4644 C  CE  . MET B 1 118 ? 7.460   -1.464  45.933  1.00 49.60  ? 118  MET B CE  1 
ATOM   4645 N  N   . MET B 1 119 ? 1.094   -1.590  49.793  1.00 29.43  ? 119  MET B N   1 
ATOM   4646 C  CA  . MET B 1 119 ? -0.085  -2.236  50.345  1.00 27.48  ? 119  MET B CA  1 
ATOM   4647 C  C   . MET B 1 119 ? -1.323  -1.811  49.577  1.00 29.78  ? 119  MET B C   1 
ATOM   4648 O  O   . MET B 1 119 ? -2.198  -2.635  49.281  1.00 28.91  ? 119  MET B O   1 
ATOM   4649 C  CB  . MET B 1 119 ? -0.244  -1.882  51.815  1.00 27.18  ? 119  MET B CB  1 
ATOM   4650 C  CG  . MET B 1 119 ? 0.746   -2.631  52.714  1.00 31.50  ? 119  MET B CG  1 
ATOM   4651 S  SD  . MET B 1 119 ? 0.397   -2.220  54.416  1.00 30.69  ? 119  MET B SD  1 
ATOM   4652 C  CE  . MET B 1 119 ? 1.844   -2.890  55.229  1.00 28.39  ? 119  MET B CE  1 
ATOM   4653 N  N   . VAL B 1 120 ? -1.408  -0.523  49.242  1.00 29.98  ? 120  VAL B N   1 
ATOM   4654 C  CA  . VAL B 1 120 ? -2.558  -0.024  48.490  1.00 28.72  ? 120  VAL B CA  1 
ATOM   4655 C  C   . VAL B 1 120 ? -2.636  -0.705  47.130  1.00 30.11  ? 120  VAL B C   1 
ATOM   4656 O  O   . VAL B 1 120 ? -3.728  -1.032  46.645  1.00 30.30  ? 120  VAL B O   1 
ATOM   4657 C  CB  . VAL B 1 120 ? -2.485  1.512   48.359  1.00 31.50  ? 120  VAL B CB  1 
ATOM   4658 C  CG1 . VAL B 1 120 ? -3.587  2.032   47.422  1.00 34.07  ? 120  VAL B CG1 1 
ATOM   4659 C  CG2 . VAL B 1 120 ? -2.623  2.180   49.729  1.00 31.28  ? 120  VAL B CG2 1 
ATOM   4660 N  N   . ASP B 1 121 ? -1.481  -0.933  46.498  1.00 29.55  ? 121  ASP B N   1 
ATOM   4661 C  CA  . ASP B 1 121 ? -1.447  -1.582  45.188  1.00 30.56  ? 121  ASP B CA  1 
ATOM   4662 C  C   . ASP B 1 121 ? -2.198  -2.911  45.221  1.00 31.83  ? 121  ASP B C   1 
ATOM   4663 O  O   . ASP B 1 121 ? -3.091  -3.165  44.399  1.00 32.39  ? 121  ASP B O   1 
ATOM   4664 C  CB  . ASP B 1 121 ? 0.022   -1.776  44.768  1.00 29.20  ? 121  ASP B CB  1 
ATOM   4665 C  CG  . ASP B 1 121 ? 0.184   -2.430  43.386  1.00 35.31  ? 121  ASP B CG  1 
ATOM   4666 O  OD1 . ASP B 1 121 ? -0.277  -3.583  43.187  1.00 32.40  ? 121  ASP B OD1 1 
ATOM   4667 O  OD2 . ASP B 1 121 ? 0.817   -1.792  42.508  1.00 34.50  ? 121  ASP B OD2 1 
ATOM   4668 N  N   . ILE B 1 122 ? -1.895  -3.750  46.218  1.00 28.83  ? 122  ILE B N   1 
ATOM   4669 C  CA  . ILE B 1 122 ? -2.534  -5.056  46.284  1.00 29.64  ? 122  ILE B CA  1 
ATOM   4670 C  C   . ILE B 1 122 ? -3.990  -4.920  46.714  1.00 29.77  ? 122  ILE B C   1 
ATOM   4671 O  O   . ILE B 1 122 ? -4.870  -5.644  46.219  1.00 29.19  ? 122  ILE B O   1 
ATOM   4672 C  CB  . ILE B 1 122 ? -1.755  -5.985  47.232  1.00 28.23  ? 122  ILE B CB  1 
ATOM   4673 C  CG1 . ILE B 1 122 ? -0.256  -6.028  46.868  1.00 29.22  ? 122  ILE B CG1 1 
ATOM   4674 C  CG2 . ILE B 1 122 ? -2.401  -7.371  47.243  1.00 29.99  ? 122  ILE B CG2 1 
ATOM   4675 C  CD1 . ILE B 1 122 ? 0.032   -6.406  45.401  1.00 28.27  ? 122  ILE B CD1 1 
ATOM   4676 N  N   . ALA B 1 123 ? -4.261  -4.017  47.659  1.00 30.55  ? 123  ALA B N   1 
ATOM   4677 C  CA  . ALA B 1 123 ? -5.628  -3.800  48.124  1.00 29.25  ? 123  ALA B CA  1 
ATOM   4678 C  C   . ALA B 1 123 ? -6.527  -3.379  46.977  1.00 29.89  ? 123  ALA B C   1 
ATOM   4679 O  O   . ALA B 1 123 ? -7.660  -3.852  46.865  1.00 30.94  ? 123  ALA B O   1 
ATOM   4680 C  CB  . ALA B 1 123 ? -5.650  -2.746  49.239  1.00 29.60  ? 123  ALA B CB  1 
ATOM   4681 N  N   . VAL B 1 124 ? -6.032  -2.499  46.105  1.00 30.49  ? 124  VAL B N   1 
ATOM   4682 C  CA  . VAL B 1 124 ? -6.817  -2.089  44.942  1.00 29.77  ? 124  VAL B CA  1 
ATOM   4683 C  C   . VAL B 1 124 ? -7.081  -3.280  44.022  1.00 27.26  ? 124  VAL B C   1 
ATOM   4684 O  O   . VAL B 1 124 ? -8.189  -3.434  43.495  1.00 30.12  ? 124  VAL B O   1 
ATOM   4685 C  CB  . VAL B 1 124 ? -6.114  -0.932  44.213  1.00 30.97  ? 124  VAL B CB  1 
ATOM   4686 C  CG1 . VAL B 1 124 ? -6.774  -0.683  42.857  1.00 30.29  ? 124  VAL B CG1 1 
ATOM   4687 C  CG2 . VAL B 1 124 ? -6.159  0.332   45.080  1.00 31.83  ? 124  VAL B CG2 1 
ATOM   4688 N  N   . GLN B 1 125 ? -6.090  -4.169  43.837  1.00 28.41  ? 125  GLN B N   1 
ATOM   4689 C  CA  . GLN B 1 125 ? -6.359  -5.368  43.039  1.00 31.23  ? 125  GLN B CA  1 
ATOM   4690 C  C   . GLN B 1 125 ? -7.492  -6.190  43.635  1.00 33.43  ? 125  GLN B C   1 
ATOM   4691 O  O   . GLN B 1 125 ? -8.316  -6.742  42.899  1.00 30.09  ? 125  GLN B O   1 
ATOM   4692 C  CB  . GLN B 1 125 ? -5.106  -6.236  42.896  1.00 29.34  ? 125  GLN B CB  1 
ATOM   4693 C  CG  . GLN B 1 125 ? -4.001  -5.539  42.130  1.00 30.01  ? 125  GLN B CG  1 
ATOM   4694 C  CD  . GLN B 1 125 ? -2.856  -6.480  41.829  1.00 31.76  ? 125  GLN B CD  1 
ATOM   4695 O  OE1 . GLN B 1 125 ? -3.076  -7.595  41.368  1.00 28.99  ? 125  GLN B OE1 1 
ATOM   4696 N  NE2 . GLN B 1 125 ? -1.623  -6.035  42.084  1.00 29.05  ? 125  GLN B NE2 1 
ATOM   4697 N  N   . LEU B 1 126 ? -7.548  -6.291  44.969  1.00 30.94  ? 126  LEU B N   1 
ATOM   4698 C  CA  . LEU B 1 126 ? -8.645  -7.013  45.611  1.00 28.77  ? 126  LEU B CA  1 
ATOM   4699 C  C   . LEU B 1 126 ? -9.991  -6.361  45.315  1.00 29.41  ? 126  LEU B C   1 
ATOM   4700 O  O   . LEU B 1 126 ? -10.951 -7.033  44.906  1.00 30.00  ? 126  LEU B O   1 
ATOM   4701 C  CB  . LEU B 1 126 ? -8.419  -7.078  47.124  1.00 27.19  ? 126  LEU B CB  1 
ATOM   4702 C  CG  . LEU B 1 126 ? -9.625  -7.707  47.844  1.00 31.16  ? 126  LEU B CG  1 
ATOM   4703 C  CD1 . LEU B 1 126 ? -9.660  -9.218  47.634  1.00 31.12  ? 126  LEU B CD1 1 
ATOM   4704 C  CD2 . LEU B 1 126 ? -9.582  -7.393  49.326  1.00 34.90  ? 126  LEU B CD2 1 
ATOM   4705 N  N   . VAL B 1 127 ? -10.094 -5.054  45.553  1.00 30.43  ? 127  VAL B N   1 
ATOM   4706 C  CA  . VAL B 1 127 ? -11.367 -4.369  45.331  1.00 27.80  ? 127  VAL B CA  1 
ATOM   4707 C  C   . VAL B 1 127 ? -11.795 -4.518  43.870  1.00 31.12  ? 127  VAL B C   1 
ATOM   4708 O  O   . VAL B 1 127 ? -12.967 -4.782  43.569  1.00 30.93  ? 127  VAL B O   1 
ATOM   4709 C  CB  . VAL B 1 127 ? -11.240 -2.892  45.756  1.00 28.61  ? 127  VAL B CB  1 
ATOM   4710 C  CG1 . VAL B 1 127 ? -12.463 -2.079  45.339  1.00 28.78  ? 127  VAL B CG1 1 
ATOM   4711 C  CG2 . VAL B 1 127 ? -11.020 -2.784  47.280  1.00 30.53  ? 127  VAL B CG2 1 
ATOM   4712 N  N   . GLN B 1 128 ? -10.846 -4.378  42.938  1.00 29.45  ? 128  GLN B N   1 
ATOM   4713 C  CA  . GLN B 1 128 ? -11.186 -4.510  41.521  1.00 30.01  ? 128  GLN B CA  1 
ATOM   4714 C  C   . GLN B 1 128 ? -11.668 -5.912  41.190  1.00 30.82  ? 128  GLN B C   1 
ATOM   4715 O  O   . GLN B 1 128 ? -12.603 -6.084  40.392  1.00 29.26  ? 128  GLN B O   1 
ATOM   4716 C  CB  . GLN B 1 128 ? -9.985  -4.132  40.655  1.00 29.67  ? 128  GLN B CB  1 
ATOM   4717 C  CG  . GLN B 1 128 ? -9.740  -2.647  40.691  1.00 34.92  ? 128  GLN B CG  1 
ATOM   4718 C  CD  . GLN B 1 128 ? -8.713  -2.166  39.714  1.00 46.29  ? 128  GLN B CD  1 
ATOM   4719 O  OE1 . GLN B 1 128 ? -7.642  -2.759  39.573  1.00 48.13  ? 128  GLN B OE1 1 
ATOM   4720 N  NE2 . GLN B 1 128 ? -9.021  -1.058  39.038  1.00 50.85  ? 128  GLN B NE2 1 
ATOM   4721 N  N   . LYS B 1 129 ? -11.044 -6.936  41.775  1.00 29.79  ? 129  LYS B N   1 
ATOM   4722 C  CA  . LYS B 1 129 ? -11.515 -8.293  41.528  1.00 28.54  ? 129  LYS B CA  1 
ATOM   4723 C  C   . LYS B 1 129 ? -12.987 -8.419  41.905  1.00 29.92  ? 129  LYS B C   1 
ATOM   4724 O  O   . LYS B 1 129 ? -13.804 -8.934  41.131  1.00 30.84  ? 129  LYS B O   1 
ATOM   4725 C  CB  . LYS B 1 129 ? -10.680 -9.307  42.314  1.00 29.97  ? 129  LYS B CB  1 
ATOM   4726 C  CG  . LYS B 1 129 ? -11.317 -10.705 42.253  1.00 31.69  ? 129  LYS B CG  1 
ATOM   4727 C  CD  . LYS B 1 129 ? -10.432 -11.800 42.796  1.00 34.57  ? 129  LYS B CD  1 
ATOM   4728 C  CE  . LYS B 1 129 ? -11.148 -13.148 42.773  1.00 35.00  ? 129  LYS B CE  1 
ATOM   4729 N  NZ  . LYS B 1 129 ? -10.240 -14.257 43.203  1.00 33.94  ? 129  LYS B NZ  1 
ATOM   4730 N  N   . TRP B 1 130 ? -13.350 -7.917  43.089  1.00 29.73  ? 130  TRP B N   1 
ATOM   4731 C  CA  . TRP B 1 130 ? -14.728 -8.037  43.551  1.00 28.74  ? 130  TRP B CA  1 
ATOM   4732 C  C   . TRP B 1 130 ? -15.673 -7.139  42.758  1.00 29.49  ? 130  TRP B C   1 
ATOM   4733 O  O   . TRP B 1 130 ? -16.826 -7.512  42.530  1.00 31.83  ? 130  TRP B O   1 
ATOM   4734 C  CB  . TRP B 1 130 ? -14.809 -7.726  45.047  1.00 29.71  ? 130  TRP B CB  1 
ATOM   4735 C  CG  . TRP B 1 130 ? -14.092 -8.731  45.894  1.00 30.38  ? 130  TRP B CG  1 
ATOM   4736 C  CD1 . TRP B 1 130 ? -13.483 -9.894  45.477  1.00 30.98  ? 130  TRP B CD1 1 
ATOM   4737 C  CD2 . TRP B 1 130 ? -13.941 -8.684  47.310  1.00 27.33  ? 130  TRP B CD2 1 
ATOM   4738 N  NE1 . TRP B 1 130 ? -12.955 -10.565 46.559  1.00 31.07  ? 130  TRP B NE1 1 
ATOM   4739 C  CE2 . TRP B 1 130 ? -13.225 -9.843  47.696  1.00 30.58  ? 130  TRP B CE2 1 
ATOM   4740 C  CE3 . TRP B 1 130 ? -14.344 -7.775  48.296  1.00 28.56  ? 130  TRP B CE3 1 
ATOM   4741 C  CZ2 . TRP B 1 130 ? -12.896 -10.102 49.016  1.00 30.20  ? 130  TRP B CZ2 1 
ATOM   4742 C  CZ3 . TRP B 1 130 ? -14.012 -8.044  49.615  1.00 28.37  ? 130  TRP B CZ3 1 
ATOM   4743 C  CH2 . TRP B 1 130 ? -13.305 -9.191  49.960  1.00 30.38  ? 130  TRP B CH2 1 
ATOM   4744 N  N   . GLU B 1 131 ? -15.224 -5.937  42.375  1.00 28.91  ? 131  GLU B N   1 
ATOM   4745 C  CA  . GLU B 1 131 ? -16.052 -5.078  41.528  1.00 29.52  ? 131  GLU B CA  1 
ATOM   4746 C  C   . GLU B 1 131 ? -16.409 -5.768  40.222  1.00 31.33  ? 131  GLU B C   1 
ATOM   4747 O  O   . GLU B 1 131 ? -17.451 -5.457  39.617  1.00 31.42  ? 131  GLU B O   1 
ATOM   4748 C  CB  . GLU B 1 131 ? -15.347 -3.762  41.178  1.00 32.78  ? 131  GLU B CB  1 
ATOM   4749 C  CG  . GLU B 1 131 ? -15.093 -2.788  42.331  1.00 33.60  ? 131  GLU B CG  1 
ATOM   4750 C  CD  . GLU B 1 131 ? -16.335 -2.041  42.763  1.00 36.66  ? 131  GLU B CD  1 
ATOM   4751 O  OE1 . GLU B 1 131 ? -17.455 -2.506  42.456  1.00 34.82  ? 131  GLU B OE1 1 
ATOM   4752 O  OE2 . GLU B 1 131 ? -16.182 -0.981  43.406  1.00 38.72  ? 131  GLU B OE2 1 
ATOM   4753 N  N   . ARG B 1 132 ? -15.543 -6.668  39.754  1.00 28.86  ? 132  ARG B N   1 
ATOM   4754 C  CA  . ARG B 1 132 ? -15.701 -7.267  38.438  1.00 31.61  ? 132  ARG B CA  1 
ATOM   4755 C  C   . ARG B 1 132 ? -16.446 -8.588  38.465  1.00 32.06  ? 132  ARG B C   1 
ATOM   4756 O  O   . ARG B 1 132 ? -16.610 -9.199  37.408  1.00 32.11  ? 132  ARG B O   1 
ATOM   4757 C  CB  . ARG B 1 132 ? -14.324 -7.440  37.769  1.00 30.76  ? 132  ARG B CB  1 
ATOM   4758 C  CG  . ARG B 1 132 ? -13.733 -6.101  37.395  1.00 29.65  ? 132  ARG B CG  1 
ATOM   4759 C  CD  . ARG B 1 132 ? -12.238 -6.170  37.096  1.00 31.37  ? 132  ARG B CD  1 
ATOM   4760 N  NE  . ARG B 1 132 ? -11.783 -4.866  36.635  1.00 30.05  ? 132  ARG B NE  1 
ATOM   4761 C  CZ  . ARG B 1 132 ? -10.513 -4.496  36.503  1.00 32.06  ? 132  ARG B CZ  1 
ATOM   4762 N  NH1 . ARG B 1 132 ? -9.518  -5.303  36.821  1.00 32.67  ? 132  ARG B NH1 1 
ATOM   4763 N  NH2 . ARG B 1 132 ? -10.238 -3.282  36.029  1.00 37.37  ? 132  ARG B NH2 1 
ATOM   4764 N  N   . LEU B 1 133 ? -16.918 -9.037  39.630  1.00 30.03  ? 133  LEU B N   1 
ATOM   4765 C  CA  . LEU B 1 133 ? -17.735 -10.239 39.674  1.00 32.22  ? 133  LEU B CA  1 
ATOM   4766 C  C   . LEU B 1 133 ? -19.094 -9.984  39.026  1.00 33.19  ? 133  LEU B C   1 
ATOM   4767 O  O   . LEU B 1 133 ? -19.631 -8.874  39.070  1.00 35.97  ? 133  LEU B O   1 
ATOM   4768 C  CB  . LEU B 1 133 ? -17.927 -10.704 41.116  1.00 33.59  ? 133  LEU B CB  1 
ATOM   4769 C  CG  . LEU B 1 133 ? -16.641 -11.091 41.849  1.00 30.58  ? 133  LEU B CG  1 
ATOM   4770 C  CD1 . LEU B 1 133 ? -16.914 -11.507 43.307  1.00 35.09  ? 133  LEU B CD1 1 
ATOM   4771 C  CD2 . LEU B 1 133 ? -15.955 -12.238 41.103  1.00 33.67  ? 133  LEU B CD2 1 
ATOM   4772 N  N   . ASN B 1 134 ? -19.643 -11.029 38.412  1.00 32.33  ? 134  ASN B N   1 
ATOM   4773 C  CA  . ASN B 1 134 ? -20.964 -10.967 37.805  1.00 32.27  ? 134  ASN B CA  1 
ATOM   4774 C  C   . ASN B 1 134 ? -22.056 -11.174 38.846  1.00 37.95  ? 134  ASN B C   1 
ATOM   4775 O  O   . ASN B 1 134 ? -21.808 -11.599 39.976  1.00 35.36  ? 134  ASN B O   1 
ATOM   4776 C  CB  . ASN B 1 134 ? -21.108 -12.024 36.718  1.00 31.07  ? 134  ASN B CB  1 
ATOM   4777 C  CG  . ASN B 1 134 ? -20.062 -11.881 35.651  1.00 31.84  ? 134  ASN B CG  1 
ATOM   4778 O  OD1 . ASN B 1 134 ? -20.058 -10.895 34.921  1.00 32.99  ? 134  ASN B OD1 1 
ATOM   4779 N  ND2 . ASN B 1 134 ? -19.160 -12.856 35.555  1.00 35.50  ? 134  ASN B ND2 1 
ATOM   4780 N  N   . ALA B 1 135 ? -23.290 -10.902 38.417  1.00 38.90  ? 135  ALA B N   1 
ATOM   4781 C  CA  . ALA B 1 135 ? -24.468 -11.064 39.255  1.00 44.08  ? 135  ALA B CA  1 
ATOM   4782 C  C   . ALA B 1 135 ? -24.441 -12.403 39.967  1.00 39.74  ? 135  ALA B C   1 
ATOM   4783 O  O   . ALA B 1 135 ? -24.243 -13.452 39.347  1.00 39.14  ? 135  ALA B O   1 
ATOM   4784 C  CB  . ALA B 1 135 ? -25.739 -10.951 38.406  1.00 43.65  ? 135  ALA B CB  1 
ATOM   4785 N  N   . ASP B 1 136 ? -24.594 -12.346 41.285  1.00 47.07  ? 136  ASP B N   1 
ATOM   4786 C  CA  . ASP B 1 136 ? -24.819 -13.492 42.147  1.00 44.96  ? 136  ASP B CA  1 
ATOM   4787 C  C   . ASP B 1 136 ? -23.634 -14.444 42.218  1.00 45.50  ? 136  ASP B C   1 
ATOM   4788 O  O   . ASP B 1 136 ? -23.768 -15.541 42.769  1.00 45.16  ? 136  ASP B O   1 
ATOM   4789 C  CB  . ASP B 1 136 ? -26.085 -14.235 41.719  1.00 54.83  ? 136  ASP B CB  1 
ATOM   4790 C  CG  . ASP B 1 136 ? -27.341 -13.498 42.143  1.00 59.46  ? 136  ASP B CG  1 
ATOM   4791 O  OD1 . ASP B 1 136 ? -27.338 -12.927 43.260  1.00 59.91  ? 136  ASP B OD1 1 
ATOM   4792 O  OD2 . ASP B 1 136 ? -28.305 -13.450 41.348  1.00 64.92  ? 136  ASP B OD2 1 
ATOM   4793 N  N   . GLU B 1 137 ? -22.481 -14.068 41.673  1.00 36.20  ? 137  GLU B N   1 
ATOM   4794 C  CA  . GLU B 1 137 ? -21.251 -14.759 42.030  1.00 33.13  ? 137  GLU B CA  1 
ATOM   4795 C  C   . GLU B 1 137 ? -20.879 -14.409 43.468  1.00 35.65  ? 137  GLU B C   1 
ATOM   4796 O  O   . GLU B 1 137 ? -21.291 -13.376 44.003  1.00 40.19  ? 137  GLU B O   1 
ATOM   4797 C  CB  . GLU B 1 137 ? -20.126 -14.379 41.069  1.00 33.49  ? 137  GLU B CB  1 
ATOM   4798 C  CG  . GLU B 1 137 ? -20.428 -14.855 39.642  1.00 34.62  ? 137  GLU B CG  1 
ATOM   4799 C  CD  . GLU B 1 137 ? -19.370 -14.483 38.616  1.00 36.77  ? 137  GLU B CD  1 
ATOM   4800 O  OE1 . GLU B 1 137 ? -18.476 -13.661 38.905  1.00 34.20  ? 137  GLU B OE1 1 
ATOM   4801 O  OE2 . GLU B 1 137 ? -19.469 -15.006 37.492  1.00 40.03  ? 137  GLU B OE2 1 
ATOM   4802 N  N   . HIS B 1 138 ? -20.096 -15.274 44.100  1.00 35.81  ? 138  HIS B N   1 
ATOM   4803 C  CA  . HIS B 1 138 ? -19.740 -15.062 45.496  1.00 32.10  ? 138  HIS B CA  1 
ATOM   4804 C  C   . HIS B 1 138 ? -18.226 -14.969 45.633  1.00 34.33  ? 138  HIS B C   1 
ATOM   4805 O  O   . HIS B 1 138 ? -17.472 -15.163 44.671  1.00 31.82  ? 138  HIS B O   1 
ATOM   4806 C  CB  . HIS B 1 138 ? -20.306 -16.176 46.391  1.00 32.07  ? 138  HIS B CB  1 
ATOM   4807 C  CG  . HIS B 1 138 ? -19.739 -17.528 46.110  1.00 36.23  ? 138  HIS B CG  1 
ATOM   4808 N  ND1 . HIS B 1 138 ? -20.357 -18.434 45.271  1.00 40.76  ? 138  HIS B ND1 1 
ATOM   4809 C  CD2 . HIS B 1 138 ? -18.615 -18.135 46.559  1.00 36.71  ? 138  HIS B CD2 1 
ATOM   4810 C  CE1 . HIS B 1 138 ? -19.637 -19.539 45.218  1.00 44.42  ? 138  HIS B CE1 1 
ATOM   4811 N  NE2 . HIS B 1 138 ? -18.572 -19.383 45.985  1.00 42.25  ? 138  HIS B NE2 1 
ATOM   4812 N  N   . ILE B 1 139 ? -17.805 -14.632 46.850  1.00 31.87  ? 139  ILE B N   1 
ATOM   4813 C  CA  . ILE B 1 139 ? -16.399 -14.427 47.204  1.00 30.56  ? 139  ILE B CA  1 
ATOM   4814 C  C   . ILE B 1 139 ? -15.983 -15.564 48.122  1.00 30.52  ? 139  ILE B C   1 
ATOM   4815 O  O   . ILE B 1 139 ? -16.696 -15.875 49.084  1.00 31.19  ? 139  ILE B O   1 
ATOM   4816 C  CB  . ILE B 1 139 ? -16.184 -13.077 47.913  1.00 32.22  ? 139  ILE B CB  1 
ATOM   4817 C  CG1 . ILE B 1 139 ? -16.400 -11.907 46.958  1.00 32.12  ? 139  ILE B CG1 1 
ATOM   4818 C  CG2 . ILE B 1 139 ? -14.802 -13.030 48.606  1.00 29.41  ? 139  ILE B CG2 1 
ATOM   4819 C  CD1 . ILE B 1 139 ? -16.792 -10.631 47.675  1.00 33.71  ? 139  ILE B CD1 1 
ATOM   4820 N  N   . GLU B 1 140 ? -14.831 -16.176 47.828  1.00 29.77  ? 140  GLU B N   1 
ATOM   4821 C  CA  . GLU B 1 140 ? -14.206 -17.166 48.705  1.00 30.65  ? 140  GLU B CA  1 
ATOM   4822 C  C   . GLU B 1 140 ? -13.265 -16.387 49.615  1.00 30.68  ? 140  GLU B C   1 
ATOM   4823 O  O   . GLU B 1 140 ? -12.221 -15.901 49.180  1.00 31.19  ? 140  GLU B O   1 
ATOM   4824 C  CB  . GLU B 1 140 ? -13.478 -18.233 47.889  1.00 32.60  ? 140  GLU B CB  1 
ATOM   4825 C  CG  . GLU B 1 140 ? -14.417 -19.037 46.982  1.00 34.19  ? 140  GLU B CG  1 
ATOM   4826 C  CD  . GLU B 1 140 ? -13.678 -20.096 46.194  1.00 41.34  ? 140  GLU B CD  1 
ATOM   4827 O  OE1 . GLU B 1 140 ? -12.465 -19.916 45.974  1.00 41.07  ? 140  GLU B OE1 1 
ATOM   4828 O  OE2 . GLU B 1 140 ? -14.307 -21.105 45.809  1.00 43.18  ? 140  GLU B OE2 1 
ATOM   4829 N  N   . VAL B 1 141 ? -13.678 -16.186 50.858  1.00 28.82  ? 141  VAL B N   1 
ATOM   4830 C  CA  . VAL B 1 141 ? -13.080 -15.145 51.689  1.00 27.04  ? 141  VAL B CA  1 
ATOM   4831 C  C   . VAL B 1 141 ? -11.650 -15.503 52.073  1.00 27.16  ? 141  VAL B C   1 
ATOM   4832 O  O   . VAL B 1 141 ? -10.734 -14.744 51.730  1.00 30.57  ? 141  VAL B O   1 
ATOM   4833 C  CB  . VAL B 1 141 ? -13.946 -14.858 52.925  1.00 30.03  ? 141  VAL B CB  1 
ATOM   4834 C  CG1 . VAL B 1 141 ? -13.210 -13.920 53.874  1.00 31.57  ? 141  VAL B CG1 1 
ATOM   4835 C  CG2 . VAL B 1 141 ? -15.270 -14.227 52.485  1.00 29.51  ? 141  VAL B CG2 1 
ATOM   4836 N  N   . PRO B 1 142 ? -11.390 -16.636 52.735  1.00 26.90  ? 142  PRO B N   1 
ATOM   4837 C  CA  . PRO B 1 142 ? -9.996  -16.923 53.127  1.00 28.13  ? 142  PRO B CA  1 
ATOM   4838 C  C   . PRO B 1 142 ? -9.083  -17.058 51.930  1.00 31.23  ? 142  PRO B C   1 
ATOM   4839 O  O   . PRO B 1 142 ? -7.905  -16.675 51.988  1.00 28.64  ? 142  PRO B O   1 
ATOM   4840 C  CB  . PRO B 1 142 ? -10.100 -18.233 53.922  1.00 29.71  ? 142  PRO B CB  1 
ATOM   4841 C  CG  . PRO B 1 142 ? -11.480 -18.794 53.583  1.00 35.56  ? 142  PRO B CG  1 
ATOM   4842 C  CD  . PRO B 1 142 ? -12.338 -17.598 53.328  1.00 30.22  ? 142  PRO B CD  1 
ATOM   4843 N  N   . GLU B 1 143 ? -9.612  -17.562 50.819  1.00 29.32  ? 143  GLU B N   1 
ATOM   4844 C  CA  . GLU B 1 143 ? -8.807  -17.693 49.612  1.00 30.64  ? 143  GLU B CA  1 
ATOM   4845 C  C   . GLU B 1 143 ? -8.352  -16.328 49.110  1.00 29.20  ? 143  GLU B C   1 
ATOM   4846 O  O   . GLU B 1 143 ? -7.172  -16.137 48.794  1.00 31.91  ? 143  GLU B O   1 
ATOM   4847 C  CB  . GLU B 1 143 ? -9.612  -18.429 48.537  1.00 28.40  ? 143  GLU B CB  1 
ATOM   4848 C  CG  . GLU B 1 143 ? -9.797  -19.919 48.848  1.00 33.30  ? 143  GLU B CG  1 
ATOM   4849 C  CD  . GLU B 1 143 ? -10.869 -20.219 49.903  1.00 36.26  ? 143  GLU B CD  1 
ATOM   4850 O  OE1 . GLU B 1 143 ? -11.662 -19.322 50.276  1.00 31.58  ? 143  GLU B OE1 1 
ATOM   4851 O  OE2 . GLU B 1 143 ? -10.906 -21.375 50.371  1.00 39.75  ? 143  GLU B OE2 1 
ATOM   4852 N  N   . ASP B 1 144 ? -9.276  -15.359 49.028  1.00 27.59  ? 144  ASP B N   1 
ATOM   4853 C  CA  . ASP B 1 144 ? -8.895  -14.036 48.540  1.00 28.92  ? 144  ASP B CA  1 
ATOM   4854 C  C   . ASP B 1 144 ? -8.071  -13.263 49.576  1.00 28.05  ? 144  ASP B C   1 
ATOM   4855 O  O   . ASP B 1 144 ? -7.184  -12.484 49.202  1.00 28.42  ? 144  ASP B O   1 
ATOM   4856 C  CB  . ASP B 1 144 ? -10.137 -13.237 48.135  1.00 28.76  ? 144  ASP B CB  1 
ATOM   4857 C  CG  . ASP B 1 144 ? -10.528 -13.472 46.683  1.00 31.74  ? 144  ASP B CG  1 
ATOM   4858 O  OD1 . ASP B 1 144 ? -9.714  -14.035 45.920  1.00 30.16  ? 144  ASP B OD1 1 
ATOM   4859 O  OD2 . ASP B 1 144 ? -11.638 -13.064 46.294  1.00 31.62  ? 144  ASP B OD2 1 
ATOM   4860 N  N   . MET B 1 145 ? -8.336  -13.463 50.875  1.00 28.84  ? 145  MET B N   1 
ATOM   4861 C  CA  . MET B 1 145 ? -7.482  -12.836 51.892  1.00 28.46  ? 145  MET B CA  1 
ATOM   4862 C  C   . MET B 1 145 ? -6.048  -13.334 51.809  1.00 29.00  ? 145  MET B C   1 
ATOM   4863 O  O   . MET B 1 145 ? -5.111  -12.561 52.022  1.00 29.59  ? 145  MET B O   1 
ATOM   4864 C  CB  . MET B 1 145 ? -8.068  -13.060 53.294  1.00 28.60  ? 145  MET B CB  1 
ATOM   4865 C  CG  . MET B 1 145 ? -9.452  -12.372 53.524  1.00 30.39  ? 145  MET B CG  1 
ATOM   4866 S  SD  . MET B 1 145 ? -9.514  -10.593 53.102  1.00 30.10  ? 145  MET B SD  1 
ATOM   4867 C  CE  . MET B 1 145 ? -10.249 -10.491 51.442  1.00 31.55  ? 145  MET B CE  1 
ATOM   4868 N  N   . THR B 1 146 ? -5.861  -14.615 51.496  1.00 28.12  ? 146  THR B N   1 
ATOM   4869 C  CA  . THR B 1 146 ? -4.511  -15.154 51.326  1.00 28.41  ? 146  THR B CA  1 
ATOM   4870 C  C   . THR B 1 146 ? -3.863  -14.616 50.058  1.00 29.83  ? 146  THR B C   1 
ATOM   4871 O  O   . THR B 1 146 ? -2.668  -14.300 50.055  1.00 30.15  ? 146  THR B O   1 
ATOM   4872 C  CB  . THR B 1 146 ? -4.577  -16.684 51.309  1.00 32.55  ? 146  THR B CB  1 
ATOM   4873 O  OG1 . THR B 1 146 ? -4.882  -17.144 52.629  1.00 34.16  ? 146  THR B OG1 1 
ATOM   4874 C  CG2 . THR B 1 146 ? -3.248  -17.283 50.869  1.00 35.79  ? 146  THR B CG2 1 
ATOM   4875 N  N   . ARG B 1 147 ? -4.624  -14.489 48.966  1.00 29.82  ? 147  ARG B N   1 
ATOM   4876 C  CA  . ARG B 1 147 ? -4.076  -13.805 47.795  1.00 29.43  ? 147  ARG B CA  1 
ATOM   4877 C  C   . ARG B 1 147 ? -3.560  -12.427 48.182  1.00 30.64  ? 147  ARG B C   1 
ATOM   4878 O  O   . ARG B 1 147 ? -2.446  -12.042 47.813  1.00 32.15  ? 147  ARG B O   1 
ATOM   4879 C  CB  . ARG B 1 147 ? -5.130  -13.669 46.687  1.00 31.02  ? 147  ARG B CB  1 
ATOM   4880 C  CG  . ARG B 1 147 ? -5.549  -14.960 46.022  1.00 30.94  ? 147  ARG B CG  1 
ATOM   4881 C  CD  . ARG B 1 147 ? -6.499  -14.646 44.850  1.00 30.52  ? 147  ARG B CD  1 
ATOM   4882 N  NE  . ARG B 1 147 ? -6.746  -15.849 44.056  1.00 34.65  ? 147  ARG B NE  1 
ATOM   4883 C  CZ  . ARG B 1 147 ? -7.672  -16.763 44.328  1.00 38.87  ? 147  ARG B CZ  1 
ATOM   4884 N  NH1 . ARG B 1 147 ? -8.563  -16.594 45.302  1.00 32.92  ? 147  ARG B NH1 1 
ATOM   4885 N  NH2 . ARG B 1 147 ? -7.713  -17.877 43.598  1.00 38.54  ? 147  ARG B NH2 1 
ATOM   4886 N  N   . LEU B 1 148 ? -4.357  -11.671 48.946  1.00 27.15  ? 148  LEU B N   1 
ATOM   4887 C  CA  . LEU B 1 148 ? -3.960  -10.315 49.309  1.00 29.09  ? 148  LEU B CA  1 
ATOM   4888 C  C   . LEU B 1 148 ? -2.730  -10.321 50.210  1.00 30.18  ? 148  LEU B C   1 
ATOM   4889 O  O   . LEU B 1 148 ? -1.774  -9.574  49.973  1.00 29.68  ? 148  LEU B O   1 
ATOM   4890 C  CB  . LEU B 1 148 ? -5.120  -9.584  49.988  1.00 29.94  ? 148  LEU B CB  1 
ATOM   4891 C  CG  . LEU B 1 148 ? -4.617  -8.203  50.435  1.00 32.60  ? 148  LEU B CG  1 
ATOM   4892 C  CD1 . LEU B 1 148 ? -5.473  -7.087  49.847  1.00 36.26  ? 148  LEU B CD1 1 
ATOM   4893 C  CD2 . LEU B 1 148 ? -4.515  -8.122  51.968  1.00 32.71  ? 148  LEU B CD2 1 
ATOM   4894 N  N   . THR B 1 149 ? -2.736  -11.133 51.267  1.00 29.25  ? 149  THR B N   1 
ATOM   4895 C  CA  . THR B 1 149 ? -1.661  -10.961 52.248  1.00 26.82  ? 149  THR B CA  1 
ATOM   4896 C  C   . THR B 1 149 ? -0.334  -11.512 51.734  1.00 30.64  ? 149  THR B C   1 
ATOM   4897 O  O   . THR B 1 149 ? 0.714   -10.909 51.987  1.00 28.87  ? 149  THR B O   1 
ATOM   4898 C  CB  . THR B 1 149 ? -2.033  -11.595 53.596  1.00 29.11  ? 149  THR B CB  1 
ATOM   4899 O  OG1 . THR B 1 149 ? -2.315  -12.985 53.420  1.00 29.48  ? 149  THR B OG1 1 
ATOM   4900 C  CG2 . THR B 1 149 ? -3.269  -10.898 54.197  1.00 31.14  ? 149  THR B CG2 1 
ATOM   4901 N  N   . LEU B 1 150 ? -0.347  -12.631 50.996  1.00 30.27  ? 150  LEU B N   1 
ATOM   4902 C  CA  . LEU B 1 150 ? 0.891   -13.107 50.372  1.00 28.71  ? 150  LEU B CA  1 
ATOM   4903 C  C   . LEU B 1 150 ? 1.450   -12.060 49.414  1.00 30.72  ? 150  LEU B C   1 
ATOM   4904 O  O   . LEU B 1 150 ? 2.647   -11.746 49.428  1.00 29.75  ? 150  LEU B O   1 
ATOM   4905 C  CB  . LEU B 1 150 ? 0.651   -14.422 49.613  1.00 30.26  ? 150  LEU B CB  1 
ATOM   4906 C  CG  . LEU B 1 150 ? 1.914   -14.943 48.911  1.00 32.82  ? 150  LEU B CG  1 
ATOM   4907 C  CD1 . LEU B 1 150 ? 2.880   -15.518 49.942  1.00 35.27  ? 150  LEU B CD1 1 
ATOM   4908 C  CD2 . LEU B 1 150 ? 1.584   -15.970 47.829  1.00 37.09  ? 150  LEU B CD2 1 
ATOM   4909 N  N   . ASP B 1 151 ? 0.597   -11.514 48.551  1.00 29.22  ? 151  ASP B N   1 
ATOM   4910 C  CA  . ASP B 1 151 ? 1.100   -10.534 47.597  1.00 27.55  ? 151  ASP B CA  1 
ATOM   4911 C  C   . ASP B 1 151 ? 1.626   -9.289  48.302  1.00 29.50  ? 151  ASP B C   1 
ATOM   4912 O  O   . ASP B 1 151 ? 2.596   -8.673  47.845  1.00 29.56  ? 151  ASP B O   1 
ATOM   4913 C  CB  . ASP B 1 151 ? 0.002   -10.182 46.601  1.00 29.94  ? 151  ASP B CB  1 
ATOM   4914 C  CG  . ASP B 1 151 ? -0.082  -11.194 45.469  1.00 26.86  ? 151  ASP B CG  1 
ATOM   4915 O  OD1 . ASP B 1 151 ? 0.317   -12.357 45.694  1.00 31.12  ? 151  ASP B OD1 1 
ATOM   4916 O  OD2 . ASP B 1 151 ? -0.534  -10.810 44.388  1.00 33.06  ? 151  ASP B OD2 1 
ATOM   4917 N  N   . THR B 1 152 ? 1.007   -8.906  49.418  1.00 27.67  ? 152  THR B N   1 
ATOM   4918 C  CA  . THR B 1 152 ? 1.466   -7.717  50.136  1.00 27.09  ? 152  THR B CA  1 
ATOM   4919 C  C   . THR B 1 152 ? 2.856   -7.915  50.730  1.00 29.17  ? 152  THR B C   1 
ATOM   4920 O  O   . THR B 1 152 ? 3.717   -7.040  50.590  1.00 30.16  ? 152  THR B O   1 
ATOM   4921 C  CB  . THR B 1 152 ? 0.443   -7.328  51.199  1.00 28.87  ? 152  THR B CB  1 
ATOM   4922 O  OG1 . THR B 1 152 ? -0.801  -7.039  50.527  1.00 29.27  ? 152  THR B OG1 1 
ATOM   4923 C  CG2 . THR B 1 152 ? 0.907   -6.057  51.964  1.00 31.47  ? 152  THR B CG2 1 
ATOM   4924 N  N   . ILE B 1 153 ? 3.105   -9.041  51.409  1.00 29.03  ? 153  ILE B N   1 
ATOM   4925 C  CA  . ILE B 1 153 ? 4.455   -9.229  51.948  1.00 28.99  ? 153  ILE B CA  1 
ATOM   4926 C  C   . ILE B 1 153 ? 5.461   -9.435  50.815  1.00 29.27  ? 153  ILE B C   1 
ATOM   4927 O  O   . ILE B 1 153 ? 6.604   -8.963  50.892  1.00 28.84  ? 153  ILE B O   1 
ATOM   4928 C  CB  . ILE B 1 153 ? 4.504   -10.371 52.982  1.00 26.12  ? 153  ILE B CB  1 
ATOM   4929 C  CG1 . ILE B 1 153 ? 5.893   -10.424 53.655  1.00 30.62  ? 153  ILE B CG1 1 
ATOM   4930 C  CG2 . ILE B 1 153 ? 4.219   -11.729 52.352  1.00 27.83  ? 153  ILE B CG2 1 
ATOM   4931 C  CD1 . ILE B 1 153 ? 6.226   -9.184  54.469  1.00 32.36  ? 153  ILE B CD1 1 
ATOM   4932 N  N   . GLY B 1 154 ? 5.061   -10.117 49.741  1.00 29.83  ? 154  GLY B N   1 
ATOM   4933 C  CA  . GLY B 1 154 ? 5.970   -10.279 48.616  1.00 29.97  ? 154  GLY B CA  1 
ATOM   4934 C  C   . GLY B 1 154 ? 6.399   -8.947  48.031  1.00 30.65  ? 154  GLY B C   1 
ATOM   4935 O  O   . GLY B 1 154 ? 7.589   -8.713  47.781  1.00 29.98  ? 154  GLY B O   1 
ATOM   4936 N  N   . LEU B 1 155 ? 5.432   -8.048  47.810  1.00 28.88  ? 155  LEU B N   1 
ATOM   4937 C  CA  . LEU B 1 155 ? 5.731   -6.763  47.190  1.00 26.95  ? 155  LEU B CA  1 
ATOM   4938 C  C   . LEU B 1 155 ? 6.402   -5.811  48.175  1.00 31.15  ? 155  LEU B C   1 
ATOM   4939 O  O   . LEU B 1 155 ? 7.479   -5.276  47.894  1.00 31.50  ? 155  LEU B O   1 
ATOM   4940 C  CB  . LEU B 1 155 ? 4.445   -6.153  46.617  1.00 31.89  ? 155  LEU B CB  1 
ATOM   4941 C  CG  . LEU B 1 155 ? 4.563   -4.857  45.805  1.00 33.26  ? 155  LEU B CG  1 
ATOM   4942 C  CD1 . LEU B 1 155 ? 5.467   -5.019  44.601  1.00 31.86  ? 155  LEU B CD1 1 
ATOM   4943 C  CD2 . LEU B 1 155 ? 3.180   -4.343  45.388  1.00 32.51  ? 155  LEU B CD2 1 
ATOM   4944 N  N   . CYS B 1 156 ? 5.787   -5.594  49.342  1.00 28.87  ? 156  CYS B N   1 
ATOM   4945 C  CA  . CYS B 1 156 ? 6.379   -4.693  50.332  1.00 28.49  ? 156  CYS B CA  1 
ATOM   4946 C  C   . CYS B 1 156 ? 7.732   -5.201  50.793  1.00 32.53  ? 156  CYS B C   1 
ATOM   4947 O  O   . CYS B 1 156 ? 8.687   -4.423  50.922  1.00 35.78  ? 156  CYS B O   1 
ATOM   4948 C  CB  . CYS B 1 156 ? 5.462   -4.533  51.551  1.00 28.24  ? 156  CYS B CB  1 
ATOM   4949 S  SG  . CYS B 1 156 ? 3.871   -3.802  51.183  1.00 33.85  ? 156  CYS B SG  1 
ATOM   4950 N  N   . GLY B 1 157 ? 7.826   -6.492  51.075  1.00 30.97  ? 157  GLY B N   1 
ATOM   4951 C  CA  . GLY B 1 157 ? 9.023   -7.023  51.698  1.00 29.61  ? 157  GLY B CA  1 
ATOM   4952 C  C   . GLY B 1 157 ? 10.147  -7.256  50.715  1.00 33.95  ? 157  GLY B C   1 
ATOM   4953 O  O   . GLY B 1 157 ? 11.319  -7.019  51.032  1.00 32.69  ? 157  GLY B O   1 
ATOM   4954 N  N   . PHE B 1 158 ? 9.804   -7.688  49.502  1.00 29.40  ? 158  PHE B N   1 
ATOM   4955 C  CA  . PHE B 1 158 ? 10.806  -8.233  48.597  1.00 30.30  ? 158  PHE B CA  1 
ATOM   4956 C  C   . PHE B 1 158 ? 10.721  -7.653  47.195  1.00 31.48  ? 158  PHE B C   1 
ATOM   4957 O  O   . PHE B 1 158 ? 11.484  -8.082  46.318  1.00 33.53  ? 158  PHE B O   1 
ATOM   4958 C  CB  . PHE B 1 158 ? 10.697  -9.764  48.576  1.00 32.35  ? 158  PHE B CB  1 
ATOM   4959 C  CG  . PHE B 1 158 ? 10.783  -10.364 49.951  1.00 31.38  ? 158  PHE B CG  1 
ATOM   4960 C  CD1 . PHE B 1 158 ? 12.008  -10.624 50.525  1.00 31.67  ? 158  PHE B CD1 1 
ATOM   4961 C  CD2 . PHE B 1 158 ? 9.636   -10.581 50.703  1.00 32.44  ? 158  PHE B CD2 1 
ATOM   4962 C  CE1 . PHE B 1 158 ? 12.102  -11.122 51.812  1.00 35.10  ? 158  PHE B CE1 1 
ATOM   4963 C  CE2 . PHE B 1 158 ? 9.725   -11.093 51.995  1.00 32.30  ? 158  PHE B CE2 1 
ATOM   4964 C  CZ  . PHE B 1 158 ? 10.961  -11.361 52.549  1.00 35.09  ? 158  PHE B CZ  1 
ATOM   4965 N  N   . ASN B 1 159 ? 9.865   -6.660  46.974  1.00 30.69  ? 159  ASN B N   1 
ATOM   4966 C  CA  . ASN B 1 159 ? 9.639   -6.128  45.626  1.00 32.18  ? 159  ASN B CA  1 
ATOM   4967 C  C   . ASN B 1 159 ? 9.433   -7.252  44.610  1.00 35.39  ? 159  ASN B C   1 
ATOM   4968 O  O   . ASN B 1 159 ? 9.927   -7.203  43.476  1.00 35.25  ? 159  ASN B O   1 
ATOM   4969 C  CB  . ASN B 1 159 ? 10.787  -5.216  45.201  1.00 39.58  ? 159  ASN B CB  1 
ATOM   4970 C  CG  . ASN B 1 159 ? 10.367  -4.219  44.144  1.00 46.21  ? 159  ASN B CG  1 
ATOM   4971 O  OD1 . ASN B 1 159 ? 9.177   -3.946  43.972  1.00 41.69  ? 159  ASN B OD1 1 
ATOM   4972 N  ND2 . ASN B 1 159 ? 11.341  -3.685  43.413  1.00 49.99  ? 159  ASN B ND2 1 
ATOM   4973 N  N   . TYR B 1 160 ? 8.670   -8.271  45.005  1.00 31.61  ? 160  TYR B N   1 
ATOM   4974 C  CA  . TYR B 1 160 ? 8.395   -9.417  44.152  1.00 33.03  ? 160  TYR B CA  1 
ATOM   4975 C  C   . TYR B 1 160 ? 6.889   -9.569  44.020  1.00 32.36  ? 160  TYR B C   1 
ATOM   4976 O  O   . TYR B 1 160 ? 6.189   -9.536  45.030  1.00 29.72  ? 160  TYR B O   1 
ATOM   4977 C  CB  . TYR B 1 160 ? 8.985   -10.694 44.736  1.00 34.71  ? 160  TYR B CB  1 
ATOM   4978 C  CG  . TYR B 1 160 ? 8.863   -11.889 43.823  1.00 36.45  ? 160  TYR B CG  1 
ATOM   4979 C  CD1 . TYR B 1 160 ? 9.792   -12.100 42.812  1.00 40.72  ? 160  TYR B CD1 1 
ATOM   4980 C  CD2 . TYR B 1 160 ? 7.832   -12.818 43.981  1.00 35.89  ? 160  TYR B CD2 1 
ATOM   4981 C  CE1 . TYR B 1 160 ? 9.695   -13.189 41.976  1.00 45.43  ? 160  TYR B CE1 1 
ATOM   4982 C  CE2 . TYR B 1 160 ? 7.732   -13.912 43.149  1.00 42.84  ? 160  TYR B CE2 1 
ATOM   4983 C  CZ  . TYR B 1 160 ? 8.669   -14.092 42.145  1.00 43.74  ? 160  TYR B CZ  1 
ATOM   4984 O  OH  . TYR B 1 160 ? 8.581   -15.189 41.310  1.00 52.45  ? 160  TYR B OH  1 
ATOM   4985 N  N   . ARG B 1 161 ? 6.390   -9.767  42.794  1.00 32.02  ? 161  ARG B N   1 
ATOM   4986 C  CA  . ARG B 1 161 ? 4.940   -9.889  42.573  1.00 29.50  ? 161  ARG B CA  1 
ATOM   4987 C  C   . ARG B 1 161 ? 4.542   -11.356 42.411  1.00 31.48  ? 161  ARG B C   1 
ATOM   4988 O  O   . ARG B 1 161 ? 4.858   -11.993 41.404  1.00 30.44  ? 161  ARG B O   1 
ATOM   4989 C  CB  . ARG B 1 161 ? 4.497   -9.045  41.374  1.00 30.84  ? 161  ARG B CB  1 
ATOM   4990 C  CG  . ARG B 1 161 ? 4.555   -7.550  41.700  1.00 33.76  ? 161  ARG B CG  1 
ATOM   4991 C  CD  . ARG B 1 161 ? 3.922   -6.671  40.658  1.00 36.67  ? 161  ARG B CD  1 
ATOM   4992 N  NE  . ARG B 1 161 ? 4.052   -5.262  40.996  1.00 34.55  ? 161  ARG B NE  1 
ATOM   4993 C  CZ  . ARG B 1 161 ? 3.099   -4.516  41.537  1.00 30.21  ? 161  ARG B CZ  1 
ATOM   4994 N  NH1 . ARG B 1 161 ? 1.892   -5.011  41.793  1.00 30.09  ? 161  ARG B NH1 1 
ATOM   4995 N  NH2 . ARG B 1 161 ? 3.350   -3.232  41.796  1.00 32.56  ? 161  ARG B NH2 1 
ATOM   4996 N  N   . PHE B 1 162 ? 3.844   -11.898 43.415  1.00 29.74  ? 162  PHE B N   1 
ATOM   4997 C  CA  . PHE B 1 162 ? 3.314   -13.247 43.271  1.00 31.29  ? 162  PHE B CA  1 
ATOM   4998 C  C   . PHE B 1 162 ? 2.140   -13.278 42.302  1.00 29.38  ? 162  PHE B C   1 
ATOM   4999 O  O   . PHE B 1 162 ? 1.799   -14.351 41.799  1.00 30.98  ? 162  PHE B O   1 
ATOM   5000 C  CB  . PHE B 1 162 ? 2.873   -13.800 44.628  1.00 33.11  ? 162  PHE B CB  1 
ATOM   5001 C  CG  . PHE B 1 162 ? 4.010   -14.113 45.557  1.00 35.91  ? 162  PHE B CG  1 
ATOM   5002 C  CD1 . PHE B 1 162 ? 4.737   -15.281 45.412  1.00 42.70  ? 162  PHE B CD1 1 
ATOM   5003 C  CD2 . PHE B 1 162 ? 4.325   -13.257 46.594  1.00 32.75  ? 162  PHE B CD2 1 
ATOM   5004 C  CE1 . PHE B 1 162 ? 5.782   -15.578 46.274  1.00 43.04  ? 162  PHE B CE1 1 
ATOM   5005 C  CE2 . PHE B 1 162 ? 5.377   -13.539 47.457  1.00 34.12  ? 162  PHE B CE2 1 
ATOM   5006 C  CZ  . PHE B 1 162 ? 6.108   -14.704 47.290  1.00 37.60  ? 162  PHE B CZ  1 
ATOM   5007 N  N   . ASN B 1 163 ? 1.529   -12.122 42.036  1.00 29.71  ? 163  ASN B N   1 
ATOM   5008 C  CA  . ASN B 1 163 ? 0.391   -12.018 41.117  1.00 28.82  ? 163  ASN B CA  1 
ATOM   5009 C  C   . ASN B 1 163 ? -0.688  -13.057 41.433  1.00 31.45  ? 163  ASN B C   1 
ATOM   5010 O  O   . ASN B 1 163 ? -1.222  -13.742 40.559  1.00 31.15  ? 163  ASN B O   1 
ATOM   5011 C  CB  . ASN B 1 163 ? 0.884   -12.095 39.671  1.00 29.85  ? 163  ASN B CB  1 
ATOM   5012 C  CG  . ASN B 1 163 ? 1.626   -10.831 39.277  1.00 32.12  ? 163  ASN B CG  1 
ATOM   5013 O  OD1 . ASN B 1 163 ? 1.156   -9.737  39.559  1.00 33.55  ? 163  ASN B OD1 1 
ATOM   5014 N  ND2 . ASN B 1 163 ? 2.806   -10.970 38.684  1.00 32.21  ? 163  ASN B ND2 1 
ATOM   5015 N  N   . SER B 1 164 ? -1.057  -13.125 42.718  1.00 29.96  ? 164  SER B N   1 
ATOM   5016 C  CA  . SER B 1 164 ? -2.039  -14.117 43.138  1.00 29.36  ? 164  SER B CA  1 
ATOM   5017 C  C   . SER B 1 164 ? -3.418  -13.846 42.563  1.00 32.81  ? 164  SER B C   1 
ATOM   5018 O  O   . SER B 1 164 ? -4.215  -14.781 42.433  1.00 30.90  ? 164  SER B O   1 
ATOM   5019 C  CB  . SER B 1 164 ? -2.138  -14.163 44.659  1.00 31.42  ? 164  SER B CB  1 
ATOM   5020 O  OG  . SER B 1 164 ? -0.899  -14.579 45.217  1.00 31.64  ? 164  SER B OG  1 
ATOM   5021 N  N   . PHE B 1 165 ? -3.741  -12.586 42.275  1.00 30.31  ? 165  PHE B N   1 
ATOM   5022 C  CA  . PHE B 1 165 ? -5.054  -12.281 41.715  1.00 32.67  ? 165  PHE B CA  1 
ATOM   5023 C  C   . PHE B 1 165 ? -5.125  -12.591 40.236  1.00 37.69  ? 165  PHE B C   1 
ATOM   5024 O  O   . PHE B 1 165 ? -6.211  -12.486 39.649  1.00 35.06  ? 165  PHE B O   1 
ATOM   5025 C  CB  . PHE B 1 165 ? -5.434  -10.821 41.979  1.00 31.25  ? 165  PHE B CB  1 
ATOM   5026 C  CG  . PHE B 1 165 ? -5.800  -10.568 43.418  1.00 28.32  ? 165  PHE B CG  1 
ATOM   5027 C  CD1 . PHE B 1 165 ? -6.935  -11.152 43.973  1.00 31.34  ? 165  PHE B CD1 1 
ATOM   5028 C  CD2 . PHE B 1 165 ? -4.969  -9.811  44.238  1.00 29.46  ? 165  PHE B CD2 1 
ATOM   5029 C  CE1 . PHE B 1 165 ? -7.256  -10.942 45.319  1.00 31.55  ? 165  PHE B CE1 1 
ATOM   5030 C  CE2 . PHE B 1 165 ? -5.287  -9.600  45.580  1.00 31.41  ? 165  PHE B CE2 1 
ATOM   5031 C  CZ  . PHE B 1 165 ? -6.414  -10.168 46.118  1.00 30.44  ? 165  PHE B CZ  1 
ATOM   5032 N  N   . TYR B 1 166 ? -4.003  -12.990 39.631  1.00 30.43  ? 166  TYR B N   1 
ATOM   5033 C  CA  . TYR B 1 166 ? -4.002  -13.492 38.260  1.00 34.46  ? 166  TYR B CA  1 
ATOM   5034 C  C   . TYR B 1 166 ? -4.164  -15.009 38.186  1.00 37.30  ? 166  TYR B C   1 
ATOM   5035 O  O   . TYR B 1 166 ? -4.053  -15.573 37.097  1.00 37.49  ? 166  TYR B O   1 
ATOM   5036 C  CB  . TYR B 1 166 ? -2.725  -13.035 37.540  1.00 33.61  ? 166  TYR B CB  1 
ATOM   5037 C  CG  . TYR B 1 166 ? -2.730  -11.544 37.347  1.00 31.26  ? 166  TYR B CG  1 
ATOM   5038 C  CD1 . TYR B 1 166 ? -2.310  -10.688 38.362  1.00 30.30  ? 166  TYR B CD1 1 
ATOM   5039 C  CD2 . TYR B 1 166 ? -3.221  -10.984 36.172  1.00 33.34  ? 166  TYR B CD2 1 
ATOM   5040 C  CE1 . TYR B 1 166 ? -2.356  -9.313  38.198  1.00 29.62  ? 166  TYR B CE1 1 
ATOM   5041 C  CE2 . TYR B 1 166 ? -3.270  -9.628  35.999  1.00 28.58  ? 166  TYR B CE2 1 
ATOM   5042 C  CZ  . TYR B 1 166 ? -2.847  -8.787  37.020  1.00 29.56  ? 166  TYR B CZ  1 
ATOM   5043 O  OH  . TYR B 1 166 ? -2.897  -7.427  36.860  1.00 31.41  ? 166  TYR B OH  1 
ATOM   5044 N  N   . ARG B 1 167 ? -4.439  -15.674 39.314  1.00 36.45  ? 167  ARG B N   1 
ATOM   5045 C  CA  . ARG B 1 167 ? -4.585  -17.123 39.373  1.00 38.24  ? 167  ARG B CA  1 
ATOM   5046 C  C   . ARG B 1 167 ? -5.933  -17.486 39.976  1.00 42.38  ? 167  ARG B C   1 
ATOM   5047 O  O   . ARG B 1 167 ? -6.334  -16.916 40.995  1.00 40.33  ? 167  ARG B O   1 
ATOM   5048 C  CB  . ARG B 1 167 ? -3.469  -17.761 40.204  1.00 42.97  ? 167  ARG B CB  1 
ATOM   5049 C  CG  . ARG B 1 167 ? -2.091  -17.313 39.796  1.00 42.15  ? 167  ARG B CG  1 
ATOM   5050 C  CD  . ARG B 1 167 ? -1.090  -17.526 40.912  1.00 43.20  ? 167  ARG B CD  1 
ATOM   5051 N  NE  . ARG B 1 167 ? 0.154   -16.815 40.648  1.00 47.79  ? 167  ARG B NE  1 
ATOM   5052 C  CZ  . ARG B 1 167 ? 1.194   -17.347 40.021  1.00 50.57  ? 167  ARG B CZ  1 
ATOM   5053 N  NH1 . ARG B 1 167 ? 1.171   -18.598 39.584  1.00 48.92  ? 167  ARG B NH1 1 
ATOM   5054 N  NH2 . ARG B 1 167 ? 2.286   -16.609 39.834  1.00 46.52  ? 167  ARG B NH2 1 
ATOM   5055 N  N   . ASP B 1 168 ? -6.632  -18.434 39.344  1.00 43.08  ? 168  ASP B N   1 
ATOM   5056 C  CA  . ASP B 1 168 ? -7.872  -18.958 39.909  1.00 45.49  ? 168  ASP B CA  1 
ATOM   5057 C  C   . ASP B 1 168 ? -7.610  -20.076 40.906  1.00 48.54  ? 168  ASP B C   1 
ATOM   5058 O  O   . ASP B 1 168 ? -8.486  -20.379 41.722  1.00 48.01  ? 168  ASP B O   1 
ATOM   5059 C  CB  . ASP B 1 168 ? -8.806  -19.449 38.790  1.00 46.16  ? 168  ASP B CB  1 
ATOM   5060 C  CG  . ASP B 1 168 ? -8.157  -20.502 37.904  1.00 51.38  ? 168  ASP B CG  1 
ATOM   5061 O  OD1 . ASP B 1 168 ? -8.440  -21.707 38.084  1.00 62.52  ? 168  ASP B OD1 1 
ATOM   5062 O  OD2 . ASP B 1 168 ? -7.351  -20.129 37.026  1.00 57.36  ? 168  ASP B OD2 1 
ATOM   5063 N  N   . GLN B 1 169 ? -6.431  -20.683 40.854  1.00 45.46  ? 169  GLN B N   1 
ATOM   5064 C  CA  . GLN B 1 169 ? -5.959  -21.657 41.820  1.00 51.51  ? 169  GLN B CA  1 
ATOM   5065 C  C   . GLN B 1 169 ? -5.035  -20.991 42.829  1.00 50.01  ? 169  GLN B C   1 
ATOM   5066 O  O   . GLN B 1 169 ? -4.537  -19.886 42.597  1.00 46.49  ? 169  GLN B O   1 
ATOM   5067 C  CB  . GLN B 1 169 ? -5.225  -22.795 41.106  1.00 53.98  ? 169  GLN B CB  1 
ATOM   5068 C  CG  . GLN B 1 169 ? -5.880  -24.163 41.291  1.00 65.92  ? 169  GLN B CG  1 
ATOM   5069 C  CD  . GLN B 1 169 ? -4.929  -25.316 41.005  1.00 70.35  ? 169  GLN B CD  1 
ATOM   5070 O  OE1 . GLN B 1 169 ? -4.784  -25.743 39.856  1.00 78.17  ? 169  GLN B OE1 1 
ATOM   5071 N  NE2 . GLN B 1 169 ? -4.267  -25.818 42.048  1.00 64.52  ? 169  GLN B NE2 1 
ATOM   5072 N  N   . PRO B 1 170 ? -4.793  -21.626 43.976  1.00 51.09  ? 170  PRO B N   1 
ATOM   5073 C  CA  . PRO B 1 170 ? -3.809  -21.078 44.915  1.00 47.52  ? 170  PRO B CA  1 
ATOM   5074 C  C   . PRO B 1 170 ? -2.441  -20.990 44.256  1.00 49.08  ? 170  PRO B C   1 
ATOM   5075 O  O   . PRO B 1 170 ? -2.092  -21.798 43.389  1.00 44.69  ? 170  PRO B O   1 
ATOM   5076 C  CB  . PRO B 1 170 ? -3.808  -22.089 46.071  1.00 47.20  ? 170  PRO B CB  1 
ATOM   5077 C  CG  . PRO B 1 170 ? -5.091  -22.825 45.953  1.00 53.68  ? 170  PRO B CG  1 
ATOM   5078 C  CD  . PRO B 1 170 ? -5.441  -22.843 44.490  1.00 49.30  ? 170  PRO B CD  1 
ATOM   5079 N  N   . HIS B 1 171 ? -1.675  -19.975 44.652  1.00 45.62  ? 171  HIS B N   1 
ATOM   5080 C  CA  . HIS B 1 171 ? -0.292  -19.889 44.204  1.00 45.00  ? 171  HIS B CA  1 
ATOM   5081 C  C   . HIS B 1 171 ? 0.445   -21.163 44.610  1.00 47.80  ? 171  HIS B C   1 
ATOM   5082 O  O   . HIS B 1 171 ? 0.196   -21.699 45.696  1.00 43.25  ? 171  HIS B O   1 
ATOM   5083 C  CB  . HIS B 1 171 ? 0.411   -18.671 44.821  1.00 44.64  ? 171  HIS B CB  1 
ATOM   5084 C  CG  . HIS B 1 171 ? 1.745   -18.361 44.211  1.00 45.01  ? 171  HIS B CG  1 
ATOM   5085 N  ND1 . HIS B 1 171 ? 2.869   -19.128 44.434  1.00 46.30  ? 171  HIS B ND1 1 
ATOM   5086 C  CD2 . HIS B 1 171 ? 2.136   -17.355 43.393  1.00 46.97  ? 171  HIS B CD2 1 
ATOM   5087 C  CE1 . HIS B 1 171 ? 3.891   -18.617 43.771  1.00 47.69  ? 171  HIS B CE1 1 
ATOM   5088 N  NE2 . HIS B 1 171 ? 3.474   -17.537 43.134  1.00 47.34  ? 171  HIS B NE2 1 
ATOM   5089 N  N   . PRO B 1 172 ? 1.353   -21.671 43.772  1.00 48.22  ? 172  PRO B N   1 
ATOM   5090 C  CA  . PRO B 1 172 ? 2.113   -22.880 44.151  1.00 45.72  ? 172  PRO B CA  1 
ATOM   5091 C  C   . PRO B 1 172 ? 2.813   -22.784 45.505  1.00 44.71  ? 172  PRO B C   1 
ATOM   5092 O  O   . PRO B 1 172 ? 2.907   -23.791 46.228  1.00 43.26  ? 172  PRO B O   1 
ATOM   5093 C  CB  . PRO B 1 172 ? 3.127   -23.019 43.006  1.00 46.58  ? 172  PRO B CB  1 
ATOM   5094 C  CG  . PRO B 1 172 ? 2.480   -22.345 41.840  1.00 46.56  ? 172  PRO B CG  1 
ATOM   5095 C  CD  . PRO B 1 172 ? 1.620   -21.240 42.387  1.00 48.66  ? 172  PRO B CD  1 
ATOM   5096 N  N   . PHE B 1 173 ? 3.348   -21.612 45.858  1.00 44.82  ? 173  PHE B N   1 
ATOM   5097 C  CA  . PHE B 1 173 ? 3.945   -21.472 47.184  1.00 40.38  ? 173  PHE B CA  1 
ATOM   5098 C  C   . PHE B 1 173 ? 2.911   -21.773 48.255  1.00 41.02  ? 173  PHE B C   1 
ATOM   5099 O  O   . PHE B 1 173 ? 3.202   -22.464 49.237  1.00 41.08  ? 173  PHE B O   1 
ATOM   5100 C  CB  . PHE B 1 173 ? 4.532   -20.068 47.368  1.00 41.99  ? 173  PHE B CB  1 
ATOM   5101 C  CG  . PHE B 1 173 ? 5.269   -19.875 48.684  1.00 41.98  ? 173  PHE B CG  1 
ATOM   5102 C  CD1 . PHE B 1 173 ? 4.586   -19.484 49.829  1.00 43.34  ? 173  PHE B CD1 1 
ATOM   5103 C  CD2 . PHE B 1 173 ? 6.642   -20.075 48.767  1.00 37.56  ? 173  PHE B CD2 1 
ATOM   5104 C  CE1 . PHE B 1 173 ? 5.267   -19.301 51.044  1.00 38.73  ? 173  PHE B CE1 1 
ATOM   5105 C  CE2 . PHE B 1 173 ? 7.322   -19.893 49.962  1.00 40.82  ? 173  PHE B CE2 1 
ATOM   5106 C  CZ  . PHE B 1 173 ? 6.629   -19.509 51.107  1.00 41.60  ? 173  PHE B CZ  1 
ATOM   5107 N  N   . ILE B 1 174 ? 1.679   -21.309 48.054  1.00 37.83  ? 174  ILE B N   1 
ATOM   5108 C  CA  . ILE B 1 174 ? 0.631   -21.494 49.055  1.00 40.16  ? 174  ILE B CA  1 
ATOM   5109 C  C   . ILE B 1 174 ? 0.272   -22.970 49.189  1.00 39.10  ? 174  ILE B C   1 
ATOM   5110 O  O   . ILE B 1 174 ? 0.137   -23.493 50.305  1.00 38.50  ? 174  ILE B O   1 
ATOM   5111 C  CB  . ILE B 1 174 ? -0.598  -20.632 48.711  1.00 39.42  ? 174  ILE B CB  1 
ATOM   5112 C  CG1 . ILE B 1 174 ? -0.260  -19.131 48.806  1.00 40.36  ? 174  ILE B CG1 1 
ATOM   5113 C  CG2 . ILE B 1 174 ? -1.790  -20.999 49.589  1.00 36.81  ? 174  ILE B CG2 1 
ATOM   5114 C  CD1 . ILE B 1 174 ? 0.157   -18.654 50.221  1.00 35.28  ? 174  ILE B CD1 1 
ATOM   5115 N  N   . THR B 1 175 ? 0.120   -23.665 48.056  1.00 39.90  ? 175  THR B N   1 
ATOM   5116 C  CA  . THR B 1 175 ? -0.201  -25.089 48.090  1.00 38.94  ? 175  THR B CA  1 
ATOM   5117 C  C   . THR B 1 175 ? 0.855   -25.865 48.863  1.00 40.01  ? 175  THR B C   1 
ATOM   5118 O  O   . THR B 1 175 ? 0.535   -26.724 49.693  1.00 38.79  ? 175  THR B O   1 
ATOM   5119 C  CB  . THR B 1 175 ? -0.327  -25.632 46.666  1.00 42.68  ? 175  THR B CB  1 
ATOM   5120 O  OG1 . THR B 1 175 ? -1.465  -25.038 46.033  1.00 45.45  ? 175  THR B OG1 1 
ATOM   5121 C  CG2 . THR B 1 175 ? -0.490  -27.151 46.685  1.00 43.72  ? 175  THR B CG2 1 
ATOM   5122 N  N   . SER B 1 176 ? 2.130   -25.562 48.611  1.00 38.89  ? 176  SER B N   1 
ATOM   5123 C  CA  . SER B 1 176 ? 3.203   -26.269 49.296  1.00 36.50  ? 176  SER B CA  1 
ATOM   5124 C  C   . SER B 1 176 ? 3.297   -25.859 50.766  1.00 38.81  ? 176  SER B C   1 
ATOM   5125 O  O   . SER B 1 176 ? 3.545   -26.705 51.631  1.00 38.31  ? 176  SER B O   1 
ATOM   5126 C  CB  . SER B 1 176 ? 4.531   -26.032 48.567  1.00 41.85  ? 176  SER B CB  1 
ATOM   5127 O  OG  . SER B 1 176 ? 4.649   -26.913 47.463  1.00 41.93  ? 176  SER B OG  1 
ATOM   5128 N  N   . MET B 1 177 ? 3.089   -24.578 51.089  1.00 34.94  ? 177  MET B N   1 
ATOM   5129 C  CA  . MET B 1 177 ? 3.293   -24.200 52.481  1.00 35.41  ? 177  MET B CA  1 
ATOM   5130 C  C   . MET B 1 177 ? 2.129   -24.706 53.322  1.00 36.30  ? 177  MET B C   1 
ATOM   5131 O  O   . MET B 1 177 ? 2.323   -25.158 54.457  1.00 35.19  ? 177  MET B O   1 
ATOM   5132 C  CB  . MET B 1 177 ? 3.475   -22.679 52.650  1.00 38.90  ? 177  MET B CB  1 
ATOM   5133 C  CG  . MET B 1 177 ? 2.987   -22.107 54.011  1.00 39.03  ? 177  MET B CG  1 
ATOM   5134 S  SD  . MET B 1 177 ? 2.278   -20.433 54.166  1.00 37.98  ? 177  MET B SD  1 
ATOM   5135 C  CE  . MET B 1 177 ? 0.538   -20.824 53.877  1.00 35.63  ? 177  MET B CE  1 
ATOM   5136 N  N   . VAL B 1 178 ? 0.912   -24.673 52.769  1.00 39.45  ? 178  VAL B N   1 
ATOM   5137 C  CA  . VAL B 1 178 ? -0.234  -25.222 53.489  1.00 37.82  ? 178  VAL B CA  1 
ATOM   5138 C  C   . VAL B 1 178 ? -0.020  -26.706 53.772  1.00 41.41  ? 178  VAL B C   1 
ATOM   5139 O  O   . VAL B 1 178 ? -0.267  -27.187 54.887  1.00 38.40  ? 178  VAL B O   1 
ATOM   5140 C  CB  . VAL B 1 178 ? -1.539  -24.977 52.706  1.00 38.54  ? 178  VAL B CB  1 
ATOM   5141 C  CG1 . VAL B 1 178 ? -2.670  -25.846 53.271  1.00 41.57  ? 178  VAL B CG1 1 
ATOM   5142 C  CG2 . VAL B 1 178 ? -1.923  -23.483 52.751  1.00 37.32  ? 178  VAL B CG2 1 
ATOM   5143 N  N   . ARG B 1 179 ? 0.459   -27.448 52.773  1.00 41.03  ? 179  ARG B N   1 
ATOM   5144 C  CA  . ARG B 1 179 ? 0.677   -28.881 52.941  1.00 38.94  ? 179  ARG B CA  1 
ATOM   5145 C  C   . ARG B 1 179 ? 1.768   -29.164 53.963  1.00 41.14  ? 179  ARG B C   1 
ATOM   5146 O  O   . ARG B 1 179 ? 1.677   -30.147 54.709  1.00 40.41  ? 179  ARG B O   1 
ATOM   5147 C  CB  . ARG B 1 179 ? 1.011   -29.511 51.585  1.00 42.85  ? 179  ARG B CB  1 
ATOM   5148 C  CG  . ARG B 1 179 ? 0.792   -31.008 51.508  1.00 43.62  ? 179  ARG B CG  1 
ATOM   5149 C  CD  . ARG B 1 179 ? 0.542   -31.451 50.047  1.00 45.86  ? 179  ARG B CD  1 
ATOM   5150 N  NE  . ARG B 1 179 ? 1.546   -30.932 49.121  1.00 43.91  ? 179  ARG B NE  1 
ATOM   5151 C  CZ  . ARG B 1 179 ? 1.303   -30.624 47.853  1.00 48.87  ? 179  ARG B CZ  1 
ATOM   5152 N  NH1 . ARG B 1 179 ? 0.106   -30.813 47.308  1.00 48.60  ? 179  ARG B NH1 1 
ATOM   5153 N  NH2 . ARG B 1 179 ? 2.279   -30.110 47.111  1.00 44.25  ? 179  ARG B NH2 1 
ATOM   5154 N  N   . ALA B 1 180 ? 2.802   -28.311 54.017  1.00 36.52  ? 180  ALA B N   1 
ATOM   5155 C  CA  . ALA B 1 180 ? 3.862   -28.465 55.012  1.00 40.03  ? 180  ALA B CA  1 
ATOM   5156 C  C   . ALA B 1 180 ? 3.349   -28.178 56.418  1.00 41.49  ? 180  ALA B C   1 
ATOM   5157 O  O   . ALA B 1 180 ? 3.683   -28.893 57.371  1.00 35.60  ? 180  ALA B O   1 
ATOM   5158 C  CB  . ALA B 1 180 ? 5.036   -27.544 54.682  1.00 38.09  ? 180  ALA B CB  1 
ATOM   5159 N  N   . LEU B 1 181 ? 2.555   -27.120 56.574  1.00 35.60  ? 181  LEU B N   1 
ATOM   5160 C  CA  . LEU B 1 181 ? 1.970   -26.851 57.881  1.00 38.09  ? 181  LEU B CA  1 
ATOM   5161 C  C   . LEU B 1 181 ? 1.055   -27.989 58.293  1.00 40.51  ? 181  LEU B C   1 
ATOM   5162 O  O   . LEU B 1 181 ? 1.034   -28.385 59.465  1.00 38.48  ? 181  LEU B O   1 
ATOM   5163 C  CB  . LEU B 1 181 ? 1.195   -25.529 57.854  1.00 35.78  ? 181  LEU B CB  1 
ATOM   5164 C  CG  . LEU B 1 181 ? 2.069   -24.296 57.617  1.00 34.46  ? 181  LEU B CG  1 
ATOM   5165 C  CD1 . LEU B 1 181 ? 1.213   -23.049 57.455  1.00 36.35  ? 181  LEU B CD1 1 
ATOM   5166 C  CD2 . LEU B 1 181 ? 3.050   -24.129 58.800  1.00 35.73  ? 181  LEU B CD2 1 
ATOM   5167 N  N   . ASP B 1 182 ? 0.270   -28.507 57.338  1.00 41.19  ? 182  ASP B N   1 
ATOM   5168 C  CA  . ASP B 1 182 ? -0.573  -29.670 57.595  1.00 41.38  ? 182  ASP B CA  1 
ATOM   5169 C  C   . ASP B 1 182 ? 0.268   -30.815 58.131  1.00 38.99  ? 182  ASP B C   1 
ATOM   5170 O  O   . ASP B 1 182 ? -0.087  -31.469 59.119  1.00 42.17  ? 182  ASP B O   1 
ATOM   5171 C  CB  . ASP B 1 182 ? -1.267  -30.127 56.307  1.00 38.87  ? 182  ASP B CB  1 
ATOM   5172 C  CG  . ASP B 1 182 ? -2.502  -29.338 55.985  1.00 51.39  ? 182  ASP B CG  1 
ATOM   5173 O  OD1 . ASP B 1 182 ? -3.155  -28.815 56.910  1.00 55.05  ? 182  ASP B OD1 1 
ATOM   5174 O  OD2 . ASP B 1 182 ? -2.834  -29.274 54.781  1.00 53.87  ? 182  ASP B OD2 1 
ATOM   5175 N  N   . GLU B 1 183 ? 1.377   -31.092 57.453  1.00 35.68  ? 183  GLU B N   1 
ATOM   5176 C  CA  . GLU B 1 183 ? 2.239   -32.191 57.860  1.00 38.94  ? 183  GLU B CA  1 
ATOM   5177 C  C   . GLU B 1 183 ? 2.798   -31.947 59.258  1.00 39.93  ? 183  GLU B C   1 
ATOM   5178 O  O   . GLU B 1 183 ? 2.750   -32.830 60.124  1.00 39.24  ? 183  GLU B O   1 
ATOM   5179 C  CB  . GLU B 1 183 ? 3.347   -32.363 56.819  1.00 39.74  ? 183  GLU B CB  1 
ATOM   5180 C  CG  . GLU B 1 183 ? 4.459   -33.333 57.182  1.00 43.91  ? 183  GLU B CG  1 
ATOM   5181 C  CD  . GLU B 1 183 ? 4.021   -34.793 57.218  1.00 42.90  ? 183  GLU B CD  1 
ATOM   5182 O  OE1 . GLU B 1 183 ? 2.851   -35.098 56.896  1.00 44.37  ? 183  GLU B OE1 1 
ATOM   5183 O  OE2 . GLU B 1 183 ? 4.876   -35.639 57.552  1.00 42.17  ? 183  GLU B OE2 1 
ATOM   5184 N  N   . ALA B 1 184 ? 3.294   -30.734 59.512  1.00 38.60  ? 184  ALA B N   1 
ATOM   5185 C  CA  . ALA B 1 184 ? 3.812   -30.429 60.842  1.00 34.80  ? 184  ALA B CA  1 
ATOM   5186 C  C   . ALA B 1 184 ? 2.749   -30.654 61.906  1.00 40.40  ? 184  ALA B C   1 
ATOM   5187 O  O   . ALA B 1 184 ? 3.045   -31.189 62.976  1.00 37.94  ? 184  ALA B O   1 
ATOM   5188 C  CB  . ALA B 1 184 ? 4.340   -28.994 60.897  1.00 40.11  ? 184  ALA B CB  1 
ATOM   5189 N  N   . MET B 1 185 ? 1.497   -30.287 61.631  1.00 35.15  ? 185  MET B N   1 
ATOM   5190 C  CA  . MET B 1 185 ? 0.526   -30.458 62.701  1.00 35.68  ? 185  MET B CA  1 
ATOM   5191 C  C   . MET B 1 185 ? 0.060   -31.910 62.799  1.00 39.70  ? 185  MET B C   1 
ATOM   5192 O  O   . MET B 1 185 ? -0.157  -32.403 63.913  1.00 37.96  ? 185  MET B O   1 
ATOM   5193 C  CB  . MET B 1 185 ? -0.617  -29.442 62.543  1.00 40.09  ? 185  MET B CB  1 
ATOM   5194 C  CG  . MET B 1 185 ? -1.824  -29.630 63.455  1.00 34.72  ? 185  MET B CG  1 
ATOM   5195 S  SD  . MET B 1 185 ? -3.334  -28.813 62.840  1.00 37.78  ? 185  MET B SD  1 
ATOM   5196 C  CE  . MET B 1 185 ? -4.056  -30.121 61.831  1.00 39.29  ? 185  MET B CE  1 
ATOM   5197 N  N   . ASN B 1 186 ? -0.038  -32.630 61.672  1.00 41.61  ? 186  ASN B N   1 
ATOM   5198 C  CA  . ASN B 1 186 ? -0.304  -34.070 61.737  1.00 40.54  ? 186  ASN B CA  1 
ATOM   5199 C  C   . ASN B 1 186 ? 0.848   -34.835 62.377  1.00 40.37  ? 186  ASN B C   1 
ATOM   5200 O  O   . ASN B 1 186 ? 0.618   -35.818 63.093  1.00 43.42  ? 186  ASN B O   1 
ATOM   5201 C  CB  . ASN B 1 186 ? -0.588  -34.637 60.344  1.00 41.64  ? 186  ASN B CB  1 
ATOM   5202 C  CG  . ASN B 1 186 ? -1.307  -35.986 60.395  1.00 49.49  ? 186  ASN B CG  1 
ATOM   5203 O  OD1 . ASN B 1 186 ? -0.669  -37.045 60.320  1.00 51.37  ? 186  ASN B OD1 1 
ATOM   5204 N  ND2 . ASN B 1 186 ? -2.628  -35.956 60.539  1.00 52.82  ? 186  ASN B ND2 1 
ATOM   5205 N  N   . LYS B 1 187 ? 2.083   -34.397 62.144  1.00 36.85  ? 187  LYS B N   1 
ATOM   5206 C  CA  . LYS B 1 187 ? 3.220   -35.073 62.751  1.00 42.12  ? 187  LYS B CA  1 
ATOM   5207 C  C   . LYS B 1 187 ? 3.162   -35.021 64.278  1.00 40.64  ? 187  LYS B C   1 
ATOM   5208 O  O   . LYS B 1 187 ? 3.667   -35.931 64.945  1.00 40.67  ? 187  LYS B O   1 
ATOM   5209 C  CB  . LYS B 1 187 ? 4.517   -34.462 62.229  1.00 40.50  ? 187  LYS B CB  1 
ATOM   5210 C  CG  . LYS B 1 187 ? 5.237   -35.338 61.250  1.00 49.42  ? 187  LYS B CG  1 
ATOM   5211 C  CD  . LYS B 1 187 ? 6.732   -35.066 61.249  1.00 50.31  ? 187  LYS B CD  1 
ATOM   5212 C  CE  . LYS B 1 187 ? 7.053   -33.755 60.574  1.00 49.32  ? 187  LYS B CE  1 
ATOM   5213 N  NZ  . LYS B 1 187 ? 8.461   -33.775 60.080  1.00 50.40  ? 187  LYS B NZ  1 
ATOM   5214 N  N   . LEU B 1 188 ? 2.516   -33.995 64.847  1.00 39.94  ? 188  LEU B N   1 
ATOM   5215 C  CA  . LEU B 1 188 ? 2.493   -33.829 66.301  1.00 41.27  ? 188  LEU B CA  1 
ATOM   5216 C  C   . LEU B 1 188 ? 1.898   -35.037 67.011  1.00 37.14  ? 188  LEU B C   1 
ATOM   5217 O  O   . LEU B 1 188 ? 2.302   -35.355 68.134  1.00 42.35  ? 188  LEU B O   1 
ATOM   5218 C  CB  . LEU B 1 188 ? 1.685   -32.588 66.691  1.00 43.80  ? 188  LEU B CB  1 
ATOM   5219 C  CG  . LEU B 1 188 ? 2.210   -31.241 66.201  1.00 38.61  ? 188  LEU B CG  1 
ATOM   5220 C  CD1 . LEU B 1 188 ? 1.192   -30.128 66.482  1.00 39.01  ? 188  LEU B CD1 1 
ATOM   5221 C  CD2 . LEU B 1 188 ? 3.560   -30.957 66.853  1.00 44.05  ? 188  LEU B CD2 1 
ATOM   5222 N  N   . GLN B 1 189 ? 0.930   -35.701 66.396  1.00 40.53  ? 189  GLN B N   1 
ATOM   5223 C  CA  . GLN B 1 189 ? 0.178   -36.746 67.072  1.00 40.83  ? 189  GLN B CA  1 
ATOM   5224 C  C   . GLN B 1 189 ? 0.662   -38.149 66.736  1.00 45.89  ? 189  GLN B C   1 
ATOM   5225 O  O   . GLN B 1 189 ? 0.095   -39.122 67.251  1.00 43.06  ? 189  GLN B O   1 
ATOM   5226 C  CB  . GLN B 1 189 ? -1.314  -36.615 66.731  1.00 45.06  ? 189  GLN B CB  1 
ATOM   5227 C  CG  . GLN B 1 189 ? -1.607  -36.506 65.232  1.00 43.01  ? 189  GLN B CG  1 
ATOM   5228 C  CD  . GLN B 1 189 ? -1.868  -37.856 64.580  1.00 47.89  ? 189  GLN B CD  1 
ATOM   5229 O  OE1 . GLN B 1 189 ? -2.770  -38.591 64.991  1.00 52.18  ? 189  GLN B OE1 1 
ATOM   5230 N  NE2 . GLN B 1 189 ? -1.099  -38.177 63.539  1.00 48.43  ? 189  GLN B NE2 1 
ATOM   5231 N  N   . ARG B 1 190 ? 1.687   -38.286 65.888  1.00 43.05  ? 190  ARG B N   1 
ATOM   5232 C  CA  . ARG B 1 190 ? 2.133   -39.611 65.459  1.00 42.69  ? 190  ARG B CA  1 
ATOM   5233 C  C   . ARG B 1 190 ? 2.951   -40.272 66.561  1.00 47.24  ? 190  ARG B C   1 
ATOM   5234 O  O   . ARG B 1 190 ? 4.035   -39.792 66.910  1.00 46.62  ? 190  ARG B O   1 
ATOM   5235 C  CB  . ARG B 1 190 ? 2.954   -39.522 64.173  1.00 42.69  ? 190  ARG B CB  1 
ATOM   5236 C  CG  . ARG B 1 190 ? 2.167   -39.072 62.961  1.00 43.67  ? 190  ARG B CG  1 
ATOM   5237 C  CD  . ARG B 1 190 ? 3.050   -38.908 61.730  1.00 38.63  ? 190  ARG B CD  1 
ATOM   5238 N  NE  . ARG B 1 190 ? 2.277   -38.256 60.682  1.00 39.82  ? 190  ARG B NE  1 
ATOM   5239 C  CZ  . ARG B 1 190 ? 2.783   -37.667 59.609  1.00 40.26  ? 190  ARG B CZ  1 
ATOM   5240 N  NH1 . ARG B 1 190 ? 4.084   -37.662 59.366  1.00 41.24  ? 190  ARG B NH1 1 
ATOM   5241 N  NH2 . ARG B 1 190 ? 1.960   -37.048 58.765  1.00 40.44  ? 190  ARG B NH2 1 
ATOM   5242 N  N   . ALA B 1 191 ? 2.437   -41.380 67.099  1.00 45.83  ? 191  ALA B N   1 
ATOM   5243 C  CA  . ALA B 1 191 ? 3.170   -42.117 68.123  1.00 45.98  ? 191  ALA B CA  1 
ATOM   5244 C  C   . ALA B 1 191 ? 4.413   -42.790 67.551  1.00 51.07  ? 191  ALA B C   1 
ATOM   5245 O  O   . ALA B 1 191 ? 5.438   -42.890 68.239  1.00 49.40  ? 191  ALA B O   1 
ATOM   5246 C  CB  . ALA B 1 191 ? 2.257   -43.154 68.773  1.00 48.84  ? 191  ALA B CB  1 
ATOM   5247 N  N   A ASN B 1 192 ? 4.335   -43.297 66.319  0.40 48.72  ? 192  ASN B N   1 
ATOM   5248 N  N   B ASN B 1 192 ? 4.351   -43.229 66.291  0.60 48.72  ? 192  ASN B N   1 
ATOM   5249 C  CA  A ASN B 1 192 ? 5.490   -43.880 65.635  0.40 47.27  ? 192  ASN B CA  1 
ATOM   5250 C  CA  B ASN B 1 192 ? 5.461   -43.893 65.611  0.60 47.24  ? 192  ASN B CA  1 
ATOM   5251 C  C   A ASN B 1 192 ? 5.730   -43.104 64.348  0.40 47.73  ? 192  ASN B C   1 
ATOM   5252 C  C   B ASN B 1 192 ? 5.758   -43.126 64.327  0.60 47.71  ? 192  ASN B C   1 
ATOM   5253 O  O   A ASN B 1 192 ? 5.254   -43.496 63.271  0.40 48.15  ? 192  ASN B O   1 
ATOM   5254 O  O   B ASN B 1 192 ? 5.350   -43.548 63.234  0.60 48.13  ? 192  ASN B O   1 
ATOM   5255 C  CB  A ASN B 1 192 ? 5.297   -45.367 65.351  0.40 48.89  ? 192  ASN B CB  1 
ATOM   5256 C  CB  B ASN B 1 192 ? 5.132   -45.357 65.319  0.60 48.98  ? 192  ASN B CB  1 
ATOM   5257 C  CG  A ASN B 1 192 ? 6.551   -46.010 64.786  0.40 47.96  ? 192  ASN B CG  1 
ATOM   5258 C  CG  B ASN B 1 192 ? 4.431   -46.036 66.479  0.60 45.39  ? 192  ASN B CG  1 
ATOM   5259 O  OD1 A ASN B 1 192 ? 7.605   -45.376 64.711  0.40 47.20  ? 192  ASN B OD1 1 
ATOM   5260 O  OD1 B ASN B 1 192 ? 4.937   -46.042 67.596  0.60 47.88  ? 192  ASN B OD1 1 
ATOM   5261 N  ND2 A ASN B 1 192 ? 6.445   -47.272 64.386  0.40 53.25  ? 192  ASN B ND2 1 
ATOM   5262 N  ND2 B ASN B 1 192 ? 3.259   -46.599 66.223  0.60 47.98  ? 192  ASN B ND2 1 
ATOM   5263 N  N   . PRO B 1 193 ? 6.475   -42.001 64.416  1.00 48.83  ? 193  PRO B N   1 
ATOM   5264 C  CA  . PRO B 1 193 ? 6.724   -41.201 63.205  1.00 44.80  ? 193  PRO B CA  1 
ATOM   5265 C  C   . PRO B 1 193 ? 7.403   -41.979 62.092  1.00 50.20  ? 193  PRO B C   1 
ATOM   5266 O  O   . PRO B 1 193 ? 7.335   -41.558 60.931  1.00 45.53  ? 193  PRO B O   1 
ATOM   5267 C  CB  . PRO B 1 193 ? 7.625   -40.057 63.699  1.00 45.54  ? 193  PRO B CB  1 
ATOM   5268 C  CG  . PRO B 1 193 ? 7.833   -40.249 65.149  1.00 52.44  ? 193  PRO B CG  1 
ATOM   5269 C  CD  . PRO B 1 193 ? 7.076   -41.438 65.634  1.00 51.61  ? 193  PRO B CD  1 
ATOM   5270 N  N   . ASP B 1 194 ? 8.074   -43.084 62.406  1.00 47.51  ? 194  ASP B N   1 
ATOM   5271 C  CA  . ASP B 1 194 ? 8.844   -43.822 61.418  1.00 50.60  ? 194  ASP B CA  1 
ATOM   5272 C  C   . ASP B 1 194 ? 8.065   -44.981 60.818  1.00 51.27  ? 194  ASP B C   1 
ATOM   5273 O  O   . ASP B 1 194 ? 8.618   -45.735 60.011  1.00 50.31  ? 194  ASP B O   1 
ATOM   5274 C  CB  . ASP B 1 194 ? 10.142  -44.319 62.052  1.00 55.03  ? 194  ASP B CB  1 
ATOM   5275 C  CG  . ASP B 1 194 ? 11.230  -43.272 62.010  1.00 61.69  ? 194  ASP B CG  1 
ATOM   5276 O  OD1 . ASP B 1 194 ? 10.922  -42.120 61.625  1.00 60.96  ? 194  ASP B OD1 1 
ATOM   5277 O  OD2 . ASP B 1 194 ? 12.382  -43.587 62.372  1.00 70.53  ? 194  ASP B OD2 1 
ATOM   5278 N  N   . ASP B 1 195 ? 6.801   -45.132 61.189  1.00 47.66  ? 195  ASP B N   1 
ATOM   5279 C  CA  . ASP B 1 195 ? 5.921   -46.096 60.553  1.00 48.89  ? 195  ASP B CA  1 
ATOM   5280 C  C   . ASP B 1 195 ? 5.950   -45.901 59.034  1.00 50.68  ? 195  ASP B C   1 
ATOM   5281 O  O   . ASP B 1 195 ? 5.898   -44.756 58.560  1.00 50.05  ? 195  ASP B O   1 
ATOM   5282 C  CB  . ASP B 1 195 ? 4.503   -45.911 61.099  1.00 48.61  ? 195  ASP B CB  1 
ATOM   5283 C  CG  . ASP B 1 195 ? 3.548   -47.004 60.666  1.00 52.88  ? 195  ASP B CG  1 
ATOM   5284 O  OD1 . ASP B 1 195 ? 3.328   -47.184 59.448  1.00 52.91  ? 195  ASP B OD1 1 
ATOM   5285 O  OD2 . ASP B 1 195 ? 3.002   -47.679 61.562  1.00 60.73  ? 195  ASP B OD2 1 
ATOM   5286 N  N   . PRO B 1 196 ? 6.050   -46.974 58.245  1.00 49.05  ? 196  PRO B N   1 
ATOM   5287 C  CA  . PRO B 1 196 ? 6.077   -46.806 56.782  1.00 46.91  ? 196  PRO B CA  1 
ATOM   5288 C  C   . PRO B 1 196 ? 4.849   -46.105 56.236  1.00 45.16  ? 196  PRO B C   1 
ATOM   5289 O  O   . PRO B 1 196 ? 4.901   -45.571 55.125  1.00 47.68  ? 196  PRO B O   1 
ATOM   5290 C  CB  . PRO B 1 196 ? 6.174   -48.247 56.260  1.00 48.41  ? 196  PRO B CB  1 
ATOM   5291 C  CG  . PRO B 1 196 ? 6.741   -49.032 57.410  1.00 47.77  ? 196  PRO B CG  1 
ATOM   5292 C  CD  . PRO B 1 196 ? 6.191   -48.385 58.649  1.00 51.01  ? 196  PRO B CD  1 
ATOM   5293 N  N   . ALA B 1 197 ? 3.741   -46.097 56.981  1.00 44.95  ? 197  ALA B N   1 
ATOM   5294 C  CA  . ALA B 1 197 ? 2.558   -45.373 56.533  1.00 46.42  ? 197  ALA B CA  1 
ATOM   5295 C  C   . ALA B 1 197 ? 2.857   -43.904 56.254  1.00 45.31  ? 197  ALA B C   1 
ATOM   5296 O  O   . ALA B 1 197 ? 2.122   -43.268 55.489  1.00 46.95  ? 197  ALA B O   1 
ATOM   5297 C  CB  . ALA B 1 197 ? 1.446   -45.506 57.581  1.00 48.31  ? 197  ALA B CB  1 
ATOM   5298 N  N   . TYR B 1 198 ? 3.938   -43.362 56.825  1.00 41.44  ? 198  TYR B N   1 
ATOM   5299 C  CA  . TYR B 1 198 ? 4.281   -41.950 56.687  1.00 45.37  ? 198  TYR B CA  1 
ATOM   5300 C  C   . TYR B 1 198 ? 5.396   -41.700 55.679  1.00 44.72  ? 198  TYR B C   1 
ATOM   5301 O  O   . TYR B 1 198 ? 5.826   -40.551 55.528  1.00 42.69  ? 198  TYR B O   1 
ATOM   5302 C  CB  . TYR B 1 198 ? 4.686   -41.375 58.055  1.00 38.13  ? 198  TYR B CB  1 
ATOM   5303 C  CG  . TYR B 1 198 ? 3.645   -41.594 59.127  1.00 40.23  ? 198  TYR B CG  1 
ATOM   5304 C  CD1 . TYR B 1 198 ? 3.954   -42.293 60.281  1.00 43.78  ? 198  TYR B CD1 1 
ATOM   5305 C  CD2 . TYR B 1 198 ? 2.350   -41.118 58.973  1.00 42.46  ? 198  TYR B CD2 1 
ATOM   5306 C  CE1 . TYR B 1 198 ? 3.004   -42.508 61.262  1.00 47.28  ? 198  TYR B CE1 1 
ATOM   5307 C  CE2 . TYR B 1 198 ? 1.396   -41.322 59.944  1.00 45.79  ? 198  TYR B CE2 1 
ATOM   5308 C  CZ  . TYR B 1 198 ? 1.725   -42.017 61.089  1.00 47.23  ? 198  TYR B CZ  1 
ATOM   5309 O  OH  . TYR B 1 198 ? 0.777   -42.221 62.066  1.00 51.23  ? 198  TYR B OH  1 
ATOM   5310 N  N   . ASP B 1 199 ? 5.879   -42.745 54.993  1.00 42.83  ? 199  ASP B N   1 
ATOM   5311 C  CA  . ASP B 1 199 ? 6.964   -42.574 54.027  1.00 43.95  ? 199  ASP B CA  1 
ATOM   5312 C  C   . ASP B 1 199 ? 6.605   -41.542 52.964  1.00 46.02  ? 199  ASP B C   1 
ATOM   5313 O  O   . ASP B 1 199 ? 7.412   -40.665 52.634  1.00 47.03  ? 199  ASP B O   1 
ATOM   5314 C  CB  . ASP B 1 199 ? 7.305   -43.914 53.365  1.00 45.37  ? 199  ASP B CB  1 
ATOM   5315 C  CG  . ASP B 1 199 ? 8.065   -44.846 54.292  1.00 50.55  ? 199  ASP B CG  1 
ATOM   5316 O  OD1 . ASP B 1 199 ? 8.458   -44.395 55.388  1.00 46.63  ? 199  ASP B OD1 1 
ATOM   5317 O  OD2 . ASP B 1 199 ? 8.283   -46.023 53.922  1.00 51.36  ? 199  ASP B OD2 1 
ATOM   5318 N  N   . GLU B 1 200 ? 5.399   -41.652 52.401  1.00 46.67  ? 200  GLU B N   1 
ATOM   5319 C  CA  . GLU B 1 200 ? 4.952   -40.707 51.384  1.00 50.28  ? 200  GLU B CA  1 
ATOM   5320 C  C   . GLU B 1 200 ? 4.793   -39.302 51.961  1.00 47.20  ? 200  GLU B C   1 
ATOM   5321 O  O   . GLU B 1 200 ? 5.161   -38.316 51.312  1.00 46.95  ? 200  GLU B O   1 
ATOM   5322 C  CB  . GLU B 1 200 ? 3.640   -41.198 50.768  1.00 47.85  ? 200  GLU B CB  1 
ATOM   5323 C  CG  . GLU B 1 200 ? 3.078   -40.318 49.670  1.00 50.05  ? 200  GLU B CG  1 
ATOM   5324 C  CD  . GLU B 1 200 ? 4.088   -40.019 48.573  1.00 57.24  ? 200  GLU B CD  1 
ATOM   5325 O  OE1 . GLU B 1 200 ? 3.887   -39.036 47.831  1.00 62.59  ? 200  GLU B OE1 1 
ATOM   5326 O  OE2 . GLU B 1 200 ? 5.085   -40.761 48.451  1.00 65.01  ? 200  GLU B OE2 1 
ATOM   5327 N  N   . ASN B 1 201 ? 4.237   -39.188 53.170  1.00 43.55  ? 201  ASN B N   1 
ATOM   5328 C  CA  . ASN B 1 201 ? 4.159   -37.883 53.823  1.00 40.40  ? 201  ASN B CA  1 
ATOM   5329 C  C   . ASN B 1 201 ? 5.524   -37.218 53.856  1.00 43.03  ? 201  ASN B C   1 
ATOM   5330 O  O   . ASN B 1 201 ? 5.657   -36.026 53.553  1.00 45.48  ? 201  ASN B O   1 
ATOM   5331 C  CB  . ASN B 1 201 ? 3.608   -38.024 55.240  1.00 45.64  ? 201  ASN B CB  1 
ATOM   5332 C  CG  . ASN B 1 201 ? 2.204   -38.567 55.268  1.00 49.71  ? 201  ASN B CG  1 
ATOM   5333 O  OD1 . ASN B 1 201 ? 1.973   -39.714 55.654  1.00 51.95  ? 201  ASN B OD1 1 
ATOM   5334 N  ND2 . ASN B 1 201 ? 1.249   -37.740 54.871  1.00 50.71  ? 201  ASN B ND2 1 
ATOM   5335 N  N   . LYS B 1 202 ? 6.560   -37.985 54.212  1.00 41.46  ? 202  LYS B N   1 
ATOM   5336 C  CA  . LYS B 1 202 ? 7.903   -37.424 54.292  1.00 44.74  ? 202  LYS B CA  1 
ATOM   5337 C  C   . LYS B 1 202 ? 8.409   -37.026 52.913  1.00 45.81  ? 202  LYS B C   1 
ATOM   5338 O  O   . LYS B 1 202 ? 9.036   -35.972 52.754  1.00 43.23  ? 202  LYS B O   1 
ATOM   5339 C  CB  . LYS B 1 202 ? 8.847   -38.430 54.952  1.00 43.11  ? 202  LYS B CB  1 
ATOM   5340 C  CG  . LYS B 1 202 ? 8.422   -38.829 56.361  1.00 45.65  ? 202  LYS B CG  1 
ATOM   5341 C  CD  . LYS B 1 202 ? 9.290   -39.946 56.948  1.00 47.02  ? 202  LYS B CD  1 
ATOM   5342 C  CE  . LYS B 1 202 ? 8.901   -40.213 58.406  1.00 45.67  ? 202  LYS B CE  1 
ATOM   5343 N  NZ  . LYS B 1 202 ? 9.572   -41.410 58.958  1.00 45.90  ? 202  LYS B NZ  1 
ATOM   5344 N  N   . ARG B 1 203 ? 8.143   -37.857 51.906  1.00 46.03  ? 203  ARG B N   1 
ATOM   5345 C  CA  . ARG B 1 203 ? 8.482   -37.497 50.534  1.00 44.53  ? 203  ARG B CA  1 
ATOM   5346 C  C   . ARG B 1 203 ? 7.800   -36.198 50.128  1.00 43.36  ? 203  ARG B C   1 
ATOM   5347 O  O   . ARG B 1 203 ? 8.442   -35.275 49.616  1.00 44.48  ? 203  ARG B O   1 
ATOM   5348 C  CB  . ARG B 1 203 ? 8.084   -38.629 49.587  1.00 46.70  ? 203  ARG B CB  1 
ATOM   5349 C  CG  . ARG B 1 203 ? 8.800   -38.584 48.241  1.00 57.34  ? 203  ARG B CG  1 
ATOM   5350 C  CD  . ARG B 1 203 ? 7.939   -39.199 47.135  1.00 58.21  ? 203  ARG B CD  1 
ATOM   5351 N  NE  . ARG B 1 203 ? 6.627   -38.562 47.046  1.00 61.76  ? 203  ARG B NE  1 
ATOM   5352 C  CZ  . ARG B 1 203 ? 6.381   -37.410 46.433  1.00 63.42  ? 203  ARG B CZ  1 
ATOM   5353 N  NH1 . ARG B 1 203 ? 7.342   -36.726 45.829  1.00 59.83  ? 203  ARG B NH1 1 
ATOM   5354 N  NH2 . ARG B 1 203 ? 5.141   -36.926 46.436  1.00 59.47  ? 203  ARG B NH2 1 
ATOM   5355 N  N   . GLN B 1 204 ? 6.485   -36.114 50.338  1.00 43.33  ? 204  GLN B N   1 
ATOM   5356 C  CA  . GLN B 1 204 ? 5.761   -34.898 49.983  1.00 43.69  ? 204  GLN B CA  1 
ATOM   5357 C  C   . GLN B 1 204 ? 6.293   -33.697 50.752  1.00 41.73  ? 204  GLN B C   1 
ATOM   5358 O  O   . GLN B 1 204 ? 6.427   -32.602 50.195  1.00 42.54  ? 204  GLN B O   1 
ATOM   5359 C  CB  . GLN B 1 204 ? 4.268   -35.083 50.249  1.00 42.99  ? 204  GLN B CB  1 
ATOM   5360 C  CG  . GLN B 1 204 ? 3.456   -33.860 49.928  1.00 44.01  ? 204  GLN B CG  1 
ATOM   5361 C  CD  . GLN B 1 204 ? 3.438   -33.572 48.443  1.00 46.88  ? 204  GLN B CD  1 
ATOM   5362 O  OE1 . GLN B 1 204 ? 4.168   -32.705 47.955  1.00 48.65  ? 204  GLN B OE1 1 
ATOM   5363 N  NE2 . GLN B 1 204 ? 2.615   -34.306 47.714  1.00 50.58  ? 204  GLN B NE2 1 
ATOM   5364 N  N   . PHE B 1 205 ? 6.588   -33.885 52.042  1.00 39.44  ? 205  PHE B N   1 
ATOM   5365 C  CA  . PHE B 1 205 ? 7.138   -32.804 52.854  1.00 40.83  ? 205  PHE B CA  1 
ATOM   5366 C  C   . PHE B 1 205 ? 8.419   -32.251 52.235  1.00 42.24  ? 205  PHE B C   1 
ATOM   5367 O  O   . PHE B 1 205 ? 8.582   -31.033 52.092  1.00 40.56  ? 205  PHE B O   1 
ATOM   5368 C  CB  . PHE B 1 205 ? 7.375   -33.319 54.277  1.00 38.58  ? 205  PHE B CB  1 
ATOM   5369 C  CG  . PHE B 1 205 ? 7.705   -32.241 55.292  1.00 40.49  ? 205  PHE B CG  1 
ATOM   5370 C  CD1 . PHE B 1 205 ? 6.809   -31.223 55.573  1.00 37.59  ? 205  PHE B CD1 1 
ATOM   5371 C  CD2 . PHE B 1 205 ? 8.898   -32.292 56.005  1.00 41.52  ? 205  PHE B CD2 1 
ATOM   5372 C  CE1 . PHE B 1 205 ? 7.113   -30.251 56.534  1.00 37.16  ? 205  PHE B CE1 1 
ATOM   5373 C  CE2 . PHE B 1 205 ? 9.210   -31.334 56.954  1.00 37.73  ? 205  PHE B CE2 1 
ATOM   5374 C  CZ  . PHE B 1 205 ? 8.321   -30.312 57.219  1.00 40.09  ? 205  PHE B CZ  1 
ATOM   5375 N  N   . GLN B 1 206 ? 9.334   -33.130 51.834  1.00 43.75  ? 206  GLN B N   1 
ATOM   5376 C  CA  . GLN B 1 206 ? 10.573  -32.623 51.261  1.00 42.23  ? 206  GLN B CA  1 
ATOM   5377 C  C   . GLN B 1 206 ? 10.318  -31.933 49.932  1.00 41.99  ? 206  GLN B C   1 
ATOM   5378 O  O   . GLN B 1 206 ? 10.986  -30.946 49.606  1.00 42.45  ? 206  GLN B O   1 
ATOM   5379 C  CB  . GLN B 1 206 ? 11.591  -33.751 51.121  1.00 44.87  ? 206  GLN B CB  1 
ATOM   5380 C  CG  . GLN B 1 206 ? 11.937  -34.300 52.487  1.00 47.72  ? 206  GLN B CG  1 
ATOM   5381 C  CD  . GLN B 1 206 ? 12.854  -33.377 53.274  1.00 53.33  ? 206  GLN B CD  1 
ATOM   5382 O  OE1 . GLN B 1 206 ? 13.591  -32.568 52.703  1.00 56.61  ? 206  GLN B OE1 1 
ATOM   5383 N  NE2 . GLN B 1 206 ? 12.734  -33.425 54.597  1.00 47.30  ? 206  GLN B NE2 1 
ATOM   5384 N  N   . GLU B 1 207 ? 9.338   -32.417 49.170  1.00 39.31  ? 207  GLU B N   1 
ATOM   5385 C  CA  . GLU B 1 207 ? 9.005   -31.772 47.906  1.00 43.11  ? 207  GLU B CA  1 
ATOM   5386 C  C   . GLU B 1 207 ? 8.422   -30.382 48.136  1.00 43.73  ? 207  GLU B C   1 
ATOM   5387 O  O   . GLU B 1 207 ? 8.750   -29.435 47.409  1.00 40.72  ? 207  GLU B O   1 
ATOM   5388 C  CB  . GLU B 1 207 ? 8.037   -32.658 47.121  1.00 45.73  ? 207  GLU B CB  1 
ATOM   5389 C  CG  . GLU B 1 207 ? 7.413   -31.996 45.908  1.00 55.64  ? 207  GLU B CG  1 
ATOM   5390 C  CD  . GLU B 1 207 ? 6.189   -32.743 45.405  1.00 66.55  ? 207  GLU B CD  1 
ATOM   5391 O  OE1 . GLU B 1 207 ? 5.141   -32.096 45.185  1.00 68.19  ? 207  GLU B OE1 1 
ATOM   5392 O  OE2 . GLU B 1 207 ? 6.282   -33.979 45.228  1.00 69.08  ? 207  GLU B OE2 1 
ATOM   5393 N  N   . ASP B 1 208 ? 7.551   -30.246 49.141  1.00 40.73  ? 208  ASP B N   1 
ATOM   5394 C  CA  . ASP B 1 208 ? 6.995   -28.940 49.473  1.00 40.10  ? 208  ASP B CA  1 
ATOM   5395 C  C   . ASP B 1 208 ? 8.074   -27.993 49.981  1.00 41.21  ? 208  ASP B C   1 
ATOM   5396 O  O   . ASP B 1 208 ? 8.036   -26.787 49.702  1.00 41.45  ? 208  ASP B O   1 
ATOM   5397 C  CB  . ASP B 1 208 ? 5.878   -29.095 50.506  1.00 38.79  ? 208  ASP B CB  1 
ATOM   5398 C  CG  . ASP B 1 208 ? 4.622   -29.684 49.911  1.00 44.69  ? 208  ASP B CG  1 
ATOM   5399 O  OD1 . ASP B 1 208 ? 4.381   -29.441 48.708  1.00 43.84  ? 208  ASP B OD1 1 
ATOM   5400 O  OD2 . ASP B 1 208 ? 3.874   -30.378 50.641  1.00 43.45  ? 208  ASP B OD2 1 
ATOM   5401 N  N   . ILE B 1 209 ? 9.048   -28.514 50.729  1.00 41.28  ? 209  ILE B N   1 
ATOM   5402 C  CA  . ILE B 1 209 ? 10.152  -27.669 51.171  1.00 39.78  ? 209  ILE B CA  1 
ATOM   5403 C  C   . ILE B 1 209 ? 10.927  -27.155 49.965  1.00 40.63  ? 209  ILE B C   1 
ATOM   5404 O  O   . ILE B 1 209 ? 11.380  -26.002 49.939  1.00 42.94  ? 209  ILE B O   1 
ATOM   5405 C  CB  . ILE B 1 209 ? 11.051  -28.442 52.154  1.00 40.23  ? 209  ILE B CB  1 
ATOM   5406 C  CG1 . ILE B 1 209 ? 10.302  -28.650 53.478  1.00 40.06  ? 209  ILE B CG1 1 
ATOM   5407 C  CG2 . ILE B 1 209 ? 12.380  -27.705 52.375  1.00 41.38  ? 209  ILE B CG2 1 
ATOM   5408 C  CD1 . ILE B 1 209 ? 11.052  -29.480 54.507  1.00 43.54  ? 209  ILE B CD1 1 
ATOM   5409 N  N   . LYS B 1 210 ? 11.074  -27.990 48.938  1.00 41.05  ? 210  LYS B N   1 
ATOM   5410 C  CA  . LYS B 1 210 ? 11.863  -27.573 47.785  1.00 40.40  ? 210  LYS B CA  1 
ATOM   5411 C  C   . LYS B 1 210 ? 11.115  -26.532 46.960  1.00 40.75  ? 210  LYS B C   1 
ATOM   5412 O  O   . LYS B 1 210 ? 11.729  -25.597 46.431  1.00 43.14  ? 210  LYS B O   1 
ATOM   5413 C  CB  . LYS B 1 210 ? 12.238  -28.776 46.923  1.00 42.92  ? 210  LYS B CB  1 
ATOM   5414 C  CG  . LYS B 1 210 ? 12.388  -28.419 45.449  1.00 54.40  ? 210  LYS B CG  1 
ATOM   5415 C  CD  . LYS B 1 210 ? 13.097  -29.521 44.669  1.00 61.01  ? 210  LYS B CD  1 
ATOM   5416 C  CE  . LYS B 1 210 ? 13.668  -28.979 43.364  1.00 57.97  ? 210  LYS B CE  1 
ATOM   5417 N  NZ  . LYS B 1 210 ? 12.594  -28.571 42.415  1.00 64.14  ? 210  LYS B NZ  1 
ATOM   5418 N  N   . VAL B 1 211 ? 9.789   -26.661 46.865  1.00 38.34  ? 211  VAL B N   1 
ATOM   5419 C  CA  . VAL B 1 211 ? 8.983   -25.641 46.194  1.00 42.03  ? 211  VAL B CA  1 
ATOM   5420 C  C   . VAL B 1 211 ? 9.182   -24.286 46.864  1.00 40.49  ? 211  VAL B C   1 
ATOM   5421 O  O   . VAL B 1 211 ? 9.364   -23.258 46.197  1.00 40.90  ? 211  VAL B O   1 
ATOM   5422 C  CB  . VAL B 1 211 ? 7.497   -26.051 46.179  1.00 38.87  ? 211  VAL B CB  1 
ATOM   5423 C  CG1 . VAL B 1 211 ? 6.617   -24.869 45.783  1.00 39.79  ? 211  VAL B CG1 1 
ATOM   5424 C  CG2 . VAL B 1 211 ? 7.274   -27.206 45.208  1.00 42.56  ? 211  VAL B CG2 1 
ATOM   5425 N  N   . MET B 1 212 ? 9.143   -24.256 48.199  1.00 41.27  ? 212  MET B N   1 
ATOM   5426 C  CA  . MET B 1 212 ? 9.338   -22.977 48.874  1.00 40.50  ? 212  MET B CA  1 
ATOM   5427 C  C   . MET B 1 212 ? 10.749  -22.440 48.657  1.00 40.18  ? 212  MET B C   1 
ATOM   5428 O  O   . MET B 1 212 ? 10.917  -21.242 48.417  1.00 43.14  ? 212  MET B O   1 
ATOM   5429 C  CB  . MET B 1 212 ? 8.985   -23.087 50.364  1.00 38.88  ? 212  MET B CB  1 
ATOM   5430 C  CG  . MET B 1 212 ? 7.546   -23.537 50.588  1.00 37.94  ? 212  MET B CG  1 
ATOM   5431 S  SD  . MET B 1 212 ? 7.065   -23.519 52.342  1.00 45.90  ? 212  MET B SD  1 
ATOM   5432 C  CE  . MET B 1 212 ? 8.566   -24.257 52.990  1.00 41.35  ? 212  MET B CE  1 
ATOM   5433 N  N   . ASN B 1 213 ? 11.773  -23.303 48.706  1.00 38.30  ? 213  ASN B N   1 
ATOM   5434 C  CA  . ASN B 1 213 ? 13.134  -22.819 48.464  1.00 37.01  ? 213  ASN B CA  1 
ATOM   5435 C  C   . ASN B 1 213 ? 13.347  -22.389 47.019  1.00 44.52  ? 213  ASN B C   1 
ATOM   5436 O  O   . ASN B 1 213 ? 14.140  -21.477 46.761  1.00 46.79  ? 213  ASN B O   1 
ATOM   5437 C  CB  . ASN B 1 213 ? 14.175  -23.870 48.855  1.00 39.72  ? 213  ASN B CB  1 
ATOM   5438 C  CG  . ASN B 1 213 ? 14.429  -23.911 50.354  1.00 47.41  ? 213  ASN B CG  1 
ATOM   5439 O  OD1 . ASN B 1 213 ? 13.712  -24.567 51.110  1.00 47.72  ? 213  ASN B OD1 1 
ATOM   5440 N  ND2 . ASN B 1 213 ? 15.474  -23.213 50.788  1.00 52.15  ? 213  ASN B ND2 1 
ATOM   5441 N  N   . ASP B 1 214 ? 12.675  -23.029 46.063  1.00 42.82  ? 214  ASP B N   1 
ATOM   5442 C  CA  . ASP B 1 214 ? 12.785  -22.564 44.683  1.00 45.05  ? 214  ASP B CA  1 
ATOM   5443 C  C   . ASP B 1 214 ? 12.321  -21.116 44.564  1.00 42.42  ? 214  ASP B C   1 
ATOM   5444 O  O   . ASP B 1 214 ? 12.978  -20.288 43.922  1.00 45.10  ? 214  ASP B O   1 
ATOM   5445 C  CB  . ASP B 1 214 ? 11.984  -23.472 43.751  1.00 47.17  ? 214  ASP B CB  1 
ATOM   5446 C  CG  . ASP B 1 214 ? 12.655  -24.817 43.527  1.00 49.32  ? 214  ASP B CG  1 
ATOM   5447 O  OD1 . ASP B 1 214 ? 13.822  -24.988 43.954  1.00 50.13  ? 214  ASP B OD1 1 
ATOM   5448 O  OD2 . ASP B 1 214 ? 12.013  -25.700 42.917  1.00 56.02  ? 214  ASP B OD2 1 
ATOM   5449 N  N   . LEU B 1 215 ? 11.194  -20.785 45.197  1.00 41.96  ? 215  LEU B N   1 
ATOM   5450 C  CA  . LEU B 1 215 ? 10.708  -19.410 45.149  1.00 40.42  ? 215  LEU B CA  1 
ATOM   5451 C  C   . LEU B 1 215 ? 11.688  -18.451 45.813  1.00 46.08  ? 215  LEU B C   1 
ATOM   5452 O  O   . LEU B 1 215 ? 11.923  -17.346 45.308  1.00 43.24  ? 215  LEU B O   1 
ATOM   5453 C  CB  . LEU B 1 215 ? 9.334   -19.309 45.802  1.00 43.25  ? 215  LEU B CB  1 
ATOM   5454 C  CG  . LEU B 1 215 ? 8.907   -17.848 45.910  1.00 44.40  ? 215  LEU B CG  1 
ATOM   5455 C  CD1 . LEU B 1 215 ? 8.359   -17.363 44.570  1.00 49.99  ? 215  LEU B CD1 1 
ATOM   5456 C  CD2 . LEU B 1 215 ? 7.885   -17.705 46.994  1.00 48.98  ? 215  LEU B CD2 1 
ATOM   5457 N  N   . VAL B 1 216 ? 12.264  -18.852 46.952  1.00 39.79  ? 216  VAL B N   1 
ATOM   5458 C  CA  . VAL B 1 216 ? 13.292  -18.034 47.595  1.00 39.58  ? 216  VAL B CA  1 
ATOM   5459 C  C   . VAL B 1 216 ? 14.450  -17.776 46.639  1.00 44.51  ? 216  VAL B C   1 
ATOM   5460 O  O   . VAL B 1 216 ? 15.005  -16.670 46.604  1.00 47.09  ? 216  VAL B O   1 
ATOM   5461 C  CB  . VAL B 1 216 ? 13.768  -18.707 48.897  1.00 38.67  ? 216  VAL B CB  1 
ATOM   5462 C  CG1 . VAL B 1 216 ? 14.947  -17.949 49.491  1.00 39.22  ? 216  VAL B CG1 1 
ATOM   5463 C  CG2 . VAL B 1 216 ? 12.628  -18.784 49.862  1.00 37.62  ? 216  VAL B CG2 1 
ATOM   5464 N  N   . ASP B 1 217 ? 14.842  -18.788 45.854  1.00 47.61  ? 217  ASP B N   1 
ATOM   5465 C  CA  . ASP B 1 217 ? 15.877  -18.583 44.840  1.00 46.53  ? 217  ASP B CA  1 
ATOM   5466 C  C   . ASP B 1 217 ? 15.478  -17.478 43.870  1.00 48.95  ? 217  ASP B C   1 
ATOM   5467 O  O   . ASP B 1 217 ? 16.278  -16.585 43.558  1.00 47.15  ? 217  ASP B O   1 
ATOM   5468 C  CB  . ASP B 1 217 ? 16.148  -19.877 44.060  1.00 49.93  ? 217  ASP B CB  1 
ATOM   5469 C  CG  . ASP B 1 217 ? 16.758  -20.982 44.912  1.00 51.09  ? 217  ASP B CG  1 
ATOM   5470 O  OD1 . ASP B 1 217 ? 17.316  -20.688 45.985  1.00 55.55  ? 217  ASP B OD1 1 
ATOM   5471 O  OD2 . ASP B 1 217 ? 16.693  -22.156 44.480  1.00 56.17  ? 217  ASP B OD2 1 
ATOM   5472 N  N   . LYS B 1 218 ? 14.244  -17.543 43.359  1.00 46.76  ? 218  LYS B N   1 
ATOM   5473 C  CA  . LYS B 1 218 ? 13.763  -16.545 42.407  1.00 44.65  ? 218  LYS B CA  1 
ATOM   5474 C  C   . LYS B 1 218 ? 13.804  -15.144 43.003  1.00 50.01  ? 218  LYS B C   1 
ATOM   5475 O  O   . LYS B 1 218 ? 14.157  -14.175 42.315  1.00 45.76  ? 218  LYS B O   1 
ATOM   5476 C  CB  . LYS B 1 218 ? 12.344  -16.914 41.957  1.00 48.71  ? 218  LYS B CB  1 
ATOM   5477 C  CG  . LYS B 1 218 ? 12.308  -17.893 40.780  1.00 52.55  ? 218  LYS B CG  1 
ATOM   5478 C  CD  . LYS B 1 218 ? 10.991  -18.664 40.673  1.00 58.29  ? 218  LYS B CD  1 
ATOM   5479 C  CE  . LYS B 1 218 ? 11.054  -19.968 41.497  1.00 58.04  ? 218  LYS B CE  1 
ATOM   5480 N  NZ  . LYS B 1 218 ? 9.786   -20.368 42.201  1.00 51.65  ? 218  LYS B NZ  1 
ATOM   5481 N  N   . ILE B 1 219 ? 13.453  -15.014 44.284  1.00 40.39  ? 219  ILE B N   1 
ATOM   5482 C  CA  . ILE B 1 219 ? 13.436  -13.693 44.901  1.00 39.86  ? 219  ILE B CA  1 
ATOM   5483 C  C   . ILE B 1 219 ? 14.848  -13.144 45.020  1.00 42.69  ? 219  ILE B C   1 
ATOM   5484 O  O   . ILE B 1 219 ? 15.091  -11.959 44.757  1.00 40.66  ? 219  ILE B O   1 
ATOM   5485 C  CB  . ILE B 1 219 ? 12.728  -13.745 46.268  1.00 39.62  ? 219  ILE B CB  1 
ATOM   5486 C  CG1 . ILE B 1 219 ? 11.226  -13.998 46.077  1.00 38.97  ? 219  ILE B CG1 1 
ATOM   5487 C  CG2 . ILE B 1 219 ? 12.987  -12.458 47.050  1.00 42.04  ? 219  ILE B CG2 1 
ATOM   5488 C  CD1 . ILE B 1 219 ? 10.472  -14.286 47.377  1.00 34.67  ? 219  ILE B CD1 1 
ATOM   5489 N  N   . ILE B 1 220 ? 15.802  -13.992 45.407  1.00 43.19  ? 220  ILE B N   1 
ATOM   5490 C  CA  . ILE B 1 220 ? 17.175  -13.528 45.585  1.00 41.78  ? 220  ILE B CA  1 
ATOM   5491 C  C   . ILE B 1 220 ? 17.793  -13.162 44.245  1.00 47.31  ? 220  ILE B C   1 
ATOM   5492 O  O   . ILE B 1 220 ? 18.490  -12.146 44.125  1.00 49.62  ? 220  ILE B O   1 
ATOM   5493 C  CB  . ILE B 1 220 ? 18.006  -14.594 46.318  1.00 41.56  ? 220  ILE B CB  1 
ATOM   5494 C  CG1 . ILE B 1 220 ? 17.453  -14.817 47.727  1.00 47.01  ? 220  ILE B CG1 1 
ATOM   5495 C  CG2 . ILE B 1 220 ? 19.491  -14.193 46.353  1.00 45.13  ? 220  ILE B CG2 1 
ATOM   5496 C  CD1 . ILE B 1 220 ? 18.133  -15.944 48.482  1.00 55.77  ? 220  ILE B CD1 1 
ATOM   5497 N  N   . ALA B 1 221 ? 17.558  -13.988 43.221  1.00 49.78  ? 221  ALA B N   1 
ATOM   5498 C  CA  . ALA B 1 221 ? 18.059  -13.685 41.881  1.00 56.62  ? 221  ALA B CA  1 
ATOM   5499 C  C   . ALA B 1 221 ? 17.432  -12.410 41.328  1.00 54.67  ? 221  ALA B C   1 
ATOM   5500 O  O   . ALA B 1 221 ? 18.124  -11.586 40.717  1.00 59.37  ? 221  ALA B O   1 
ATOM   5501 C  CB  . ALA B 1 221 ? 17.794  -14.863 40.941  1.00 51.16  ? 221  ALA B CB  1 
ATOM   5502 N  N   . ASP B 1 222 ? 16.119  -12.238 41.519  1.00 54.48  ? 222  ASP B N   1 
ATOM   5503 C  CA  . ASP B 1 222 ? 15.441  -11.013 41.102  1.00 50.77  ? 222  ASP B CA  1 
ATOM   5504 C  C   . ASP B 1 222 ? 16.137  -9.786  41.677  1.00 58.63  ? 222  ASP B C   1 
ATOM   5505 O  O   . ASP B 1 222 ? 16.416  -8.816  40.963  1.00 59.15  ? 222  ASP B O   1 
ATOM   5506 C  CB  . ASP B 1 222 ? 13.969  -11.067 41.538  1.00 54.60  ? 222  ASP B CB  1 
ATOM   5507 C  CG  . ASP B 1 222 ? 13.157  -9.861  41.071  1.00 55.44  ? 222  ASP B CG  1 
ATOM   5508 O  OD1 . ASP B 1 222 ? 13.177  -8.812  41.756  1.00 55.98  ? 222  ASP B OD1 1 
ATOM   5509 O  OD2 . ASP B 1 222 ? 12.489  -9.965  40.017  1.00 51.55  ? 222  ASP B OD2 1 
ATOM   5510 N  N   . ARG B 1 223 ? 16.447  -9.826  42.974  1.00 52.23  ? 223  ARG B N   1 
ATOM   5511 C  CA  . ARG B 1 223 ? 17.083  -8.681  43.613  1.00 52.02  ? 223  ARG B CA  1 
ATOM   5512 C  C   . ARG B 1 223 ? 18.519  -8.498  43.138  1.00 58.61  ? 223  ARG B C   1 
ATOM   5513 O  O   . ARG B 1 223 ? 18.954  -7.366  42.902  1.00 57.76  ? 223  ARG B O   1 
ATOM   5514 C  CB  . ARG B 1 223 ? 17.051  -8.836  45.129  1.00 44.56  ? 223  ARG B CB  1 
ATOM   5515 C  CG  . ARG B 1 223 ? 17.715  -7.685  45.839  1.00 46.39  ? 223  ARG B CG  1 
ATOM   5516 C  CD  . ARG B 1 223 ? 17.017  -6.401  45.460  1.00 44.20  ? 223  ARG B CD  1 
ATOM   5517 N  NE  . ARG B 1 223 ? 15.588  -6.452  45.760  1.00 41.73  ? 223  ARG B NE  1 
ATOM   5518 C  CZ  . ARG B 1 223 ? 15.038  -5.933  46.851  1.00 42.92  ? 223  ARG B CZ  1 
ATOM   5519 N  NH1 . ARG B 1 223 ? 15.767  -5.318  47.766  1.00 41.85  ? 223  ARG B NH1 1 
ATOM   5520 N  NH2 . ARG B 1 223 ? 13.720  -6.035  47.030  1.00 41.22  ? 223  ARG B NH2 1 
ATOM   5521 N  N   . LYS B 1 224 ? 19.280  -9.590  43.016  1.00 56.38  ? 224  LYS B N   1 
ATOM   5522 C  CA  . LYS B 1 224 ? 20.663  -9.458  42.566  1.00 66.22  ? 224  LYS B CA  1 
ATOM   5523 C  C   . LYS B 1 224 ? 20.742  -8.897  41.151  1.00 68.77  ? 224  LYS B C   1 
ATOM   5524 O  O   . LYS B 1 224 ? 21.718  -8.219  40.807  1.00 73.11  ? 224  LYS B O   1 
ATOM   5525 C  CB  . LYS B 1 224 ? 21.386  -10.805 42.641  1.00 66.30  ? 224  LYS B CB  1 
ATOM   5526 C  CG  . LYS B 1 224 ? 22.906  -10.671 42.548  1.00 79.44  ? 224  LYS B CG  1 
ATOM   5527 C  CD  . LYS B 1 224 ? 23.623  -11.944 42.979  1.00 87.50  ? 224  LYS B CD  1 
ATOM   5528 C  CE  . LYS B 1 224 ? 24.586  -12.439 41.905  1.00 90.60  ? 224  LYS B CE  1 
ATOM   5529 N  NZ  . LYS B 1 224 ? 23.949  -13.412 40.971  1.00 91.72  ? 224  LYS B NZ  1 
ATOM   5530 N  N   . ALA B 1 225 ? 19.732  -9.157  40.325  1.00 67.34  ? 225  ALA B N   1 
ATOM   5531 C  CA  . ALA B 1 225 ? 19.705  -8.702  38.942  1.00 70.09  ? 225  ALA B CA  1 
ATOM   5532 C  C   . ALA B 1 225 ? 19.005  -7.363  38.770  1.00 76.92  ? 225  ALA B C   1 
ATOM   5533 O  O   . ALA B 1 225 ? 18.956  -6.846  37.648  1.00 77.94  ? 225  ALA B O   1 
ATOM   5534 C  CB  . ALA B 1 225 ? 19.021  -9.748  38.057  1.00 65.52  ? 225  ALA B CB  1 
ATOM   5535 N  N   . SER B 1 226 ? 18.466  -6.793  39.844  1.00 75.66  ? 226  SER B N   1 
ATOM   5536 C  CA  . SER B 1 226 ? 17.679  -5.568  39.758  1.00 82.06  ? 226  SER B CA  1 
ATOM   5537 C  C   . SER B 1 226 ? 18.611  -4.365  39.682  1.00 91.67  ? 226  SER B C   1 
ATOM   5538 O  O   . SER B 1 226 ? 19.294  -4.037  40.659  1.00 90.51  ? 226  SER B O   1 
ATOM   5539 C  CB  . SER B 1 226 ? 16.741  -5.453  40.955  1.00 80.95  ? 226  SER B CB  1 
ATOM   5540 O  OG  . SER B 1 226 ? 16.103  -4.190  40.973  1.00 90.80  ? 226  SER B OG  1 
ATOM   5541 N  N   . GLY B 1 227 ? 18.647  -3.710  38.518  1.00 97.14  ? 227  GLY B N   1 
ATOM   5542 C  CA  . GLY B 1 227 ? 19.331  -2.433  38.420  1.00 97.07  ? 227  GLY B CA  1 
ATOM   5543 C  C   . GLY B 1 227 ? 18.615  -1.342  39.188  1.00 98.81  ? 227  GLY B C   1 
ATOM   5544 O  O   . GLY B 1 227 ? 19.240  -0.373  39.630  1.00 100.14 ? 227  GLY B O   1 
ATOM   5545 N  N   . GLU B 1 228 ? 17.302  -1.483  39.352  1.00 96.83  ? 228  GLU B N   1 
ATOM   5546 C  CA  . GLU B 1 228 ? 16.542  -0.615  40.239  1.00 98.14  ? 228  GLU B CA  1 
ATOM   5547 C  C   . GLU B 1 228 ? 16.967  -0.855  41.684  1.00 99.77  ? 228  GLU B C   1 
ATOM   5548 O  O   . GLU B 1 228 ? 17.081  -2.003  42.126  1.00 98.25  ? 228  GLU B O   1 
ATOM   5549 C  CB  . GLU B 1 228 ? 15.046  -0.888  40.069  1.00 97.64  ? 228  GLU B CB  1 
ATOM   5550 C  CG  . GLU B 1 228 ? 14.243  -0.893  41.365  1.00 95.34  ? 228  GLU B CG  1 
ATOM   5551 C  CD  . GLU B 1 228 ? 12.783  -1.265  41.147  1.00 92.63  ? 228  GLU B CD  1 
ATOM   5552 O  OE1 . GLU B 1 228 ? 12.500  -2.051  40.217  1.00 89.51  ? 228  GLU B OE1 1 
ATOM   5553 O  OE2 . GLU B 1 228 ? 11.916  -0.771  41.901  1.00 89.35  ? 228  GLU B OE2 1 
ATOM   5554 N  N   . GLN B 1 229 ? 17.212  0.225   42.420  1.00 98.26  ? 229  GLN B N   1 
ATOM   5555 C  CA  . GLN B 1 229 ? 17.551  0.112   43.831  1.00 95.37  ? 229  GLN B CA  1 
ATOM   5556 C  C   . GLN B 1 229 ? 16.283  0.126   44.675  1.00 90.80  ? 229  GLN B C   1 
ATOM   5557 O  O   . GLN B 1 229 ? 15.328  0.850   44.375  1.00 91.05  ? 229  GLN B O   1 
ATOM   5558 C  CB  . GLN B 1 229 ? 18.485  1.241   44.273  1.00 95.52  ? 229  GLN B CB  1 
ATOM   5559 C  CG  . GLN B 1 229 ? 17.979  2.643   43.980  1.00 98.04  ? 229  GLN B CG  1 
ATOM   5560 C  CD  . GLN B 1 229 ? 18.938  3.713   44.470  1.00 102.21 ? 229  GLN B CD  1 
ATOM   5561 O  OE1 . GLN B 1 229 ? 20.086  3.783   44.029  1.00 102.68 ? 229  GLN B OE1 1 
ATOM   5562 N  NE2 . GLN B 1 229 ? 18.472  4.551   45.392  1.00 99.25  ? 229  GLN B NE2 1 
ATOM   5563 N  N   . SER B 1 230 ? 16.278  -0.685  45.729  1.00 82.30  ? 230  SER B N   1 
ATOM   5564 C  CA  . SER B 1 230 ? 15.172  -0.761  46.670  1.00 73.29  ? 230  SER B CA  1 
ATOM   5565 C  C   . SER B 1 230 ? 15.672  -0.442  48.075  1.00 70.92  ? 230  SER B C   1 
ATOM   5566 O  O   . SER B 1 230 ? 16.879  -0.364  48.332  1.00 64.60  ? 230  SER B O   1 
ATOM   5567 C  CB  . SER B 1 230 ? 14.512  -2.148  46.639  1.00 67.47  ? 230  SER B CB  1 
ATOM   5568 O  OG  . SER B 1 230 ? 13.950  -2.434  45.368  1.00 67.48  ? 230  SER B OG  1 
ATOM   5569 N  N   . ASP B 1 231 ? 14.718  -0.240  48.999  1.00 61.87  ? 231  ASP B N   1 
ATOM   5570 C  CA  . ASP B 1 231 ? 15.031  -0.010  50.406  1.00 63.83  ? 231  ASP B CA  1 
ATOM   5571 C  C   . ASP B 1 231 ? 13.931  -0.674  51.245  1.00 62.50  ? 231  ASP B C   1 
ATOM   5572 O  O   . ASP B 1 231 ? 13.138  -0.020  51.917  1.00 66.40  ? 231  ASP B O   1 
ATOM   5573 C  CB  . ASP B 1 231 ? 15.162  1.482   50.722  1.00 69.17  ? 231  ASP B CB  1 
ATOM   5574 C  CG  . ASP B 1 231 ? 15.740  1.735   52.108  1.00 78.05  ? 231  ASP B CG  1 
ATOM   5575 O  OD1 . ASP B 1 231 ? 16.349  0.804   52.679  1.00 72.76  ? 231  ASP B OD1 1 
ATOM   5576 O  OD2 . ASP B 1 231 ? 15.594  2.866   52.624  1.00 82.13  ? 231  ASP B OD2 1 
ATOM   5577 N  N   . ASP B 1 232 ? 13.894  -2.008  51.207  1.00 53.20  ? 232  ASP B N   1 
ATOM   5578 C  CA  . ASP B 1 232 ? 12.840  -2.772  51.864  1.00 46.85  ? 232  ASP B CA  1 
ATOM   5579 C  C   . ASP B 1 232 ? 13.396  -3.851  52.789  1.00 44.91  ? 232  ASP B C   1 
ATOM   5580 O  O   . ASP B 1 232 ? 14.588  -3.843  53.122  1.00 41.42  ? 232  ASP B O   1 
ATOM   5581 C  CB  . ASP B 1 232 ? 11.937  -3.395  50.801  1.00 43.13  ? 232  ASP B CB  1 
ATOM   5582 C  CG  . ASP B 1 232 ? 12.711  -4.218  49.797  1.00 41.35  ? 232  ASP B CG  1 
ATOM   5583 O  OD1 . ASP B 1 232 ? 13.911  -4.494  50.027  1.00 46.33  ? 232  ASP B OD1 1 
ATOM   5584 O  OD2 . ASP B 1 232 ? 12.125  -4.603  48.772  1.00 43.13  ? 232  ASP B OD2 1 
ATOM   5585 N  N   . LEU B 1 233 ? 12.539  -4.781  53.227  1.00 39.07  ? 233  LEU B N   1 
ATOM   5586 C  CA  . LEU B 1 233 ? 12.994  -5.844  54.119  1.00 37.41  ? 233  LEU B CA  1 
ATOM   5587 C  C   . LEU B 1 233 ? 14.185  -6.588  53.518  1.00 36.54  ? 233  LEU B C   1 
ATOM   5588 O  O   . LEU B 1 233 ? 15.198  -6.828  54.190  1.00 37.67  ? 233  LEU B O   1 
ATOM   5589 C  CB  . LEU B 1 233 ? 11.830  -6.796  54.425  1.00 36.31  ? 233  LEU B CB  1 
ATOM   5590 C  CG  . LEU B 1 233 ? 11.993  -7.930  55.430  1.00 43.58  ? 233  LEU B CG  1 
ATOM   5591 C  CD1 . LEU B 1 233 ? 12.283  -7.388  56.828  1.00 41.10  ? 233  LEU B CD1 1 
ATOM   5592 C  CD2 . LEU B 1 233 ? 10.721  -8.770  55.437  1.00 38.76  ? 233  LEU B CD2 1 
ATOM   5593 N  N   . LEU B 1 234 ? 14.098  -6.938  52.240  1.00 37.64  ? 234  LEU B N   1 
ATOM   5594 C  CA  . LEU B 1 234 ? 15.195  -7.667  51.616  1.00 32.95  ? 234  LEU B CA  1 
ATOM   5595 C  C   . LEU B 1 234 ? 16.468  -6.824  51.556  1.00 38.21  ? 234  LEU B C   1 
ATOM   5596 O  O   . LEU B 1 234 ? 17.576  -7.365  51.676  1.00 39.72  ? 234  LEU B O   1 
ATOM   5597 C  CB  . LEU B 1 234 ? 14.783  -8.117  50.216  1.00 38.35  ? 234  LEU B CB  1 
ATOM   5598 C  CG  . LEU B 1 234 ? 15.792  -9.001  49.485  1.00 34.51  ? 234  LEU B CG  1 
ATOM   5599 C  CD1 . LEU B 1 234 ? 16.168  -10.223 50.317  1.00 37.53  ? 234  LEU B CD1 1 
ATOM   5600 C  CD2 . LEU B 1 234 ? 15.236  -9.439  48.124  1.00 37.96  ? 234  LEU B CD2 1 
ATOM   5601 N  N   . THR B 1 235 ? 16.345  -5.504  51.376  1.00 35.92  ? 235  THR B N   1 
ATOM   5602 C  CA  . THR B 1 235 ? 17.546  -4.667  51.405  1.00 38.33  ? 235  THR B CA  1 
ATOM   5603 C  C   . THR B 1 235 ? 18.249  -4.778  52.749  1.00 36.66  ? 235  THR B C   1 
ATOM   5604 O  O   . THR B 1 235 ? 19.477  -4.902  52.808  1.00 41.56  ? 235  THR B O   1 
ATOM   5605 C  CB  . THR B 1 235 ? 17.223  -3.202  51.094  1.00 43.93  ? 235  THR B CB  1 
ATOM   5606 O  OG1 . THR B 1 235 ? 16.358  -3.118  49.958  1.00 40.74  ? 235  THR B OG1 1 
ATOM   5607 C  CG2 . THR B 1 235 ? 18.511  -2.422  50.812  1.00 47.23  ? 235  THR B CG2 1 
ATOM   5608 N  N   . HIS B 1 236 ? 17.485  -4.740  53.840  1.00 37.56  ? 236  HIS B N   1 
ATOM   5609 C  CA  . HIS B 1 236 ? 18.103  -4.851  55.159  1.00 39.21  ? 236  HIS B CA  1 
ATOM   5610 C  C   . HIS B 1 236 ? 18.698  -6.238  55.361  1.00 40.14  ? 236  HIS B C   1 
ATOM   5611 O  O   . HIS B 1 236 ? 19.790  -6.377  55.928  1.00 42.67  ? 236  HIS B O   1 
ATOM   5612 C  CB  . HIS B 1 236 ? 17.075  -4.534  56.249  1.00 40.56  ? 236  HIS B CB  1 
ATOM   5613 C  CG  . HIS B 1 236 ? 16.743  -3.078  56.359  1.00 46.57  ? 236  HIS B CG  1 
ATOM   5614 N  ND1 . HIS B 1 236 ? 15.753  -2.484  55.605  1.00 50.32  ? 236  HIS B ND1 1 
ATOM   5615 C  CD2 . HIS B 1 236 ? 17.263  -2.097  57.137  1.00 56.24  ? 236  HIS B CD2 1 
ATOM   5616 C  CE1 . HIS B 1 236 ? 15.681  -1.200  55.908  1.00 55.22  ? 236  HIS B CE1 1 
ATOM   5617 N  NE2 . HIS B 1 236 ? 16.584  -0.940  56.837  1.00 57.84  ? 236  HIS B NE2 1 
ATOM   5618 N  N   . MET B 1 237 ? 17.997  -7.280  54.918  1.00 38.50  ? 237  MET B N   1 
ATOM   5619 C  CA  . MET B 1 237 ? 18.562  -8.624  55.008  1.00 36.91  ? 237  MET B CA  1 
ATOM   5620 C  C   . MET B 1 237 ? 19.929  -8.699  54.344  1.00 42.73  ? 237  MET B C   1 
ATOM   5621 O  O   . MET B 1 237 ? 20.867  -9.284  54.901  1.00 44.38  ? 237  MET B O   1 
ATOM   5622 C  CB  . MET B 1 237 ? 17.603  -9.649  54.392  1.00 41.30  ? 237  MET B CB  1 
ATOM   5623 C  CG  . MET B 1 237 ? 16.455  -10.129 55.305  1.00 39.19  ? 237  MET B CG  1 
ATOM   5624 S  SD  . MET B 1 237 ? 15.398  -11.268 54.360  1.00 38.96  ? 237  MET B SD  1 
ATOM   5625 C  CE  . MET B 1 237 ? 13.847  -11.129 55.278  1.00 37.68  ? 237  MET B CE  1 
ATOM   5626 N  N   . LEU B 1 238 ? 20.072  -8.084  53.165  1.00 42.58  ? 238  LEU B N   1 
ATOM   5627 C  CA  . LEU B 1 238 ? 21.289  -8.228  52.373  1.00 41.84  ? 238  LEU B CA  1 
ATOM   5628 C  C   . LEU B 1 238 ? 22.403  -7.291  52.816  1.00 41.74  ? 238  LEU B C   1 
ATOM   5629 O  O   . LEU B 1 238 ? 23.581  -7.632  52.672  1.00 51.77  ? 238  LEU B O   1 
ATOM   5630 C  CB  . LEU B 1 238 ? 20.990  -7.982  50.893  1.00 43.71  ? 238  LEU B CB  1 
ATOM   5631 C  CG  . LEU B 1 238 ? 20.053  -9.007  50.257  1.00 45.44  ? 238  LEU B CG  1 
ATOM   5632 C  CD1 . LEU B 1 238 ? 19.640  -8.550  48.858  1.00 42.14  ? 238  LEU B CD1 1 
ATOM   5633 C  CD2 . LEU B 1 238 ? 20.686  -10.397 50.227  1.00 48.66  ? 238  LEU B CD2 1 
ATOM   5634 N  N   . ASN B 1 239 ? 22.070  -6.111  53.332  1.00 43.91  ? 239  ASN B N   1 
ATOM   5635 C  CA  . ASN B 1 239 ? 23.065  -5.074  53.555  1.00 43.81  ? 239  ASN B CA  1 
ATOM   5636 C  C   . ASN B 1 239 ? 23.207  -4.621  54.997  1.00 45.70  ? 239  ASN B C   1 
ATOM   5637 O  O   . ASN B 1 239 ? 24.256  -4.073  55.341  1.00 45.75  ? 239  ASN B O   1 
ATOM   5638 C  CB  . ASN B 1 239 ? 22.745  -3.841  52.694  1.00 46.46  ? 239  ASN B CB  1 
ATOM   5639 C  CG  . ASN B 1 239 ? 22.673  -4.174  51.219  1.00 51.48  ? 239  ASN B CG  1 
ATOM   5640 O  OD1 . ASN B 1 239 ? 23.696  -4.268  50.549  1.00 54.75  ? 239  ASN B OD1 1 
ATOM   5641 N  ND2 . ASN B 1 239 ? 21.463  -4.378  50.711  1.00 51.20  ? 239  ASN B ND2 1 
ATOM   5642 N  N   . GLY B 1 240 ? 22.197  -4.817  55.839  1.00 40.33  ? 240  GLY B N   1 
ATOM   5643 C  CA  . GLY B 1 240 ? 22.234  -4.243  57.169  1.00 38.14  ? 240  GLY B CA  1 
ATOM   5644 C  C   . GLY B 1 240 ? 23.229  -4.956  58.067  1.00 39.02  ? 240  GLY B C   1 
ATOM   5645 O  O   . GLY B 1 240 ? 23.469  -6.156  57.939  1.00 38.84  ? 240  GLY B O   1 
ATOM   5646 N  N   . LYS B 1 241 ? 23.812  -4.195  58.995  1.00 37.59  ? 241  LYS B N   1 
ATOM   5647 C  CA  . LYS B 1 241 ? 24.773  -4.732  59.951  1.00 37.58  ? 241  LYS B CA  1 
ATOM   5648 C  C   . LYS B 1 241 ? 24.213  -4.642  61.359  1.00 30.68  ? 241  LYS B C   1 
ATOM   5649 O  O   . LYS B 1 241 ? 23.666  -3.606  61.756  1.00 36.16  ? 241  LYS B O   1 
ATOM   5650 C  CB  . LYS B 1 241 ? 26.110  -3.981  59.883  1.00 39.18  ? 241  LYS B CB  1 
ATOM   5651 C  CG  . LYS B 1 241 ? 26.704  -3.871  58.502  1.00 43.01  ? 241  LYS B CG  1 
ATOM   5652 C  CD  . LYS B 1 241 ? 27.337  -5.157  58.040  1.00 48.10  ? 241  LYS B CD  1 
ATOM   5653 C  CE  . LYS B 1 241 ? 28.301  -4.891  56.874  1.00 48.12  ? 241  LYS B CE  1 
ATOM   5654 N  NZ  . LYS B 1 241 ? 29.116  -3.662  57.097  1.00 60.22  ? 241  LYS B NZ  1 
ATOM   5655 N  N   . ASP B 1 242 ? 24.385  -5.723  62.116  1.00 30.03  ? 242  ASP B N   1 
ATOM   5656 C  CA  . ASP B 1 242 ? 24.021  -5.765  63.516  1.00 33.10  ? 242  ASP B CA  1 
ATOM   5657 C  C   . ASP B 1 242 ? 24.988  -4.901  64.306  1.00 33.70  ? 242  ASP B C   1 
ATOM   5658 O  O   . ASP B 1 242 ? 26.194  -5.173  64.287  1.00 34.03  ? 242  ASP B O   1 
ATOM   5659 C  CB  . ASP B 1 242 ? 24.077  -7.205  64.019  1.00 30.44  ? 242  ASP B CB  1 
ATOM   5660 C  CG  . ASP B 1 242 ? 24.058  -7.297  65.521  1.00 30.38  ? 242  ASP B CG  1 
ATOM   5661 O  OD1 . ASP B 1 242 ? 23.431  -6.436  66.172  1.00 32.38  ? 242  ASP B OD1 1 
ATOM   5662 O  OD2 . ASP B 1 242 ? 24.653  -8.260  66.055  1.00 32.89  ? 242  ASP B OD2 1 
ATOM   5663 N  N   . PRO B 1 243 ? 24.525  -3.866  65.007  1.00 32.91  ? 243  PRO B N   1 
ATOM   5664 C  CA  . PRO B 1 243 ? 25.464  -3.010  65.746  1.00 34.62  ? 243  PRO B CA  1 
ATOM   5665 C  C   . PRO B 1 243 ? 26.226  -3.755  66.812  1.00 36.57  ? 243  PRO B C   1 
ATOM   5666 O  O   . PRO B 1 243 ? 27.332  -3.322  67.184  1.00 36.09  ? 243  PRO B O   1 
ATOM   5667 C  CB  . PRO B 1 243 ? 24.556  -1.933  66.363  1.00 38.14  ? 243  PRO B CB  1 
ATOM   5668 C  CG  . PRO B 1 243 ? 23.299  -1.981  65.540  1.00 41.83  ? 243  PRO B CG  1 
ATOM   5669 C  CD  . PRO B 1 243 ? 23.133  -3.405  65.143  1.00 35.89  ? 243  PRO B CD  1 
ATOM   5670 N  N   . GLU B 1 244 ? 25.683  -4.862  67.326  1.00 33.95  ? 244  GLU B N   1 
ATOM   5671 C  CA  . GLU B 1 244 ? 26.363  -5.534  68.423  1.00 33.43  ? 244  GLU B CA  1 
ATOM   5672 C  C   . GLU B 1 244 ? 27.537  -6.361  67.898  1.00 34.34  ? 244  GLU B C   1 
ATOM   5673 O  O   . GLU B 1 244 ? 28.692  -6.062  68.212  1.00 35.63  ? 244  GLU B O   1 
ATOM   5674 C  CB  . GLU B 1 244 ? 25.385  -6.375  69.256  1.00 34.78  ? 244  GLU B CB  1 
ATOM   5675 C  CG  . GLU B 1 244 ? 26.114  -7.277  70.244  1.00 38.53  ? 244  GLU B CG  1 
ATOM   5676 C  CD  . GLU B 1 244 ? 25.221  -8.244  71.007  1.00 46.58  ? 244  GLU B CD  1 
ATOM   5677 O  OE1 . GLU B 1 244 ? 24.040  -8.450  70.643  1.00 39.27  ? 244  GLU B OE1 1 
ATOM   5678 O  OE2 . GLU B 1 244 ? 25.721  -8.806  72.002  1.00 54.76  ? 244  GLU B OE2 1 
ATOM   5679 N  N   . THR B 1 245 ? 27.271  -7.369  67.054  1.00 32.00  ? 245  THR B N   1 
ATOM   5680 C  CA  . THR B 1 245 ? 28.363  -8.143  66.450  1.00 34.07  ? 245  THR B CA  1 
ATOM   5681 C  C   . THR B 1 245 ? 29.102  -7.378  65.359  1.00 37.28  ? 245  THR B C   1 
ATOM   5682 O  O   . THR B 1 245 ? 30.235  -7.747  65.028  1.00 35.31  ? 245  THR B O   1 
ATOM   5683 C  CB  . THR B 1 245 ? 27.844  -9.451  65.844  1.00 32.60  ? 245  THR B CB  1 
ATOM   5684 O  OG1 . THR B 1 245 ? 26.982  -9.169  64.723  1.00 33.87  ? 245  THR B OG1 1 
ATOM   5685 C  CG2 . THR B 1 245 ? 27.101  -10.284 66.881  1.00 33.67  ? 245  THR B CG2 1 
ATOM   5686 N  N   . GLY B 1 246 ? 28.488  -6.341  64.790  1.00 31.57  ? 246  GLY B N   1 
ATOM   5687 C  CA  . GLY B 1 246 ? 28.975  -5.646  63.613  1.00 32.65  ? 246  GLY B CA  1 
ATOM   5688 C  C   . GLY B 1 246 ? 28.821  -6.395  62.308  1.00 30.18  ? 246  GLY B C   1 
ATOM   5689 O  O   . GLY B 1 246 ? 29.288  -5.906  61.273  1.00 33.74  ? 246  GLY B O   1 
ATOM   5690 N  N   . GLU B 1 247 ? 28.158  -7.618  62.310  1.00 33.83  ? 247  GLU B N   1 
ATOM   5691 C  CA  . GLU B 1 247 ? 28.089  -8.504  61.152  1.00 32.85  ? 247  GLU B CA  1 
ATOM   5692 C  C   . GLU B 1 247 ? 26.756  -8.376  60.429  1.00 32.68  ? 247  GLU B C   1 
ATOM   5693 O  O   . GLU B 1 247 ? 25.732  -8.109  61.060  1.00 31.44  ? 247  GLU B O   1 
ATOM   5694 C  CB  . GLU B 1 247 ? 28.234  -9.965  61.573  1.00 32.15  ? 247  GLU B CB  1 
ATOM   5695 C  CG  . GLU B 1 247 ? 29.492  -10.293 62.362  1.00 34.80  ? 247  GLU B CG  1 
ATOM   5696 C  CD  . GLU B 1 247 ? 29.350  -11.602 63.106  1.00 36.31  ? 247  GLU B CD  1 
ATOM   5697 O  OE1 . GLU B 1 247 ? 28.372  -12.331 62.846  1.00 34.46  ? 247  GLU B OE1 1 
ATOM   5698 O  OE2 . GLU B 1 247 ? 30.194  -11.896 63.977  1.00 34.09  ? 247  GLU B OE2 1 
ATOM   5699 N  N   . PRO B 1 248 ? 26.755  -8.606  59.121  1.00 31.87  ? 248  PRO B N   1 
ATOM   5700 C  CA  . PRO B 1 248 ? 25.507  -8.793  58.377  1.00 35.27  ? 248  PRO B CA  1 
ATOM   5701 C  C   . PRO B 1 248 ? 25.064  -10.247 58.481  1.00 36.27  ? 248  PRO B C   1 
ATOM   5702 O  O   . PRO B 1 248 ? 25.817  -11.117 58.910  1.00 35.48  ? 248  PRO B O   1 
ATOM   5703 C  CB  . PRO B 1 248 ? 25.919  -8.460  56.940  1.00 37.04  ? 248  PRO B CB  1 
ATOM   5704 C  CG  . PRO B 1 248 ? 27.338  -9.002  56.873  1.00 38.24  ? 248  PRO B CG  1 
ATOM   5705 C  CD  . PRO B 1 248 ? 27.940  -8.692  58.243  1.00 36.12  ? 248  PRO B CD  1 
ATOM   5706 N  N   . LEU B 1 249 ? 23.817  -10.500 58.086  1.00 34.30  ? 249  LEU B N   1 
ATOM   5707 C  CA  . LEU B 1 249 ? 23.381  -11.887 58.032  1.00 34.63  ? 249  LEU B CA  1 
ATOM   5708 C  C   . LEU B 1 249 ? 24.150  -12.644 56.958  1.00 32.25  ? 249  LEU B C   1 
ATOM   5709 O  O   . LEU B 1 249 ? 24.512  -12.088 55.926  1.00 35.27  ? 249  LEU B O   1 
ATOM   5710 C  CB  . LEU B 1 249 ? 21.885  -11.972 57.738  1.00 39.68  ? 249  LEU B CB  1 
ATOM   5711 C  CG  . LEU B 1 249 ? 20.958  -11.343 58.770  1.00 35.48  ? 249  LEU B CG  1 
ATOM   5712 C  CD1 . LEU B 1 249 ? 19.500  -11.446 58.249  1.00 37.46  ? 249  LEU B CD1 1 
ATOM   5713 C  CD2 . LEU B 1 249 ? 21.122  -11.985 60.156  1.00 31.19  ? 249  LEU B CD2 1 
ATOM   5714 N  N   . ASP B 1 250 ? 24.397  -13.925 57.198  1.00 34.46  ? 250  ASP B N   1 
ATOM   5715 C  CA  . ASP B 1 250 ? 24.974  -14.745 56.139  1.00 39.88  ? 250  ASP B CA  1 
ATOM   5716 C  C   . ASP B 1 250 ? 23.890  -15.308 55.212  1.00 40.41  ? 250  ASP B C   1 
ATOM   5717 O  O   . ASP B 1 250 ? 22.684  -15.198 55.466  1.00 35.36  ? 250  ASP B O   1 
ATOM   5718 C  CB  . ASP B 1 250 ? 25.854  -15.854 56.723  1.00 42.14  ? 250  ASP B CB  1 
ATOM   5719 C  CG  . ASP B 1 250 ? 25.097  -16.786 57.627  1.00 47.35  ? 250  ASP B CG  1 
ATOM   5720 O  OD1 . ASP B 1 250 ? 24.188  -17.497 57.155  1.00 39.75  ? 250  ASP B OD1 1 
ATOM   5721 O  OD2 . ASP B 1 250 ? 25.427  -16.797 58.836  1.00 51.61  ? 250  ASP B OD2 1 
ATOM   5722 N  N   . ASP B 1 251 ? 24.346  -15.890 54.094  1.00 39.56  ? 251  ASP B N   1 
ATOM   5723 C  CA  . ASP B 1 251 ? 23.425  -16.295 53.035  1.00 41.81  ? 251  ASP B CA  1 
ATOM   5724 C  C   . ASP B 1 251 ? 22.457  -17.367 53.518  1.00 37.87  ? 251  ASP B C   1 
ATOM   5725 O  O   . ASP B 1 251 ? 21.267  -17.330 53.187  1.00 39.50  ? 251  ASP B O   1 
ATOM   5726 C  CB  . ASP B 1 251 ? 24.210  -16.793 51.817  1.00 44.03  ? 251  ASP B CB  1 
ATOM   5727 C  CG  . ASP B 1 251 ? 24.737  -15.656 50.953  1.00 52.79  ? 251  ASP B CG  1 
ATOM   5728 O  OD1 . ASP B 1 251 ? 24.308  -14.498 51.151  1.00 54.05  ? 251  ASP B OD1 1 
ATOM   5729 O  OD2 . ASP B 1 251 ? 25.589  -15.920 50.078  1.00 57.88  ? 251  ASP B OD2 1 
ATOM   5730 N  N   . GLU B 1 252 ? 22.953  -18.345 54.277  1.00 37.65  ? 252  GLU B N   1 
ATOM   5731 C  CA  . GLU B 1 252 ? 22.075  -19.394 54.782  1.00 37.28  ? 252  GLU B CA  1 
ATOM   5732 C  C   . GLU B 1 252 ? 20.956  -18.802 55.629  1.00 36.61  ? 252  GLU B C   1 
ATOM   5733 O  O   . GLU B 1 252 ? 19.781  -19.158 55.470  1.00 34.93  ? 252  GLU B O   1 
ATOM   5734 C  CB  . GLU B 1 252 ? 22.876  -20.403 55.600  1.00 41.37  ? 252  GLU B CB  1 
ATOM   5735 C  CG  . GLU B 1 252 ? 22.069  -21.603 56.044  1.00 43.93  ? 252  GLU B CG  1 
ATOM   5736 C  CD  . GLU B 1 252 ? 22.840  -22.481 57.000  1.00 53.34  ? 252  GLU B CD  1 
ATOM   5737 O  OE1 . GLU B 1 252 ? 23.986  -22.849 56.662  1.00 61.06  ? 252  GLU B OE1 1 
ATOM   5738 O  OE2 . GLU B 1 252 ? 22.321  -22.766 58.106  1.00 49.61  ? 252  GLU B OE2 1 
ATOM   5739 N  N   . ASN B 1 253 ? 21.308  -17.911 56.555  1.00 33.06  ? 253  ASN B N   1 
ATOM   5740 C  CA  . ASN B 1 253 ? 20.277  -17.339 57.414  1.00 30.53  ? 253  ASN B CA  1 
ATOM   5741 C  C   . ASN B 1 253 ? 19.326  -16.448 56.626  1.00 34.49  ? 253  ASN B C   1 
ATOM   5742 O  O   . ASN B 1 253 ? 18.130  -16.392 56.940  1.00 31.98  ? 253  ASN B O   1 
ATOM   5743 C  CB  . ASN B 1 253 ? 20.903  -16.562 58.571  1.00 33.13  ? 253  ASN B CB  1 
ATOM   5744 C  CG  . ASN B 1 253 ? 19.868  -16.121 59.594  1.00 30.02  ? 253  ASN B CG  1 
ATOM   5745 O  OD1 . ASN B 1 253 ? 19.530  -14.941 59.673  1.00 33.44  ? 253  ASN B OD1 1 
ATOM   5746 N  ND2 . ASN B 1 253 ? 19.336  -17.075 60.353  1.00 30.59  ? 253  ASN B ND2 1 
ATOM   5747 N  N   . ILE B 1 254 ? 19.831  -15.744 55.611  1.00 32.81  ? 254  ILE B N   1 
ATOM   5748 C  CA  . ILE B 1 254 ? 18.955  -14.923 54.777  1.00 32.04  ? 254  ILE B CA  1 
ATOM   5749 C  C   . ILE B 1 254 ? 17.857  -15.781 54.156  1.00 32.72  ? 254  ILE B C   1 
ATOM   5750 O  O   . ILE B 1 254 ? 16.677  -15.398 54.157  1.00 32.62  ? 254  ILE B O   1 
ATOM   5751 C  CB  . ILE B 1 254 ? 19.769  -14.182 53.701  1.00 34.60  ? 254  ILE B CB  1 
ATOM   5752 C  CG1 . ILE B 1 254 ? 20.638  -13.091 54.337  1.00 33.66  ? 254  ILE B CG1 1 
ATOM   5753 C  CG2 . ILE B 1 254 ? 18.828  -13.588 52.655  1.00 35.94  ? 254  ILE B CG2 1 
ATOM   5754 C  CD1 . ILE B 1 254 ? 21.638  -12.495 53.355  1.00 40.97  ? 254  ILE B CD1 1 
ATOM   5755 N  N   . ARG B 1 255 ? 18.218  -16.957 53.633  1.00 32.59  ? 255  ARG B N   1 
ATOM   5756 C  CA  . ARG B 1 255 ? 17.204  -17.824 53.027  1.00 33.48  ? 255  ARG B CA  1 
ATOM   5757 C  C   . ARG B 1 255 ? 16.140  -18.214 54.041  1.00 31.31  ? 255  ARG B C   1 
ATOM   5758 O  O   . ARG B 1 255 ? 14.944  -18.245 53.723  1.00 34.49  ? 255  ARG B O   1 
ATOM   5759 C  CB  . ARG B 1 255 ? 17.837  -19.081 52.428  1.00 37.05  ? 255  ARG B CB  1 
ATOM   5760 C  CG  . ARG B 1 255 ? 18.952  -18.854 51.408  1.00 43.88  ? 255  ARG B CG  1 
ATOM   5761 C  CD  . ARG B 1 255 ? 19.418  -20.187 50.789  1.00 49.08  ? 255  ARG B CD  1 
ATOM   5762 N  NE  . ARG B 1 255 ? 18.305  -20.919 50.193  1.00 54.64  ? 255  ARG B NE  1 
ATOM   5763 C  CZ  . ARG B 1 255 ? 17.912  -20.805 48.930  1.00 56.88  ? 255  ARG B CZ  1 
ATOM   5764 N  NH1 . ARG B 1 255 ? 18.575  -20.052 48.063  1.00 54.70  ? 255  ARG B NH1 1 
ATOM   5765 N  NH2 . ARG B 1 255 ? 16.821  -21.454 48.529  1.00 47.96  ? 255  ARG B NH2 1 
ATOM   5766 N  N   . TYR B 1 256 ? 16.557  -18.518 55.271  1.00 30.63  ? 256  TYR B N   1 
ATOM   5767 C  CA  . TYR B 1 256 ? 15.587  -18.858 56.309  1.00 31.34  ? 256  TYR B CA  1 
ATOM   5768 C  C   . TYR B 1 256 ? 14.714  -17.663 56.672  1.00 31.49  ? 256  TYR B C   1 
ATOM   5769 O  O   . TYR B 1 256 ? 13.526  -17.833 56.974  1.00 30.36  ? 256  TYR B O   1 
ATOM   5770 C  CB  . TYR B 1 256 ? 16.298  -19.371 57.560  1.00 30.91  ? 256  TYR B CB  1 
ATOM   5771 C  CG  . TYR B 1 256 ? 16.877  -20.762 57.440  1.00 32.30  ? 256  TYR B CG  1 
ATOM   5772 C  CD1 . TYR B 1 256 ? 16.165  -21.799 56.842  1.00 32.45  ? 256  TYR B CD1 1 
ATOM   5773 C  CD2 . TYR B 1 256 ? 18.153  -21.042 57.941  1.00 34.50  ? 256  TYR B CD2 1 
ATOM   5774 C  CE1 . TYR B 1 256 ? 16.710  -23.085 56.751  1.00 36.44  ? 256  TYR B CE1 1 
ATOM   5775 C  CE2 . TYR B 1 256 ? 18.696  -22.315 57.850  1.00 37.56  ? 256  TYR B CE2 1 
ATOM   5776 C  CZ  . TYR B 1 256 ? 17.983  -23.326 57.260  1.00 40.93  ? 256  TYR B CZ  1 
ATOM   5777 O  OH  . TYR B 1 256 ? 18.552  -24.584 57.181  1.00 42.70  ? 256  TYR B OH  1 
ATOM   5778 N  N   . GLN B 1 257 ? 15.285  -16.454 56.702  1.00 32.51  ? 257  GLN B N   1 
ATOM   5779 C  CA  . GLN B 1 257 ? 14.457  -15.292 57.010  1.00 30.81  ? 257  GLN B CA  1 
ATOM   5780 C  C   . GLN B 1 257 ? 13.416  -15.064 55.929  1.00 31.54  ? 257  GLN B C   1 
ATOM   5781 O  O   . GLN B 1 257 ? 12.275  -14.705 56.235  1.00 31.14  ? 257  GLN B O   1 
ATOM   5782 C  CB  . GLN B 1 257 ? 15.289  -14.022 57.194  1.00 33.33  ? 257  GLN B CB  1 
ATOM   5783 C  CG  . GLN B 1 257 ? 16.380  -14.084 58.293  1.00 27.79  ? 257  GLN B CG  1 
ATOM   5784 C  CD  . GLN B 1 257 ? 15.846  -14.345 59.703  1.00 31.35  ? 257  GLN B CD  1 
ATOM   5785 O  OE1 . GLN B 1 257 ? 14.626  -14.327 59.959  1.00 27.74  ? 257  GLN B OE1 1 
ATOM   5786 N  NE2 . GLN B 1 257 ? 16.772  -14.577 60.638  1.00 30.57  ? 257  GLN B NE2 1 
ATOM   5787 N  N   . ILE B 1 258 ? 13.780  -15.268 54.662  1.00 31.81  ? 258  ILE B N   1 
ATOM   5788 C  CA  . ILE B 1 258 ? 12.806  -15.046 53.593  1.00 31.29  ? 258  ILE B CA  1 
ATOM   5789 C  C   . ILE B 1 258 ? 11.659  -16.041 53.702  1.00 29.70  ? 258  ILE B C   1 
ATOM   5790 O  O   . ILE B 1 258 ? 10.480  -15.671 53.612  1.00 30.71  ? 258  ILE B O   1 
ATOM   5791 C  CB  . ILE B 1 258 ? 13.481  -15.101 52.213  1.00 35.11  ? 258  ILE B CB  1 
ATOM   5792 C  CG1 . ILE B 1 258 ? 14.507  -13.964 52.106  1.00 35.29  ? 258  ILE B CG1 1 
ATOM   5793 C  CG2 . ILE B 1 258 ? 12.428  -14.978 51.109  1.00 32.98  ? 258  ILE B CG2 1 
ATOM   5794 C  CD1 . ILE B 1 258 ? 15.379  -14.015 50.837  1.00 36.86  ? 258  ILE B CD1 1 
ATOM   5795 N  N   . ILE B 1 259 ? 11.978  -17.317 53.919  1.00 32.66  ? 259  ILE B N   1 
ATOM   5796 C  CA  . ILE B 1 259 ? 10.915  -18.301 54.140  1.00 31.86  ? 259  ILE B CA  1 
ATOM   5797 C  C   . ILE B 1 259 ? 10.057  -17.886 55.331  1.00 30.82  ? 259  ILE B C   1 
ATOM   5798 O  O   . ILE B 1 259 ? 8.814   -17.915 55.275  1.00 29.43  ? 259  ILE B O   1 
ATOM   5799 C  CB  . ILE B 1 259 ? 11.528  -19.698 54.335  1.00 32.29  ? 259  ILE B CB  1 
ATOM   5800 C  CG1 . ILE B 1 259 ? 12.170  -20.161 53.020  1.00 32.44  ? 259  ILE B CG1 1 
ATOM   5801 C  CG2 . ILE B 1 259 ? 10.493  -20.708 54.835  1.00 33.49  ? 259  ILE B CG2 1 
ATOM   5802 C  CD1 . ILE B 1 259 ? 13.072  -21.344 53.193  1.00 38.66  ? 259  ILE B CD1 1 
ATOM   5803 N  N   . THR B 1 260 ? 10.711  -17.493 56.429  1.00 28.25  ? 260  THR B N   1 
ATOM   5804 C  CA  . THR B 1 260 ? 9.988   -17.114 57.641  1.00 28.15  ? 260  THR B CA  1 
ATOM   5805 C  C   . THR B 1 260 ? 9.035   -15.955 57.366  1.00 29.67  ? 260  THR B C   1 
ATOM   5806 O  O   . THR B 1 260 ? 7.855   -15.993 57.738  1.00 29.91  ? 260  THR B O   1 
ATOM   5807 C  CB  . THR B 1 260 ? 10.993  -16.737 58.733  1.00 28.57  ? 260  THR B CB  1 
ATOM   5808 O  OG1 . THR B 1 260 ? 11.822  -17.874 59.030  1.00 29.79  ? 260  THR B OG1 1 
ATOM   5809 C  CG2 . THR B 1 260 ? 10.277  -16.272 59.996  1.00 28.78  ? 260  THR B CG2 1 
ATOM   5810 N  N   . PHE B 1 261 ? 9.522   -14.915 56.690  1.00 31.00  ? 261  PHE B N   1 
ATOM   5811 C  CA  . PHE B 1 261 ? 8.663   -13.757 56.462  1.00 29.93  ? 261  PHE B CA  1 
ATOM   5812 C  C   . PHE B 1 261 ? 7.598   -14.018 55.396  1.00 32.15  ? 261  PHE B C   1 
ATOM   5813 O  O   . PHE B 1 261 ? 6.494   -13.464 55.485  1.00 32.30  ? 261  PHE B O   1 
ATOM   5814 C  CB  . PHE B 1 261 ? 9.524   -12.532 56.141  1.00 30.77  ? 261  PHE B CB  1 
ATOM   5815 C  CG  . PHE B 1 261 ? 10.099  -11.895 57.374  1.00 32.19  ? 261  PHE B CG  1 
ATOM   5816 C  CD1 . PHE B 1 261 ? 9.382   -10.962 58.084  1.00 34.48  ? 261  PHE B CD1 1 
ATOM   5817 C  CD2 . PHE B 1 261 ? 11.336  -12.294 57.859  1.00 37.74  ? 261  PHE B CD2 1 
ATOM   5818 C  CE1 . PHE B 1 261 ? 9.889   -10.406 59.243  1.00 34.53  ? 261  PHE B CE1 1 
ATOM   5819 C  CE2 . PHE B 1 261 ? 11.853  -11.742 59.005  1.00 33.71  ? 261  PHE B CE2 1 
ATOM   5820 C  CZ  . PHE B 1 261 ? 11.135  -10.793 59.704  1.00 34.32  ? 261  PHE B CZ  1 
ATOM   5821 N  N   . LEU B 1 262 ? 7.870   -14.874 54.410  1.00 28.89  ? 262  LEU B N   1 
ATOM   5822 C  CA  . LEU B 1 262 ? 6.804   -15.184 53.455  1.00 31.97  ? 262  LEU B CA  1 
ATOM   5823 C  C   . LEU B 1 262 ? 5.667   -15.910 54.142  1.00 33.59  ? 262  LEU B C   1 
ATOM   5824 O  O   . LEU B 1 262 ? 4.493   -15.697 53.797  1.00 36.15  ? 262  LEU B O   1 
ATOM   5825 C  CB  . LEU B 1 262 ? 7.326   -16.038 52.296  1.00 31.87  ? 262  LEU B CB  1 
ATOM   5826 C  CG  . LEU B 1 262 ? 8.245   -15.257 51.358  1.00 32.80  ? 262  LEU B CG  1 
ATOM   5827 C  CD1 . LEU B 1 262 ? 8.831   -16.167 50.297  1.00 33.51  ? 262  LEU B CD1 1 
ATOM   5828 C  CD2 . LEU B 1 262 ? 7.493   -14.078 50.746  1.00 30.23  ? 262  LEU B CD2 1 
ATOM   5829 N  N   . ILE B 1 263 ? 5.989   -16.748 55.128  1.00 30.78  ? 263  ILE B N   1 
ATOM   5830 C  CA  . ILE B 1 263 ? 4.964   -17.528 55.817  1.00 30.35  ? 263  ILE B CA  1 
ATOM   5831 C  C   . ILE B 1 263 ? 4.321   -16.718 56.932  1.00 30.38  ? 263  ILE B C   1 
ATOM   5832 O  O   . ILE B 1 263 ? 3.116   -16.432 56.904  1.00 35.40  ? 263  ILE B O   1 
ATOM   5833 C  CB  . ILE B 1 263 ? 5.562   -18.837 56.350  1.00 31.74  ? 263  ILE B CB  1 
ATOM   5834 C  CG1 . ILE B 1 263 ? 5.971   -19.729 55.170  1.00 33.39  ? 263  ILE B CG1 1 
ATOM   5835 C  CG2 . ILE B 1 263 ? 4.574   -19.540 57.279  1.00 32.88  ? 263  ILE B CG2 1 
ATOM   5836 C  CD1 . ILE B 1 263 ? 6.704   -20.973 55.621  1.00 32.44  ? 263  ILE B CD1 1 
ATOM   5837 N  N   . ALA B 1 264 ? 5.114   -16.345 57.935  1.00 29.24  ? 264  ALA B N   1 
ATOM   5838 C  CA  . ALA B 1 264 ? 4.578   -15.575 59.050  1.00 31.98  ? 264  ALA B CA  1 
ATOM   5839 C  C   . ALA B 1 264 ? 4.089   -14.210 58.601  1.00 29.82  ? 264  ALA B C   1 
ATOM   5840 O  O   . ALA B 1 264 ? 3.164   -13.655 59.206  1.00 33.24  ? 264  ALA B O   1 
ATOM   5841 C  CB  . ALA B 1 264 ? 5.638   -15.423 60.147  1.00 31.28  ? 264  ALA B CB  1 
ATOM   5842 N  N   . GLY B 1 265 ? 4.664   -13.671 57.518  1.00 31.72  ? 265  GLY B N   1 
ATOM   5843 C  CA  . GLY B 1 265 ? 4.281   -12.384 56.978  1.00 32.82  ? 265  GLY B CA  1 
ATOM   5844 C  C   . GLY B 1 265 ? 2.966   -12.338 56.232  1.00 33.77  ? 265  GLY B C   1 
ATOM   5845 O  O   . GLY B 1 265 ? 2.552   -11.243 55.843  1.00 33.39  ? 265  GLY B O   1 
ATOM   5846 N  N   . HIS B 1 266 ? 2.291   -13.467 56.024  1.00 33.57  ? 266  HIS B N   1 
ATOM   5847 C  CA  . HIS B 1 266 ? 0.978   -13.395 55.380  1.00 29.02  ? 266  HIS B CA  1 
ATOM   5848 C  C   . HIS B 1 266 ? -0.087  -14.284 56.002  1.00 32.91  ? 266  HIS B C   1 
ATOM   5849 O  O   . HIS B 1 266 ? -1.267  -13.924 55.987  1.00 31.91  ? 266  HIS B O   1 
ATOM   5850 C  CB  . HIS B 1 266 ? 1.086   -13.730 53.886  1.00 32.66  ? 266  HIS B CB  1 
ATOM   5851 C  CG  . HIS B 1 266 ? 0.807   -15.168 53.563  1.00 35.16  ? 266  HIS B CG  1 
ATOM   5852 N  ND1 . HIS B 1 266 ? 1.775   -16.147 53.610  1.00 35.36  ? 266  HIS B ND1 1 
ATOM   5853 C  CD2 . HIS B 1 266 ? -0.337  -15.791 53.183  1.00 32.34  ? 266  HIS B CD2 1 
ATOM   5854 C  CE1 . HIS B 1 266 ? 1.241   -17.313 53.281  1.00 32.79  ? 266  HIS B CE1 1 
ATOM   5855 N  NE2 . HIS B 1 266 ? -0.042  -17.123 53.023  1.00 33.51  ? 266  HIS B NE2 1 
ATOM   5856 N  N   . GLU B 1 267 ? 0.287   -15.458 56.505  1.00 30.80  ? 267  GLU B N   1 
ATOM   5857 C  CA  . GLU B 1 267 ? -0.736  -16.450 56.816  1.00 30.10  ? 267  GLU B CA  1 
ATOM   5858 C  C   . GLU B 1 267 ? -1.623  -15.995 57.964  1.00 29.85  ? 267  GLU B C   1 
ATOM   5859 O  O   . GLU B 1 267 ? -2.854  -16.047 57.867  1.00 32.11  ? 267  GLU B O   1 
ATOM   5860 C  CB  . GLU B 1 267 ? -0.082  -17.793 57.111  1.00 33.56  ? 267  GLU B CB  1 
ATOM   5861 C  CG  . GLU B 1 267 ? -0.927  -18.715 57.952  1.00 33.00  ? 267  GLU B CG  1 
ATOM   5862 C  CD  . GLU B 1 267 ? -2.101  -19.309 57.192  1.00 37.87  ? 267  GLU B CD  1 
ATOM   5863 O  OE1 . GLU B 1 267 ? -1.989  -19.524 55.968  1.00 39.34  ? 267  GLU B OE1 1 
ATOM   5864 O  OE2 . GLU B 1 267 ? -3.123  -19.611 57.856  1.00 42.17  ? 267  GLU B OE2 1 
ATOM   5865 N  N   . THR B 1 268 ? -1.019  -15.534 59.050  1.00 27.70  ? 268  THR B N   1 
ATOM   5866 C  CA  . THR B 1 268 ? -1.814  -15.108 60.196  1.00 30.35  ? 268  THR B CA  1 
ATOM   5867 C  C   . THR B 1 268 ? -2.659  -13.883 59.881  1.00 29.50  ? 268  THR B C   1 
ATOM   5868 O  O   . THR B 1 268 ? -3.735  -13.725 60.465  1.00 29.39  ? 268  THR B O   1 
ATOM   5869 C  CB  . THR B 1 268 ? -0.908  -14.841 61.388  1.00 33.27  ? 268  THR B CB  1 
ATOM   5870 O  OG1 . THR B 1 268 ? 0.245   -14.128 60.940  1.00 32.43  ? 268  THR B OG1 1 
ATOM   5871 C  CG2 . THR B 1 268 ? -0.468  -16.174 62.058  1.00 31.51  ? 268  THR B CG2 1 
ATOM   5872 N  N   . THR B 1 269 ? -2.206  -13.014 58.974  1.00 26.80  ? 269  THR B N   1 
ATOM   5873 C  CA  . THR B 1 269 ? -2.997  -11.836 58.627  1.00 26.98  ? 269  THR B CA  1 
ATOM   5874 C  C   . THR B 1 269 ? -4.177  -12.207 57.747  1.00 30.11  ? 269  THR B C   1 
ATOM   5875 O  O   . THR B 1 269 ? -5.249  -11.586 57.839  1.00 28.51  ? 269  THR B O   1 
ATOM   5876 C  CB  . THR B 1 269 ? -2.103  -10.791 57.938  1.00 28.31  ? 269  THR B CB  1 
ATOM   5877 O  OG1 . THR B 1 269 ? -0.984  -10.489 58.792  1.00 28.70  ? 269  THR B OG1 1 
ATOM   5878 C  CG2 . THR B 1 269 ? -2.877  -9.488  57.666  1.00 28.54  ? 269  THR B CG2 1 
ATOM   5879 N  N   . SER B 1 270 ? -4.001  -13.212 56.888  1.00 26.69  ? 270  SER B N   1 
ATOM   5880 C  CA  . SER B 1 270 ? -5.141  -13.709 56.121  1.00 28.34  ? 270  SER B CA  1 
ATOM   5881 C  C   . SER B 1 270 ? -6.206  -14.271 57.053  1.00 29.51  ? 270  SER B C   1 
ATOM   5882 O  O   . SER B 1 270 ? -7.409  -14.039 56.856  1.00 30.00  ? 270  SER B O   1 
ATOM   5883 C  CB  . SER B 1 270 ? -4.670  -14.778 55.127  1.00 28.95  ? 270  SER B CB  1 
ATOM   5884 O  OG  . SER B 1 270 ? -5.812  -15.439 54.590  1.00 38.61  ? 270  SER B OG  1 
ATOM   5885 N  N   . GLY B 1 271 ? -5.783  -15.023 58.069  1.00 28.67  ? 271  GLY B N   1 
ATOM   5886 C  CA  . GLY B 1 271 ? -6.725  -15.490 59.072  1.00 27.77  ? 271  GLY B CA  1 
ATOM   5887 C  C   . GLY B 1 271 ? -7.440  -14.354 59.780  1.00 28.15  ? 271  GLY B C   1 
ATOM   5888 O  O   . GLY B 1 271 ? -8.653  -14.409 59.977  1.00 29.06  ? 271  GLY B O   1 
ATOM   5889 N  N   . LEU B 1 272 ? -6.702  -13.311 60.173  1.00 27.08  ? 272  LEU B N   1 
ATOM   5890 C  CA  . LEU B 1 272 ? -7.332  -12.187 60.875  1.00 28.01  ? 272  LEU B CA  1 
ATOM   5891 C  C   . LEU B 1 272 ? -8.408  -11.536 60.012  1.00 27.46  ? 272  LEU B C   1 
ATOM   5892 O  O   . LEU B 1 272 ? -9.543  -11.315 60.458  1.00 28.37  ? 272  LEU B O   1 
ATOM   5893 C  CB  . LEU B 1 272 ? -6.274  -11.157 61.266  1.00 28.57  ? 272  LEU B CB  1 
ATOM   5894 C  CG  . LEU B 1 272 ? -6.811  -9.805  61.755  1.00 27.40  ? 272  LEU B CG  1 
ATOM   5895 C  CD1 . LEU B 1 272 ? -7.808  -9.970  62.932  1.00 27.11  ? 272  LEU B CD1 1 
ATOM   5896 C  CD2 . LEU B 1 272 ? -5.645  -8.907  62.154  1.00 28.21  ? 272  LEU B CD2 1 
ATOM   5897 N  N   . LEU B 1 273 ? -8.064  -11.197 58.769  1.00 26.08  ? 273  LEU B N   1 
ATOM   5898 C  CA  . LEU B 1 273 ? -9.047  -10.574 57.891  1.00 25.30  ? 273  LEU B CA  1 
ATOM   5899 C  C   . LEU B 1 273 ? -10.258 -11.469 57.709  1.00 29.86  ? 273  LEU B C   1 
ATOM   5900 O  O   . LEU B 1 273 ? -11.393 -10.984 57.682  1.00 28.23  ? 273  LEU B O   1 
ATOM   5901 C  CB  . LEU B 1 273 ? -8.409  -10.242 56.539  1.00 26.22  ? 273  LEU B CB  1 
ATOM   5902 C  CG  . LEU B 1 273 ? -7.576  -8.961  56.592  1.00 28.28  ? 273  LEU B CG  1 
ATOM   5903 C  CD1 . LEU B 1 273 ? -6.630  -8.859  55.369  1.00 29.82  ? 273  LEU B CD1 1 
ATOM   5904 C  CD2 . LEU B 1 273 ? -8.477  -7.734  56.706  1.00 32.59  ? 273  LEU B CD2 1 
ATOM   5905 N  N   . SER B 1 274 ? -10.036 -12.780 57.556  1.00 26.22  ? 274  SER B N   1 
ATOM   5906 C  CA  . SER B 1 274 ? -11.156 -13.701 57.368  1.00 29.14  ? 274  SER B CA  1 
ATOM   5907 C  C   . SER B 1 274 ? -12.058 -13.745 58.601  1.00 29.91  ? 274  SER B C   1 
ATOM   5908 O  O   . SER B 1 274 ? -13.287 -13.701 58.483  1.00 30.14  ? 274  SER B O   1 
ATOM   5909 C  CB  . SER B 1 274 ? -10.630 -15.101 57.025  1.00 30.22  ? 274  SER B CB  1 
ATOM   5910 O  OG  . SER B 1 274 ? -9.854  -15.073 55.820  1.00 28.80  ? 274  SER B OG  1 
ATOM   5911 N  N   . PHE B 1 275 ? -11.473 -13.879 59.796  1.00 26.97  ? 275  PHE B N   1 
ATOM   5912 C  CA  . PHE B 1 275 ? -12.288 -13.863 61.013  1.00 26.53  ? 275  PHE B CA  1 
ATOM   5913 C  C   . PHE B 1 275 ? -12.997 -12.524 61.182  1.00 29.22  ? 275  PHE B C   1 
ATOM   5914 O  O   . PHE B 1 275 ? -14.166 -12.470 61.605  1.00 27.88  ? 275  PHE B O   1 
ATOM   5915 C  CB  . PHE B 1 275 ? -11.418 -14.167 62.236  1.00 28.53  ? 275  PHE B CB  1 
ATOM   5916 C  CG  . PHE B 1 275 ? -11.171 -15.636 62.477  1.00 28.53  ? 275  PHE B CG  1 
ATOM   5917 C  CD1 . PHE B 1 275 ? -12.211 -16.480 62.868  1.00 29.19  ? 275  PHE B CD1 1 
ATOM   5918 C  CD2 . PHE B 1 275 ? -9.881  -16.163 62.357  1.00 28.04  ? 275  PHE B CD2 1 
ATOM   5919 C  CE1 . PHE B 1 275 ? -11.989 -17.845 63.118  1.00 29.54  ? 275  PHE B CE1 1 
ATOM   5920 C  CE2 . PHE B 1 275 ? -9.636  -17.526 62.612  1.00 31.97  ? 275  PHE B CE2 1 
ATOM   5921 C  CZ  . PHE B 1 275 ? -10.700 -18.369 62.990  1.00 31.05  ? 275  PHE B CZ  1 
ATOM   5922 N  N   . ALA B 1 276 ? -12.316 -11.427 60.859  1.00 28.05  ? 276  ALA B N   1 
ATOM   5923 C  CA  . ALA B 1 276 ? -12.945 -10.124 61.050  1.00 28.63  ? 276  ALA B CA  1 
ATOM   5924 C  C   . ALA B 1 276 ? -14.185 -9.981  60.169  1.00 28.78  ? 276  ALA B C   1 
ATOM   5925 O  O   . ALA B 1 276 ? -15.241 -9.517  60.626  1.00 29.75  ? 276  ALA B O   1 
ATOM   5926 C  CB  . ALA B 1 276 ? -11.938 -9.008  60.764  1.00 29.22  ? 276  ALA B CB  1 
ATOM   5927 N  N   . LEU B 1 277 ? -14.078 -10.358 58.890  1.00 27.21  ? 277  LEU B N   1 
ATOM   5928 C  CA  . LEU B 1 277 ? -15.260 -10.271 58.030  1.00 27.71  ? 277  LEU B CA  1 
ATOM   5929 C  C   . LEU B 1 277 ? -16.350 -11.218 58.497  1.00 29.73  ? 277  LEU B C   1 
ATOM   5930 O  O   . LEU B 1 277 ? -17.537 -10.858 58.462  1.00 27.74  ? 277  LEU B O   1 
ATOM   5931 C  CB  . LEU B 1 277 ? -14.894 -10.537 56.565  1.00 28.85  ? 277  LEU B CB  1 
ATOM   5932 C  CG  . LEU B 1 277 ? -16.053 -10.283 55.584  1.00 33.47  ? 277  LEU B CG  1 
ATOM   5933 C  CD1 . LEU B 1 277 ? -16.542 -8.826  55.614  1.00 31.68  ? 277  LEU B CD1 1 
ATOM   5934 C  CD2 . LEU B 1 277 ? -15.635 -10.685 54.173  1.00 32.26  ? 277  LEU B CD2 1 
ATOM   5935 N  N   . TYR B 1 278 ? -15.982 -12.428 58.934  1.00 27.97  ? 278  TYR B N   1 
ATOM   5936 C  CA  . TYR B 1 278 ? -16.981 -13.322 59.531  1.00 26.62  ? 278  TYR B CA  1 
ATOM   5937 C  C   . TYR B 1 278 ? -17.729 -12.619 60.656  1.00 30.87  ? 278  TYR B C   1 
ATOM   5938 O  O   . TYR B 1 278 ? -18.963 -12.553 60.657  1.00 29.23  ? 278  TYR B O   1 
ATOM   5939 C  CB  . TYR B 1 278 ? -16.317 -14.613 60.043  1.00 27.70  ? 278  TYR B CB  1 
ATOM   5940 C  CG  . TYR B 1 278 ? -17.216 -15.412 60.932  1.00 28.33  ? 278  TYR B CG  1 
ATOM   5941 C  CD1 . TYR B 1 278 ? -18.150 -16.306 60.396  1.00 30.44  ? 278  TYR B CD1 1 
ATOM   5942 C  CD2 . TYR B 1 278 ? -17.141 -15.284 62.308  1.00 29.45  ? 278  TYR B CD2 1 
ATOM   5943 C  CE1 . TYR B 1 278 ? -18.999 -17.026 61.228  1.00 29.93  ? 278  TYR B CE1 1 
ATOM   5944 C  CE2 . TYR B 1 278 ? -17.992 -16.009 63.154  1.00 30.45  ? 278  TYR B CE2 1 
ATOM   5945 C  CZ  . TYR B 1 278 ? -18.918 -16.872 62.600  1.00 31.05  ? 278  TYR B CZ  1 
ATOM   5946 O  OH  . TYR B 1 278 ? -19.756 -17.573 63.445  1.00 33.64  ? 278  TYR B OH  1 
ATOM   5947 N  N   . PHE B 1 279 ? -17.000 -12.076 61.633  1.00 26.83  ? 279  PHE B N   1 
ATOM   5948 C  CA  . PHE B 1 279 ? -17.697 -11.445 62.755  1.00 26.39  ? 279  PHE B CA  1 
ATOM   5949 C  C   . PHE B 1 279 ? -18.520 -10.244 62.311  1.00 28.41  ? 279  PHE B C   1 
ATOM   5950 O  O   . PHE B 1 279 ? -19.601 -9.998  62.859  1.00 29.01  ? 279  PHE B O   1 
ATOM   5951 C  CB  . PHE B 1 279 ? -16.694 -11.054 63.846  1.00 29.96  ? 279  PHE B CB  1 
ATOM   5952 C  CG  . PHE B 1 279 ? -16.271 -12.223 64.695  1.00 30.83  ? 279  PHE B CG  1 
ATOM   5953 C  CD1 . PHE B 1 279 ? -17.202 -12.922 65.440  1.00 28.52  ? 279  PHE B CD1 1 
ATOM   5954 C  CD2 . PHE B 1 279 ? -14.948 -12.642 64.713  1.00 31.87  ? 279  PHE B CD2 1 
ATOM   5955 C  CE1 . PHE B 1 279 ? -16.820 -14.004 66.227  1.00 33.13  ? 279  PHE B CE1 1 
ATOM   5956 C  CE2 . PHE B 1 279 ? -14.556 -13.742 65.485  1.00 30.45  ? 279  PHE B CE2 1 
ATOM   5957 C  CZ  . PHE B 1 279 ? -15.497 -14.420 66.252  1.00 31.62  ? 279  PHE B CZ  1 
ATOM   5958 N  N   . LEU B 1 280 ? -18.066 -9.515  61.296  1.00 29.44  ? 280  LEU B N   1 
ATOM   5959 C  CA  . LEU B 1 280 ? -18.851 -8.370  60.840  1.00 28.41  ? 280  LEU B CA  1 
ATOM   5960 C  C   . LEU B 1 280 ? -20.178 -8.814  60.238  1.00 29.51  ? 280  LEU B C   1 
ATOM   5961 O  O   . LEU B 1 280 ? -21.221 -8.249  60.564  1.00 29.97  ? 280  LEU B O   1 
ATOM   5962 C  CB  . LEU B 1 280 ? -18.059 -7.541  59.833  1.00 29.64  ? 280  LEU B CB  1 
ATOM   5963 C  CG  . LEU B 1 280 ? -16.931 -6.768  60.513  1.00 29.35  ? 280  LEU B CG  1 
ATOM   5964 C  CD1 . LEU B 1 280 ? -16.064 -6.051  59.465  1.00 31.74  ? 280  LEU B CD1 1 
ATOM   5965 C  CD2 . LEU B 1 280 ? -17.449 -5.774  61.579  1.00 35.71  ? 280  LEU B CD2 1 
ATOM   5966 N  N   . VAL B 1 281 ? -20.169 -9.816  59.355  1.00 30.28  ? 281  VAL B N   1 
ATOM   5967 C  CA  . VAL B 1 281 ? -21.454 -10.195 58.756  1.00 28.06  ? 281  VAL B CA  1 
ATOM   5968 C  C   . VAL B 1 281 ? -22.369 -10.867 59.777  1.00 31.14  ? 281  VAL B C   1 
ATOM   5969 O  O   . VAL B 1 281 ? -23.602 -10.869 59.599  1.00 34.51  ? 281  VAL B O   1 
ATOM   5970 C  CB  . VAL B 1 281 ? -21.259 -11.079 57.503  1.00 29.76  ? 281  VAL B CB  1 
ATOM   5971 C  CG1 . VAL B 1 281 ? -20.416 -10.355 56.467  1.00 32.73  ? 281  VAL B CG1 1 
ATOM   5972 C  CG2 . VAL B 1 281 ? -20.687 -12.452 57.844  1.00 29.71  ? 281  VAL B CG2 1 
ATOM   5973 N  N   . LYS B 1 282 ? -21.818 -11.426 60.858  1.00 28.31  ? 282  LYS B N   1 
ATOM   5974 C  CA  . LYS B 1 282 ? -22.654 -12.004 61.910  1.00 29.73  ? 282  LYS B CA  1 
ATOM   5975 C  C   . LYS B 1 282 ? -23.135 -10.972 62.931  1.00 28.43  ? 282  LYS B C   1 
ATOM   5976 O  O   . LYS B 1 282 ? -23.935 -11.315 63.818  1.00 31.96  ? 282  LYS B O   1 
ATOM   5977 C  CB  . LYS B 1 282 ? -21.892 -13.125 62.636  1.00 31.70  ? 282  LYS B CB  1 
ATOM   5978 C  CG  . LYS B 1 282 ? -21.515 -14.329 61.749  1.00 29.27  ? 282  LYS B CG  1 
ATOM   5979 C  CD  . LYS B 1 282 ? -22.769 -15.019 61.196  1.00 32.66  ? 282  LYS B CD  1 
ATOM   5980 C  CE  . LYS B 1 282 ? -22.411 -16.414 60.653  1.00 30.73  ? 282  LYS B CE  1 
ATOM   5981 N  NZ  . LYS B 1 282 ? -23.568 -16.996 59.896  1.00 30.74  ? 282  LYS B NZ  1 
ATOM   5982 N  N   . ASN B 1 283 ? -22.687 -9.722  62.837  1.00 30.62  ? 283  ASN B N   1 
ATOM   5983 C  CA  . ASN B 1 283 ? -23.004 -8.699  63.842  1.00 30.07  ? 283  ASN B CA  1 
ATOM   5984 C  C   . ASN B 1 283 ? -23.275 -7.390  63.122  1.00 30.39  ? 283  ASN B C   1 
ATOM   5985 O  O   . ASN B 1 283 ? -22.440 -6.484  63.100  1.00 29.91  ? 283  ASN B O   1 
ATOM   5986 C  CB  . ASN B 1 283 ? -21.868 -8.551  64.862  1.00 29.91  ? 283  ASN B CB  1 
ATOM   5987 C  CG  . ASN B 1 283 ? -21.713 -9.772  65.739  1.00 32.71  ? 283  ASN B CG  1 
ATOM   5988 O  OD1 . ASN B 1 283 ? -22.393 -9.899  66.758  1.00 31.14  ? 283  ASN B OD1 1 
ATOM   5989 N  ND2 . ASN B 1 283 ? -20.810 -10.686 65.350  1.00 30.56  ? 283  ASN B ND2 1 
ATOM   5990 N  N   . PRO B 1 284 ? -24.446 -7.263  62.504  1.00 29.18  ? 284  PRO B N   1 
ATOM   5991 C  CA  . PRO B 1 284 ? -24.697 -6.102  61.636  1.00 28.91  ? 284  PRO B CA  1 
ATOM   5992 C  C   . PRO B 1 284 ? -24.608 -4.746  62.329  1.00 29.21  ? 284  PRO B C   1 
ATOM   5993 O  O   . PRO B 1 284 ? -24.277 -3.755  61.659  1.00 30.04  ? 284  PRO B O   1 
ATOM   5994 C  CB  . PRO B 1 284 ? -26.115 -6.372  61.091  1.00 33.17  ? 284  PRO B CB  1 
ATOM   5995 C  CG  . PRO B 1 284 ? -26.641 -7.557  61.852  1.00 35.35  ? 284  PRO B CG  1 
ATOM   5996 C  CD  . PRO B 1 284 ? -25.453 -8.321  62.341  1.00 31.49  ? 284  PRO B CD  1 
ATOM   5997 N  N   . HIS B 1 285 ? -24.903 -4.650  63.631  1.00 28.30  ? 285  HIS B N   1 
ATOM   5998 C  CA  . HIS B 1 285 ? -24.695 -3.376  64.318  1.00 30.44  ? 285  HIS B CA  1 
ATOM   5999 C  C   . HIS B 1 285 ? -23.236 -2.964  64.238  1.00 29.66  ? 285  HIS B C   1 
ATOM   6000 O  O   . HIS B 1 285 ? -22.917 -1.792  64.004  1.00 30.94  ? 285  HIS B O   1 
ATOM   6001 C  CB  . HIS B 1 285 ? -25.105 -3.473  65.791  1.00 33.31  ? 285  HIS B CB  1 
ATOM   6002 C  CG  . HIS B 1 285 ? -26.581 -3.511  66.013  1.00 33.56  ? 285  HIS B CG  1 
ATOM   6003 N  ND1 . HIS B 1 285 ? -27.433 -2.550  65.521  1.00 36.86  ? 285  HIS B ND1 1 
ATOM   6004 C  CD2 . HIS B 1 285 ? -27.357 -4.410  66.661  1.00 34.55  ? 285  HIS B CD2 1 
ATOM   6005 C  CE1 . HIS B 1 285 ? -28.673 -2.841  65.878  1.00 31.74  ? 285  HIS B CE1 1 
ATOM   6006 N  NE2 . HIS B 1 285 ? -28.653 -3.965  66.566  1.00 33.62  ? 285  HIS B NE2 1 
ATOM   6007 N  N   . VAL B 1 286 ? -22.337 -3.922  64.453  1.00 28.73  ? 286  VAL B N   1 
ATOM   6008 C  CA  . VAL B 1 286 ? -20.906 -3.627  64.404  1.00 29.99  ? 286  VAL B CA  1 
ATOM   6009 C  C   . VAL B 1 286 ? -20.474 -3.319  62.977  1.00 29.05  ? 286  VAL B C   1 
ATOM   6010 O  O   . VAL B 1 286 ? -19.682 -2.398  62.724  1.00 28.33  ? 286  VAL B O   1 
ATOM   6011 C  CB  . VAL B 1 286 ? -20.117 -4.806  64.998  1.00 31.32  ? 286  VAL B CB  1 
ATOM   6012 C  CG1 . VAL B 1 286 ? -18.611 -4.556  64.902  1.00 28.60  ? 286  VAL B CG1 1 
ATOM   6013 C  CG2 . VAL B 1 286 ? -20.524 -5.056  66.439  1.00 30.14  ? 286  VAL B CG2 1 
ATOM   6014 N  N   . LEU B 1 287 ? -20.976 -4.090  62.019  1.00 28.78  ? 287  LEU B N   1 
ATOM   6015 C  CA  . LEU B 1 287 ? -20.657 -3.812  60.630  1.00 28.40  ? 287  LEU B CA  1 
ATOM   6016 C  C   . LEU B 1 287 ? -21.056 -2.388  60.255  1.00 30.79  ? 287  LEU B C   1 
ATOM   6017 O  O   . LEU B 1 287 ? -20.298 -1.673  59.590  1.00 32.80  ? 287  LEU B O   1 
ATOM   6018 C  CB  . LEU B 1 287 ? -21.336 -4.860  59.743  1.00 29.05  ? 287  LEU B CB  1 
ATOM   6019 C  CG  . LEU B 1 287 ? -21.202 -4.664  58.245  1.00 35.51  ? 287  LEU B CG  1 
ATOM   6020 C  CD1 . LEU B 1 287 ? -19.788 -4.253  57.901  1.00 37.34  ? 287  LEU B CD1 1 
ATOM   6021 C  CD2 . LEU B 1 287 ? -21.574 -5.967  57.534  1.00 41.64  ? 287  LEU B CD2 1 
ATOM   6022 N  N   . GLN B 1 288 ? -22.224 -1.935  60.721  1.00 30.82  ? 288  GLN B N   1 
ATOM   6023 C  CA  . GLN B 1 288 ? -22.668 -0.582  60.396  1.00 32.00  ? 288  GLN B CA  1 
ATOM   6024 C  C   . GLN B 1 288 ? -21.719 0.462   60.969  1.00 28.28  ? 288  GLN B C   1 
ATOM   6025 O  O   . GLN B 1 288 ? -21.360 1.427   60.282  1.00 30.17  ? 288  GLN B O   1 
ATOM   6026 C  CB  . GLN B 1 288 ? -24.087 -0.357  60.917  1.00 35.71  ? 288  GLN B CB  1 
ATOM   6027 C  CG  . GLN B 1 288 ? -24.564 1.082   60.821  1.00 40.59  ? 288  GLN B CG  1 
ATOM   6028 C  CD  . GLN B 1 288 ? -26.059 1.218   61.067  1.00 56.31  ? 288  GLN B CD  1 
ATOM   6029 O  OE1 . GLN B 1 288 ? -26.478 1.766   62.086  1.00 59.40  ? 288  GLN B OE1 1 
ATOM   6030 N  NE2 . GLN B 1 288 ? -26.869 0.719   60.135  1.00 58.64  ? 288  GLN B NE2 1 
ATOM   6031 N  N   . LYS B 1 289 ? -21.276 0.275   62.220  1.00 28.26  ? 289  LYS B N   1 
ATOM   6032 C  CA  . LYS B 1 289 ? -20.386 1.270   62.827  1.00 27.67  ? 289  LYS B CA  1 
ATOM   6033 C  C   . LYS B 1 289 ? -19.045 1.303   62.110  1.00 30.74  ? 289  LYS B C   1 
ATOM   6034 O  O   . LYS B 1 289 ? -18.468 2.375   61.894  1.00 30.74  ? 289  LYS B O   1 
ATOM   6035 C  CB  . LYS B 1 289 ? -20.181 0.968   64.319  1.00 30.60  ? 289  LYS B CB  1 
ATOM   6036 C  CG  . LYS B 1 289 ? -21.321 1.466   65.223  1.00 38.65  ? 289  LYS B CG  1 
ATOM   6037 C  CD  . LYS B 1 289 ? -21.119 1.052   66.692  1.00 36.49  ? 289  LYS B CD  1 
ATOM   6038 C  CE  . LYS B 1 289 ? -20.035 1.863   67.421  1.00 33.06  ? 289  LYS B CE  1 
ATOM   6039 N  NZ  . LYS B 1 289 ? -20.162 1.743   68.945  1.00 31.77  ? 289  LYS B NZ  1 
ATOM   6040 N  N   . ALA B 1 290 ? -18.538 0.133   61.729  1.00 30.14  ? 290  ALA B N   1 
ATOM   6041 C  CA  . ALA B 1 290 ? -17.258 0.088   61.033  1.00 28.33  ? 290  ALA B CA  1 
ATOM   6042 C  C   . ALA B 1 290 ? -17.367 0.695   59.643  1.00 28.42  ? 290  ALA B C   1 
ATOM   6043 O  O   . ALA B 1 290 ? -16.460 1.408   59.188  1.00 29.99  ? 290  ALA B O   1 
ATOM   6044 C  CB  . ALA B 1 290 ? -16.770 -1.361  60.935  1.00 28.15  ? 290  ALA B CB  1 
ATOM   6045 N  N   . ALA B 1 291 ? -18.448 0.380   58.933  1.00 28.35  ? 291  ALA B N   1 
ATOM   6046 C  CA  . ALA B 1 291 ? -18.633 0.916   57.594  1.00 30.66  ? 291  ALA B CA  1 
ATOM   6047 C  C   . ALA B 1 291 ? -18.836 2.431   57.624  1.00 28.99  ? 291  ALA B C   1 
ATOM   6048 O  O   . ALA B 1 291 ? -18.376 3.144   56.722  1.00 29.22  ? 291  ALA B O   1 
ATOM   6049 C  CB  . ALA B 1 291 ? -19.814 0.205   56.917  1.00 31.41  ? 291  ALA B CB  1 
ATOM   6050 N  N   . GLU B 1 292 ? -19.538 2.944   58.637  1.00 28.37  ? 292  GLU B N   1 
ATOM   6051 C  CA  . GLU B 1 292 ? -19.661 4.393   58.778  1.00 32.04  ? 292  GLU B CA  1 
ATOM   6052 C  C   . GLU B 1 292 ? -18.293 5.041   58.833  1.00 31.59  ? 292  GLU B C   1 
ATOM   6053 O  O   . GLU B 1 292 ? -18.040 6.044   58.162  1.00 30.19  ? 292  GLU B O   1 
ATOM   6054 C  CB  . GLU B 1 292 ? -20.452 4.747   60.041  1.00 31.98  ? 292  GLU B CB  1 
ATOM   6055 C  CG  . GLU B 1 292 ? -20.821 6.235   60.135  1.00 31.65  ? 292  GLU B CG  1 
ATOM   6056 C  CD  . GLU B 1 292 ? -19.680 7.155   60.585  1.00 33.48  ? 292  GLU B CD  1 
ATOM   6057 O  OE1 . GLU B 1 292 ? -18.775 6.717   61.327  1.00 33.08  ? 292  GLU B OE1 1 
ATOM   6058 O  OE2 . GLU B 1 292 ? -19.696 8.348   60.193  1.00 32.59  ? 292  GLU B OE2 1 
ATOM   6059 N  N   . GLU B 1 293 ? -17.407 4.490   59.660  1.00 28.99  ? 293  GLU B N   1 
ATOM   6060 C  CA  . GLU B 1 293 ? -16.089 5.088   59.821  1.00 28.81  ? 293  GLU B CA  1 
ATOM   6061 C  C   . GLU B 1 293 ? -15.310 5.039   58.519  1.00 29.50  ? 293  GLU B C   1 
ATOM   6062 O  O   . GLU B 1 293 ? -14.690 6.034   58.108  1.00 28.80  ? 293  GLU B O   1 
ATOM   6063 C  CB  . GLU B 1 293 ? -15.331 4.361   60.926  1.00 29.21  ? 293  GLU B CB  1 
ATOM   6064 C  CG  . GLU B 1 293 ? -13.968 4.972   61.230  1.00 29.51  ? 293  GLU B CG  1 
ATOM   6065 C  CD  . GLU B 1 293 ? -13.268 4.209   62.333  1.00 31.11  ? 293  GLU B CD  1 
ATOM   6066 O  OE1 . GLU B 1 293 ? -12.727 3.123   62.027  1.00 31.50  ? 293  GLU B OE1 1 
ATOM   6067 O  OE2 . GLU B 1 293 ? -13.279 4.673   63.498  1.00 29.50  ? 293  GLU B OE2 1 
ATOM   6068 N  N   . ALA B 1 294 ? -15.324 3.880   57.855  1.00 29.55  ? 294  ALA B N   1 
ATOM   6069 C  CA  . ALA B 1 294 ? -14.584 3.746   56.602  1.00 28.93  ? 294  ALA B CA  1 
ATOM   6070 C  C   . ALA B 1 294 ? -15.074 4.755   55.572  1.00 30.20  ? 294  ALA B C   1 
ATOM   6071 O  O   . ALA B 1 294 ? -14.270 5.387   54.878  1.00 33.07  ? 294  ALA B O   1 
ATOM   6072 C  CB  . ALA B 1 294 ? -14.705 2.319   56.057  1.00 30.61  ? 294  ALA B CB  1 
ATOM   6073 N  N   . ALA B 1 295 ? -16.401 4.899   55.436  1.00 30.60  ? 295  ALA B N   1 
ATOM   6074 C  CA  . ALA B 1 295 ? -16.926 5.836   54.444  1.00 32.64  ? 295  ALA B CA  1 
ATOM   6075 C  C   . ALA B 1 295 ? -16.543 7.264   54.795  1.00 34.23  ? 295  ALA B C   1 
ATOM   6076 O  O   . ALA B 1 295 ? -16.242 8.078   53.912  1.00 35.56  ? 295  ALA B O   1 
ATOM   6077 C  CB  . ALA B 1 295 ? -18.447 5.696   54.334  1.00 33.33  ? 295  ALA B CB  1 
ATOM   6078 N  N   . ARG B 1 296 ? -16.523 7.585   56.087  1.00 31.50  ? 296  ARG B N   1 
ATOM   6079 C  CA  . ARG B 1 296 ? -16.262 8.958   56.492  1.00 31.46  ? 296  ARG B CA  1 
ATOM   6080 C  C   . ARG B 1 296 ? -14.784 9.316   56.403  1.00 34.46  ? 296  ARG B C   1 
ATOM   6081 O  O   . ARG B 1 296 ? -14.435 10.455  56.058  1.00 33.93  ? 296  ARG B O   1 
ATOM   6082 C  CB  . ARG B 1 296 ? -16.764 9.176   57.918  1.00 31.16  ? 296  ARG B CB  1 
ATOM   6083 C  CG  . ARG B 1 296 ? -16.275 10.478  58.545  1.00 34.87  ? 296  ARG B CG  1 
ATOM   6084 C  CD  . ARG B 1 296 ? -17.101 10.809  59.788  1.00 37.54  ? 296  ARG B CD  1 
ATOM   6085 N  NE  . ARG B 1 296 ? -17.231 9.673   60.694  1.00 34.77  ? 296  ARG B NE  1 
ATOM   6086 C  CZ  . ARG B 1 296 ? -16.347 9.359   61.635  1.00 35.56  ? 296  ARG B CZ  1 
ATOM   6087 N  NH1 . ARG B 1 296 ? -15.238 10.063  61.804  1.00 37.74  ? 296  ARG B NH1 1 
ATOM   6088 N  NH2 . ARG B 1 296 ? -16.573 8.303   62.418  1.00 34.29  ? 296  ARG B NH2 1 
ATOM   6089 N  N   . VAL B 1 297 ? -13.908 8.374   56.732  1.00 30.40  ? 297  VAL B N   1 
ATOM   6090 C  CA  . VAL B 1 297 ? -12.477 8.658   56.812  1.00 30.55  ? 297  VAL B CA  1 
ATOM   6091 C  C   . VAL B 1 297 ? -11.795 8.509   55.456  1.00 32.35  ? 297  VAL B C   1 
ATOM   6092 O  O   . VAL B 1 297 ? -10.931 9.317   55.096  1.00 31.49  ? 297  VAL B O   1 
ATOM   6093 C  CB  . VAL B 1 297 ? -11.843 7.742   57.874  1.00 30.63  ? 297  VAL B CB  1 
ATOM   6094 C  CG1 . VAL B 1 297 ? -10.289 7.757   57.767  1.00 30.27  ? 297  VAL B CG1 1 
ATOM   6095 C  CG2 . VAL B 1 297 ? -12.255 8.202   59.252  1.00 30.61  ? 297  VAL B CG2 1 
ATOM   6096 N  N   . LEU B 1 298 ? -12.147 7.476   54.691  1.00 31.80  ? 298  LEU B N   1 
ATOM   6097 C  CA  . LEU B 1 298 ? -11.435 7.181   53.444  1.00 30.08  ? 298  LEU B CA  1 
ATOM   6098 C  C   . LEU B 1 298 ? -12.059 7.975   52.295  1.00 33.69  ? 298  LEU B C   1 
ATOM   6099 O  O   . LEU B 1 298 ? -12.720 7.438   51.407  1.00 33.65  ? 298  LEU B O   1 
ATOM   6100 C  CB  . LEU B 1 298 ? -11.449 5.684   53.165  1.00 29.83  ? 298  LEU B CB  1 
ATOM   6101 C  CG  . LEU B 1 298 ? -10.811 4.812   54.235  1.00 30.48  ? 298  LEU B CG  1 
ATOM   6102 C  CD1 . LEU B 1 298 ? -10.867 3.329   53.834  1.00 32.44  ? 298  LEU B CD1 1 
ATOM   6103 C  CD2 . LEU B 1 298 ? -9.385  5.260   54.432  1.00 30.44  ? 298  LEU B CD2 1 
ATOM   6104 N  N   . VAL B 1 299 ? -11.820 9.293   52.326  1.00 32.14  ? 299  VAL B N   1 
ATOM   6105 C  CA  . VAL B 1 299 ? -12.504 10.191  51.399  1.00 37.31  ? 299  VAL B CA  1 
ATOM   6106 C  C   . VAL B 1 299 ? -11.872 10.237  50.019  1.00 38.10  ? 299  VAL B C   1 
ATOM   6107 O  O   . VAL B 1 299 ? -12.470 10.813  49.098  1.00 39.16  ? 299  VAL B O   1 
ATOM   6108 C  CB  . VAL B 1 299 ? -12.557 11.620  51.973  1.00 37.63  ? 299  VAL B CB  1 
ATOM   6109 C  CG1 . VAL B 1 299 ? -13.476 11.650  53.199  1.00 40.28  ? 299  VAL B CG1 1 
ATOM   6110 C  CG2 . VAL B 1 299 ? -11.164 12.103  52.327  1.00 35.57  ? 299  VAL B CG2 1 
ATOM   6111 N  N   . ASP B 1 300 ? -10.678 9.666   49.849  1.00 35.08  ? 300  ASP B N   1 
ATOM   6112 C  CA  . ASP B 1 300 ? -9.974  9.712   48.582  1.00 40.07  ? 300  ASP B CA  1 
ATOM   6113 C  C   . ASP B 1 300 ? -9.958  8.341   47.914  1.00 37.55  ? 300  ASP B C   1 
ATOM   6114 O  O   . ASP B 1 300 ? -9.966  7.310   48.595  1.00 37.40  ? 300  ASP B O   1 
ATOM   6115 C  CB  . ASP B 1 300 ? -8.529  10.188  48.786  1.00 36.11  ? 300  ASP B CB  1 
ATOM   6116 C  CG  . ASP B 1 300 ? -8.454  11.579  49.393  1.00 40.73  ? 300  ASP B CG  1 
ATOM   6117 O  OD1 . ASP B 1 300 ? -9.159  12.471  48.890  1.00 41.27  ? 300  ASP B OD1 1 
ATOM   6118 O  OD2 . ASP B 1 300 ? -7.700  11.780  50.376  1.00 42.18  ? 300  ASP B OD2 1 
ATOM   6119 N  N   . PRO B 1 301 ? -9.898  8.299   46.580  1.00 38.37  ? 301  PRO B N   1 
ATOM   6120 C  CA  . PRO B 1 301 ? -9.827  6.998   45.897  1.00 36.54  ? 301  PRO B CA  1 
ATOM   6121 C  C   . PRO B 1 301 ? -8.663  6.142   46.360  1.00 34.40  ? 301  PRO B C   1 
ATOM   6122 O  O   . PRO B 1 301 ? -8.792  4.917   46.414  1.00 37.52  ? 301  PRO B O   1 
ATOM   6123 C  CB  . PRO B 1 301 ? -9.684  7.383   44.415  1.00 40.89  ? 301  PRO B CB  1 
ATOM   6124 C  CG  . PRO B 1 301 ? -10.215 8.767   44.314  1.00 42.77  ? 301  PRO B CG  1 
ATOM   6125 C  CD  . PRO B 1 301 ? -9.983  9.433   45.645  1.00 41.64  ? 301  PRO B CD  1 
ATOM   6126 N  N   . VAL B 1 302 ? -7.524  6.755   46.671  1.00 35.03  ? 302  VAL B N   1 
ATOM   6127 C  CA  . VAL B 1 302 ? -6.329  6.078   47.164  1.00 39.55  ? 302  VAL B CA  1 
ATOM   6128 C  C   . VAL B 1 302 ? -6.187  6.422   48.648  1.00 38.97  ? 302  VAL B C   1 
ATOM   6129 O  O   . VAL B 1 302 ? -5.906  7.579   48.979  1.00 39.98  ? 302  VAL B O   1 
ATOM   6130 C  CB  . VAL B 1 302 ? -5.081  6.502   46.372  1.00 38.86  ? 302  VAL B CB  1 
ATOM   6131 C  CG1 . VAL B 1 302 ? -3.844  5.793   46.883  1.00 40.77  ? 302  VAL B CG1 1 
ATOM   6132 C  CG2 . VAL B 1 302 ? -5.264  6.261   44.868  1.00 44.28  ? 302  VAL B CG2 1 
ATOM   6133 N  N   . PRO B 1 303 ? -6.370  5.473   49.573  1.00 35.08  ? 303  PRO B N   1 
ATOM   6134 C  CA  . PRO B 1 303 ? -6.204  5.804   51.000  1.00 34.47  ? 303  PRO B CA  1 
ATOM   6135 C  C   . PRO B 1 303 ? -4.774  6.203   51.321  1.00 32.90  ? 303  PRO B C   1 
ATOM   6136 O  O   . PRO B 1 303 ? -3.820  5.643   50.782  1.00 34.52  ? 303  PRO B O   1 
ATOM   6137 C  CB  . PRO B 1 303 ? -6.591  4.504   51.716  1.00 38.04  ? 303  PRO B CB  1 
ATOM   6138 C  CG  . PRO B 1 303 ? -7.442  3.765   50.715  1.00 39.76  ? 303  PRO B CG  1 
ATOM   6139 C  CD  . PRO B 1 303 ? -6.831  4.089   49.382  1.00 36.58  ? 303  PRO B CD  1 
ATOM   6140 N  N   . SER B 1 304 ? -4.629  7.192   52.201  1.00 30.50  ? 304  SER B N   1 
ATOM   6141 C  CA  . SER B 1 304 ? -3.307  7.594   52.656  1.00 33.69  ? 304  SER B CA  1 
ATOM   6142 C  C   . SER B 1 304 ? -2.954  6.906   53.973  1.00 29.89  ? 304  SER B C   1 
ATOM   6143 O  O   . SER B 1 304 ? -3.816  6.400   54.695  1.00 30.99  ? 304  SER B O   1 
ATOM   6144 C  CB  . SER B 1 304 ? -3.242  9.113   52.836  1.00 33.44  ? 304  SER B CB  1 
ATOM   6145 O  OG  . SER B 1 304 ? -4.031  9.504   53.956  1.00 33.65  ? 304  SER B OG  1 
ATOM   6146 N  N   . TYR B 1 305 ? -1.658  6.913   54.289  1.00 31.98  ? 305  TYR B N   1 
ATOM   6147 C  CA  . TYR B 1 305 ? -1.207  6.407   55.578  1.00 31.18  ? 305  TYR B CA  1 
ATOM   6148 C  C   . TYR B 1 305 ? -1.947  7.083   56.725  1.00 32.70  ? 305  TYR B C   1 
ATOM   6149 O  O   . TYR B 1 305 ? -2.425  6.415   57.647  1.00 31.74  ? 305  TYR B O   1 
ATOM   6150 C  CB  . TYR B 1 305 ? 0.305   6.609   55.695  1.00 33.96  ? 305  TYR B CB  1 
ATOM   6151 C  CG  . TYR B 1 305 ? 0.889   6.198   57.016  1.00 35.43  ? 305  TYR B CG  1 
ATOM   6152 C  CD1 . TYR B 1 305 ? 1.340   4.904   57.234  1.00 34.59  ? 305  TYR B CD1 1 
ATOM   6153 C  CD2 . TYR B 1 305 ? 1.011   7.127   58.046  1.00 39.70  ? 305  TYR B CD2 1 
ATOM   6154 C  CE1 . TYR B 1 305 ? 1.879   4.543   58.464  1.00 38.62  ? 305  TYR B CE1 1 
ATOM   6155 C  CE2 . TYR B 1 305 ? 1.537   6.783   59.254  1.00 43.14  ? 305  TYR B CE2 1 
ATOM   6156 C  CZ  . TYR B 1 305 ? 1.975   5.493   59.462  1.00 44.16  ? 305  TYR B CZ  1 
ATOM   6157 O  OH  . TYR B 1 305 ? 2.502   5.184   60.693  1.00 52.41  ? 305  TYR B OH  1 
ATOM   6158 N  N   . LYS B 1 306 ? -2.058  8.416   56.689  1.00 31.13  ? 306  LYS B N   1 
ATOM   6159 C  CA  . LYS B 1 306 ? -2.720  9.112   57.792  1.00 33.02  ? 306  LYS B CA  1 
ATOM   6160 C  C   . LYS B 1 306 ? -4.180  8.701   57.919  1.00 30.60  ? 306  LYS B C   1 
ATOM   6161 O  O   . LYS B 1 306 ? -4.703  8.575   59.035  1.00 31.93  ? 306  LYS B O   1 
ATOM   6162 C  CB  . LYS B 1 306 ? -2.622  10.630  57.608  1.00 39.81  ? 306  LYS B CB  1 
ATOM   6163 C  CG  . LYS B 1 306 ? -1.310  11.224  58.094  1.00 44.79  ? 306  LYS B CG  1 
ATOM   6164 C  CD  . LYS B 1 306 ? -1.135  12.667  57.634  1.00 53.35  ? 306  LYS B CD  1 
ATOM   6165 C  CE  . LYS B 1 306 ? -0.053  13.379  58.443  1.00 62.21  ? 306  LYS B CE  1 
ATOM   6166 N  NZ  . LYS B 1 306 ? 1.233   13.485  57.693  1.00 70.25  ? 306  LYS B NZ  1 
ATOM   6167 N  N   . GLN B 1 307 ? -4.855  8.485   56.792  1.00 32.02  ? 307  GLN B N   1 
ATOM   6168 C  CA  . GLN B 1 307 ? -6.257  8.077   56.858  1.00 31.05  ? 307  GLN B CA  1 
ATOM   6169 C  C   . GLN B 1 307 ? -6.396  6.694   57.486  1.00 31.70  ? 307  GLN B C   1 
ATOM   6170 O  O   . GLN B 1 307 ? -7.290  6.465   58.312  1.00 30.96  ? 307  GLN B O   1 
ATOM   6171 C  CB  . GLN B 1 307 ? -6.876  8.109   55.457  1.00 32.47  ? 307  GLN B CB  1 
ATOM   6172 C  CG  . GLN B 1 307 ? -7.176  9.523   54.949  1.00 34.23  ? 307  GLN B CG  1 
ATOM   6173 C  CD  . GLN B 1 307 ? -7.378  9.573   53.441  1.00 35.34  ? 307  GLN B CD  1 
ATOM   6174 O  OE1 . GLN B 1 307 ? -7.088  8.607   52.736  1.00 34.35  ? 307  GLN B OE1 1 
ATOM   6175 N  NE2 . GLN B 1 307 ? -7.885  10.696  52.944  1.00 36.34  ? 307  GLN B NE2 1 
ATOM   6176 N  N   . VAL B 1 308 ? -5.515  5.755   57.126  1.00 30.32  ? 308  VAL B N   1 
ATOM   6177 C  CA  . VAL B 1 308 ? -5.584  4.435   57.754  1.00 31.00  ? 308  VAL B CA  1 
ATOM   6178 C  C   . VAL B 1 308 ? -5.437  4.553   59.274  1.00 31.68  ? 308  VAL B C   1 
ATOM   6179 O  O   . VAL B 1 308 ? -6.127  3.866   60.039  1.00 32.31  ? 308  VAL B O   1 
ATOM   6180 C  CB  . VAL B 1 308 ? -4.529  3.492   57.143  1.00 29.63  ? 308  VAL B CB  1 
ATOM   6181 C  CG1 . VAL B 1 308 ? -4.479  2.179   57.937  1.00 32.98  ? 308  VAL B CG1 1 
ATOM   6182 C  CG2 . VAL B 1 308 ? -4.851  3.213   55.662  1.00 31.57  ? 308  VAL B CG2 1 
ATOM   6183 N  N   . LYS B 1 309 ? -4.548  5.432   59.742  1.00 30.78  ? 309  LYS B N   1 
ATOM   6184 C  CA  . LYS B 1 309 ? -4.371  5.601   61.181  1.00 31.24  ? 309  LYS B CA  1 
ATOM   6185 C  C   . LYS B 1 309 ? -5.619  6.144   61.867  1.00 33.68  ? 309  LYS B C   1 
ATOM   6186 O  O   . LYS B 1 309 ? -5.738  6.024   63.095  1.00 33.34  ? 309  LYS B O   1 
ATOM   6187 C  CB  . LYS B 1 309 ? -3.201  6.551   61.469  1.00 33.29  ? 309  LYS B CB  1 
ATOM   6188 C  CG  . LYS B 1 309 ? -1.857  6.035   60.979  1.00 37.62  ? 309  LYS B CG  1 
ATOM   6189 C  CD  . LYS B 1 309 ? -1.590  4.654   61.530  1.00 42.39  ? 309  LYS B CD  1 
ATOM   6190 C  CE  . LYS B 1 309 ? -0.104  4.365   61.599  1.00 52.03  ? 309  LYS B CE  1 
ATOM   6191 N  NZ  . LYS B 1 309 ? 0.177   3.077   62.307  1.00 56.32  ? 309  LYS B NZ  1 
ATOM   6192 N  N   . GLN B 1 310 ? -6.513  6.786   61.122  1.00 30.27  ? 310  GLN B N   1 
ATOM   6193 C  CA  . GLN B 1 310 ? -7.747  7.312   61.692  1.00 29.46  ? 310  GLN B CA  1 
ATOM   6194 C  C   . GLN B 1 310 ? -8.846  6.267   61.780  1.00 29.47  ? 310  GLN B C   1 
ATOM   6195 O  O   . GLN B 1 310 ? -9.922  6.572   62.307  1.00 32.73  ? 310  GLN B O   1 
ATOM   6196 C  CB  . GLN B 1 310 ? -8.274  8.497   60.861  1.00 30.67  ? 310  GLN B CB  1 
ATOM   6197 C  CG  . GLN B 1 310 ? -7.452  9.786   60.929  1.00 33.23  ? 310  GLN B CG  1 
ATOM   6198 C  CD  . GLN B 1 310 ? -7.994  10.815  59.953  1.00 38.57  ? 310  GLN B CD  1 
ATOM   6199 O  OE1 . GLN B 1 310 ? -7.888  10.638  58.742  1.00 38.83  ? 310  GLN B OE1 1 
ATOM   6200 N  NE2 . GLN B 1 310 ? -8.618  11.864  60.468  1.00 41.40  ? 310  GLN B NE2 1 
ATOM   6201 N  N   . LEU B 1 311 ? -8.636  5.056   61.268  1.00 30.14  ? 311  LEU B N   1 
ATOM   6202 C  CA  . LEU B 1 311 ? -9.689  4.034   61.316  1.00 29.19  ? 311  LEU B CA  1 
ATOM   6203 C  C   . LEU B 1 311 ? -9.655  3.327   62.671  1.00 28.29  ? 311  LEU B C   1 
ATOM   6204 O  O   . LEU B 1 311 ? -9.334  2.142   62.796  1.00 29.62  ? 311  LEU B O   1 
ATOM   6205 C  CB  . LEU B 1 311 ? -9.534  3.056   60.161  1.00 27.95  ? 311  LEU B CB  1 
ATOM   6206 C  CG  . LEU B 1 311 ? -9.713  3.656   58.764  1.00 28.79  ? 311  LEU B CG  1 
ATOM   6207 C  CD1 . LEU B 1 311 ? -9.382  2.620   57.690  1.00 33.01  ? 311  LEU B CD1 1 
ATOM   6208 C  CD2 . LEU B 1 311 ? -11.147 4.229   58.588  1.00 29.66  ? 311  LEU B CD2 1 
ATOM   6209 N  N   . LYS B 1 312 ? -10.027 4.085   63.709  1.00 30.71  ? 312  LYS B N   1 
ATOM   6210 C  CA  . LYS B 1 312 ? -9.925  3.578   65.074  1.00 30.18  ? 312  LYS B CA  1 
ATOM   6211 C  C   . LYS B 1 312 ? -10.876 2.398   65.310  1.00 29.58  ? 312  LYS B C   1 
ATOM   6212 O  O   . LYS B 1 312 ? -10.473 1.368   65.871  1.00 30.21  ? 312  LYS B O   1 
ATOM   6213 C  CB  . LYS B 1 312 ? -10.202 4.716   66.062  1.00 34.32  ? 312  LYS B CB  1 
ATOM   6214 C  CG  . LYS B 1 312 ? -10.310 4.272   67.524  1.00 42.14  ? 312  LYS B CG  1 
ATOM   6215 C  CD  . LYS B 1 312 ? -10.626 5.473   68.422  1.00 50.22  ? 312  LYS B CD  1 
ATOM   6216 C  CE  . LYS B 1 312 ? -9.897  5.394   69.767  1.00 52.41  ? 312  LYS B CE  1 
ATOM   6217 N  NZ  . LYS B 1 312 ? -10.246 4.155   70.503  1.00 49.63  ? 312  LYS B NZ  1 
ATOM   6218 N  N   . TYR B 1 313 ? -12.149 2.533   64.914  1.00 28.89  ? 313  TYR B N   1 
ATOM   6219 C  CA  . TYR B 1 313 ? -13.101 1.448   65.164  1.00 29.16  ? 313  TYR B CA  1 
ATOM   6220 C  C   . TYR B 1 313 ? -12.792 0.227   64.299  1.00 29.17  ? 313  TYR B C   1 
ATOM   6221 O  O   . TYR B 1 313 ? -12.954 -0.920  64.743  1.00 30.10  ? 313  TYR B O   1 
ATOM   6222 C  CB  . TYR B 1 313 ? -14.543 1.939   64.941  1.00 29.24  ? 313  TYR B CB  1 
ATOM   6223 C  CG  . TYR B 1 313 ? -15.578 0.972   65.461  1.00 30.56  ? 313  TYR B CG  1 
ATOM   6224 C  CD1 . TYR B 1 313 ? -15.988 1.012   66.795  1.00 29.99  ? 313  TYR B CD1 1 
ATOM   6225 C  CD2 . TYR B 1 313 ? -16.145 0.009   64.622  1.00 29.14  ? 313  TYR B CD2 1 
ATOM   6226 C  CE1 . TYR B 1 313 ? -16.918 0.119   67.279  1.00 30.83  ? 313  TYR B CE1 1 
ATOM   6227 C  CE2 . TYR B 1 313 ? -17.088 -0.895  65.099  1.00 30.68  ? 313  TYR B CE2 1 
ATOM   6228 C  CZ  . TYR B 1 313 ? -17.477 -0.826  66.428  1.00 31.21  ? 313  TYR B CZ  1 
ATOM   6229 O  OH  . TYR B 1 313 ? -18.402 -1.728  66.912  1.00 29.65  ? 313  TYR B OH  1 
ATOM   6230 N  N   . VAL B 1 314 ? -12.347 0.440   63.056  1.00 27.10  ? 314  VAL B N   1 
ATOM   6231 C  CA  . VAL B 1 314 ? -11.862 -0.690  62.265  1.00 28.66  ? 314  VAL B CA  1 
ATOM   6232 C  C   . VAL B 1 314 ? -10.742 -1.410  63.014  1.00 30.41  ? 314  VAL B C   1 
ATOM   6233 O  O   . VAL B 1 314 ? -10.713 -2.644  63.094  1.00 27.85  ? 314  VAL B O   1 
ATOM   6234 C  CB  . VAL B 1 314 ? -11.419 -0.211  60.869  1.00 29.24  ? 314  VAL B CB  1 
ATOM   6235 C  CG1 . VAL B 1 314 ? -10.804 -1.355  60.078  1.00 29.73  ? 314  VAL B CG1 1 
ATOM   6236 C  CG2 . VAL B 1 314 ? -12.621 0.366   60.089  1.00 28.15  ? 314  VAL B CG2 1 
ATOM   6237 N  N   . GLY B 1 315 ? -9.820  -0.652  63.607  1.00 30.39  ? 315  GLY B N   1 
ATOM   6238 C  CA  . GLY B 1 315 ? -8.774  -1.283  64.403  1.00 31.21  ? 315  GLY B CA  1 
ATOM   6239 C  C   . GLY B 1 315 ? -9.333  -2.047  65.591  1.00 30.56  ? 315  GLY B C   1 
ATOM   6240 O  O   . GLY B 1 315 ? -8.821  -3.103  65.964  1.00 29.50  ? 315  GLY B O   1 
ATOM   6241 N  N   . MET B 1 316 ? -10.401 -1.526  66.191  1.00 29.02  ? 316  MET B N   1 
ATOM   6242 C  CA  . MET B 1 316 ? -11.028 -2.182  67.330  1.00 28.71  ? 316  MET B CA  1 
ATOM   6243 C  C   . MET B 1 316 ? -11.671 -3.505  66.904  1.00 28.15  ? 316  MET B C   1 
ATOM   6244 O  O   . MET B 1 316 ? -11.595 -4.510  67.621  1.00 28.65  ? 316  MET B O   1 
ATOM   6245 C  CB  . MET B 1 316 ? -12.079 -1.218  67.900  1.00 31.16  ? 316  MET B CB  1 
ATOM   6246 C  CG  . MET B 1 316 ? -11.484 -0.182  68.863  1.00 32.13  ? 316  MET B CG  1 
ATOM   6247 S  SD  . MET B 1 316 ? -12.607 1.254   69.015  1.00 36.46  ? 316  MET B SD  1 
ATOM   6248 C  CE  . MET B 1 316 ? -13.999 0.502   69.801  1.00 37.36  ? 316  MET B CE  1 
ATOM   6249 N  N   . VAL B 1 317 ? -12.329 -3.512  65.741  1.00 27.75  ? 317  VAL B N   1 
ATOM   6250 C  CA  . VAL B 1 317 ? -12.859 -4.745  65.160  1.00 28.17  ? 317  VAL B CA  1 
ATOM   6251 C  C   . VAL B 1 317 ? -11.747 -5.783  65.013  1.00 28.73  ? 317  VAL B C   1 
ATOM   6252 O  O   . VAL B 1 317 ? -11.914 -6.964  65.352  1.00 28.66  ? 317  VAL B O   1 
ATOM   6253 C  CB  . VAL B 1 317 ? -13.513 -4.436  63.797  1.00 27.58  ? 317  VAL B CB  1 
ATOM   6254 C  CG1 . VAL B 1 317 ? -13.809 -5.719  63.025  1.00 27.82  ? 317  VAL B CG1 1 
ATOM   6255 C  CG2 . VAL B 1 317 ? -14.790 -3.600  63.961  1.00 29.05  ? 317  VAL B CG2 1 
ATOM   6256 N  N   . LEU B 1 318 ? -10.603 -5.368  64.458  1.00 27.52  ? 318  LEU B N   1 
ATOM   6257 C  CA  . LEU B 1 318 ? -9.516  -6.331  64.256  1.00 27.79  ? 318  LEU B CA  1 
ATOM   6258 C  C   . LEU B 1 318 ? -9.000  -6.873  65.588  1.00 28.83  ? 318  LEU B C   1 
ATOM   6259 O  O   . LEU B 1 318 ? -8.749  -8.077  65.725  1.00 28.72  ? 318  LEU B O   1 
ATOM   6260 C  CB  . LEU B 1 318 ? -8.387  -5.685  63.455  1.00 29.73  ? 318  LEU B CB  1 
ATOM   6261 C  CG  . LEU B 1 318 ? -8.770  -5.322  62.015  1.00 29.28  ? 318  LEU B CG  1 
ATOM   6262 C  CD1 . LEU B 1 318 ? -7.744  -4.388  61.385  1.00 31.50  ? 318  LEU B CD1 1 
ATOM   6263 C  CD2 . LEU B 1 318 ? -8.946  -6.581  61.167  1.00 29.76  ? 318  LEU B CD2 1 
ATOM   6264 N  N   . ASN B 1 319 ? -8.858  -6.010  66.588  1.00 27.54  ? 319  ASN B N   1 
ATOM   6265 C  CA  . ASN B 1 319 ? -8.394  -6.504  67.879  1.00 29.03  ? 319  ASN B CA  1 
ATOM   6266 C  C   . ASN B 1 319 ? -9.405  -7.456  68.502  1.00 27.25  ? 319  ASN B C   1 
ATOM   6267 O  O   . ASN B 1 319 ? -9.025  -8.450  69.133  1.00 28.06  ? 319  ASN B O   1 
ATOM   6268 C  CB  . ASN B 1 319 ? -8.085  -5.329  68.809  1.00 30.02  ? 319  ASN B CB  1 
ATOM   6269 C  CG  . ASN B 1 319 ? -6.691  -4.770  68.564  1.00 35.41  ? 319  ASN B CG  1 
ATOM   6270 O  OD1 . ASN B 1 319 ? -5.775  -5.514  68.218  1.00 35.13  ? 319  ASN B OD1 1 
ATOM   6271 N  ND2 . ASN B 1 319 ? -6.533  -3.465  68.717  1.00 39.06  ? 319  ASN B ND2 1 
ATOM   6272 N  N   . GLU B 1 320 ? -10.702 -7.174  68.351  1.00 27.67  ? 320  GLU B N   1 
ATOM   6273 C  CA  . GLU B 1 320 ? -11.702 -8.074  68.912  1.00 27.84  ? 320  GLU B CA  1 
ATOM   6274 C  C   . GLU B 1 320 ? -11.716 -9.410  68.172  1.00 29.69  ? 320  GLU B C   1 
ATOM   6275 O  O   . GLU B 1 320 ? -11.973 -10.457 68.778  1.00 28.18  ? 320  GLU B O   1 
ATOM   6276 C  CB  . GLU B 1 320 ? -13.083 -7.395  68.868  1.00 27.87  ? 320  GLU B CB  1 
ATOM   6277 C  CG  . GLU B 1 320 ? -14.262 -8.205  69.422  1.00 29.82  ? 320  GLU B CG  1 
ATOM   6278 C  CD  . GLU B 1 320 ? -14.230 -8.394  70.942  1.00 30.45  ? 320  GLU B CD  1 
ATOM   6279 O  OE1 . GLU B 1 320 ? -13.165 -8.178  71.577  1.00 28.43  ? 320  GLU B OE1 1 
ATOM   6280 O  OE2 . GLU B 1 320 ? -15.287 -8.757  71.523  1.00 29.72  ? 320  GLU B OE2 1 
ATOM   6281 N  N   . ALA B 1 321 ? -11.418 -9.394  66.874  1.00 28.21  ? 321  ALA B N   1 
ATOM   6282 C  CA  . ALA B 1 321 ? -11.245 -10.640 66.137  1.00 25.65  ? 321  ALA B CA  1 
ATOM   6283 C  C   . ALA B 1 321 ? -10.017 -11.400 66.623  1.00 25.66  ? 321  ALA B C   1 
ATOM   6284 O  O   . ALA B 1 321 ? -10.064 -12.630 66.771  1.00 27.85  ? 321  ALA B O   1 
ATOM   6285 C  CB  . ALA B 1 321 ? -11.146 -10.342 64.636  1.00 28.90  ? 321  ALA B CB  1 
ATOM   6286 N  N   . LEU B 1 322 ? -8.915  -10.681 66.896  1.00 27.63  ? 322  LEU B N   1 
ATOM   6287 C  CA  . LEU B 1 322 ? -7.743  -11.315 67.505  1.00 27.82  ? 322  LEU B CA  1 
ATOM   6288 C  C   . LEU B 1 322 ? -8.019  -11.800 68.928  1.00 26.25  ? 322  LEU B C   1 
ATOM   6289 O  O   . LEU B 1 322 ? -7.397  -12.772 69.385  1.00 29.53  ? 322  LEU B O   1 
ATOM   6290 C  CB  . LEU B 1 322 ? -6.563  -10.345 67.524  1.00 28.47  ? 322  LEU B CB  1 
ATOM   6291 C  CG  . LEU B 1 322 ? -5.909  -10.040 66.170  1.00 30.00  ? 322  LEU B CG  1 
ATOM   6292 C  CD1 . LEU B 1 322 ? -4.775  -9.052  66.391  1.00 31.00  ? 322  LEU B CD1 1 
ATOM   6293 C  CD2 . LEU B 1 322 ? -5.425  -11.332 65.484  1.00 28.01  ? 322  LEU B CD2 1 
ATOM   6294 N  N   . ARG B 1 323 ? -8.927  -11.141 69.657  1.00 26.48  ? 323  ARG B N   1 
ATOM   6295 C  CA  . ARG B 1 323 ? -9.265  -11.647 70.976  1.00 26.26  ? 323  ARG B CA  1 
ATOM   6296 C  C   . ARG B 1 323 ? -9.917  -13.017 70.863  1.00 28.16  ? 323  ARG B C   1 
ATOM   6297 O  O   . ARG B 1 323 ? -9.495  -13.971 71.515  1.00 29.36  ? 323  ARG B O   1 
ATOM   6298 C  CB  . ARG B 1 323 ? -10.178 -10.663 71.732  1.00 29.01  ? 323  ARG B CB  1 
ATOM   6299 C  CG  . ARG B 1 323 ? -10.410 -11.109 73.205  1.00 29.08  ? 323  ARG B CG  1 
ATOM   6300 C  CD  . ARG B 1 323 ? -11.390 -10.202 73.968  1.00 29.25  ? 323  ARG B CD  1 
ATOM   6301 N  NE  . ARG B 1 323 ? -12.738 -10.268 73.410  1.00 28.94  ? 323  ARG B NE  1 
ATOM   6302 C  CZ  . ARG B 1 323 ? -13.609 -11.248 73.621  1.00 31.93  ? 323  ARG B CZ  1 
ATOM   6303 N  NH1 . ARG B 1 323 ? -13.332 -12.271 74.421  1.00 29.45  ? 323  ARG B NH1 1 
ATOM   6304 N  NH2 . ARG B 1 323 ? -14.798 -11.197 73.024  1.00 29.66  ? 323  ARG B NH2 1 
ATOM   6305 N  N   . LEU B 1 324 ? -10.952 -13.138 70.030  1.00 29.94  ? 324  LEU B N   1 
ATOM   6306 C  CA  . LEU B 1 324 ? -11.682 -14.399 70.011  1.00 27.16  ? 324  LEU B CA  1 
ATOM   6307 C  C   . LEU B 1 324 ? -10.897 -15.490 69.299  1.00 27.55  ? 324  LEU B C   1 
ATOM   6308 O  O   . LEU B 1 324 ? -10.871 -16.635 69.761  1.00 28.49  ? 324  LEU B O   1 
ATOM   6309 C  CB  . LEU B 1 324 ? -13.067 -14.197 69.384  1.00 27.81  ? 324  LEU B CB  1 
ATOM   6310 C  CG  . LEU B 1 324 ? -14.054 -13.567 70.384  1.00 29.61  ? 324  LEU B CG  1 
ATOM   6311 C  CD1 . LEU B 1 324 ? -15.277 -13.034 69.658  1.00 33.12  ? 324  LEU B CD1 1 
ATOM   6312 C  CD2 . LEU B 1 324 ? -14.465 -14.583 71.484  1.00 32.13  ? 324  LEU B CD2 1 
ATOM   6313 N  N   . TRP B 1 325 ? -10.222 -15.167 68.195  1.00 27.34  ? 325  TRP B N   1 
ATOM   6314 C  CA  . TRP B 1 325 ? -9.554  -16.192 67.387  1.00 26.66  ? 325  TRP B CA  1 
ATOM   6315 C  C   . TRP B 1 325 ? -8.159  -15.727 66.995  1.00 24.96  ? 325  TRP B C   1 
ATOM   6316 O  O   . TRP B 1 325 ? -7.859  -15.519 65.816  1.00 28.53  ? 325  TRP B O   1 
ATOM   6317 C  CB  . TRP B 1 325 ? -10.406 -16.565 66.163  1.00 29.48  ? 325  TRP B CB  1 
ATOM   6318 C  CG  . TRP B 1 325 ? -11.606 -17.350 66.632  1.00 27.82  ? 325  TRP B CG  1 
ATOM   6319 C  CD1 . TRP B 1 325 ? -12.910 -16.949 66.630  1.00 30.80  ? 325  TRP B CD1 1 
ATOM   6320 C  CD2 . TRP B 1 325 ? -11.584 -18.649 67.253  1.00 27.92  ? 325  TRP B CD2 1 
ATOM   6321 N  NE1 . TRP B 1 325 ? -13.704 -17.928 67.203  1.00 29.45  ? 325  TRP B NE1 1 
ATOM   6322 C  CE2 . TRP B 1 325 ? -12.910 -18.977 67.593  1.00 33.02  ? 325  TRP B CE2 1 
ATOM   6323 C  CE3 . TRP B 1 325 ? -10.566 -19.554 67.566  1.00 29.64  ? 325  TRP B CE3 1 
ATOM   6324 C  CZ2 . TRP B 1 325 ? -13.245 -20.183 68.201  1.00 33.29  ? 325  TRP B CZ2 1 
ATOM   6325 C  CZ3 . TRP B 1 325 ? -10.901 -20.752 68.177  1.00 32.95  ? 325  TRP B CZ3 1 
ATOM   6326 C  CH2 . TRP B 1 325 ? -12.230 -21.058 68.484  1.00 31.79  ? 325  TRP B CH2 1 
ATOM   6327 N  N   . PRO B 1 326 ? -7.258  -15.613 67.966  1.00 28.95  ? 326  PRO B N   1 
ATOM   6328 C  CA  . PRO B 1 326 ? -5.867  -15.269 67.633  1.00 26.72  ? 326  PRO B CA  1 
ATOM   6329 C  C   . PRO B 1 326 ? -5.298  -16.316 66.687  1.00 29.21  ? 326  PRO B C   1 
ATOM   6330 O  O   . PRO B 1 326 ? -5.326  -17.510 66.982  1.00 28.76  ? 326  PRO B O   1 
ATOM   6331 C  CB  . PRO B 1 326 ? -5.168  -15.283 68.997  1.00 30.19  ? 326  PRO B CB  1 
ATOM   6332 C  CG  . PRO B 1 326 ? -5.998  -16.247 69.837  1.00 28.18  ? 326  PRO B CG  1 
ATOM   6333 C  CD  . PRO B 1 326 ? -7.415  -15.969 69.391  1.00 30.35  ? 326  PRO B CD  1 
ATOM   6334 N  N   . THR B 1 327 ? -4.783  -15.867 65.533  1.00 25.99  ? 327  THR B N   1 
ATOM   6335 C  CA  . THR B 1 327 ? -4.570  -16.809 64.435  1.00 28.51  ? 327  THR B CA  1 
ATOM   6336 C  C   . THR B 1 327 ? -3.260  -17.579 64.554  1.00 28.77  ? 327  THR B C   1 
ATOM   6337 O  O   . THR B 1 327 ? -3.079  -18.583 63.856  1.00 29.73  ? 327  THR B O   1 
ATOM   6338 C  CB  . THR B 1 327 ? -4.637  -16.080 63.092  1.00 28.51  ? 327  THR B CB  1 
ATOM   6339 O  OG1 . THR B 1 327 ? -3.820  -14.906 63.160  1.00 29.76  ? 327  THR B OG1 1 
ATOM   6340 C  CG2 . THR B 1 327 ? -6.097  -15.624 62.818  1.00 28.26  ? 327  THR B CG2 1 
ATOM   6341 N  N   . ALA B 1 328 ? -2.354  -17.145 65.432  1.00 28.11  ? 328  ALA B N   1 
ATOM   6342 C  CA  . ALA B 1 328 ? -1.241  -17.979 65.881  1.00 27.83  ? 328  ALA B CA  1 
ATOM   6343 C  C   . ALA B 1 328 ? -1.549  -18.334 67.329  1.00 28.72  ? 328  ALA B C   1 
ATOM   6344 O  O   . ALA B 1 328 ? -1.191  -17.586 68.249  1.00 31.13  ? 328  ALA B O   1 
ATOM   6345 C  CB  . ALA B 1 328 ? 0.095   -17.238 65.755  1.00 29.83  ? 328  ALA B CB  1 
ATOM   6346 N  N   . PRO B 1 329 ? -2.269  -19.429 67.586  1.00 27.74  ? 329  PRO B N   1 
ATOM   6347 C  CA  . PRO B 1 329 ? -3.077  -19.513 68.815  1.00 29.47  ? 329  PRO B CA  1 
ATOM   6348 C  C   . PRO B 1 329 ? -2.341  -19.953 70.068  1.00 29.17  ? 329  PRO B C   1 
ATOM   6349 O  O   . PRO B 1 329 ? -2.962  -20.036 71.139  1.00 28.44  ? 329  PRO B O   1 
ATOM   6350 C  CB  . PRO B 1 329 ? -4.151  -20.541 68.438  1.00 30.89  ? 329  PRO B CB  1 
ATOM   6351 C  CG  . PRO B 1 329 ? -3.494  -21.405 67.408  1.00 30.98  ? 329  PRO B CG  1 
ATOM   6352 C  CD  . PRO B 1 329 ? -2.651  -20.453 66.591  1.00 29.51  ? 329  PRO B CD  1 
ATOM   6353 N  N   . ALA B 1 330 ? -1.044  -20.215 70.009  1.00 27.13  ? 330  ALA B N   1 
ATOM   6354 C  CA  . ALA B 1 330 ? -0.356  -20.595 71.231  1.00 27.50  ? 330  ALA B CA  1 
ATOM   6355 C  C   . ALA B 1 330 ? 1.091   -20.196 71.078  1.00 29.23  ? 330  ALA B C   1 
ATOM   6356 O  O   . ALA B 1 330 ? 1.582   -20.010 69.962  1.00 30.29  ? 330  ALA B O   1 
ATOM   6357 C  CB  . ALA B 1 330 ? -0.455  -22.102 71.507  1.00 29.77  ? 330  ALA B CB  1 
ATOM   6358 N  N   . PHE B 1 331 ? 1.767   -20.069 72.213  1.00 28.13  ? 331  PHE B N   1 
ATOM   6359 C  CA  . PHE B 1 331 ? 3.225   -20.001 72.227  1.00 28.05  ? 331  PHE B CA  1 
ATOM   6360 C  C   . PHE B 1 331 ? 3.716   -20.755 73.453  1.00 31.08  ? 331  PHE B C   1 
ATOM   6361 O  O   . PHE B 1 331 ? 2.958   -21.043 74.382  1.00 31.14  ? 331  PHE B O   1 
ATOM   6362 C  CB  . PHE B 1 331 ? 3.781   -18.555 72.179  1.00 28.56  ? 331  PHE B CB  1 
ATOM   6363 C  CG  . PHE B 1 331 ? 3.262   -17.610 73.252  1.00 29.72  ? 331  PHE B CG  1 
ATOM   6364 C  CD1 . PHE B 1 331 ? 2.070   -16.924 73.080  1.00 28.91  ? 331  PHE B CD1 1 
ATOM   6365 C  CD2 . PHE B 1 331 ? 4.028   -17.334 74.376  1.00 31.04  ? 331  PHE B CD2 1 
ATOM   6366 C  CE1 . PHE B 1 331 ? 1.608   -16.041 74.049  1.00 30.21  ? 331  PHE B CE1 1 
ATOM   6367 C  CE2 . PHE B 1 331 ? 3.586   -16.449 75.351  1.00 34.58  ? 331  PHE B CE2 1 
ATOM   6368 C  CZ  . PHE B 1 331 ? 2.367   -15.800 75.189  1.00 32.01  ? 331  PHE B CZ  1 
ATOM   6369 N  N   . SER B 1 332 ? 4.999   -21.103 73.426  1.00 29.35  ? 332  SER B N   1 
ATOM   6370 C  CA  . SER B 1 332 ? 5.599   -21.987 74.412  1.00 29.43  ? 332  SER B CA  1 
ATOM   6371 C  C   . SER B 1 332 ? 6.726   -21.269 75.147  1.00 31.20  ? 332  SER B C   1 
ATOM   6372 O  O   . SER B 1 332 ? 7.424   -20.430 74.573  1.00 29.56  ? 332  SER B O   1 
ATOM   6373 C  CB  . SER B 1 332 ? 6.133   -23.264 73.726  1.00 28.60  ? 332  SER B CB  1 
ATOM   6374 O  OG  . SER B 1 332 ? 6.493   -24.226 74.697  1.00 31.19  ? 332  SER B OG  1 
ATOM   6375 N  N   . LEU B 1 333 ? 6.910   -21.635 76.420  1.00 30.21  ? 333  LEU B N   1 
ATOM   6376 C  CA  . LEU B 1 333 ? 7.948   -21.079 77.279  1.00 29.83  ? 333  LEU B CA  1 
ATOM   6377 C  C   . LEU B 1 333 ? 8.635   -22.204 78.042  1.00 28.88  ? 333  LEU B C   1 
ATOM   6378 O  O   . LEU B 1 333 ? 8.069   -23.279 78.236  1.00 31.46  ? 333  LEU B O   1 
ATOM   6379 C  CB  . LEU B 1 333 ? 7.342   -20.075 78.268  1.00 32.10  ? 333  LEU B CB  1 
ATOM   6380 C  CG  . LEU B 1 333 ? 6.572   -18.970 77.535  1.00 31.58  ? 333  LEU B CG  1 
ATOM   6381 C  CD1 . LEU B 1 333 ? 5.468   -18.387 78.399  1.00 36.54  ? 333  LEU B CD1 1 
ATOM   6382 C  CD2 . LEU B 1 333 ? 7.525   -17.887 77.061  1.00 30.70  ? 333  LEU B CD2 1 
ATOM   6383 N  N   . TYR B 1 334 ? 9.871   -21.950 78.493  1.00 30.50  ? 334  TYR B N   1 
ATOM   6384 C  CA  . TYR B 1 334 ? 10.510  -22.843 79.448  1.00 32.22  ? 334  TYR B CA  1 
ATOM   6385 C  C   . TYR B 1 334 ? 11.002  -22.030 80.636  1.00 30.10  ? 334  TYR B C   1 
ATOM   6386 O  O   . TYR B 1 334 ? 11.322  -20.843 80.513  1.00 29.46  ? 334  TYR B O   1 
ATOM   6387 C  CB  . TYR B 1 334 ? 11.685  -23.644 78.819  1.00 31.80  ? 334  TYR B CB  1 
ATOM   6388 C  CG  . TYR B 1 334 ? 12.859  -22.781 78.478  1.00 32.17  ? 334  TYR B CG  1 
ATOM   6389 C  CD1 . TYR B 1 334 ? 12.940  -22.154 77.243  1.00 31.53  ? 334  TYR B CD1 1 
ATOM   6390 C  CD2 . TYR B 1 334 ? 13.902  -22.600 79.384  1.00 34.12  ? 334  TYR B CD2 1 
ATOM   6391 C  CE1 . TYR B 1 334 ? 14.019  -21.341 76.912  1.00 32.56  ? 334  TYR B CE1 1 
ATOM   6392 C  CE2 . TYR B 1 334 ? 14.977  -21.796 79.069  1.00 35.33  ? 334  TYR B CE2 1 
ATOM   6393 C  CZ  . TYR B 1 334 ? 15.037  -21.173 77.833  1.00 35.19  ? 334  TYR B CZ  1 
ATOM   6394 O  OH  . TYR B 1 334 ? 16.110  -20.370 77.523  1.00 39.22  ? 334  TYR B OH  1 
ATOM   6395 N  N   . ALA B 1 335 ? 11.012  -22.674 81.797  1.00 30.83  ? 335  ALA B N   1 
ATOM   6396 C  CA  . ALA B 1 335 ? 11.478  -22.035 83.023  1.00 31.42  ? 335  ALA B CA  1 
ATOM   6397 C  C   . ALA B 1 335 ? 12.995  -21.909 82.999  1.00 32.01  ? 335  ALA B C   1 
ATOM   6398 O  O   . ALA B 1 335 ? 13.706  -22.909 82.850  1.00 34.29  ? 335  ALA B O   1 
ATOM   6399 C  CB  . ALA B 1 335 ? 11.036  -22.851 84.235  1.00 33.24  ? 335  ALA B CB  1 
ATOM   6400 N  N   . LYS B 1 336 ? 13.492  -20.682 83.143  1.00 32.40  ? 336  LYS B N   1 
ATOM   6401 C  CA  . LYS B 1 336 ? 14.939  -20.482 83.133  1.00 32.87  ? 336  LYS B CA  1 
ATOM   6402 C  C   . LYS B 1 336 ? 15.604  -21.077 84.373  1.00 38.26  ? 336  LYS B C   1 
ATOM   6403 O  O   . LYS B 1 336 ? 16.744  -21.564 84.304  1.00 37.00  ? 336  LYS B O   1 
ATOM   6404 C  CB  . LYS B 1 336 ? 15.245  -18.990 83.038  1.00 32.84  ? 336  LYS B CB  1 
ATOM   6405 C  CG  . LYS B 1 336 ? 14.950  -18.382 81.663  1.00 36.42  ? 336  LYS B CG  1 
ATOM   6406 C  CD  . LYS B 1 336 ? 14.686  -16.878 81.764  1.00 35.64  ? 336  LYS B CD  1 
ATOM   6407 C  CE  . LYS B 1 336 ? 15.952  -16.109 82.177  1.00 40.32  ? 336  LYS B CE  1 
ATOM   6408 N  NZ  . LYS B 1 336 ? 17.056  -16.281 81.185  1.00 42.64  ? 336  LYS B NZ  1 
ATOM   6409 N  N   . GLU B 1 337 ? 14.923  -21.024 85.508  1.00 35.12  ? 337  GLU B N   1 
ATOM   6410 C  CA  . GLU B 1 337 ? 15.405  -21.602 86.756  1.00 38.76  ? 337  GLU B CA  1 
ATOM   6411 C  C   . GLU B 1 337 ? 14.215  -22.232 87.461  1.00 38.34  ? 337  GLU B C   1 
ATOM   6412 O  O   . GLU B 1 337 ? 13.064  -21.997 87.091  1.00 38.10  ? 337  GLU B O   1 
ATOM   6413 C  CB  . GLU B 1 337 ? 16.063  -20.542 87.656  1.00 38.94  ? 337  GLU B CB  1 
ATOM   6414 C  CG  . GLU B 1 337 ? 17.246  -19.788 87.027  1.00 42.02  ? 337  GLU B CG  1 
ATOM   6415 C  CD  . GLU B 1 337 ? 18.485  -20.657 86.774  1.00 44.74  ? 337  GLU B CD  1 
ATOM   6416 O  OE1 . GLU B 1 337 ? 18.594  -21.760 87.350  1.00 41.59  ? 337  GLU B OE1 1 
ATOM   6417 O  OE2 . GLU B 1 337 ? 19.349  -20.229 85.977  1.00 45.24  ? 337  GLU B OE2 1 
ATOM   6418 N  N   . ASP B 1 338 ? 14.484  -23.048 88.485  1.00 37.80  ? 338  ASP B N   1 
ATOM   6419 C  CA  . ASP B 1 338 ? 13.393  -23.493 89.348  1.00 36.77  ? 338  ASP B CA  1 
ATOM   6420 C  C   . ASP B 1 338 ? 12.597  -22.283 89.810  1.00 38.12  ? 338  ASP B C   1 
ATOM   6421 O  O   . ASP B 1 338 ? 13.163  -21.246 90.164  1.00 40.10  ? 338  ASP B O   1 
ATOM   6422 C  CB  . ASP B 1 338 ? 13.897  -24.233 90.593  1.00 39.62  ? 338  ASP B CB  1 
ATOM   6423 C  CG  . ASP B 1 338 ? 14.713  -25.469 90.291  1.00 41.04  ? 338  ASP B CG  1 
ATOM   6424 O  OD1 . ASP B 1 338 ? 14.735  -25.981 89.150  1.00 41.01  ? 338  ASP B OD1 1 
ATOM   6425 O  OD2 . ASP B 1 338 ? 15.362  -25.935 91.256  1.00 47.09  ? 338  ASP B OD2 1 
ATOM   6426 N  N   . THR B 1 339 ? 11.274  -22.424 89.830  1.00 36.48  ? 339  THR B N   1 
ATOM   6427 C  CA  . THR B 1 339 ? 10.416  -21.322 90.235  1.00 38.74  ? 339  THR B CA  1 
ATOM   6428 C  C   . THR B 1 339 ? 9.042   -21.899 90.547  1.00 40.07  ? 339  THR B C   1 
ATOM   6429 O  O   . THR B 1 339 ? 8.704   -22.997 90.100  1.00 42.04  ? 339  THR B O   1 
ATOM   6430 C  CB  . THR B 1 339 ? 10.351  -20.245 89.142  1.00 40.91  ? 339  THR B CB  1 
ATOM   6431 O  OG1 . THR B 1 339 ? 9.737   -19.060 89.650  1.00 40.67  ? 339  THR B OG1 1 
ATOM   6432 C  CG2 . THR B 1 339 ? 9.565   -20.748 87.918  1.00 37.34  ? 339  THR B CG2 1 
ATOM   6433 N  N   . VAL B 1 340 ? 8.246   -21.152 91.309  1.00 38.56  ? 340  VAL B N   1 
ATOM   6434 C  CA  . VAL B 1 340 ? 6.895   -21.585 91.665  1.00 37.31  ? 340  VAL B CA  1 
ATOM   6435 C  C   . VAL B 1 340 ? 5.912   -20.711 90.905  1.00 36.48  ? 340  VAL B C   1 
ATOM   6436 O  O   . VAL B 1 340 ? 5.914   -19.481 91.055  1.00 41.41  ? 340  VAL B O   1 
ATOM   6437 C  CB  . VAL B 1 340 ? 6.633   -21.506 93.177  1.00 41.44  ? 340  VAL B CB  1 
ATOM   6438 C  CG1 . VAL B 1 340 ? 5.199   -21.943 93.474  1.00 40.30  ? 340  VAL B CG1 1 
ATOM   6439 C  CG2 . VAL B 1 340 ? 7.625   -22.366 93.932  1.00 42.99  ? 340  VAL B CG2 1 
ATOM   6440 N  N   . LEU B 1 341 ? 5.071   -21.345 90.091  1.00 38.25  ? 341  LEU B N   1 
ATOM   6441 C  CA  . LEU B 1 341 ? 4.078   -20.627 89.311  1.00 37.53  ? 341  LEU B CA  1 
ATOM   6442 C  C   . LEU B 1 341 ? 2.828   -20.392 90.149  1.00 40.00  ? 341  LEU B C   1 
ATOM   6443 O  O   . LEU B 1 341 ? 2.236   -21.344 90.666  1.00 36.64  ? 341  LEU B O   1 
ATOM   6444 C  CB  . LEU B 1 341 ? 3.737   -21.427 88.059  1.00 35.10  ? 341  LEU B CB  1 
ATOM   6445 C  CG  . LEU B 1 341 ? 2.836   -20.748 87.048  1.00 37.36  ? 341  LEU B CG  1 
ATOM   6446 C  CD1 . LEU B 1 341 ? 3.584   -19.572 86.420  1.00 36.80  ? 341  LEU B CD1 1 
ATOM   6447 C  CD2 . LEU B 1 341 ? 2.440   -21.796 86.007  1.00 38.80  ? 341  LEU B CD2 1 
ATOM   6448 N  N   . GLY B 1 342 ? 2.422   -19.131 90.273  1.00 36.57  ? 342  GLY B N   1 
ATOM   6449 C  CA  . GLY B 1 342 ? 1.152   -18.813 90.903  1.00 40.12  ? 342  GLY B CA  1 
ATOM   6450 C  C   . GLY B 1 342 ? 1.065   -19.165 92.367  1.00 41.25  ? 342  GLY B C   1 
ATOM   6451 O  O   . GLY B 1 342 ? -0.039  -19.365 92.883  1.00 41.35  ? 342  GLY B O   1 
ATOM   6452 N  N   . GLY B 1 343 ? 2.203   -19.253 93.052  1.00 40.83  ? 343  GLY B N   1 
ATOM   6453 C  CA  . GLY B 1 343 ? 2.218   -19.653 94.444  1.00 41.37  ? 343  GLY B CA  1 
ATOM   6454 C  C   . GLY B 1 343 ? 1.786   -21.075 94.703  1.00 44.98  ? 343  GLY B C   1 
ATOM   6455 O  O   . GLY B 1 343 ? 1.658   -21.465 95.870  1.00 47.99  ? 343  GLY B O   1 
ATOM   6456 N  N   . GLU B 1 344 ? 1.572   -21.875 93.655  1.00 40.61  ? 344  GLU B N   1 
ATOM   6457 C  CA  . GLU B 1 344 ? 0.947   -23.184 93.816  1.00 42.82  ? 344  GLU B CA  1 
ATOM   6458 C  C   . GLU B 1 344 ? 1.578   -24.302 93.004  1.00 43.70  ? 344  GLU B C   1 
ATOM   6459 O  O   . GLU B 1 344 ? 1.388   -25.466 93.369  1.00 42.75  ? 344  GLU B O   1 
ATOM   6460 C  CB  . GLU B 1 344 ? -0.543  -23.097 93.457  1.00 44.72  ? 344  GLU B CB  1 
ATOM   6461 C  CG  . GLU B 1 344 ? -1.321  -22.114 94.326  1.00 50.32  ? 344  GLU B CG  1 
ATOM   6462 C  CD  . GLU B 1 344 ? -2.757  -21.912 93.874  1.00 56.25  ? 344  GLU B CD  1 
ATOM   6463 O  OE1 . GLU B 1 344 ? -3.025  -22.007 92.662  1.00 50.45  ? 344  GLU B OE1 1 
ATOM   6464 O  OE2 . GLU B 1 344 ? -3.623  -21.657 94.736  1.00 61.45  ? 344  GLU B OE2 1 
ATOM   6465 N  N   . TYR B 1 345 ? 2.298   -24.018 91.919  1.00 39.37  ? 345  TYR B N   1 
ATOM   6466 C  CA  . TYR B 1 345 ? 2.774   -25.050 91.000  1.00 38.66  ? 345  TYR B CA  1 
ATOM   6467 C  C   . TYR B 1 345 ? 4.285   -24.975 90.859  1.00 39.37  ? 345  TYR B C   1 
ATOM   6468 O  O   . TYR B 1 345 ? 4.797   -24.168 90.067  1.00 39.48  ? 345  TYR B O   1 
ATOM   6469 C  CB  . TYR B 1 345 ? 2.102   -24.888 89.639  1.00 36.95  ? 345  TYR B CB  1 
ATOM   6470 C  CG  . TYR B 1 345 ? 0.607   -25.001 89.757  1.00 36.25  ? 345  TYR B CG  1 
ATOM   6471 C  CD1 . TYR B 1 345 ? 0.018   -26.235 89.965  1.00 40.72  ? 345  TYR B CD1 1 
ATOM   6472 C  CD2 . TYR B 1 345 ? -0.206  -23.883 89.690  1.00 35.89  ? 345  TYR B CD2 1 
ATOM   6473 C  CE1 . TYR B 1 345 ? -1.341  -26.365 90.086  1.00 41.23  ? 345  TYR B CE1 1 
ATOM   6474 C  CE2 . TYR B 1 345 ? -1.583  -23.998 89.821  1.00 40.71  ? 345  TYR B CE2 1 
ATOM   6475 C  CZ  . TYR B 1 345 ? -2.139  -25.248 90.020  1.00 41.34  ? 345  TYR B CZ  1 
ATOM   6476 O  OH  . TYR B 1 345 ? -3.503  -25.393 90.150  1.00 42.74  ? 345  TYR B OH  1 
ATOM   6477 N  N   . PRO B 1 346 ? 5.034   -25.779 91.604  1.00 40.13  ? 346  PRO B N   1 
ATOM   6478 C  CA  . PRO B 1 346 ? 6.493   -25.745 91.475  1.00 37.49  ? 346  PRO B CA  1 
ATOM   6479 C  C   . PRO B 1 346 ? 6.939   -26.258 90.118  1.00 35.58  ? 346  PRO B C   1 
ATOM   6480 O  O   . PRO B 1 346 ? 6.457   -27.281 89.623  1.00 38.13  ? 346  PRO B O   1 
ATOM   6481 C  CB  . PRO B 1 346 ? 6.980   -26.655 92.615  1.00 44.79  ? 346  PRO B CB  1 
ATOM   6482 C  CG  . PRO B 1 346 ? 5.805   -26.783 93.544  1.00 42.21  ? 346  PRO B CG  1 
ATOM   6483 C  CD  . PRO B 1 346 ? 4.592   -26.700 92.664  1.00 41.50  ? 346  PRO B CD  1 
ATOM   6484 N  N   . LEU B 1 347 ? 7.873   -25.528 89.516  1.00 36.43  ? 347  LEU B N   1 
ATOM   6485 C  CA  . LEU B 1 347 ? 8.478   -25.915 88.255  1.00 37.96  ? 347  LEU B CA  1 
ATOM   6486 C  C   . LEU B 1 347 ? 9.986   -26.011 88.433  1.00 37.48  ? 347  LEU B C   1 
ATOM   6487 O  O   . LEU B 1 347 ? 10.590  -25.242 89.189  1.00 36.72  ? 347  LEU B O   1 
ATOM   6488 C  CB  . LEU B 1 347 ? 8.156   -24.902 87.142  1.00 37.21  ? 347  LEU B CB  1 
ATOM   6489 C  CG  . LEU B 1 347 ? 6.682   -24.615 86.861  1.00 36.31  ? 347  LEU B CG  1 
ATOM   6490 C  CD1 . LEU B 1 347 ? 6.604   -23.464 85.864  1.00 34.60  ? 347  LEU B CD1 1 
ATOM   6491 C  CD2 . LEU B 1 347 ? 5.953   -25.847 86.308  1.00 36.47  ? 347  LEU B CD2 1 
ATOM   6492 N  N   . GLU B 1 348 ? 10.580  -26.950 87.722  1.00 37.41  ? 348  GLU B N   1 
ATOM   6493 C  CA  . GLU B 1 348 ? 12.028  -27.072 87.687  1.00 36.23  ? 348  GLU B CA  1 
ATOM   6494 C  C   . GLU B 1 348 ? 12.570  -26.420 86.426  1.00 35.52  ? 348  GLU B C   1 
ATOM   6495 O  O   . GLU B 1 348 ? 11.888  -26.338 85.397  1.00 35.31  ? 348  GLU B O   1 
ATOM   6496 C  CB  . GLU B 1 348 ? 12.473  -28.533 87.752  1.00 39.85  ? 348  GLU B CB  1 
ATOM   6497 C  CG  . GLU B 1 348 ? 12.110  -29.193 89.077  1.00 48.99  ? 348  GLU B CG  1 
ATOM   6498 C  CD  . GLU B 1 348 ? 12.252  -30.698 89.061  1.00 52.29  ? 348  GLU B CD  1 
ATOM   6499 O  OE1 . GLU B 1 348 ? 12.110  -31.309 90.141  1.00 61.87  ? 348  GLU B OE1 1 
ATOM   6500 O  OE2 . GLU B 1 348 ? 12.525  -31.271 87.989  1.00 58.82  ? 348  GLU B OE2 1 
ATOM   6501 N  N   . LYS B 1 349 ? 13.803  -25.939 86.529  1.00 36.11  ? 349  LYS B N   1 
ATOM   6502 C  CA  . LYS B 1 349 ? 14.508  -25.395 85.384  1.00 34.08  ? 349  LYS B CA  1 
ATOM   6503 C  C   . LYS B 1 349 ? 14.305  -26.296 84.179  1.00 36.08  ? 349  LYS B C   1 
ATOM   6504 O  O   . LYS B 1 349 ? 14.487  -27.517 84.262  1.00 35.69  ? 349  LYS B O   1 
ATOM   6505 C  CB  . LYS B 1 349 ? 16.001  -25.267 85.717  1.00 38.49  ? 349  LYS B CB  1 
ATOM   6506 C  CG  . LYS B 1 349 ? 16.885  -24.926 84.541  1.00 37.20  ? 349  LYS B CG  1 
ATOM   6507 C  CD  . LYS B 1 349 ? 18.340  -24.832 84.979  1.00 44.00  ? 349  LYS B CD  1 
ATOM   6508 C  CE  . LYS B 1 349 ? 19.218  -24.394 83.829  1.00 46.68  ? 349  LYS B CE  1 
ATOM   6509 N  NZ  . LYS B 1 349 ? 20.659  -24.453 84.223  1.00 50.31  ? 349  LYS B NZ  1 
ATOM   6510 N  N   . GLY B 1 350 ? 13.894  -25.692 83.057  1.00 32.08  ? 350  GLY B N   1 
ATOM   6511 C  CA  . GLY B 1 350 ? 13.674  -26.428 81.840  1.00 31.99  ? 350  GLY B CA  1 
ATOM   6512 C  C   . GLY B 1 350 ? 12.246  -26.880 81.612  1.00 34.35  ? 350  GLY B C   1 
ATOM   6513 O  O   . GLY B 1 350 ? 11.920  -27.277 80.490  1.00 35.24  ? 350  GLY B O   1 
ATOM   6514 N  N   . ASP B 1 351 ? 11.397  -26.838 82.641  1.00 31.31  ? 351  ASP B N   1 
ATOM   6515 C  CA  . ASP B 1 351 ? 10.005  -27.240 82.476  1.00 33.02  ? 351  ASP B CA  1 
ATOM   6516 C  C   . ASP B 1 351 ? 9.309   -26.296 81.503  1.00 35.07  ? 351  ASP B C   1 
ATOM   6517 O  O   . ASP B 1 351 ? 9.537   -25.082 81.520  1.00 33.15  ? 351  ASP B O   1 
ATOM   6518 C  CB  . ASP B 1 351 ? 9.276   -27.208 83.821  1.00 34.74  ? 351  ASP B CB  1 
ATOM   6519 C  CG  . ASP B 1 351 ? 9.555   -28.425 84.697  1.00 34.11  ? 351  ASP B CG  1 
ATOM   6520 O  OD1 . ASP B 1 351 ? 10.192  -29.407 84.244  1.00 35.31  ? 351  ASP B OD1 1 
ATOM   6521 O  OD2 . ASP B 1 351 ? 9.114   -28.386 85.866  1.00 38.14  ? 351  ASP B OD2 1 
ATOM   6522 N  N   . GLU B 1 352 ? 8.433   -26.866 80.679  1.00 32.89  ? 352  GLU B N   1 
ATOM   6523 C  CA  . GLU B 1 352 ? 7.789   -26.205 79.561  1.00 34.22  ? 352  GLU B CA  1 
ATOM   6524 C  C   . GLU B 1 352 ? 6.365   -25.783 79.923  1.00 33.92  ? 352  GLU B C   1 
ATOM   6525 O  O   . GLU B 1 352 ? 5.686   -26.437 80.719  1.00 34.45  ? 352  GLU B O   1 
ATOM   6526 C  CB  . GLU B 1 352 ? 7.766   -27.179 78.384  1.00 33.12  ? 352  GLU B CB  1 
ATOM   6527 C  CG  . GLU B 1 352 ? 9.148   -27.468 77.850  1.00 39.76  ? 352  GLU B CG  1 
ATOM   6528 C  CD  . GLU B 1 352 ? 9.126   -28.287 76.582  1.00 46.51  ? 352  GLU B CD  1 
ATOM   6529 O  OE1 . GLU B 1 352 ? 8.019   -28.555 76.065  1.00 45.11  ? 352  GLU B OE1 1 
ATOM   6530 O  OE2 . GLU B 1 352 ? 10.220  -28.703 76.136  1.00 56.58  ? 352  GLU B OE2 1 
ATOM   6531 N  N   . LEU B 1 353 ? 5.926   -24.675 79.332  1.00 33.10  ? 353  LEU B N   1 
ATOM   6532 C  CA  . LEU B 1 353 ? 4.559   -24.191 79.416  1.00 31.98  ? 353  LEU B CA  1 
ATOM   6533 C  C   . LEU B 1 353 ? 4.034   -23.912 78.019  1.00 34.24  ? 353  LEU B C   1 
ATOM   6534 O  O   . LEU B 1 353 ? 4.783   -23.526 77.114  1.00 30.84  ? 353  LEU B O   1 
ATOM   6535 C  CB  . LEU B 1 353 ? 4.454   -22.894 80.219  1.00 30.91  ? 353  LEU B CB  1 
ATOM   6536 C  CG  . LEU B 1 353 ? 5.070   -22.861 81.611  1.00 31.43  ? 353  LEU B CG  1 
ATOM   6537 C  CD1 . LEU B 1 353 ? 5.100   -21.441 82.101  1.00 30.58  ? 353  LEU B CD1 1 
ATOM   6538 C  CD2 . LEU B 1 353 ? 4.243   -23.729 82.542  1.00 34.01  ? 353  LEU B CD2 1 
ATOM   6539 N  N   . MET B 1 354 ? 2.724   -24.062 77.868  1.00 30.48  ? 354  MET B N   1 
ATOM   6540 C  CA  . MET B 1 354 ? 2.024   -23.774 76.624  1.00 31.67  ? 354  MET B CA  1 
ATOM   6541 C  C   . MET B 1 354 ? 0.995   -22.710 76.972  1.00 29.15  ? 354  MET B C   1 
ATOM   6542 O  O   . MET B 1 354 ? 0.174   -22.924 77.873  1.00 32.95  ? 354  MET B O   1 
ATOM   6543 C  CB  . MET B 1 354 ? 1.325   -25.043 76.138  1.00 32.48  ? 354  MET B CB  1 
ATOM   6544 C  CG  . MET B 1 354 ? 2.009   -25.970 75.147  1.00 33.69  ? 354  MET B CG  1 
ATOM   6545 S  SD  . MET B 1 354 ? 3.324   -25.410 74.045  1.00 34.58  ? 354  MET B SD  1 
ATOM   6546 C  CE  . MET B 1 354 ? 2.234   -24.720 72.818  1.00 34.22  ? 354  MET B CE  1 
ATOM   6547 N  N   . VAL B 1 355 ? 1.031   -21.567 76.289  1.00 29.85  ? 355  VAL B N   1 
ATOM   6548 C  CA  . VAL B 1 355 ? 0.045   -20.509 76.518  1.00 28.52  ? 355  VAL B CA  1 
ATOM   6549 C  C   . VAL B 1 355 ? -1.075  -20.677 75.502  1.00 27.39  ? 355  VAL B C   1 
ATOM   6550 O  O   . VAL B 1 355 ? -0.839  -20.612 74.294  1.00 28.76  ? 355  VAL B O   1 
ATOM   6551 C  CB  . VAL B 1 355 ? 0.680   -19.114 76.405  1.00 29.25  ? 355  VAL B CB  1 
ATOM   6552 C  CG1 . VAL B 1 355 ? -0.397  -18.024 76.532  1.00 29.10  ? 355  VAL B CG1 1 
ATOM   6553 C  CG2 . VAL B 1 355 ? 1.753   -18.929 77.479  1.00 30.46  ? 355  VAL B CG2 1 
ATOM   6554 N  N   . LEU B 1 356 ? -2.298  -20.901 75.985  1.00 28.65  ? 356  LEU B N   1 
ATOM   6555 C  CA  . LEU B 1 356 ? -3.447  -21.105 75.100  1.00 32.28  ? 356  LEU B CA  1 
ATOM   6556 C  C   . LEU B 1 356 ? -4.141  -19.764 74.902  1.00 30.46  ? 356  LEU B C   1 
ATOM   6557 O  O   . LEU B 1 356 ? -5.032  -19.395 75.667  1.00 30.12  ? 356  LEU B O   1 
ATOM   6558 C  CB  . LEU B 1 356 ? -4.398  -22.131 75.705  1.00 33.03  ? 356  LEU B CB  1 
ATOM   6559 C  CG  . LEU B 1 356 ? -5.207  -23.117 74.870  1.00 43.94  ? 356  LEU B CG  1 
ATOM   6560 C  CD1 . LEU B 1 356 ? -4.465  -23.579 73.598  1.00 43.96  ? 356  LEU B CD1 1 
ATOM   6561 C  CD2 . LEU B 1 356 ? -5.636  -24.300 75.769  1.00 36.56  ? 356  LEU B CD2 1 
ATOM   6562 N  N   . ILE B 1 357 ? -3.760  -19.035 73.846  1.00 28.83  ? 357  ILE B N   1 
ATOM   6563 C  CA  . ILE B 1 357 ? -4.181  -17.639 73.733  1.00 26.71  ? 357  ILE B CA  1 
ATOM   6564 C  C   . ILE B 1 357 ? -5.694  -17.520 73.646  1.00 28.48  ? 357  ILE B C   1 
ATOM   6565 O  O   . ILE B 1 357 ? -6.253  -16.594 74.249  1.00 30.15  ? 357  ILE B O   1 
ATOM   6566 C  CB  . ILE B 1 357 ? -3.468  -16.957 72.557  1.00 27.33  ? 357  ILE B CB  1 
ATOM   6567 C  CG1 . ILE B 1 357 ? -1.958  -17.160 72.635  1.00 27.58  ? 357  ILE B CG1 1 
ATOM   6568 C  CG2 . ILE B 1 357 ? -3.771  -15.433 72.593  1.00 28.02  ? 357  ILE B CG2 1 
ATOM   6569 C  CD1 . ILE B 1 357 ? -1.247  -16.605 71.384  1.00 28.75  ? 357  ILE B CD1 1 
ATOM   6570 N  N   . PRO B 1 358 ? -6.417  -18.376 72.911  1.00 29.92  ? 358  PRO B N   1 
ATOM   6571 C  CA  . PRO B 1 358 ? -7.877  -18.210 72.871  1.00 28.80  ? 358  PRO B CA  1 
ATOM   6572 C  C   . PRO B 1 358 ? -8.510  -18.315 74.240  1.00 31.24  ? 358  PRO B C   1 
ATOM   6573 O  O   . PRO B 1 358 ? -9.514  -17.638 74.511  1.00 28.53  ? 358  PRO B O   1 
ATOM   6574 C  CB  . PRO B 1 358 ? -8.339  -19.346 71.943  1.00 29.60  ? 358  PRO B CB  1 
ATOM   6575 C  CG  . PRO B 1 358 ? -7.151  -19.643 71.089  1.00 27.87  ? 358  PRO B CG  1 
ATOM   6576 C  CD  . PRO B 1 358 ? -5.973  -19.464 72.011  1.00 28.26  ? 358  PRO B CD  1 
ATOM   6577 N  N   . GLN B 1 359 ? -7.942  -19.143 75.123  1.00 30.59  ? 359  GLN B N   1 
ATOM   6578 C  CA  . GLN B 1 359 ? -8.500  -19.262 76.462  1.00 32.74  ? 359  GLN B CA  1 
ATOM   6579 C  C   . GLN B 1 359 ? -8.144  -18.060 77.316  1.00 32.01  ? 359  GLN B C   1 
ATOM   6580 O  O   . GLN B 1 359 ? -8.972  -17.580 78.091  1.00 30.87  ? 359  GLN B O   1 
ATOM   6581 C  CB  . GLN B 1 359 ? -8.007  -20.550 77.126  1.00 32.12  ? 359  GLN B CB  1 
ATOM   6582 C  CG  . GLN B 1 359 ? -8.562  -21.812 76.484  1.00 34.54  ? 359  GLN B CG  1 
ATOM   6583 C  CD  . GLN B 1 359 ? -10.094 -21.851 76.468  1.00 35.16  ? 359  GLN B CD  1 
ATOM   6584 O  OE1 . GLN B 1 359 ? -10.710 -21.774 75.415  1.00 37.16  ? 359  GLN B OE1 1 
ATOM   6585 N  NE2 . GLN B 1 359 ? -10.700 -21.974 77.637  1.00 38.53  ? 359  GLN B NE2 1 
ATOM   6586 N  N   . LEU B 1 360 ? -6.905  -17.586 77.221  1.00 29.67  ? 360  LEU B N   1 
ATOM   6587 C  CA  . LEU B 1 360 ? -6.545  -16.350 77.895  1.00 28.92  ? 360  LEU B CA  1 
ATOM   6588 C  C   . LEU B 1 360 ? -7.564  -15.258 77.587  1.00 29.05  ? 360  LEU B C   1 
ATOM   6589 O  O   . LEU B 1 360 ? -8.034  -14.546 78.486  1.00 31.19  ? 360  LEU B O   1 
ATOM   6590 C  CB  . LEU B 1 360 ? -5.138  -15.915 77.460  1.00 28.71  ? 360  LEU B CB  1 
ATOM   6591 C  CG  . LEU B 1 360 ? -4.724  -14.511 77.897  1.00 30.52  ? 360  LEU B CG  1 
ATOM   6592 C  CD1 . LEU B 1 360 ? -4.495  -14.432 79.400  1.00 29.24  ? 360  LEU B CD1 1 
ATOM   6593 C  CD2 . LEU B 1 360 ? -3.464  -14.041 77.161  1.00 30.16  ? 360  LEU B CD2 1 
ATOM   6594 N  N   . HIS B 1 361 ? -7.907  -15.117 76.307  1.00 28.30  ? 361  HIS B N   1 
ATOM   6595 C  CA  . HIS B 1 361 ? -8.780  -14.061 75.813  1.00 27.56  ? 361  HIS B CA  1 
ATOM   6596 C  C   . HIS B 1 361 ? -10.234 -14.288 76.181  1.00 31.97  ? 361  HIS B C   1 
ATOM   6597 O  O   . HIS B 1 361 ? -11.076 -13.434 75.864  1.00 30.50  ? 361  HIS B O   1 
ATOM   6598 C  CB  . HIS B 1 361 ? -8.619  -13.955 74.298  1.00 29.12  ? 361  HIS B CB  1 
ATOM   6599 C  CG  . HIS B 1 361 ? -7.281  -13.427 73.880  1.00 29.00  ? 361  HIS B CG  1 
ATOM   6600 N  ND1 . HIS B 1 361 ? -6.874  -13.406 72.565  1.00 28.22  ? 361  HIS B ND1 1 
ATOM   6601 C  CD2 . HIS B 1 361 ? -6.265  -12.896 74.604  1.00 30.68  ? 361  HIS B CD2 1 
ATOM   6602 C  CE1 . HIS B 1 361 ? -5.669  -12.858 72.491  1.00 27.99  ? 361  HIS B CE1 1 
ATOM   6603 N  NE2 . HIS B 1 361 ? -5.274  -12.546 73.714  1.00 27.77  ? 361  HIS B NE2 1 
ATOM   6604 N  N   . ARG B 1 362 ? -10.533 -15.419 76.826  1.00 28.82  ? 362  ARG B N   1 
ATOM   6605 C  CA  . ARG B 1 362 ? -11.869 -15.712 77.340  1.00 29.81  ? 362  ARG B CA  1 
ATOM   6606 C  C   . ARG B 1 362 ? -11.912 -15.751 78.867  1.00 31.34  ? 362  ARG B C   1 
ATOM   6607 O  O   . ARG B 1 362 ? -12.855 -16.298 79.447  1.00 34.18  ? 362  ARG B O   1 
ATOM   6608 C  CB  . ARG B 1 362 ? -12.364 -17.035 76.757  1.00 29.74  ? 362  ARG B CB  1 
ATOM   6609 C  CG  . ARG B 1 362 ? -12.730 -16.960 75.263  1.00 29.80  ? 362  ARG B CG  1 
ATOM   6610 C  CD  . ARG B 1 362 ? -12.813 -18.374 74.653  1.00 27.98  ? 362  ARG B CD  1 
ATOM   6611 N  NE  . ARG B 1 362 ? -13.407 -18.350 73.318  1.00 31.17  ? 362  ARG B NE  1 
ATOM   6612 C  CZ  . ARG B 1 362 ? -12.751 -17.991 72.223  1.00 32.39  ? 362  ARG B CZ  1 
ATOM   6613 N  NH1 . ARG B 1 362 ? -11.481 -17.628 72.274  1.00 28.73  ? 362  ARG B NH1 1 
ATOM   6614 N  NH2 . ARG B 1 362 ? -13.386 -17.986 71.053  1.00 30.36  ? 362  ARG B NH2 1 
ATOM   6615 N  N   . ASP B 1 363 ? -10.878 -15.231 79.527  1.00 30.12  ? 363  ASP B N   1 
ATOM   6616 C  CA  . ASP B 1 363 ? -10.822 -15.197 80.988  1.00 32.45  ? 363  ASP B CA  1 
ATOM   6617 C  C   . ASP B 1 363 ? -11.884 -14.233 81.501  1.00 31.92  ? 363  ASP B C   1 
ATOM   6618 O  O   . ASP B 1 363 ? -11.746 -13.012 81.369  1.00 31.86  ? 363  ASP B O   1 
ATOM   6619 C  CB  . ASP B 1 363 ? -9.416  -14.786 81.428  1.00 31.50  ? 363  ASP B CB  1 
ATOM   6620 C  CG  . ASP B 1 363 ? -9.207  -14.874 82.933  1.00 31.85  ? 363  ASP B CG  1 
ATOM   6621 O  OD1 . ASP B 1 363 ? -10.197 -14.867 83.683  1.00 32.12  ? 363  ASP B OD1 1 
ATOM   6622 O  OD2 . ASP B 1 363 ? -8.036  -14.943 83.362  1.00 33.08  ? 363  ASP B OD2 1 
ATOM   6623 N  N   . LYS B 1 364 ? -12.949 -14.780 82.091  1.00 32.67  ? 364  LYS B N   1 
ATOM   6624 C  CA  . LYS B 1 364 ? -14.045 -13.933 82.543  1.00 33.13  ? 364  LYS B CA  1 
ATOM   6625 C  C   . LYS B 1 364 ? -13.640 -12.997 83.668  1.00 33.75  ? 364  LYS B C   1 
ATOM   6626 O  O   . LYS B 1 364 ? -14.281 -11.956 83.840  1.00 33.97  ? 364  LYS B O   1 
ATOM   6627 C  CB  . LYS B 1 364 ? -15.226 -14.802 82.978  1.00 34.90  ? 364  LYS B CB  1 
ATOM   6628 C  CG  . LYS B 1 364 ? -15.809 -15.585 81.832  1.00 38.21  ? 364  LYS B CG  1 
ATOM   6629 C  CD  . LYS B 1 364 ? -16.984 -16.441 82.257  1.00 42.98  ? 364  LYS B CD  1 
ATOM   6630 C  CE  . LYS B 1 364 ? -17.843 -16.799 81.054  1.00 51.11  ? 364  LYS B CE  1 
ATOM   6631 N  NZ  . LYS B 1 364 ? -18.861 -17.833 81.390  1.00 57.19  ? 364  LYS B NZ  1 
ATOM   6632 N  N   . THR B 1 365 ? -12.611 -13.333 84.451  1.00 33.31  ? 365  THR B N   1 
ATOM   6633 C  CA  . THR B 1 365 ? -12.197 -12.409 85.504  1.00 34.73  ? 365  THR B CA  1 
ATOM   6634 C  C   . THR B 1 365 ? -11.581 -11.140 84.926  1.00 36.22  ? 365  THR B C   1 
ATOM   6635 O  O   . THR B 1 365 ? -11.472 -10.136 85.638  1.00 35.54  ? 365  THR B O   1 
ATOM   6636 C  CB  . THR B 1 365 ? -11.207 -13.067 86.474  1.00 36.04  ? 365  THR B CB  1 
ATOM   6637 O  OG1 . THR B 1 365 ? -9.931  -13.209 85.839  1.00 38.06  ? 365  THR B OG1 1 
ATOM   6638 C  CG2 . THR B 1 365 ? -11.702 -14.443 86.927  1.00 36.57  ? 365  THR B CG2 1 
ATOM   6639 N  N   . ILE B 1 366 ? -11.190 -11.164 83.654  1.00 33.83  ? 366  ILE B N   1 
ATOM   6640 C  CA  . ILE B 1 366 ? -10.618 -10.005 82.967  1.00 32.73  ? 366  ILE B CA  1 
ATOM   6641 C  C   . ILE B 1 366 ? -11.660 -9.286  82.137  1.00 35.04  ? 366  ILE B C   1 
ATOM   6642 O  O   . ILE B 1 366 ? -11.823 -8.070  82.237  1.00 36.56  ? 366  ILE B O   1 
ATOM   6643 C  CB  . ILE B 1 366 ? -9.435  -10.450 82.075  1.00 32.83  ? 366  ILE B CB  1 
ATOM   6644 C  CG1 . ILE B 1 366 ? -8.321  -11.057 82.928  1.00 33.24  ? 366  ILE B CG1 1 
ATOM   6645 C  CG2 . ILE B 1 366 ? -8.948  -9.296  81.183  1.00 35.15  ? 366  ILE B CG2 1 
ATOM   6646 C  CD1 . ILE B 1 366 ? -7.601  -10.058 83.825  1.00 37.93  ? 366  ILE B CD1 1 
ATOM   6647 N  N   . TRP B 1 367 ? -12.367 -10.039 81.300  1.00 32.51  ? 367  TRP B N   1 
ATOM   6648 C  CA  . TRP B 1 367 ? -13.197 -9.481  80.250  1.00 31.95  ? 367  TRP B CA  1 
ATOM   6649 C  C   . TRP B 1 367 ? -14.666 -9.391  80.630  1.00 37.76  ? 367  TRP B C   1 
ATOM   6650 O  O   . TRP B 1 367 ? -15.432 -8.731  79.922  1.00 38.78  ? 367  TRP B O   1 
ATOM   6651 C  CB  . TRP B 1 367 ? -13.048 -10.323 78.982  1.00 34.24  ? 367  TRP B CB  1 
ATOM   6652 C  CG  . TRP B 1 367 ? -11.625 -10.399 78.509  1.00 32.32  ? 367  TRP B CG  1 
ATOM   6653 C  CD1 . TRP B 1 367 ? -10.715 -11.383 78.769  1.00 32.58  ? 367  TRP B CD1 1 
ATOM   6654 C  CD2 . TRP B 1 367 ? -10.949 -9.425  77.703  1.00 31.26  ? 367  TRP B CD2 1 
ATOM   6655 N  NE1 . TRP B 1 367 ? -9.509  -11.087 78.155  1.00 31.60  ? 367  TRP B NE1 1 
ATOM   6656 C  CE2 . TRP B 1 367 ? -9.628  -9.889  77.500  1.00 33.18  ? 367  TRP B CE2 1 
ATOM   6657 C  CE3 . TRP B 1 367 ? -11.335 -8.214  77.128  1.00 33.14  ? 367  TRP B CE3 1 
ATOM   6658 C  CZ2 . TRP B 1 367 ? -8.694  -9.182  76.739  1.00 31.12  ? 367  TRP B CZ2 1 
ATOM   6659 C  CZ3 . TRP B 1 367 ? -10.404 -7.502  76.375  1.00 32.07  ? 367  TRP B CZ3 1 
ATOM   6660 C  CH2 . TRP B 1 367 ? -9.099  -7.988  76.184  1.00 29.51  ? 367  TRP B CH2 1 
ATOM   6661 N  N   . GLY B 1 368 ? -15.080 -10.042 81.705  1.00 36.90  ? 368  GLY B N   1 
ATOM   6662 C  CA  . GLY B 1 368 ? -16.479 -10.036 82.084  1.00 34.51  ? 368  GLY B CA  1 
ATOM   6663 C  C   . GLY B 1 368 ? -17.211 -11.260 81.579  1.00 39.80  ? 368  GLY B C   1 
ATOM   6664 O  O   . GLY B 1 368 ? -16.640 -12.177 80.984  1.00 37.01  ? 368  GLY B O   1 
ATOM   6665 N  N   . ASP B 1 369 ? -18.522 -11.263 81.817  1.00 38.88  ? 369  ASP B N   1 
ATOM   6666 C  CA  . ASP B 1 369 ? -19.307 -12.459 81.545  1.00 41.44  ? 369  ASP B CA  1 
ATOM   6667 C  C   . ASP B 1 369 ? -19.556 -12.677 80.060  1.00 40.77  ? 369  ASP B C   1 
ATOM   6668 O  O   . ASP B 1 369 ? -19.797 -13.811 79.648  1.00 48.07  ? 369  ASP B O   1 
ATOM   6669 C  CB  . ASP B 1 369 ? -20.645 -12.374 82.271  1.00 46.90  ? 369  ASP B CB  1 
ATOM   6670 C  CG  . ASP B 1 369 ? -20.479 -12.327 83.758  1.00 52.61  ? 369  ASP B CG  1 
ATOM   6671 O  OD1 . ASP B 1 369 ? -19.672 -13.127 84.276  1.00 53.53  ? 369  ASP B OD1 1 
ATOM   6672 O  OD2 . ASP B 1 369 ? -21.128 -11.470 84.394  1.00 55.29  ? 369  ASP B OD2 1 
ATOM   6673 N  N   . ASP B 1 370 ? -19.508 -11.624 79.255  1.00 37.46  ? 370  ASP B N   1 
ATOM   6674 C  CA  . ASP B 1 370 ? -19.931 -11.699 77.855  1.00 38.80  ? 370  ASP B CA  1 
ATOM   6675 C  C   . ASP B 1 370 ? -18.783 -12.048 76.909  1.00 37.20  ? 370  ASP B C   1 
ATOM   6676 O  O   . ASP B 1 370 ? -18.754 -11.542 75.784  1.00 36.75  ? 370  ASP B O   1 
ATOM   6677 C  CB  . ASP B 1 370 ? -20.594 -10.371 77.481  1.00 40.18  ? 370  ASP B CB  1 
ATOM   6678 C  CG  . ASP B 1 370 ? -19.630 -9.184  77.548  1.00 43.32  ? 370  ASP B CG  1 
ATOM   6679 O  OD1 . ASP B 1 370 ? -19.993 -8.096  77.032  1.00 45.35  ? 370  ASP B OD1 1 
ATOM   6680 O  OD2 . ASP B 1 370 ? -18.496 -9.342  78.064  1.00 44.30  ? 370  ASP B OD2 1 
ATOM   6681 N  N   . VAL B 1 371 ? -17.857 -12.934 77.314  1.00 36.42  ? 371  VAL B N   1 
ATOM   6682 C  CA  . VAL B 1 371 ? -16.593 -13.089 76.585  1.00 33.20  ? 371  VAL B CA  1 
ATOM   6683 C  C   . VAL B 1 371 ? -16.794 -13.658 75.194  1.00 35.78  ? 371  VAL B C   1 
ATOM   6684 O  O   . VAL B 1 371 ? -15.946 -13.452 74.314  1.00 34.31  ? 371  VAL B O   1 
ATOM   6685 C  CB  . VAL B 1 371 ? -15.576 -13.963 77.355  1.00 38.06  ? 371  VAL B CB  1 
ATOM   6686 C  CG1 . VAL B 1 371 ? -15.067 -13.252 78.600  1.00 43.35  ? 371  VAL B CG1 1 
ATOM   6687 C  CG2 . VAL B 1 371 ? -16.172 -15.335 77.704  1.00 41.81  ? 371  VAL B CG2 1 
ATOM   6688 N  N   . GLU B 1 372 ? -17.875 -14.405 74.961  1.00 32.40  ? 372  GLU B N   1 
ATOM   6689 C  CA  . GLU B 1 372 ? -18.071 -14.968 73.630  1.00 32.16  ? 372  GLU B CA  1 
ATOM   6690 C  C   . GLU B 1 372 ? -18.649 -13.964 72.640  1.00 30.23  ? 372  GLU B C   1 
ATOM   6691 O  O   . GLU B 1 372 ? -18.628 -14.223 71.431  1.00 32.50  ? 372  GLU B O   1 
ATOM   6692 C  CB  . GLU B 1 372 ? -18.981 -16.200 73.709  1.00 35.57  ? 372  GLU B CB  1 
ATOM   6693 C  CG  . GLU B 1 372 ? -18.347 -17.387 74.432  1.00 34.45  ? 372  GLU B CG  1 
ATOM   6694 C  CD  . GLU B 1 372 ? -17.217 -18.015 73.627  1.00 39.13  ? 372  GLU B CD  1 
ATOM   6695 O  OE1 . GLU B 1 372 ? -17.319 -18.058 72.379  1.00 42.09  ? 372  GLU B OE1 1 
ATOM   6696 O  OE2 . GLU B 1 372 ? -16.230 -18.459 74.252  1.00 42.43  ? 372  GLU B OE2 1 
ATOM   6697 N  N   . GLU B 1 373 ? -19.154 -12.829 73.112  1.00 30.14  ? 373  GLU B N   1 
ATOM   6698 C  CA  . GLU B 1 373 ? -19.774 -11.867 72.212  1.00 31.28  ? 373  GLU B CA  1 
ATOM   6699 C  C   . GLU B 1 373 ? -18.712 -11.030 71.508  1.00 33.30  ? 373  GLU B C   1 
ATOM   6700 O  O   . GLU B 1 373 ? -17.635 -10.758 72.060  1.00 31.08  ? 373  GLU B O   1 
ATOM   6701 C  CB  . GLU B 1 373 ? -20.757 -10.979 72.992  1.00 35.84  ? 373  GLU B CB  1 
ATOM   6702 C  CG  . GLU B 1 373 ? -22.026 -11.758 73.333  1.00 37.11  ? 373  GLU B CG  1 
ATOM   6703 C  CD  . GLU B 1 373 ? -22.945 -11.068 74.325  1.00 43.63  ? 373  GLU B CD  1 
ATOM   6704 O  OE1 . GLU B 1 373 ? -22.674 -9.917  74.724  1.00 40.94  ? 373  GLU B OE1 1 
ATOM   6705 O  OE2 . GLU B 1 373 ? -23.945 -11.706 74.709  1.00 43.98  ? 373  GLU B OE2 1 
ATOM   6706 N  N   . PHE B 1 374 ? -19.020 -10.641 70.268  1.00 31.52  ? 374  PHE B N   1 
ATOM   6707 C  CA  . PHE B 1 374 ? -18.122 -9.831  69.454  1.00 28.19  ? 374  PHE B CA  1 
ATOM   6708 C  C   . PHE B 1 374 ? -18.467 -8.366  69.697  1.00 31.14  ? 374  PHE B C   1 
ATOM   6709 O  O   . PHE B 1 374 ? -19.442 -7.840  69.145  1.00 29.89  ? 374  PHE B O   1 
ATOM   6710 C  CB  . PHE B 1 374 ? -18.244 -10.199 67.976  1.00 30.33  ? 374  PHE B CB  1 
ATOM   6711 C  CG  . PHE B 1 374 ? -17.200 -9.561  67.119  1.00 28.83  ? 374  PHE B CG  1 
ATOM   6712 C  CD1 . PHE B 1 374 ? -15.912 -10.096 67.060  1.00 29.04  ? 374  PHE B CD1 1 
ATOM   6713 C  CD2 . PHE B 1 374 ? -17.482 -8.398  66.402  1.00 30.45  ? 374  PHE B CD2 1 
ATOM   6714 C  CE1 . PHE B 1 374 ? -14.941 -9.501  66.281  1.00 29.56  ? 374  PHE B CE1 1 
ATOM   6715 C  CE2 . PHE B 1 374 ? -16.497 -7.797  65.627  1.00 29.10  ? 374  PHE B CE2 1 
ATOM   6716 C  CZ  . PHE B 1 374 ? -15.220 -8.358  65.586  1.00 33.66  ? 374  PHE B CZ  1 
ATOM   6717 N  N   . ARG B 1 375 ? -17.669 -7.701  70.532  1.00 29.60  ? 375  ARG B N   1 
ATOM   6718 C  CA  . ARG B 1 375 ? -17.919 -6.321  70.954  1.00 26.92  ? 375  ARG B CA  1 
ATOM   6719 C  C   . ARG B 1 375 ? -16.630 -5.518  70.845  1.00 31.24  ? 375  ARG B C   1 
ATOM   6720 O  O   . ARG B 1 375 ? -15.878 -5.389  71.820  1.00 31.10  ? 375  ARG B O   1 
ATOM   6721 C  CB  . ARG B 1 375 ? -18.477 -6.276  72.380  1.00 30.38  ? 375  ARG B CB  1 
ATOM   6722 C  CG  . ARG B 1 375 ? -19.787 -7.047  72.535  1.00 33.37  ? 375  ARG B CG  1 
ATOM   6723 C  CD  . ARG B 1 375 ? -20.362 -6.867  73.939  1.00 37.98  ? 375  ARG B CD  1 
ATOM   6724 N  NE  . ARG B 1 375 ? -21.698 -7.444  73.996  1.00 38.95  ? 375  ARG B NE  1 
ATOM   6725 C  CZ  . ARG B 1 375 ? -22.783 -6.837  73.536  1.00 42.45  ? 375  ARG B CZ  1 
ATOM   6726 N  NH1 . ARG B 1 375 ? -22.734 -5.597  73.064  1.00 37.34  ? 375  ARG B NH1 1 
ATOM   6727 N  NH2 . ARG B 1 375 ? -23.948 -7.483  73.564  1.00 40.67  ? 375  ARG B NH2 1 
ATOM   6728 N  N   . PRO B 1 376 ? -16.350 -4.942  69.668  1.00 28.35  ? 376  PRO B N   1 
ATOM   6729 C  CA  . PRO B 1 376 ? -15.140 -4.119  69.518  1.00 28.84  ? 376  PRO B CA  1 
ATOM   6730 C  C   . PRO B 1 376 ? -15.054 -2.991  70.541  1.00 29.89  ? 376  PRO B C   1 
ATOM   6731 O  O   . PRO B 1 376 ? -13.963 -2.504  70.834  1.00 30.64  ? 376  PRO B O   1 
ATOM   6732 C  CB  . PRO B 1 376 ? -15.260 -3.577  68.090  1.00 29.29  ? 376  PRO B CB  1 
ATOM   6733 C  CG  . PRO B 1 376 ? -16.128 -4.593  67.384  1.00 31.08  ? 376  PRO B CG  1 
ATOM   6734 C  CD  . PRO B 1 376 ? -17.134 -5.007  68.416  1.00 28.33  ? 376  PRO B CD  1 
ATOM   6735 N  N   . GLU B 1 377 ? -16.190 -2.571  71.093  1.00 31.72  ? 377  GLU B N   1 
ATOM   6736 C  CA  . GLU B 1 377 ? -16.177 -1.522  72.111  1.00 33.15  ? 377  GLU B CA  1 
ATOM   6737 C  C   . GLU B 1 377 ? -15.293 -1.860  73.313  1.00 33.28  ? 377  GLU B C   1 
ATOM   6738 O  O   . GLU B 1 377 ? -14.889 -0.946  74.040  1.00 34.51  ? 377  GLU B O   1 
ATOM   6739 C  CB  . GLU B 1 377 ? -17.613 -1.231  72.567  1.00 33.41  ? 377  GLU B CB  1 
ATOM   6740 C  CG  . GLU B 1 377 ? -18.478 -0.527  71.504  1.00 34.01  ? 377  GLU B CG  1 
ATOM   6741 C  CD  . GLU B 1 377 ? -18.919 -1.454  70.379  1.00 30.45  ? 377  GLU B CD  1 
ATOM   6742 O  OE1 . GLU B 1 377 ? -18.913 -2.694  70.584  1.00 30.94  ? 377  GLU B OE1 1 
ATOM   6743 O  OE2 . GLU B 1 377 ? -19.298 -0.947  69.298  1.00 31.79  ? 377  GLU B OE2 1 
ATOM   6744 N  N   . ARG B 1 378 ? -14.989 -3.147  73.546  1.00 31.11  ? 378  ARG B N   1 
ATOM   6745 C  CA  . ARG B 1 378 ? -14.029 -3.521  74.588  1.00 34.62  ? 378  ARG B CA  1 
ATOM   6746 C  C   . ARG B 1 378 ? -12.711 -2.790  74.452  1.00 34.92  ? 378  ARG B C   1 
ATOM   6747 O  O   . ARG B 1 378 ? -11.994 -2.625  75.444  1.00 37.42  ? 378  ARG B O   1 
ATOM   6748 C  CB  . ARG B 1 378 ? -13.702 -5.017  74.531  1.00 33.25  ? 378  ARG B CB  1 
ATOM   6749 C  CG  . ARG B 1 378 ? -14.812 -5.912  74.871  1.00 38.58  ? 378  ARG B CG  1 
ATOM   6750 C  CD  . ARG B 1 378 ? -14.318 -7.322  74.668  1.00 31.97  ? 378  ARG B CD  1 
ATOM   6751 N  NE  . ARG B 1 378 ? -15.419 -8.157  74.241  1.00 33.64  ? 378  ARG B NE  1 
ATOM   6752 C  CZ  . ARG B 1 378 ? -16.294 -8.716  75.062  1.00 35.20  ? 378  ARG B CZ  1 
ATOM   6753 N  NH1 . ARG B 1 378 ? -16.198 -8.576  76.381  1.00 32.96  ? 378  ARG B NH1 1 
ATOM   6754 N  NH2 . ARG B 1 378 ? -17.287 -9.433  74.549  1.00 33.25  ? 378  ARG B NH2 1 
ATOM   6755 N  N   . PHE B 1 379 ? -12.328 -2.433  73.229  1.00 30.22  ? 379  PHE B N   1 
ATOM   6756 C  CA  . PHE B 1 379 ? -11.013 -1.871  72.965  1.00 32.21  ? 379  PHE B CA  1 
ATOM   6757 C  C   . PHE B 1 379 ? -11.056 -0.359  72.815  1.00 35.36  ? 379  PHE B C   1 
ATOM   6758 O  O   . PHE B 1 379 ? -10.064 0.248   72.394  1.00 35.97  ? 379  PHE B O   1 
ATOM   6759 C  CB  . PHE B 1 379 ? -10.402 -2.545  71.726  1.00 32.80  ? 379  PHE B CB  1 
ATOM   6760 C  CG  . PHE B 1 379 ? -10.005 -3.972  71.971  1.00 30.59  ? 379  PHE B CG  1 
ATOM   6761 C  CD1 . PHE B 1 379 ? -8.751  -4.271  72.501  1.00 31.89  ? 379  PHE B CD1 1 
ATOM   6762 C  CD2 . PHE B 1 379 ? -10.888 -5.013  71.720  1.00 33.13  ? 379  PHE B CD2 1 
ATOM   6763 C  CE1 . PHE B 1 379 ? -8.369  -5.581  72.759  1.00 31.11  ? 379  PHE B CE1 1 
ATOM   6764 C  CE2 . PHE B 1 379 ? -10.521 -6.341  71.992  1.00 31.41  ? 379  PHE B CE2 1 
ATOM   6765 C  CZ  . PHE B 1 379 ? -9.255  -6.631  72.504  1.00 30.31  ? 379  PHE B CZ  1 
ATOM   6766 N  N   . GLU B 1 380 ? -12.177 0.263   73.182  1.00 35.80  ? 380  GLU B N   1 
ATOM   6767 C  CA  . GLU B 1 380 ? -12.315 1.708   73.027  1.00 38.40  ? 380  GLU B CA  1 
ATOM   6768 C  C   . GLU B 1 380 ? -11.217 2.434   73.789  1.00 45.40  ? 380  GLU B C   1 
ATOM   6769 O  O   . GLU B 1 380 ? -10.636 3.407   73.293  1.00 48.15  ? 380  GLU B O   1 
ATOM   6770 C  CB  . GLU B 1 380 ? -13.688 2.141   73.532  1.00 42.71  ? 380  GLU B CB  1 
ATOM   6771 C  CG  . GLU B 1 380 ? -14.766 2.148   72.479  1.00 47.19  ? 380  GLU B CG  1 
ATOM   6772 C  CD  . GLU B 1 380 ? -16.133 2.503   73.042  1.00 45.71  ? 380  GLU B CD  1 
ATOM   6773 O  OE1 . GLU B 1 380 ? -17.122 2.436   72.285  1.00 56.60  ? 380  GLU B OE1 1 
ATOM   6774 O  OE2 . GLU B 1 380 ? -16.213 2.845   74.238  1.00 56.18  ? 380  GLU B OE2 1 
ATOM   6775 N  N   . ASN B 1 381 ? -10.903 1.943   74.986  1.00 40.81  ? 381  ASN B N   1 
ATOM   6776 C  CA  . ASN B 1 381 ? -9.944  2.536   75.914  1.00 46.96  ? 381  ASN B CA  1 
ATOM   6777 C  C   . ASN B 1 381 ? -8.805  1.550   76.131  1.00 40.39  ? 381  ASN B C   1 
ATOM   6778 O  O   . ASN B 1 381 ? -8.864  0.717   77.046  1.00 44.72  ? 381  ASN B O   1 
ATOM   6779 C  CB  . ASN B 1 381 ? -10.640 2.881   77.228  1.00 47.39  ? 381  ASN B CB  1 
ATOM   6780 C  CG  . ASN B 1 381 ? -9.739  3.604   78.206  1.00 51.47  ? 381  ASN B CG  1 
ATOM   6781 O  OD1 . ASN B 1 381 ? -8.565  3.862   77.927  1.00 52.71  ? 381  ASN B OD1 1 
ATOM   6782 N  ND2 . ASN B 1 381 ? -10.287 3.916   79.378  1.00 52.70  ? 381  ASN B ND2 1 
ATOM   6783 N  N   . PRO B 1 382 ? -7.738  1.625   75.332  1.00 44.35  ? 382  PRO B N   1 
ATOM   6784 C  CA  . PRO B 1 382 ? -6.659  0.630   75.458  1.00 50.51  ? 382  PRO B CA  1 
ATOM   6785 C  C   . PRO B 1 382 ? -6.081  0.552   76.859  1.00 49.59  ? 382  PRO B C   1 
ATOM   6786 O  O   . PRO B 1 382 ? -5.578  -0.511  77.247  1.00 43.92  ? 382  PRO B O   1 
ATOM   6787 C  CB  . PRO B 1 382 ? -5.600  1.098   74.449  1.00 53.07  ? 382  PRO B CB  1 
ATOM   6788 C  CG  . PRO B 1 382 ? -6.058  2.400   73.910  1.00 54.94  ? 382  PRO B CG  1 
ATOM   6789 C  CD  . PRO B 1 382 ? -7.419  2.733   74.417  1.00 50.60  ? 382  PRO B CD  1 
ATOM   6790 N  N   . SER B 1 383 ? -6.148  1.649   77.625  1.00 48.26  ? 383  SER B N   1 
ATOM   6791 C  CA  . SER B 1 383 ? -5.589  1.673   78.978  1.00 51.78  ? 383  SER B CA  1 
ATOM   6792 C  C   . SER B 1 383 ? -6.319  0.734   79.918  1.00 50.03  ? 383  SER B C   1 
ATOM   6793 O  O   . SER B 1 383 ? -5.753  0.309   80.931  1.00 50.08  ? 383  SER B O   1 
ATOM   6794 C  CB  . SER B 1 383 ? -5.634  3.092   79.556  1.00 47.39  ? 383  SER B CB  1 
ATOM   6795 O  OG  . SER B 1 383 ? -4.935  4.001   78.741  1.00 56.22  ? 383  SER B OG  1 
ATOM   6796 N  N   . ALA B 1 384 ? -7.576  0.418   79.621  1.00 48.04  ? 384  ALA B N   1 
ATOM   6797 C  CA  . ALA B 1 384 ? -8.355  -0.434  80.501  1.00 49.30  ? 384  ALA B CA  1 
ATOM   6798 C  C   . ALA B 1 384 ? -7.966  -1.907  80.407  1.00 47.57  ? 384  ALA B C   1 
ATOM   6799 O  O   . ALA B 1 384 ? -8.431  -2.701  81.230  1.00 46.95  ? 384  ALA B O   1 
ATOM   6800 C  CB  . ALA B 1 384 ? -9.843  -0.260  80.191  1.00 51.22  ? 384  ALA B CB  1 
ATOM   6801 N  N   . ILE B 1 385 ? -7.144  -2.291  79.437  1.00 44.52  ? 385  ILE B N   1 
ATOM   6802 C  CA  . ILE B 1 385 ? -6.744  -3.688  79.259  1.00 45.16  ? 385  ILE B CA  1 
ATOM   6803 C  C   . ILE B 1 385 ? -5.564  -3.998  80.174  1.00 43.42  ? 385  ILE B C   1 
ATOM   6804 O  O   . ILE B 1 385 ? -4.479  -3.429  79.988  1.00 42.05  ? 385  ILE B O   1 
ATOM   6805 C  CB  . ILE B 1 385 ? -6.375  -3.983  77.794  1.00 44.53  ? 385  ILE B CB  1 
ATOM   6806 C  CG1 . ILE B 1 385 ? -7.418  -3.404  76.828  1.00 50.64  ? 385  ILE B CG1 1 
ATOM   6807 C  CG2 . ILE B 1 385 ? -6.184  -5.479  77.580  1.00 44.68  ? 385  ILE B CG2 1 
ATOM   6808 C  CD1 . ILE B 1 385 ? -8.688  -4.224  76.706  1.00 45.67  ? 385  ILE B CD1 1 
ATOM   6809 N  N   . PRO B 1 386 ? -5.715  -4.891  81.155  1.00 40.45  ? 386  PRO B N   1 
ATOM   6810 C  CA  . PRO B 1 386 ? -4.582  -5.236  82.026  1.00 39.56  ? 386  PRO B CA  1 
ATOM   6811 C  C   . PRO B 1 386 ? -3.401  -5.781  81.237  1.00 42.80  ? 386  PRO B C   1 
ATOM   6812 O  O   . PRO B 1 386 ? -3.561  -6.367  80.168  1.00 39.79  ? 386  PRO B O   1 
ATOM   6813 C  CB  . PRO B 1 386 ? -5.168  -6.307  82.954  1.00 41.88  ? 386  PRO B CB  1 
ATOM   6814 C  CG  . PRO B 1 386 ? -6.629  -6.031  82.951  1.00 39.79  ? 386  PRO B CG  1 
ATOM   6815 C  CD  . PRO B 1 386 ? -6.958  -5.563  81.570  1.00 44.36  ? 386  PRO B CD  1 
ATOM   6816 N  N   . GLN B 1 387 ? -2.199  -5.592  81.787  1.00 39.03  ? 387  GLN B N   1 
ATOM   6817 C  CA  . GLN B 1 387 ? -1.003  -6.134  81.160  1.00 40.80  ? 387  GLN B CA  1 
ATOM   6818 C  C   . GLN B 1 387 ? -1.100  -7.654  81.098  1.00 38.49  ? 387  GLN B C   1 
ATOM   6819 O  O   . GLN B 1 387 ? -1.528  -8.307  82.056  1.00 38.20  ? 387  GLN B O   1 
ATOM   6820 C  CB  . GLN B 1 387 ? 0.253   -5.685  81.928  1.00 45.04  ? 387  GLN B CB  1 
ATOM   6821 C  CG  . GLN B 1 387 ? 1.601   -6.045  81.261  1.00 45.60  ? 387  GLN B CG  1 
ATOM   6822 C  CD  . GLN B 1 387 ? 2.800   -5.974  82.215  1.00 52.19  ? 387  GLN B CD  1 
ATOM   6823 O  OE1 . GLN B 1 387 ? 2.696   -6.284  83.403  1.00 58.28  ? 387  GLN B OE1 1 
ATOM   6824 N  NE2 . GLN B 1 387 ? 3.944   -5.549  81.689  1.00 55.13  ? 387  GLN B NE2 1 
ATOM   6825 N  N   . HIS B 1 388 ? -0.706  -8.213  79.951  1.00 35.23  ? 388  HIS B N   1 
ATOM   6826 C  CA  . HIS B 1 388 ? -0.706  -9.644  79.654  1.00 32.67  ? 388  HIS B CA  1 
ATOM   6827 C  C   . HIS B 1 388 ? -2.100  -10.255 79.591  1.00 33.16  ? 388  HIS B C   1 
ATOM   6828 O  O   . HIS B 1 388 ? -2.228  -11.480 79.601  1.00 36.35  ? 388  HIS B O   1 
ATOM   6829 C  CB  . HIS B 1 388 ? 0.156   -10.428 80.648  1.00 36.92  ? 388  HIS B CB  1 
ATOM   6830 C  CG  . HIS B 1 388 ? 1.562   -9.930  80.722  1.00 37.91  ? 388  HIS B CG  1 
ATOM   6831 N  ND1 . HIS B 1 388 ? 2.278   -9.576  79.598  1.00 41.12  ? 388  HIS B ND1 1 
ATOM   6832 C  CD2 . HIS B 1 388 ? 2.385   -9.724  81.777  1.00 40.80  ? 388  HIS B CD2 1 
ATOM   6833 C  CE1 . HIS B 1 388 ? 3.486   -9.179  79.959  1.00 43.54  ? 388  HIS B CE1 1 
ATOM   6834 N  NE2 . HIS B 1 388 ? 3.575   -9.256  81.275  1.00 40.68  ? 388  HIS B NE2 1 
ATOM   6835 N  N   . ALA B 1 389 ? -3.149  -9.440  79.481  1.00 30.85  ? 389  ALA B N   1 
ATOM   6836 C  CA  . ALA B 1 389 ? -4.486  -9.980  79.265  1.00 31.28  ? 389  ALA B CA  1 
ATOM   6837 C  C   . ALA B 1 389 ? -4.757  -10.265 77.793  1.00 32.56  ? 389  ALA B C   1 
ATOM   6838 O  O   . ALA B 1 389 ? -5.579  -11.131 77.472  1.00 30.32  ? 389  ALA B O   1 
ATOM   6839 C  CB  . ALA B 1 389 ? -5.539  -9.014  79.796  1.00 32.30  ? 389  ALA B CB  1 
ATOM   6840 N  N   . PHE B 1 390 ? -4.079  -9.558  76.894  1.00 29.67  ? 390  PHE B N   1 
ATOM   6841 C  CA  . PHE B 1 390 ? -4.379  -9.616  75.461  1.00 28.53  ? 390  PHE B CA  1 
ATOM   6842 C  C   . PHE B 1 390 ? -3.055  -9.841  74.740  1.00 29.92  ? 390  PHE B C   1 
ATOM   6843 O  O   . PHE B 1 390 ? -2.206  -8.945  74.718  1.00 31.85  ? 390  PHE B O   1 
ATOM   6844 C  CB  . PHE B 1 390 ? -5.068  -8.312  75.026  1.00 30.50  ? 390  PHE B CB  1 
ATOM   6845 C  CG  . PHE B 1 390 ? -5.406  -8.233  73.543  1.00 30.61  ? 390  PHE B CG  1 
ATOM   6846 C  CD1 . PHE B 1 390 ? -6.336  -9.093  72.984  1.00 30.68  ? 390  PHE B CD1 1 
ATOM   6847 C  CD2 . PHE B 1 390 ? -4.808  -7.274  72.735  1.00 30.18  ? 390  PHE B CD2 1 
ATOM   6848 C  CE1 . PHE B 1 390 ? -6.668  -9.002  71.637  1.00 30.62  ? 390  PHE B CE1 1 
ATOM   6849 C  CE2 . PHE B 1 390 ? -5.113  -7.181  71.375  1.00 30.64  ? 390  PHE B CE2 1 
ATOM   6850 C  CZ  . PHE B 1 390 ? -6.050  -8.045  70.835  1.00 31.01  ? 390  PHE B CZ  1 
ATOM   6851 N  N   . LYS B 1 391 ? -2.843  -11.050 74.217  1.00 28.75  ? 391  LYS B N   1 
ATOM   6852 C  CA  . LYS B 1 391 ? -1.513  -11.433 73.742  1.00 29.42  ? 391  LYS B CA  1 
ATOM   6853 C  C   . LYS B 1 391 ? -1.542  -12.129 72.387  1.00 27.58  ? 391  LYS B C   1 
ATOM   6854 O  O   . LYS B 1 391 ? -0.859  -13.145 72.202  1.00 29.03  ? 391  LYS B O   1 
ATOM   6855 C  CB  . LYS B 1 391 ? -0.815  -12.353 74.756  1.00 30.90  ? 391  LYS B CB  1 
ATOM   6856 C  CG  . LYS B 1 391 ? -0.773  -11.798 76.179  1.00 34.26  ? 391  LYS B CG  1 
ATOM   6857 C  CD  . LYS B 1 391 ? 0.168   -10.622 76.289  1.00 38.36  ? 391  LYS B CD  1 
ATOM   6858 C  CE  . LYS B 1 391 ? 1.625   -11.092 76.336  1.00 39.33  ? 391  LYS B CE  1 
ATOM   6859 N  NZ  . LYS B 1 391 ? 2.535   -9.937  76.634  1.00 37.99  ? 391  LYS B NZ  1 
ATOM   6860 N  N   . PRO B 1 392 ? -2.271  -11.603 71.398  1.00 29.01  ? 392  PRO B N   1 
ATOM   6861 C  CA  . PRO B 1 392 ? -2.288  -12.256 70.084  1.00 28.48  ? 392  PRO B CA  1 
ATOM   6862 C  C   . PRO B 1 392 ? -0.962  -12.167 69.366  1.00 28.62  ? 392  PRO B C   1 
ATOM   6863 O  O   . PRO B 1 392 ? -0.777  -12.870 68.364  1.00 26.73  ? 392  PRO B O   1 
ATOM   6864 C  CB  . PRO B 1 392 ? -3.365  -11.477 69.320  1.00 28.35  ? 392  PRO B CB  1 
ATOM   6865 C  CG  . PRO B 1 392 ? -3.275  -10.094 69.901  1.00 29.57  ? 392  PRO B CG  1 
ATOM   6866 C  CD  . PRO B 1 392 ? -2.998  -10.324 71.386  1.00 28.02  ? 392  PRO B CD  1 
ATOM   6867 N  N   A HIS B 1 393 ? -0.032  -11.337 69.826  0.68 28.76  ? 393  HIS B N   1 
ATOM   6868 N  N   B HIS B 1 393 ? -0.052  -11.316 69.848  0.32 28.77  ? 393  HIS B N   1 
ATOM   6869 C  CA  A HIS B 1 393 ? 1.252   -11.216 69.141  0.68 29.38  ? 393  HIS B CA  1 
ATOM   6870 C  CA  B HIS B 1 393 ? 1.241   -11.076 69.222  0.32 29.41  ? 393  HIS B CA  1 
ATOM   6871 C  C   A HIS B 1 393 ? 2.398   -11.644 70.048  0.68 29.71  ? 393  HIS B C   1 
ATOM   6872 C  C   B HIS B 1 393 ? 2.391   -11.768 69.946  0.32 29.64  ? 393  HIS B C   1 
ATOM   6873 O  O   A HIS B 1 393 ? 3.527   -11.177 69.900  0.68 29.25  ? 393  HIS B O   1 
ATOM   6874 O  O   B HIS B 1 393 ? 3.546   -11.586 69.553  0.32 29.20  ? 393  HIS B O   1 
ATOM   6875 C  CB  A HIS B 1 393 ? 1.455   -9.798  68.612  0.68 29.67  ? 393  HIS B CB  1 
ATOM   6876 C  CB  B HIS B 1 393 ? 1.525   -9.566  69.150  0.32 28.76  ? 393  HIS B CB  1 
ATOM   6877 C  CG  A HIS B 1 393 ? 0.653   -9.504  67.377  0.68 29.41  ? 393  HIS B CG  1 
ATOM   6878 C  CG  B HIS B 1 393 ? 0.330   -8.723  68.813  0.32 31.45  ? 393  HIS B CG  1 
ATOM   6879 N  ND1 A HIS B 1 393 ? -0.490  -8.738  67.405  0.68 34.79  ? 393  HIS B ND1 1 
ATOM   6880 N  ND1 B HIS B 1 393 ? -0.229  -8.692  67.555  0.32 33.84  ? 393  HIS B ND1 1 
ATOM   6881 C  CD2 A HIS B 1 393 ? 0.824   -9.880  66.085  0.68 31.33  ? 393  HIS B CD2 1 
ATOM   6882 C  CD2 B HIS B 1 393 ? -0.388  -7.851  69.565  0.32 34.05  ? 393  HIS B CD2 1 
ATOM   6883 C  CE1 A HIS B 1 393 ? -0.989  -8.650  66.185  0.68 31.94  ? 393  HIS B CE1 1 
ATOM   6884 C  CE1 B HIS B 1 393 ? -1.249  -7.852  67.548  0.32 33.97  ? 393  HIS B CE1 1 
ATOM   6885 N  NE2 A HIS B 1 393 ? -0.210  -9.334  65.364  0.68 32.69  ? 393  HIS B NE2 1 
ATOM   6886 N  NE2 B HIS B 1 393 ? -1.365  -7.325  68.755  0.32 32.61  ? 393  HIS B NE2 1 
ATOM   6887 N  N   . GLY B 1 394 ? 2.117   -12.543 70.992  1.00 28.24  ? 394  GLY B N   1 
ATOM   6888 C  CA  . GLY B 1 394 ? 3.190   -13.130 71.776  1.00 29.83  ? 394  GLY B CA  1 
ATOM   6889 C  C   . GLY B 1 394 ? 3.660   -12.184 72.863  1.00 31.84  ? 394  GLY B C   1 
ATOM   6890 O  O   . GLY B 1 394 ? 2.917   -11.303 73.308  1.00 29.45  ? 394  GLY B O   1 
ATOM   6891 N  N   . ASN B 1 395 ? 4.915   -12.375 73.308  1.00 29.02  ? 395  ASN B N   1 
ATOM   6892 C  CA  . ASN B 1 395 ? 5.350   -11.705 74.523  1.00 31.05  ? 395  ASN B CA  1 
ATOM   6893 C  C   . ASN B 1 395 ? 6.790   -11.214 74.430  1.00 30.55  ? 395  ASN B C   1 
ATOM   6894 O  O   . ASN B 1 395 ? 7.671   -11.923 73.925  1.00 30.04  ? 395  ASN B O   1 
ATOM   6895 C  CB  . ASN B 1 395 ? 5.243   -12.620 75.749  1.00 28.38  ? 395  ASN B CB  1 
ATOM   6896 C  CG  . ASN B 1 395 ? 5.656   -11.893 77.015  1.00 31.85  ? 395  ASN B CG  1 
ATOM   6897 O  OD1 . ASN B 1 395 ? 4.993   -10.936 77.441  1.00 33.37  ? 395  ASN B OD1 1 
ATOM   6898 N  ND2 . ASN B 1 395 ? 6.770   -12.313 77.603  1.00 31.71  ? 395  ASN B ND2 1 
ATOM   6899 N  N   . GLY B 1 396 ? 7.014   -10.001 74.938  1.00 32.06  ? 396  GLY B N   1 
ATOM   6900 C  CA  . GLY B 1 396 ? 8.358   -9.537  75.275  1.00 31.87  ? 396  GLY B CA  1 
ATOM   6901 C  C   . GLY B 1 396 ? 9.248   -9.382  74.056  1.00 30.97  ? 396  GLY B C   1 
ATOM   6902 O  O   . GLY B 1 396 ? 8.801   -9.017  72.961  1.00 31.03  ? 396  GLY B O   1 
ATOM   6903 N  N   . GLN B 1 397 ? 10.548  -9.638  74.259  1.00 30.01  ? 397  GLN B N   1 
ATOM   6904 C  CA  . GLN B 1 397 ? 11.488  -9.507  73.152  1.00 29.61  ? 397  GLN B CA  1 
ATOM   6905 C  C   . GLN B 1 397 ? 11.230  -10.541 72.067  1.00 30.25  ? 397  GLN B C   1 
ATOM   6906 O  O   . GLN B 1 397 ? 11.704  -10.361 70.949  1.00 30.26  ? 397  GLN B O   1 
ATOM   6907 C  CB  . GLN B 1 397 ? 12.941  -9.622  73.646  1.00 32.47  ? 397  GLN B CB  1 
ATOM   6908 C  CG  . GLN B 1 397 ? 13.378  -11.022 74.076  1.00 29.25  ? 397  GLN B CG  1 
ATOM   6909 C  CD  . GLN B 1 397 ? 14.805  -11.036 74.635  1.00 34.96  ? 397  GLN B CD  1 
ATOM   6910 O  OE1 . GLN B 1 397 ? 15.599  -10.143 74.346  1.00 34.25  ? 397  GLN B OE1 1 
ATOM   6911 N  NE2 . GLN B 1 397 ? 15.128  -12.053 75.427  1.00 35.00  ? 397  GLN B NE2 1 
ATOM   6912 N  N   . ARG B 1 398 ? 10.512  -11.626 72.378  1.00 27.53  ? 398  ARG B N   1 
ATOM   6913 C  CA  . ARG B 1 398 ? 10.139  -12.605 71.368  1.00 28.65  ? 398  ARG B CA  1 
ATOM   6914 C  C   . ARG B 1 398 ? 8.732   -12.360 70.830  1.00 29.49  ? 398  ARG B C   1 
ATOM   6915 O  O   . ARG B 1 398 ? 8.129   -13.268 70.251  1.00 28.69  ? 398  ARG B O   1 
ATOM   6916 C  CB  . ARG B 1 398 ? 10.270  -14.026 71.922  1.00 28.50  ? 398  ARG B CB  1 
ATOM   6917 C  CG  . ARG B 1 398 ? 11.721  -14.440 72.341  1.00 26.43  ? 398  ARG B CG  1 
ATOM   6918 C  CD  . ARG B 1 398 ? 12.748  -14.190 71.214  1.00 29.90  ? 398  ARG B CD  1 
ATOM   6919 N  NE  . ARG B 1 398 ? 12.446  -14.891 69.971  1.00 27.14  ? 398  ARG B NE  1 
ATOM   6920 C  CZ  . ARG B 1 398 ? 12.877  -16.107 69.657  1.00 28.55  ? 398  ARG B CZ  1 
ATOM   6921 N  NH1 . ARG B 1 398 ? 13.600  -16.830 70.507  1.00 27.13  ? 398  ARG B NH1 1 
ATOM   6922 N  NH2 . ARG B 1 398 ? 12.586  -16.609 68.457  1.00 28.56  ? 398  ARG B NH2 1 
ATOM   6923 N  N   . ALA B 1 399 ? 8.198   -11.162 71.025  1.00 27.71  ? 399  ALA B N   1 
ATOM   6924 C  CA  . ALA B 1 399 ? 6.902   -10.833 70.442  1.00 28.21  ? 399  ALA B CA  1 
ATOM   6925 C  C   . ALA B 1 399 ? 6.997   -10.727 68.924  1.00 27.65  ? 399  ALA B C   1 
ATOM   6926 O  O   . ALA B 1 399 ? 8.076   -10.649 68.330  1.00 30.60  ? 399  ALA B O   1 
ATOM   6927 C  CB  . ALA B 1 399 ? 6.364   -9.528  71.015  1.00 30.33  ? 399  ALA B CB  1 
ATOM   6928 N  N   . CYS B 1 400 ? 5.835   -10.700 68.295  1.00 28.10  ? 400  CYS B N   1 
ATOM   6929 C  CA  . CYS B 1 400 ? 5.761   -10.638 66.839  1.00 26.21  ? 400  CYS B CA  1 
ATOM   6930 C  C   . CYS B 1 400 ? 6.409   -9.362  66.297  1.00 27.03  ? 400  CYS B C   1 
ATOM   6931 O  O   . CYS B 1 400 ? 5.978   -8.245  66.607  1.00 29.76  ? 400  CYS B O   1 
ATOM   6932 C  CB  . CYS B 1 400 ? 4.293   -10.717 66.415  1.00 28.21  ? 400  CYS B CB  1 
ATOM   6933 S  SG  . CYS B 1 400 ? 4.079   -10.547 64.623  1.00 29.47  ? 400  CYS B SG  1 
ATOM   6934 N  N   . ILE B 1 401 ? 7.432   -9.522  65.456  1.00 28.06  ? 401  ILE B N   1 
ATOM   6935 C  CA  . ILE B 1 401 ? 8.092   -8.351  64.895  1.00 27.47  ? 401  ILE B CA  1 
ATOM   6936 C  C   . ILE B 1 401 ? 7.203   -7.670  63.864  1.00 30.19  ? 401  ILE B C   1 
ATOM   6937 O  O   . ILE B 1 401 ? 7.399   -6.490  63.560  1.00 31.08  ? 401  ILE B O   1 
ATOM   6938 C  CB  . ILE B 1 401 ? 9.443   -8.760  64.279  1.00 27.66  ? 401  ILE B CB  1 
ATOM   6939 C  CG1 . ILE B 1 401 ? 10.351  -7.543  64.097  1.00 29.01  ? 401  ILE B CG1 1 
ATOM   6940 C  CG2 . ILE B 1 401 ? 9.221   -9.452  62.958  1.00 29.09  ? 401  ILE B CG2 1 
ATOM   6941 C  CD1 . ILE B 1 401 ? 11.799  -7.903  63.601  1.00 30.25  ? 401  ILE B CD1 1 
ATOM   6942 N  N   . GLY B 1 402 ? 6.231   -8.391  63.313  1.00 29.62  ? 402  GLY B N   1 
ATOM   6943 C  CA  . GLY B 1 402 ? 5.381   -7.922  62.236  1.00 31.38  ? 402  GLY B CA  1 
ATOM   6944 C  C   . GLY B 1 402 ? 4.062   -7.325  62.679  1.00 29.40  ? 402  GLY B C   1 
ATOM   6945 O  O   . GLY B 1 402 ? 3.201   -7.073  61.828  1.00 30.00  ? 402  GLY B O   1 
ATOM   6946 N  N   . GLN B 1 403 ? 3.887   -7.093  63.984  1.00 27.63  ? 403  GLN B N   1 
ATOM   6947 C  CA  . GLN B 1 403 ? 2.581   -6.702  64.514  1.00 29.09  ? 403  GLN B CA  1 
ATOM   6948 C  C   . GLN B 1 403 ? 2.052   -5.438  63.846  1.00 32.66  ? 403  GLN B C   1 
ATOM   6949 O  O   . GLN B 1 403 ? 0.873   -5.370  63.465  1.00 32.71  ? 403  GLN B O   1 
ATOM   6950 C  CB  . GLN B 1 403 ? 2.668   -6.506  66.032  1.00 31.07  ? 403  GLN B CB  1 
ATOM   6951 C  CG  . GLN B 1 403 ? 1.347   -6.007  66.690  1.00 35.96  ? 403  GLN B CG  1 
ATOM   6952 C  CD  . GLN B 1 403 ? 1.557   -5.554  68.138  1.00 44.67  ? 403  GLN B CD  1 
ATOM   6953 O  OE1 . GLN B 1 403 ? 2.468   -6.032  68.809  1.00 40.93  ? 403  GLN B OE1 1 
ATOM   6954 N  NE2 . GLN B 1 403 ? 0.709   -4.628  68.619  1.00 45.87  ? 403  GLN B NE2 1 
ATOM   6955 N  N   A GLN B 1 404 ? 2.900   -4.412  63.723  0.41 31.81  ? 404  GLN B N   1 
ATOM   6956 N  N   B GLN B 1 404 ? 2.902   -4.415  63.708  0.59 31.76  ? 404  GLN B N   1 
ATOM   6957 C  CA  A GLN B 1 404 ? 2.460   -3.160  63.120  0.41 33.68  ? 404  GLN B CA  1 
ATOM   6958 C  CA  B GLN B 1 404 ? 2.443   -3.160  63.123  0.59 33.66  ? 404  GLN B CA  1 
ATOM   6959 C  C   A GLN B 1 404 ? 2.172   -3.339  61.638  0.41 31.53  ? 404  GLN B C   1 
ATOM   6960 C  C   B GLN B 1 404 ? 2.187   -3.314  61.631  0.59 31.50  ? 404  GLN B C   1 
ATOM   6961 O  O   A GLN B 1 404 ? 1.213   -2.764  61.110  0.41 32.73  ? 404  GLN B O   1 
ATOM   6962 O  O   B GLN B 1 404 ? 1.266   -2.694  61.087  0.59 32.71  ? 404  GLN B O   1 
ATOM   6963 C  CB  A GLN B 1 404 ? 3.518   -2.076  63.329  0.41 36.51  ? 404  GLN B CB  1 
ATOM   6964 C  CB  B GLN B 1 404 ? 3.467   -2.049  63.379  0.59 36.52  ? 404  GLN B CB  1 
ATOM   6965 C  CG  A GLN B 1 404 ? 3.722   -1.717  64.787  0.41 38.61  ? 404  GLN B CG  1 
ATOM   6966 C  CG  B GLN B 1 404 ? 3.669   -1.713  64.859  0.59 38.61  ? 404  GLN B CG  1 
ATOM   6967 C  CD  A GLN B 1 404 ? 2.424   -1.306  65.441  0.41 39.38  ? 404  GLN B CD  1 
ATOM   6968 C  CD  B GLN B 1 404 ? 4.521   -2.734  65.585  0.59 40.47  ? 404  GLN B CD  1 
ATOM   6969 O  OE1 A GLN B 1 404 ? 1.948   -0.188  65.241  0.41 45.12  ? 404  GLN B OE1 1 
ATOM   6970 O  OE1 B GLN B 1 404 ? 5.463   -3.285  65.022  0.59 41.64  ? 404  GLN B OE1 1 
ATOM   6971 N  NE2 A GLN B 1 404 ? 1.828   -2.213  66.207  0.41 43.96  ? 404  GLN B NE2 1 
ATOM   6972 N  NE2 B GLN B 1 404 ? 4.203   -2.973  66.854  0.59 45.60  ? 404  GLN B NE2 1 
ATOM   6973 N  N   . PHE B 1 405 ? 3.002   -4.124  60.951  1.00 30.30  ? 405  PHE B N   1 
ATOM   6974 C  CA  . PHE B 1 405 ? 2.769   -4.407  59.537  1.00 29.28  ? 405  PHE B CA  1 
ATOM   6975 C  C   . PHE B 1 405 ? 1.405   -5.053  59.341  1.00 28.95  ? 405  PHE B C   1 
ATOM   6976 O  O   . PHE B 1 405 ? 0.595   -4.594  58.525  1.00 29.60  ? 405  PHE B O   1 
ATOM   6977 C  CB  . PHE B 1 405 ? 3.900   -5.312  59.017  1.00 29.42  ? 405  PHE B CB  1 
ATOM   6978 C  CG  . PHE B 1 405 ? 3.901   -5.527  57.528  1.00 29.34  ? 405  PHE B CG  1 
ATOM   6979 C  CD1 . PHE B 1 405 ? 3.077   -6.496  56.963  1.00 30.11  ? 405  PHE B CD1 1 
ATOM   6980 C  CD2 . PHE B 1 405 ? 4.747   -4.804  56.690  1.00 31.88  ? 405  PHE B CD2 1 
ATOM   6981 C  CE1 . PHE B 1 405 ? 3.091   -6.729  55.599  1.00 30.39  ? 405  PHE B CE1 1 
ATOM   6982 C  CE2 . PHE B 1 405 ? 4.757   -5.025  55.319  1.00 31.81  ? 405  PHE B CE2 1 
ATOM   6983 C  CZ  . PHE B 1 405 ? 3.925   -5.980  54.767  1.00 32.43  ? 405  PHE B CZ  1 
ATOM   6984 N  N   . ALA B 1 406 ? 1.143   -6.131  60.082  1.00 28.05  ? 406  ALA B N   1 
ATOM   6985 C  CA  . ALA B 1 406 ? -0.126  -6.843  59.972  1.00 30.12  ? 406  ALA B CA  1 
ATOM   6986 C  C   . ALA B 1 406 ? -1.311  -5.921  60.223  1.00 30.01  ? 406  ALA B C   1 
ATOM   6987 O  O   . ALA B 1 406 ? -2.287  -5.920  59.456  1.00 29.00  ? 406  ALA B O   1 
ATOM   6988 C  CB  . ALA B 1 406 ? -0.153  -8.015  60.958  1.00 28.83  ? 406  ALA B CB  1 
ATOM   6989 N  N   . LEU B 1 407 ? -1.268  -5.150  61.318  1.00 30.08  ? 407  LEU B N   1 
ATOM   6990 C  CA  . LEU B 1 407 ? -2.431  -4.327  61.652  1.00 30.39  ? 407  LEU B CA  1 
ATOM   6991 C  C   . LEU B 1 407 ? -2.611  -3.175  60.664  1.00 29.98  ? 407  LEU B C   1 
ATOM   6992 O  O   . LEU B 1 407 ? -3.749  -2.789  60.370  1.00 31.25  ? 407  LEU B O   1 
ATOM   6993 C  CB  . LEU B 1 407 ? -2.318  -3.814  63.095  1.00 31.79  ? 407  LEU B CB  1 
ATOM   6994 C  CG  . LEU B 1 407 ? -2.526  -4.921  64.139  1.00 37.11  ? 407  LEU B CG  1 
ATOM   6995 C  CD1 . LEU B 1 407 ? -2.419  -4.375  65.577  1.00 41.58  ? 407  LEU B CD1 1 
ATOM   6996 C  CD2 . LEU B 1 407 ? -3.845  -5.653  63.922  1.00 42.26  ? 407  LEU B CD2 1 
ATOM   6997 N  N   . HIS B 1 408 ? -1.523  -2.607  60.135  1.00 29.82  ? 408  HIS B N   1 
ATOM   6998 C  CA  . HIS B 1 408 ? -1.698  -1.557  59.135  1.00 29.54  ? 408  HIS B CA  1 
ATOM   6999 C  C   . HIS B 1 408 ? -2.317  -2.129  57.865  1.00 30.60  ? 408  HIS B C   1 
ATOM   7000 O  O   . HIS B 1 408 ? -3.254  -1.557  57.297  1.00 30.21  ? 408  HIS B O   1 
ATOM   7001 C  CB  . HIS B 1 408 ? -0.362  -0.868  58.810  1.00 30.47  ? 408  HIS B CB  1 
ATOM   7002 C  CG  . HIS B 1 408 ? -0.526  0.384   57.998  1.00 27.87  ? 408  HIS B CG  1 
ATOM   7003 N  ND1 . HIS B 1 408 ? -0.913  1.582   58.560  1.00 29.66  ? 408  HIS B ND1 1 
ATOM   7004 C  CD2 . HIS B 1 408 ? -0.410  0.610   56.663  1.00 30.14  ? 408  HIS B CD2 1 
ATOM   7005 C  CE1 . HIS B 1 408 ? -1.022  2.495   57.608  1.00 33.96  ? 408  HIS B CE1 1 
ATOM   7006 N  NE2 . HIS B 1 408 ? -0.709  1.936   56.449  1.00 29.81  ? 408  HIS B NE2 1 
ATOM   7007 N  N   . GLU B 1 409 ? -1.787  -3.255  57.404  1.00 26.94  ? 409  GLU B N   1 
ATOM   7008 C  CA  . GLU B 1 409 ? -2.337  -3.900  56.222  1.00 28.12  ? 409  GLU B CA  1 
ATOM   7009 C  C   . GLU B 1 409 ? -3.799  -4.246  56.440  1.00 27.80  ? 409  GLU B C   1 
ATOM   7010 O  O   . GLU B 1 409 ? -4.656  -3.942  55.599  1.00 29.07  ? 409  GLU B O   1 
ATOM   7011 C  CB  . GLU B 1 409 ? -1.513  -5.148  55.883  1.00 29.25  ? 409  GLU B CB  1 
ATOM   7012 C  CG  . GLU B 1 409 ? -2.152  -5.988  54.771  1.00 29.87  ? 409  GLU B CG  1 
ATOM   7013 C  CD  . GLU B 1 409 ? -1.360  -7.230  54.451  1.00 32.33  ? 409  GLU B CD  1 
ATOM   7014 O  OE1 . GLU B 1 409 ? -0.425  -7.546  55.208  1.00 30.98  ? 409  GLU B OE1 1 
ATOM   7015 O  OE2 . GLU B 1 409 ? -1.649  -7.873  53.431  1.00 30.75  ? 409  GLU B OE2 1 
ATOM   7016 N  N   . ALA B 1 410 ? -4.115  -4.857  57.586  1.00 27.02  ? 410  ALA B N   1 
ATOM   7017 C  CA  . ALA B 1 410 ? -5.488  -5.327  57.778  1.00 29.21  ? 410  ALA B CA  1 
ATOM   7018 C  C   . ALA B 1 410 ? -6.452  -4.158  57.946  1.00 28.50  ? 410  ALA B C   1 
ATOM   7019 O  O   . ALA B 1 410 ? -7.604  -4.230  57.503  1.00 28.61  ? 410  ALA B O   1 
ATOM   7020 C  CB  . ALA B 1 410 ? -5.573  -6.290  58.976  1.00 29.28  ? 410  ALA B CB  1 
ATOM   7021 N  N   . THR B 1 411 ? -6.008  -3.079  58.593  1.00 28.36  ? 411  THR B N   1 
ATOM   7022 C  CA  . THR B 1 411 ? -6.884  -1.919  58.747  1.00 28.02  ? 411  THR B CA  1 
ATOM   7023 C  C   . THR B 1 411 ? -7.153  -1.257  57.404  1.00 29.57  ? 411  THR B C   1 
ATOM   7024 O  O   . THR B 1 411 ? -8.297  -0.891  57.102  1.00 29.55  ? 411  THR B O   1 
ATOM   7025 C  CB  . THR B 1 411 ? -6.271  -0.926  59.738  1.00 30.08  ? 411  THR B CB  1 
ATOM   7026 O  OG1 . THR B 1 411 ? -6.048  -1.594  60.984  1.00 29.74  ? 411  THR B OG1 1 
ATOM   7027 C  CG2 . THR B 1 411 ? -7.199  0.267   59.972  1.00 27.14  ? 411  THR B CG2 1 
ATOM   7028 N  N   . LEU B 1 412 ? -6.113  -1.101  56.587  1.00 29.44  ? 412  LEU B N   1 
ATOM   7029 C  CA  . LEU B 1 412 ? -6.290  -0.527  55.260  1.00 28.41  ? 412  LEU B CA  1 
ATOM   7030 C  C   . LEU B 1 412 ? -7.265  -1.351  54.440  1.00 28.64  ? 412  LEU B C   1 
ATOM   7031 O  O   . LEU B 1 412 ? -8.194  -0.814  53.814  1.00 29.57  ? 412  LEU B O   1 
ATOM   7032 C  CB  . LEU B 1 412 ? -4.932  -0.458  54.554  1.00 28.59  ? 412  LEU B CB  1 
ATOM   7033 C  CG  . LEU B 1 412 ? -5.035  -0.352  53.037  1.00 31.69  ? 412  LEU B CG  1 
ATOM   7034 C  CD1 . LEU B 1 412 ? -5.557  1.053   52.650  1.00 33.00  ? 412  LEU B CD1 1 
ATOM   7035 C  CD2 . LEU B 1 412 ? -3.699  -0.649  52.394  1.00 34.25  ? 412  LEU B CD2 1 
ATOM   7036 N  N   . VAL B 1 413 ? -7.055  -2.670  54.414  1.00 28.65  ? 413  VAL B N   1 
ATOM   7037 C  CA  . VAL B 1 413 ? -7.821  -3.531  53.519  1.00 29.21  ? 413  VAL B CA  1 
ATOM   7038 C  C   . VAL B 1 413 ? -9.263  -3.630  53.992  1.00 30.35  ? 413  VAL B C   1 
ATOM   7039 O  O   . VAL B 1 413 ? -10.202 -3.505  53.194  1.00 30.90  ? 413  VAL B O   1 
ATOM   7040 C  CB  . VAL B 1 413 ? -7.153  -4.916  53.431  1.00 32.08  ? 413  VAL B CB  1 
ATOM   7041 C  CG1 . VAL B 1 413 ? -8.031  -5.934  52.718  1.00 33.32  ? 413  VAL B CG1 1 
ATOM   7042 C  CG2 . VAL B 1 413 ? -5.805  -4.790  52.748  1.00 32.37  ? 413  VAL B CG2 1 
ATOM   7043 N  N   . LEU B 1 414 ? -9.460  -3.882  55.286  1.00 28.46  ? 414  LEU B N   1 
ATOM   7044 C  CA  . LEU B 1 414 ? -10.826 -3.951  55.801  1.00 28.23  ? 414  LEU B CA  1 
ATOM   7045 C  C   . LEU B 1 414 ? -11.534 -2.611  55.634  1.00 31.36  ? 414  LEU B C   1 
ATOM   7046 O  O   . LEU B 1 414 ? -12.721 -2.565  55.298  1.00 29.31  ? 414  LEU B O   1 
ATOM   7047 C  CB  . LEU B 1 414 ? -10.830 -4.384  57.271  1.00 28.91  ? 414  LEU B CB  1 
ATOM   7048 C  CG  . LEU B 1 414 ? -12.179 -4.728  57.908  1.00 30.03  ? 414  LEU B CG  1 
ATOM   7049 C  CD1 . LEU B 1 414 ? -12.951 -5.713  57.071  1.00 32.04  ? 414  LEU B CD1 1 
ATOM   7050 C  CD2 . LEU B 1 414 ? -11.939 -5.330  59.303  1.00 30.39  ? 414  LEU B CD2 1 
ATOM   7051 N  N   . GLY B 1 415 ? -10.812 -1.510  55.842  1.00 29.03  ? 415  GLY B N   1 
ATOM   7052 C  CA  . GLY B 1 415 ? -11.386 -0.199  55.574  1.00 29.74  ? 415  GLY B CA  1 
ATOM   7053 C  C   . GLY B 1 415 ? -11.848 -0.062  54.133  1.00 30.05  ? 415  GLY B C   1 
ATOM   7054 O  O   . GLY B 1 415 ? -12.963 0.392   53.863  1.00 29.69  ? 415  GLY B O   1 
ATOM   7055 N  N   . MET B 1 416 ? -11.010 -0.494  53.185  1.00 29.17  ? 416  MET B N   1 
ATOM   7056 C  CA  . MET B 1 416 ? -11.386 -0.377  51.777  1.00 30.86  ? 416  MET B CA  1 
ATOM   7057 C  C   . MET B 1 416 ? -12.562 -1.300  51.449  1.00 29.40  ? 416  MET B C   1 
ATOM   7058 O  O   . MET B 1 416 ? -13.459 -0.932  50.678  1.00 30.04  ? 416  MET B O   1 
ATOM   7059 C  CB  . MET B 1 416 ? -10.170 -0.713  50.908  1.00 26.57  ? 416  MET B CB  1 
ATOM   7060 C  CG  . MET B 1 416 ? -9.251  0.503   50.819  1.00 31.06  ? 416  MET B CG  1 
ATOM   7061 S  SD  . MET B 1 416 ? -7.853  0.292   49.705  1.00 34.96  ? 416  MET B SD  1 
ATOM   7062 C  CE  . MET B 1 416 ? -8.676  0.418   48.122  1.00 33.99  ? 416  MET B CE  1 
ATOM   7063 N  N   . MET B 1 417 ? -12.562 -2.514  52.007  1.00 28.65  ? 417  MET B N   1 
ATOM   7064 C  CA  . MET B 1 417 ? -13.671 -3.438  51.776  1.00 28.56  ? 417  MET B CA  1 
ATOM   7065 C  C   . MET B 1 417 ? -14.988 -2.839  52.238  1.00 31.86  ? 417  MET B C   1 
ATOM   7066 O  O   . MET B 1 417 ? -15.991 -2.882  51.511  1.00 29.44  ? 417  MET B O   1 
ATOM   7067 C  CB  . MET B 1 417 ? -13.416 -4.781  52.471  1.00 30.28  ? 417  MET B CB  1 
ATOM   7068 C  CG  . MET B 1 417 ? -12.150 -5.476  52.002  1.00 30.22  ? 417  MET B CG  1 
ATOM   7069 S  SD  . MET B 1 417 ? -11.672 -6.898  53.024  1.00 32.73  ? 417  MET B SD  1 
ATOM   7070 C  CE  . MET B 1 417 ? -13.259 -7.648  53.417  1.00 34.71  ? 417  MET B CE  1 
ATOM   7071 N  N   . LEU B 1 418 ? -14.988 -2.242  53.429  1.00 29.00  ? 418  LEU B N   1 
ATOM   7072 C  CA  . LEU B 1 418 ? -16.219 -1.686  53.987  1.00 29.76  ? 418  LEU B CA  1 
ATOM   7073 C  C   . LEU B 1 418 ? -16.640 -0.422  53.268  1.00 30.98  ? 418  LEU B C   1 
ATOM   7074 O  O   . LEU B 1 418 ? -17.837 -0.101  53.226  1.00 31.41  ? 418  LEU B O   1 
ATOM   7075 C  CB  . LEU B 1 418 ? -16.037 -1.402  55.481  1.00 27.33  ? 418  LEU B CB  1 
ATOM   7076 C  CG  . LEU B 1 418 ? -15.878 -2.680  56.310  1.00 34.55  ? 418  LEU B CG  1 
ATOM   7077 C  CD1 . LEU B 1 418 ? -15.704 -2.336  57.775  1.00 34.06  ? 418  LEU B CD1 1 
ATOM   7078 C  CD2 . LEU B 1 418 ? -17.082 -3.615  56.117  1.00 36.53  ? 418  LEU B CD2 1 
ATOM   7079 N  N   . LYS B 1 419 ? -15.679 0.319   52.728  1.00 27.73  ? 419  LYS B N   1 
ATOM   7080 C  CA  . LYS B 1 419 ? -16.018 1.507   51.953  1.00 27.76  ? 419  LYS B CA  1 
ATOM   7081 C  C   . LYS B 1 419 ? -16.705 1.133   50.647  1.00 30.84  ? 419  LYS B C   1 
ATOM   7082 O  O   . LYS B 1 419 ? -17.638 1.819   50.213  1.00 30.11  ? 419  LYS B O   1 
ATOM   7083 C  CB  . LYS B 1 419 ? -14.761 2.326   51.654  1.00 30.06  ? 419  LYS B CB  1 
ATOM   7084 C  CG  . LYS B 1 419 ? -14.966 3.434   50.596  1.00 31.50  ? 419  LYS B CG  1 
ATOM   7085 C  CD  . LYS B 1 419 ? -13.650 4.147   50.292  1.00 33.17  ? 419  LYS B CD  1 
ATOM   7086 C  CE  . LYS B 1 419 ? -13.804 5.194   49.184  1.00 31.84  ? 419  LYS B CE  1 
ATOM   7087 N  NZ  . LYS B 1 419 ? -12.507 5.914   49.037  1.00 31.90  ? 419  LYS B NZ  1 
ATOM   7088 N  N   . HIS B 1 420 ? -16.240 0.068   49.989  1.00 31.03  ? 420  HIS B N   1 
ATOM   7089 C  CA  . HIS B 1 420 ? -16.620 -0.155  48.606  1.00 30.45  ? 420  HIS B CA  1 
ATOM   7090 C  C   . HIS B 1 420 ? -17.770 -1.138  48.413  1.00 31.41  ? 420  HIS B C   1 
ATOM   7091 O  O   . HIS B 1 420 ? -18.347 -1.167  47.314  1.00 33.07  ? 420  HIS B O   1 
ATOM   7092 C  CB  . HIS B 1 420 ? -15.392 -0.611  47.804  1.00 31.58  ? 420  HIS B CB  1 
ATOM   7093 C  CG  . HIS B 1 420 ? -14.459 0.512   47.478  1.00 29.78  ? 420  HIS B CG  1 
ATOM   7094 N  ND1 . HIS B 1 420 ? -14.696 1.394   46.440  1.00 31.90  ? 420  HIS B ND1 1 
ATOM   7095 C  CD2 . HIS B 1 420 ? -13.309 0.923   48.067  1.00 29.80  ? 420  HIS B CD2 1 
ATOM   7096 C  CE1 . HIS B 1 420 ? -13.724 2.288   46.395  1.00 34.52  ? 420  HIS B CE1 1 
ATOM   7097 N  NE2 . HIS B 1 420 ? -12.870 2.024   47.370  1.00 32.57  ? 420  HIS B NE2 1 
ATOM   7098 N  N   . PHE B 1 421 ? -18.127 -1.928  49.427  1.00 29.89  ? 421  PHE B N   1 
ATOM   7099 C  CA  . PHE B 1 421 ? -19.129 -2.977  49.266  1.00 31.81  ? 421  PHE B CA  1 
ATOM   7100 C  C   . PHE B 1 421 ? -20.016 -3.075  50.499  1.00 33.47  ? 421  PHE B C   1 
ATOM   7101 O  O   . PHE B 1 421 ? -19.570 -2.817  51.617  1.00 31.84  ? 421  PHE B O   1 
ATOM   7102 C  CB  . PHE B 1 421 ? -18.481 -4.358  49.050  1.00 31.07  ? 421  PHE B CB  1 
ATOM   7103 C  CG  . PHE B 1 421 ? -17.517 -4.393  47.905  1.00 31.17  ? 421  PHE B CG  1 
ATOM   7104 C  CD1 . PHE B 1 421 ? -17.973 -4.596  46.610  1.00 32.11  ? 421  PHE B CD1 1 
ATOM   7105 C  CD2 . PHE B 1 421 ? -16.169 -4.172  48.113  1.00 30.06  ? 421  PHE B CD2 1 
ATOM   7106 C  CE1 . PHE B 1 421 ? -17.092 -4.606  45.535  1.00 31.61  ? 421  PHE B CE1 1 
ATOM   7107 C  CE2 . PHE B 1 421 ? -15.261 -4.165  47.033  1.00 29.18  ? 421  PHE B CE2 1 
ATOM   7108 C  CZ  . PHE B 1 421 ? -15.729 -4.393  45.746  1.00 31.98  ? 421  PHE B CZ  1 
ATOM   7109 N  N   . ASP B 1 422 ? -21.271 -3.482  50.280  1.00 32.18  ? 422  ASP B N   1 
ATOM   7110 C  CA  . ASP B 1 422 ? -22.077 -4.101  51.326  1.00 34.17  ? 422  ASP B CA  1 
ATOM   7111 C  C   . ASP B 1 422 ? -21.884 -5.610  51.233  1.00 34.46  ? 422  ASP B C   1 
ATOM   7112 O  O   . ASP B 1 422 ? -21.655 -6.154  50.149  1.00 38.87  ? 422  ASP B O   1 
ATOM   7113 C  CB  . ASP B 1 422 ? -23.563 -3.756  51.168  1.00 35.46  ? 422  ASP B CB  1 
ATOM   7114 C  CG  . ASP B 1 422 ? -23.860 -2.310  51.478  1.00 38.80  ? 422  ASP B CG  1 
ATOM   7115 O  OD1 . ASP B 1 422 ? -23.668 -1.912  52.640  1.00 40.68  ? 422  ASP B OD1 1 
ATOM   7116 O  OD2 . ASP B 1 422 ? -24.274 -1.575  50.556  1.00 46.03  ? 422  ASP B OD2 1 
ATOM   7117 N  N   . PHE B 1 423 ? -21.973 -6.293  52.365  1.00 32.37  ? 423  PHE B N   1 
ATOM   7118 C  CA  . PHE B 1 423 ? -21.684 -7.716  52.383  1.00 30.01  ? 423  PHE B CA  1 
ATOM   7119 C  C   . PHE B 1 423 ? -22.893 -8.504  52.856  1.00 34.89  ? 423  PHE B C   1 
ATOM   7120 O  O   . PHE B 1 423 ? -23.622 -8.059  53.750  1.00 38.06  ? 423  PHE B O   1 
ATOM   7121 C  CB  . PHE B 1 423 ? -20.468 -8.018  53.267  1.00 32.98  ? 423  PHE B CB  1 
ATOM   7122 C  CG  . PHE B 1 423 ? -19.180 -7.477  52.713  1.00 32.53  ? 423  PHE B CG  1 
ATOM   7123 C  CD1 . PHE B 1 423 ? -18.459 -8.208  51.782  1.00 34.73  ? 423  PHE B CD1 1 
ATOM   7124 C  CD2 . PHE B 1 423 ? -18.714 -6.223  53.085  1.00 34.27  ? 423  PHE B CD2 1 
ATOM   7125 C  CE1 . PHE B 1 423 ? -17.274 -7.716  51.255  1.00 34.37  ? 423  PHE B CE1 1 
ATOM   7126 C  CE2 . PHE B 1 423 ? -17.530 -5.725  52.567  1.00 35.13  ? 423  PHE B CE2 1 
ATOM   7127 C  CZ  . PHE B 1 423 ? -16.814 -6.467  51.637  1.00 31.89  ? 423  PHE B CZ  1 
ATOM   7128 N  N   . GLU B 1 424 ? -23.100 -9.673  52.248  1.00 32.87  ? 424  GLU B N   1 
ATOM   7129 C  CA  . GLU B 1 424 ? -24.226 -10.535 52.581  1.00 35.35  ? 424  GLU B CA  1 
ATOM   7130 C  C   . GLU B 1 424 ? -23.722 -11.925 52.934  1.00 35.07  ? 424  GLU B C   1 
ATOM   7131 O  O   . GLU B 1 424 ? -22.967 -12.530 52.170  1.00 34.95  ? 424  GLU B O   1 
ATOM   7132 C  CB  . GLU B 1 424 ? -25.233 -10.625 51.424  1.00 36.29  ? 424  GLU B CB  1 
ATOM   7133 C  CG  . GLU B 1 424 ? -26.411 -11.555 51.738  1.00 38.24  ? 424  GLU B CG  1 
ATOM   7134 C  CD  . GLU B 1 424 ? -27.269 -11.863 50.519  1.00 45.60  ? 424  GLU B CD  1 
ATOM   7135 O  OE1 . GLU B 1 424 ? -26.912 -11.430 49.406  1.00 47.75  ? 424  GLU B OE1 1 
ATOM   7136 O  OE2 . GLU B 1 424 ? -28.306 -12.539 50.680  1.00 49.84  ? 424  GLU B OE2 1 
ATOM   7137 N  N   . ASP B 1 425 ? -24.124 -12.414 54.102  1.00 32.05  ? 425  ASP B N   1 
ATOM   7138 C  CA  . ASP B 1 425 ? -23.860 -13.793 54.520  1.00 30.74  ? 425  ASP B CA  1 
ATOM   7139 C  C   . ASP B 1 425 ? -24.955 -14.673 53.912  1.00 34.21  ? 425  ASP B C   1 
ATOM   7140 O  O   . ASP B 1 425 ? -25.866 -15.167 54.584  1.00 32.70  ? 425  ASP B O   1 
ATOM   7141 C  CB  . ASP B 1 425 ? -23.806 -13.849 56.041  1.00 31.99  ? 425  ASP B CB  1 
ATOM   7142 C  CG  . ASP B 1 425 ? -23.712 -15.257 56.599  1.00 32.96  ? 425  ASP B CG  1 
ATOM   7143 O  OD1 . ASP B 1 425 ? -23.193 -16.163 55.927  1.00 32.88  ? 425  ASP B OD1 1 
ATOM   7144 O  OD2 . ASP B 1 425 ? -24.171 -15.437 57.746  1.00 32.63  ? 425  ASP B OD2 1 
ATOM   7145 N  N   . HIS B 1 426 ? -24.854 -14.848 52.592  1.00 35.57  ? 426  HIS B N   1 
ATOM   7146 C  CA  . HIS B 1 426 ? -25.948 -15.434 51.819  1.00 33.88  ? 426  HIS B CA  1 
ATOM   7147 C  C   . HIS B 1 426 ? -26.152 -16.922 52.093  1.00 37.83  ? 426  HIS B C   1 
ATOM   7148 O  O   . HIS B 1 426 ? -27.229 -17.447 51.782  1.00 36.68  ? 426  HIS B O   1 
ATOM   7149 C  CB  . HIS B 1 426 ? -25.712 -15.209 50.324  1.00 34.23  ? 426  HIS B CB  1 
ATOM   7150 C  CG  . HIS B 1 426 ? -24.518 -15.937 49.789  1.00 34.99  ? 426  HIS B CG  1 
ATOM   7151 N  ND1 . HIS B 1 426 ? -23.231 -15.659 50.205  1.00 35.25  ? 426  HIS B ND1 1 
ATOM   7152 C  CD2 . HIS B 1 426 ? -24.415 -16.933 48.878  1.00 36.50  ? 426  HIS B CD2 1 
ATOM   7153 C  CE1 . HIS B 1 426 ? -22.387 -16.451 49.568  1.00 35.88  ? 426  HIS B CE1 1 
ATOM   7154 N  NE2 . HIS B 1 426 ? -23.078 -17.236 48.757  1.00 35.47  ? 426  HIS B NE2 1 
ATOM   7155 N  N   . THR B 1 427 ? -25.169 -17.620 52.662  1.00 33.54  ? 427  THR B N   1 
ATOM   7156 C  CA  . THR B 1 427 ? -25.344 -19.031 52.999  1.00 32.59  ? 427  THR B CA  1 
ATOM   7157 C  C   . THR B 1 427 ? -25.634 -19.260 54.477  1.00 30.33  ? 427  THR B C   1 
ATOM   7158 O  O   . THR B 1 427 ? -25.766 -20.416 54.895  1.00 34.35  ? 427  THR B O   1 
ATOM   7159 C  CB  . THR B 1 427 ? -24.115 -19.857 52.608  1.00 34.12  ? 427  THR B CB  1 
ATOM   7160 O  OG1 . THR B 1 427 ? -23.022 -19.581 53.511  1.00 34.12  ? 427  THR B OG1 1 
ATOM   7161 C  CG2 . THR B 1 427 ? -23.707 -19.598 51.154  1.00 31.65  ? 427  THR B CG2 1 
ATOM   7162 N  N   . ASN B 1 428 ? -25.744 -18.203 55.277  1.00 30.62  ? 428  ASN B N   1 
ATOM   7163 C  CA  . ASN B 1 428 ? -25.792 -18.325 56.729  1.00 32.77  ? 428  ASN B CA  1 
ATOM   7164 C  C   . ASN B 1 428 ? -24.689 -19.270 57.204  1.00 33.31  ? 428  ASN B C   1 
ATOM   7165 O  O   . ASN B 1 428 ? -24.913 -20.308 57.835  1.00 34.63  ? 428  ASN B O   1 
ATOM   7166 C  CB  . ASN B 1 428 ? -27.174 -18.786 57.208  1.00 35.78  ? 428  ASN B CB  1 
ATOM   7167 C  CG  . ASN B 1 428 ? -27.317 -18.692 58.696  1.00 43.59  ? 428  ASN B CG  1 
ATOM   7168 O  OD1 . ASN B 1 428 ? -26.550 -17.997 59.354  1.00 41.12  ? 428  ASN B OD1 1 
ATOM   7169 N  ND2 . ASN B 1 428 ? -28.301 -19.391 59.245  1.00 48.27  ? 428  ASN B ND2 1 
ATOM   7170 N  N   . TYR B 1 429 ? -23.466 -18.861 56.892  1.00 28.60  ? 429  TYR B N   1 
ATOM   7171 C  CA  . TYR B 1 429 ? -22.298 -19.714 57.051  1.00 34.90  ? 429  TYR B CA  1 
ATOM   7172 C  C   . TYR B 1 429 ? -22.093 -20.162 58.497  1.00 32.50  ? 429  TYR B C   1 
ATOM   7173 O  O   . TYR B 1 429 ? -22.136 -19.349 59.430  1.00 32.50  ? 429  TYR B O   1 
ATOM   7174 C  CB  . TYR B 1 429 ? -21.081 -18.939 56.553  1.00 29.93  ? 429  TYR B CB  1 
ATOM   7175 C  CG  . TYR B 1 429 ? -19.742 -19.526 56.955  1.00 32.66  ? 429  TYR B CG  1 
ATOM   7176 C  CD1 . TYR B 1 429 ? -19.248 -20.669 56.332  1.00 33.04  ? 429  TYR B CD1 1 
ATOM   7177 C  CD2 . TYR B 1 429 ? -18.968 -18.916 57.941  1.00 30.51  ? 429  TYR B CD2 1 
ATOM   7178 C  CE1 . TYR B 1 429 ? -18.005 -21.204 56.693  1.00 30.53  ? 429  TYR B CE1 1 
ATOM   7179 C  CE2 . TYR B 1 429 ? -17.731 -19.435 58.307  1.00 31.88  ? 429  TYR B CE2 1 
ATOM   7180 C  CZ  . TYR B 1 429 ? -17.261 -20.583 57.677  1.00 32.54  ? 429  TYR B CZ  1 
ATOM   7181 O  OH  . TYR B 1 429 ? -16.023 -21.085 58.042  1.00 30.59  ? 429  TYR B OH  1 
ATOM   7182 N  N   . GLU B 1 430 ? -21.836 -21.463 58.686  1.00 29.15  ? 430  GLU B N   1 
ATOM   7183 C  CA  . GLU B 1 430 ? -21.512 -21.996 60.007  1.00 32.21  ? 430  GLU B CA  1 
ATOM   7184 C  C   . GLU B 1 430 ? -19.996 -22.005 60.182  1.00 32.10  ? 430  GLU B C   1 
ATOM   7185 O  O   . GLU B 1 430 ? -19.285 -22.662 59.414  1.00 32.06  ? 430  GLU B O   1 
ATOM   7186 C  CB  . GLU B 1 430 ? -22.062 -23.413 60.175  1.00 35.88  ? 430  GLU B CB  1 
ATOM   7187 C  CG  . GLU B 1 430 ? -21.731 -24.031 61.517  1.00 41.03  ? 430  GLU B CG  1 
ATOM   7188 C  CD  . GLU B 1 430 ? -22.426 -25.363 61.719  1.00 53.98  ? 430  GLU B CD  1 
ATOM   7189 O  OE1 . GLU B 1 430 ? -23.306 -25.697 60.893  1.00 61.52  ? 430  GLU B OE1 1 
ATOM   7190 O  OE2 . GLU B 1 430 ? -22.108 -26.059 62.708  1.00 64.47  ? 430  GLU B OE2 1 
ATOM   7191 N  N   . LEU B 1 431 ? -19.507 -21.294 61.193  1.00 31.09  ? 431  LEU B N   1 
ATOM   7192 C  CA  . LEU B 1 431 ? -18.066 -21.187 61.381  1.00 30.30  ? 431  LEU B CA  1 
ATOM   7193 C  C   . LEU B 1 431 ? -17.428 -22.568 61.458  1.00 32.90  ? 431  LEU B C   1 
ATOM   7194 O  O   . LEU B 1 431 ? -17.841 -23.423 62.252  1.00 33.96  ? 431  LEU B O   1 
ATOM   7195 C  CB  . LEU B 1 431 ? -17.742 -20.384 62.640  1.00 36.09  ? 431  LEU B CB  1 
ATOM   7196 C  CG  . LEU B 1 431 ? -16.254 -20.091 62.902  1.00 35.09  ? 431  LEU B CG  1 
ATOM   7197 C  CD1 . LEU B 1 431 ? -15.604 -19.406 61.708  1.00 32.59  ? 431  LEU B CD1 1 
ATOM   7198 C  CD2 . LEU B 1 431 ? -16.104 -19.241 64.172  1.00 35.78  ? 431  LEU B CD2 1 
ATOM   7199 N  N   . ASP B 1 432 ? -16.399 -22.762 60.633  1.00 30.82  ? 432  ASP B N   1 
ATOM   7200 C  CA  . ASP B 1 432 ? -15.636 -24.000 60.549  1.00 32.64  ? 432  ASP B CA  1 
ATOM   7201 C  C   . ASP B 1 432 ? -14.178 -23.566 60.508  1.00 28.70  ? 432  ASP B C   1 
ATOM   7202 O  O   . ASP B 1 432 ? -13.753 -22.937 59.532  1.00 32.29  ? 432  ASP B O   1 
ATOM   7203 C  CB  . ASP B 1 432 ? -16.038 -24.780 59.300  1.00 32.48  ? 432  ASP B CB  1 
ATOM   7204 C  CG  . ASP B 1 432 ? -15.334 -26.103 59.161  1.00 35.98  ? 432  ASP B CG  1 
ATOM   7205 O  OD1 . ASP B 1 432 ? -14.569 -26.494 60.058  1.00 36.60  ? 432  ASP B OD1 1 
ATOM   7206 O  OD2 . ASP B 1 432 ? -15.545 -26.751 58.110  1.00 38.79  ? 432  ASP B OD2 1 
ATOM   7207 N  N   . ILE B 1 433 ? -13.437 -23.825 61.585  1.00 31.06  ? 433  ILE B N   1 
ATOM   7208 C  CA  . ILE B 1 433 ? -12.089 -23.285 61.734  1.00 28.49  ? 433  ILE B CA  1 
ATOM   7209 C  C   . ILE B 1 433 ? -11.084 -24.373 61.378  1.00 33.09  ? 433  ILE B C   1 
ATOM   7210 O  O   . ILE B 1 433 ? -10.929 -25.363 62.105  1.00 31.65  ? 433  ILE B O   1 
ATOM   7211 C  CB  . ILE B 1 433 ? -11.849 -22.729 63.142  1.00 28.76  ? 433  ILE B CB  1 
ATOM   7212 C  CG1 . ILE B 1 433 ? -12.843 -21.603 63.465  1.00 31.15  ? 433  ILE B CG1 1 
ATOM   7213 C  CG2 . ILE B 1 433 ? -10.384 -22.224 63.261  1.00 29.45  ? 433  ILE B CG2 1 
ATOM   7214 C  CD1 . ILE B 1 433 ? -12.766 -21.131 64.916  1.00 31.79  ? 433  ILE B CD1 1 
ATOM   7215 N  N   . LYS B 1 434 ? -10.403 -24.181 60.244  1.00 31.23  ? 434  LYS B N   1 
ATOM   7216 C  CA  . LYS B 1 434 ? -9.368  -25.100 59.790  1.00 32.15  ? 434  LYS B CA  1 
ATOM   7217 C  C   . LYS B 1 434 ? -8.090  -24.819 60.557  1.00 30.34  ? 434  LYS B C   1 
ATOM   7218 O  O   . LYS B 1 434 ? -7.751  -23.660 60.812  1.00 31.38  ? 434  LYS B O   1 
ATOM   7219 C  CB  . LYS B 1 434 ? -9.115  -24.933 58.288  1.00 31.78  ? 434  LYS B CB  1 
ATOM   7220 C  CG  . LYS B 1 434 ? -8.077  -25.902 57.709  1.00 31.44  ? 434  LYS B CG  1 
ATOM   7221 C  CD  . LYS B 1 434 ? -7.996  -25.756 56.178  1.00 37.90  ? 434  LYS B CD  1 
ATOM   7222 C  CE  . LYS B 1 434 ? -6.887  -26.626 55.576  1.00 46.52  ? 434  LYS B CE  1 
ATOM   7223 N  NZ  . LYS B 1 434 ? -7.101  -28.074 55.882  1.00 45.53  ? 434  LYS B NZ  1 
ATOM   7224 N  N   . GLU B 1 435 ? -7.394  -25.879 60.947  1.00 29.54  ? 435  GLU B N   1 
ATOM   7225 C  CA  . GLU B 1 435 ? -6.166  -25.740 61.720  1.00 29.06  ? 435  GLU B CA  1 
ATOM   7226 C  C   . GLU B 1 435 ? -5.004  -26.208 60.866  1.00 29.61  ? 435  GLU B C   1 
ATOM   7227 O  O   . GLU B 1 435 ? -5.033  -27.326 60.344  1.00 32.52  ? 435  GLU B O   1 
ATOM   7228 C  CB  . GLU B 1 435 ? -6.250  -26.537 63.012  1.00 28.91  ? 435  GLU B CB  1 
ATOM   7229 C  CG  . GLU B 1 435 ? -7.375  -26.039 63.900  1.00 29.85  ? 435  GLU B CG  1 
ATOM   7230 C  CD  . GLU B 1 435 ? -7.164  -26.377 65.355  1.00 30.72  ? 435  GLU B CD  1 
ATOM   7231 O  OE1 . GLU B 1 435 ? -6.008  -26.662 65.745  1.00 30.71  ? 435  GLU B OE1 1 
ATOM   7232 O  OE2 . GLU B 1 435 ? -8.143  -26.328 66.112  1.00 30.00  ? 435  GLU B OE2 1 
ATOM   7233 N  N   . THR B 1 436 ? -4.015  -25.331 60.695  1.00 28.93  ? 436  THR B N   1 
ATOM   7234 C  CA  . THR B 1 436 ? -2.731  -25.612 60.050  1.00 30.98  ? 436  THR B CA  1 
ATOM   7235 C  C   . THR B 1 436 ? -1.610  -25.070 60.931  1.00 29.45  ? 436  THR B C   1 
ATOM   7236 O  O   . THR B 1 436 ? -0.726  -24.331 60.489  1.00 32.28  ? 436  THR B O   1 
ATOM   7237 C  CB  . THR B 1 436 ? -2.656  -25.016 58.642  1.00 30.28  ? 436  THR B CB  1 
ATOM   7238 O  OG1 . THR B 1 436 ? -2.858  -23.600 58.690  1.00 33.23  ? 436  THR B OG1 1 
ATOM   7239 C  CG2 . THR B 1 436 ? -3.731  -25.627 57.726  1.00 32.35  ? 436  THR B CG2 1 
ATOM   7240 N  N   . LEU B 1 437 ? -1.659  -25.438 62.210  1.00 29.12  ? 437  LEU B N   1 
ATOM   7241 C  CA  . LEU B 1 437 ? -0.974  -24.740 63.297  1.00 31.84  ? 437  LEU B CA  1 
ATOM   7242 C  C   . LEU B 1 437 ? -1.672  -23.398 63.539  1.00 35.33  ? 437  LEU B C   1 
ATOM   7243 O  O   . LEU B 1 437 ? -2.211  -23.169 64.637  1.00 32.29  ? 437  LEU B O   1 
ATOM   7244 C  CB  . LEU B 1 437 ? 0.531   -24.569 63.005  1.00 32.83  ? 437  LEU B CB  1 
ATOM   7245 C  CG  . LEU B 1 437 ? 1.317   -25.857 62.683  1.00 34.18  ? 437  LEU B CG  1 
ATOM   7246 C  CD1 . LEU B 1 437 ? 2.786   -25.534 62.583  1.00 35.94  ? 437  LEU B CD1 1 
ATOM   7247 C  CD2 . LEU B 1 437 ? 1.093   -26.939 63.757  1.00 32.05  ? 437  LEU B CD2 1 
ATOM   7248 N  N   . THR B 1 438 ? -1.687  -22.529 62.525  1.00 33.08  ? 438  THR B N   1 
ATOM   7249 C  CA  . THR B 1 438 ? -2.510  -21.316 62.504  1.00 30.44  ? 438  THR B CA  1 
ATOM   7250 C  C   . THR B 1 438 ? -3.994  -21.653 62.298  1.00 29.72  ? 438  THR B C   1 
ATOM   7251 O  O   . THR B 1 438 ? -4.355  -22.753 61.892  1.00 31.12  ? 438  THR B O   1 
ATOM   7252 C  CB  . THR B 1 438 ? -2.056  -20.386 61.387  1.00 34.57  ? 438  THR B CB  1 
ATOM   7253 O  OG1 . THR B 1 438 ? -2.098  -21.113 60.149  1.00 34.57  ? 438  THR B OG1 1 
ATOM   7254 C  CG2 . THR B 1 438 ? -0.629  -19.903 61.631  1.00 32.41  ? 438  THR B CG2 1 
ATOM   7255 N  N   . LEU B 1 439 ? -4.863  -20.671 62.560  1.00 30.10  ? 439  LEU B N   1 
ATOM   7256 C  CA  . LEU B 1 439 ? -6.310  -20.866 62.480  1.00 28.99  ? 439  LEU B CA  1 
ATOM   7257 C  C   . LEU B 1 439 ? -6.909  -19.994 61.392  1.00 31.16  ? 439  LEU B C   1 
ATOM   7258 O  O   . LEU B 1 439 ? -6.526  -18.831 61.239  1.00 31.65  ? 439  LEU B O   1 
ATOM   7259 C  CB  . LEU B 1 439 ? -6.997  -20.508 63.789  1.00 28.23  ? 439  LEU B CB  1 
ATOM   7260 C  CG  . LEU B 1 439 ? -6.454  -21.161 65.054  1.00 30.78  ? 439  LEU B CG  1 
ATOM   7261 C  CD1 . LEU B 1 439 ? -7.234  -20.685 66.272  1.00 29.08  ? 439  LEU B CD1 1 
ATOM   7262 C  CD2 . LEU B 1 439 ? -6.543  -22.661 64.897  1.00 29.43  ? 439  LEU B CD2 1 
ATOM   7263 N  N   . LYS B 1 440 ? -7.905  -20.532 60.677  1.00 28.87  ? 440  LYS B N   1 
ATOM   7264 C  CA  . LYS B 1 440 ? -8.542  -19.701 59.658  1.00 28.05  ? 440  LYS B CA  1 
ATOM   7265 C  C   . LYS B 1 440 ? -9.896  -20.310 59.334  1.00 33.02  ? 440  LYS B C   1 
ATOM   7266 O  O   . LYS B 1 440 ? -9.992  -21.545 59.282  1.00 32.69  ? 440  LYS B O   1 
ATOM   7267 C  CB  . LYS B 1 440 ? -7.665  -19.624 58.398  1.00 33.28  ? 440  LYS B CB  1 
ATOM   7268 C  CG  . LYS B 1 440 ? -8.081  -18.552 57.393  1.00 36.01  ? 440  LYS B CG  1 
ATOM   7269 C  CD  . LYS B 1 440 ? -7.167  -18.556 56.165  1.00 37.87  ? 440  LYS B CD  1 
ATOM   7270 C  CE  . LYS B 1 440 ? -5.707  -18.677 56.579  1.00 43.50  ? 440  LYS B CE  1 
ATOM   7271 N  NZ  . LYS B 1 440 ? -5.000  -19.739 55.820  1.00 49.64  ? 440  LYS B NZ  1 
ATOM   7272 N  N   . PRO B 1 441 ? -10.943 -19.511 59.114  1.00 32.00  ? 441  PRO B N   1 
ATOM   7273 C  CA  . PRO B 1 441 ? -12.205 -20.085 58.627  1.00 31.82  ? 441  PRO B CA  1 
ATOM   7274 C  C   . PRO B 1 441 ? -12.000 -20.852 57.326  1.00 30.51  ? 441  PRO B C   1 
ATOM   7275 O  O   . PRO B 1 441 ? -11.223 -20.444 56.448  1.00 32.34  ? 441  PRO B O   1 
ATOM   7276 C  CB  . PRO B 1 441 ? -13.104 -18.857 58.412  1.00 31.03  ? 441  PRO B CB  1 
ATOM   7277 C  CG  . PRO B 1 441 ? -12.546 -17.808 59.306  1.00 31.88  ? 441  PRO B CG  1 
ATOM   7278 C  CD  . PRO B 1 441 ? -11.040 -18.048 59.274  1.00 29.64  ? 441  PRO B CD  1 
ATOM   7279 N  N   . GLU B 1 442 ? -12.706 -21.972 57.215  1.00 31.47  ? 442  GLU B N   1 
ATOM   7280 C  CA  . GLU B 1 442 ? -12.807 -22.758 55.992  1.00 30.59  ? 442  GLU B CA  1 
ATOM   7281 C  C   . GLU B 1 442 ? -14.199 -22.645 55.386  1.00 29.53  ? 442  GLU B C   1 
ATOM   7282 O  O   . GLU B 1 442 ? -15.193 -22.717 56.104  1.00 31.13  ? 442  GLU B O   1 
ATOM   7283 C  CB  . GLU B 1 442 ? -12.533 -24.241 56.266  1.00 33.88  ? 442  GLU B CB  1 
ATOM   7284 C  CG  . GLU B 1 442 ? -12.250 -25.004 54.990  1.00 40.50  ? 442  GLU B CG  1 
ATOM   7285 C  CD  . GLU B 1 442 ? -11.897 -26.454 55.226  1.00 42.30  ? 442  GLU B CD  1 
ATOM   7286 O  OE1 . GLU B 1 442 ? -11.755 -26.872 56.395  1.00 42.90  ? 442  GLU B OE1 1 
ATOM   7287 O  OE2 . GLU B 1 442 ? -11.776 -27.177 54.225  1.00 53.01  ? 442  GLU B OE2 1 
ATOM   7288 N  N   . GLY B 1 443 ? -14.259 -22.489 54.065  1.00 30.91  ? 443  GLY B N   1 
ATOM   7289 C  CA  . GLY B 1 443 ? -15.533 -22.505 53.367  1.00 32.28  ? 443  GLY B CA  1 
ATOM   7290 C  C   . GLY B 1 443 ? -16.372 -21.269 53.565  1.00 34.95  ? 443  GLY B C   1 
ATOM   7291 O  O   . GLY B 1 443 ? -17.554 -21.275 53.213  1.00 33.45  ? 443  GLY B O   1 
ATOM   7292 N  N   . PHE B 1 444 ? -15.795 -20.220 54.136  1.00 30.94  ? 444  PHE B N   1 
ATOM   7293 C  CA  . PHE B 1 444 ? -16.495 -18.963 54.373  1.00 31.51  ? 444  PHE B CA  1 
ATOM   7294 C  C   . PHE B 1 444 ? -16.639 -18.224 53.053  1.00 32.28  ? 444  PHE B C   1 
ATOM   7295 O  O   . PHE B 1 444 ? -15.640 -17.900 52.410  1.00 30.87  ? 444  PHE B O   1 
ATOM   7296 C  CB  . PHE B 1 444 ? -15.721 -18.135 55.398  1.00 32.17  ? 444  PHE B CB  1 
ATOM   7297 C  CG  . PHE B 1 444 ? -16.330 -16.782 55.704  1.00 29.94  ? 444  PHE B CG  1 
ATOM   7298 C  CD1 . PHE B 1 444 ? -17.704 -16.597 55.705  1.00 29.98  ? 444  PHE B CD1 1 
ATOM   7299 C  CD2 . PHE B 1 444 ? -15.506 -15.690 56.003  1.00 29.92  ? 444  PHE B CD2 1 
ATOM   7300 C  CE1 . PHE B 1 444 ? -18.245 -15.348 56.002  1.00 30.46  ? 444  PHE B CE1 1 
ATOM   7301 C  CE2 . PHE B 1 444 ? -16.026 -14.457 56.282  1.00 30.70  ? 444  PHE B CE2 1 
ATOM   7302 C  CZ  . PHE B 1 444 ? -17.414 -14.278 56.279  1.00 31.83  ? 444  PHE B CZ  1 
ATOM   7303 N  N   . VAL B 1 445 ? -17.886 -17.978 52.641  1.00 31.16  ? 445  VAL B N   1 
ATOM   7304 C  CA  . VAL B 1 445 ? -18.201 -17.270 51.414  1.00 29.62  ? 445  VAL B CA  1 
ATOM   7305 C  C   . VAL B 1 445 ? -19.209 -16.179 51.753  1.00 32.46  ? 445  VAL B C   1 
ATOM   7306 O  O   . VAL B 1 445 ? -20.004 -16.310 52.691  1.00 31.19  ? 445  VAL B O   1 
ATOM   7307 C  CB  . VAL B 1 445 ? -18.763 -18.210 50.315  1.00 29.40  ? 445  VAL B CB  1 
ATOM   7308 C  CG1 . VAL B 1 445 ? -17.701 -19.219 49.887  1.00 34.63  ? 445  VAL B CG1 1 
ATOM   7309 C  CG2 . VAL B 1 445 ? -20.011 -18.931 50.813  1.00 34.66  ? 445  VAL B CG2 1 
ATOM   7310 N  N   . VAL B 1 446 ? -19.164 -15.097 50.979  1.00 29.50  ? 446  VAL B N   1 
ATOM   7311 C  CA  . VAL B 1 446 ? -20.099 -13.984 51.092  1.00 33.18  ? 446  VAL B CA  1 
ATOM   7312 C  C   . VAL B 1 446 ? -20.408 -13.493 49.683  1.00 33.22  ? 446  VAL B C   1 
ATOM   7313 O  O   . VAL B 1 446 ? -19.700 -13.801 48.721  1.00 32.81  ? 446  VAL B O   1 
ATOM   7314 C  CB  . VAL B 1 446 ? -19.540 -12.814 51.940  1.00 31.44  ? 446  VAL B CB  1 
ATOM   7315 C  CG1 . VAL B 1 446 ? -19.175 -13.266 53.346  1.00 33.11  ? 446  VAL B CG1 1 
ATOM   7316 C  CG2 . VAL B 1 446 ? -18.344 -12.156 51.230  1.00 33.76  ? 446  VAL B CG2 1 
ATOM   7317 N  N   . LYS B 1 447 ? -21.482 -12.718 49.565  1.00 31.36  ? 447  LYS B N   1 
ATOM   7318 C  CA  . LYS B 1 447 ? -21.731 -11.925 48.374  1.00 31.66  ? 447  LYS B CA  1 
ATOM   7319 C  C   . LYS B 1 447 ? -21.474 -10.458 48.697  1.00 34.02  ? 447  LYS B C   1 
ATOM   7320 O  O   . LYS B 1 447 ? -21.815 -9.973  49.786  1.00 34.47  ? 447  LYS B O   1 
ATOM   7321 C  CB  . LYS B 1 447 ? -23.165 -12.126 47.865  1.00 33.90  ? 447  LYS B CB  1 
ATOM   7322 C  CG  . LYS B 1 447 ? -23.406 -13.519 47.309  1.00 35.46  ? 447  LYS B CG  1 
ATOM   7323 C  CD  . LYS B 1 447 ? -24.830 -13.667 46.758  1.00 36.27  ? 447  LYS B CD  1 
ATOM   7324 C  CE  . LYS B 1 447 ? -24.960 -14.969 45.996  1.00 42.65  ? 447  LYS B CE  1 
ATOM   7325 N  NZ  . LYS B 1 447 ? -26.342 -15.141 45.460  1.00 45.93  ? 447  LYS B NZ  1 
ATOM   7326 N  N   . ALA B 1 448 ? -20.850 -9.756  47.764  1.00 32.10  ? 448  ALA B N   1 
ATOM   7327 C  CA  . ALA B 1 448 ? -20.578 -8.336  47.926  1.00 33.65  ? 448  ALA B CA  1 
ATOM   7328 C  C   . ALA B 1 448 ? -21.445 -7.575  46.938  1.00 43.41  ? 448  ALA B C   1 
ATOM   7329 O  O   . ALA B 1 448 ? -21.599 -7.994  45.785  1.00 48.09  ? 448  ALA B O   1 
ATOM   7330 C  CB  . ALA B 1 448 ? -19.094 -8.018  47.719  1.00 40.16  ? 448  ALA B CB  1 
ATOM   7331 N  N   . LYS B 1 449 ? -22.049 -6.492  47.398  1.00 39.03  ? 449  LYS B N   1 
ATOM   7332 C  CA  . LYS B 1 449 ? -22.815 -5.610  46.528  1.00 40.96  ? 449  LYS B CA  1 
ATOM   7333 C  C   . LYS B 1 449 ? -22.066 -4.288  46.478  1.00 35.95  ? 449  LYS B C   1 
ATOM   7334 O  O   . LYS B 1 449 ? -21.949 -3.604  47.501  1.00 36.06  ? 449  LYS B O   1 
ATOM   7335 C  CB  . LYS B 1 449 ? -24.241 -5.427  47.040  1.00 43.70  ? 449  LYS B CB  1 
ATOM   7336 C  CG  . LYS B 1 449 ? -25.209 -4.873  45.997  1.00 52.66  ? 449  LYS B CG  1 
ATOM   7337 C  CD  . LYS B 1 449 ? -26.452 -4.299  46.678  1.00 58.32  ? 449  LYS B CD  1 
ATOM   7338 C  CE  . LYS B 1 449 ? -27.114 -3.219  45.834  1.00 59.14  ? 449  LYS B CE  1 
ATOM   7339 N  NZ  . LYS B 1 449 ? -27.526 -2.057  46.685  1.00 65.33  ? 449  LYS B NZ  1 
ATOM   7340 N  N   . SER B 1 450 ? -21.543 -3.948  45.304  1.00 34.17  ? 450  SER B N   1 
ATOM   7341 C  CA  . SER B 1 450 ? -20.748 -2.737  45.155  1.00 33.92  ? 450  SER B CA  1 
ATOM   7342 C  C   . SER B 1 450 ? -21.548 -1.498  45.534  1.00 38.03  ? 450  SER B C   1 
ATOM   7343 O  O   . SER B 1 450 ? -22.717 -1.356  45.169  1.00 37.49  ? 450  SER B O   1 
ATOM   7344 C  CB  . SER B 1 450 ? -20.263 -2.604  43.714  1.00 33.92  ? 450  SER B CB  1 
ATOM   7345 O  OG  . SER B 1 450 ? -19.515 -1.414  43.536  1.00 34.74  ? 450  SER B OG  1 
ATOM   7346 N  N   . LYS B 1 451 ? -20.912 -0.593  46.270  1.00 32.49  ? 451  LYS B N   1 
ATOM   7347 C  CA  . LYS B 1 451 ? -21.471 0.740   46.464  1.00 35.87  ? 451  LYS B CA  1 
ATOM   7348 C  C   . LYS B 1 451 ? -21.128 1.671   45.311  1.00 37.91  ? 451  LYS B C   1 
ATOM   7349 O  O   . LYS B 1 451 ? -21.473 2.859   45.362  1.00 41.10  ? 451  LYS B O   1 
ATOM   7350 C  CB  . LYS B 1 451 ? -20.986 1.343   47.791  1.00 36.71  ? 451  LYS B CB  1 
ATOM   7351 C  CG  . LYS B 1 451 ? -21.317 0.495   49.008  1.00 35.93  ? 451  LYS B CG  1 
ATOM   7352 C  CD  . LYS B 1 451 ? -20.782 1.136   50.281  1.00 40.55  ? 451  LYS B CD  1 
ATOM   7353 C  CE  . LYS B 1 451 ? -21.286 0.412   51.511  1.00 40.79  ? 451  LYS B CE  1 
ATOM   7354 N  NZ  . LYS B 1 451 ? -22.697 0.786   51.798  1.00 51.48  ? 451  LYS B NZ  1 
ATOM   7355 N  N   . LYS B 1 452 ? -20.451 1.158   44.285  1.00 34.67  ? 452  LYS B N   1 
ATOM   7356 C  CA  . LYS B 1 452 ? -20.119 1.904   43.070  1.00 39.55  ? 452  LYS B CA  1 
ATOM   7357 C  C   . LYS B 1 452 ? -19.390 3.207   43.391  1.00 42.68  ? 452  LYS B C   1 
ATOM   7358 O  O   . LYS B 1 452 ? -19.748 4.291   42.920  1.00 40.20  ? 452  LYS B O   1 
ATOM   7359 C  CB  . LYS B 1 452 ? -21.378 2.161   42.235  1.00 42.66  ? 452  LYS B CB  1 
ATOM   7360 C  CG  . LYS B 1 452 ? -22.155 0.890   41.890  1.00 42.53  ? 452  LYS B CG  1 
ATOM   7361 C  CD  . LYS B 1 452 ? -21.391 -0.001  40.912  1.00 45.16  ? 452  LYS B CD  1 
ATOM   7362 C  CE  . LYS B 1 452 ? -22.208 -1.241  40.519  1.00 48.16  ? 452  LYS B CE  1 
ATOM   7363 N  NZ  . LYS B 1 452 ? -21.385 -2.278  39.812  1.00 51.55  ? 452  LYS B NZ  1 
ATOM   7364 N  N   . ILE B 1 453 ? -18.341 3.097   44.197  1.00 37.36  ? 453  ILE B N   1 
ATOM   7365 C  CA  . ILE B 1 453 ? -17.467 4.222   44.509  1.00 36.57  ? 453  ILE B CA  1 
ATOM   7366 C  C   . ILE B 1 453 ? -16.190 4.062   43.691  1.00 39.95  ? 453  ILE B C   1 
ATOM   7367 O  O   . ILE B 1 453 ? -15.513 3.028   43.822  1.00 35.87  ? 453  ILE B O   1 
ATOM   7368 C  CB  . ILE B 1 453 ? -17.154 4.296   46.011  1.00 37.16  ? 453  ILE B CB  1 
ATOM   7369 C  CG1 . ILE B 1 453 ? -18.458 4.435   46.799  1.00 38.57  ? 453  ILE B CG1 1 
ATOM   7370 C  CG2 . ILE B 1 453 ? -16.206 5.465   46.301  1.00 35.20  ? 453  ILE B CG2 1 
ATOM   7371 C  CD1 . ILE B 1 453 ? -18.281 4.377   48.307  1.00 41.13  ? 453  ILE B CD1 1 
ATOM   7372 N  N   . PRO B 1 454 ? -15.826 5.035   42.854  1.00 42.77  ? 454  PRO B N   1 
ATOM   7373 C  CA  . PRO B 1 454 ? -14.686 4.842   41.953  1.00 43.51  ? 454  PRO B CA  1 
ATOM   7374 C  C   . PRO B 1 454 ? -13.371 4.759   42.708  1.00 42.14  ? 454  PRO B C   1 
ATOM   7375 O  O   . PRO B 1 454 ? -13.205 5.327   43.792  1.00 41.08  ? 454  PRO B O   1 
ATOM   7376 C  CB  . PRO B 1 454 ? -14.725 6.087   41.052  1.00 45.77  ? 454  PRO B CB  1 
ATOM   7377 C  CG  . PRO B 1 454 ? -16.114 6.617   41.179  1.00 44.76  ? 454  PRO B CG  1 
ATOM   7378 C  CD  . PRO B 1 454 ? -16.527 6.302   42.586  1.00 45.21  ? 454  PRO B CD  1 
ATOM   7379 N  N   . LEU B 1 455 ? -12.437 4.029   42.110  1.00 41.65  ? 455  LEU B N   1 
ATOM   7380 C  CA  . LEU B 1 455 ? -11.067 3.948   42.586  1.00 43.69  ? 455  LEU B CA  1 
ATOM   7381 C  C   . LEU B 1 455 ? -10.208 4.972   41.850  1.00 46.03  ? 455  LEU B C   1 
ATOM   7382 O  O   . LEU B 1 455 ? -10.702 5.694   40.977  1.00 46.71  ? 455  LEU B O   1 
ATOM   7383 C  CB  . LEU B 1 455 ? -10.525 2.533   42.371  1.00 41.77  ? 455  LEU B CB  1 
ATOM   7384 C  CG  . LEU B 1 455 ? -10.996 1.498   43.387  1.00 39.50  ? 455  LEU B CG  1 
ATOM   7385 C  CD1 . LEU B 1 455 ? -10.675 0.110   42.881  1.00 37.61  ? 455  LEU B CD1 1 
ATOM   7386 C  CD2 . LEU B 1 455 ? -10.292 1.742   44.715  1.00 38.92  ? 455  LEU B CD2 1 
ATOM   7387 O  OXT . LEU B 1 455 ? -9.011  5.101   42.107  1.00 45.85  ? 455  LEU B OXT 1 
HETATM 7388 C  CHA . HEM C 2 .   ? -17.762 -14.186 9.048   1.00 27.44  ? 501  HEM A CHA 1 
HETATM 7389 C  CHB . HEM C 2 .   ? -12.976 -13.429 9.357   1.00 31.65  ? 501  HEM A CHB 1 
HETATM 7390 C  CHC . HEM C 2 .   ? -13.597 -11.202 13.702  1.00 28.17  ? 501  HEM A CHC 1 
HETATM 7391 C  CHD . HEM C 2 .   ? -18.335 -12.222 13.484  1.00 30.79  ? 501  HEM A CHD 1 
HETATM 7392 C  C1A . HEM C 2 .   ? -16.408 -14.148 8.782   1.00 27.59  ? 501  HEM A C1A 1 
HETATM 7393 C  C2A . HEM C 2 .   ? -15.838 -14.663 7.591   1.00 29.52  ? 501  HEM A C2A 1 
HETATM 7394 C  C3A . HEM C 2 .   ? -14.491 -14.465 7.675   1.00 27.10  ? 501  HEM A C3A 1 
HETATM 7395 C  C4A . HEM C 2 .   ? -14.231 -13.809 8.901   1.00 28.08  ? 501  HEM A C4A 1 
HETATM 7396 C  CMA . HEM C 2 .   ? -13.429 -14.835 6.653   1.00 28.24  ? 501  HEM A CMA 1 
HETATM 7397 C  CAA . HEM C 2 .   ? -16.577 -15.295 6.425   1.00 26.18  ? 501  HEM A CAA 1 
HETATM 7398 C  CBA . HEM C 2 .   ? -16.790 -16.799 6.637   1.00 27.62  ? 501  HEM A CBA 1 
HETATM 7399 C  CGA . HEM C 2 .   ? -17.380 -17.506 5.439   1.00 28.15  ? 501  HEM A CGA 1 
HETATM 7400 O  O1A . HEM C 2 .   ? -17.681 -18.722 5.590   1.00 29.69  ? 501  HEM A O1A 1 
HETATM 7401 O  O2A . HEM C 2 .   ? -17.536 -16.947 4.322   1.00 26.87  ? 501  HEM A O2A 1 
HETATM 7402 C  C1B . HEM C 2 .   ? -12.768 -12.741 10.567  1.00 30.80  ? 501  HEM A C1B 1 
HETATM 7403 C  C2B . HEM C 2 .   ? -11.487 -12.317 11.013  1.00 29.21  ? 501  HEM A C2B 1 
HETATM 7404 C  C3B . HEM C 2 .   ? -11.642 -11.684 12.221  1.00 29.32  ? 501  HEM A C3B 1 
HETATM 7405 C  C4B . HEM C 2 .   ? -13.075 -11.742 12.525  1.00 29.69  ? 501  HEM A C4B 1 
HETATM 7406 C  CMB . HEM C 2 .   ? -10.178 -12.518 10.258  1.00 27.77  ? 501  HEM A CMB 1 
HETATM 7407 C  CAB . HEM C 2 .   ? -10.655 -11.056 13.138  1.00 31.64  ? 501  HEM A CAB 1 
HETATM 7408 C  CBB . HEM C 2 .   ? -9.515  -10.519 12.678  1.00 30.50  ? 501  HEM A CBB 1 
HETATM 7409 C  C1C . HEM C 2 .   ? -14.952 -11.269 14.015  1.00 26.79  ? 501  HEM A C1C 1 
HETATM 7410 C  C2C . HEM C 2 .   ? -15.558 -10.715 15.160  1.00 31.24  ? 501  HEM A C2C 1 
HETATM 7411 C  C3C . HEM C 2 .   ? -16.909 -11.035 15.094  1.00 30.78  ? 501  HEM A C3C 1 
HETATM 7412 C  C4C . HEM C 2 .   ? -17.115 -11.731 13.878  1.00 28.78  ? 501  HEM A C4C 1 
HETATM 7413 C  CMC . HEM C 2 .   ? -14.832 -9.975  16.254  1.00 33.77  ? 501  HEM A CMC 1 
HETATM 7414 C  CAC . HEM C 2 .   ? -17.973 -10.656 16.045  1.00 30.40  ? 501  HEM A CAC 1 
HETATM 7415 C  CBC . HEM C 2 .   ? -17.888 -9.490  16.692  1.00 32.27  ? 501  HEM A CBC 1 
HETATM 7416 C  C1D . HEM C 2 .   ? -18.499 -12.847 12.246  1.00 29.94  ? 501  HEM A C1D 1 
HETATM 7417 C  C2D . HEM C 2 .   ? -19.816 -13.331 11.829  1.00 29.60  ? 501  HEM A C2D 1 
HETATM 7418 C  C3D . HEM C 2 .   ? -19.667 -13.865 10.609  1.00 28.92  ? 501  HEM A C3D 1 
HETATM 7419 C  C4D . HEM C 2 .   ? -18.240 -13.713 10.269  1.00 28.28  ? 501  HEM A C4D 1 
HETATM 7420 C  CMD . HEM C 2 .   ? -21.124 -13.226 12.599  1.00 28.44  ? 501  HEM A CMD 1 
HETATM 7421 C  CAD . HEM C 2 .   ? -20.802 -14.410 9.768   1.00 27.68  ? 501  HEM A CAD 1 
HETATM 7422 C  CBD . HEM C 2 .   ? -21.295 -13.199 8.942   1.00 29.88  ? 501  HEM A CBD 1 
HETATM 7423 C  CGD . HEM C 2 .   ? -22.505 -13.478 8.067   1.00 30.20  ? 501  HEM A CGD 1 
HETATM 7424 O  O1D . HEM C 2 .   ? -22.454 -14.378 7.201   1.00 28.59  ? 501  HEM A O1D 1 
HETATM 7425 O  O2D . HEM C 2 .   ? -23.554 -12.784 8.183   1.00 31.63  ? 501  HEM A O2D 1 
HETATM 7426 N  NA  . HEM C 2 .   ? -15.409 -13.637 9.596   1.00 28.39  ? 501  HEM A NA  1 
HETATM 7427 N  NB  . HEM C 2 .   ? -13.669 -12.402 11.510  1.00 27.12  ? 501  HEM A NB  1 
HETATM 7428 N  NC  . HEM C 2 .   ? -15.900 -11.884 13.259  1.00 29.48  ? 501  HEM A NC  1 
HETATM 7429 N  ND  . HEM C 2 .   ? -17.578 -13.125 11.305  1.00 25.29  ? 501  HEM A ND  1 
HETATM 7430 FE FE  . HEM C 2 .   ? -15.704 -12.761 11.386  1.00 29.72  ? 501  HEM A FE  1 
HETATM 7431 C  C1  . D0L D 3 .   ? -12.726 -30.494 1.782   1.00 37.12  ? 502  D0L A C1  1 
HETATM 7432 C  C2  . D0L D 3 .   ? -12.804 -30.682 3.159   1.00 36.49  ? 502  D0L A C2  1 
HETATM 7433 C  C15 . D0L D 3 .   ? -11.372 -24.565 6.538   1.00 40.77  ? 502  D0L A C15 1 
HETATM 7434 C  C14 . D0L D 3 .   ? -10.270 -26.125 8.016   1.00 41.01  ? 502  D0L A C14 1 
HETATM 7435 C  C7  . D0L D 3 .   ? -12.141 -29.707 4.106   1.00 34.50  ? 502  D0L A C7  1 
HETATM 7436 C  C12 . D0L D 3 .   ? -9.078  -27.351 6.319   1.00 37.44  ? 502  D0L A C12 1 
HETATM 7437 C  C10 . D0L D 3 .   ? -10.810 -26.898 4.549   1.00 34.36  ? 502  D0L A C10 1 
HETATM 7438 C  C3  . D0L D 3 .   ? -13.471 -31.795 3.665   1.00 40.95  ? 502  D0L A C3  1 
HETATM 7439 C  C13 . D0L D 3 .   ? -9.475  -27.402 7.791   1.00 39.63  ? 502  D0L A C13 1 
HETATM 7440 C  C11 . D0L D 3 .   ? -10.039 -26.337 5.700   1.00 33.92  ? 502  D0L A C11 1 
HETATM 7441 C  C6  . D0L D 3 .   ? -13.332 -31.400 0.910   1.00 39.43  ? 502  D0L A C6  1 
HETATM 7442 C  C8  . D0L D 3 .   ? -12.736 -28.302 3.993   1.00 32.47  ? 502  D0L A C8  1 
HETATM 7443 C  C5  . D0L D 3 .   ? -14.001 -32.509 1.417   1.00 39.38  ? 502  D0L A C5  1 
HETATM 7444 C  C9  . D0L D 3 .   ? -14.152 -28.329 4.482   1.00 34.78  ? 502  D0L A C9  1 
HETATM 7445 C  C4  . D0L D 3 .   ? -14.072 -32.700 2.797   1.00 42.98  ? 502  D0L A C4  1 
HETATM 7446 O  O2  . D0L D 3 .   ? -14.338 -28.088 5.705   1.00 33.12  ? 502  D0L A O2  1 
HETATM 7447 O  O3  . D0L D 3 .   ? -10.359 -26.850 3.409   1.00 34.67  ? 502  D0L A O3  1 
HETATM 7448 O  O1  . D0L D 3 .   ? -15.078 -28.607 3.692   1.00 34.79  ? 502  D0L A O1  1 
HETATM 7449 N  N2  . D0L D 3 .   ? -10.991 -25.966 6.756   1.00 37.55  ? 502  D0L A N2  1 
HETATM 7450 C  C16 . D0L D 3 .   ? -12.475 -24.205 7.507   1.00 45.00  ? 502  D0L A C16 1 
HETATM 7451 C  C17 . D0L D 3 .   ? -12.731 -22.709 7.471   1.00 46.89  ? 502  D0L A C17 1 
HETATM 7452 C  C18 . D0L D 3 .   ? -14.086 -22.413 8.098   1.00 52.15  ? 502  D0L A C18 1 
HETATM 7453 C  C19 . D0L D 3 .   ? -13.929 -22.001 9.553   1.00 47.03  ? 502  D0L A C19 1 
HETATM 7454 C  C20 . D0L D 3 .   ? -12.973 -20.825 9.672   1.00 47.02  ? 502  D0L A C20 1 
HETATM 7455 C  C21 . D0L D 3 .   ? -13.135 -20.161 11.020  1.00 46.06  ? 502  D0L A C21 1 
HETATM 7456 N  N1  . D0L D 3 .   ? -11.980 -27.438 4.871   1.00 34.68  ? 502  D0L A N1  1 
HETATM 7457 C  CAF . SYN E 4 .   ? -15.231 -18.143 13.329  0.81 37.62  ? 503  SYN A CAF 1 
HETATM 7458 C  CAD . SYN E 4 .   ? -14.444 -18.695 14.323  0.81 37.44  ? 503  SYN A CAD 1 
HETATM 7459 C  CAC . SYN E 4 .   ? -14.547 -20.034 14.624  0.81 39.25  ? 503  SYN A CAC 1 
HETATM 7460 C  CAE . SYN E 4 .   ? -15.447 -20.824 13.946  0.81 40.59  ? 503  SYN A CAE 1 
HETATM 7461 C  CAG . SYN E 4 .   ? -16.241 -20.277 12.952  0.81 38.53  ? 503  SYN A CAG 1 
HETATM 7462 C  CAH . SYN E 4 .   ? -16.149 -18.923 12.626  0.81 40.08  ? 503  SYN A CAH 1 
HETATM 7463 C  CAB . SYN E 4 .   ? -16.989 -18.329 11.573  0.81 36.79  ? 503  SYN A CAB 1 
HETATM 7464 C  CAA . SYN E 4 .   ? -16.820 -17.162 11.015  0.81 40.25  ? 503  SYN A CAA 1 
HETATM 7465 O  O1  . OXY F 5 .   ? -15.299 -14.439 12.233  0.75 32.72  ? 504  OXY A O1  1 
HETATM 7466 O  O2  . OXY F 5 .   ? -14.503 -14.762 13.133  0.75 27.84  ? 504  OXY A O2  1 
HETATM 7467 C  C1  . GOL G 6 .   ? -28.379 -15.523 -2.850  1.00 47.98  ? 505  GOL A C1  1 
HETATM 7468 O  O1  . GOL G 6 .   ? -27.317 -15.828 -3.782  1.00 42.23  ? 505  GOL A O1  1 
HETATM 7469 C  C2  . GOL G 6 .   ? -29.593 -16.409 -3.206  1.00 51.29  ? 505  GOL A C2  1 
HETATM 7470 O  O2  . GOL G 6 .   ? -29.683 -16.582 -4.558  1.00 56.01  ? 505  GOL A O2  1 
HETATM 7471 C  C3  . GOL G 6 .   ? -29.358 -17.687 -2.384  1.00 51.12  ? 505  GOL A C3  1 
HETATM 7472 O  O3  . GOL G 6 .   ? -30.433 -18.563 -2.691  1.00 57.38  ? 505  GOL A O3  1 
HETATM 7473 H  H11 . GOL G 6 .   ? -28.646 -14.591 -2.886  1.00 57.61  ? 505  GOL A H11 1 
HETATM 7474 H  H12 . GOL G 6 .   ? -28.124 -15.691 -1.930  1.00 57.61  ? 505  GOL A H12 1 
HETATM 7475 H  HO1 . GOL G 6 .   ? -27.469 -16.611 -4.094  1.00 50.70  ? 505  GOL A HO1 1 
HETATM 7476 H  H2  . GOL G 6 .   ? -30.447 -16.022 -2.957  1.00 61.57  ? 505  GOL A H2  1 
HETATM 7477 H  HO2 . GOL G 6 .   ? -29.715 -17.409 -4.701  1.00 67.24  ? 505  GOL A HO2 1 
HETATM 7478 H  H31 . GOL G 6 .   ? -29.306 -17.453 -1.443  1.00 61.37  ? 505  GOL A H31 1 
HETATM 7479 H  H32 . GOL G 6 .   ? -28.486 -18.050 -2.606  1.00 61.37  ? 505  GOL A H32 1 
HETATM 7480 H  HO3 . GOL G 6 .   ? -31.135 -18.082 -2.681  1.00 68.88  ? 505  GOL A HO3 1 
HETATM 7481 C  CHA . HEM H 2 .   ? 6.128   -14.105 66.077  1.00 29.14  ? 501  HEM B CHA 1 
HETATM 7482 C  CHB . HEM H 2 .   ? 1.301   -13.635 65.930  1.00 28.33  ? 501  HEM B CHB 1 
HETATM 7483 C  CHC . HEM H 2 .   ? 1.680   -11.265 61.631  1.00 30.05  ? 501  HEM B CHC 1 
HETATM 7484 C  CHD . HEM H 2 .   ? 6.486   -12.036 61.665  1.00 28.32  ? 501  HEM B CHD 1 
HETATM 7485 C  C1A . HEM H 2 .   ? 4.786   -14.146 66.391  1.00 27.87  ? 501  HEM B C1A 1 
HETATM 7486 C  C2A . HEM H 2 .   ? 4.288   -14.724 67.596  1.00 28.45  ? 501  HEM B C2A 1 
HETATM 7487 C  C3A . HEM H 2 .   ? 2.921   -14.597 67.554  1.00 26.76  ? 501  HEM B C3A 1 
HETATM 7488 C  C4A . HEM H 2 .   ? 2.594   -13.938 66.341  1.00 27.32  ? 501  HEM B C4A 1 
HETATM 7489 C  CMA . HEM H 2 .   ? 1.913   -15.026 68.596  1.00 27.07  ? 501  HEM B CMA 1 
HETATM 7490 C  CAA . HEM H 2 .   ? 5.108   -15.327 68.721  1.00 28.84  ? 501  HEM B CAA 1 
HETATM 7491 C  CBA . HEM H 2 .   ? 5.298   -16.825 68.494  1.00 28.27  ? 501  HEM B CBA 1 
HETATM 7492 C  CGA . HEM H 2 .   ? 6.009   -17.507 69.643  1.00 26.53  ? 501  HEM B CGA 1 
HETATM 7493 O  O1A . HEM H 2 .   ? 6.349   -18.697 69.443  1.00 28.17  ? 501  HEM B O1A 1 
HETATM 7494 O  O2A . HEM H 2 .   ? 6.267   -16.924 70.732  1.00 27.59  ? 501  HEM B O2A 1 
HETATM 7495 C  C1B . HEM H 2 .   ? 1.023   -12.930 64.738  1.00 28.13  ? 501  HEM B C1B 1 
HETATM 7496 C  C2B . HEM H 2 .   ? -0.301  -12.578 64.322  1.00 27.80  ? 501  HEM B C2B 1 
HETATM 7497 C  C3B . HEM H 2 .   ? -0.204  -11.909 63.137  1.00 25.45  ? 501  HEM B C3B 1 
HETATM 7498 C  C4B . HEM H 2 .   ? 1.222   -11.875 62.801  1.00 30.00  ? 501  HEM B C4B 1 
HETATM 7499 C  CMB . HEM H 2 .   ? -1.578  -12.868 65.082  1.00 28.14  ? 501  HEM B CMB 1 
HETATM 7500 C  CAB . HEM H 2 .   ? -1.238  -11.316 62.256  1.00 27.42  ? 501  HEM B CAB 1 
HETATM 7501 C  CBB . HEM H 2 .   ? -2.386  -10.831 62.729  1.00 30.22  ? 501  HEM B CBB 1 
HETATM 7502 C  C1C . HEM H 2 .   ? 3.031   -11.258 61.268  1.00 28.22  ? 501  HEM B C1C 1 
HETATM 7503 C  C2C . HEM H 2 .   ? 3.554   -10.642 60.123  1.00 31.12  ? 501  HEM B C2C 1 
HETATM 7504 C  C3C . HEM H 2 .   ? 4.930   -10.876 60.118  1.00 27.47  ? 501  HEM B C3C 1 
HETATM 7505 C  C4C . HEM H 2 .   ? 5.225   -11.596 61.316  1.00 30.43  ? 501  HEM B C4C 1 
HETATM 7506 C  CMC . HEM H 2 .   ? 2.713   -9.919  59.093  1.00 30.51  ? 501  HEM B CMC 1 
HETATM 7507 C  CAC . HEM H 2 .   ? 5.939   -10.430 59.130  1.00 29.78  ? 501  HEM B CAC 1 
HETATM 7508 C  CBC . HEM H 2 .   ? 5.875   -9.242  58.504  1.00 31.20  ? 501  HEM B CBC 1 
HETATM 7509 C  C1D . HEM H 2 .   ? 6.719   -12.683 62.887  1.00 28.77  ? 501  HEM B C1D 1 
HETATM 7510 C  C2D . HEM H 2 .   ? 8.078   -13.105 63.251  1.00 28.65  ? 501  HEM B C2D 1 
HETATM 7511 C  C3D . HEM H 2 .   ? 7.986   -13.664 64.477  1.00 29.18  ? 501  HEM B C3D 1 
HETATM 7512 C  C4D . HEM H 2 .   ? 6.555   -13.596 64.854  1.00 28.75  ? 501  HEM B C4D 1 
HETATM 7513 C  CMD . HEM H 2 .   ? 9.336   -12.912 62.417  1.00 28.73  ? 501  HEM B CMD 1 
HETATM 7514 C  CAD . HEM H 2 .   ? 9.129   -14.182 65.320  1.00 28.82  ? 501  HEM B CAD 1 
HETATM 7515 C  CBD . HEM H 2 .   ? 9.612   -12.966 66.145  1.00 30.33  ? 501  HEM B CBD 1 
HETATM 7516 C  CGD . HEM H 2 .   ? 10.871  -13.232 66.957  1.00 34.08  ? 501  HEM B CGD 1 
HETATM 7517 O  O1D . HEM H 2 .   ? 10.865  -14.122 67.824  1.00 30.01  ? 501  HEM B O1D 1 
HETATM 7518 O  O2D . HEM H 2 .   ? 11.913  -12.556 66.758  1.00 32.25  ? 501  HEM B O2D 1 
HETATM 7519 N  NA  . HEM H 2 .   ? 3.733   -13.682 65.611  1.00 29.85  ? 501  HEM B NA  1 
HETATM 7520 N  NB  . HEM H 2 .   ? 1.858   -12.526 63.779  1.00 27.61  ? 501  HEM B NB  1 
HETATM 7521 N  NC  . HEM H 2 .   ? 4.038   -11.837 61.977  1.00 29.41  ? 501  HEM B NC  1 
HETATM 7522 N  ND  . HEM H 2 .   ? 5.831   -13.021 63.854  1.00 26.33  ? 501  HEM B ND  1 
HETATM 7523 FE FE  . HEM H 2 .   ? 3.911   -12.762 63.831  1.00 29.14  ? 501  HEM B FE  1 
HETATM 7524 C  C1  . D0L I 3 .   ? 2.154   -30.951 73.276  1.00 38.37  ? 502  D0L B C1  1 
HETATM 7525 C  C2  . D0L I 3 .   ? 2.141   -31.119 71.892  1.00 37.00  ? 502  D0L B C2  1 
HETATM 7526 C  C15 . D0L I 3 .   ? 0.478   -24.887 68.734  1.00 40.44  ? 502  D0L B C15 1 
HETATM 7527 C  C14 . D0L I 3 .   ? -0.718  -26.381 67.188  1.00 42.52  ? 502  D0L B C14 1 
HETATM 7528 C  C7  . D0L I 3 .   ? 1.472   -30.104 70.983  1.00 35.47  ? 502  D0L B C7  1 
HETATM 7529 C  C12 . D0L I 3 .   ? -1.730  -27.823 68.854  1.00 39.40  ? 502  D0L B C12 1 
HETATM 7530 C  C10 . D0L I 3 .   ? -0.018  -27.367 70.602  1.00 33.35  ? 502  D0L B C10 1 
HETATM 7531 C  C3  . D0L I 3 .   ? 2.705   -32.267 71.339  1.00 38.52  ? 502  D0L B C3  1 
HETATM 7532 C  C13 . D0L I 3 .   ? -1.349  -27.756 67.368  1.00 40.56  ? 502  D0L B C13 1 
HETATM 7533 C  C11 . D0L I 3 .   ? -0.849  -26.774 69.508  1.00 32.72  ? 502  D0L B C11 1 
HETATM 7534 C  C6  . D0L I 3 .   ? 2.752   -31.922 74.087  1.00 38.79  ? 502  D0L B C6  1 
HETATM 7535 C  C8  . D0L I 3 .   ? 2.019   -28.677 71.073  1.00 33.40  ? 502  D0L B C8  1 
HETATM 7536 C  C5  . D0L I 3 .   ? 3.323   -33.064 73.534  1.00 37.31  ? 502  D0L B C5  1 
HETATM 7537 C  C9  . D0L I 3 .   ? 3.430   -28.625 70.543  1.00 33.76  ? 502  D0L B C9  1 
HETATM 7538 C  C4  . D0L I 3 .   ? 3.298   -33.237 72.153  1.00 41.31  ? 502  D0L B C4  1 
HETATM 7539 O  O2  . D0L I 3 .   ? 4.409   -28.887 71.286  1.00 34.32  ? 502  D0L B O2  1 
HETATM 7540 O  O3  . D0L I 3 .   ? -0.434  -27.392 71.757  1.00 33.35  ? 502  D0L B O3  1 
HETATM 7541 O  O1  . D0L I 3 .   ? 3.583   -28.307 69.346  1.00 32.40  ? 502  D0L B O1  1 
HETATM 7542 N  N2  . D0L I 3 .   ? 0.031   -26.264 68.430  1.00 36.90  ? 502  D0L B N2  1 
HETATM 7543 C  C16 . D0L I 3 .   ? 1.417   -24.382 67.650  1.00 44.18  ? 502  D0L B C16 1 
HETATM 7544 C  C17 . D0L I 3 .   ? 1.925   -22.983 67.962  1.00 48.22  ? 502  D0L B C17 1 
HETATM 7545 C  C18 . D0L I 3 .   ? 2.417   -22.278 66.701  1.00 50.83  ? 502  D0L B C18 1 
HETATM 7546 C  C19 . D0L I 3 .   ? 1.281   -21.454 66.120  1.00 42.94  ? 502  D0L B C19 1 
HETATM 7547 C  C20 . D0L I 3 .   ? 1.737   -20.617 64.929  1.00 44.46  ? 502  D0L B C20 1 
HETATM 7548 C  C21 . D0L I 3 .   ? 2.945   -21.257 64.296  1.00 51.34  ? 502  D0L B C21 1 
HETATM 7549 N  N1  . D0L I 3 .   ? 1.160   -27.860 70.229  1.00 31.79  ? 502  D0L B N1  1 
HETATM 7550 C  CAF . SYN J 4 .   ? 5.028   -20.110 62.146  0.87 42.95  ? 503  SYN B CAF 1 
HETATM 7551 C  CAD . SYN J 4 .   ? 4.304   -20.798 61.187  0.87 44.11  ? 503  SYN B CAD 1 
HETATM 7552 C  CAC . SYN J 4 .   ? 3.266   -20.180 60.528  0.87 37.45  ? 503  SYN B CAC 1 
HETATM 7553 C  CAE . SYN J 4 .   ? 2.952   -18.868 60.815  0.87 42.22  ? 503  SYN B CAE 1 
HETATM 7554 C  CAG . SYN J 4 .   ? 3.669   -18.176 61.777  0.87 38.44  ? 503  SYN B CAG 1 
HETATM 7555 C  CAH . SYN J 4 .   ? 4.727   -18.784 62.455  0.87 41.86  ? 503  SYN B CAH 1 
HETATM 7556 C  CAB . SYN J 4 .   ? 5.494   -18.055 63.478  0.87 37.97  ? 503  SYN B CAB 1 
HETATM 7557 C  CAA . SYN J 4 .   ? 5.093   -17.031 64.177  0.87 40.84  ? 503  SYN B CAA 1 
HETATM 7558 O  O1  . OXY K 5 .   ? 3.650   -14.455 62.933  0.80 31.65  ? 504  OXY B O1  1 
HETATM 7559 O  O2  . OXY K 5 .   ? 2.799   -14.793 62.085  0.80 31.55  ? 504  OXY B O2  1 
HETATM 7560 C  C1  . GOL L 6 .   ? -19.481 -7.246  43.252  1.00 49.78  ? 505  GOL B C1  1 
HETATM 7561 O  O1  . GOL L 6 .   ? -19.111 -8.470  43.910  1.00 44.11  ? 505  GOL B O1  1 
HETATM 7562 C  C2  . GOL L 6 .   ? -20.978 -7.242  42.861  1.00 56.92  ? 505  GOL B C2  1 
HETATM 7563 O  O2  . GOL L 6 .   ? -21.321 -5.985  42.297  1.00 58.25  ? 505  GOL B O2  1 
HETATM 7564 C  C3  . GOL L 6 .   ? -21.184 -8.393  41.877  1.00 53.73  ? 505  GOL B C3  1 
HETATM 7565 O  O3  . GOL L 6 .   ? -21.536 -7.806  40.634  1.00 55.23  ? 505  GOL B O3  1 
HETATM 7566 H  H11 . GOL L 6 .   ? -18.961 -7.102  42.445  1.00 59.77  ? 505  GOL B H11 1 
HETATM 7567 H  H12 . GOL L 6 .   ? -19.317 -6.473  43.815  1.00 59.77  ? 505  GOL B H12 1 
HETATM 7568 H  HO1 . GOL L 6 .   ? -19.797 -8.732  44.336  1.00 52.95  ? 505  GOL B HO1 1 
HETATM 7569 H  H2  . GOL L 6 .   ? -21.539 -7.389  43.639  1.00 68.33  ? 505  GOL B H2  1 
HETATM 7570 H  HO2 . GOL L 6 .   ? -20.699 -5.775  41.733  1.00 69.93  ? 505  GOL B HO2 1 
HETATM 7571 H  H31 . GOL L 6 .   ? -21.864 -8.990  42.227  1.00 64.50  ? 505  GOL B H31 1 
HETATM 7572 H  H32 . GOL L 6 .   ? -20.373 -8.923  41.837  1.00 64.50  ? 505  GOL B H32 1 
HETATM 7573 H  HO3 . GOL L 6 .   ? -22.197 -7.283  40.796  1.00 66.31  ? 505  GOL B HO3 1 
HETATM 7574 C  C1  . GOL M 6 .   ? 18.815  -16.882 76.958  1.00 51.55  ? 506  GOL B C1  1 
HETATM 7575 O  O1  . GOL M 6 .   ? 18.094  -17.888 76.318  1.00 51.43  ? 506  GOL B O1  1 
HETATM 7576 C  C2  . GOL M 6 .   ? 18.070  -16.516 78.242  1.00 51.05  ? 506  GOL B C2  1 
HETATM 7577 O  O2  . GOL M 6 .   ? 18.842  -15.734 79.078  1.00 52.03  ? 506  GOL B O2  1 
HETATM 7578 C  C3  . GOL M 6 .   ? 16.823  -15.797 77.713  1.00 46.70  ? 506  GOL B C3  1 
HETATM 7579 O  O3  . GOL M 6 .   ? 16.124  -15.399 78.828  1.00 43.14  ? 506  GOL B O3  1 
HETATM 7580 H  H11 . GOL M 6 .   ? 18.910  -16.087 76.410  1.00 61.88  ? 506  GOL B H11 1 
HETATM 7581 H  H12 . GOL M 6 .   ? 19.717  -17.158 77.184  1.00 61.88  ? 506  GOL B H12 1 
HETATM 7582 H  HO1 . GOL M 6 .   ? 17.401  -18.027 76.778  1.00 61.74  ? 506  GOL B HO1 1 
HETATM 7583 H  H2  . GOL M 6 .   ? 17.837  -17.293 78.775  1.00 61.29  ? 506  GOL B H2  1 
HETATM 7584 H  HO2 . GOL M 6 .   ? 19.288  -15.212 78.598  1.00 62.46  ? 506  GOL B HO2 1 
HETATM 7585 H  H31 . GOL M 6 .   ? 16.326  -16.399 77.137  1.00 56.06  ? 506  GOL B H31 1 
HETATM 7586 H  H32 . GOL M 6 .   ? 17.095  -15.062 77.142  1.00 56.06  ? 506  GOL B H32 1 
HETATM 7587 H  HO3 . GOL M 6 .   ? 15.740  -16.094 79.121  1.00 51.79  ? 506  GOL B HO3 1 
HETATM 7588 C  C1  . GOL N 6 .   ? 4.038   -8.708  74.151  1.00 52.01  ? 507  GOL B C1  1 
HETATM 7589 O  O1  . GOL N 6 .   ? 4.686   -8.111  75.285  1.00 42.50  ? 507  GOL B O1  1 
HETATM 7590 C  C2  . GOL N 6 .   ? 2.713   -7.939  73.821  1.00 49.35  ? 507  GOL B C2  1 
HETATM 7591 O  O2  . GOL N 6 .   ? 2.363   -7.059  74.788  1.00 59.53  ? 507  GOL B O2  1 
HETATM 7592 C  C3  . GOL N 6 .   ? 3.077   -7.274  72.444  1.00 55.58  ? 507  GOL B C3  1 
HETATM 7593 O  O3  . GOL N 6 .   ? 1.900   -6.982  71.733  1.00 53.07  ? 507  GOL B O3  1 
HETATM 7594 H  H11 . GOL N 6 .   ? 3.820   -9.640  74.308  1.00 62.43  ? 507  GOL B H11 1 
HETATM 7595 H  H12 . GOL N 6 .   ? 4.603   -8.696  73.363  1.00 62.43  ? 507  GOL B H12 1 
HETATM 7596 H  HO1 . GOL N 6 .   ? 4.169   -8.254  75.945  1.00 51.02  ? 507  GOL B HO1 1 
HETATM 7597 H  H2  . GOL N 6 .   ? 1.938   -8.519  73.757  1.00 59.24  ? 507  GOL B H2  1 
HETATM 7598 H  HO2 . GOL N 6 .   ? 2.045   -6.389  74.388  1.00 71.46  ? 507  GOL B HO2 1 
HETATM 7599 H  H31 . GOL N 6 .   ? 3.664   -7.879  71.965  1.00 66.72  ? 507  GOL B H31 1 
HETATM 7600 H  H32 . GOL N 6 .   ? 3.612   -6.486  72.624  1.00 66.72  ? 507  GOL B H32 1 
HETATM 7601 H  HO3 . GOL N 6 .   ? 1.308   -7.507  72.024  1.00 63.71  ? 507  GOL B HO3 1 
HETATM 7602 C  C1  . GOL O 6 .   ? -4.459  1.870   62.324  1.00 47.14  ? 508  GOL B C1  1 
HETATM 7603 O  O1  . GOL O 6 .   ? -3.176  2.179   62.861  1.00 52.50  ? 508  GOL B O1  1 
HETATM 7604 C  C2  . GOL O 6 .   ? -5.269  1.371   63.551  1.00 50.01  ? 508  GOL B C2  1 
HETATM 7605 O  O2  . GOL O 6 .   ? -6.495  2.021   63.722  1.00 49.93  ? 508  GOL B O2  1 
HETATM 7606 C  C3  . GOL O 6 .   ? -5.464  -0.138  63.269  1.00 33.79  ? 508  GOL B C3  1 
HETATM 7607 O  O3  . GOL O 6 .   ? -5.278  -0.858  64.473  1.00 60.17  ? 508  GOL B O3  1 
HETATM 7608 H  H11 . GOL O 6 .   ? -4.433  1.185   61.638  1.00 56.59  ? 508  GOL B H11 1 
HETATM 7609 H  H12 . GOL O 6 .   ? -4.900  2.634   61.919  1.00 56.59  ? 508  GOL B H12 1 
HETATM 7610 H  HO1 . GOL O 6 .   ? -2.641  2.206   62.211  1.00 63.02  ? 508  GOL B HO1 1 
HETATM 7611 H  H2  . GOL O 6 .   ? -4.776  1.547   64.367  1.00 60.04  ? 508  GOL B H2  1 
HETATM 7612 H  HO2 . GOL O 6 .   ? -6.848  2.095   62.967  1.00 59.95  ? 508  GOL B HO2 1 
HETATM 7613 H  H31 . GOL O 6 .   ? -4.842  -0.399  62.572  1.00 40.57  ? 508  GOL B H31 1 
HETATM 7614 H  H32 . GOL O 6 .   ? -6.346  -0.263  62.886  1.00 40.57  ? 508  GOL B H32 1 
HETATM 7615 H  HO3 . GOL O 6 .   ? -5.736  -0.467  65.068  1.00 72.23  ? 508  GOL B HO3 1 
HETATM 7616 O  O   . HOH P 7 .   ? -27.645 -23.365 -14.453 1.00 46.68  ? 601  HOH A O   1 
HETATM 7617 O  O   . HOH P 7 .   ? -11.295 1.575   14.246  1.00 46.46  ? 602  HOH A O   1 
HETATM 7618 O  O   . HOH P 7 .   ? -16.548 -7.048  6.474   1.00 42.10  ? 603  HOH A O   1 
HETATM 7619 O  O   . HOH P 7 .   ? -16.724 -26.925 -0.916  1.00 38.47  ? 604  HOH A O   1 
HETATM 7620 O  O   . HOH P 7 .   ? -8.575  9.682   26.109  1.00 46.42  ? 605  HOH A O   1 
HETATM 7621 O  O   . HOH P 7 .   ? 1.419   1.554   32.892  1.00 47.05  ? 606  HOH A O   1 
HETATM 7622 O  O   . HOH P 7 .   ? 1.229   7.589   11.568  1.00 52.39  ? 607  HOH A O   1 
HETATM 7623 O  O   . HOH P 7 .   ? 8.200   -21.109 22.843  1.00 47.03  ? 608  HOH A O   1 
HETATM 7624 O  O   . HOH P 7 .   ? -20.119 -31.908 14.592  1.00 53.96  ? 609  HOH A O   1 
HETATM 7625 O  O   . HOH P 7 .   ? -15.402 -35.141 6.047   1.00 48.99  ? 610  HOH A O   1 
HETATM 7626 O  O   . HOH P 7 .   ? 5.379   -17.553 -0.613  1.00 45.95  ? 611  HOH A O   1 
HETATM 7627 O  O   . HOH P 7 .   ? 9.829   -17.741 12.702  1.00 37.13  ? 612  HOH A O   1 
HETATM 7628 O  O   . HOH P 7 .   ? -13.540 -43.207 9.965   1.00 65.77  ? 613  HOH A O   1 
HETATM 7629 O  O   . HOH P 7 .   ? -6.098  -10.856 -12.402 1.00 42.47  ? 614  HOH A O   1 
HETATM 7630 O  O   . HOH P 7 .   ? -29.172 -18.728 -6.957  1.00 47.15  ? 615  HOH A O   1 
HETATM 7631 O  O   . HOH P 7 .   ? -22.117 -17.253 -15.722 1.00 50.57  ? 616  HOH A O   1 
HETATM 7632 O  O   . HOH P 7 .   ? -42.640 -7.846  15.184  1.00 46.44  ? 617  HOH A O   1 
HETATM 7633 O  O   . HOH P 7 .   ? -20.340 -15.550 6.489   1.00 29.06  ? 618  HOH A O   1 
HETATM 7634 O  O   . HOH P 7 .   ? -18.858 -29.995 -12.746 1.00 48.59  ? 619  HOH A O   1 
HETATM 7635 O  O   . HOH P 7 .   ? 9.368   0.039   21.169  1.00 46.73  ? 620  HOH A O   1 
HETATM 7636 O  O   . HOH P 7 .   ? -13.088 2.095   30.378  1.00 45.46  ? 621  HOH A O   1 
HETATM 7637 O  O   . HOH P 7 .   ? -4.826  -22.849 -14.540 1.00 46.94  ? 622  HOH A O   1 
HETATM 7638 O  O   . HOH P 7 .   ? -1.229  -22.673 26.436  1.00 47.45  ? 623  HOH A O   1 
HETATM 7639 O  O   . HOH P 7 .   ? 11.234  -16.363 31.285  1.00 53.26  ? 624  HOH A O   1 
HETATM 7640 O  O   . HOH P 7 .   ? 1.929   9.222   24.043  1.00 43.14  ? 625  HOH A O   1 
HETATM 7641 O  O   . HOH P 7 .   ? -30.498 -5.163  27.076  1.00 54.51  ? 626  HOH A O   1 
HETATM 7642 O  O   . HOH P 7 .   ? -33.976 -7.243  3.786   1.00 47.51  ? 627  HOH A O   1 
HETATM 7643 O  O   . HOH P 7 .   ? -32.955 -21.623 9.664   1.00 40.89  ? 628  HOH A O   1 
HETATM 7644 O  O   . HOH P 7 .   ? -13.842 -9.790  31.866  1.00 31.93  ? 629  HOH A O   1 
HETATM 7645 O  O   . HOH P 7 .   ? 1.082   -26.129 16.526  1.00 41.60  ? 630  HOH A O   1 
HETATM 7646 O  O   . HOH P 7 .   ? -22.051 -9.465  6.506   1.00 41.67  ? 631  HOH A O   1 
HETATM 7647 O  O   . HOH P 7 .   ? -4.521  -21.859 -17.114 1.00 56.92  ? 632  HOH A O   1 
HETATM 7648 O  O   . HOH P 7 .   ? 10.859  -15.314 21.972  1.00 34.76  ? 633  HOH A O   1 
HETATM 7649 O  O   . HOH P 7 .   ? -25.684 -20.064 -16.455 1.00 55.98  ? 634  HOH A O   1 
HETATM 7650 O  O   . HOH P 7 .   ? -13.111 -9.683  20.891  1.00 30.89  ? 635  HOH A O   1 
HETATM 7651 O  O   . HOH P 7 .   ? -8.715  13.109  24.451  1.00 55.10  ? 636  HOH A O   1 
HETATM 7652 O  O   . HOH P 7 .   ? -23.702 -10.195 8.480   1.00 39.44  ? 637  HOH A O   1 
HETATM 7653 O  O   . HOH P 7 .   ? 0.710   -21.815 23.038  1.00 38.01  ? 638  HOH A O   1 
HETATM 7654 O  O   . HOH P 7 .   ? -14.455 0.313   32.957  1.00 49.57  ? 639  HOH A O   1 
HETATM 7655 O  O   . HOH P 7 .   ? 6.418   -7.259  31.511  1.00 44.16  ? 640  HOH A O   1 
HETATM 7656 O  O   . HOH P 7 .   ? -23.779 -27.415 -3.683  1.00 53.90  ? 641  HOH A O   1 
HETATM 7657 O  O   . HOH P 7 .   ? -6.613  -4.806  36.469  1.00 34.70  ? 642  HOH A O   1 
HETATM 7658 O  O   . HOH P 7 .   ? 11.767  5.916   17.808  1.00 57.79  ? 643  HOH A O   1 
HETATM 7659 O  O   . HOH P 7 .   ? 11.200  -5.756  19.371  1.00 49.81  ? 644  HOH A O   1 
HETATM 7660 O  O   . HOH P 7 .   ? -12.507 -12.605 16.471  1.00 33.75  ? 645  HOH A O   1 
HETATM 7661 O  O   . HOH P 7 .   ? -9.554  12.286  22.072  1.00 42.53  ? 646  HOH A O   1 
HETATM 7662 O  O   . HOH P 7 .   ? -21.683 3.717   10.965  1.00 48.85  ? 647  HOH A O   1 
HETATM 7663 O  O   . HOH P 7 .   ? -3.642  -14.158 -10.204 1.00 34.31  ? 648  HOH A O   1 
HETATM 7664 O  O   . HOH P 7 .   ? 14.162  -10.519 12.584  1.00 46.93  ? 649  HOH A O   1 
HETATM 7665 O  O   . HOH P 7 .   ? -4.856  2.118   8.396   1.00 40.35  ? 650  HOH A O   1 
HETATM 7666 O  O   . HOH P 7 .   ? -25.861 -19.806 1.092   1.00 31.09  ? 651  HOH A O   1 
HETATM 7667 O  O   . HOH P 7 .   ? -33.247 -24.230 7.216   1.00 37.55  ? 652  HOH A O   1 
HETATM 7668 O  O   . HOH P 7 .   ? 7.947   -21.820 10.836  1.00 53.14  ? 653  HOH A O   1 
HETATM 7669 O  O   . HOH P 7 .   ? -10.157 -14.137 -14.350 1.00 41.29  ? 654  HOH A O   1 
HETATM 7670 O  O   . HOH P 7 .   ? -7.656  -7.038  40.325  1.00 32.78  ? 655  HOH A O   1 
HETATM 7671 O  O   . HOH P 7 .   ? -13.315 -15.092 -17.369 1.00 48.24  ? 656  HOH A O   1 
HETATM 7672 O  O   . HOH P 7 .   ? 8.960   -7.523  40.461  1.00 49.05  ? 657  HOH A O   1 
HETATM 7673 O  O   . HOH P 7 .   ? -7.733  -1.983  35.648  1.00 41.42  ? 658  HOH A O   1 
HETATM 7674 O  O   . HOH P 7 .   ? 9.223   -4.088  6.043   1.00 46.08  ? 659  HOH A O   1 
HETATM 7675 O  O   . HOH P 7 .   ? -13.291 -2.690  35.596  1.00 34.67  ? 660  HOH A O   1 
HETATM 7676 O  O   . HOH P 7 .   ? 2.575   -19.074 24.039  1.00 34.99  ? 661  HOH A O   1 
HETATM 7677 O  O   . HOH P 7 .   ? -24.463 -12.615 -13.549 1.00 42.52  ? 662  HOH A O   1 
HETATM 7678 O  O   . HOH P 7 .   ? -18.458 0.603   26.594  1.00 40.42  ? 663  HOH A O   1 
HETATM 7679 O  O   . HOH P 7 .   ? -2.603  -27.818 14.892  1.00 34.31  ? 664  HOH A O   1 
HETATM 7680 O  O   . HOH P 7 .   ? -23.205 -29.284 -9.090  1.00 48.79  ? 665  HOH A O   1 
HETATM 7681 O  O   . HOH P 7 .   ? 7.384   7.896   12.683  1.00 54.31  ? 666  HOH A O   1 
HETATM 7682 O  O   . HOH P 7 .   ? -34.459 -9.550  17.693  1.00 39.17  ? 667  HOH A O   1 
HETATM 7683 O  O   . HOH P 7 .   ? -20.314 -30.621 2.950   1.00 55.41  ? 668  HOH A O   1 
HETATM 7684 O  O   . HOH P 7 .   ? 3.615   -23.305 7.800   1.00 44.03  ? 669  HOH A O   1 
HETATM 7685 O  O   . HOH P 7 .   ? -3.796  -11.618 -3.688  1.00 33.26  ? 670  HOH A O   1 
HETATM 7686 O  O   . HOH P 7 .   ? -7.281  -20.159 22.167  1.00 51.88  ? 671  HOH A O   1 
HETATM 7687 O  O   . HOH P 7 .   ? 12.791  -7.534  18.029  1.00 43.22  ? 672  HOH A O   1 
HETATM 7688 O  O   . HOH P 7 .   ? 2.329   -21.427 0.497   1.00 43.06  ? 673  HOH A O   1 
HETATM 7689 O  O   . HOH P 7 .   ? -39.694 -14.178 16.164  1.00 43.99  ? 674  HOH A O   1 
HETATM 7690 O  O   . HOH P 7 .   ? -37.363 -16.582 11.891  1.00 41.20  ? 675  HOH A O   1 
HETATM 7691 O  O   . HOH P 7 .   ? -25.851 -25.021 20.701  1.00 44.93  ? 676  HOH A O   1 
HETATM 7692 O  O   . HOH P 7 .   ? -1.414  -34.080 4.295   1.00 41.79  ? 677  HOH A O   1 
HETATM 7693 O  O   . HOH P 7 .   ? 1.655   -8.700  -12.191 1.00 49.90  ? 678  HOH A O   1 
HETATM 7694 O  O   . HOH P 7 .   ? -8.243  -2.450  -2.269  1.00 37.98  ? 679  HOH A O   1 
HETATM 7695 O  O   . HOH P 7 .   ? -21.141 -8.968  -9.617  1.00 50.74  ? 680  HOH A O   1 
HETATM 7696 O  O   . HOH P 7 .   ? -3.063  -11.276 -11.110 1.00 48.48  ? 681  HOH A O   1 
HETATM 7697 O  O   . HOH P 7 .   ? -6.624  -43.933 -5.692  1.00 32.22  ? 682  HOH A O   1 
HETATM 7698 O  O   . HOH P 7 .   ? 8.417   -1.478  6.178   1.00 46.85  ? 683  HOH A O   1 
HETATM 7699 O  O   . HOH P 7 .   ? -21.984 1.938   25.709  1.00 51.94  ? 684  HOH A O   1 
HETATM 7700 O  O   . HOH P 7 .   ? -25.649 -24.246 -19.176 1.00 51.09  ? 685  HOH A O   1 
HETATM 7701 O  O   . HOH P 7 .   ? 4.220   1.737   30.526  1.00 37.49  ? 686  HOH A O   1 
HETATM 7702 O  O   . HOH P 7 .   ? 10.237  5.250   11.810  1.00 56.20  ? 687  HOH A O   1 
HETATM 7703 O  O   . HOH P 7 .   ? -25.173 -14.201 -3.909  1.00 35.06  ? 688  HOH A O   1 
HETATM 7704 O  O   . HOH P 7 .   ? -29.618 -20.859 -3.843  1.00 46.65  ? 689  HOH A O   1 
HETATM 7705 O  O   . HOH P 7 .   ? -26.149 -28.728 -11.712 1.00 45.97  ? 690  HOH A O   1 
HETATM 7706 O  O   . HOH P 7 .   ? -18.845 -29.598 -5.958  1.00 35.75  ? 691  HOH A O   1 
HETATM 7707 O  O   . HOH P 7 .   ? 8.446   -22.893 18.055  1.00 40.87  ? 692  HOH A O   1 
HETATM 7708 O  O   . HOH P 7 .   ? 6.461   9.462   18.380  1.00 43.17  ? 693  HOH A O   1 
HETATM 7709 O  O   . HOH P 7 .   ? -35.431 -16.440 27.658  1.00 65.50  ? 694  HOH A O   1 
HETATM 7710 O  O   . HOH P 7 .   ? 6.349   -14.807 5.885   1.00 47.29  ? 695  HOH A O   1 
HETATM 7711 O  O   . HOH P 7 .   ? -15.717 -10.212 29.768  1.00 29.08  ? 696  HOH A O   1 
HETATM 7712 O  O   . HOH P 7 .   ? -35.208 -10.570 6.391   1.00 38.16  ? 697  HOH A O   1 
HETATM 7713 O  O   . HOH P 7 .   ? -10.238 -10.329 33.220  1.00 30.22  ? 698  HOH A O   1 
HETATM 7714 O  O   . HOH P 7 .   ? -3.514  -25.406 -10.907 1.00 35.90  ? 699  HOH A O   1 
HETATM 7715 O  O   . HOH P 7 .   ? -22.528 0.417   21.387  1.00 41.81  ? 700  HOH A O   1 
HETATM 7716 O  O   . HOH P 7 .   ? -22.415 -6.898  -1.452  1.00 49.22  ? 701  HOH A O   1 
HETATM 7717 O  O   . HOH P 7 .   ? -2.507  4.641   27.537  1.00 39.52  ? 702  HOH A O   1 
HETATM 7718 O  O   . HOH P 7 .   ? 1.528   -35.780 1.960   1.00 48.23  ? 703  HOH A O   1 
HETATM 7719 O  O   . HOH P 7 .   ? -17.918 -20.688 3.729   1.00 29.00  ? 704  HOH A O   1 
HETATM 7720 O  O   . HOH P 7 .   ? -36.062 -11.010 20.188  1.00 46.24  ? 705  HOH A O   1 
HETATM 7721 O  O   . HOH P 7 .   ? -31.966 -4.015  15.428  1.00 46.05  ? 706  HOH A O   1 
HETATM 7722 O  O   . HOH P 7 .   ? -4.448  -0.435  6.219   1.00 42.21  ? 707  HOH A O   1 
HETATM 7723 O  O   . HOH P 7 .   ? 6.973   -0.217  21.567  1.00 38.69  ? 708  HOH A O   1 
HETATM 7724 O  O   . HOH P 7 .   ? -9.090  -4.780  6.405   1.00 39.66  ? 709  HOH A O   1 
HETATM 7725 O  O   . HOH P 7 .   ? -14.966 -17.204 -17.766 1.00 44.34  ? 710  HOH A O   1 
HETATM 7726 O  O   . HOH P 7 .   ? -11.007 -7.241  2.187   1.00 48.80  ? 711  HOH A O   1 
HETATM 7727 O  O   . HOH P 7 .   ? -0.323  -16.720 30.389  1.00 37.61  ? 712  HOH A O   1 
HETATM 7728 O  O   . HOH P 7 .   ? -23.104 -19.157 -11.545 1.00 42.06  ? 713  HOH A O   1 
HETATM 7729 O  O   . HOH P 7 .   ? -17.417 -38.996 14.335  1.00 56.60  ? 714  HOH A O   1 
HETATM 7730 O  O   . HOH P 7 .   ? -14.030 -27.291 -14.151 1.00 42.95  ? 715  HOH A O   1 
HETATM 7731 O  O   . HOH P 7 .   ? -31.997 -14.746 4.369   1.00 33.64  ? 716  HOH A O   1 
HETATM 7732 O  O   . HOH P 7 .   ? -9.513  -27.696 25.617  1.00 56.66  ? 717  HOH A O   1 
HETATM 7733 O  O   . HOH P 7 .   ? -6.523  -2.719  9.874   1.00 45.45  ? 718  HOH A O   1 
HETATM 7734 O  O   . HOH P 7 .   ? -17.519 -12.285 -12.725 1.00 46.76  ? 719  HOH A O   1 
HETATM 7735 O  O   . HOH P 7 .   ? -4.806  -37.581 -8.162  1.00 45.41  ? 720  HOH A O   1 
HETATM 7736 O  O   . HOH P 7 .   ? -0.957  0.553   -1.612  1.00 45.05  ? 721  HOH A O   1 
HETATM 7737 O  O   . HOH P 7 .   ? -2.181  8.926   34.627  1.00 56.55  ? 722  HOH A O   1 
HETATM 7738 O  O   . HOH P 7 .   ? 5.471   -20.402 28.898  1.00 50.45  ? 723  HOH A O   1 
HETATM 7739 O  O   . HOH P 7 .   ? -9.288  -14.682 7.722   1.00 30.42  ? 724  HOH A O   1 
HETATM 7740 O  O   . HOH P 7 .   ? -33.056 -21.003 15.323  1.00 40.96  ? 725  HOH A O   1 
HETATM 7741 O  O   . HOH P 7 .   ? 4.391   -16.635 -3.315  1.00 46.09  ? 726  HOH A O   1 
HETATM 7742 O  O   . HOH P 7 .   ? -9.987  10.467  14.549  1.00 45.47  ? 727  HOH A O   1 
HETATM 7743 O  O   . HOH P 7 .   ? -34.634 -22.016 12.669  1.00 50.13  ? 728  HOH A O   1 
HETATM 7744 O  O   . HOH P 7 .   ? -7.530  -25.480 10.257  1.00 33.30  ? 729  HOH A O   1 
HETATM 7745 O  O   . HOH P 7 .   ? -17.575 4.074   25.027  1.00 35.73  ? 730  HOH A O   1 
HETATM 7746 O  O   . HOH P 7 .   ? -23.315 -19.118 13.229  1.00 30.87  ? 731  HOH A O   1 
HETATM 7747 O  O   . HOH P 7 .   ? -13.895 -4.523  -5.183  1.00 39.22  ? 732  HOH A O   1 
HETATM 7748 O  O   . HOH P 7 .   ? -17.743 -14.432 3.158   1.00 28.97  ? 733  HOH A O   1 
HETATM 7749 O  O   . HOH P 7 .   ? 1.266   -14.511 29.769  1.00 32.68  ? 734  HOH A O   1 
HETATM 7750 O  O   . HOH P 7 .   ? 0.769   -31.025 1.616   1.00 37.04  ? 735  HOH A O   1 
HETATM 7751 O  O   . HOH P 7 .   ? -9.518  -1.668  33.413  1.00 36.87  ? 736  HOH A O   1 
HETATM 7752 O  O   . HOH P 7 .   ? 3.402   -24.382 11.594  1.00 34.18  ? 737  HOH A O   1 
HETATM 7753 O  O   . HOH P 7 .   ? -22.401 -4.021  27.425  1.00 41.60  ? 738  HOH A O   1 
HETATM 7754 O  O   . HOH P 7 .   ? -4.335  8.494   24.454  1.00 38.50  ? 739  HOH A O   1 
HETATM 7755 O  O   . HOH P 7 .   ? -26.395 -27.819 -14.156 1.00 47.94  ? 740  HOH A O   1 
HETATM 7756 O  O   . HOH P 7 .   ? 2.439   -24.838 4.138   1.00 43.69  ? 741  HOH A O   1 
HETATM 7757 O  O   . HOH P 7 .   ? 11.202  -17.853 28.250  1.00 48.13  ? 742  HOH A O   1 
HETATM 7758 O  O   . HOH P 7 .   ? -29.819 -10.873 0.632   1.00 45.83  ? 743  HOH A O   1 
HETATM 7759 O  O   . HOH P 7 .   ? 18.319  -18.994 17.713  1.00 47.25  ? 744  HOH A O   1 
HETATM 7760 O  O   . HOH P 7 .   ? -15.995 -22.354 5.127   1.00 32.89  ? 745  HOH A O   1 
HETATM 7761 O  O   . HOH P 7 .   ? -13.155 -8.202  33.911  1.00 31.09  ? 746  HOH A O   1 
HETATM 7762 O  O   . HOH P 7 .   ? -5.208  0.577   3.989   1.00 48.37  ? 747  HOH A O   1 
HETATM 7763 O  O   . HOH P 7 .   ? 11.230  -7.678  38.731  1.00 50.02  ? 748  HOH A O   1 
HETATM 7764 O  O   . HOH P 7 .   ? -24.874 -29.326 10.185  1.00 44.06  ? 749  HOH A O   1 
HETATM 7765 O  O   . HOH P 7 .   ? -5.133  -26.849 -15.246 1.00 54.27  ? 750  HOH A O   1 
HETATM 7766 O  O   . HOH P 7 .   ? 3.958   -13.467 37.621  1.00 42.10  ? 751  HOH A O   1 
HETATM 7767 O  O   . HOH P 7 .   ? -37.312 -20.154 20.037  1.00 49.36  ? 752  HOH A O   1 
HETATM 7768 O  O   . HOH P 7 .   ? -38.802 -17.077 21.409  1.00 48.30  ? 753  HOH A O   1 
HETATM 7769 O  O   . HOH P 7 .   ? -29.884 -3.146  9.240   1.00 46.56  ? 754  HOH A O   1 
HETATM 7770 O  O   . HOH P 7 .   ? 8.768   -12.120 6.665   1.00 51.99  ? 755  HOH A O   1 
HETATM 7771 O  O   . HOH P 7 .   ? -18.558 -17.981 1.815   1.00 28.59  ? 756  HOH A O   1 
HETATM 7772 O  O   . HOH P 7 .   ? -27.608 -14.098 -10.475 1.00 54.61  ? 757  HOH A O   1 
HETATM 7773 O  O   . HOH P 7 .   ? -3.200  -12.488 11.345  1.00 31.36  ? 758  HOH A O   1 
HETATM 7774 O  O   . HOH P 7 .   ? -7.164  0.328   12.199  1.00 39.63  ? 759  HOH A O   1 
HETATM 7775 O  O   . HOH P 7 .   ? -35.503 -13.168 6.184   1.00 37.71  ? 760  HOH A O   1 
HETATM 7776 O  O   . HOH P 7 .   ? -4.948  -0.229  -9.393  1.00 44.20  ? 761  HOH A O   1 
HETATM 7777 O  O   . HOH P 7 .   ? -16.437 -14.987 35.162  1.00 41.94  ? 762  HOH A O   1 
HETATM 7778 O  O   . HOH P 7 .   ? 5.032   6.453   12.620  1.00 45.59  ? 763  HOH A O   1 
HETATM 7779 O  O   . HOH P 7 .   ? -17.997 -29.058 -15.053 1.00 47.08  ? 764  HOH A O   1 
HETATM 7780 O  O   . HOH P 7 .   ? -5.003  -23.858 -5.393  1.00 34.03  ? 765  HOH A O   1 
HETATM 7781 O  O   . HOH P 7 .   ? 4.780   -18.085 5.021   1.00 42.92  ? 766  HOH A O   1 
HETATM 7782 O  O   . HOH P 7 .   ? -25.595 -10.497 30.554  1.00 48.02  ? 767  HOH A O   1 
HETATM 7783 O  O   . HOH P 7 .   ? 9.031   -13.104 -0.782  1.00 45.92  ? 768  HOH A O   1 
HETATM 7784 O  O   . HOH P 7 .   ? -2.189  -21.374 20.044  1.00 39.44  ? 769  HOH A O   1 
HETATM 7785 O  O   . HOH P 7 .   ? -9.953  -47.926 -1.003  1.00 54.46  ? 770  HOH A O   1 
HETATM 7786 O  O   . HOH P 7 .   ? -8.595  -22.162 19.137  1.00 42.19  ? 771  HOH A O   1 
HETATM 7787 O  O   . HOH P 7 .   ? -12.302 -9.677  3.111   1.00 29.99  ? 772  HOH A O   1 
HETATM 7788 O  O   . HOH P 7 .   ? -15.660 2.226   13.051  1.00 62.04  ? 773  HOH A O   1 
HETATM 7789 O  O   . HOH P 7 .   ? 2.950   -13.928 31.798  1.00 38.23  ? 774  HOH A O   1 
HETATM 7790 O  O   . HOH P 7 .   ? -18.535 -2.601  33.861  1.00 52.67  ? 775  HOH A O   1 
HETATM 7791 O  O   . HOH P 7 .   ? -31.232 -2.973  29.656  1.00 75.02  ? 776  HOH A O   1 
HETATM 7792 O  O   . HOH P 7 .   ? 6.306   -2.391  35.039  1.00 42.57  ? 777  HOH A O   1 
HETATM 7793 O  O   . HOH P 7 .   ? -27.479 -7.922  1.786   1.00 43.85  ? 778  HOH A O   1 
HETATM 7794 O  O   . HOH P 7 .   ? -22.009 -13.082 -0.491  1.00 31.73  ? 779  HOH A O   1 
HETATM 7795 O  O   . HOH P 7 .   ? -35.215 -19.902 15.081  1.00 46.66  ? 780  HOH A O   1 
HETATM 7796 O  O   . HOH P 7 .   ? -16.496 6.716   22.353  1.00 42.87  ? 781  HOH A O   1 
HETATM 7797 O  O   . HOH P 7 .   ? -19.528 -14.694 -4.336  1.00 32.63  ? 782  HOH A O   1 
HETATM 7798 O  O   . HOH P 7 .   ? -7.052  -8.000  35.689  1.00 31.90  ? 783  HOH A O   1 
HETATM 7799 O  O   . HOH P 7 .   ? -36.024 -2.583  15.909  1.00 50.28  ? 784  HOH A O   1 
HETATM 7800 O  O   . HOH P 7 .   ? -14.431 -28.829 -12.005 1.00 42.10  ? 785  HOH A O   1 
HETATM 7801 O  O   . HOH P 7 .   ? -22.391 -28.213 0.820   1.00 48.97  ? 786  HOH A O   1 
HETATM 7802 O  O   . HOH P 7 .   ? 10.323  -2.882  21.352  1.00 40.38  ? 787  HOH A O   1 
HETATM 7803 O  O   . HOH P 7 .   ? -0.511  3.679   36.182  1.00 55.67  ? 788  HOH A O   1 
HETATM 7804 O  O   . HOH P 7 .   ? 5.784   4.135   22.000  1.00 39.80  ? 789  HOH A O   1 
HETATM 7805 O  O   . HOH P 7 .   ? -26.386 -30.658 17.598  1.00 52.22  ? 790  HOH A O   1 
HETATM 7806 O  O   . HOH P 7 .   ? -10.854 -37.314 -10.255 1.00 57.18  ? 791  HOH A O   1 
HETATM 7807 O  O   . HOH P 7 .   ? -15.391 -31.707 21.625  1.00 51.97  ? 792  HOH A O   1 
HETATM 7808 O  O   . HOH P 7 .   ? 9.826   -8.974  6.573   1.00 40.34  ? 793  HOH A O   1 
HETATM 7809 O  O   . HOH P 7 .   ? -28.664 -15.920 11.355  1.00 29.81  ? 794  HOH A O   1 
HETATM 7810 O  O   . HOH P 7 .   ? -3.842  12.543  19.423  1.00 40.36  ? 795  HOH A O   1 
HETATM 7811 O  O   . HOH P 7 .   ? -7.287  -17.253 15.294  1.00 36.85  ? 796  HOH A O   1 
HETATM 7812 O  O   . HOH P 7 .   ? 2.906   -5.389  -2.684  1.00 39.86  ? 797  HOH A O   1 
HETATM 7813 O  O   . HOH P 7 .   ? -16.223 -6.707  -7.652  1.00 40.91  ? 798  HOH A O   1 
HETATM 7814 O  O   . HOH P 7 .   ? 5.326   5.673   24.303  1.00 41.13  ? 799  HOH A O   1 
HETATM 7815 O  O   . HOH P 7 .   ? -17.896 -4.752  12.802  1.00 41.91  ? 800  HOH A O   1 
HETATM 7816 O  O   . HOH P 7 .   ? 3.234   0.695   -1.212  1.00 53.71  ? 801  HOH A O   1 
HETATM 7817 O  O   . HOH P 7 .   ? -1.417  -22.155 -11.520 1.00 44.21  ? 802  HOH A O   1 
HETATM 7818 O  O   . HOH P 7 .   ? -8.636  -14.981 -16.617 1.00 46.78  ? 803  HOH A O   1 
HETATM 7819 O  O   . HOH P 7 .   ? 7.520   -16.487 9.431   1.00 51.57  ? 804  HOH A O   1 
HETATM 7820 O  O   . HOH P 7 .   ? -10.112 -4.667  24.221  1.00 31.79  ? 805  HOH A O   1 
HETATM 7821 O  O   . HOH P 7 .   ? 11.997  -1.507  17.409  1.00 44.68  ? 806  HOH A O   1 
HETATM 7822 O  O   . HOH P 7 .   ? -17.305 -33.278 3.250   1.00 46.49  ? 807  HOH A O   1 
HETATM 7823 O  O   . HOH P 7 .   ? -29.818 -14.604 -7.600  1.00 56.52  ? 808  HOH A O   1 
HETATM 7824 O  O   . HOH P 7 .   ? -22.602 -0.255  23.939  1.00 48.33  ? 809  HOH A O   1 
HETATM 7825 O  O   . HOH P 7 .   ? -15.424 -20.215 6.474   1.00 32.08  ? 810  HOH A O   1 
HETATM 7826 O  O   . HOH P 7 .   ? -24.301 -14.132 -1.423  1.00 34.63  ? 811  HOH A O   1 
HETATM 7827 O  O   . HOH P 7 .   ? -15.097 -44.268 22.092  1.00 62.72  ? 812  HOH A O   1 
HETATM 7828 O  O   . HOH P 7 .   ? -11.895 -5.909  -3.831  1.00 34.58  ? 813  HOH A O   1 
HETATM 7829 O  O   . HOH P 7 .   ? -12.571 -0.439  13.105  1.00 44.06  ? 814  HOH A O   1 
HETATM 7830 O  O   . HOH P 7 .   ? -9.021  -4.891  -3.503  1.00 39.05  ? 815  HOH A O   1 
HETATM 7831 O  O   . HOH P 7 .   ? -0.329  -16.084 33.195  1.00 41.48  ? 816  HOH A O   1 
HETATM 7832 O  O   . HOH P 7 .   ? 14.499  -11.906 16.840  1.00 43.56  ? 817  HOH A O   1 
HETATM 7833 O  O   . HOH P 7 .   ? 2.671   -16.627 -6.821  1.00 40.12  ? 818  HOH A O   1 
HETATM 7834 O  O   . HOH P 7 .   ? 13.886  -8.811  20.127  1.00 40.94  ? 819  HOH A O   1 
HETATM 7835 O  O   . HOH P 7 .   ? -1.248  -17.714 -5.279  1.00 44.60  ? 820  HOH A O   1 
HETATM 7836 O  O   . HOH P 7 .   ? -27.690 -23.810 -0.844  1.00 40.40  ? 821  HOH A O   1 
HETATM 7837 O  O   . HOH P 7 .   ? -5.515  -22.336 16.445  1.00 36.59  ? 822  HOH A O   1 
HETATM 7838 O  O   . HOH P 7 .   ? -13.835 7.701   23.203  1.00 41.73  ? 823  HOH A O   1 
HETATM 7839 O  O   . HOH P 7 .   ? 6.657   -5.558  37.947  1.00 42.88  ? 824  HOH A O   1 
HETATM 7840 O  O   . HOH P 7 .   ? 7.591   -9.597  30.121  1.00 40.97  ? 825  HOH A O   1 
HETATM 7841 O  O   . HOH P 7 .   ? 10.459  -20.434 21.616  1.00 42.14  ? 826  HOH A O   1 
HETATM 7842 O  O   . HOH P 7 .   ? -12.515 -28.338 -16.123 1.00 47.33  ? 827  HOH A O   1 
HETATM 7843 O  O   . HOH P 7 .   ? -5.922  13.612  21.045  1.00 43.60  ? 828  HOH A O   1 
HETATM 7844 O  O   . HOH P 7 .   ? -17.815 -8.998  -3.907  1.00 42.46  ? 829  HOH A O   1 
HETATM 7845 O  O   . HOH P 7 .   ? 8.950   -11.406 9.124   1.00 40.02  ? 830  HOH A O   1 
HETATM 7846 O  O   . HOH P 7 .   ? -9.697  -41.972 -5.658  1.00 49.80  ? 831  HOH A O   1 
HETATM 7847 O  O   . HOH P 7 .   ? -11.347 -34.874 18.824  1.00 52.32  ? 832  HOH A O   1 
HETATM 7848 O  O   . HOH P 7 .   ? -19.442 -28.652 1.858   1.00 45.38  ? 833  HOH A O   1 
HETATM 7849 O  O   . HOH P 7 .   ? -27.761 -27.517 15.179  1.00 47.71  ? 834  HOH A O   1 
HETATM 7850 O  O   . HOH P 7 .   ? -20.431 -9.276  -6.768  1.00 41.68  ? 835  HOH A O   1 
HETATM 7851 O  O   . HOH P 7 .   ? -16.133 -37.636 -4.763  1.00 47.95  ? 836  HOH A O   1 
HETATM 7852 O  O   . HOH P 7 .   ? 14.003  -14.985 13.502  1.00 51.34  ? 837  HOH A O   1 
HETATM 7853 O  O   . HOH P 7 .   ? 0.726   -10.165 36.217  1.00 33.25  ? 838  HOH A O   1 
HETATM 7854 O  O   . HOH P 7 .   ? -6.142  -18.040 27.299  1.00 43.51  ? 839  HOH A O   1 
HETATM 7855 O  O   . HOH P 7 .   ? -26.571 -8.324  31.496  1.00 48.69  ? 840  HOH A O   1 
HETATM 7856 O  O   . HOH P 7 .   ? -19.762 -14.263 -1.538  1.00 29.35  ? 841  HOH A O   1 
HETATM 7857 O  O   . HOH P 7 .   ? -34.405 -19.719 8.900   1.00 38.37  ? 842  HOH A O   1 
HETATM 7858 O  O   . HOH P 7 .   ? 14.847  -20.927 18.135  1.00 53.91  ? 843  HOH A O   1 
HETATM 7859 O  O   . HOH P 7 .   ? -22.846 -33.049 11.712  1.00 59.70  ? 844  HOH A O   1 
HETATM 7860 O  O   . HOH P 7 .   ? 10.727  -21.561 19.023  1.00 41.51  ? 845  HOH A O   1 
HETATM 7861 O  O   . HOH P 7 .   ? -2.947  -33.837 -11.111 1.00 44.43  ? 846  HOH A O   1 
HETATM 7862 O  O   . HOH P 7 .   ? -8.538  -5.386  -10.381 1.00 31.65  ? 847  HOH A O   1 
HETATM 7863 O  O   . HOH P 7 .   ? 13.639  -18.873 14.789  1.00 48.46  ? 848  HOH A O   1 
HETATM 7864 O  O   . HOH P 7 .   ? -19.891 -32.245 -3.607  1.00 46.10  ? 849  HOH A O   1 
HETATM 7865 O  O   . HOH P 7 .   ? -35.609 -15.861 14.594  1.00 40.74  ? 850  HOH A O   1 
HETATM 7866 O  O   . HOH P 7 .   ? -0.234  -28.387 15.869  1.00 42.55  ? 851  HOH A O   1 
HETATM 7867 O  O   . HOH P 7 .   ? -3.882  -13.999 33.949  1.00 38.23  ? 852  HOH A O   1 
HETATM 7868 O  O   . HOH P 7 .   ? 6.194   -25.714 -0.623  1.00 55.52  ? 853  HOH A O   1 
HETATM 7869 O  O   . HOH P 7 .   ? 2.892   -35.390 -1.667  1.00 49.53  ? 854  HOH A O   1 
HETATM 7870 O  O   . HOH P 7 .   ? -7.908  -17.424 31.262  1.00 40.28  ? 855  HOH A O   1 
HETATM 7871 O  O   . HOH P 7 .   ? 5.252   -16.226 7.997   1.00 43.90  ? 856  HOH A O   1 
HETATM 7872 O  O   . HOH P 7 .   ? -19.002 -6.550  1.698   1.00 52.07  ? 857  HOH A O   1 
HETATM 7873 O  O   . HOH P 7 .   ? -16.112 -31.211 -12.013 1.00 44.97  ? 858  HOH A O   1 
HETATM 7874 O  O   . HOH P 7 .   ? -19.275 -18.170 -17.844 1.00 47.46  ? 859  HOH A O   1 
HETATM 7875 O  O   . HOH P 7 .   ? -16.241 -8.163  -0.180  1.00 39.92  ? 860  HOH A O   1 
HETATM 7876 O  O   . HOH P 7 .   ? 11.068  -8.587  31.111  1.00 50.75  ? 861  HOH A O   1 
HETATM 7877 O  O   . HOH P 7 .   ? 12.254  -4.163  10.159  1.00 47.91  ? 862  HOH A O   1 
HETATM 7878 O  O   . HOH P 7 .   ? -0.244  -34.845 -3.795  1.00 39.33  ? 863  HOH A O   1 
HETATM 7879 O  O   . HOH P 7 .   ? -0.780  -5.672  -8.520  1.00 52.63  ? 864  HOH A O   1 
HETATM 7880 O  O   . HOH P 7 .   ? -9.407  -7.150  -1.995  1.00 35.78  ? 865  HOH A O   1 
HETATM 7881 O  O   . HOH P 7 .   ? 4.156   -28.449 16.463  1.00 60.97  ? 866  HOH A O   1 
HETATM 7882 O  O   . HOH P 7 .   ? 11.586  -13.588 38.323  1.00 59.58  ? 867  HOH A O   1 
HETATM 7883 O  O   . HOH P 7 .   ? -26.837 -27.353 19.831  1.00 51.75  ? 868  HOH A O   1 
HETATM 7884 O  O   . HOH P 7 .   ? -20.342 -24.354 -17.447 1.00 50.58  ? 869  HOH A O   1 
HETATM 7885 O  O   . HOH P 7 .   ? -7.618  -46.376 1.363   1.00 52.76  ? 870  HOH A O   1 
HETATM 7886 O  O   . HOH P 7 .   ? -0.093  -16.652 -9.280  1.00 51.67  ? 871  HOH A O   1 
HETATM 7887 O  O   . HOH P 7 .   ? -7.668  -7.823  -11.489 1.00 31.96  ? 872  HOH A O   1 
HETATM 7888 O  O   . HOH P 7 .   ? -29.413 -12.507 -1.497  1.00 54.72  ? 873  HOH A O   1 
HETATM 7889 O  O   . HOH P 7 .   ? -1.370  -7.124  -10.517 1.00 50.60  ? 874  HOH A O   1 
HETATM 7890 O  O   . HOH P 7 .   ? -30.708 -22.764 20.369  1.00 46.79  ? 875  HOH A O   1 
HETATM 7891 O  O   . HOH P 7 .   ? 17.409  -11.329 22.380  1.00 52.90  ? 876  HOH A O   1 
HETATM 7892 O  O   . HOH P 7 .   ? -22.687 -32.879 7.346   1.00 56.77  ? 877  HOH A O   1 
HETATM 7893 O  O   . HOH P 7 .   ? 6.011   -24.442 19.646  1.00 57.47  ? 878  HOH A O   1 
HETATM 7894 O  O   . HOH P 7 .   ? -6.585  15.283  24.812  1.00 63.30  ? 879  HOH A O   1 
HETATM 7895 O  O   . HOH P 7 .   ? 0.936   -29.356 7.312   1.00 45.91  ? 880  HOH A O   1 
HETATM 7896 O  O   . HOH P 7 .   ? -34.737 -11.804 2.033   1.00 52.87  ? 881  HOH A O   1 
HETATM 7897 O  O   . HOH P 7 .   ? -7.162  0.186   36.739  1.00 50.41  ? 882  HOH A O   1 
HETATM 7898 O  O   . HOH P 7 .   ? -27.778 -27.491 6.172   1.00 46.01  ? 883  HOH A O   1 
HETATM 7899 O  O   . HOH P 7 .   ? 6.926   -16.340 32.990  1.00 41.72  ? 884  HOH A O   1 
HETATM 7900 O  O   . HOH P 7 .   ? 16.725  -13.316 15.162  1.00 47.43  ? 885  HOH A O   1 
HETATM 7901 O  O   . HOH P 7 .   ? -10.459 -21.134 34.719  1.00 50.87  ? 886  HOH A O   1 
HETATM 7902 O  O   . HOH P 7 .   ? -24.080 -10.499 35.405  1.00 47.64  ? 887  HOH A O   1 
HETATM 7903 O  O   . HOH P 7 .   ? -0.701  -21.615 -5.653  1.00 47.98  ? 888  HOH A O   1 
HETATM 7904 O  O   . HOH P 7 .   ? -45.042 -13.160 11.697  1.00 50.92  ? 889  HOH A O   1 
HETATM 7905 O  O   . HOH P 7 .   ? -7.087  9.867   29.800  1.00 52.45  ? 890  HOH A O   1 
HETATM 7906 O  O   . HOH P 7 .   ? 0.171   -32.779 -5.130  1.00 48.61  ? 891  HOH A O   1 
HETATM 7907 O  O   . HOH P 7 .   ? -0.688  -1.310  -8.801  1.00 58.19  ? 892  HOH A O   1 
HETATM 7908 O  O   . HOH P 7 .   ? -13.375 9.938   21.125  1.00 39.34  ? 893  HOH A O   1 
HETATM 7909 O  O   . HOH P 7 .   ? -16.540 -37.991 3.140   1.00 49.74  ? 894  HOH A O   1 
HETATM 7910 O  O   . HOH P 7 .   ? -19.616 10.993  18.312  1.00 56.96  ? 895  HOH A O   1 
HETATM 7911 O  O   . HOH P 7 .   ? -6.188  -9.900  37.723  1.00 31.25  ? 896  HOH A O   1 
HETATM 7912 O  O   . HOH P 7 .   ? -39.044 -16.355 14.717  1.00 47.14  ? 897  HOH A O   1 
HETATM 7913 O  O   . HOH P 7 .   ? -8.773  -12.047 -15.871 1.00 49.45  ? 898  HOH A O   1 
HETATM 7914 O  O   . HOH P 7 .   ? -32.850 -19.079 25.464  1.00 57.53  ? 899  HOH A O   1 
HETATM 7915 O  O   . HOH P 7 .   ? -10.751 -15.499 -18.583 1.00 53.49  ? 900  HOH A O   1 
HETATM 7916 O  O   . HOH P 7 .   ? -38.603 -10.053 21.089  1.00 53.96  ? 901  HOH A O   1 
HETATM 7917 O  O   . HOH P 7 .   ? -12.023 6.976   26.507  1.00 57.18  ? 902  HOH A O   1 
HETATM 7918 O  O   . HOH P 7 .   ? 12.319  -17.462 13.167  1.00 46.42  ? 903  HOH A O   1 
HETATM 7919 O  O   . HOH P 7 .   ? -5.369  6.348   -6.322  1.00 44.57  ? 904  HOH A O   1 
HETATM 7920 O  O   . HOH P 7 .   ? -6.822  -38.858 -9.375  1.00 55.68  ? 905  HOH A O   1 
HETATM 7921 O  O   . HOH P 7 .   ? -15.721 -6.734  3.599   1.00 55.29  ? 906  HOH A O   1 
HETATM 7922 O  O   . HOH P 7 .   ? 14.765  -5.344  10.947  1.00 54.04  ? 907  HOH A O   1 
HETATM 7923 O  O   . HOH P 7 .   ? -11.157 -45.847 -5.807  1.00 51.95  ? 908  HOH A O   1 
HETATM 7924 O  O   . HOH P 7 .   ? -29.953 -4.915  2.062   1.00 68.79  ? 909  HOH A O   1 
HETATM 7925 O  O   . HOH P 7 .   ? -8.668  -17.869 28.841  1.00 49.80  ? 910  HOH A O   1 
HETATM 7926 O  O   . HOH P 7 .   ? -19.498 3.942   26.965  1.00 55.50  ? 911  HOH A O   1 
HETATM 7927 O  O   . HOH P 7 .   ? -7.775  12.191  17.644  1.00 45.38  ? 912  HOH A O   1 
HETATM 7928 O  O   . HOH P 7 .   ? -24.356 2.819   21.999  1.00 58.47  ? 913  HOH A O   1 
HETATM 7929 O  O   . HOH P 7 .   ? -8.483  2.372   12.948  1.00 56.35  ? 914  HOH A O   1 
HETATM 7930 O  O   . HOH P 7 .   ? -18.861 -15.493 0.609   1.00 31.77  ? 915  HOH A O   1 
HETATM 7931 O  O   . HOH P 7 .   ? -11.124 -0.469  10.604  1.00 55.02  ? 916  HOH A O   1 
HETATM 7932 O  O   . HOH P 7 .   ? -22.057 -7.397  5.168   1.00 53.38  ? 917  HOH A O   1 
HETATM 7933 O  O   . HOH P 7 .   ? -1.895  -19.717 -7.095  1.00 47.39  ? 918  HOH A O   1 
HETATM 7934 O  O   . HOH P 7 .   ? -12.197 -16.233 38.178  1.00 58.60  ? 919  HOH A O   1 
HETATM 7935 O  O   . HOH P 7 .   ? -0.601  -36.426 -7.454  1.00 53.58  ? 920  HOH A O   1 
HETATM 7936 O  O   . HOH P 7 .   ? -12.220 12.532  22.002  1.00 52.62  ? 921  HOH A O   1 
HETATM 7937 O  O   . HOH P 7 .   ? -2.187  14.427  19.059  1.00 53.08  ? 922  HOH A O   1 
HETATM 7938 O  O   . HOH P 7 .   ? -3.255  -24.812 -13.445 1.00 47.00  ? 923  HOH A O   1 
HETATM 7939 O  O   . HOH P 7 .   ? -21.521 -22.574 -18.752 1.00 54.83  ? 924  HOH A O   1 
HETATM 7940 O  O   . HOH P 7 .   ? 8.791   -24.762 16.524  1.00 57.53  ? 925  HOH A O   1 
HETATM 7941 O  O   . HOH P 7 .   ? 5.328   -32.141 -9.490  1.00 60.08  ? 926  HOH A O   1 
HETATM 7942 O  O   . HOH P 7 .   ? -24.460 -17.670 -13.345 1.00 51.20  ? 927  HOH A O   1 
HETATM 7943 O  O   . HOH P 7 .   ? 2.561   -29.006 5.652   1.00 51.63  ? 928  HOH A O   1 
HETATM 7944 O  O   . HOH P 7 .   ? 0.027   1.518   35.541  1.00 58.00  ? 929  HOH A O   1 
HETATM 7945 O  O   . HOH P 7 .   ? 2.480   -23.931 24.230  1.00 55.30  ? 930  HOH A O   1 
HETATM 7946 O  O   . HOH P 7 .   ? -8.892  -44.237 -7.005  1.00 43.29  ? 931  HOH A O   1 
HETATM 7947 O  O   . HOH P 7 .   ? -13.049 -13.563 39.252  1.00 45.26  ? 932  HOH A O   1 
HETATM 7948 O  O   . HOH P 7 .   ? 4.363   -20.488 3.863   1.00 55.56  ? 933  HOH A O   1 
HETATM 7949 O  O   . HOH P 7 .   ? -5.722  -8.366  -15.268 1.00 53.03  ? 934  HOH A O   1 
HETATM 7950 O  O   . HOH P 7 .   ? -9.635  -48.562 -4.609  1.00 54.69  ? 935  HOH A O   1 
HETATM 7951 O  O   . HOH P 7 .   ? 6.108   11.462  19.927  1.00 56.61  ? 936  HOH A O   1 
HETATM 7952 O  O   . HOH P 7 .   ? -10.028 -4.555  3.948   1.00 53.75  ? 937  HOH A O   1 
HETATM 7953 O  O   . HOH P 7 .   ? 3.145   6.667   10.563  1.00 55.03  ? 938  HOH A O   1 
HETATM 7954 O  O   . HOH P 7 .   ? 3.804   -20.893 25.808  1.00 42.80  ? 939  HOH A O   1 
HETATM 7955 O  O   . HOH P 7 .   ? -28.671 -24.127 -3.300  1.00 53.13  ? 940  HOH A O   1 
HETATM 7956 O  O   . HOH P 7 .   ? -0.336  6.492   -2.353  1.00 53.96  ? 941  HOH A O   1 
HETATM 7957 O  O   . HOH P 7 .   ? -28.777 -26.052 -14.275 1.00 52.36  ? 942  HOH A O   1 
HETATM 7958 O  O   . HOH P 7 .   ? -10.470 1.759   31.866  1.00 52.02  ? 943  HOH A O   1 
HETATM 7959 O  O   . HOH P 7 .   ? -23.346 -1.931  27.777  1.00 53.01  ? 944  HOH A O   1 
HETATM 7960 O  O   . HOH P 7 .   ? -6.055  -41.094 -9.918  1.00 53.73  ? 945  HOH A O   1 
HETATM 7961 O  O   . HOH P 7 .   ? -4.151  12.702  15.152  1.00 50.37  ? 946  HOH A O   1 
HETATM 7962 O  O   . HOH P 7 .   ? 2.233   -31.761 -0.705  1.00 46.93  ? 947  HOH A O   1 
HETATM 7963 O  O   . HOH P 7 .   ? -15.608 6.224   25.728  1.00 55.36  ? 948  HOH A O   1 
HETATM 7964 O  O   . HOH P 7 .   ? 7.694   -23.686 22.159  1.00 59.62  ? 949  HOH A O   1 
HETATM 7965 O  O   . HOH P 7 .   ? 18.181  -18.429 21.588  1.00 57.62  ? 950  HOH A O   1 
HETATM 7966 O  O   . HOH P 7 .   ? 10.731  0.797   19.029  1.00 47.92  ? 951  HOH A O   1 
HETATM 7967 O  O   . HOH P 7 .   ? 0.129   -34.081 -1.095  1.00 43.11  ? 952  HOH A O   1 
HETATM 7968 O  O   . HOH P 7 .   ? -9.165  12.993  15.470  1.00 48.22  ? 953  HOH A O   1 
HETATM 7969 O  O   . HOH P 7 .   ? 11.401  -3.486  8.131   1.00 49.26  ? 954  HOH A O   1 
HETATM 7970 O  O   . HOH P 7 .   ? -27.279 -25.071 -5.672  1.00 52.72  ? 955  HOH A O   1 
HETATM 7971 O  O   . HOH P 7 .   ? -2.204  -15.747 -11.941 1.00 50.53  ? 956  HOH A O   1 
HETATM 7972 O  O   . HOH P 7 .   ? 11.862  -3.382  19.051  1.00 48.83  ? 957  HOH A O   1 
HETATM 7973 O  O   . HOH P 7 .   ? 0.623   -33.008 5.671   1.00 44.62  ? 958  HOH A O   1 
HETATM 7974 O  O   . HOH P 7 .   ? 1.871   -14.772 34.179  1.00 48.24  ? 959  HOH A O   1 
HETATM 7975 O  O   . HOH P 7 .   ? 13.103  -23.009 18.527  1.00 56.26  ? 960  HOH A O   1 
HETATM 7976 O  O   . HOH P 7 .   ? -8.298  13.571  20.049  1.00 40.79  ? 961  HOH A O   1 
HETATM 7977 O  O   . HOH P 7 .   ? 4.345   8.036   24.984  1.00 45.66  ? 962  HOH A O   1 
HETATM 7978 O  O   . HOH P 7 .   ? 18.275  -14.381 18.961  1.00 46.46  ? 963  HOH A O   1 
HETATM 7979 O  O   . HOH P 7 .   ? -19.535 1.678   28.670  1.00 49.91  ? 964  HOH A O   1 
HETATM 7980 O  O   . HOH P 7 .   ? 16.277  -9.753  19.751  1.00 53.85  ? 965  HOH A O   1 
HETATM 7981 O  O   . HOH P 7 .   ? -3.076  -8.545  -11.639 1.00 51.07  ? 966  HOH A O   1 
HETATM 7982 O  O   . HOH P 7 .   ? -37.109 -20.133 9.768   1.00 51.91  ? 967  HOH A O   1 
HETATM 7983 O  O   . HOH P 7 .   ? -34.469 -13.924 3.503   1.00 39.39  ? 968  HOH A O   1 
HETATM 7984 O  O   . HOH P 7 .   ? -6.587  -22.770 20.527  1.00 50.41  ? 969  HOH A O   1 
HETATM 7985 O  O   . HOH P 7 .   ? -16.563 -30.461 -17.055 1.00 60.40  ? 970  HOH A O   1 
HETATM 7986 O  O   . HOH P 7 .   ? -5.150  -7.371  -12.708 1.00 47.66  ? 971  HOH A O   1 
HETATM 7987 O  O   . HOH P 7 .   ? 11.628  -13.970 10.174  1.00 55.88  ? 972  HOH A O   1 
HETATM 7988 O  O   . HOH P 7 .   ? -5.334  11.655  17.306  1.00 41.77  ? 973  HOH A O   1 
HETATM 7989 O  O   . HOH P 7 .   ? 3.181   -27.972 8.035   1.00 56.70  ? 974  HOH A O   1 
HETATM 7990 O  O   . HOH P 7 .   ? -4.700  -22.111 19.034  1.00 40.60  ? 975  HOH A O   1 
HETATM 7991 O  O   . HOH P 7 .   ? -15.575 10.453  19.626  1.00 53.13  ? 976  HOH A O   1 
HETATM 7992 O  O   . HOH P 7 .   ? 2.125   -31.245 4.009   1.00 43.14  ? 977  HOH A O   1 
HETATM 7993 O  O   . HOH P 7 .   ? -4.901  4.174   6.198   1.00 54.43  ? 978  HOH A O   1 
HETATM 7994 O  O   . HOH P 7 .   ? 7.714   6.792   24.733  1.00 47.81  ? 979  HOH A O   1 
HETATM 7995 O  O   . HOH P 7 .   ? 5.392   -21.195 8.721   1.00 53.83  ? 980  HOH A O   1 
HETATM 7996 O  O   . HOH P 7 .   ? -0.263  -33.528 1.604   1.00 41.67  ? 981  HOH A O   1 
HETATM 7997 O  O   . HOH P 7 .   ? 8.669   -21.551 25.899  1.00 62.41  ? 982  HOH A O   1 
HETATM 7998 O  O   . HOH P 7 .   ? -17.455 9.067   21.327  1.00 55.07  ? 983  HOH A O   1 
HETATM 7999 O  O   . HOH P 7 .   ? -7.510  -3.814  0.123   1.00 49.48  ? 984  HOH A O   1 
HETATM 8000 O  O   . HOH Q 7 .   ? -0.334  -47.029 80.859  1.00 48.68  ? 601  HOH B O   1 
HETATM 8001 O  O   . HOH Q 7 .   ? 5.994   -27.378 75.989  1.00 40.71  ? 602  HOH B O   1 
HETATM 8002 O  O   . HOH Q 7 .   ? -4.952  9.669   49.455  1.00 47.24  ? 603  HOH B O   1 
HETATM 8003 O  O   . HOH Q 7 .   ? -2.286  -36.685 86.492  1.00 52.26  ? 604  HOH B O   1 
HETATM 8004 O  O   . HOH Q 7 .   ? 4.601   -7.080  68.826  1.00 36.30  ? 605  HOH B O   1 
HETATM 8005 O  O   . HOH Q 7 .   ? 16.116  -23.949 45.947  1.00 51.79  ? 606  HOH B O   1 
HETATM 8006 O  O   . HOH Q 7 .   ? 14.052  -14.186 78.760  1.00 36.70  ? 607  HOH B O   1 
HETATM 8007 O  O   . HOH Q 7 .   ? -6.198  12.067  57.783  1.00 53.23  ? 608  HOH B O   1 
HETATM 8008 O  O   . HOH Q 7 .   ? -0.068  -14.927 89.517  1.00 42.34  ? 609  HOH B O   1 
HETATM 8009 O  O   . HOH Q 7 .   ? 6.783   -42.403 49.020  1.00 58.25  ? 610  HOH B O   1 
HETATM 8010 O  O   . HOH Q 7 .   ? 8.030   -2.474  42.407  1.00 51.52  ? 611  HOH B O   1 
HETATM 8011 O  O   . HOH Q 7 .   ? 1.999   1.471   63.454  1.00 48.82  ? 612  HOH B O   1 
HETATM 8012 O  O   . HOH Q 7 .   ? -1.454  1.509   61.253  1.00 43.01  ? 613  HOH B O   1 
HETATM 8013 O  O   . HOH Q 7 .   ? 1.940   -41.618 53.633  1.00 55.71  ? 614  HOH B O   1 
HETATM 8014 O  O   . HOH Q 7 .   ? 13.510  -32.225 56.639  1.00 52.80  ? 615  HOH B O   1 
HETATM 8015 O  O   . HOH Q 7 .   ? 11.571  -17.823 90.800  1.00 53.14  ? 616  HOH B O   1 
HETATM 8016 O  O   . HOH Q 7 .   ? -21.354 -16.036 36.180  1.00 45.33  ? 617  HOH B O   1 
HETATM 8017 O  O   . HOH Q 7 .   ? -4.471  11.968  53.685  1.00 42.68  ? 618  HOH B O   1 
HETATM 8018 O  O   . HOH Q 7 .   ? -2.418  -18.494 53.708  1.00 39.59  ? 619  HOH B O   1 
HETATM 8019 O  O   . HOH Q 7 .   ? -22.494 -17.112 53.541  1.00 32.90  ? 620  HOH B O   1 
HETATM 8020 O  O   . HOH Q 7 .   ? -5.139  -28.814 53.853  1.00 56.26  ? 621  HOH B O   1 
HETATM 8021 O  O   . HOH Q 7 .   ? -16.315 -19.090 76.719  1.00 46.86  ? 622  HOH B O   1 
HETATM 8022 O  O   . HOH Q 7 .   ? 18.715  -17.290 43.296  1.00 54.93  ? 623  HOH B O   1 
HETATM 8023 O  O   . HOH Q 7 .   ? 9.670   -48.049 54.633  1.00 50.84  ? 624  HOH B O   1 
HETATM 8024 O  O   . HOH Q 7 .   ? 9.690   -15.067 39.010  1.00 53.47  ? 625  HOH B O   1 
HETATM 8025 O  O   . HOH Q 7 .   ? -5.421  -23.600 89.947  1.00 48.13  ? 626  HOH B O   1 
HETATM 8026 O  O   . HOH Q 7 .   ? 8.793   -15.451 68.541  1.00 28.09  ? 627  HOH B O   1 
HETATM 8027 O  O   . HOH Q 7 .   ? 22.262  -23.446 67.099  1.00 35.87  ? 628  HOH B O   1 
HETATM 8028 O  O   . HOH Q 7 .   ? -17.641 -16.550 70.329  1.00 39.50  ? 629  HOH B O   1 
HETATM 8029 O  O   . HOH Q 7 .   ? -14.466 0.739   42.582  1.00 42.03  ? 630  HOH B O   1 
HETATM 8030 O  O   . HOH Q 7 .   ? -6.131  -12.364 86.670  1.00 42.18  ? 631  HOH B O   1 
HETATM 8031 O  O   . HOH Q 7 .   ? -12.034 -27.188 58.928  1.00 40.96  ? 632  HOH B O   1 
HETATM 8032 O  O   . HOH Q 7 .   ? 8.775   -30.437 87.374  1.00 45.15  ? 633  HOH B O   1 
HETATM 8033 O  O   . HOH Q 7 .   ? -1.879  -27.575 49.921  1.00 49.18  ? 634  HOH B O   1 
HETATM 8034 O  O   . HOH Q 7 .   ? -4.360  -20.468 53.440  1.00 45.82  ? 635  HOH B O   1 
HETATM 8035 O  O   . HOH Q 7 .   ? -16.838 -21.440 46.108  1.00 49.05  ? 636  HOH B O   1 
HETATM 8036 O  O   . HOH Q 7 .   ? -19.536 -22.818 52.665  1.00 45.42  ? 637  HOH B O   1 
HETATM 8037 O  O   . HOH Q 7 .   ? 0.952   -9.606  54.522  1.00 29.62  ? 638  HOH B O   1 
HETATM 8038 O  O   . HOH Q 7 .   ? 7.952   -43.086 57.869  1.00 42.16  ? 639  HOH B O   1 
HETATM 8039 O  O   . HOH Q 7 .   ? -18.555 4.677   63.042  1.00 31.11  ? 640  HOH B O   1 
HETATM 8040 O  O   . HOH Q 7 .   ? 13.507  -30.651 50.052  1.00 51.89  ? 641  HOH B O   1 
HETATM 8041 O  O   . HOH Q 7 .   ? -9.176  -34.671 70.928  1.00 40.46  ? 642  HOH B O   1 
HETATM 8042 O  O   . HOH Q 7 .   ? 21.753  -20.923 64.722  1.00 36.66  ? 643  HOH B O   1 
HETATM 8043 O  O   . HOH Q 7 .   ? -1.930  -40.153 68.488  1.00 50.78  ? 644  HOH B O   1 
HETATM 8044 O  O   . HOH Q 7 .   ? -4.704  -6.815  35.112  1.00 33.26  ? 645  HOH B O   1 
HETATM 8045 O  O   . HOH Q 7 .   ? 9.916   -36.880 45.592  1.00 57.19  ? 646  HOH B O   1 
HETATM 8046 O  O   . HOH Q 7 .   ? -19.786 -9.415  83.567  1.00 50.84  ? 647  HOH B O   1 
HETATM 8047 O  O   . HOH Q 7 .   ? -24.308 -1.717  47.970  1.00 45.23  ? 648  HOH B O   1 
HETATM 8048 O  O   . HOH Q 7 .   ? -8.328  -28.597 60.421  1.00 36.50  ? 649  HOH B O   1 
HETATM 8049 O  O   . HOH Q 7 .   ? 7.585   -6.731  72.784  1.00 47.56  ? 650  HOH B O   1 
HETATM 8050 O  O   . HOH Q 7 .   ? -21.740 -6.708  69.586  1.00 34.94  ? 651  HOH B O   1 
HETATM 8051 O  O   . HOH Q 7 .   ? -12.240 -40.627 73.993  1.00 46.87  ? 652  HOH B O   1 
HETATM 8052 O  O   . HOH Q 7 .   ? -9.545  -23.387 49.441  1.00 53.21  ? 653  HOH B O   1 
HETATM 8053 O  O   . HOH Q 7 .   ? -12.044 -22.593 52.368  1.00 35.54  ? 654  HOH B O   1 
HETATM 8054 O  O   . HOH Q 7 .   ? -6.122  -4.819  39.105  1.00 33.98  ? 655  HOH B O   1 
HETATM 8055 O  O   . HOH Q 7 .   ? -1.177  -24.609 43.481  1.00 55.99  ? 656  HOH B O   1 
HETATM 8056 O  O   . HOH Q 7 .   ? 20.677  -14.277 70.285  1.00 31.64  ? 657  HOH B O   1 
HETATM 8057 O  O   . HOH Q 7 .   ? -13.828 7.732   44.586  1.00 43.65  ? 658  HOH B O   1 
HETATM 8058 O  O   . HOH Q 7 .   ? -21.246 -8.577  34.746  1.00 49.01  ? 659  HOH B O   1 
HETATM 8059 O  O   . HOH Q 7 .   ? -13.017 -32.363 63.731  1.00 47.53  ? 660  HOH B O   1 
HETATM 8060 O  O   . HOH Q 7 .   ? -5.618  -24.453 80.753  1.00 30.54  ? 661  HOH B O   1 
HETATM 8061 O  O   . HOH Q 7 .   ? -7.383  7.057   41.497  1.00 52.72  ? 662  HOH B O   1 
HETATM 8062 O  O   . HOH Q 7 .   ? -11.535 8.175   40.905  1.00 53.66  ? 663  HOH B O   1 
HETATM 8063 O  O   . HOH Q 7 .   ? 1.511   -9.470  43.450  1.00 32.46  ? 664  HOH B O   1 
HETATM 8064 O  O   . HOH Q 7 .   ? -11.502 -0.253  76.453  1.00 45.09  ? 665  HOH B O   1 
HETATM 8065 O  O   . HOH Q 7 .   ? 0.161   -37.962 85.416  1.00 54.09  ? 666  HOH B O   1 
HETATM 8066 O  O   . HOH Q 7 .   ? -18.136 -7.601  79.999  1.00 47.01  ? 667  HOH B O   1 
HETATM 8067 O  O   . HOH Q 7 .   ? -21.257 -19.641 62.819  1.00 34.67  ? 668  HOH B O   1 
HETATM 8068 O  O   . HOH Q 7 .   ? 9.923   -3.403  47.966  1.00 40.84  ? 669  HOH B O   1 
HETATM 8069 O  O   . HOH Q 7 .   ? 10.338  -9.365  68.759  1.00 34.40  ? 670  HOH B O   1 
HETATM 8070 O  O   . HOH Q 7 .   ? 5.361   1.238   49.030  1.00 40.04  ? 671  HOH B O   1 
HETATM 8071 O  O   . HOH Q 7 .   ? 7.909   -29.474 89.810  1.00 48.13  ? 672  HOH B O   1 
HETATM 8072 O  O   . HOH Q 7 .   ? 3.191   6.983   62.494  1.00 58.10  ? 673  HOH B O   1 
HETATM 8073 O  O   . HOH Q 7 .   ? -21.329 9.308   58.342  1.00 51.59  ? 674  HOH B O   1 
HETATM 8074 O  O   . HOH Q 7 .   ? -5.103  -2.149  40.020  1.00 38.99  ? 675  HOH B O   1 
HETATM 8075 O  O   . HOH Q 7 .   ? 8.868   -31.573 83.479  1.00 44.93  ? 676  HOH B O   1 
HETATM 8076 O  O   . HOH Q 7 .   ? 29.577  -4.570  70.220  1.00 41.51  ? 677  HOH B O   1 
HETATM 8077 O  O   . HOH Q 7 .   ? -8.187  1.110   67.200  1.00 39.77  ? 678  HOH B O   1 
HETATM 8078 O  O   . HOH Q 7 .   ? -15.741 -19.443 70.751  1.00 37.57  ? 679  HOH B O   1 
HETATM 8079 O  O   . HOH Q 7 .   ? 20.825  -21.636 84.273  1.00 59.40  ? 680  HOH B O   1 
HETATM 8080 O  O   . HOH Q 7 .   ? -17.302 0.567   45.253  1.00 32.88  ? 681  HOH B O   1 
HETATM 8081 O  O   . HOH Q 7 .   ? 22.204  -8.450  57.052  1.00 40.09  ? 682  HOH B O   1 
HETATM 8082 O  O   . HOH Q 7 .   ? -6.949  -14.811 85.800  1.00 33.91  ? 683  HOH B O   1 
HETATM 8083 O  O   . HOH Q 7 .   ? 6.376   -14.557 71.970  1.00 29.58  ? 684  HOH B O   1 
HETATM 8084 O  O   . HOH Q 7 .   ? 13.040  -27.301 78.061  1.00 49.19  ? 685  HOH B O   1 
HETATM 8085 O  O   . HOH Q 7 .   ? 21.352  -2.343  61.290  1.00 50.28  ? 686  HOH B O   1 
HETATM 8086 O  O   . HOH Q 7 .   ? 5.323   -16.347 41.601  1.00 48.29  ? 687  HOH B O   1 
HETATM 8087 O  O   . HOH Q 7 .   ? -2.147  -15.050 67.613  1.00 28.78  ? 688  HOH B O   1 
HETATM 8088 O  O   . HOH Q 7 .   ? -14.373 -24.149 67.876  1.00 44.64  ? 689  HOH B O   1 
HETATM 8089 O  O   . HOH Q 7 .   ? 0.656   -12.648 58.740  1.00 31.94  ? 690  HOH B O   1 
HETATM 8090 O  O   . HOH Q 7 .   ? -22.193 -1.558  54.854  1.00 45.72  ? 691  HOH B O   1 
HETATM 8091 O  O   . HOH Q 7 .   ? 8.255   -29.884 80.702  1.00 35.72  ? 692  HOH B O   1 
HETATM 8092 O  O   . HOH Q 7 .   ? 10.673  -13.012 75.480  1.00 30.98  ? 693  HOH B O   1 
HETATM 8093 O  O   . HOH Q 7 .   ? -0.869  -20.343 39.673  1.00 55.43  ? 694  HOH B O   1 
HETATM 8094 O  O   . HOH Q 7 .   ? 12.020  -9.888  66.461  1.00 33.61  ? 695  HOH B O   1 
HETATM 8095 O  O   . HOH Q 7 .   ? 1.539   0.797   42.603  1.00 48.37  ? 696  HOH B O   1 
HETATM 8096 O  O   . HOH Q 7 .   ? -19.067 -3.492  40.501  1.00 43.98  ? 697  HOH B O   1 
HETATM 8097 O  O   . HOH Q 7 .   ? 0.455   -2.124  39.859  1.00 35.39  ? 698  HOH B O   1 
HETATM 8098 O  O   . HOH Q 7 .   ? 6.299   -39.077 60.742  1.00 44.51  ? 699  HOH B O   1 
HETATM 8099 O  O   . HOH Q 7 .   ? 4.137   -31.404 53.120  1.00 41.59  ? 700  HOH B O   1 
HETATM 8100 O  O   . HOH Q 7 .   ? -19.187 -17.891 66.062  1.00 49.52  ? 701  HOH B O   1 
HETATM 8101 O  O   . HOH Q 7 .   ? 0.471   -34.374 55.847  1.00 51.61  ? 702  HOH B O   1 
HETATM 8102 O  O   . HOH Q 7 .   ? 5.670   -1.855  41.909  1.00 53.25  ? 703  HOH B O   1 
HETATM 8103 O  O   . HOH Q 7 .   ? -13.353 -22.258 74.847  1.00 35.99  ? 704  HOH B O   1 
HETATM 8104 O  O   . HOH Q 7 .   ? 5.021   -22.522 69.972  1.00 29.59  ? 705  HOH B O   1 
HETATM 8105 O  O   . HOH Q 7 .   ? -25.793 -9.296  48.176  1.00 45.70  ? 706  HOH B O   1 
HETATM 8106 O  O   . HOH Q 7 .   ? 12.800  -29.677 83.560  1.00 43.75  ? 707  HOH B O   1 
HETATM 8107 O  O   . HOH Q 7 .   ? -0.163  2.634   45.408  1.00 45.35  ? 708  HOH B O   1 
HETATM 8108 O  O   . HOH Q 7 .   ? -19.563 -24.434 57.381  1.00 37.63  ? 709  HOH B O   1 
HETATM 8109 O  O   . HOH Q 7 .   ? 17.287  -23.413 89.058  1.00 40.66  ? 710  HOH B O   1 
HETATM 8110 O  O   . HOH Q 7 .   ? 18.709  -18.148 84.359  1.00 48.95  ? 711  HOH B O   1 
HETATM 8111 O  O   . HOH Q 7 .   ? 21.414  -20.251 59.068  1.00 36.97  ? 712  HOH B O   1 
HETATM 8112 O  O   . HOH Q 7 .   ? -13.215 7.955   47.395  1.00 42.39  ? 713  HOH B O   1 
HETATM 8113 O  O   . HOH Q 7 .   ? 5.787   -37.270 65.983  1.00 53.25  ? 714  HOH B O   1 
HETATM 8114 O  O   . HOH Q 7 .   ? 4.774   -18.041 93.054  1.00 47.09  ? 715  HOH B O   1 
HETATM 8115 O  O   . HOH Q 7 .   ? 0.870   -7.785  41.426  1.00 30.18  ? 716  HOH B O   1 
HETATM 8116 O  O   . HOH Q 7 .   ? -6.793  -25.979 86.381  1.00 34.49  ? 717  HOH B O   1 
HETATM 8117 O  O   . HOH Q 7 .   ? -10.036 11.426  56.556  1.00 42.36  ? 718  HOH B O   1 
HETATM 8118 O  O   . HOH Q 7 .   ? 0.135   -42.519 66.213  1.00 50.40  ? 719  HOH B O   1 
HETATM 8119 O  O   . HOH Q 7 .   ? 16.095  -7.642  73.407  1.00 48.42  ? 720  HOH B O   1 
HETATM 8120 O  O   . HOH Q 7 .   ? -18.675 -5.724  77.196  1.00 53.82  ? 721  HOH B O   1 
HETATM 8121 O  O   . HOH Q 7 .   ? 3.500   -9.761  45.523  1.00 29.54  ? 722  HOH B O   1 
HETATM 8122 O  O   . HOH Q 7 .   ? -14.456 -25.378 63.952  1.00 32.85  ? 723  HOH B O   1 
HETATM 8123 O  O   . HOH Q 7 .   ? -26.486 -14.347 58.673  1.00 46.30  ? 724  HOH B O   1 
HETATM 8124 O  O   . HOH Q 7 .   ? 3.111   -16.042 92.359  1.00 46.59  ? 725  HOH B O   1 
HETATM 8125 O  O   . HOH Q 7 .   ? -4.364  -17.753 59.982  1.00 33.31  ? 726  HOH B O   1 
HETATM 8126 O  O   . HOH Q 7 .   ? -13.658 7.332   63.948  1.00 43.90  ? 727  HOH B O   1 
HETATM 8127 O  O   . HOH Q 7 .   ? 5.231   -10.586 84.296  1.00 46.66  ? 728  HOH B O   1 
HETATM 8128 O  O   . HOH Q 7 .   ? -3.795  -33.654 63.369  1.00 49.97  ? 729  HOH B O   1 
HETATM 8129 O  O   . HOH Q 7 .   ? 18.689  -20.459 78.401  1.00 49.86  ? 730  HOH B O   1 
HETATM 8130 O  O   . HOH Q 7 .   ? 14.891  -19.539 73.598  1.00 30.69  ? 731  HOH B O   1 
HETATM 8131 O  O   . HOH Q 7 .   ? -10.220 -28.943 87.356  1.00 46.78  ? 732  HOH B O   1 
HETATM 8132 O  O   . HOH Q 7 .   ? 11.816  -18.689 61.640  1.00 29.97  ? 733  HOH B O   1 
HETATM 8133 O  O   . HOH Q 7 .   ? 19.488  -3.053  59.240  1.00 47.86  ? 734  HOH B O   1 
HETATM 8134 O  O   . HOH Q 7 .   ? 4.800   -35.070 69.212  1.00 42.58  ? 735  HOH B O   1 
HETATM 8135 O  O   . HOH Q 7 .   ? 25.809  -15.390 62.774  1.00 41.37  ? 736  HOH B O   1 
HETATM 8136 O  O   . HOH Q 7 .   ? 16.100  -28.319 88.734  1.00 48.78  ? 737  HOH B O   1 
HETATM 8137 O  O   . HOH Q 7 .   ? -3.164  -5.032  68.893  1.00 39.33  ? 738  HOH B O   1 
HETATM 8138 O  O   . HOH Q 7 .   ? 4.282   4.577   50.624  1.00 37.87  ? 739  HOH B O   1 
HETATM 8139 O  O   . HOH Q 7 .   ? -19.831 -14.105 68.972  1.00 48.80  ? 740  HOH B O   1 
HETATM 8140 O  O   . HOH Q 7 .   ? 24.183  -9.869  54.136  1.00 45.17  ? 741  HOH B O   1 
HETATM 8141 O  O   . HOH Q 7 .   ? -7.139  -12.115 79.501  1.00 31.90  ? 742  HOH B O   1 
HETATM 8142 O  O   . HOH Q 7 .   ? 13.072  -14.116 76.320  1.00 33.83  ? 743  HOH B O   1 
HETATM 8143 O  O   . HOH Q 7 .   ? 3.162   -26.505 45.185  1.00 43.87  ? 744  HOH B O   1 
HETATM 8144 O  O   . HOH Q 7 .   ? -19.781 -1.927  54.212  1.00 36.78  ? 745  HOH B O   1 
HETATM 8145 O  O   . HOH Q 7 .   ? -26.908 -0.132  64.309  1.00 49.96  ? 746  HOH B O   1 
HETATM 8146 O  O   . HOH Q 7 .   ? -15.589 7.468   51.305  1.00 40.27  ? 747  HOH B O   1 
HETATM 8147 O  O   . HOH Q 7 .   ? -16.155 12.499  55.377  1.00 49.12  ? 748  HOH B O   1 
HETATM 8148 O  O   . HOH Q 7 .   ? -9.239  7.588   51.340  1.00 33.57  ? 749  HOH B O   1 
HETATM 8149 O  O   . HOH Q 7 .   ? -22.692 -17.823 43.891  1.00 46.12  ? 750  HOH B O   1 
HETATM 8150 O  O   . HOH Q 7 .   ? -12.186 -9.786  88.284  1.00 45.80  ? 751  HOH B O   1 
HETATM 8151 O  O   . HOH Q 7 .   ? -14.158 -20.000 51.249  1.00 34.64  ? 752  HOH B O   1 
HETATM 8152 O  O   . HOH Q 7 .   ? -13.109 -10.768 39.184  1.00 32.28  ? 753  HOH B O   1 
HETATM 8153 O  O   . HOH Q 7 .   ? -16.071 -14.066 37.603  1.00 38.28  ? 754  HOH B O   1 
HETATM 8154 O  O   . HOH Q 7 .   ? -13.325 -35.174 79.240  1.00 54.17  ? 755  HOH B O   1 
HETATM 8155 O  O   . HOH Q 7 .   ? 20.336  -12.676 39.466  1.00 62.61  ? 756  HOH B O   1 
HETATM 8156 O  O   . HOH Q 7 .   ? -3.348  -1.604  42.131  1.00 34.67  ? 757  HOH B O   1 
HETATM 8157 O  O   . HOH Q 7 .   ? 6.784   -20.727 71.270  1.00 28.66  ? 758  HOH B O   1 
HETATM 8158 O  O   . HOH Q 7 .   ? -1.683  -3.733  83.769  1.00 51.32  ? 759  HOH B O   1 
HETATM 8159 O  O   . HOH Q 7 .   ? 4.635   -14.391 40.041  1.00 40.80  ? 760  HOH B O   1 
HETATM 8160 O  O   . HOH Q 7 .   ? -14.970 -14.664 43.595  1.00 39.61  ? 761  HOH B O   1 
HETATM 8161 O  O   . HOH Q 7 .   ? 23.571  -9.672  68.202  1.00 32.28  ? 762  HOH B O   1 
HETATM 8162 O  O   . HOH Q 7 .   ? -2.233  -41.308 64.947  1.00 54.10  ? 763  HOH B O   1 
HETATM 8163 O  O   . HOH Q 7 .   ? 31.673  -10.027 65.666  1.00 46.97  ? 764  HOH B O   1 
HETATM 8164 O  O   . HOH Q 7 .   ? 4.219   -29.448 86.914  1.00 45.43  ? 765  HOH B O   1 
HETATM 8165 O  O   . HOH Q 7 .   ? 8.175   -4.670  65.500  1.00 41.52  ? 766  HOH B O   1 
HETATM 8166 O  O   . HOH Q 7 .   ? 6.634   -13.042 87.865  1.00 39.19  ? 767  HOH B O   1 
HETATM 8167 O  O   . HOH Q 7 .   ? -18.794 3.988   51.495  1.00 37.59  ? 768  HOH B O   1 
HETATM 8168 O  O   . HOH Q 7 .   ? -9.069  -21.862 55.424  1.00 37.34  ? 769  HOH B O   1 
HETATM 8169 O  O   . HOH Q 7 .   ? -2.033  -10.186 42.137  1.00 29.02  ? 770  HOH B O   1 
HETATM 8170 O  O   . HOH Q 7 .   ? -6.094  -29.074 58.268  1.00 48.05  ? 771  HOH B O   1 
HETATM 8171 O  O   . HOH Q 7 .   ? 20.962  -23.063 86.715  1.00 56.95  ? 772  HOH B O   1 
HETATM 8172 O  O   . HOH Q 7 .   ? -19.027 2.314   53.909  1.00 37.90  ? 773  HOH B O   1 
HETATM 8173 O  O   . HOH Q 7 .   ? 13.927  -28.843 64.473  1.00 43.00  ? 774  HOH B O   1 
HETATM 8174 O  O   . HOH Q 7 .   ? 15.587  -20.596 91.357  1.00 47.37  ? 775  HOH B O   1 
HETATM 8175 O  O   . HOH Q 7 .   ? -14.921 -30.519 62.567  1.00 54.67  ? 776  HOH B O   1 
HETATM 8176 O  O   . HOH Q 7 .   ? -8.594  -13.403 64.171  1.00 31.85  ? 777  HOH B O   1 
HETATM 8177 O  O   . HOH Q 7 .   ? 2.460   -49.579 58.334  1.00 51.91  ? 778  HOH B O   1 
HETATM 8178 O  O   . HOH Q 7 .   ? -24.877 -3.677  58.945  1.00 36.64  ? 779  HOH B O   1 
HETATM 8179 O  O   . HOH Q 7 .   ? -14.562 -6.754  78.170  1.00 35.76  ? 780  HOH B O   1 
HETATM 8180 O  O   . HOH Q 7 .   ? -1.643  -40.865 62.279  1.00 56.88  ? 781  HOH B O   1 
HETATM 8181 O  O   . HOH Q 7 .   ? -21.853 -22.093 53.798  1.00 37.63  ? 782  HOH B O   1 
HETATM 8182 O  O   . HOH Q 7 .   ? 24.030  -14.703 60.031  1.00 39.04  ? 783  HOH B O   1 
HETATM 8183 O  O   . HOH Q 7 .   ? 12.510  -19.196 86.460  1.00 37.75  ? 784  HOH B O   1 
HETATM 8184 O  O   . HOH Q 7 .   ? 4.181   -20.232 68.600  1.00 30.68  ? 785  HOH B O   1 
HETATM 8185 O  O   . HOH Q 7 .   ? -11.451 -16.440 41.956  1.00 40.49  ? 786  HOH B O   1 
HETATM 8186 O  O   . HOH Q 7 .   ? -11.098 8.795   63.518  1.00 46.46  ? 787  HOH B O   1 
HETATM 8187 O  O   . HOH Q 7 .   ? -10.057 -29.086 56.307  1.00 49.44  ? 788  HOH B O   1 
HETATM 8188 O  O   . HOH Q 7 .   ? -8.481  -11.159 87.059  1.00 47.84  ? 789  HOH B O   1 
HETATM 8189 O  O   . HOH Q 7 .   ? -3.728  10.046  61.199  1.00 38.58  ? 790  HOH B O   1 
HETATM 8190 O  O   . HOH Q 7 .   ? -21.743 -11.040 69.223  1.00 33.69  ? 791  HOH B O   1 
HETATM 8191 O  O   . HOH Q 7 .   ? -13.233 -15.236 45.555  1.00 32.50  ? 792  HOH B O   1 
HETATM 8192 O  O   . HOH Q 7 .   ? -4.578  -44.784 80.690  1.00 32.42  ? 793  HOH B O   1 
HETATM 8193 O  O   . HOH Q 7 .   ? -26.203 -22.705 57.190  1.00 52.48  ? 794  HOH B O   1 
HETATM 8194 O  O   . HOH Q 7 .   ? -20.005 -10.917 45.363  1.00 39.10  ? 795  HOH B O   1 
HETATM 8195 O  O   . HOH Q 7 .   ? 23.546  -1.410  58.920  1.00 47.56  ? 796  HOH B O   1 
HETATM 8196 O  O   . HOH Q 7 .   ? -25.089 -9.623  57.579  1.00 48.53  ? 797  HOH B O   1 
HETATM 8197 O  O   . HOH Q 7 .   ? 18.164  -3.869  47.906  1.00 51.56  ? 798  HOH B O   1 
HETATM 8198 O  O   . HOH Q 7 .   ? 16.569  -26.702 59.709  1.00 47.54  ? 799  HOH B O   1 
HETATM 8199 O  O   . HOH Q 7 .   ? 5.577   -4.620  62.520  1.00 38.82  ? 800  HOH B O   1 
HETATM 8200 O  O   . HOH Q 7 .   ? -25.052 -20.936 60.571  1.00 47.34  ? 801  HOH B O   1 
HETATM 8201 O  O   . HOH Q 7 .   ? 3.792   -27.981 89.068  1.00 41.20  ? 802  HOH B O   1 
HETATM 8202 O  O   . HOH Q 7 .   ? 25.717  -18.808 54.511  1.00 47.39  ? 803  HOH B O   1 
HETATM 8203 O  O   . HOH Q 7 .   ? 18.403  -10.331 74.212  1.00 47.79  ? 804  HOH B O   1 
HETATM 8204 O  O   . HOH Q 7 .   ? -2.799  -22.450 56.121  1.00 40.41  ? 805  HOH B O   1 
HETATM 8205 O  O   . HOH Q 7 .   ? 8.483   -14.309 76.598  1.00 31.87  ? 806  HOH B O   1 
HETATM 8206 O  O   . HOH Q 7 .   ? -0.864  -48.833 76.504  1.00 48.90  ? 807  HOH B O   1 
HETATM 8207 O  O   . HOH Q 7 .   ? 17.051  -15.275 63.428  1.00 28.32  ? 808  HOH B O   1 
HETATM 8208 O  O   . HOH Q 7 .   ? -24.364 -2.753  43.357  1.00 50.57  ? 809  HOH B O   1 
HETATM 8209 O  O   . HOH Q 7 .   ? 5.086   -44.174 77.266  1.00 58.03  ? 810  HOH B O   1 
HETATM 8210 O  O   . HOH Q 7 .   ? 23.811  -18.977 59.605  1.00 46.51  ? 811  HOH B O   1 
HETATM 8211 O  O   . HOH Q 7 .   ? -1.475  -15.631 91.821  1.00 45.04  ? 812  HOH B O   1 
HETATM 8212 O  O   . HOH Q 7 .   ? 22.073  -6.408  70.902  1.00 44.31  ? 813  HOH B O   1 
HETATM 8213 O  O   . HOH Q 7 .   ? 7.321   -17.966 73.135  1.00 28.56  ? 814  HOH B O   1 
HETATM 8214 O  O   . HOH Q 7 .   ? 8.492   -14.989 79.278  1.00 30.97  ? 815  HOH B O   1 
HETATM 8215 O  O   . HOH Q 7 .   ? -20.090 7.628   57.026  1.00 39.66  ? 816  HOH B O   1 
HETATM 8216 O  O   . HOH Q 7 .   ? 18.246  -21.740 81.910  1.00 55.31  ? 817  HOH B O   1 
HETATM 8217 O  O   . HOH Q 7 .   ? -9.466  -18.347 81.021  1.00 40.59  ? 818  HOH B O   1 
HETATM 8218 O  O   . HOH Q 7 .   ? 0.730   -9.892  72.192  1.00 30.32  ? 819  HOH B O   1 
HETATM 8219 O  O   . HOH Q 7 .   ? 6.497   -33.587 71.425  1.00 47.43  ? 820  HOH B O   1 
HETATM 8220 O  O   . HOH Q 7 .   ? -11.437 -31.738 73.680  1.00 34.19  ? 821  HOH B O   1 
HETATM 8221 O  O   . HOH Q 7 .   ? -3.423  -25.886 64.881  1.00 32.95  ? 822  HOH B O   1 
HETATM 8222 O  O   . HOH Q 7 .   ? -0.729  -1.118  65.174  1.00 54.65  ? 823  HOH B O   1 
HETATM 8223 O  O   . HOH Q 7 .   ? 23.205  -18.680 65.463  1.00 35.31  ? 824  HOH B O   1 
HETATM 8224 O  O   . HOH Q 7 .   ? 32.686  -12.998 63.181  1.00 42.03  ? 825  HOH B O   1 
HETATM 8225 O  O   . HOH Q 7 .   ? -13.133 -25.380 70.994  1.00 39.65  ? 826  HOH B O   1 
HETATM 8226 O  O   . HOH Q 7 .   ? -26.629 -6.570  73.803  1.00 47.72  ? 827  HOH B O   1 
HETATM 8227 O  O   . HOH Q 7 .   ? 25.145  -1.331  62.603  1.00 48.19  ? 828  HOH B O   1 
HETATM 8228 O  O   . HOH Q 7 .   ? -8.241  -1.222  69.085  1.00 39.50  ? 829  HOH B O   1 
HETATM 8229 O  O   . HOH Q 7 .   ? -5.301  -7.986  39.641  1.00 31.66  ? 830  HOH B O   1 
HETATM 8230 O  O   . HOH Q 7 .   ? 11.697  -33.012 68.027  1.00 54.73  ? 831  HOH B O   1 
HETATM 8231 O  O   . HOH Q 7 .   ? -17.317 10.434  52.731  1.00 50.13  ? 832  HOH B O   1 
HETATM 8232 O  O   . HOH Q 7 .   ? 31.300  -3.061  58.821  1.00 48.58  ? 833  HOH B O   1 
HETATM 8233 O  O   . HOH Q 7 .   ? -10.754 3.788   48.141  1.00 34.65  ? 834  HOH B O   1 
HETATM 8234 O  O   . HOH Q 7 .   ? -14.876 -18.306 79.409  1.00 45.10  ? 835  HOH B O   1 
HETATM 8235 O  O   . HOH Q 7 .   ? 14.559  -24.410 54.006  1.00 39.87  ? 836  HOH B O   1 
HETATM 8236 O  O   . HOH Q 7 .   ? -15.314 -21.145 73.978  1.00 48.06  ? 837  HOH B O   1 
HETATM 8237 O  O   . HOH Q 7 .   ? -4.545  -1.681  67.714  1.00 47.58  ? 838  HOH B O   1 
HETATM 8238 O  O   . HOH Q 7 .   ? -19.178 -6.573  37.443  1.00 41.75  ? 839  HOH B O   1 
HETATM 8239 O  O   . HOH Q 7 .   ? -7.829  14.519  51.175  1.00 55.17  ? 840  HOH B O   1 
HETATM 8240 O  O   . HOH Q 7 .   ? -1.609  -16.022 47.578  1.00 41.00  ? 841  HOH B O   1 
HETATM 8241 O  O   . HOH Q 7 .   ? 23.990  -12.238 68.463  1.00 35.19  ? 842  HOH B O   1 
HETATM 8242 O  O   . HOH Q 7 .   ? -11.466 -30.564 68.067  1.00 39.75  ? 843  HOH B O   1 
HETATM 8243 O  O   . HOH Q 7 .   ? -3.778  -17.430 43.868  1.00 37.90  ? 844  HOH B O   1 
HETATM 8244 O  O   . HOH Q 7 .   ? 3.519   -34.113 53.548  1.00 42.75  ? 845  HOH B O   1 
HETATM 8245 O  O   . HOH Q 7 .   ? -13.152 -17.558 82.779  1.00 36.90  ? 846  HOH B O   1 
HETATM 8246 O  O   . HOH Q 7 .   ? -3.348  -46.837 73.820  1.00 54.29  ? 847  HOH B O   1 
HETATM 8247 O  O   . HOH Q 7 .   ? -1.257  -42.828 80.865  1.00 41.36  ? 848  HOH B O   1 
HETATM 8248 O  O   . HOH Q 7 .   ? -22.868 2.403   58.041  1.00 42.67  ? 849  HOH B O   1 
HETATM 8249 O  O   . HOH Q 7 .   ? 3.021   7.051   53.331  1.00 45.12  ? 850  HOH B O   1 
HETATM 8250 O  O   . HOH Q 7 .   ? -21.955 -23.324 56.492  1.00 36.43  ? 851  HOH B O   1 
HETATM 8251 O  O   . HOH Q 7 .   ? 10.511  -30.499 73.903  1.00 53.85  ? 852  HOH B O   1 
HETATM 8252 O  O   . HOH Q 7 .   ? -0.007  -0.571  62.573  1.00 38.75  ? 853  HOH B O   1 
HETATM 8253 O  O   . HOH Q 7 .   ? -10.727 -33.216 80.506  1.00 45.85  ? 854  HOH B O   1 
HETATM 8254 O  O   . HOH Q 7 .   ? -10.905 -17.434 84.803  1.00 51.61  ? 855  HOH B O   1 
HETATM 8255 O  O   . HOH Q 7 .   ? 15.910  -29.180 86.148  1.00 42.30  ? 856  HOH B O   1 
HETATM 8256 O  O   . HOH Q 7 .   ? 14.384  -5.895  71.677  1.00 53.74  ? 857  HOH B O   1 
HETATM 8257 O  O   . HOH Q 7 .   ? 4.001   -44.156 52.760  1.00 49.18  ? 858  HOH B O   1 
HETATM 8258 O  O   . HOH Q 7 .   ? -17.834 -17.376 37.230  1.00 55.91  ? 859  HOH B O   1 
HETATM 8259 O  O   . HOH Q 7 .   ? -25.212 -6.830  65.505  1.00 39.49  ? 860  HOH B O   1 
HETATM 8260 O  O   . HOH Q 7 .   ? -22.553 -19.656 47.262  1.00 47.10  ? 861  HOH B O   1 
HETATM 8261 O  O   . HOH Q 7 .   ? 0.423   -46.584 60.825  1.00 64.59  ? 862  HOH B O   1 
HETATM 8262 O  O   . HOH Q 7 .   ? 9.153   -18.859 92.832  1.00 48.68  ? 863  HOH B O   1 
HETATM 8263 O  O   . HOH Q 7 .   ? -11.543 -17.392 44.883  1.00 42.89  ? 864  HOH B O   1 
HETATM 8264 O  O   . HOH Q 7 .   ? -19.996 -15.114 76.808  1.00 42.00  ? 865  HOH B O   1 
HETATM 8265 O  O   . HOH Q 7 .   ? -5.726  -22.856 58.897  1.00 33.67  ? 866  HOH B O   1 
HETATM 8266 O  O   . HOH Q 7 .   ? -5.608  -18.431 47.946  1.00 39.86  ? 867  HOH B O   1 
HETATM 8267 O  O   . HOH Q 7 .   ? -7.453  3.696   44.120  1.00 41.71  ? 868  HOH B O   1 
HETATM 8268 O  O   . HOH Q 7 .   ? -2.466  -4.766  51.247  1.00 34.80  ? 869  HOH B O   1 
HETATM 8269 O  O   . HOH Q 7 .   ? 6.814   -9.013  78.644  1.00 51.41  ? 870  HOH B O   1 
HETATM 8270 O  O   . HOH Q 7 .   ? 0.403   7.990   52.539  1.00 39.76  ? 871  HOH B O   1 
HETATM 8271 O  O   . HOH Q 7 .   ? -10.730 -29.365 59.597  1.00 43.59  ? 872  HOH B O   1 
HETATM 8272 O  O   . HOH Q 7 .   ? -10.299 -35.453 79.114  1.00 38.55  ? 873  HOH B O   1 
HETATM 8273 O  O   . HOH Q 7 .   ? -18.640 -26.146 61.580  1.00 54.10  ? 874  HOH B O   1 
HETATM 8274 O  O   . HOH Q 7 .   ? -8.012  -14.273 41.321  1.00 36.27  ? 875  HOH B O   1 
HETATM 8275 O  O   . HOH Q 7 .   ? 8.380   3.861   64.812  1.00 53.24  ? 876  HOH B O   1 
HETATM 8276 O  O   . HOH Q 7 .   ? -20.605 -3.599  73.022  1.00 37.87  ? 877  HOH B O   1 
HETATM 8277 O  O   . HOH Q 7 .   ? -1.667  -16.553 35.727  1.00 50.55  ? 878  HOH B O   1 
HETATM 8278 O  O   . HOH Q 7 .   ? 5.549   -38.349 79.888  1.00 47.23  ? 879  HOH B O   1 
HETATM 8279 O  O   . HOH Q 7 .   ? -7.062  -34.844 86.597  1.00 43.87  ? 880  HOH B O   1 
HETATM 8280 O  O   . HOH Q 7 .   ? 23.326  -21.310 61.506  1.00 54.19  ? 881  HOH B O   1 
HETATM 8281 O  O   . HOH Q 7 .   ? -13.347 10.404  64.018  1.00 45.81  ? 882  HOH B O   1 
HETATM 8282 O  O   . HOH Q 7 .   ? -19.188 1.744   74.252  1.00 46.60  ? 883  HOH B O   1 
HETATM 8283 O  O   . HOH Q 7 .   ? 9.502   -30.715 71.814  1.00 50.54  ? 884  HOH B O   1 
HETATM 8284 O  O   . HOH Q 7 .   ? 9.235   -9.393  81.631  1.00 45.37  ? 885  HOH B O   1 
HETATM 8285 O  O   . HOH Q 7 .   ? -10.278 6.282   73.776  1.00 52.97  ? 886  HOH B O   1 
HETATM 8286 O  O   . HOH Q 7 .   ? -8.213  12.901  54.857  1.00 43.45  ? 887  HOH B O   1 
HETATM 8287 O  O   . HOH Q 7 .   ? -6.219  -0.156  39.091  1.00 55.06  ? 888  HOH B O   1 
HETATM 8288 O  O   . HOH Q 7 .   ? -10.742 12.996  46.450  1.00 60.05  ? 889  HOH B O   1 
HETATM 8289 O  O   . HOH Q 7 .   ? 17.816  -12.243 76.643  1.00 51.99  ? 890  HOH B O   1 
HETATM 8290 O  O   . HOH Q 7 .   ? 16.648  -26.991 68.335  1.00 43.31  ? 891  HOH B O   1 
HETATM 8291 O  O   . HOH Q 7 .   ? 9.216   -32.795 78.905  1.00 47.47  ? 892  HOH B O   1 
HETATM 8292 O  O   . HOH Q 7 .   ? 1.881   -43.287 64.601  1.00 51.57  ? 893  HOH B O   1 
HETATM 8293 O  O   . HOH Q 7 .   ? 0.693   -6.964  77.652  1.00 47.66  ? 894  HOH B O   1 
HETATM 8294 O  O   . HOH Q 7 .   ? -2.442  -7.129  77.393  1.00 39.91  ? 895  HOH B O   1 
HETATM 8295 O  O   . HOH Q 7 .   ? 17.733  -2.475  66.023  1.00 50.82  ? 896  HOH B O   1 
HETATM 8296 O  O   . HOH Q 7 .   ? -20.683 -13.399 66.560  1.00 36.91  ? 897  HOH B O   1 
HETATM 8297 O  O   . HOH Q 7 .   ? -6.526  -19.576 52.153  1.00 41.32  ? 898  HOH B O   1 
HETATM 8298 O  O   . HOH Q 7 .   ? 5.534   -38.631 72.078  1.00 46.24  ? 899  HOH B O   1 
HETATM 8299 O  O   . HOH Q 7 .   ? -13.741 12.178  60.344  1.00 39.75  ? 900  HOH B O   1 
HETATM 8300 O  O   . HOH Q 7 .   ? -17.153 -27.967 62.063  1.00 55.90  ? 901  HOH B O   1 
HETATM 8301 O  O   . HOH Q 7 .   ? -26.077 -10.815 55.687  1.00 42.63  ? 902  HOH B O   1 
HETATM 8302 O  O   . HOH Q 7 .   ? 6.265   -8.935  82.523  1.00 51.57  ? 903  HOH B O   1 
HETATM 8303 O  O   . HOH Q 7 .   ? -13.597 12.905  57.550  1.00 52.33  ? 904  HOH B O   1 
HETATM 8304 O  O   . HOH Q 7 .   ? 8.889   -28.743 72.963  1.00 50.05  ? 905  HOH B O   1 
HETATM 8305 O  O   . HOH Q 7 .   ? -9.131  -22.888 87.183  1.00 38.15  ? 906  HOH B O   1 
HETATM 8306 O  O   . HOH Q 7 .   ? -6.192  -38.467 83.548  1.00 40.33  ? 907  HOH B O   1 
HETATM 8307 O  O   . HOH Q 7 .   ? -18.888 -17.432 42.399  1.00 41.59  ? 908  HOH B O   1 
HETATM 8308 O  O   . HOH Q 7 .   ? 10.317  -24.997 92.169  1.00 45.42  ? 909  HOH B O   1 
HETATM 8309 O  O   . HOH Q 7 .   ? -5.862  -42.102 63.187  1.00 58.25  ? 910  HOH B O   1 
HETATM 8310 O  O   . HOH Q 7 .   ? -16.656 -17.632 67.738  1.00 41.06  ? 911  HOH B O   1 
HETATM 8311 O  O   . HOH Q 7 .   ? 19.031  -21.888 54.434  1.00 44.22  ? 912  HOH B O   1 
HETATM 8312 O  O   . HOH Q 7 .   ? 18.400  -18.973 81.450  1.00 49.67  ? 913  HOH B O   1 
HETATM 8313 O  O   . HOH Q 7 .   ? 26.368  -8.497  53.487  1.00 47.25  ? 914  HOH B O   1 
HETATM 8314 O  O   . HOH Q 7 .   ? -0.306  10.022  54.809  1.00 37.95  ? 915  HOH B O   1 
HETATM 8315 O  O   . HOH Q 7 .   ? 20.908  -18.403 49.074  1.00 55.93  ? 916  HOH B O   1 
HETATM 8316 O  O   . HOH Q 7 .   ? 27.295  -15.782 53.400  1.00 51.00  ? 917  HOH B O   1 
HETATM 8317 O  O   . HOH Q 7 .   ? -13.042 2.787   39.401  1.00 51.17  ? 918  HOH B O   1 
HETATM 8318 O  O   . HOH Q 7 .   ? -3.205  -17.921 46.297  1.00 44.33  ? 919  HOH B O   1 
HETATM 8319 O  O   . HOH Q 7 .   ? -6.646  9.554   45.844  1.00 43.11  ? 920  HOH B O   1 
HETATM 8320 O  O   . HOH Q 7 .   ? -12.329 -21.752 80.900  1.00 53.36  ? 921  HOH B O   1 
HETATM 8321 O  O   . HOH Q 7 .   ? -9.316  -37.644 68.965  1.00 53.48  ? 922  HOH B O   1 
HETATM 8322 O  O   . HOH Q 7 .   ? 24.560  -15.822 71.391  1.00 48.27  ? 923  HOH B O   1 
HETATM 8323 O  O   . HOH Q 7 .   ? 24.400  -1.035  55.773  1.00 62.82  ? 924  HOH B O   1 
HETATM 8324 O  O   . HOH Q 7 .   ? -17.176 -11.687 85.346  1.00 52.54  ? 925  HOH B O   1 
HETATM 8325 O  O   . HOH Q 7 .   ? 15.449  -26.511 54.734  1.00 50.37  ? 926  HOH B O   1 
HETATM 8326 O  O   . HOH Q 7 .   ? 5.832   -31.588 86.963  1.00 53.82  ? 927  HOH B O   1 
HETATM 8327 O  O   . HOH Q 7 .   ? -0.651  -30.332 44.358  1.00 58.65  ? 928  HOH B O   1 
HETATM 8328 O  O   . HOH Q 7 .   ? -9.798  -22.310 81.178  1.00 41.99  ? 929  HOH B O   1 
HETATM 8329 O  O   . HOH Q 7 .   ? -11.268 -35.246 64.323  1.00 52.77  ? 930  HOH B O   1 
HETATM 8330 O  O   . HOH Q 7 .   ? -12.259 -36.124 73.153  1.00 44.70  ? 931  HOH B O   1 
HETATM 8331 O  O   . HOH Q 7 .   ? -5.137  -36.321 62.702  1.00 53.98  ? 932  HOH B O   1 
HETATM 8332 O  O   . HOH Q 7 .   ? -21.150 -15.771 65.574  1.00 55.35  ? 933  HOH B O   1 
HETATM 8333 O  O   . HOH Q 7 .   ? 21.307  -14.929 40.162  1.00 61.36  ? 934  HOH B O   1 
HETATM 8334 O  O   . HOH Q 7 .   ? -24.489 -7.537  49.807  1.00 46.88  ? 935  HOH B O   1 
HETATM 8335 O  O   . HOH Q 7 .   ? 30.670  -6.669  58.514  1.00 46.95  ? 936  HOH B O   1 
HETATM 8336 O  O   . HOH Q 7 .   ? 11.140  -9.062  83.509  1.00 56.24  ? 937  HOH B O   1 
HETATM 8337 O  O   . HOH Q 7 .   ? 2.484   -29.073 91.138  1.00 47.90  ? 938  HOH B O   1 
HETATM 8338 O  O   . HOH Q 7 .   ? -6.689  -22.400 56.358  1.00 34.96  ? 939  HOH B O   1 
HETATM 8339 O  O   . HOH Q 7 .   ? -13.152 5.526   70.429  1.00 50.30  ? 940  HOH B O   1 
HETATM 8340 O  O   . HOH Q 7 .   ? -22.888 -8.909  70.865  1.00 43.60  ? 941  HOH B O   1 
HETATM 8341 O  O   . HOH Q 7 .   ? -13.437 -39.177 72.300  1.00 50.23  ? 942  HOH B O   1 
HETATM 8342 O  O   . HOH Q 7 .   ? 13.819  -8.717  77.191  1.00 57.03  ? 943  HOH B O   1 
HETATM 8343 O  O   . HOH Q 7 .   ? -1.140  5.976   48.944  1.00 52.07  ? 944  HOH B O   1 
HETATM 8344 O  O   . HOH Q 7 .   ? -23.796 -19.153 62.370  1.00 46.71  ? 945  HOH B O   1 
HETATM 8345 O  O   . HOH Q 7 .   ? -1.995  -2.734  68.493  1.00 50.59  ? 946  HOH B O   1 
HETATM 8346 O  O   . HOH Q 7 .   ? 1.941   10.586  56.269  1.00 51.72  ? 947  HOH B O   1 
HETATM 8347 O  O   . HOH Q 7 .   ? -13.417 -35.597 76.779  1.00 45.29  ? 948  HOH B O   1 
HETATM 8348 O  O   . HOH Q 7 .   ? -25.242 0.343   46.619  1.00 60.66  ? 949  HOH B O   1 
HETATM 8349 O  O   . HOH Q 7 .   ? -25.262 -9.741  71.508  1.00 56.37  ? 950  HOH B O   1 
HETATM 8350 O  O   . HOH Q 7 .   ? -8.425  -21.172 52.597  1.00 46.02  ? 951  HOH B O   1 
HETATM 8351 O  O   . HOH Q 7 .   ? 17.980  -25.438 61.463  1.00 49.85  ? 952  HOH B O   1 
HETATM 8352 O  O   . HOH Q 7 .   ? 30.684  -2.846  61.266  1.00 53.37  ? 953  HOH B O   1 
HETATM 8353 O  O   . HOH Q 7 .   ? 6.298   4.742   48.985  1.00 51.68  ? 954  HOH B O   1 
HETATM 8354 O  O   . HOH Q 7 .   ? 0.543   -15.757 36.943  1.00 57.10  ? 955  HOH B O   1 
HETATM 8355 O  O   . HOH Q 7 .   ? -15.750 9.601   49.416  1.00 59.31  ? 956  HOH B O   1 
HETATM 8356 O  O   . HOH Q 7 .   ? -8.745  -20.397 82.523  1.00 42.20  ? 957  HOH B O   1 
HETATM 8357 O  O   . HOH Q 7 .   ? -21.713 3.193   55.555  1.00 47.96  ? 958  HOH B O   1 
HETATM 8358 O  O   . HOH Q 7 .   ? -16.471 -26.905 64.857  1.00 59.17  ? 959  HOH B O   1 
HETATM 8359 O  O   . HOH Q 7 .   ? -24.569 2.631   64.963  1.00 45.88  ? 960  HOH B O   1 
HETATM 8360 O  O   . HOH Q 7 .   ? -6.978  -20.329 46.480  1.00 50.23  ? 961  HOH B O   1 
HETATM 8361 O  O   . HOH Q 7 .   ? 7.099   -12.881 90.342  1.00 52.00  ? 962  HOH B O   1 
HETATM 8362 O  O   . HOH Q 7 .   ? -23.526 -13.311 66.752  1.00 55.31  ? 963  HOH B O   1 
HETATM 8363 O  O   . HOH Q 7 .   ? -6.901  -25.748 89.075  1.00 51.37  ? 964  HOH B O   1 
HETATM 8364 O  O   . HOH Q 7 .   ? 4.511   -11.766 87.122  1.00 49.13  ? 965  HOH B O   1 
HETATM 8365 O  O   . HOH Q 7 .   ? 0.958   -15.963 93.872  1.00 55.73  ? 966  HOH B O   1 
HETATM 8366 O  O   . HOH Q 7 .   ? -4.740  10.327  46.944  1.00 57.41  ? 967  HOH B O   1 
HETATM 8367 O  O   . HOH Q 7 .   ? 7.528   -15.527 74.342  1.00 31.83  ? 968  HOH B O   1 
HETATM 8368 O  O   . HOH Q 7 .   ? -16.722 -18.047 42.589  1.00 63.60  ? 969  HOH B O   1 
HETATM 8369 O  O   . HOH Q 7 .   ? -4.972  -23.262 54.801  1.00 41.60  ? 970  HOH B O   1 
HETATM 8370 O  O   . HOH Q 7 .   ? 18.450  -25.937 88.928  1.00 58.76  ? 971  HOH B O   1 
HETATM 8371 O  O   . HOH Q 7 .   ? 0.969   -12.935 36.084  1.00 43.81  ? 972  HOH B O   1 
HETATM 8372 O  O   . HOH Q 7 .   ? -16.795 -27.786 80.177  1.00 51.44  ? 973  HOH B O   1 
HETATM 8373 O  O   . HOH Q 7 .   ? -13.580 -24.696 51.024  1.00 49.23  ? 974  HOH B O   1 
HETATM 8374 O  O   . HOH Q 7 .   ? -1.544  12.409  54.033  1.00 49.69  ? 975  HOH B O   1 
HETATM 8375 O  O   . HOH Q 7 .   ? 12.107  -6.034  71.732  1.00 56.81  ? 976  HOH B O   1 
HETATM 8376 O  O   . HOH Q 7 .   ? 3.741   -0.691  44.753  1.00 45.78  ? 977  HOH B O   1 
HETATM 8377 O  O   . HOH Q 7 .   ? 1.922   6.380   49.988  1.00 56.82  ? 978  HOH B O   1 
HETATM 8378 O  O   . HOH Q 7 .   ? -23.759 -1.721  57.183  1.00 42.02  ? 979  HOH B O   1 
HETATM 8379 O  O   . HOH Q 7 .   ? -12.609 -32.530 76.122  1.00 47.16  ? 980  HOH B O   1 
HETATM 8380 O  O   . HOH Q 7 .   ? -17.709 6.584   50.617  1.00 50.16  ? 981  HOH B O   1 
HETATM 8381 O  O   . HOH Q 7 .   ? 5.601   -48.332 52.264  1.00 52.72  ? 982  HOH B O   1 
HETATM 8382 O  O   . HOH Q 7 .   ? -19.767 9.563   55.140  1.00 53.13  ? 983  HOH B O   1 
HETATM 8383 O  O   . HOH Q 7 .   ? -15.133 -21.953 49.554  1.00 42.15  ? 984  HOH B O   1 
HETATM 8384 O  O   . HOH Q 7 .   ? -24.348 4.944   61.174  1.00 46.13  ? 985  HOH B O   1 
HETATM 8385 O  O   . HOH Q 7 .   ? -13.285 -31.777 66.299  1.00 54.74  ? 986  HOH B O   1 
HETATM 8386 O  O   . HOH Q 7 .   ? -2.259  -45.319 82.065  1.00 40.31  ? 987  HOH B O   1 
HETATM 8387 O  O   . HOH Q 7 .   ? -11.280 -33.545 69.487  1.00 45.00  ? 988  HOH B O   1 
HETATM 8388 O  O   . HOH Q 7 .   ? 8.134   -5.219  67.990  1.00 54.56  ? 989  HOH B O   1 
HETATM 8389 O  O   . HOH Q 7 .   ? -14.457 -2.073  37.526  1.00 52.55  ? 990  HOH B O   1 
HETATM 8390 O  O   . HOH Q 7 .   ? 17.566  -27.850 81.781  1.00 53.32  ? 991  HOH B O   1 
HETATM 8391 O  O   . HOH Q 7 .   ? -8.300  -16.409 87.568  1.00 44.07  ? 992  HOH B O   1 
HETATM 8392 O  O   . HOH Q 7 .   ? 3.340   -31.940 87.194  1.00 58.91  ? 993  HOH B O   1 
HETATM 8393 O  O   . HOH Q 7 .   ? -17.096 -19.931 68.122  1.00 51.70  ? 994  HOH B O   1 
HETATM 8394 O  O   . HOH Q 7 .   ? 13.388  -17.586 88.446  1.00 50.05  ? 995  HOH B O   1 
HETATM 8395 O  O   . HOH Q 7 .   ? -19.761 -26.636 58.793  1.00 52.65  ? 996  HOH B O   1 
HETATM 8396 O  O   . HOH Q 7 .   ? 20.270  -12.157 73.733  1.00 58.31  ? 997  HOH B O   1 
HETATM 8397 O  O   . HOH Q 7 .   ? -4.921  -42.459 85.243  1.00 54.49  ? 998  HOH B O   1 
HETATM 8398 O  O   . HOH Q 7 .   ? -10.983 -34.690 76.334  1.00 46.22  ? 999  HOH B O   1 
HETATM 8399 O  O   . HOH Q 7 .   ? 1.094   -33.622 88.669  1.00 56.82  ? 1000 HOH B O   1 
HETATM 8400 O  O   . HOH Q 7 .   ? -22.895 3.814   63.516  1.00 37.12  ? 1001 HOH B O   1 
HETATM 8401 O  O   . HOH Q 7 .   ? 14.390  -32.496 47.917  1.00 59.81  ? 1002 HOH B O   1 
HETATM 8402 O  O   . HOH Q 7 .   ? -12.915 9.266   42.666  1.00 54.00  ? 1003 HOH B O   1 
HETATM 8403 O  O   . HOH Q 7 .   ? 20.204  -0.601  63.479  1.00 57.29  ? 1004 HOH B O   1 
HETATM 8404 O  O   . HOH Q 7 .   ? -5.605  -20.149 49.885  1.00 43.84  ? 1005 HOH B O   1 
HETATM 8405 O  O   . HOH Q 7 .   ? 9.961   -6.853  69.624  1.00 50.25  ? 1006 HOH B O   1 
HETATM 8406 O  O   . HOH Q 7 .   ? -15.222 -26.110 52.191  1.00 60.62  ? 1007 HOH B O   1 
HETATM 8407 O  O   . HOH Q 7 .   ? 6.367   2.353   47.065  1.00 51.69  ? 1008 HOH B O   1 
HETATM 8408 O  O   . HOH Q 7 .   ? -14.298 -29.021 67.938  1.00 63.27  ? 1009 HOH B O   1 
HETATM 8409 O  O   . HOH Q 7 .   ? -2.754  -49.293 79.117  1.00 50.86  ? 1010 HOH B O   1 
HETATM 8410 O  O   . HOH Q 7 .   ? 23.020  -13.214 70.953  1.00 35.83  ? 1011 HOH B O   1 
HETATM 8411 O  O   . HOH Q 7 .   ? -20.817 -21.275 65.267  1.00 46.00  ? 1012 HOH B O   1 
HETATM 8412 O  O   . HOH Q 7 .   ? 14.128  -30.819 81.392  1.00 58.71  ? 1013 HOH B O   1 
HETATM 8413 O  O   . HOH Q 7 .   ? 7.693   1.249   66.344  1.00 63.28  ? 1014 HOH B O   1 
HETATM 8414 O  O   . HOH Q 7 .   ? -14.476 -35.864 82.403  1.00 51.85  ? 1015 HOH B O   1 
HETATM 8415 O  O   . HOH Q 7 .   ? -5.178  3.248   42.783  1.00 48.10  ? 1016 HOH B O   1 
HETATM 8416 O  O   . HOH Q 7 .   ? -13.947 -15.345 41.287  1.00 43.10  ? 1017 HOH B O   1 
HETATM 8417 O  O   . HOH Q 7 .   ? -13.585 0.332   40.177  1.00 46.19  ? 1018 HOH B O   1 
HETATM 8418 O  O   . HOH Q 7 .   ? -23.355 -23.730 52.321  1.00 52.18  ? 1019 HOH B O   1 
HETATM 8419 O  O   . HOH Q 7 .   ? 6.319   -50.706 79.694  1.00 52.78  ? 1020 HOH B O   1 
HETATM 8420 O  O   . HOH Q 7 .   ? 25.826  -18.977 64.535  1.00 50.07  ? 1021 HOH B O   1 
HETATM 8421 O  O   . HOH Q 7 .   ? -18.975 -3.459  75.300  1.00 49.11  ? 1022 HOH B O   1 
HETATM 8422 O  O   . HOH Q 7 .   ? -21.196 4.852   51.096  1.00 49.60  ? 1023 HOH B O   1 
HETATM 8423 O  O   . HOH Q 7 .   ? -27.746 -9.533  58.898  1.00 45.84  ? 1024 HOH B O   1 
HETATM 8424 O  O   . HOH Q 7 .   ? -7.277  -22.884 48.279  1.00 50.47  ? 1025 HOH B O   1 
HETATM 8425 O  O   . HOH Q 7 .   ? 12.156  -35.258 67.135  1.00 54.62  ? 1026 HOH B O   1 
HETATM 8426 O  O   . HOH Q 7 .   ? 26.529  -12.502 69.540  1.00 44.97  ? 1027 HOH B O   1 
HETATM 8427 O  O   . HOH Q 7 .   ? -21.962 5.985   55.872  1.00 50.30  ? 1028 HOH B O   1 
HETATM 8428 O  O   . HOH Q 7 .   ? -13.024 -31.805 71.523  1.00 45.32  ? 1029 HOH B O   1 
HETATM 8429 O  O   . HOH Q 7 .   ? -0.199  5.288   46.141  1.00 53.40  ? 1030 HOH B O   1 
HETATM 8430 O  O   . HOH Q 7 .   ? -19.738 -20.335 67.165  1.00 59.77  ? 1031 HOH B O   1 
HETATM 8431 O  O   . HOH Q 7 .   ? -11.821 11.791  44.215  1.00 62.50  ? 1032 HOH B O   1 
HETATM 8432 O  O   . HOH Q 7 .   ? -18.841 11.936  55.960  1.00 54.62  ? 1033 HOH B O   1 
HETATM 8433 O  O   . HOH Q 7 .   ? -24.178 4.688   58.515  1.00 55.17  ? 1034 HOH B O   1 
HETATM 8434 O  O   . HOH Q 7 .   ? -16.491 -22.449 67.035  1.00 50.73  ? 1035 HOH B O   1 
HETATM 8435 O  O   . HOH Q 7 .   ? -24.325 3.294   55.435  1.00 62.26  ? 1036 HOH B O   1 
HETATM 8436 O  O   . HOH Q 7 .   ? 4.735   -26.327 42.687  1.00 54.05  ? 1037 HOH B O   1 
HETATM 8437 O  O   . HOH Q 7 .   ? -25.438 -5.968  57.636  1.00 48.36  ? 1038 HOH B O   1 
HETATM 8438 O  O   . HOH Q 7 .   ? -8.861  -29.429 89.647  1.00 57.53  ? 1039 HOH B O   1 
HETATM 8439 O  O   . HOH Q 7 .   ? 3.728   9.226   54.748  1.00 55.35  ? 1040 HOH B O   1 
HETATM 8440 O  O   . HOH Q 7 .   ? -10.493 -34.238 73.538  1.00 41.05  ? 1041 HOH B O   1 
HETATM 8441 O  O   . HOH Q 7 .   ? -1.005  -48.150 72.550  1.00 59.20  ? 1042 HOH B O   1 
HETATM 8442 O  O   . HOH Q 7 .   ? -9.417  15.328  53.505  1.00 54.41  ? 1043 HOH B O   1 
# 
