data_8YB2
# 
_entry.id   8YB2 
# 
_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   8YB2         pdb_00008yb2 10.2210/pdb8yb2/pdb 
WWPDB D_1300044635 ?            ?                   
# 
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                        8YB2 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              minoru.kubo@riken.jp 
_pdbx_contact_author.name_first         Minoru 
_pdbx_contact_author.name_last          Kubo 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1470-942X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nagao, S.'       1  ? 
'Kuwano, W.'      2  ? 
'Tosha, T.'       3  ? 
'Yamashita, K.'   4  ? 
'Stanfield, J.K.' 5  ? 
'Kasai, C.'       6  ? 
'Ariyasu, S.'     7  ? 
'Shoji, O.'       8  ? 
'Sugimoto, H.'    9  ? 
'Kubo, M.'        10 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3669 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                63 
_citation.page_last                 63 
_citation.title                     
'XFEL crystallography reveals catalytic cycle dynamics during non-native substrate oxidation by cytochrome P450BM3.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42004-025-01440-2 
_citation.pdbx_database_id_PubMed   40075209 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nagao, S.'       1  ? 
primary 'Kuwano, W.'      2  ? 
primary 'Tosha, T.'       3  ? 
primary 'Yamashita, K.'   4  ? 
primary 'Stanfield, J.K.' 5  ? 
primary 'Kasai, C.'       6  ? 
primary 'Ariyasu, S.'     7  ? 
primary 'Hirata, K.'      8  ? 
primary 'Ueno, G.'        9  ? 
primary 'Murakami, H.'    10 ? 
primary 'Ago, H.'         11 ? 
primary 'Yamamoto, M.'    12 ? 
primary 'Shoji, O.'       13 ? 
primary 'Sugimoto, H.'    14 ? 
primary 'Kubo, M.'        15 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Bifunctional cytochrome P450/NADPH--P450 reductase'                           52160.434 2   1.14.14.1,1.6.2.4 
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    8   ?                 ? 
? ? 
7 water       nat water                                                                          18.015    779 ?                 ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytochrome P450(BM-3),Cytochrome P450BM-3,Fatty acid monooxygenase,Flavocytochrome P450 BM3' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRD
FAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPHGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRD
FAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNY
RFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNG
KDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNE
ALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPHGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                              HEM 
3 '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' D0L 
4 ethenylbenzene                                                                 SYN 
5 '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  PHE n 
1 88  THR n 
1 89  SER n 
1 90  TRP n 
1 91  THR n 
1 92  HIS n 
1 93  GLU n 
1 94  LYS n 
1 95  ASN n 
1 96  TRP n 
1 97  LYS n 
1 98  LYS n 
1 99  ALA n 
1 100 HIS n 
1 101 ASN n 
1 102 ILE n 
1 103 LEU n 
1 104 LEU n 
1 105 PRO n 
1 106 SER n 
1 107 PHE n 
1 108 SER n 
1 109 GLN n 
1 110 GLN n 
1 111 ALA n 
1 112 MET n 
1 113 LYS n 
1 114 GLY n 
1 115 TYR n 
1 116 HIS n 
1 117 ALA n 
1 118 MET n 
1 119 MET n 
1 120 VAL n 
1 121 ASP n 
1 122 ILE n 
1 123 ALA n 
1 124 VAL n 
1 125 GLN n 
1 126 LEU n 
1 127 VAL n 
1 128 GLN n 
1 129 LYS n 
1 130 TRP n 
1 131 GLU n 
1 132 ARG n 
1 133 LEU n 
1 134 ASN n 
1 135 ALA n 
1 136 ASP n 
1 137 GLU n 
1 138 HIS n 
1 139 ILE n 
1 140 GLU n 
1 141 VAL n 
1 142 PRO n 
1 143 GLU n 
1 144 ASP n 
1 145 MET n 
1 146 THR n 
1 147 ARG n 
1 148 LEU n 
1 149 THR n 
1 150 LEU n 
1 151 ASP n 
1 152 THR n 
1 153 ILE n 
1 154 GLY n 
1 155 LEU n 
1 156 CYS n 
1 157 GLY n 
1 158 PHE n 
1 159 ASN n 
1 160 TYR n 
1 161 ARG n 
1 162 PHE n 
1 163 ASN n 
1 164 SER n 
1 165 PHE n 
1 166 TYR n 
1 167 ARG n 
1 168 ASP n 
1 169 GLN n 
1 170 PRO n 
1 171 HIS n 
1 172 PRO n 
1 173 PHE n 
1 174 ILE n 
1 175 THR n 
1 176 SER n 
1 177 MET n 
1 178 VAL n 
1 179 ARG n 
1 180 ALA n 
1 181 LEU n 
1 182 ASP n 
1 183 GLU n 
1 184 ALA n 
1 185 MET n 
1 186 ASN n 
1 187 LYS n 
1 188 LEU n 
1 189 GLN n 
1 190 ARG n 
1 191 ALA n 
1 192 ASN n 
1 193 PRO n 
1 194 ASP n 
1 195 ASP n 
1 196 PRO n 
1 197 ALA n 
1 198 TYR n 
1 199 ASP n 
1 200 GLU n 
1 201 ASN n 
1 202 LYS n 
1 203 ARG n 
1 204 GLN n 
1 205 PHE n 
1 206 GLN n 
1 207 GLU n 
1 208 ASP n 
1 209 ILE n 
1 210 LYS n 
1 211 VAL n 
1 212 MET n 
1 213 ASN n 
1 214 ASP n 
1 215 LEU n 
1 216 VAL n 
1 217 ASP n 
1 218 LYS n 
1 219 ILE n 
1 220 ILE n 
1 221 ALA n 
1 222 ASP n 
1 223 ARG n 
1 224 LYS n 
1 225 ALA n 
1 226 SER n 
1 227 GLY n 
1 228 GLU n 
1 229 GLN n 
1 230 SER n 
1 231 ASP n 
1 232 ASP n 
1 233 LEU n 
1 234 LEU n 
1 235 THR n 
1 236 HIS n 
1 237 MET n 
1 238 LEU n 
1 239 ASN n 
1 240 GLY n 
1 241 LYS n 
1 242 ASP n 
1 243 PRO n 
1 244 GLU n 
1 245 THR n 
1 246 GLY n 
1 247 GLU n 
1 248 PRO n 
1 249 LEU n 
1 250 ASP n 
1 251 ASP n 
1 252 GLU n 
1 253 ASN n 
1 254 ILE n 
1 255 ARG n 
1 256 TYR n 
1 257 GLN n 
1 258 ILE n 
1 259 ILE n 
1 260 THR n 
1 261 PHE n 
1 262 LEU n 
1 263 ILE n 
1 264 ALA n 
1 265 GLY n 
1 266 HIS n 
1 267 GLU n 
1 268 THR n 
1 269 THR n 
1 270 SER n 
1 271 GLY n 
1 272 LEU n 
1 273 LEU n 
1 274 SER n 
1 275 PHE n 
1 276 ALA n 
1 277 LEU n 
1 278 TYR n 
1 279 PHE n 
1 280 LEU n 
1 281 VAL n 
1 282 LYS n 
1 283 ASN n 
1 284 PRO n 
1 285 HIS n 
1 286 VAL n 
1 287 LEU n 
1 288 GLN n 
1 289 LYS n 
1 290 ALA n 
1 291 ALA n 
1 292 GLU n 
1 293 GLU n 
1 294 ALA n 
1 295 ALA n 
1 296 ARG n 
1 297 VAL n 
1 298 LEU n 
1 299 VAL n 
1 300 ASP n 
1 301 PRO n 
1 302 VAL n 
1 303 PRO n 
1 304 SER n 
1 305 TYR n 
1 306 LYS n 
1 307 GLN n 
1 308 VAL n 
1 309 LYS n 
1 310 GLN n 
1 311 LEU n 
1 312 LYS n 
1 313 TYR n 
1 314 VAL n 
1 315 GLY n 
1 316 MET n 
1 317 VAL n 
1 318 LEU n 
1 319 ASN n 
1 320 GLU n 
1 321 ALA n 
1 322 LEU n 
1 323 ARG n 
1 324 LEU n 
1 325 TRP n 
1 326 PRO n 
1 327 THR n 
1 328 ALA n 
1 329 PRO n 
1 330 ALA n 
1 331 PHE n 
1 332 SER n 
1 333 LEU n 
1 334 TYR n 
1 335 ALA n 
1 336 LYS n 
1 337 GLU n 
1 338 ASP n 
1 339 THR n 
1 340 VAL n 
1 341 LEU n 
1 342 GLY n 
1 343 GLY n 
1 344 GLU n 
1 345 TYR n 
1 346 PRO n 
1 347 LEU n 
1 348 GLU n 
1 349 LYS n 
1 350 GLY n 
1 351 ASP n 
1 352 GLU n 
1 353 LEU n 
1 354 MET n 
1 355 VAL n 
1 356 LEU n 
1 357 ILE n 
1 358 PRO n 
1 359 GLN n 
1 360 LEU n 
1 361 HIS n 
1 362 ARG n 
1 363 ASP n 
1 364 LYS n 
1 365 THR n 
1 366 ILE n 
1 367 TRP n 
1 368 GLY n 
1 369 ASP n 
1 370 ASP n 
1 371 VAL n 
1 372 GLU n 
1 373 GLU n 
1 374 PHE n 
1 375 ARG n 
1 376 PRO n 
1 377 GLU n 
1 378 ARG n 
1 379 PHE n 
1 380 GLU n 
1 381 ASN n 
1 382 PRO n 
1 383 SER n 
1 384 ALA n 
1 385 ILE n 
1 386 PRO n 
1 387 GLN n 
1 388 HIS n 
1 389 ALA n 
1 390 PHE n 
1 391 LYS n 
1 392 PRO n 
1 393 HIS n 
1 394 GLY n 
1 395 ASN n 
1 396 GLY n 
1 397 GLN n 
1 398 ARG n 
1 399 ALA n 
1 400 CYS n 
1 401 ILE n 
1 402 GLY n 
1 403 GLN n 
1 404 GLN n 
1 405 PHE n 
1 406 ALA n 
1 407 LEU n 
1 408 HIS n 
1 409 GLU n 
1 410 ALA n 
1 411 THR n 
1 412 LEU n 
1 413 VAL n 
1 414 LEU n 
1 415 GLY n 
1 416 MET n 
1 417 MET n 
1 418 LEU n 
1 419 LYS n 
1 420 HIS n 
1 421 PHE n 
1 422 ASP n 
1 423 PHE n 
1 424 GLU n 
1 425 ASP n 
1 426 HIS n 
1 427 THR n 
1 428 ASN n 
1 429 TYR n 
1 430 GLU n 
1 431 LEU n 
1 432 ASP n 
1 433 ILE n 
1 434 LYS n 
1 435 GLU n 
1 436 THR n 
1 437 LEU n 
1 438 THR n 
1 439 LEU n 
1 440 LYS n 
1 441 PRO n 
1 442 GLU n 
1 443 GLY n 
1 444 PHE n 
1 445 VAL n 
1 446 VAL n 
1 447 LYS n 
1 448 ALA n 
1 449 LYS n 
1 450 SER n 
1 451 LYS n 
1 452 LYS n 
1 453 ILE n 
1 454 PRO n 
1 455 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   455 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'NBRC 15308 = ATCC 14581' 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Priestia megaterium NBRC 15308 = ATCC 14581' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1348623 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                        ? 'C3 H7 N O2'       
89.093  
ARG 'L-peptide linking' y ARGININE                                                                       ? 'C6 H15 N4 O2 1'   
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                     ? 'C4 H8 N2 O3'      
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                ? 'C4 H7 N O4'       
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                       ? 'C3 H7 N O2 S'     
121.158 
D0L non-polymer         . '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' ? 'C21 H32 N2 O3'    
360.490 
GLN 'L-peptide linking' y GLUTAMINE                                                                      ? 'C5 H10 N2 O3'     
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                ? 'C5 H9 N O4'       
147.129 
GLY 'peptide linking'   y GLYCINE                                                                        ? 'C2 H5 N O2'       
75.067  
GOL non-polymer         . GLYCEROL                                                                       
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                              HEME 'C34 H32 Fe N4 O4' 
616.487 
HIS 'L-peptide linking' y HISTIDINE                                                                      ? 'C6 H10 N3 O2 1'   
156.162 
HOH non-polymer         . WATER                                                                          ? 'H2 O'             
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                     ? 'C6 H13 N O2'      
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                        ? 'C6 H13 N O2'      
131.173 
LYS 'L-peptide linking' y LYSINE                                                                         ? 'C6 H15 N2 O2 1'   
147.195 
MET 'L-peptide linking' y METHIONINE                                                                     ? 'C5 H11 N O2 S'    
149.211 
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  PHE 87  87  87  PHE PHE A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  TRP 90  90  90  TRP TRP A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  TRP 96  96  96  TRP TRP A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 MET 112 112 112 MET MET A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 HIS 116 116 116 HIS HIS A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLN 125 125 125 GLN GLN A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 TRP 130 130 130 TRP TRP A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 MET 145 145 145 MET MET A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 ASN 163 163 163 ASN ASN A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 HIS 171 171 171 HIS HIS A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 MET 177 177 177 MET MET A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ASN 192 192 192 ASN ASN A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 ASP 194 194 194 ASP ASP A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 LYS 202 202 202 LYS LYS A . n 
A 1 203 ARG 203 203 203 ARG ARG A . n 
A 1 204 GLN 204 204 204 GLN GLN A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 GLN 206 206 206 GLN GLN A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 LYS 210 210 210 LYS LYS A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 MET 212 212 212 MET MET A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 ASP 217 217 217 ASP ASP A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 HIS 236 236 236 HIS HIS A . n 
A 1 237 MET 237 237 237 MET MET A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 GLU 252 252 252 GLU GLU A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 ILE 254 254 254 ILE ILE A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 THR 260 260 260 THR THR A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 HIS 266 266 266 HIS HIS A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 TYR 278 278 278 TYR TYR A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 VAL 281 281 281 VAL VAL A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 ASN 283 283 283 ASN ASN A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 HIS 285 285 285 HIS HIS A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 ASP 300 300 300 ASP ASP A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 TYR 305 305 305 TYR TYR A . n 
A 1 306 LYS 306 306 306 LYS LYS A . n 
A 1 307 GLN 307 307 307 GLN GLN A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 TYR 313 313 313 TYR TYR A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 MET 316 316 316 MET MET A . n 
A 1 317 VAL 317 317 317 VAL VAL A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 ASN 319 319 319 ASN ASN A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 ARG 323 323 323 ARG ARG A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 TRP 325 325 325 TRP TRP A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 PRO 329 329 329 PRO PRO A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 PHE 331 331 331 PHE PHE A . n 
A 1 332 SER 332 332 332 SER SER A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 TYR 334 334 334 TYR TYR A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 ASP 338 338 338 ASP ASP A . n 
A 1 339 THR 339 339 339 THR THR A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 TYR 345 345 345 TYR TYR A . n 
A 1 346 PRO 346 346 346 PRO PRO A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 GLU 348 348 348 GLU GLU A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 ASP 351 351 351 ASP ASP A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 MET 354 354 354 MET MET A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 PRO 358 358 358 PRO PRO A . n 
A 1 359 GLN 359 359 359 GLN GLN A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 HIS 361 361 361 HIS HIS A . n 
A 1 362 ARG 362 362 362 ARG ARG A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 LYS 364 364 364 LYS LYS A . n 
A 1 365 THR 365 365 365 THR THR A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 TRP 367 367 367 TRP TRP A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 ASP 370 370 370 ASP ASP A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 PHE 374 374 374 PHE PHE A . n 
A 1 375 ARG 375 375 375 ARG ARG A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 GLU 377 377 377 GLU GLU A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 PHE 379 379 379 PHE PHE A . n 
A 1 380 GLU 380 380 380 GLU GLU A . n 
A 1 381 ASN 381 381 381 ASN ASN A . n 
A 1 382 PRO 382 382 382 PRO PRO A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 ALA 384 384 384 ALA ALA A . n 
A 1 385 ILE 385 385 385 ILE ILE A . n 
A 1 386 PRO 386 386 386 PRO PRO A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 HIS 388 388 388 HIS HIS A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 PHE 390 390 390 PHE PHE A . n 
A 1 391 LYS 391 391 391 LYS LYS A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 HIS 393 393 393 HIS HIS A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 GLY 396 396 396 GLY GLY A . n 
A 1 397 GLN 397 397 397 GLN GLN A . n 
A 1 398 ARG 398 398 398 ARG ARG A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 CYS 400 400 400 CYS CYS A . n 
A 1 401 ILE 401 401 401 ILE ILE A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 GLN 403 403 403 GLN GLN A . n 
A 1 404 GLN 404 404 404 GLN GLN A . n 
A 1 405 PHE 405 405 405 PHE PHE A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 LEU 407 407 407 LEU LEU A . n 
A 1 408 HIS 408 408 408 HIS HIS A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 THR 411 411 411 THR THR A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 VAL 413 413 413 VAL VAL A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 GLY 415 415 415 GLY GLY A . n 
A 1 416 MET 416 416 416 MET MET A . n 
A 1 417 MET 417 417 417 MET MET A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 LYS 419 419 419 LYS LYS A . n 
A 1 420 HIS 420 420 420 HIS HIS A . n 
A 1 421 PHE 421 421 421 PHE PHE A . n 
A 1 422 ASP 422 422 422 ASP ASP A . n 
A 1 423 PHE 423 423 423 PHE PHE A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 HIS 426 426 426 HIS HIS A . n 
A 1 427 THR 427 427 427 THR THR A . n 
A 1 428 ASN 428 428 428 ASN ASN A . n 
A 1 429 TYR 429 429 429 TYR TYR A . n 
A 1 430 GLU 430 430 430 GLU GLU A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 ILE 433 433 433 ILE ILE A . n 
A 1 434 LYS 434 434 434 LYS LYS A . n 
A 1 435 GLU 435 435 435 GLU GLU A . n 
A 1 436 THR 436 436 436 THR THR A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 PRO 441 441 441 PRO PRO A . n 
A 1 442 GLU 442 442 442 GLU GLU A . n 
A 1 443 GLY 443 443 443 GLY GLY A . n 
A 1 444 PHE 444 444 444 PHE PHE A . n 
A 1 445 VAL 445 445 445 VAL VAL A . n 
A 1 446 VAL 446 446 446 VAL VAL A . n 
A 1 447 LYS 447 447 447 LYS LYS A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 LYS 449 449 449 LYS LYS A . n 
A 1 450 SER 450 450 450 SER SER A . n 
A 1 451 LYS 451 451 451 LYS LYS A . n 
A 1 452 LYS 452 452 452 LYS LYS A . n 
A 1 453 ILE 453 453 453 ILE ILE A . n 
A 1 454 PRO 454 454 454 PRO PRO A . n 
A 1 455 LEU 455 455 455 LEU LEU A . n 
B 1 1   THR 1   1   1   THR THR B . n 
B 1 2   ILE 2   2   2   ILE ILE B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   GLU 4   4   4   GLU GLU B . n 
B 1 5   MET 5   5   5   MET MET B . n 
B 1 6   PRO 6   6   6   PRO PRO B . n 
B 1 7   GLN 7   7   7   GLN GLN B . n 
B 1 8   PRO 8   8   8   PRO PRO B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  THR 10  10  10  THR THR B . n 
B 1 11  PHE 11  11  11  PHE PHE B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  GLU 13  13  13  GLU GLU B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  PRO 18  18  18  PRO PRO B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  ASN 21  21  21  ASN ASN B . n 
B 1 22  THR 22  22  22  THR THR B . n 
B 1 23  ASP 23  23  23  ASP ASP B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  VAL 26  26  26  VAL VAL B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  MET 30  30  30  MET MET B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  ALA 33  33  33  ALA ALA B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  GLU 38  38  38  GLU GLU B . n 
B 1 39  ILE 39  39  39  ILE ILE B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  PHE 42  42  42  PHE PHE B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  GLN 55  55  55  GLN GLN B . n 
B 1 56  ARG 56  56  56  ARG ARG B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  CYS 62  62  62  CYS CYS B . n 
B 1 63  ASP 63  63  63  ASP ASP B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  PHE 67  67  67  PHE PHE B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  GLN 73  73  73  GLN GLN B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  PHE 77  77  77  PHE PHE B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  PHE 81  81  81  PHE PHE B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  TRP 90  90  90  TRP TRP B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  HIS 92  92  92  HIS HIS B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  TRP 96  96  96  TRP TRP B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  LYS 98  98  98  LYS LYS B . n 
B 1 99  ALA 99  99  99  ALA ALA B . n 
B 1 100 HIS 100 100 100 HIS HIS B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 PRO 105 105 105 PRO PRO B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 PHE 107 107 107 PHE PHE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLN 109 109 109 GLN GLN B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 MET 112 112 112 MET MET B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 TYR 115 115 115 TYR TYR B . n 
B 1 116 HIS 116 116 116 HIS HIS B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 MET 118 118 118 MET MET B . n 
B 1 119 MET 119 119 119 MET MET B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 GLN 125 125 125 GLN GLN B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 GLN 128 128 128 GLN GLN B . n 
B 1 129 LYS 129 129 129 LYS LYS B . n 
B 1 130 TRP 130 130 130 TRP TRP B . n 
B 1 131 GLU 131 131 131 GLU GLU B . n 
B 1 132 ARG 132 132 132 ARG ARG B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 GLU 143 143 143 GLU GLU B . n 
B 1 144 ASP 144 144 144 ASP ASP B . n 
B 1 145 MET 145 145 145 MET MET B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 ARG 147 147 147 ARG ARG B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 ASP 151 151 151 ASP ASP B . n 
B 1 152 THR 152 152 152 THR THR B . n 
B 1 153 ILE 153 153 153 ILE ILE B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 GLY 157 157 157 GLY GLY B . n 
B 1 158 PHE 158 158 158 PHE PHE B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 TYR 160 160 160 TYR TYR B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 PHE 162 162 162 PHE PHE B . n 
B 1 163 ASN 163 163 163 ASN ASN B . n 
B 1 164 SER 164 164 164 SER SER B . n 
B 1 165 PHE 165 165 165 PHE PHE B . n 
B 1 166 TYR 166 166 166 TYR TYR B . n 
B 1 167 ARG 167 167 167 ARG ARG B . n 
B 1 168 ASP 168 168 168 ASP ASP B . n 
B 1 169 GLN 169 169 169 GLN GLN B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 HIS 171 171 171 HIS HIS B . n 
B 1 172 PRO 172 172 172 PRO PRO B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 ILE 174 174 174 ILE ILE B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 SER 176 176 176 SER SER B . n 
B 1 177 MET 177 177 177 MET MET B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 ARG 179 179 179 ARG ARG B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 ASP 182 182 182 ASP ASP B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 ALA 184 184 184 ALA ALA B . n 
B 1 185 MET 185 185 185 MET MET B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 LYS 187 187 187 LYS LYS B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 ARG 190 190 190 ARG ARG B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 ASN 192 192 192 ASN ASN B . n 
B 1 193 PRO 193 193 193 PRO PRO B . n 
B 1 194 ASP 194 194 194 ASP ASP B . n 
B 1 195 ASP 195 195 195 ASP ASP B . n 
B 1 196 PRO 196 196 196 PRO PRO B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 TYR 198 198 198 TYR TYR B . n 
B 1 199 ASP 199 199 199 ASP ASP B . n 
B 1 200 GLU 200 200 200 GLU GLU B . n 
B 1 201 ASN 201 201 201 ASN ASN B . n 
B 1 202 LYS 202 202 202 LYS LYS B . n 
B 1 203 ARG 203 203 203 ARG ARG B . n 
B 1 204 GLN 204 204 204 GLN GLN B . n 
B 1 205 PHE 205 205 205 PHE PHE B . n 
B 1 206 GLN 206 206 206 GLN GLN B . n 
B 1 207 GLU 207 207 207 GLU GLU B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 ILE 209 209 209 ILE ILE B . n 
B 1 210 LYS 210 210 210 LYS LYS B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 MET 212 212 212 MET MET B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 ASP 214 214 214 ASP ASP B . n 
B 1 215 LEU 215 215 215 LEU LEU B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 ASP 217 217 217 ASP ASP B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 ALA 221 221 221 ALA ALA B . n 
B 1 222 ASP 222 222 222 ASP ASP B . n 
B 1 223 ARG 223 223 223 ARG ARG B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 SER 226 226 226 SER SER B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 SER 230 230 230 SER SER B . n 
B 1 231 ASP 231 231 231 ASP ASP B . n 
B 1 232 ASP 232 232 232 ASP ASP B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 THR 235 235 235 THR THR B . n 
B 1 236 HIS 236 236 236 HIS HIS B . n 
B 1 237 MET 237 237 237 MET MET B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 ASN 239 239 239 ASN ASN B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 LYS 241 241 241 LYS LYS B . n 
B 1 242 ASP 242 242 242 ASP ASP B . n 
B 1 243 PRO 243 243 243 PRO PRO B . n 
B 1 244 GLU 244 244 244 GLU GLU B . n 
B 1 245 THR 245 245 245 THR THR B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 PRO 248 248 248 PRO PRO B . n 
B 1 249 LEU 249 249 249 LEU LEU B . n 
B 1 250 ASP 250 250 250 ASP ASP B . n 
B 1 251 ASP 251 251 251 ASP ASP B . n 
B 1 252 GLU 252 252 252 GLU GLU B . n 
B 1 253 ASN 253 253 253 ASN ASN B . n 
B 1 254 ILE 254 254 254 ILE ILE B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 TYR 256 256 256 TYR TYR B . n 
B 1 257 GLN 257 257 257 GLN GLN B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 THR 260 260 260 THR THR B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ILE 263 263 263 ILE ILE B . n 
B 1 264 ALA 264 264 264 ALA ALA B . n 
B 1 265 GLY 265 265 265 GLY GLY B . n 
B 1 266 HIS 266 266 266 HIS HIS B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 THR 268 268 268 THR THR B . n 
B 1 269 THR 269 269 269 THR THR B . n 
B 1 270 SER 270 270 270 SER SER B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 SER 274 274 274 SER SER B . n 
B 1 275 PHE 275 275 275 PHE PHE B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 TYR 278 278 278 TYR TYR B . n 
B 1 279 PHE 279 279 279 PHE PHE B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 VAL 281 281 281 VAL VAL B . n 
B 1 282 LYS 282 282 282 LYS LYS B . n 
B 1 283 ASN 283 283 283 ASN ASN B . n 
B 1 284 PRO 284 284 284 PRO PRO B . n 
B 1 285 HIS 285 285 285 HIS HIS B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLN 288 288 288 GLN GLN B . n 
B 1 289 LYS 289 289 289 LYS LYS B . n 
B 1 290 ALA 290 290 290 ALA ALA B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 GLU 292 292 292 GLU GLU B . n 
B 1 293 GLU 293 293 293 GLU GLU B . n 
B 1 294 ALA 294 294 294 ALA ALA B . n 
B 1 295 ALA 295 295 295 ALA ALA B . n 
B 1 296 ARG 296 296 296 ARG ARG B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 LEU 298 298 298 LEU LEU B . n 
B 1 299 VAL 299 299 299 VAL VAL B . n 
B 1 300 ASP 300 300 300 ASP ASP B . n 
B 1 301 PRO 301 301 301 PRO PRO B . n 
B 1 302 VAL 302 302 302 VAL VAL B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 SER 304 304 304 SER SER B . n 
B 1 305 TYR 305 305 305 TYR TYR B . n 
B 1 306 LYS 306 306 306 LYS LYS B . n 
B 1 307 GLN 307 307 307 GLN GLN B . n 
B 1 308 VAL 308 308 308 VAL VAL B . n 
B 1 309 LYS 309 309 309 LYS LYS B . n 
B 1 310 GLN 310 310 310 GLN GLN B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 LYS 312 312 312 LYS LYS B . n 
B 1 313 TYR 313 313 313 TYR TYR B . n 
B 1 314 VAL 314 314 314 VAL VAL B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 MET 316 316 316 MET MET B . n 
B 1 317 VAL 317 317 317 VAL VAL B . n 
B 1 318 LEU 318 318 318 LEU LEU B . n 
B 1 319 ASN 319 319 319 ASN ASN B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 ALA 321 321 321 ALA ALA B . n 
B 1 322 LEU 322 322 322 LEU LEU B . n 
B 1 323 ARG 323 323 323 ARG ARG B . n 
B 1 324 LEU 324 324 324 LEU LEU B . n 
B 1 325 TRP 325 325 325 TRP TRP B . n 
B 1 326 PRO 326 326 326 PRO PRO B . n 
B 1 327 THR 327 327 327 THR THR B . n 
B 1 328 ALA 328 328 328 ALA ALA B . n 
B 1 329 PRO 329 329 329 PRO PRO B . n 
B 1 330 ALA 330 330 330 ALA ALA B . n 
B 1 331 PHE 331 331 331 PHE PHE B . n 
B 1 332 SER 332 332 332 SER SER B . n 
B 1 333 LEU 333 333 333 LEU LEU B . n 
B 1 334 TYR 334 334 334 TYR TYR B . n 
B 1 335 ALA 335 335 335 ALA ALA B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 GLU 337 337 337 GLU GLU B . n 
B 1 338 ASP 338 338 338 ASP ASP B . n 
B 1 339 THR 339 339 339 THR THR B . n 
B 1 340 VAL 340 340 340 VAL VAL B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 GLY 342 342 342 GLY GLY B . n 
B 1 343 GLY 343 343 343 GLY GLY B . n 
B 1 344 GLU 344 344 344 GLU GLU B . n 
B 1 345 TYR 345 345 345 TYR TYR B . n 
B 1 346 PRO 346 346 346 PRO PRO B . n 
B 1 347 LEU 347 347 347 LEU LEU B . n 
B 1 348 GLU 348 348 348 GLU GLU B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 GLY 350 350 350 GLY GLY B . n 
B 1 351 ASP 351 351 351 ASP ASP B . n 
B 1 352 GLU 352 352 352 GLU GLU B . n 
B 1 353 LEU 353 353 353 LEU LEU B . n 
B 1 354 MET 354 354 354 MET MET B . n 
B 1 355 VAL 355 355 355 VAL VAL B . n 
B 1 356 LEU 356 356 356 LEU LEU B . n 
B 1 357 ILE 357 357 357 ILE ILE B . n 
B 1 358 PRO 358 358 358 PRO PRO B . n 
B 1 359 GLN 359 359 359 GLN GLN B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 HIS 361 361 361 HIS HIS B . n 
B 1 362 ARG 362 362 362 ARG ARG B . n 
B 1 363 ASP 363 363 363 ASP ASP B . n 
B 1 364 LYS 364 364 364 LYS LYS B . n 
B 1 365 THR 365 365 365 THR THR B . n 
B 1 366 ILE 366 366 366 ILE ILE B . n 
B 1 367 TRP 367 367 367 TRP TRP B . n 
B 1 368 GLY 368 368 368 GLY GLY B . n 
B 1 369 ASP 369 369 369 ASP ASP B . n 
B 1 370 ASP 370 370 370 ASP ASP B . n 
B 1 371 VAL 371 371 371 VAL VAL B . n 
B 1 372 GLU 372 372 372 GLU GLU B . n 
B 1 373 GLU 373 373 373 GLU GLU B . n 
B 1 374 PHE 374 374 374 PHE PHE B . n 
B 1 375 ARG 375 375 375 ARG ARG B . n 
B 1 376 PRO 376 376 376 PRO PRO B . n 
B 1 377 GLU 377 377 377 GLU GLU B . n 
B 1 378 ARG 378 378 378 ARG ARG B . n 
B 1 379 PHE 379 379 379 PHE PHE B . n 
B 1 380 GLU 380 380 380 GLU GLU B . n 
B 1 381 ASN 381 381 381 ASN ASN B . n 
B 1 382 PRO 382 382 382 PRO PRO B . n 
B 1 383 SER 383 383 383 SER SER B . n 
B 1 384 ALA 384 384 384 ALA ALA B . n 
B 1 385 ILE 385 385 385 ILE ILE B . n 
B 1 386 PRO 386 386 386 PRO PRO B . n 
B 1 387 GLN 387 387 387 GLN GLN B . n 
B 1 388 HIS 388 388 388 HIS HIS B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 PHE 390 390 390 PHE PHE B . n 
B 1 391 LYS 391 391 391 LYS LYS B . n 
B 1 392 PRO 392 392 392 PRO PRO B . n 
B 1 393 HIS 393 393 393 HIS HIS B . n 
B 1 394 GLY 394 394 394 GLY GLY B . n 
B 1 395 ASN 395 395 395 ASN ASN B . n 
B 1 396 GLY 396 396 396 GLY GLY B . n 
B 1 397 GLN 397 397 397 GLN GLN B . n 
B 1 398 ARG 398 398 398 ARG ARG B . n 
B 1 399 ALA 399 399 399 ALA ALA B . n 
B 1 400 CYS 400 400 400 CYS CYS B . n 
B 1 401 ILE 401 401 401 ILE ILE B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 GLN 403 403 403 GLN GLN B . n 
B 1 404 GLN 404 404 404 GLN GLN B . n 
B 1 405 PHE 405 405 405 PHE PHE B . n 
B 1 406 ALA 406 406 406 ALA ALA B . n 
B 1 407 LEU 407 407 407 LEU LEU B . n 
B 1 408 HIS 408 408 408 HIS HIS B . n 
B 1 409 GLU 409 409 409 GLU GLU B . n 
B 1 410 ALA 410 410 410 ALA ALA B . n 
B 1 411 THR 411 411 411 THR THR B . n 
B 1 412 LEU 412 412 412 LEU LEU B . n 
B 1 413 VAL 413 413 413 VAL VAL B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 GLY 415 415 415 GLY GLY B . n 
B 1 416 MET 416 416 416 MET MET B . n 
B 1 417 MET 417 417 417 MET MET B . n 
B 1 418 LEU 418 418 418 LEU LEU B . n 
B 1 419 LYS 419 419 419 LYS LYS B . n 
B 1 420 HIS 420 420 420 HIS HIS B . n 
B 1 421 PHE 421 421 421 PHE PHE B . n 
B 1 422 ASP 422 422 422 ASP ASP B . n 
B 1 423 PHE 423 423 423 PHE PHE B . n 
B 1 424 GLU 424 424 424 GLU GLU B . n 
B 1 425 ASP 425 425 425 ASP ASP B . n 
B 1 426 HIS 426 426 426 HIS HIS B . n 
B 1 427 THR 427 427 427 THR THR B . n 
B 1 428 ASN 428 428 428 ASN ASN B . n 
B 1 429 TYR 429 429 429 TYR TYR B . n 
B 1 430 GLU 430 430 430 GLU GLU B . n 
B 1 431 LEU 431 431 431 LEU LEU B . n 
B 1 432 ASP 432 432 432 ASP ASP B . n 
B 1 433 ILE 433 433 433 ILE ILE B . n 
B 1 434 LYS 434 434 434 LYS LYS B . n 
B 1 435 GLU 435 435 435 GLU GLU B . n 
B 1 436 THR 436 436 436 THR THR B . n 
B 1 437 LEU 437 437 437 LEU LEU B . n 
B 1 438 THR 438 438 438 THR THR B . n 
B 1 439 LEU 439 439 439 LEU LEU B . n 
B 1 440 LYS 440 440 440 LYS LYS B . n 
B 1 441 PRO 441 441 441 PRO PRO B . n 
B 1 442 GLU 442 442 442 GLU GLU B . n 
B 1 443 GLY 443 443 443 GLY GLY B . n 
B 1 444 PHE 444 444 444 PHE PHE B . n 
B 1 445 VAL 445 445 445 VAL VAL B . n 
B 1 446 VAL 446 446 446 VAL VAL B . n 
B 1 447 LYS 447 447 447 LYS LYS B . n 
B 1 448 ALA 448 448 448 ALA ALA B . n 
B 1 449 LYS 449 449 449 LYS LYS B . n 
B 1 450 SER 450 450 450 SER SER B . n 
B 1 451 LYS 451 451 451 LYS LYS B . n 
B 1 452 LYS 452 452 452 LYS LYS B . n 
B 1 453 ILE 453 453 453 ILE ILE B . n 
B 1 454 PRO 454 454 454 PRO PRO B . n 
B 1 455 LEU 455 455 455 LEU LEU B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 HEM ? ? HEM ? ? 'SUBJECT OF INVESTIGATION' ? 
2 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 6 GOL 1   506  604 GOL GOL A . 
I 6 GOL 1   507  605 GOL GOL A . 
J 2 HEM 1   501  501 HEM HEM B . 
K 3 D0L 1   502  503 D0L 7PF B . 
L 4 SYN 1   503  601 SYN SYN B . 
M 5 OXY 1   504  602 OXY OXY B . 
N 6 GOL 1   505  603 GOL GOL B . 
O 6 GOL 1   506  604 GOL GOL B . 
P 6 GOL 1   507  606 GOL GOL B . 
Q 6 GOL 1   508  607 GOL GOL B . 
R 6 GOL 1   509  608 GOL GOL B . 
S 7 HOH 1   601  412 HOH HOH A . 
S 7 HOH 2   602  571 HOH HOH A . 
S 7 HOH 3   603  301 HOH HOH A . 
S 7 HOH 4   604  441 HOH HOH A . 
S 7 HOH 5   605  470 HOH HOH A . 
S 7 HOH 6   606  210 HOH HOH A . 
S 7 HOH 7   607  502 HOH HOH A . 
S 7 HOH 8   608  118 HOH HOH A . 
S 7 HOH 9   609  608 HOH HOH A . 
S 7 HOH 10  610  565 HOH HOH A . 
S 7 HOH 11  611  636 HOH HOH A . 
S 7 HOH 12  612  365 HOH HOH A . 
S 7 HOH 13  613  243 HOH HOH A . 
S 7 HOH 14  614  197 HOH HOH A . 
S 7 HOH 15  615  370 HOH HOH A . 
S 7 HOH 16  616  754 HOH HOH A . 
S 7 HOH 17  617  538 HOH HOH A . 
S 7 HOH 18  618  481 HOH HOH A . 
S 7 HOH 19  619  586 HOH HOH A . 
S 7 HOH 20  620  535 HOH HOH A . 
S 7 HOH 21  621  525 HOH HOH A . 
S 7 HOH 22  622  630 HOH HOH A . 
S 7 HOH 23  623  306 HOH HOH A . 
S 7 HOH 24  624  779 HOH HOH A . 
S 7 HOH 25  625  59  HOH HOH A . 
S 7 HOH 26  626  765 HOH HOH A . 
S 7 HOH 27  627  560 HOH HOH A . 
S 7 HOH 28  628  372 HOH HOH A . 
S 7 HOH 29  629  684 HOH HOH A . 
S 7 HOH 30  630  590 HOH HOH A . 
S 7 HOH 31  631  465 HOH HOH A . 
S 7 HOH 32  632  90  HOH HOH A . 
S 7 HOH 33  633  150 HOH HOH A . 
S 7 HOH 34  634  275 HOH HOH A . 
S 7 HOH 35  635  424 HOH HOH A . 
S 7 HOH 36  636  18  HOH HOH A . 
S 7 HOH 37  637  516 HOH HOH A . 
S 7 HOH 38  638  157 HOH HOH A . 
S 7 HOH 39  639  164 HOH HOH A . 
S 7 HOH 40  640  519 HOH HOH A . 
S 7 HOH 41  641  50  HOH HOH A . 
S 7 HOH 42  642  19  HOH HOH A . 
S 7 HOH 43  643  392 HOH HOH A . 
S 7 HOH 44  644  155 HOH HOH A . 
S 7 HOH 45  645  91  HOH HOH A . 
S 7 HOH 46  646  264 HOH HOH A . 
S 7 HOH 47  647  312 HOH HOH A . 
S 7 HOH 48  648  196 HOH HOH A . 
S 7 HOH 49  649  94  HOH HOH A . 
S 7 HOH 50  650  240 HOH HOH A . 
S 7 HOH 51  651  76  HOH HOH A . 
S 7 HOH 52  652  389 HOH HOH A . 
S 7 HOH 53  653  252 HOH HOH A . 
S 7 HOH 54  654  353 HOH HOH A . 
S 7 HOH 55  655  190 HOH HOH A . 
S 7 HOH 56  656  354 HOH HOH A . 
S 7 HOH 57  657  97  HOH HOH A . 
S 7 HOH 58  658  62  HOH HOH A . 
S 7 HOH 59  659  236 HOH HOH A . 
S 7 HOH 60  660  693 HOH HOH A . 
S 7 HOH 61  661  696 HOH HOH A . 
S 7 HOH 62  662  522 HOH HOH A . 
S 7 HOH 63  663  8   HOH HOH A . 
S 7 HOH 64  664  689 HOH HOH A . 
S 7 HOH 65  665  67  HOH HOH A . 
S 7 HOH 66  666  199 HOH HOH A . 
S 7 HOH 67  667  1   HOH HOH A . 
S 7 HOH 68  668  159 HOH HOH A . 
S 7 HOH 69  669  309 HOH HOH A . 
S 7 HOH 70  670  72  HOH HOH A . 
S 7 HOH 71  671  293 HOH HOH A . 
S 7 HOH 72  672  174 HOH HOH A . 
S 7 HOH 73  673  88  HOH HOH A . 
S 7 HOH 74  674  188 HOH HOH A . 
S 7 HOH 75  675  156 HOH HOH A . 
S 7 HOH 76  676  37  HOH HOH A . 
S 7 HOH 77  677  377 HOH HOH A . 
S 7 HOH 78  678  78  HOH HOH A . 
S 7 HOH 79  679  552 HOH HOH A . 
S 7 HOH 80  680  172 HOH HOH A . 
S 7 HOH 81  681  363 HOH HOH A . 
S 7 HOH 82  682  81  HOH HOH A . 
S 7 HOH 83  683  504 HOH HOH A . 
S 7 HOH 84  684  298 HOH HOH A . 
S 7 HOH 85  685  161 HOH HOH A . 
S 7 HOH 86  686  368 HOH HOH A . 
S 7 HOH 87  687  149 HOH HOH A . 
S 7 HOH 88  688  98  HOH HOH A . 
S 7 HOH 89  689  348 HOH HOH A . 
S 7 HOH 90  690  148 HOH HOH A . 
S 7 HOH 91  691  324 HOH HOH A . 
S 7 HOH 92  692  121 HOH HOH A . 
S 7 HOH 93  693  362 HOH HOH A . 
S 7 HOH 94  694  281 HOH HOH A . 
S 7 HOH 95  695  401 HOH HOH A . 
S 7 HOH 96  696  208 HOH HOH A . 
S 7 HOH 97  697  532 HOH HOH A . 
S 7 HOH 98  698  185 HOH HOH A . 
S 7 HOH 99  699  12  HOH HOH A . 
S 7 HOH 100 700  47  HOH HOH A . 
S 7 HOH 101 701  22  HOH HOH A . 
S 7 HOH 102 702  183 HOH HOH A . 
S 7 HOH 103 703  219 HOH HOH A . 
S 7 HOH 104 704  200 HOH HOH A . 
S 7 HOH 105 705  321 HOH HOH A . 
S 7 HOH 106 706  227 HOH HOH A . 
S 7 HOH 107 707  595 HOH HOH A . 
S 7 HOH 108 708  512 HOH HOH A . 
S 7 HOH 109 709  500 HOH HOH A . 
S 7 HOH 110 710  224 HOH HOH A . 
S 7 HOH 111 711  49  HOH HOH A . 
S 7 HOH 112 712  317 HOH HOH A . 
S 7 HOH 113 713  588 HOH HOH A . 
S 7 HOH 114 714  64  HOH HOH A . 
S 7 HOH 115 715  79  HOH HOH A . 
S 7 HOH 116 716  15  HOH HOH A . 
S 7 HOH 117 717  71  HOH HOH A . 
S 7 HOH 118 718  198 HOH HOH A . 
S 7 HOH 119 719  338 HOH HOH A . 
S 7 HOH 120 720  9   HOH HOH A . 
S 7 HOH 121 721  603 HOH HOH A . 
S 7 HOH 122 722  694 HOH HOH A . 
S 7 HOH 123 723  258 HOH HOH A . 
S 7 HOH 124 724  428 HOH HOH A . 
S 7 HOH 125 725  60  HOH HOH A . 
S 7 HOH 126 726  395 HOH HOH A . 
S 7 HOH 127 727  36  HOH HOH A . 
S 7 HOH 128 728  272 HOH HOH A . 
S 7 HOH 129 729  709 HOH HOH A . 
S 7 HOH 130 730  16  HOH HOH A . 
S 7 HOH 131 731  195 HOH HOH A . 
S 7 HOH 132 732  739 HOH HOH A . 
S 7 HOH 133 733  521 HOH HOH A . 
S 7 HOH 134 734  345 HOH HOH A . 
S 7 HOH 135 735  688 HOH HOH A . 
S 7 HOH 136 736  51  HOH HOH A . 
S 7 HOH 137 737  202 HOH HOH A . 
S 7 HOH 138 738  690 HOH HOH A . 
S 7 HOH 139 739  374 HOH HOH A . 
S 7 HOH 140 740  110 HOH HOH A . 
S 7 HOH 141 741  755 HOH HOH A . 
S 7 HOH 142 742  93  HOH HOH A . 
S 7 HOH 143 743  697 HOH HOH A . 
S 7 HOH 144 744  505 HOH HOH A . 
S 7 HOH 145 745  577 HOH HOH A . 
S 7 HOH 146 746  341 HOH HOH A . 
S 7 HOH 147 747  680 HOH HOH A . 
S 7 HOH 148 748  598 HOH HOH A . 
S 7 HOH 149 749  299 HOH HOH A . 
S 7 HOH 150 750  176 HOH HOH A . 
S 7 HOH 151 751  611 HOH HOH A . 
S 7 HOH 152 752  249 HOH HOH A . 
S 7 HOH 153 753  178 HOH HOH A . 
S 7 HOH 154 754  134 HOH HOH A . 
S 7 HOH 155 755  524 HOH HOH A . 
S 7 HOH 156 756  513 HOH HOH A . 
S 7 HOH 157 757  135 HOH HOH A . 
S 7 HOH 158 758  744 HOH HOH A . 
S 7 HOH 159 759  490 HOH HOH A . 
S 7 HOH 160 760  276 HOH HOH A . 
S 7 HOH 161 761  26  HOH HOH A . 
S 7 HOH 162 762  403 HOH HOH A . 
S 7 HOH 163 763  230 HOH HOH A . 
S 7 HOH 164 764  17  HOH HOH A . 
S 7 HOH 165 765  431 HOH HOH A . 
S 7 HOH 166 766  753 HOH HOH A . 
S 7 HOH 167 767  668 HOH HOH A . 
S 7 HOH 168 768  698 HOH HOH A . 
S 7 HOH 169 769  704 HOH HOH A . 
S 7 HOH 170 770  286 HOH HOH A . 
S 7 HOH 171 771  639 HOH HOH A . 
S 7 HOH 172 772  316 HOH HOH A . 
S 7 HOH 173 773  332 HOH HOH A . 
S 7 HOH 174 774  404 HOH HOH A . 
S 7 HOH 175 775  65  HOH HOH A . 
S 7 HOH 176 776  710 HOH HOH A . 
S 7 HOH 177 777  714 HOH HOH A . 
S 7 HOH 178 778  27  HOH HOH A . 
S 7 HOH 179 779  89  HOH HOH A . 
S 7 HOH 180 780  204 HOH HOH A . 
S 7 HOH 181 781  290 HOH HOH A . 
S 7 HOH 182 782  248 HOH HOH A . 
S 7 HOH 183 783  323 HOH HOH A . 
S 7 HOH 184 784  203 HOH HOH A . 
S 7 HOH 185 785  44  HOH HOH A . 
S 7 HOH 186 786  163 HOH HOH A . 
S 7 HOH 187 787  726 HOH HOH A . 
S 7 HOH 188 788  607 HOH HOH A . 
S 7 HOH 189 789  434 HOH HOH A . 
S 7 HOH 190 790  6   HOH HOH A . 
S 7 HOH 191 791  661 HOH HOH A . 
S 7 HOH 192 792  498 HOH HOH A . 
S 7 HOH 193 793  561 HOH HOH A . 
S 7 HOH 194 794  700 HOH HOH A . 
S 7 HOH 195 795  228 HOH HOH A . 
S 7 HOH 196 796  499 HOH HOH A . 
S 7 HOH 197 797  640 HOH HOH A . 
S 7 HOH 198 798  475 HOH HOH A . 
S 7 HOH 199 799  462 HOH HOH A . 
S 7 HOH 200 800  489 HOH HOH A . 
S 7 HOH 201 801  622 HOH HOH A . 
S 7 HOH 202 802  70  HOH HOH A . 
S 7 HOH 203 803  583 HOH HOH A . 
S 7 HOH 204 804  113 HOH HOH A . 
S 7 HOH 205 805  132 HOH HOH A . 
S 7 HOH 206 806  225 HOH HOH A . 
S 7 HOH 207 807  318 HOH HOH A . 
S 7 HOH 208 808  100 HOH HOH A . 
S 7 HOH 209 809  764 HOH HOH A . 
S 7 HOH 210 810  115 HOH HOH A . 
S 7 HOH 211 811  567 HOH HOH A . 
S 7 HOH 212 812  234 HOH HOH A . 
S 7 HOH 213 813  543 HOH HOH A . 
S 7 HOH 214 814  629 HOH HOH A . 
S 7 HOH 215 815  56  HOH HOH A . 
S 7 HOH 216 816  387 HOH HOH A . 
S 7 HOH 217 817  425 HOH HOH A . 
S 7 HOH 218 818  307 HOH HOH A . 
S 7 HOH 219 819  214 HOH HOH A . 
S 7 HOH 220 820  103 HOH HOH A . 
S 7 HOH 221 821  456 HOH HOH A . 
S 7 HOH 222 822  763 HOH HOH A . 
S 7 HOH 223 823  257 HOH HOH A . 
S 7 HOH 224 824  592 HOH HOH A . 
S 7 HOH 225 825  261 HOH HOH A . 
S 7 HOH 226 826  760 HOH HOH A . 
S 7 HOH 227 827  288 HOH HOH A . 
S 7 HOH 228 828  767 HOH HOH A . 
S 7 HOH 229 829  326 HOH HOH A . 
S 7 HOH 230 830  547 HOH HOH A . 
S 7 HOH 231 831  582 HOH HOH A . 
S 7 HOH 232 832  488 HOH HOH A . 
S 7 HOH 233 833  297 HOH HOH A . 
S 7 HOH 234 834  719 HOH HOH A . 
S 7 HOH 235 835  141 HOH HOH A . 
S 7 HOH 236 836  718 HOH HOH A . 
S 7 HOH 237 837  729 HOH HOH A . 
S 7 HOH 238 838  20  HOH HOH A . 
S 7 HOH 239 839  305 HOH HOH A . 
S 7 HOH 240 840  201 HOH HOH A . 
S 7 HOH 241 841  215 HOH HOH A . 
S 7 HOH 242 842  445 HOH HOH A . 
S 7 HOH 243 843  349 HOH HOH A . 
S 7 HOH 244 844  102 HOH HOH A . 
S 7 HOH 245 845  406 HOH HOH A . 
S 7 HOH 246 846  391 HOH HOH A . 
S 7 HOH 247 847  621 HOH HOH A . 
S 7 HOH 248 848  478 HOH HOH A . 
S 7 HOH 249 849  254 HOH HOH A . 
S 7 HOH 250 850  46  HOH HOH A . 
S 7 HOH 251 851  666 HOH HOH A . 
S 7 HOH 252 852  440 HOH HOH A . 
S 7 HOH 253 853  393 HOH HOH A . 
S 7 HOH 254 854  402 HOH HOH A . 
S 7 HOH 255 855  757 HOH HOH A . 
S 7 HOH 256 856  509 HOH HOH A . 
S 7 HOH 257 857  731 HOH HOH A . 
S 7 HOH 258 858  284 HOH HOH A . 
S 7 HOH 259 859  670 HOH HOH A . 
S 7 HOH 260 860  350 HOH HOH A . 
S 7 HOH 261 861  759 HOH HOH A . 
S 7 HOH 262 862  390 HOH HOH A . 
S 7 HOH 263 863  496 HOH HOH A . 
S 7 HOH 264 864  194 HOH HOH A . 
S 7 HOH 265 865  658 HOH HOH A . 
S 7 HOH 266 866  279 HOH HOH A . 
S 7 HOH 267 867  463 HOH HOH A . 
S 7 HOH 268 868  277 HOH HOH A . 
S 7 HOH 269 869  644 HOH HOH A . 
S 7 HOH 270 870  609 HOH HOH A . 
S 7 HOH 271 871  211 HOH HOH A . 
S 7 HOH 272 872  95  HOH HOH A . 
S 7 HOH 273 873  493 HOH HOH A . 
S 7 HOH 274 874  221 HOH HOH A . 
S 7 HOH 275 875  742 HOH HOH A . 
S 7 HOH 276 876  432 HOH HOH A . 
S 7 HOH 277 877  676 HOH HOH A . 
S 7 HOH 278 878  244 HOH HOH A . 
S 7 HOH 279 879  514 HOH HOH A . 
S 7 HOH 280 880  708 HOH HOH A . 
S 7 HOH 281 881  206 HOH HOH A . 
S 7 HOH 282 882  448 HOH HOH A . 
S 7 HOH 283 883  777 HOH HOH A . 
S 7 HOH 284 884  692 HOH HOH A . 
S 7 HOH 285 885  667 HOH HOH A . 
S 7 HOH 286 886  415 HOH HOH A . 
S 7 HOH 287 887  762 HOH HOH A . 
S 7 HOH 288 888  507 HOH HOH A . 
S 7 HOH 289 889  682 HOH HOH A . 
S 7 HOH 290 890  679 HOH HOH A . 
S 7 HOH 291 891  749 HOH HOH A . 
S 7 HOH 292 892  722 HOH HOH A . 
S 7 HOH 293 893  416 HOH HOH A . 
S 7 HOH 294 894  573 HOH HOH A . 
S 7 HOH 295 895  433 HOH HOH A . 
S 7 HOH 296 896  480 HOH HOH A . 
S 7 HOH 297 897  400 HOH HOH A . 
S 7 HOH 298 898  587 HOH HOH A . 
S 7 HOH 299 899  705 HOH HOH A . 
S 7 HOH 300 900  367 HOH HOH A . 
S 7 HOH 301 901  302 HOH HOH A . 
S 7 HOH 302 902  13  HOH HOH A . 
S 7 HOH 303 903  735 HOH HOH A . 
S 7 HOH 304 904  774 HOH HOH A . 
S 7 HOH 305 905  539 HOH HOH A . 
S 7 HOH 306 906  669 HOH HOH A . 
S 7 HOH 307 907  405 HOH HOH A . 
S 7 HOH 308 908  304 HOH HOH A . 
S 7 HOH 309 909  491 HOH HOH A . 
S 7 HOH 310 910  554 HOH HOH A . 
S 7 HOH 311 911  165 HOH HOH A . 
S 7 HOH 312 912  548 HOH HOH A . 
S 7 HOH 313 913  536 HOH HOH A . 
S 7 HOH 314 914  713 HOH HOH A . 
S 7 HOH 315 915  618 HOH HOH A . 
S 7 HOH 316 916  712 HOH HOH A . 
S 7 HOH 317 917  615 HOH HOH A . 
S 7 HOH 318 918  637 HOH HOH A . 
S 7 HOH 319 919  736 HOH HOH A . 
S 7 HOH 320 920  557 HOH HOH A . 
S 7 HOH 321 921  551 HOH HOH A . 
S 7 HOH 322 922  464 HOH HOH A . 
S 7 HOH 323 923  728 HOH HOH A . 
S 7 HOH 324 924  601 HOH HOH A . 
S 7 HOH 325 925  213 HOH HOH A . 
S 7 HOH 326 926  559 HOH HOH A . 
S 7 HOH 327 927  563 HOH HOH A . 
S 7 HOH 328 928  745 HOH HOH A . 
S 7 HOH 329 929  280 HOH HOH A . 
S 7 HOH 330 930  568 HOH HOH A . 
S 7 HOH 331 931  330 HOH HOH A . 
S 7 HOH 332 932  310 HOH HOH A . 
S 7 HOH 333 933  455 HOH HOH A . 
S 7 HOH 334 934  410 HOH HOH A . 
S 7 HOH 335 935  746 HOH HOH A . 
S 7 HOH 336 936  129 HOH HOH A . 
S 7 HOH 337 937  702 HOH HOH A . 
S 7 HOH 338 938  650 HOH HOH A . 
S 7 HOH 339 939  315 HOH HOH A . 
S 7 HOH 340 940  511 HOH HOH A . 
S 7 HOH 341 941  447 HOH HOH A . 
S 7 HOH 342 942  313 HOH HOH A . 
S 7 HOH 343 943  421 HOH HOH A . 
S 7 HOH 344 944  435 HOH HOH A . 
S 7 HOH 345 945  659 HOH HOH A . 
S 7 HOH 346 946  613 HOH HOH A . 
S 7 HOH 347 947  672 HOH HOH A . 
S 7 HOH 348 948  716 HOH HOH A . 
S 7 HOH 349 949  677 HOH HOH A . 
S 7 HOH 350 950  238 HOH HOH A . 
S 7 HOH 351 951  625 HOH HOH A . 
S 7 HOH 352 952  645 HOH HOH A . 
S 7 HOH 353 953  231 HOH HOH A . 
S 7 HOH 354 954  740 HOH HOH A . 
S 7 HOH 355 955  357 HOH HOH A . 
S 7 HOH 356 956  751 HOH HOH A . 
T 7 HOH 1   601  600 HOH HOH B . 
T 7 HOH 2   602  473 HOH HOH B . 
T 7 HOH 3   603  506 HOH HOH B . 
T 7 HOH 4   604  750 HOH HOH B . 
T 7 HOH 5   605  772 HOH HOH B . 
T 7 HOH 6   606  409 HOH HOH B . 
T 7 HOH 7   607  429 HOH HOH B . 
T 7 HOH 8   608  340 HOH HOH B . 
T 7 HOH 9   609  476 HOH HOH B . 
T 7 HOH 10  610  339 HOH HOH B . 
T 7 HOH 11  611  383 HOH HOH B . 
T 7 HOH 12  612  540 HOH HOH B . 
T 7 HOH 13  613  474 HOH HOH B . 
T 7 HOH 14  614  169 HOH HOH B . 
T 7 HOH 15  615  384 HOH HOH B . 
T 7 HOH 16  616  537 HOH HOH B . 
T 7 HOH 17  617  581 HOH HOH B . 
T 7 HOH 18  618  216 HOH HOH B . 
T 7 HOH 19  619  624 HOH HOH B . 
T 7 HOH 20  620  616 HOH HOH B . 
T 7 HOH 21  621  715 HOH HOH B . 
T 7 HOH 22  622  446 HOH HOH B . 
T 7 HOH 23  623  515 HOH HOH B . 
T 7 HOH 24  624  501 HOH HOH B . 
T 7 HOH 25  625  439 HOH HOH B . 
T 7 HOH 26  626  308 HOH HOH B . 
T 7 HOH 27  627  591 HOH HOH B . 
T 7 HOH 28  628  373 HOH HOH B . 
T 7 HOH 29  629  351 HOH HOH B . 
T 7 HOH 30  630  673 HOH HOH B . 
T 7 HOH 31  631  584 HOH HOH B . 
T 7 HOH 32  632  96  HOH HOH B . 
T 7 HOH 33  633  369 HOH HOH B . 
T 7 HOH 34  634  398 HOH HOH B . 
T 7 HOH 35  635  396 HOH HOH B . 
T 7 HOH 36  636  378 HOH HOH B . 
T 7 HOH 37  637  652 HOH HOH B . 
T 7 HOH 38  638  533 HOH HOH B . 
T 7 HOH 39  639  7   HOH HOH B . 
T 7 HOH 40  640  300 HOH HOH B . 
T 7 HOH 41  641  725 HOH HOH B . 
T 7 HOH 42  642  564 HOH HOH B . 
T 7 HOH 43  643  494 HOH HOH B . 
T 7 HOH 44  644  77  HOH HOH B . 
T 7 HOH 45  645  411 HOH HOH B . 
T 7 HOH 46  646  256 HOH HOH B . 
T 7 HOH 47  647  472 HOH HOH B . 
T 7 HOH 48  648  413 HOH HOH B . 
T 7 HOH 49  649  263 HOH HOH B . 
T 7 HOH 50  650  769 HOH HOH B . 
T 7 HOH 51  651  145 HOH HOH B . 
T 7 HOH 52  652  575 HOH HOH B . 
T 7 HOH 53  653  170 HOH HOH B . 
T 7 HOH 54  654  24  HOH HOH B . 
T 7 HOH 55  655  80  HOH HOH B . 
T 7 HOH 56  656  109 HOH HOH B . 
T 7 HOH 57  657  253 HOH HOH B . 
T 7 HOH 58  658  327 HOH HOH B . 
T 7 HOH 59  659  619 HOH HOH B . 
T 7 HOH 60  660  125 HOH HOH B . 
T 7 HOH 61  661  105 HOH HOH B . 
T 7 HOH 62  662  48  HOH HOH B . 
T 7 HOH 63  663  419 HOH HOH B . 
T 7 HOH 64  664  485 HOH HOH B . 
T 7 HOH 65  665  54  HOH HOH B . 
T 7 HOH 66  666  282 HOH HOH B . 
T 7 HOH 67  667  151 HOH HOH B . 
T 7 HOH 68  668  111 HOH HOH B . 
T 7 HOH 69  669  86  HOH HOH B . 
T 7 HOH 70  670  108 HOH HOH B . 
T 7 HOH 71  671  28  HOH HOH B . 
T 7 HOH 72  672  255 HOH HOH B . 
T 7 HOH 73  673  177 HOH HOH B . 
T 7 HOH 74  674  175 HOH HOH B . 
T 7 HOH 75  675  597 HOH HOH B . 
T 7 HOH 76  676  328 HOH HOH B . 
T 7 HOH 77  677  68  HOH HOH B . 
T 7 HOH 78  678  119 HOH HOH B . 
T 7 HOH 79  679  466 HOH HOH B . 
T 7 HOH 80  680  33  HOH HOH B . 
T 7 HOH 81  681  529 HOH HOH B . 
T 7 HOH 82  682  344 HOH HOH B . 
T 7 HOH 83  683  63  HOH HOH B . 
T 7 HOH 84  684  517 HOH HOH B . 
T 7 HOH 85  685  520 HOH HOH B . 
T 7 HOH 86  686  265 HOH HOH B . 
T 7 HOH 87  687  220 HOH HOH B . 
T 7 HOH 88  688  761 HOH HOH B . 
T 7 HOH 89  689  523 HOH HOH B . 
T 7 HOH 90  690  262 HOH HOH B . 
T 7 HOH 91  691  127 HOH HOH B . 
T 7 HOH 92  692  239 HOH HOH B . 
T 7 HOH 93  693  55  HOH HOH B . 
T 7 HOH 94  694  483 HOH HOH B . 
T 7 HOH 95  695  399 HOH HOH B . 
T 7 HOH 96  696  128 HOH HOH B . 
T 7 HOH 97  697  487 HOH HOH B . 
T 7 HOH 98  698  268 HOH HOH B . 
T 7 HOH 99  699  589 HOH HOH B . 
T 7 HOH 100 700  3   HOH HOH B . 
T 7 HOH 101 701  269 HOH HOH B . 
T 7 HOH 102 702  66  HOH HOH B . 
T 7 HOH 103 703  270 HOH HOH B . 
T 7 HOH 104 704  237 HOH HOH B . 
T 7 HOH 105 705  69  HOH HOH B . 
T 7 HOH 106 706  648 HOH HOH B . 
T 7 HOH 107 707  241 HOH HOH B . 
T 7 HOH 108 708  271 HOH HOH B . 
T 7 HOH 109 709  620 HOH HOH B . 
T 7 HOH 110 710  179 HOH HOH B . 
T 7 HOH 111 711  657 HOH HOH B . 
T 7 HOH 112 712  706 HOH HOH B . 
T 7 HOH 113 713  160 HOH HOH B . 
T 7 HOH 114 714  510 HOH HOH B . 
T 7 HOH 115 715  260 HOH HOH B . 
T 7 HOH 116 716  217 HOH HOH B . 
T 7 HOH 117 717  5   HOH HOH B . 
T 7 HOH 118 718  31  HOH HOH B . 
T 7 HOH 119 719  82  HOH HOH B . 
T 7 HOH 120 720  152 HOH HOH B . 
T 7 HOH 121 721  112 HOH HOH B . 
T 7 HOH 122 722  371 HOH HOH B . 
T 7 HOH 123 723  143 HOH HOH B . 
T 7 HOH 124 724  333 HOH HOH B . 
T 7 HOH 125 725  130 HOH HOH B . 
T 7 HOH 126 726  375 HOH HOH B . 
T 7 HOH 127 727  73  HOH HOH B . 
T 7 HOH 128 728  87  HOH HOH B . 
T 7 HOH 129 729  123 HOH HOH B . 
T 7 HOH 130 730  273 HOH HOH B . 
T 7 HOH 131 731  508 HOH HOH B . 
T 7 HOH 132 732  319 HOH HOH B . 
T 7 HOH 133 733  632 HOH HOH B . 
T 7 HOH 134 734  10  HOH HOH B . 
T 7 HOH 135 735  117 HOH HOH B . 
T 7 HOH 136 736  122 HOH HOH B . 
T 7 HOH 137 737  289 HOH HOH B . 
T 7 HOH 138 738  21  HOH HOH B . 
T 7 HOH 139 739  41  HOH HOH B . 
T 7 HOH 140 740  184 HOH HOH B . 
T 7 HOH 141 741  171 HOH HOH B . 
T 7 HOH 142 742  342 HOH HOH B . 
T 7 HOH 143 743  593 HOH HOH B . 
T 7 HOH 144 744  154 HOH HOH B . 
T 7 HOH 145 745  662 HOH HOH B . 
T 7 HOH 146 746  104 HOH HOH B . 
T 7 HOH 147 747  443 HOH HOH B . 
T 7 HOH 148 748  329 HOH HOH B . 
T 7 HOH 149 749  599 HOH HOH B . 
T 7 HOH 150 750  451 HOH HOH B . 
T 7 HOH 151 751  14  HOH HOH B . 
T 7 HOH 152 752  52  HOH HOH B . 
T 7 HOH 153 753  449 HOH HOH B . 
T 7 HOH 154 754  245 HOH HOH B . 
T 7 HOH 155 755  322 HOH HOH B . 
T 7 HOH 156 756  25  HOH HOH B . 
T 7 HOH 157 757  182 HOH HOH B . 
T 7 HOH 158 758  580 HOH HOH B . 
T 7 HOH 159 759  355 HOH HOH B . 
T 7 HOH 160 760  187 HOH HOH B . 
T 7 HOH 161 761  75  HOH HOH B . 
T 7 HOH 162 762  337 HOH HOH B . 
T 7 HOH 163 763  296 HOH HOH B . 
T 7 HOH 164 764  58  HOH HOH B . 
T 7 HOH 165 765  181 HOH HOH B . 
T 7 HOH 166 766  388 HOH HOH B . 
T 7 HOH 167 767  471 HOH HOH B . 
T 7 HOH 168 768  4   HOH HOH B . 
T 7 HOH 169 769  162 HOH HOH B . 
T 7 HOH 170 770  38  HOH HOH B . 
T 7 HOH 171 771  542 HOH HOH B . 
T 7 HOH 172 772  295 HOH HOH B . 
T 7 HOH 173 773  53  HOH HOH B . 
T 7 HOH 174 774  74  HOH HOH B . 
T 7 HOH 175 775  267 HOH HOH B . 
T 7 HOH 176 776  711 HOH HOH B . 
T 7 HOH 177 777  209 HOH HOH B . 
T 7 HOH 178 778  766 HOH HOH B . 
T 7 HOH 179 779  2   HOH HOH B . 
T 7 HOH 180 780  247 HOH HOH B . 
T 7 HOH 181 781  83  HOH HOH B . 
T 7 HOH 182 782  576 HOH HOH B . 
T 7 HOH 183 783  660 HOH HOH B . 
T 7 HOH 184 784  92  HOH HOH B . 
T 7 HOH 185 785  120 HOH HOH B . 
T 7 HOH 186 786  126 HOH HOH B . 
T 7 HOH 187 787  292 HOH HOH B . 
T 7 HOH 188 788  331 HOH HOH B . 
T 7 HOH 189 789  107 HOH HOH B . 
T 7 HOH 190 790  137 HOH HOH B . 
T 7 HOH 191 791  30  HOH HOH B . 
T 7 HOH 192 792  450 HOH HOH B . 
T 7 HOH 193 793  39  HOH HOH B . 
T 7 HOH 194 794  124 HOH HOH B . 
T 7 HOH 195 795  366 HOH HOH B . 
T 7 HOH 196 796  45  HOH HOH B . 
T 7 HOH 197 797  604 HOH HOH B . 
T 7 HOH 198 798  42  HOH HOH B . 
T 7 HOH 199 799  732 HOH HOH B . 
T 7 HOH 200 800  457 HOH HOH B . 
T 7 HOH 201 801  285 HOH HOH B . 
T 7 HOH 202 802  23  HOH HOH B . 
T 7 HOH 203 803  758 HOH HOH B . 
T 7 HOH 204 804  335 HOH HOH B . 
T 7 HOH 205 805  40  HOH HOH B . 
T 7 HOH 206 806  207 HOH HOH B . 
T 7 HOH 207 807  638 HOH HOH B . 
T 7 HOH 208 808  43  HOH HOH B . 
T 7 HOH 209 809  142 HOH HOH B . 
T 7 HOH 210 810  647 HOH HOH B . 
T 7 HOH 211 811  173 HOH HOH B . 
T 7 HOH 212 812  250 HOH HOH B . 
T 7 HOH 213 813  675 HOH HOH B . 
T 7 HOH 214 814  259 HOH HOH B . 
T 7 HOH 215 815  133 HOH HOH B . 
T 7 HOH 216 816  32  HOH HOH B . 
T 7 HOH 217 817  314 HOH HOH B . 
T 7 HOH 218 818  459 HOH HOH B . 
T 7 HOH 219 819  153 HOH HOH B . 
T 7 HOH 220 820  29  HOH HOH B . 
T 7 HOH 221 821  223 HOH HOH B . 
T 7 HOH 222 822  634 HOH HOH B . 
T 7 HOH 223 823  646 HOH HOH B . 
T 7 HOH 224 824  167 HOH HOH B . 
T 7 HOH 225 825  347 HOH HOH B . 
T 7 HOH 226 826  420 HOH HOH B . 
T 7 HOH 227 827  303 HOH HOH B . 
T 7 HOH 228 828  382 HOH HOH B . 
T 7 HOH 229 829  278 HOH HOH B . 
T 7 HOH 230 830  57  HOH HOH B . 
T 7 HOH 231 831  482 HOH HOH B . 
T 7 HOH 232 832  626 HOH HOH B . 
T 7 HOH 233 833  631 HOH HOH B . 
T 7 HOH 234 834  417 HOH HOH B . 
T 7 HOH 235 835  422 HOH HOH B . 
T 7 HOH 236 836  442 HOH HOH B . 
T 7 HOH 237 837  361 HOH HOH B . 
T 7 HOH 238 838  458 HOH HOH B . 
T 7 HOH 239 839  212 HOH HOH B . 
T 7 HOH 240 840  11  HOH HOH B . 
T 7 HOH 241 841  578 HOH HOH B . 
T 7 HOH 242 842  35  HOH HOH B . 
T 7 HOH 243 843  193 HOH HOH B . 
T 7 HOH 244 844  358 HOH HOH B . 
T 7 HOH 245 845  226 HOH HOH B . 
T 7 HOH 246 846  773 HOH HOH B . 
T 7 HOH 247 847  138 HOH HOH B . 
T 7 HOH 248 848  771 HOH HOH B . 
T 7 HOH 249 849  101 HOH HOH B . 
T 7 HOH 250 850  468 HOH HOH B . 
T 7 HOH 251 851  186 HOH HOH B . 
T 7 HOH 252 852  394 HOH HOH B . 
T 7 HOH 253 853  364 HOH HOH B . 
T 7 HOH 254 854  724 HOH HOH B . 
T 7 HOH 255 855  158 HOH HOH B . 
T 7 HOH 256 856  776 HOH HOH B . 
T 7 HOH 257 857  747 HOH HOH B . 
T 7 HOH 258 858  454 HOH HOH B . 
T 7 HOH 259 859  251 HOH HOH B . 
T 7 HOH 260 860  222 HOH HOH B . 
T 7 HOH 261 861  534 HOH HOH B . 
T 7 HOH 262 862  106 HOH HOH B . 
T 7 HOH 263 863  180 HOH HOH B . 
T 7 HOH 264 864  518 HOH HOH B . 
T 7 HOH 265 865  334 HOH HOH B . 
T 7 HOH 266 866  320 HOH HOH B . 
T 7 HOH 267 867  84  HOH HOH B . 
T 7 HOH 268 868  352 HOH HOH B . 
T 7 HOH 269 869  727 HOH HOH B . 
T 7 HOH 270 870  469 HOH HOH B . 
T 7 HOH 271 871  116 HOH HOH B . 
T 7 HOH 272 872  232 HOH HOH B . 
T 7 HOH 273 873  633 HOH HOH B . 
T 7 HOH 274 874  418 HOH HOH B . 
T 7 HOH 275 875  385 HOH HOH B . 
T 7 HOH 276 876  146 HOH HOH B . 
T 7 HOH 277 877  283 HOH HOH B . 
T 7 HOH 278 878  147 HOH HOH B . 
T 7 HOH 279 879  218 HOH HOH B . 
T 7 HOH 280 880  687 HOH HOH B . 
T 7 HOH 281 881  229 HOH HOH B . 
T 7 HOH 282 882  528 HOH HOH B . 
T 7 HOH 283 883  139 HOH HOH B . 
T 7 HOH 284 884  778 HOH HOH B . 
T 7 HOH 285 885  168 HOH HOH B . 
T 7 HOH 286 886  707 HOH HOH B . 
T 7 HOH 287 887  381 HOH HOH B . 
T 7 HOH 288 888  140 HOH HOH B . 
T 7 HOH 289 889  114 HOH HOH B . 
T 7 HOH 290 890  497 HOH HOH B . 
T 7 HOH 291 891  266 HOH HOH B . 
T 7 HOH 292 892  291 HOH HOH B . 
T 7 HOH 293 893  756 HOH HOH B . 
T 7 HOH 294 894  558 HOH HOH B . 
T 7 HOH 295 895  596 HOH HOH B . 
T 7 HOH 296 896  356 HOH HOH B . 
T 7 HOH 297 897  461 HOH HOH B . 
T 7 HOH 298 898  346 HOH HOH B . 
T 7 HOH 299 899  444 HOH HOH B . 
T 7 HOH 300 900  376 HOH HOH B . 
T 7 HOH 301 901  642 HOH HOH B . 
T 7 HOH 302 902  477 HOH HOH B . 
T 7 HOH 303 903  233 HOH HOH B . 
T 7 HOH 304 904  617 HOH HOH B . 
T 7 HOH 305 905  770 HOH HOH B . 
T 7 HOH 306 906  550 HOH HOH B . 
T 7 HOH 307 907  699 HOH HOH B . 
T 7 HOH 308 908  61  HOH HOH B . 
T 7 HOH 309 909  628 HOH HOH B . 
T 7 HOH 310 910  743 HOH HOH B . 
T 7 HOH 311 911  189 HOH HOH B . 
T 7 HOH 312 912  85  HOH HOH B . 
T 7 HOH 313 913  311 HOH HOH B . 
T 7 HOH 314 914  437 HOH HOH B . 
T 7 HOH 315 915  605 HOH HOH B . 
T 7 HOH 316 916  562 HOH HOH B . 
T 7 HOH 317 917  720 HOH HOH B . 
T 7 HOH 318 918  144 HOH HOH B . 
T 7 HOH 319 919  526 HOH HOH B . 
T 7 HOH 320 920  294 HOH HOH B . 
T 7 HOH 321 921  671 HOH HOH B . 
T 7 HOH 322 922  495 HOH HOH B . 
T 7 HOH 323 923  549 HOH HOH B . 
T 7 HOH 324 924  397 HOH HOH B . 
T 7 HOH 325 925  717 HOH HOH B . 
T 7 HOH 326 926  452 HOH HOH B . 
T 7 HOH 327 927  734 HOH HOH B . 
T 7 HOH 328 928  325 HOH HOH B . 
T 7 HOH 329 929  733 HOH HOH B . 
T 7 HOH 330 930  423 HOH HOH B . 
T 7 HOH 331 931  752 HOH HOH B . 
T 7 HOH 332 932  336 HOH HOH B . 
T 7 HOH 333 933  574 HOH HOH B . 
T 7 HOH 334 934  479 HOH HOH B . 
T 7 HOH 335 935  166 HOH HOH B . 
T 7 HOH 336 936  545 HOH HOH B . 
T 7 HOH 337 937  460 HOH HOH B . 
T 7 HOH 338 938  594 HOH HOH B . 
T 7 HOH 339 939  663 HOH HOH B . 
T 7 HOH 340 940  386 HOH HOH B . 
T 7 HOH 341 941  695 HOH HOH B . 
T 7 HOH 342 942  467 HOH HOH B . 
T 7 HOH 343 943  748 HOH HOH B . 
T 7 HOH 344 944  721 HOH HOH B . 
T 7 HOH 345 945  546 HOH HOH B . 
T 7 HOH 346 946  649 HOH HOH B . 
T 7 HOH 347 947  602 HOH HOH B . 
T 7 HOH 348 948  544 HOH HOH B . 
T 7 HOH 349 949  686 HOH HOH B . 
T 7 HOH 350 950  723 HOH HOH B . 
T 7 HOH 351 951  681 HOH HOH B . 
T 7 HOH 352 952  738 HOH HOH B . 
T 7 HOH 353 953  775 HOH HOH B . 
T 7 HOH 354 954  438 HOH HOH B . 
T 7 HOH 355 955  34  HOH HOH B . 
T 7 HOH 356 956  643 HOH HOH B . 
T 7 HOH 357 957  572 HOH HOH B . 
T 7 HOH 358 958  414 HOH HOH B . 
T 7 HOH 359 959  380 HOH HOH B . 
T 7 HOH 360 960  274 HOH HOH B . 
T 7 HOH 361 961  486 HOH HOH B . 
T 7 HOH 362 962  407 HOH HOH B . 
T 7 HOH 363 963  205 HOH HOH B . 
T 7 HOH 364 964  426 HOH HOH B . 
T 7 HOH 365 965  430 HOH HOH B . 
T 7 HOH 366 966  768 HOH HOH B . 
T 7 HOH 367 967  360 HOH HOH B . 
T 7 HOH 368 968  683 HOH HOH B . 
T 7 HOH 369 969  641 HOH HOH B . 
T 7 HOH 370 970  606 HOH HOH B . 
T 7 HOH 371 971  701 HOH HOH B . 
T 7 HOH 372 972  246 HOH HOH B . 
T 7 HOH 373 973  379 HOH HOH B . 
T 7 HOH 374 974  654 HOH HOH B . 
T 7 HOH 375 975  541 HOH HOH B . 
T 7 HOH 376 976  131 HOH HOH B . 
T 7 HOH 377 977  191 HOH HOH B . 
T 7 HOH 378 978  623 HOH HOH B . 
T 7 HOH 379 979  287 HOH HOH B . 
T 7 HOH 380 980  527 HOH HOH B . 
T 7 HOH 381 981  235 HOH HOH B . 
T 7 HOH 382 982  531 HOH HOH B . 
T 7 HOH 383 983  703 HOH HOH B . 
T 7 HOH 384 984  484 HOH HOH B . 
T 7 HOH 385 985  343 HOH HOH B . 
T 7 HOH 386 986  530 HOH HOH B . 
T 7 HOH 387 987  579 HOH HOH B . 
T 7 HOH 388 988  655 HOH HOH B . 
T 7 HOH 389 989  678 HOH HOH B . 
T 7 HOH 390 990  665 HOH HOH B . 
T 7 HOH 391 991  136 HOH HOH B . 
T 7 HOH 392 992  492 HOH HOH B . 
T 7 HOH 393 993  555 HOH HOH B . 
T 7 HOH 394 994  614 HOH HOH B . 
T 7 HOH 395 995  569 HOH HOH B . 
T 7 HOH 396 996  359 HOH HOH B . 
T 7 HOH 397 997  691 HOH HOH B . 
T 7 HOH 398 998  612 HOH HOH B . 
T 7 HOH 399 999  242 HOH HOH B . 
T 7 HOH 400 1000 610 HOH HOH B . 
T 7 HOH 401 1001 585 HOH HOH B . 
T 7 HOH 402 1002 566 HOH HOH B . 
T 7 HOH 403 1003 570 HOH HOH B . 
T 7 HOH 404 1004 653 HOH HOH B . 
T 7 HOH 405 1005 453 HOH HOH B . 
T 7 HOH 406 1006 553 HOH HOH B . 
T 7 HOH 407 1007 674 HOH HOH B . 
T 7 HOH 408 1008 685 HOH HOH B . 
T 7 HOH 409 1009 664 HOH HOH B . 
T 7 HOH 410 1010 436 HOH HOH B . 
T 7 HOH 411 1011 192 HOH HOH B . 
T 7 HOH 412 1012 556 HOH HOH B . 
T 7 HOH 413 1013 427 HOH HOH B . 
T 7 HOH 414 1014 99  HOH HOH B . 
T 7 HOH 415 1015 408 HOH HOH B . 
T 7 HOH 416 1016 730 HOH HOH B . 
T 7 HOH 417 1017 503 HOH HOH B . 
T 7 HOH 418 1018 741 HOH HOH B . 
T 7 HOH 419 1019 627 HOH HOH B . 
T 7 HOH 420 1020 651 HOH HOH B . 
T 7 HOH 421 1021 635 HOH HOH B . 
T 7 HOH 422 1022 656 HOH HOH B . 
T 7 HOH 423 1023 737 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                     8YB2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.830 
_cell.length_a_esd                 ? 
_cell.length_b                     128.510 
_cell.length_b_esd                 ? 
_cell.length_c                     149.420 
_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                         8YB2 
_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                   8YB2 
_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          54.56 
_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                                       8YB2 
_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                                     180786 
_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                           99.96 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                293.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.82 
_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                                   0.991 
_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                                    1.5 
_reflns_shell.d_res_low                                     1.51 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.24 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4418 
_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                                  0.438 
_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                                 8YB2 
_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                     180525 
_refine.ls_number_reflns_R_free                  8989 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1809 
_refine.ls_R_factor_R_free                       0.2085 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1795 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.40 
_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                            0.33 
_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             779 
_refine_hist.number_atoms_total               8325 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        7340 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         206 
_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 ? 7757  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.977 ? 10500 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.983 ? 1066  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055 ? 1110  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 1373  ? 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 . . 276 5672 100.00 . . . . 0.4336 . . . . . . . . . . . 0.4637 
'X-RAY DIFFRACTION' 1.52 1.53 . . 301 5635 100.00 . . . . 0.4200 . . . . . . . . . . . 0.4164 
'X-RAY DIFFRACTION' 1.53 1.55 . . 293 5672 100.00 . . . . 0.4187 . . . . . . . . . . . 0.4254 
'X-RAY DIFFRACTION' 1.55 1.57 . . 277 5667 100.00 . . . . 0.4113 . . . . . . . . . . . 0.4331 
'X-RAY DIFFRACTION' 1.57 1.59 . . 292 5699 100.00 . . . . 0.4063 . . . . . . . . . . . 0.4181 
'X-RAY DIFFRACTION' 1.59 1.62 . . 301 5603 100.00 . . . . 0.3946 . . . . . . . . . . . 0.4011 
'X-RAY DIFFRACTION' 1.62 1.64 . . 283 5693 100.00 . . . . 0.3842 . . . . . . . . . . . 0.3861 
'X-RAY DIFFRACTION' 1.64 1.66 . . 297 5640 100.00 . . . . 0.3747 . . . . . . . . . . . 0.3963 
'X-RAY DIFFRACTION' 1.66 1.69 . . 322 5666 100.00 . . . . 0.3617 . . . . . . . . . . . 0.3834 
'X-RAY DIFFRACTION' 1.69 1.72 . . 293 5653 100.00 . . . . 0.3411 . . . . . . . . . . . 0.3680 
'X-RAY DIFFRACTION' 1.72 1.75 . . 325 5672 100.00 . . . . 0.3213 . . . . . . . . . . . 0.3303 
'X-RAY DIFFRACTION' 1.75 1.78 . . 298 5686 100.00 . . . . 0.3015 . . . . . . . . . . . 0.2974 
'X-RAY DIFFRACTION' 1.78 1.81 . . 296 5651 100.00 . . . . 0.2816 . . . . . . . . . . . 0.3071 
'X-RAY DIFFRACTION' 1.81 1.85 . . 312 5691 100.00 . . . . 0.2575 . . . . . . . . . . . 0.3053 
'X-RAY DIFFRACTION' 1.85 1.89 . . 306 5707 100.00 . . . . 0.2268 . . . . . . . . . . . 0.2624 
'X-RAY DIFFRACTION' 1.89 1.93 . . 319 5640 100.00 . . . . 0.2165 . . . . . . . . . . . 0.2601 
'X-RAY DIFFRACTION' 1.93 1.98 . . 278 5731 100.00 . . . . 0.1935 . . . . . . . . . . . 0.2291 
'X-RAY DIFFRACTION' 1.98 2.03 . . 303 5718 100.00 . . . . 0.1744 . . . . . . . . . . . 0.2114 
'X-RAY DIFFRACTION' 2.03 2.09 . . 298 5680 100.00 . . . . 0.1702 . . . . . . . . . . . 0.1907 
'X-RAY DIFFRACTION' 2.09 2.16 . . 322 5697 100.00 . . . . 0.1642 . . . . . . . . . . . 0.1960 
'X-RAY DIFFRACTION' 2.16 2.23 . . 323 5701 100.00 . . . . 0.1694 . . . . . . . . . . . 0.2053 
'X-RAY DIFFRACTION' 2.23 2.32 . . 271 5771 100.00 . . . . 0.1698 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 2.32 2.43 . . 282 5748 100.00 . . . . 0.1679 . . . . . . . . . . . 0.1977 
'X-RAY DIFFRACTION' 2.43 2.55 . . 310 5744 100.00 . . . . 0.1654 . . . . . . . . . . . 0.1916 
'X-RAY DIFFRACTION' 2.55 2.71 . . 280 5770 100.00 . . . . 0.1725 . . . . . . . . . . . 0.1982 
'X-RAY DIFFRACTION' 2.71 2.91 . . 323 5756 100.00 . . . . 0.1724 . . . . . . . . . . . 0.1963 
'X-RAY DIFFRACTION' 2.91 3.20 . . 290 5795 100.00 . . . . 0.1710 . . . . . . . . . . . 0.2072 
'X-RAY DIFFRACTION' 3.20 3.64 . . 300 5847 100.00 . . . . 0.1579 . . . . . . . . . . . 0.1966 
'X-RAY DIFFRACTION' 3.64 4.52 . . 283 5906 100.00 . . . . 0.1456 . . . . . . . . . . . 0.1811 
'X-RAY DIFFRACTION' 4.52 9.99 . . 335 6025 100.00 . . . . 0.1588 . . . . . . . . . . . 0.1715 
# 
_struct.entry_id                     8YB2 
_struct.title                        
'XFEL crystal structure of the oxygen-bound form of F393H P450BM3 with N-enanthyl-L-prolyl-L-phenylalanine in complex with styrene' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8YB2 
_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 6 ? 
I N N 6 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
N N N 6 ? 
O N N 6 ? 
P N N 6 ? 
Q N N 6 ? 
R N N 6 ? 
S N N 7 ? 
T 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 8YB2 A 1 ? 455 ? P14779 2 ? 456 ? 1 455 
2 1 8YB2 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 8YB2 HIS A 393 ? UNP P14779 PHE 394 'engineered mutation' 393 1 
2 8YB2 HIS B 393 ? UNP P14779 PHE 394 'engineered mutation' 393 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly ? monomeric 1 
2 author_defined_assembly              ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,S     
2 1 B,J,K,L,M,N,O,P,Q,R,T 
# 
_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 ? ALA A 225 ? TYR A 198 ALA A 225 1 ? 28 
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 ? ? ? ? ? ? ? 2.385 ? ? 
metalc2 metalc ? ? C HEM .   FE ? ? ? 1_555 F OXY . O1 ? ? A HEM 501 A OXY 504 1_555 ? ? ? ? ? ? ? 1.975 ? ? 
metalc3 metalc ? ? B CYS 400 SG ? ? ? 1_555 J HEM . FE ? ? B CYS 400 B HEM 501 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
metalc4 metalc ? ? J HEM .   FE ? ? ? 1_555 M OXY . O1 ? ? B HEM 501 B OXY 504 1_555 ? ? ? ? ? ? ? 1.969 ? ? 
# 
_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 99.7  ? 
2  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 88.6  ? 
3  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 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 83.8  ? 
5  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 175.2 ? 
6  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 87.7  ? 
7  SG ? A CYS 400 ? A CYS 400 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 95.0  ? 
8  NA ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 91.5  ? 
9  NB ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 176.3 ? 
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_555 163.7 ? 
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 90.6  ? 
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 79.0  ? 
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 85.2  ? 
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 97.3  ? 
16 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 NA ? J HEM . ? B HEM 501 ? 1_555 98.3  ? 
17 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 NB ? J HEM . ? B HEM 501 ? 1_555 88.1  ? 
18 NA ? J HEM .   ? B HEM 501 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 NB ? J HEM . ? B HEM 501 ? 1_555 89.6  ? 
19 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 NC ? J HEM . ? B HEM 501 ? 1_555 84.0  ? 
20 NA ? J HEM .   ? B HEM 501 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 NC ? J HEM . ? B HEM 501 ? 1_555 176.6 ? 
21 NB ? J HEM .   ? B HEM 501 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 NC ? J HEM . ? B HEM 501 ? 1_555 87.8  ? 
22 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 ND ? J HEM . ? B HEM 501 ? 1_555 94.6  ? 
23 NA ? J HEM .   ? B HEM 501 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 ND ? J HEM . ? B HEM 501 ? 1_555 91.7  ? 
24 NB ? J HEM .   ? B HEM 501 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 ND ? J HEM . ? B HEM 501 ? 1_555 176.7 ? 
25 NC ? J HEM .   ? B HEM 501 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 ND ? J HEM . ? B HEM 501 ? 1_555 90.7  ? 
26 SG ? B CYS 400 ? B CYS 400 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 O1 ? M OXY . ? B OXY 504 ? 1_555 165.6 ? 
27 NA ? J HEM .   ? B HEM 501 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 O1 ? M OXY . ? B OXY 504 ? 1_555 91.0  ? 
28 NB ? J HEM .   ? B HEM 501 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 O1 ? M OXY . ? B OXY 504 ? 1_555 80.9  ? 
29 NC ? J HEM .   ? B HEM 501 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 O1 ? M OXY . ? B OXY 504 ? 1_555 86.3  ? 
30 ND ? J HEM .   ? B HEM 501 ? 1_555 FE ? J HEM . ? B HEM 501 ? 1_555 O1 ? M OXY . ? B OXY 504 ? 1_555 96.0  ? 
# 
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                   8YB2 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B HOH 917 ? ? O B HOH 943 ? ? 2.12 
2 1 OE1 A GLU 337 ? ? O A HOH 601 ? ? 2.15 
# 
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  ? ? 55.16   -127.08 
2  1 ASP A 84  ? ? -98.02  36.61   
3  1 ASP A 136 ? ? 66.89   -1.65   
4  1 ASP A 232 ? ? -128.69 -165.30 
5  1 HIS A 266 ? ? -138.61 -33.95  
6  1 ASP A 370 ? ? -74.11  33.29   
7  1 LEU A 437 ? ? 71.31   -62.57  
8  1 LYS B 15  ? ? 55.97   -125.73 
9  1 ASP B 84  ? ? -98.13  39.26   
10 1 ASP B 231 ? ? -145.72 52.61   
11 1 ASP B 232 ? ? -112.23 -164.73 
12 1 HIS B 266 ? ? -136.92 -36.63  
13 1 ASP B 370 ? ? -89.38  37.09   
14 1 LEU B 437 ? ? 70.15   -57.02  
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1023 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.90 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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          67757 
_pdbx_serial_crystallography_data_reduction.droplet_hits          ? 
_pdbx_serial_crystallography_data_reduction.frames_failed_index   ? 
_pdbx_serial_crystallography_data_reduction.frames_indexed        50478 
_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 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   Fixed-target 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_pdbx_serial_crystallography_sample_delivery_fixed_target.diffrn_id                       1 
_pdbx_serial_crystallography_sample_delivery_fixed_target.description                     
'microcrystals were mounted on mesh loop and flash-frozen by liquid nitrogen' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_holding                  'polyimide film' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.support_base                    'SPINE magnet base' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_unit_size                36 
_pdbx_serial_crystallography_sample_delivery_fixed_target.crystals_per_unit               50 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_solvent                  
'125 mM Tris-HCl (pH 8.3), 14% w/v PEG 8000, 60 mM MgCl2, saturated styrene, and 30% glycerol' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_dehydration_prevention   none 
_pdbx_serial_crystallography_sample_delivery_fixed_target.motion_control                  'stepper motors' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_horizontal             ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_vertical               ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.details                         ? 
# 
_atom_sites.entry_id                    8YB2 
_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]   0.007781 
_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   ? -11.318 -23.758 -24.761 1.00 75.78  ? 1    THR A N   1 
ATOM   2    C  CA  . THR A 1 1   ? -10.083 -23.868 -23.991 1.00 74.32  ? 1    THR A CA  1 
ATOM   3    C  C   . THR A 1 1   ? -10.328 -24.516 -22.627 1.00 68.90  ? 1    THR A C   1 
ATOM   4    O  O   . THR A 1 1   ? -9.807  -24.059 -21.609 1.00 69.67  ? 1    THR A O   1 
ATOM   5    C  CB  . THR A 1 1   ? -9.425  -22.489 -23.783 1.00 77.29  ? 1    THR A CB  1 
ATOM   6    O  OG1 . THR A 1 1   ? -8.533  -22.543 -22.660 1.00 78.99  ? 1    THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 1   ? -10.486 -21.421 -23.539 1.00 75.02  ? 1    THR A CG2 1 
ATOM   8    N  N   . ILE A 1 2   ? -11.122 -25.585 -22.617 1.00 71.79  ? 2    ILE A N   1 
ATOM   9    C  CA  . ILE A 1 2   ? -11.418 -26.308 -21.384 1.00 67.77  ? 2    ILE A CA  1 
ATOM   10   C  C   . ILE A 1 2   ? -10.174 -27.066 -20.930 1.00 68.09  ? 2    ILE A C   1 
ATOM   11   O  O   . ILE A 1 2   ? -9.676  -27.952 -21.635 1.00 68.07  ? 2    ILE A O   1 
ATOM   12   C  CB  . ILE A 1 2   ? -12.609 -27.255 -21.583 1.00 65.52  ? 2    ILE A CB  1 
ATOM   13   C  CG1 . ILE A 1 2   ? -13.791 -26.490 -22.194 1.00 69.46  ? 2    ILE A CG1 1 
ATOM   14   C  CG2 . ILE A 1 2   ? -12.986 -27.933 -20.271 1.00 63.40  ? 2    ILE A CG2 1 
ATOM   15   C  CD1 . ILE A 1 2   ? -14.721 -27.348 -23.031 1.00 73.36  ? 2    ILE A CD1 1 
ATOM   16   N  N   . LYS A 1 3   ? -9.668  -26.714 -19.747 1.00 63.94  ? 3    LYS A N   1 
ATOM   17   C  CA  . LYS A 1 3   ? -8.524  -27.376 -19.134 1.00 61.90  ? 3    LYS A CA  1 
ATOM   18   C  C   . LYS A 1 3   ? -8.978  -28.502 -18.206 1.00 63.58  ? 3    LYS A C   1 
ATOM   19   O  O   . LYS A 1 3   ? -10.103 -28.511 -17.695 1.00 62.49  ? 3    LYS A O   1 
ATOM   20   C  CB  . LYS A 1 3   ? -7.677  -26.380 -18.336 1.00 56.02  ? 3    LYS A CB  1 
ATOM   21   C  CG  . LYS A 1 3   ? -6.658  -25.596 -19.131 1.00 61.73  ? 3    LYS A CG  1 
ATOM   22   C  CD  . LYS A 1 3   ? -5.579  -25.054 -18.200 1.00 56.70  ? 3    LYS A CD  1 
ATOM   23   C  CE  . LYS A 1 3   ? -4.503  -24.293 -18.957 1.00 66.19  ? 3    LYS A CE  1 
ATOM   24   N  NZ  . LYS A 1 3   ? -4.959  -22.958 -19.435 1.00 70.39  ? 3    LYS A NZ  1 
ATOM   25   N  N   . GLU A 1 4   ? -8.071  -29.452 -17.986 1.00 62.77  ? 4    GLU A N   1 
ATOM   26   C  CA  . GLU A 1 4   ? -8.240  -30.506 -16.994 1.00 60.83  ? 4    GLU A CA  1 
ATOM   27   C  C   . GLU A 1 4   ? -7.550  -30.066 -15.710 1.00 53.33  ? 4    GLU A C   1 
ATOM   28   O  O   . GLU A 1 4   ? -6.348  -29.788 -15.706 1.00 56.59  ? 4    GLU A O   1 
ATOM   29   C  CB  . GLU A 1 4   ? -7.662  -31.831 -17.493 1.00 67.67  ? 4    GLU A CB  1 
ATOM   30   C  CG  . GLU A 1 4   ? -8.285  -33.069 -16.863 1.00 70.59  ? 4    GLU A CG  1 
ATOM   31   C  CD  . GLU A 1 4   ? -9.786  -33.151 -17.081 1.00 76.44  ? 4    GLU A CD  1 
ATOM   32   O  OE1 . GLU A 1 4   ? -10.300 -32.447 -17.978 1.00 76.43  ? 4    GLU A OE1 1 
ATOM   33   O  OE2 . GLU A 1 4   ? -10.450 -33.925 -16.357 1.00 77.84  ? 4    GLU A OE2 1 
ATOM   34   N  N   . MET A 1 5   ? -8.301  -30.005 -14.636 1.00 56.65  ? 5    MET A N   1 
ATOM   35   C  CA  . MET A 1 5   ? -7.649  -29.450 -13.457 1.00 49.07  ? 5    MET A CA  1 
ATOM   36   C  C   . MET A 1 5   ? -6.918  -30.541 -12.670 1.00 39.76  ? 5    MET A C   1 
ATOM   37   O  O   . MET A 1 5   ? -7.383  -31.677 -12.609 1.00 43.12  ? 5    MET A O   1 
ATOM   38   C  CB  . MET A 1 5   ? -8.696  -28.728 -12.605 1.00 50.60  ? 5    MET A CB  1 
ATOM   39   C  CG  . MET A 1 5   ? -9.430  -29.571 -11.608 1.00 46.17  ? 5    MET A CG  1 
ATOM   40   S  SD  . MET A 1 5   ? -10.386 -28.530 -10.479 1.00 43.50  ? 5    MET A SD  1 
ATOM   41   C  CE  . MET A 1 5   ? -11.616 -27.861 -11.594 1.00 47.09  ? 5    MET A CE  1 
ATOM   42   N  N   . PRO A 1 6   ? -5.740  -30.239 -12.121 1.00 39.39  ? 6    PRO A N   1 
ATOM   43   C  CA  . PRO A 1 6   ? -4.989  -31.247 -11.366 1.00 40.31  ? 6    PRO A CA  1 
ATOM   44   C  C   . PRO A 1 6   ? -5.717  -31.649 -10.093 1.00 47.66  ? 6    PRO A C   1 
ATOM   45   O  O   . PRO A 1 6   ? -6.709  -31.044 -9.681  1.00 40.56  ? 6    PRO A O   1 
ATOM   46   C  CB  . PRO A 1 6   ? -3.666  -30.550 -11.043 1.00 45.20  ? 6    PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 6   ? -3.971  -29.101 -11.125 1.00 42.17  ? 6    PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 6   ? -5.009  -28.966 -12.205 1.00 41.74  ? 6    PRO A CD  1 
ATOM   49   N  N   . GLN A 1 7   ? -5.195  -32.701 -9.458  1.00 41.58  ? 7    GLN A N   1 
ATOM   50   C  CA  . GLN A 1 7   ? -5.812  -33.270 -8.271  1.00 40.00  ? 7    GLN A CA  1 
ATOM   51   C  C   . GLN A 1 7   ? -4.694  -33.933 -7.484  1.00 44.90  ? 7    GLN A C   1 
ATOM   52   O  O   . GLN A 1 7   ? -3.865  -34.642 -8.088  1.00 41.31  ? 7    GLN A O   1 
ATOM   53   C  CB  . GLN A 1 7   ? -6.885  -34.297 -8.605  1.00 39.04  ? 7    GLN A CB  1 
ATOM   54   C  CG  . GLN A 1 7   ? -7.547  -34.934 -7.383  1.00 39.03  ? 7    GLN A CG  1 
ATOM   55   C  CD  . GLN A 1 7   ? -8.609  -35.927 -7.782  1.00 44.60  ? 7    GLN A CD  1 
ATOM   56   O  OE1 . GLN A 1 7   ? -8.794  -36.195 -8.967  1.00 47.44  ? 7    GLN A OE1 1 
ATOM   57   N  NE2 . GLN A 1 7   ? -9.329  -36.470 -6.803  1.00 41.04  ? 7    GLN A NE2 1 
ATOM   58   N  N   . PRO A 1 8   ? -4.634  -33.731 -6.166  1.00 40.37  ? 8    PRO A N   1 
ATOM   59   C  CA  . PRO A 1 8   ? -3.594  -34.393 -5.373  1.00 36.15  ? 8    PRO A CA  1 
ATOM   60   C  C   . PRO A 1 8   ? -3.831  -35.890 -5.251  1.00 35.83  ? 8    PRO A C   1 
ATOM   61   O  O   . PRO A 1 8   ? -4.850  -36.424 -5.703  1.00 36.85  ? 8    PRO A O   1 
ATOM   62   C  CB  . PRO A 1 8   ? -3.691  -33.701 -4.005  1.00 38.57  ? 8    PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 8   ? -5.130  -33.272 -3.916  1.00 37.65  ? 8    PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 8   ? -5.484  -32.852 -5.339  1.00 40.50  ? 8    PRO A CD  1 
ATOM   65   N  N   . LYS A 1 9   ? -2.877  -36.562 -4.616  1.00 39.36  ? 9    LYS A N   1 
ATOM   66   C  CA  . LYS A 1 9   ? -2.871  -38.019 -4.548  1.00 39.18  ? 9    LYS A CA  1 
ATOM   67   C  C   . LYS A 1 9   ? -4.104  -38.560 -3.834  1.00 38.93  ? 9    LYS A C   1 
ATOM   68   O  O   . LYS A 1 9   ? -4.565  -37.998 -2.834  1.00 40.32  ? 9    LYS A O   1 
ATOM   69   C  CB  . LYS A 1 9   ? -1.600  -38.495 -3.836  1.00 37.08  ? 9    LYS A CB  1 
ATOM   70   C  CG  . LYS A 1 9   ? -1.436  -38.015 -2.391  1.00 39.66  ? 9    LYS A CG  1 
ATOM   71   C  CD  . LYS A 1 9   ? -0.019  -38.266 -1.917  1.00 40.37  ? 9    LYS A CD  1 
ATOM   72   C  CE  . LYS A 1 9   ? 0.171   -37.853 -0.478  1.00 43.19  ? 9    LYS A CE  1 
ATOM   73   N  NZ  . LYS A 1 9   ? 1.603   -37.775 -0.071  1.00 41.97  ? 9    LYS A NZ  1 
ATOM   74   N  N   . THR A 1 10  ? -4.604  -39.687 -4.335  1.00 39.67  ? 10   THR A N   1 
ATOM   75   C  CA  . THR A 1 10  ? -5.803  -40.353 -3.852  1.00 37.57  ? 10   THR A CA  1 
ATOM   76   C  C   . THR A 1 10  ? -5.457  -41.631 -3.098  1.00 39.65  ? 10   THR A C   1 
ATOM   77   O  O   . THR A 1 10  ? -4.342  -42.170 -3.196  1.00 36.65  ? 10   THR A O   1 
ATOM   78   C  CB  . THR A 1 10  ? -6.748  -40.675 -5.014  1.00 41.16  ? 10   THR A CB  1 
ATOM   79   O  OG1 . THR A 1 10  ? -6.069  -41.513 -5.966  1.00 41.10  ? 10   THR A OG1 1 
ATOM   80   C  CG2 . THR A 1 10  ? -7.217  -39.376 -5.705  1.00 39.16  ? 10   THR A CG2 1 
ATOM   81   N  N   . PHE A 1 11  ? -6.456  -42.112 -2.355  1.00 41.71  ? 11   PHE A N   1 
ATOM   82   C  CA  . PHE A 1 11  ? -6.325  -43.244 -1.446  1.00 41.11  ? 11   PHE A CA  1 
ATOM   83   C  C   . PHE A 1 11  ? -7.462  -44.230 -1.705  1.00 43.61  ? 11   PHE A C   1 
ATOM   84   O  O   . PHE A 1 11  ? -8.235  -44.567 -0.810  1.00 45.51  ? 11   PHE A O   1 
ATOM   85   C  CB  . PHE A 1 11  ? -6.344  -42.777 0.017   1.00 37.86  ? 11   PHE A CB  1 
ATOM   86   C  CG  . PHE A 1 11  ? -5.174  -41.924 0.404   1.00 39.57  ? 11   PHE A CG  1 
ATOM   87   C  CD1 . PHE A 1 11  ? -5.082  -40.598 -0.006  1.00 36.71  ? 11   PHE A CD1 1 
ATOM   88   C  CD2 . PHE A 1 11  ? -4.161  -42.443 1.187   1.00 37.99  ? 11   PHE A CD2 1 
ATOM   89   C  CE1 . PHE A 1 11  ? -4.000  -39.814 0.364   1.00 37.41  ? 11   PHE A CE1 1 
ATOM   90   C  CE2 . PHE A 1 11  ? -3.081  -41.657 1.566   1.00 38.40  ? 11   PHE A CE2 1 
ATOM   91   C  CZ  . PHE A 1 11  ? -3.000  -40.343 1.144   1.00 39.90  ? 11   PHE A CZ  1 
ATOM   92   N  N   . GLY A 1 12  ? -7.569  -44.698 -2.946  1.00 39.69  ? 12   GLY A N   1 
ATOM   93   C  CA  . GLY A 1 12  ? -8.625  -45.642 -3.278  1.00 41.85  ? 12   GLY A CA  1 
ATOM   94   C  C   . GLY A 1 12  ? -9.997  -45.037 -3.047  1.00 47.85  ? 12   GLY A C   1 
ATOM   95   O  O   . GLY A 1 12  ? -10.269 -43.893 -3.423  1.00 44.11  ? 12   GLY A O   1 
ATOM   96   N  N   . GLU A 1 13  ? -10.881 -45.808 -2.411  1.00 45.14  ? 13   GLU A N   1 
ATOM   97   C  CA  . GLU A 1 13  ? -12.246 -45.336 -2.199  1.00 50.18  ? 13   GLU A CA  1 
ATOM   98   C  C   . GLU A 1 13  ? -12.316 -44.134 -1.267  1.00 48.00  ? 13   GLU A C   1 
ATOM   99   O  O   . GLU A 1 13  ? -13.314 -43.402 -1.301  1.00 48.81  ? 13   GLU A O   1 
ATOM   100  C  CB  . GLU A 1 13  ? -13.120 -46.463 -1.647  1.00 52.38  ? 13   GLU A CB  1 
ATOM   101  C  CG  . GLU A 1 13  ? -12.903 -47.788 -2.349  1.00 61.50  ? 13   GLU A CG  1 
ATOM   102  C  CD  . GLU A 1 13  ? -14.200 -48.474 -2.719  1.00 74.49  ? 13   GLU A CD  1 
ATOM   103  O  OE1 . GLU A 1 13  ? -14.694 -48.257 -3.848  1.00 78.86  ? 13   GLU A OE1 1 
ATOM   104  O  OE2 . GLU A 1 13  ? -14.719 -49.239 -1.877  1.00 75.52  ? 13   GLU A OE2 1 
ATOM   105  N  N   . LEU A 1 14  ? -11.299 -43.913 -0.433  1.00 44.73  ? 14   LEU A N   1 
ATOM   106  C  CA  . LEU A 1 14  ? -11.304 -42.729 0.414   1.00 44.03  ? 14   LEU A CA  1 
ATOM   107  C  C   . LEU A 1 14  ? -10.971 -41.461 -0.357  1.00 46.24  ? 14   LEU A C   1 
ATOM   108  O  O   . LEU A 1 14  ? -11.057 -40.373 0.222   1.00 44.47  ? 14   LEU A O   1 
ATOM   109  C  CB  . LEU A 1 14  ? -10.322 -42.895 1.574   1.00 42.78  ? 14   LEU A CB  1 
ATOM   110  C  CG  . LEU A 1 14  ? -10.620 -44.095 2.472   1.00 48.47  ? 14   LEU A CG  1 
ATOM   111  C  CD1 . LEU A 1 14  ? -9.604  -44.195 3.590   1.00 47.55  ? 14   LEU A CD1 1 
ATOM   112  C  CD2 . LEU A 1 14  ? -12.041 -44.001 3.021   1.00 52.05  ? 14   LEU A CD2 1 
ATOM   113  N  N   . LYS A 1 15  ? -10.576 -41.580 -1.626  1.00 42.28  ? 15   LYS A N   1 
ATOM   114  C  CA  . LYS A 1 15  ? -10.278 -40.444 -2.511  1.00 42.00  ? 15   LYS A CA  1 
ATOM   115  C  C   . LYS A 1 15  ? -9.225  -39.560 -1.837  1.00 44.62  ? 15   LYS A C   1 
ATOM   116  O  O   . LYS A 1 15  ? -8.164  -40.074 -1.458  1.00 41.06  ? 15   LYS A O   1 
ATOM   117  C  CB  . LYS A 1 15  ? -11.606 -39.790 -2.869  1.00 45.44  ? 15   LYS A CB  1 
ATOM   118  C  CG  . LYS A 1 15  ? -12.554 -40.830 -3.479  1.00 49.81  ? 15   LYS A CG  1 
ATOM   119  C  CD  . LYS A 1 15  ? -13.550 -40.266 -4.461  1.00 55.83  ? 15   LYS A CD  1 
ATOM   120  C  CE  . LYS A 1 15  ? -14.700 -41.255 -4.669  1.00 61.00  ? 15   LYS A CE  1 
ATOM   121  N  NZ  . LYS A 1 15  ? -15.784 -40.694 -5.521  1.00 67.50  ? 15   LYS A NZ  1 
ATOM   122  N  N   . ASN A 1 16  ? -9.443  -38.248 -1.683  1.00 40.00  ? 16   ASN A N   1 
ATOM   123  C  CA  . ASN A 1 16  ? -8.422  -37.389 -1.092  1.00 37.62  ? 16   ASN A CA  1 
ATOM   124  C  C   . ASN A 1 16  ? -8.564  -37.218 0.415   1.00 37.84  ? 16   ASN A C   1 
ATOM   125  O  O   . ASN A 1 16  ? -7.740  -36.533 1.021   1.00 39.28  ? 16   ASN A O   1 
ATOM   126  C  CB  . ASN A 1 16  ? -8.433  -35.990 -1.727  1.00 37.61  ? 16   ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 16  ? -8.052  -36.001 -3.189  1.00 39.05  ? 16   ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 16  ? -8.843  -35.608 -4.047  1.00 40.53  ? 16   ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 16  ? -6.836  -36.457 -3.485  1.00 39.57  ? 16   ASN A ND2 1 
ATOM   130  N  N   . LEU A 1 17  ? -9.586  -37.808 1.029   1.00 43.87  ? 17   LEU A N   1 
ATOM   131  C  CA  . LEU A 1 17  ? -9.857  -37.549 2.441   1.00 42.14  ? 17   LEU A CA  1 
ATOM   132  C  C   . LEU A 1 17  ? -8.641  -37.704 3.342   1.00 43.69  ? 17   LEU A C   1 
ATOM   133  O  O   . LEU A 1 17  ? -8.439  -36.842 4.216   1.00 40.35  ? 17   LEU A O   1 
ATOM   134  C  CB  . LEU A 1 17  ? -10.993 -38.470 2.904   1.00 44.90  ? 17   LEU A CB  1 
ATOM   135  C  CG  . LEU A 1 17  ? -11.923 -37.901 3.965   1.00 47.66  ? 17   LEU A CG  1 
ATOM   136  C  CD1 . LEU A 1 17  ? -12.388 -36.513 3.551   1.00 48.50  ? 17   LEU A CD1 1 
ATOM   137  C  CD2 . LEU A 1 17  ? -13.102 -38.844 4.123   1.00 47.88  ? 17   LEU A CD2 1 
ATOM   138  N  N   . PRO A 1 18  ? -7.798  -38.730 3.192   1.00 40.74  ? 18   PRO A N   1 
ATOM   139  C  CA  . PRO A 1 18  ? -6.680  -38.903 4.134   1.00 38.26  ? 18   PRO A CA  1 
ATOM   140  C  C   . PRO A 1 18  ? -5.676  -37.770 4.126   1.00 38.53  ? 18   PRO A C   1 
ATOM   141  O  O   . PRO A 1 18  ? -4.901  -37.643 5.084   1.00 39.53  ? 18   PRO A O   1 
ATOM   142  C  CB  . PRO A 1 18  ? -6.045  -40.227 3.680   1.00 39.87  ? 18   PRO A CB  1 
ATOM   143  C  CG  . PRO A 1 18  ? -7.185  -40.974 3.073   1.00 42.11  ? 18   PRO A CG  1 
ATOM   144  C  CD  . PRO A 1 18  ? -7.996  -39.918 2.347   1.00 41.44  ? 18   PRO A CD  1 
ATOM   145  N  N   . LEU A 1 19  ? -5.661  -36.933 3.088   1.00 37.12  ? 19   LEU A N   1 
ATOM   146  C  CA  . LEU A 1 19  ? -4.796  -35.757 3.108   1.00 37.87  ? 19   LEU A CA  1 
ATOM   147  C  C   . LEU A 1 19  ? -5.163  -34.798 4.240   1.00 37.36  ? 19   LEU A C   1 
ATOM   148  O  O   . LEU A 1 19  ? -4.327  -33.992 4.663   1.00 42.02  ? 19   LEU A O   1 
ATOM   149  C  CB  . LEU A 1 19  ? -4.879  -35.045 1.759   1.00 41.68  ? 19   LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 19  ? -4.372  -35.897 0.585   1.00 42.19  ? 19   LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 19  ? -4.583  -35.181 -0.746  1.00 41.12  ? 19   LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 19  ? -2.895  -36.254 0.806   1.00 40.08  ? 19   LEU A CD2 1 
ATOM   153  N  N   . LEU A 1 20  ? -6.387  -34.872 4.739   1.00 40.22  ? 20   LEU A N   1 
ATOM   154  C  CA  . LEU A 1 20  ? -6.799  -34.091 5.901   1.00 38.41  ? 20   LEU A CA  1 
ATOM   155  C  C   . LEU A 1 20  ? -6.443  -34.751 7.229   1.00 43.22  ? 20   LEU A C   1 
ATOM   156  O  O   . LEU A 1 20  ? -6.724  -34.174 8.289   1.00 40.90  ? 20   LEU A O   1 
ATOM   157  C  CB  . LEU A 1 20  ? -8.305  -33.846 5.848   1.00 37.60  ? 20   LEU A CB  1 
ATOM   158  C  CG  . LEU A 1 20  ? -8.691  -33.111 4.563   1.00 40.83  ? 20   LEU A CG  1 
ATOM   159  C  CD1 . LEU A 1 20  ? -10.188 -32.899 4.450   1.00 41.06  ? 20   LEU A CD1 1 
ATOM   160  C  CD2 . LEU A 1 20  ? -7.927  -31.792 4.511   1.00 37.04  ? 20   LEU A CD2 1 
ATOM   161  N  N   . ASN A 1 21  ? -5.851  -35.946 7.208   1.00 40.24  ? 21   ASN A N   1 
ATOM   162  C  CA  . ASN A 1 21  ? -5.482  -36.632 8.452   1.00 40.96  ? 21   ASN A CA  1 
ATOM   163  C  C   . ASN A 1 21  ? -4.146  -36.074 8.936   1.00 42.84  ? 21   ASN A C   1 
ATOM   164  O  O   . ASN A 1 21  ? -3.094  -36.713 8.858   1.00 46.70  ? 21   ASN A O   1 
ATOM   165  C  CB  . ASN A 1 21  ? -5.407  -38.141 8.256   1.00 44.55  ? 21   ASN A CB  1 
ATOM   166  C  CG  . ASN A 1 21  ? -5.158  -38.886 9.568   1.00 52.93  ? 21   ASN A CG  1 
ATOM   167  O  OD1 . ASN A 1 21  ? -4.971  -38.271 10.618  1.00 51.15  ? 21   ASN A OD1 1 
ATOM   168  N  ND2 . ASN A 1 21  ? -5.125  -40.209 9.503   1.00 53.77  ? 21   ASN A ND2 1 
ATOM   169  N  N   . THR A 1 22  ? -4.215  -34.848 9.446   1.00 37.84  ? 22   THR A N   1 
ATOM   170  C  CA  . THR A 1 22  ? -3.070  -34.104 9.945   1.00 38.15  ? 22   THR A CA  1 
ATOM   171  C  C   . THR A 1 22  ? -3.590  -33.063 10.925  1.00 41.92  ? 22   THR A C   1 
ATOM   172  O  O   . THR A 1 22  ? -4.757  -32.674 10.873  1.00 41.42  ? 22   THR A O   1 
ATOM   173  C  CB  . THR A 1 22  ? -2.289  -33.433 8.810   1.00 41.34  ? 22   THR A CB  1 
ATOM   174  O  OG1 . THR A 1 22  ? -1.310  -32.534 9.353   1.00 44.75  ? 22   THR A OG1 1 
ATOM   175  C  CG2 . THR A 1 22  ? -3.236  -32.673 7.881   1.00 39.09  ? 22   THR A CG2 1 
ATOM   176  N  N   . ASP A 1 23  ? -2.715  -32.627 11.833  1.00 43.16  ? 23   ASP A N   1 
ATOM   177  C  CA  . ASP A 1 23  ? -3.084  -31.567 12.758  1.00 43.42  ? 23   ASP A CA  1 
ATOM   178  C  C   . ASP A 1 23  ? -3.044  -30.203 12.098  1.00 40.01  ? 23   ASP A C   1 
ATOM   179  O  O   . ASP A 1 23  ? -3.505  -29.229 12.699  1.00 36.86  ? 23   ASP A O   1 
ATOM   180  C  CB  . ASP A 1 23  ? -2.151  -31.547 13.969  1.00 43.74  ? 23   ASP A CB  1 
ATOM   181  C  CG  . ASP A 1 23  ? -0.694  -31.557 13.566  1.00 50.52  ? 23   ASP A CG  1 
ATOM   182  O  OD1 . ASP A 1 23  ? -0.379  -32.112 12.489  1.00 55.62  ? 23   ASP A OD1 1 
ATOM   183  O  OD2 . ASP A 1 23  ? 0.143   -31.020 14.325  1.00 62.68  ? 23   ASP A OD2 1 
ATOM   184  N  N   . LYS A 1 24  ? -2.493  -30.109 10.888  1.00 38.59  ? 24   LYS A N   1 
ATOM   185  C  CA  . LYS A 1 24  ? -2.338  -28.837 10.183  1.00 37.49  ? 24   LYS A CA  1 
ATOM   186  C  C   . LYS A 1 24  ? -2.887  -28.963 8.768   1.00 35.02  ? 24   LYS A C   1 
ATOM   187  O  O   . LYS A 1 24  ? -2.143  -28.860 7.783   1.00 37.26  ? 24   LYS A O   1 
ATOM   188  C  CB  . LYS A 1 24  ? -0.872  -28.404 10.186  1.00 36.55  ? 24   LYS A CB  1 
ATOM   189  C  CG  . LYS A 1 24  ? -0.319  -28.146 11.588  1.00 40.04  ? 24   LYS A CG  1 
ATOM   190  C  CD  . LYS A 1 24  ? 1.144   -27.725 11.585  1.00 41.88  ? 24   LYS A CD  1 
ATOM   191  C  CE  . LYS A 1 24  ? 1.588   -27.415 13.013  1.00 41.63  ? 24   LYS A CE  1 
ATOM   192  N  NZ  . LYS A 1 24  ? 2.952   -26.835 13.085  1.00 41.20  ? 24   LYS A NZ  1 
ATOM   193  N  N   . PRO A 1 25  ? -4.206  -29.146 8.632   1.00 35.96  ? 25   PRO A N   1 
ATOM   194  C  CA  . PRO A 1 25  ? -4.774  -29.379 7.294   1.00 37.89  ? 25   PRO A CA  1 
ATOM   195  C  C   . PRO A 1 25  ? -4.718  -28.173 6.370   1.00 38.55  ? 25   PRO A C   1 
ATOM   196  O  O   . PRO A 1 25  ? -4.499  -28.346 5.163   1.00 36.94  ? 25   PRO A O   1 
ATOM   197  C  CB  . PRO A 1 25  ? -6.216  -29.801 7.597   1.00 35.74  ? 25   PRO A CB  1 
ATOM   198  C  CG  . PRO A 1 25  ? -6.505  -29.190 8.946   1.00 34.33  ? 25   PRO A CG  1 
ATOM   199  C  CD  . PRO A 1 25  ? -5.214  -29.275 9.701   1.00 36.39  ? 25   PRO A CD  1 
ATOM   200  N  N   . VAL A 1 26  ? -4.947  -26.959 6.878   1.00 34.28  ? 26   VAL A N   1 
ATOM   201  C  CA  . VAL A 1 26  ? -4.847  -25.795 6.003   1.00 36.19  ? 26   VAL A CA  1 
ATOM   202  C  C   . VAL A 1 26  ? -3.434  -25.661 5.461   1.00 37.82  ? 26   VAL A C   1 
ATOM   203  O  O   . VAL A 1 26  ? -3.229  -25.404 4.269   1.00 38.13  ? 26   VAL A O   1 
ATOM   204  C  CB  . VAL A 1 26  ? -5.278  -24.519 6.741   1.00 35.61  ? 26   VAL A CB  1 
ATOM   205  C  CG1 . VAL A 1 26  ? -4.946  -23.309 5.860   1.00 33.40  ? 26   VAL A CG1 1 
ATOM   206  C  CG2 . VAL A 1 26  ? -6.769  -24.584 7.038   1.00 37.89  ? 26   VAL A CG2 1 
ATOM   207  N  N   . GLN A 1 27  ? -2.436  -25.841 6.324   1.00 34.71  ? 27   GLN A N   1 
ATOM   208  C  CA  . GLN A 1 27  ? -1.061  -25.723 5.853   1.00 38.14  ? 27   GLN A CA  1 
ATOM   209  C  C   . GLN A 1 27  ? -0.706  -26.843 4.879   1.00 37.57  ? 27   GLN A C   1 
ATOM   210  O  O   . GLN A 1 27  ? 0.045   -26.614 3.926   1.00 37.97  ? 27   GLN A O   1 
ATOM   211  C  CB  . GLN A 1 27  ? -0.114  -25.682 7.057   1.00 32.98  ? 27   GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 27  ? -0.238  -24.361 7.848   1.00 34.48  ? 27   GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 27  ? 0.316   -24.460 9.242   1.00 35.81  ? 27   GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 27  ? 1.487   -24.162 9.478   1.00 35.79  ? 27   GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 27  ? -0.533  -24.859 10.193  1.00 34.69  ? 27   GLN A NE2 1 
ATOM   216  N  N   . ALA A 1 28  ? -1.257  -28.039 5.072   1.00 37.45  ? 28   ALA A N   1 
ATOM   217  C  CA  . ALA A 1 28  ? -1.051  -29.104 4.091   1.00 38.84  ? 28   ALA A CA  1 
ATOM   218  C  C   . ALA A 1 28  ? -1.677  -28.741 2.752   1.00 40.28  ? 28   ALA A C   1 
ATOM   219  O  O   . ALA A 1 28  ? -1.127  -29.062 1.683   1.00 39.56  ? 28   ALA A O   1 
ATOM   220  C  CB  . ALA A 1 28  ? -1.637  -30.415 4.611   1.00 41.30  ? 28   ALA A CB  1 
ATOM   221  N  N   . LEU A 1 29  ? -2.842  -28.085 2.790   1.00 35.28  ? 29   LEU A N   1 
ATOM   222  C  CA  . LEU A 1 29  ? -3.511  -27.690 1.558   1.00 38.00  ? 29   LEU A CA  1 
ATOM   223  C  C   . LEU A 1 29  ? -2.750  -26.583 0.844   1.00 34.72  ? 29   LEU A C   1 
ATOM   224  O  O   . LEU A 1 29  ? -2.730  -26.555 -0.392  1.00 38.91  ? 29   LEU A O   1 
ATOM   225  C  CB  . LEU A 1 29  ? -4.953  -27.255 1.851   1.00 38.92  ? 29   LEU A CB  1 
ATOM   226  C  CG  . LEU A 1 29  ? -5.932  -28.411 2.109   1.00 38.38  ? 29   LEU A CG  1 
ATOM   227  C  CD1 . LEU A 1 29  ? -7.136  -27.954 2.943   1.00 37.83  ? 29   LEU A CD1 1 
ATOM   228  C  CD2 . LEU A 1 29  ? -6.386  -29.024 0.810   1.00 37.62  ? 29   LEU A CD2 1 
ATOM   229  N  N   . MET A 1 30  ? -2.121  -25.674 1.596   1.00 36.99  ? 30   MET A N   1 
ATOM   230  C  CA  . MET A 1 30  ? -1.246  -24.674 0.987   1.00 35.32  ? 30   MET A CA  1 
ATOM   231  C  C   . MET A 1 30  ? -0.050  -25.316 0.285   1.00 39.11  ? 30   MET A C   1 
ATOM   232  O  O   . MET A 1 30  ? 0.371   -24.859 -0.784  1.00 39.62  ? 30   MET A O   1 
ATOM   233  C  CB  . MET A 1 30  ? -0.758  -23.664 2.025   1.00 36.74  ? 30   MET A CB  1 
ATOM   234  C  CG  . MET A 1 30  ? -1.867  -22.812 2.648   1.00 36.42  ? 30   MET A CG  1 
ATOM   235  S  SD  . MET A 1 30  ? -1.283  -21.898 4.069   1.00 37.68  ? 30   MET A SD  1 
ATOM   236  C  CE  . MET A 1 30  ? -0.099  -20.790 3.291   1.00 41.86  ? 30   MET A CE  1 
ATOM   237  N  N   . LYS A 1 31  ? 0.529   -26.355 0.881   1.00 37.14  ? 31   LYS A N   1 
ATOM   238  C  CA  . LYS A 1 31  ? 1.658   -27.026 0.231   1.00 37.56  ? 31   LYS A CA  1 
ATOM   239  C  C   . LYS A 1 31  ? 1.208   -27.719 -1.052  1.00 40.91  ? 31   LYS A C   1 
ATOM   240  O  O   . LYS A 1 31  ? 1.930   -27.723 -2.059  1.00 44.37  ? 31   LYS A O   1 
ATOM   241  C  CB  . LYS A 1 31  ? 2.295   -28.026 1.203   1.00 42.01  ? 31   LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 31  ? 3.623   -28.611 0.751   1.00 46.57  ? 31   LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 31  ? 4.491   -28.961 1.963   1.00 58.07  ? 31   LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 31  ? 5.014   -27.715 2.673   1.00 62.34  ? 31   LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 31  ? 5.049   -27.888 4.162   1.00 68.36  ? 31   LYS A NZ  1 
ATOM   246  N  N   . ILE A 1 32  ? 0.006   -28.294 -1.043  1.00 36.21  ? 32   ILE A N   1 
ATOM   247  C  CA  . ILE A 1 32  ? -0.554  -28.873 -2.259  1.00 38.74  ? 32   ILE A CA  1 
ATOM   248  C  C   . ILE A 1 32  ? -0.755  -27.797 -3.327  1.00 40.23  ? 32   ILE A C   1 
ATOM   249  O  O   . ILE A 1 32  ? -0.405  -27.986 -4.501  1.00 38.58  ? 32   ILE A O   1 
ATOM   250  C  CB  . ILE A 1 32  ? -1.866  -29.605 -1.940  1.00 38.72  ? 32   ILE A CB  1 
ATOM   251  C  CG1 . ILE A 1 32  ? -1.599  -30.809 -1.025  1.00 39.07  ? 32   ILE A CG1 1 
ATOM   252  C  CG2 . ILE A 1 32  ? -2.565  -30.036 -3.235  1.00 38.22  ? 32   ILE A CG2 1 
ATOM   253  C  CD1 . ILE A 1 32  ? -2.863  -31.484 -0.544  1.00 38.04  ? 32   ILE A CD1 1 
ATOM   254  N  N   . ALA A 1 33  ? -1.339  -26.657 -2.946  1.00 38.85  ? 33   ALA A N   1 
ATOM   255  C  CA  . ALA A 1 33  ? -1.472  -25.553 -3.904  1.00 38.57  ? 33   ALA A CA  1 
ATOM   256  C  C   . ALA A 1 33  ? -0.112  -25.129 -4.456  1.00 41.33  ? 33   ALA A C   1 
ATOM   257  O  O   . ALA A 1 33  ? 0.017   -24.814 -5.648  1.00 41.59  ? 33   ALA A O   1 
ATOM   258  C  CB  . ALA A 1 33  ? -2.175  -24.366 -3.233  1.00 36.94  ? 33   ALA A CB  1 
ATOM   259  N  N   . ASP A 1 34  ? 0.911   -25.102 -3.600  1.00 39.69  ? 34   ASP A N   1 
ATOM   260  C  CA  . ASP A 1 34  ? 2.263   -24.791 -4.052  1.00 40.38  ? 34   ASP A CA  1 
ATOM   261  C  C   . ASP A 1 34  ? 2.667   -25.727 -5.182  1.00 43.80  ? 34   ASP A C   1 
ATOM   262  O  O   . ASP A 1 34  ? 3.351   -25.330 -6.129  1.00 46.11  ? 34   ASP A O   1 
ATOM   263  C  CB  . ASP A 1 34  ? 3.232   -24.939 -2.880  1.00 44.87  ? 34   ASP A CB  1 
ATOM   264  C  CG  . ASP A 1 34  ? 3.426   -23.652 -2.103  1.00 49.71  ? 34   ASP A CG  1 
ATOM   265  O  OD1 . ASP A 1 34  ? 2.976   -22.584 -2.561  1.00 54.46  ? 34   ASP A OD1 1 
ATOM   266  O  OD2 . ASP A 1 34  ? 3.972   -23.728 -0.986  1.00 52.38  ? 34   ASP A OD2 1 
ATOM   267  N  N   . GLU A 1 35  ? 2.250   -26.978 -5.090  1.00 43.60  ? 35   GLU A N   1 
ATOM   268  C  CA  . GLU A 1 35  ? 2.642   -27.995 -6.050  1.00 43.92  ? 35   GLU A CA  1 
ATOM   269  C  C   . GLU A 1 35  ? 1.749   -28.001 -7.284  1.00 44.45  ? 35   GLU A C   1 
ATOM   270  O  O   . GLU A 1 35  ? 2.246   -28.168 -8.404  1.00 47.36  ? 35   GLU A O   1 
ATOM   271  C  CB  . GLU A 1 35  ? 2.629   -29.370 -5.366  1.00 47.73  ? 35   GLU A CB  1 
ATOM   272  C  CG  . GLU A 1 35  ? 2.939   -30.528 -6.303  1.00 54.87  ? 35   GLU A CG  1 
ATOM   273  C  CD  . GLU A 1 35  ? 2.953   -31.877 -5.599  1.00 61.02  ? 35   GLU A CD  1 
ATOM   274  O  OE1 . GLU A 1 35  ? 3.330   -31.931 -4.406  1.00 61.27  ? 35   GLU A OE1 1 
ATOM   275  O  OE2 . GLU A 1 35  ? 2.593   -32.885 -6.250  1.00 63.04  ? 35   GLU A OE2 1 
ATOM   276  N  N   . LEU A 1 36  ? 0.437   -27.806 -7.118  1.00 38.91  ? 36   LEU A N   1 
ATOM   277  C  CA  . LEU A 1 36  ? -0.500  -27.999 -8.215  1.00 39.36  ? 36   LEU A CA  1 
ATOM   278  C  C   . LEU A 1 36  ? -0.963  -26.707 -8.884  1.00 45.00  ? 36   LEU A C   1 
ATOM   279  O  O   . LEU A 1 36  ? -1.473  -26.768 -10.010 1.00 43.92  ? 36   LEU A O   1 
ATOM   280  C  CB  . LEU A 1 36  ? -1.727  -28.779 -7.725  1.00 40.53  ? 36   LEU A CB  1 
ATOM   281  C  CG  . LEU A 1 36  ? -1.409  -30.163 -7.141  1.00 41.14  ? 36   LEU A CG  1 
ATOM   282  C  CD1 . LEU A 1 36  ? -2.696  -30.948 -6.936  1.00 41.93  ? 36   LEU A CD1 1 
ATOM   283  C  CD2 . LEU A 1 36  ? -0.450  -30.917 -8.073  1.00 43.10  ? 36   LEU A CD2 1 
ATOM   284  N  N   . GLY A 1 37  ? -0.818  -25.562 -8.230  1.00 39.92  ? 37   GLY A N   1 
ATOM   285  C  CA  . GLY A 1 37  ? -1.180  -24.281 -8.821  1.00 37.99  ? 37   GLY A CA  1 
ATOM   286  C  C   . GLY A 1 37  ? -2.496  -23.710 -8.317  1.00 42.78  ? 37   GLY A C   1 
ATOM   287  O  O   . GLY A 1 37  ? -3.015  -24.055 -7.248  1.00 38.40  ? 37   GLY A O   1 
ATOM   288  N  N   . GLU A 1 38  ? -3.055  -22.817 -9.145  1.00 37.41  ? 38   GLU A N   1 
ATOM   289  C  CA  . GLU A 1 38  ? -4.150  -21.932 -8.738  1.00 37.36  ? 38   GLU A CA  1 
ATOM   290  C  C   . GLU A 1 38  ? -5.482  -22.650 -8.538  1.00 39.18  ? 38   GLU A C   1 
ATOM   291  O  O   . GLU A 1 38  ? -6.396  -22.070 -7.932  1.00 36.80  ? 38   GLU A O   1 
ATOM   292  C  CB  . GLU A 1 38  ? -4.324  -20.836 -9.795  1.00 37.68  ? 38   GLU A CB  1 
ATOM   293  C  CG  . GLU A 1 38  ? -4.761  -21.416 -11.139 1.00 37.85  ? 38   GLU A CG  1 
ATOM   294  C  CD  . GLU A 1 38  ? -4.969  -20.351 -12.208 1.00 43.81  ? 38   GLU A CD  1 
ATOM   295  O  OE1 . GLU A 1 38  ? -5.052  -19.156 -11.849 1.00 39.60  ? 38   GLU A OE1 1 
ATOM   296  O  OE2 . GLU A 1 38  ? -5.037  -20.713 -13.402 1.00 43.42  ? 38   GLU A OE2 1 
ATOM   297  N  N   . ILE A 1 39  ? -5.634  -23.875 -9.037  1.00 36.72  ? 39   ILE A N   1 
ATOM   298  C  CA  . ILE A 1 39  ? -6.886  -24.604 -8.856  1.00 35.48  ? 39   ILE A CA  1 
ATOM   299  C  C   . ILE A 1 39  ? -6.583  -26.096 -8.801  1.00 43.88  ? 39   ILE A C   1 
ATOM   300  O  O   . ILE A 1 39  ? -5.853  -26.620 -9.649  1.00 38.96  ? 39   ILE A O   1 
ATOM   301  C  CB  . ILE A 1 39  ? -7.903  -24.291 -9.975  1.00 36.45  ? 39   ILE A CB  1 
ATOM   302  C  CG1 . ILE A 1 39  ? -9.216  -25.040 -9.725  1.00 40.14  ? 39   ILE A CG1 1 
ATOM   303  C  CG2 . ILE A 1 39  ? -7.335  -24.633 -11.360 1.00 40.82  ? 39   ILE A CG2 1 
ATOM   304  C  CD1 . ILE A 1 39  ? -10.389 -24.531 -10.550 1.00 43.58  ? 39   ILE A CD1 1 
ATOM   305  N  N   . PHE A 1 40  ? -7.145  -26.794 -7.811  1.00 35.88  ? 40   PHE A N   1 
ATOM   306  C  CA  . PHE A 1 40  ? -7.080  -28.251 -7.842  1.00 35.63  ? 40   PHE A CA  1 
ATOM   307  C  C   . PHE A 1 40  ? -8.370  -28.869 -7.325  1.00 39.98  ? 40   PHE A C   1 
ATOM   308  O  O   . PHE A 1 40  ? -9.066  -28.298 -6.480  1.00 38.01  ? 40   PHE A O   1 
ATOM   309  C  CB  . PHE A 1 40  ? -5.849  -28.804 -7.077  1.00 35.10  ? 40   PHE A CB  1 
ATOM   310  C  CG  . PHE A 1 40  ? -5.786  -28.452 -5.595  1.00 36.18  ? 40   PHE A CG  1 
ATOM   311  C  CD1 . PHE A 1 40  ? -6.375  -29.267 -4.645  1.00 38.54  ? 40   PHE A CD1 1 
ATOM   312  C  CD2 . PHE A 1 40  ? -5.065  -27.351 -5.172  1.00 34.38  ? 40   PHE A CD2 1 
ATOM   313  C  CE1 . PHE A 1 40  ? -6.280  -28.965 -3.292  1.00 36.61  ? 40   PHE A CE1 1 
ATOM   314  C  CE2 . PHE A 1 40  ? -4.951  -27.038 -3.824  1.00 36.27  ? 40   PHE A CE2 1 
ATOM   315  C  CZ  . PHE A 1 40  ? -5.575  -27.849 -2.878  1.00 39.04  ? 40   PHE A CZ  1 
ATOM   316  N  N   . LYS A 1 41  ? -8.698  -30.029 -7.896  1.00 38.66  ? 41   LYS A N   1 
ATOM   317  C  CA  . LYS A 1 41  ? -9.849  -30.823 -7.484  1.00 37.24  ? 41   LYS A CA  1 
ATOM   318  C  C   . LYS A 1 41  ? -9.548  -31.570 -6.183  1.00 37.77  ? 41   LYS A C   1 
ATOM   319  O  O   . LYS A 1 41  ? -8.432  -32.049 -5.970  1.00 39.12  ? 41   LYS A O   1 
ATOM   320  C  CB  . LYS A 1 41  ? -10.182 -31.821 -8.592  1.00 42.78  ? 41   LYS A CB  1 
ATOM   321  C  CG  . LYS A 1 41  ? -11.300 -32.798 -8.311  1.00 44.20  ? 41   LYS A CG  1 
ATOM   322  C  CD  . LYS A 1 41  ? -11.979 -33.190 -9.621  1.00 51.49  ? 41   LYS A CD  1 
ATOM   323  C  CE  . LYS A 1 41  ? -13.257 -33.978 -9.389  1.00 54.43  ? 41   LYS A CE  1 
ATOM   324  N  NZ  . LYS A 1 41  ? -13.497 -34.988 -10.464 1.00 60.44  ? 41   LYS A NZ  1 
ATOM   325  N  N   . PHE A 1 42  ? -10.547 -31.671 -5.306  1.00 37.91  ? 42   PHE A N   1 
ATOM   326  C  CA  . PHE A 1 42  ? -10.391 -32.409 -4.054  1.00 39.57  ? 42   PHE A CA  1 
ATOM   327  C  C   . PHE A 1 42  ? -11.674 -33.188 -3.828  1.00 43.04  ? 42   PHE A C   1 
ATOM   328  O  O   . PHE A 1 42  ? -12.748 -32.588 -3.725  1.00 38.61  ? 42   PHE A O   1 
ATOM   329  C  CB  . PHE A 1 42  ? -10.107 -31.459 -2.884  1.00 41.86  ? 42   PHE A CB  1 
ATOM   330  C  CG  . PHE A 1 42  ? -9.656  -32.146 -1.608  1.00 39.76  ? 42   PHE A CG  1 
ATOM   331  C  CD1 . PHE A 1 42  ? -10.567 -32.808 -0.802  1.00 41.18  ? 42   PHE A CD1 1 
ATOM   332  C  CD2 . PHE A 1 42  ? -8.324  -32.081 -1.197  1.00 40.00  ? 42   PHE A CD2 1 
ATOM   333  C  CE1 . PHE A 1 42  ? -10.156 -33.419 0.391   1.00 40.96  ? 42   PHE A CE1 1 
ATOM   334  C  CE2 . PHE A 1 42  ? -7.908  -32.695 -0.011  1.00 41.48  ? 42   PHE A CE2 1 
ATOM   335  C  CZ  . PHE A 1 42  ? -8.836  -33.356 0.782   1.00 37.71  ? 42   PHE A CZ  1 
ATOM   336  N  N   . GLU A 1 43  ? -11.569 -34.517 -3.767  1.00 38.28  ? 43   GLU A N   1 
ATOM   337  C  CA  . GLU A 1 43  ? -12.720 -35.389 -3.604  1.00 42.06  ? 43   GLU A CA  1 
ATOM   338  C  C   . GLU A 1 43  ? -12.669 -36.107 -2.261  1.00 40.00  ? 43   GLU A C   1 
ATOM   339  O  O   . GLU A 1 43  ? -11.599 -36.447 -1.755  1.00 40.59  ? 43   GLU A O   1 
ATOM   340  C  CB  . GLU A 1 43  ? -12.801 -36.436 -4.718  1.00 42.73  ? 43   GLU A CB  1 
ATOM   341  C  CG  . GLU A 1 43  ? -13.057 -35.874 -6.095  1.00 48.28  ? 43   GLU A CG  1 
ATOM   342  C  CD  . GLU A 1 43  ? -13.002 -36.948 -7.149  1.00 54.27  ? 43   GLU A CD  1 
ATOM   343  O  OE1 . GLU A 1 43  ? -11.994 -37.683 -7.182  1.00 53.07  ? 43   GLU A OE1 1 
ATOM   344  O  OE2 . GLU A 1 43  ? -13.972 -37.070 -7.925  1.00 59.64  ? 43   GLU A OE2 1 
ATOM   345  N  N   . ALA A 1 44  ? -13.846 -36.317 -1.689  1.00 43.98  ? 44   ALA A N   1 
ATOM   346  C  CA  . ALA A 1 44  ? -14.084 -37.241 -0.591  1.00 43.75  ? 44   ALA A CA  1 
ATOM   347  C  C   . ALA A 1 44  ? -15.232 -38.133 -1.011  1.00 42.88  ? 44   ALA A C   1 
ATOM   348  O  O   . ALA A 1 44  ? -15.929 -37.844 -1.987  1.00 43.40  ? 44   ALA A O   1 
ATOM   349  C  CB  . ALA A 1 44  ? -14.435 -36.503 0.711   1.00 45.07  ? 44   ALA A CB  1 
ATOM   350  N  N   . PRO A 1 45  ? -15.464 -39.229 -0.305  1.00 45.56  ? 45   PRO A N   1 
ATOM   351  C  CA  . PRO A 1 45  ? -16.638 -40.046 -0.636  1.00 48.75  ? 45   PRO A CA  1 
ATOM   352  C  C   . PRO A 1 45  ? -17.889 -39.185 -0.676  1.00 45.80  ? 45   PRO A C   1 
ATOM   353  O  O   . PRO A 1 45  ? -18.224 -38.517 0.308   1.00 47.80  ? 45   PRO A O   1 
ATOM   354  C  CB  . PRO A 1 45  ? -16.681 -41.084 0.492   1.00 47.63  ? 45   PRO A CB  1 
ATOM   355  C  CG  . PRO A 1 45  ? -15.253 -41.203 0.925   1.00 46.60  ? 45   PRO A CG  1 
ATOM   356  C  CD  . PRO A 1 45  ? -14.648 -39.829 0.765   1.00 45.24  ? 45   PRO A CD  1 
ATOM   357  N  N   . GLY A 1 46  ? -18.547 -39.150 -1.833  1.00 49.76  ? 46   GLY A N   1 
ATOM   358  C  CA  . GLY A 1 46  ? -19.785 -38.414 -1.985  1.00 51.41  ? 46   GLY A CA  1 
ATOM   359  C  C   . GLY A 1 46  ? -19.670 -36.904 -1.999  1.00 51.28  ? 46   GLY A C   1 
ATOM   360  O  O   . GLY A 1 46  ? -20.665 -36.222 -1.736  1.00 55.14  ? 46   GLY A O   1 
ATOM   361  N  N   . ARG A 1 47  ? -18.495 -36.352 -2.304  1.00 49.73  ? 47   ARG A N   1 
ATOM   362  C  CA  . ARG A 1 47  ? -18.353 -34.903 -2.327  1.00 49.48  ? 47   ARG A CA  1 
ATOM   363  C  C   . ARG A 1 47  ? -17.158 -34.515 -3.186  1.00 48.93  ? 47   ARG A C   1 
ATOM   364  O  O   . ARG A 1 47  ? -16.124 -35.192 -3.168  1.00 43.59  ? 47   ARG A O   1 
ATOM   365  C  CB  . ARG A 1 47  ? -18.166 -34.319 -0.921  1.00 47.51  ? 47   ARG A CB  1 
ATOM   366  C  CG  . ARG A 1 47  ? -17.660 -32.882 -0.983  1.00 53.71  ? 47   ARG A CG  1 
ATOM   367  C  CD  . ARG A 1 47  ? -18.039 -32.028 0.215   1.00 52.62  ? 47   ARG A CD  1 
ATOM   368  N  NE  . ARG A 1 47  ? -17.375 -30.728 0.154   1.00 51.90  ? 47   ARG A NE  1 
ATOM   369  C  CZ  . ARG A 1 47  ? -16.843 -30.107 1.201   1.00 51.68  ? 47   ARG A CZ  1 
ATOM   370  N  NH1 . ARG A 1 47  ? -16.805 -30.678 2.394   1.00 51.55  ? 47   ARG A NH1 1 
ATOM   371  N  NH2 . ARG A 1 47  ? -16.318 -28.889 1.043   1.00 39.70  ? 47   ARG A NH2 1 
ATOM   372  N  N   . VAL A 1 48  ? -17.297 -33.400 -3.902  1.00 41.88  ? 48   VAL A N   1 
ATOM   373  C  CA  . VAL A 1 48  ? -16.217 -32.817 -4.683  1.00 40.45  ? 48   VAL A CA  1 
ATOM   374  C  C   . VAL A 1 48  ? -16.162 -31.329 -4.365  1.00 38.66  ? 48   VAL A C   1 
ATOM   375  O  O   . VAL A 1 48  ? -17.202 -30.675 -4.242  1.00 39.07  ? 48   VAL A O   1 
ATOM   376  C  CB  . VAL A 1 48  ? -16.416 -33.022 -6.200  1.00 43.74  ? 48   VAL A CB  1 
ATOM   377  C  CG1 . VAL A 1 48  ? -15.286 -32.356 -6.968  1.00 41.59  ? 48   VAL A CG1 1 
ATOM   378  C  CG2 . VAL A 1 48  ? -16.511 -34.498 -6.549  1.00 51.22  ? 48   VAL A CG2 1 
ATOM   379  N  N   . THR A 1 49  ? -14.958 -30.793 -4.238  1.00 36.87  ? 49   THR A N   1 
ATOM   380  C  CA  . THR A 1 49  ? -14.792 -29.349 -4.233  1.00 36.67  ? 49   THR A CA  1 
ATOM   381  C  C   . THR A 1 49  ? -13.520 -29.014 -4.995  1.00 39.33  ? 49   THR A C   1 
ATOM   382  O  O   . THR A 1 49  ? -12.749 -29.898 -5.388  1.00 40.99  ? 49   THR A O   1 
ATOM   383  C  CB  . THR A 1 49  ? -14.788 -28.776 -2.798  1.00 35.19  ? 49   THR A CB  1 
ATOM   384  O  OG1 . THR A 1 49  ? -14.960 -27.355 -2.841  1.00 38.45  ? 49   THR A OG1 1 
ATOM   385  C  CG2 . THR A 1 49  ? -13.497 -29.096 -2.079  1.00 36.13  ? 49   THR A CG2 1 
ATOM   386  N  N   . ARG A 1 50  ? -13.326 -27.724 -5.238  1.00 36.40  ? 50   ARG A N   1 
ATOM   387  C  CA  . ARG A 1 50  ? -12.160 -27.220 -5.951  1.00 36.56  ? 50   ARG A CA  1 
ATOM   388  C  C   . ARG A 1 50  ? -11.520 -26.102 -5.147  1.00 37.62  ? 50   ARG A C   1 
ATOM   389  O  O   . ARG A 1 50  ? -12.187 -25.115 -4.819  1.00 37.78  ? 50   ARG A O   1 
ATOM   390  C  CB  . ARG A 1 50  ? -12.558 -26.713 -7.341  1.00 42.41  ? 50   ARG A CB  1 
ATOM   391  C  CG  . ARG A 1 50  ? -13.297 -27.750 -8.149  1.00 38.07  ? 50   ARG A CG  1 
ATOM   392  C  CD  . ARG A 1 50  ? -14.559 -27.198 -8.740  1.00 41.57  ? 50   ARG A CD  1 
ATOM   393  N  NE  . ARG A 1 50  ? -15.326 -28.259 -9.377  1.00 40.36  ? 50   ARG A NE  1 
ATOM   394  C  CZ  . ARG A 1 50  ? -16.321 -28.918 -8.799  1.00 41.90  ? 50   ARG A CZ  1 
ATOM   395  N  NH1 . ARG A 1 50  ? -16.738 -28.613 -7.574  1.00 40.83  ? 50   ARG A NH1 1 
ATOM   396  N  NH2 . ARG A 1 50  ? -16.914 -29.907 -9.464  1.00 39.60  ? 50   ARG A NH2 1 
ATOM   397  N  N   . TYR A 1 51  ? -10.225 -26.231 -4.870  1.00 32.60  ? 51   TYR A N   1 
ATOM   398  C  CA  . TYR A 1 51  ? -9.486  -25.233 -4.107  1.00 35.46  ? 51   TYR A CA  1 
ATOM   399  C  C   . TYR A 1 51  ? -8.883  -24.179 -5.031  1.00 39.38  ? 51   TYR A C   1 
ATOM   400  O  O   . TYR A 1 51  ? -8.056  -24.502 -5.894  1.00 37.08  ? 51   TYR A O   1 
ATOM   401  C  CB  . TYR A 1 51  ? -8.397  -25.904 -3.282  1.00 33.60  ? 51   TYR A CB  1 
ATOM   402  C  CG  . TYR A 1 51  ? -8.952  -26.596 -2.053  1.00 35.85  ? 51   TYR A CG  1 
ATOM   403  C  CD1 . TYR A 1 51  ? -9.516  -27.864 -2.143  1.00 34.24  ? 51   TYR A CD1 1 
ATOM   404  C  CD2 . TYR A 1 51  ? -8.918  -25.969 -0.814  1.00 36.80  ? 51   TYR A CD2 1 
ATOM   405  C  CE1 . TYR A 1 51  ? -10.027 -28.500 -1.016  1.00 35.09  ? 51   TYR A CE1 1 
ATOM   406  C  CE2 . TYR A 1 51  ? -9.420  -26.585 0.317   1.00 33.17  ? 51   TYR A CE2 1 
ATOM   407  C  CZ  . TYR A 1 51  ? -9.980  -27.846 0.208   1.00 38.14  ? 51   TYR A CZ  1 
ATOM   408  O  OH  . TYR A 1 51  ? -10.486 -28.457 1.324   1.00 36.58  ? 51   TYR A OH  1 
ATOM   409  N  N   . LEU A 1 52  ? -9.289  -22.920 -4.837  1.00 35.87  ? 52   LEU A N   1 
ATOM   410  C  CA  . LEU A 1 52  ? -8.784  -21.784 -5.603  1.00 36.26  ? 52   LEU A CA  1 
ATOM   411  C  C   . LEU A 1 52  ? -7.717  -21.037 -4.808  1.00 35.44  ? 52   LEU A C   1 
ATOM   412  O  O   . LEU A 1 52  ? -7.876  -20.792 -3.609  1.00 33.65  ? 52   LEU A O   1 
ATOM   413  C  CB  . LEU A 1 52  ? -9.923  -20.823 -5.952  1.00 34.06  ? 52   LEU A CB  1 
ATOM   414  C  CG  . LEU A 1 52  ? -11.092 -21.390 -6.748  1.00 37.01  ? 52   LEU A CG  1 
ATOM   415  C  CD1 . LEU A 1 52  ? -12.038 -20.250 -7.137  1.00 38.79  ? 52   LEU A CD1 1 
ATOM   416  C  CD2 . LEU A 1 52  ? -10.597 -22.134 -7.990  1.00 38.38  ? 52   LEU A CD2 1 
ATOM   417  N  N   . SER A 1 53  ? -6.629  -20.669 -5.484  1.00 31.99  ? 53   SER A N   1 
ATOM   418  C  CA  . SER A 1 53  ? -5.519  -19.983 -4.852  1.00 35.21  ? 53   SER A CA  1 
ATOM   419  C  C   . SER A 1 53  ? -5.082  -18.706 -5.558  1.00 31.38  ? 53   SER A C   1 
ATOM   420  O  O   . SER A 1 53  ? -4.236  -17.998 -5.013  1.00 36.19  ? 53   SER A O   1 
ATOM   421  C  CB  . SER A 1 53  ? -4.296  -20.922 -4.756  1.00 37.53  ? 53   SER A CB  1 
ATOM   422  O  OG  . SER A 1 53  ? -4.532  -21.923 -3.793  1.00 45.56  ? 53   SER A OG  1 
ATOM   423  N  N   . SER A 1 54  ? -5.574  -18.418 -6.766  1.00 32.00  ? 54   SER A N   1 
ATOM   424  C  CA  . SER A 1 54  ? -5.106  -17.258 -7.514  1.00 36.77  ? 54   SER A CA  1 
ATOM   425  C  C   . SER A 1 54  ? -6.139  -16.137 -7.479  1.00 36.23  ? 54   SER A C   1 
ATOM   426  O  O   . SER A 1 54  ? -7.348  -16.381 -7.517  1.00 36.19  ? 54   SER A O   1 
ATOM   427  C  CB  . SER A 1 54  ? -4.792  -17.609 -8.988  1.00 32.63  ? 54   SER A CB  1 
ATOM   428  O  OG  . SER A 1 54  ? -5.950  -17.989 -9.714  1.00 33.62  ? 54   SER A OG  1 
ATOM   429  N  N   . GLN A 1 55  ? -5.644  -14.901 -7.461  1.00 35.09  ? 55   GLN A N   1 
ATOM   430  C  CA  . GLN A 1 55  ? -6.543  -13.762 -7.610  1.00 36.70  ? 55   GLN A CA  1 
ATOM   431  C  C   . GLN A 1 55  ? -7.256  -13.811 -8.952  1.00 36.91  ? 55   GLN A C   1 
ATOM   432  O  O   . GLN A 1 55  ? -8.433  -13.447 -9.050  1.00 35.61  ? 55   GLN A O   1 
ATOM   433  C  CB  . GLN A 1 55  ? -5.762  -12.456 -7.441  1.00 40.20  ? 55   GLN A CB  1 
ATOM   434  C  CG  . GLN A 1 55  ? -6.623  -11.202 -7.508  1.00 34.48  ? 55   GLN A CG  1 
ATOM   435  C  CD  . GLN A 1 55  ? -6.726  -10.642 -8.920  1.00 38.37  ? 55   GLN A CD  1 
ATOM   436  O  OE1 . GLN A 1 55  ? -6.116  -11.161 -9.862  1.00 37.89  ? 55   GLN A OE1 1 
ATOM   437  N  NE2 . GLN A 1 55  ? -7.503  -9.580  -9.075  1.00 36.96  ? 55   GLN A NE2 1 
ATOM   438  N  N   . ARG A 1 56  ? -6.572  -14.309 -9.992  1.00 35.13  ? 56   ARG A N   1 
ATOM   439  C  CA  . ARG A 1 56  ? -7.201  -14.460 -11.306 1.00 37.87  ? 56   ARG A CA  1 
ATOM   440  C  C   . ARG A 1 56  ? -8.552  -15.168 -11.210 1.00 37.75  ? 56   ARG A C   1 
ATOM   441  O  O   . ARG A 1 56  ? -9.544  -14.714 -11.789 1.00 37.74  ? 56   ARG A O   1 
ATOM   442  C  CB  . ARG A 1 56  ? -6.257  -15.219 -12.250 1.00 38.61  ? 56   ARG A CB  1 
ATOM   443  C  CG  . ARG A 1 56  ? -6.791  -15.428 -13.665 1.00 47.60  ? 56   ARG A CG  1 
ATOM   444  C  CD  . ARG A 1 56  ? -5.826  -16.266 -14.509 1.00 46.00  ? 56   ARG A CD  1 
ATOM   445  N  NE  . ARG A 1 56  ? -6.099  -17.699 -14.440 1.00 46.89  ? 56   ARG A NE  1 
ATOM   446  C  CZ  . ARG A 1 56  ? -6.935  -18.346 -15.245 1.00 47.33  ? 56   ARG A CZ  1 
ATOM   447  N  NH1 . ARG A 1 56  ? -7.634  -17.713 -16.175 1.00 48.67  ? 56   ARG A NH1 1 
ATOM   448  N  NH2 . ARG A 1 56  ? -7.059  -19.666 -15.128 1.00 46.59  ? 56   ARG A NH2 1 
ATOM   449  N  N   . LEU A 1 57  ? -8.606  -16.301 -10.496 1.00 35.83  ? 57   LEU A N   1 
ATOM   450  C  CA  . LEU A 1 57  ? -9.840  -17.074 -10.408 1.00 35.71  ? 57   LEU A CA  1 
ATOM   451  C  C   . LEU A 1 57  ? -10.739 -16.611 -9.268  1.00 35.15  ? 57   LEU A C   1 
ATOM   452  O  O   . LEU A 1 57  ? -11.970 -16.634 -9.398  1.00 34.59  ? 57   LEU A O   1 
ATOM   453  C  CB  . LEU A 1 57  ? -9.523  -18.564 -10.231 1.00 36.72  ? 57   LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 57  ? -8.848  -19.234 -11.433 1.00 37.62  ? 57   LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 57  ? -8.513  -20.694 -11.154 1.00 37.59  ? 57   LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 57  ? -9.767  -19.122 -12.633 1.00 35.27  ? 57   LEU A CD2 1 
ATOM   457  N  N   . ILE A 1 58  ? -10.151 -16.180 -8.160  1.00 33.32  ? 58   ILE A N   1 
ATOM   458  C  CA  . ILE A 1 58  ? -10.959 -15.842 -6.990  1.00 33.33  ? 58   ILE A CA  1 
ATOM   459  C  C   . ILE A 1 58  ? -11.773 -14.571 -7.241  1.00 35.64  ? 58   ILE A C   1 
ATOM   460  O  O   . ILE A 1 58  ? -12.893 -14.427 -6.732  1.00 37.05  ? 58   ILE A O   1 
ATOM   461  C  CB  . ILE A 1 58  ? -10.025 -15.753 -5.765  1.00 33.88  ? 58   ILE A CB  1 
ATOM   462  C  CG1 . ILE A 1 58  ? -9.686  -17.177 -5.282  1.00 35.61  ? 58   ILE A CG1 1 
ATOM   463  C  CG2 . ILE A 1 58  ? -10.657 -14.921 -4.633  1.00 33.28  ? 58   ILE A CG2 1 
ATOM   464  C  CD1 . ILE A 1 58  ? -8.472  -17.251 -4.353  1.00 31.17  ? 58   ILE A CD1 1 
ATOM   465  N  N   . LYS A 1 59  ? -11.259 -13.654 -8.071  1.00 36.49  ? 59   LYS A N   1 
ATOM   466  C  CA  . LYS A 1 59  ? -12.034 -12.462 -8.406  1.00 35.23  ? 59   LYS A CA  1 
ATOM   467  C  C   . LYS A 1 59  ? -13.326 -12.822 -9.132  1.00 35.27  ? 59   LYS A C   1 
ATOM   468  O  O   . LYS A 1 59  ? -14.332 -12.118 -8.982  1.00 40.37  ? 59   LYS A O   1 
ATOM   469  C  CB  . LYS A 1 59  ? -11.173 -11.472 -9.216  1.00 34.40  ? 59   LYS A CB  1 
ATOM   470  C  CG  . LYS A 1 59  ? -10.956 -11.810 -10.685 1.00 35.59  ? 59   LYS A CG  1 
ATOM   471  C  CD  . LYS A 1 59  ? -9.865  -10.909 -11.303 1.00 36.50  ? 59   LYS A CD  1 
ATOM   472  C  CE  . LYS A 1 59  ? -9.544  -11.312 -12.741 1.00 42.13  ? 59   LYS A CE  1 
ATOM   473  N  NZ  . LYS A 1 59  ? -8.428  -10.482 -13.304 1.00 45.54  ? 59   LYS A NZ  1 
ATOM   474  N  N   . GLU A 1 60  ? -13.342 -13.929 -9.890  1.00 34.42  ? 60   GLU A N   1 
ATOM   475  C  CA  . GLU A 1 60  ? -14.602 -14.383 -10.476 1.00 37.31  ? 60   GLU A CA  1 
ATOM   476  C  C   . GLU A 1 60  ? -15.470 -15.082 -9.436  1.00 34.67  ? 60   GLU A C   1 
ATOM   477  O  O   . GLU A 1 60  ? -16.694 -14.902 -9.417  1.00 34.15  ? 60   GLU A O   1 
ATOM   478  C  CB  . GLU A 1 60  ? -14.340 -15.312 -11.664 1.00 37.66  ? 60   GLU A CB  1 
ATOM   479  C  CG  . GLU A 1 60  ? -13.620 -14.629 -12.811 1.00 39.66  ? 60   GLU A CG  1 
ATOM   480  C  CD  . GLU A 1 60  ? -13.544 -15.480 -14.062 1.00 42.81  ? 60   GLU A CD  1 
ATOM   481  O  OE1 . GLU A 1 60  ? -14.423 -16.341 -14.258 1.00 41.36  ? 60   GLU A OE1 1 
ATOM   482  O  OE2 . GLU A 1 60  ? -12.611 -15.269 -14.863 1.00 44.96  ? 60   GLU A OE2 1 
ATOM   483  N  N   . ALA A 1 61  ? -14.846 -15.858 -8.548  1.00 35.55  ? 61   ALA A N   1 
ATOM   484  C  CA  . ALA A 1 61  ? -15.597 -16.535 -7.503  1.00 34.95  ? 61   ALA A CA  1 
ATOM   485  C  C   . ALA A 1 61  ? -16.338 -15.539 -6.618  1.00 37.01  ? 61   ALA A C   1 
ATOM   486  O  O   . ALA A 1 61  ? -17.405 -15.864 -6.081  1.00 35.95  ? 61   ALA A O   1 
ATOM   487  C  CB  . ALA A 1 61  ? -14.650 -17.402 -6.663  1.00 32.83  ? 61   ALA A CB  1 
ATOM   488  N  N   . CYS A 1 62  ? -15.803 -14.320 -6.470  1.00 33.54  ? 62   CYS A N   1 
ATOM   489  C  CA  . CYS A 1 62  ? -16.418 -13.296 -5.625  1.00 35.12  ? 62   CYS A CA  1 
ATOM   490  C  C   . CYS A 1 62  ? -17.568 -12.546 -6.292  1.00 33.88  ? 62   CYS A C   1 
ATOM   491  O  O   . CYS A 1 62  ? -18.120 -11.619 -5.681  1.00 33.22  ? 62   CYS A O   1 
ATOM   492  C  CB  . CYS A 1 62  ? -15.352 -12.316 -5.152  1.00 34.06  ? 62   CYS A CB  1 
ATOM   493  S  SG  . CYS A 1 62  ? -14.243 -13.072 -3.948  1.00 34.31  ? 62   CYS A SG  1 
ATOM   494  N  N   . ASP A 1 63  ? -17.945 -12.923 -7.509  1.00 35.89  ? 63   ASP A N   1 
ATOM   495  C  CA  . ASP A 1 63  ? -19.124 -12.378 -8.177  1.00 33.71  ? 63   ASP A CA  1 
ATOM   496  C  C   . ASP A 1 63  ? -20.381 -12.983 -7.555  1.00 33.62  ? 63   ASP A C   1 
ATOM   497  O  O   . ASP A 1 63  ? -20.694 -14.155 -7.787  1.00 36.26  ? 63   ASP A O   1 
ATOM   498  C  CB  . ASP A 1 63  ? -19.026 -12.691 -9.668  1.00 35.24  ? 63   ASP A CB  1 
ATOM   499  C  CG  . ASP A 1 63  ? -20.185 -12.152 -10.481 1.00 38.17  ? 63   ASP A CG  1 
ATOM   500  O  OD1 . ASP A 1 63  ? -21.211 -11.726 -9.913  1.00 37.19  ? 63   ASP A OD1 1 
ATOM   501  O  OD2 . ASP A 1 63  ? -20.062 -12.194 -11.727 1.00 40.49  ? 63   ASP A OD2 1 
ATOM   502  N  N   . GLU A 1 64  ? -21.114 -12.182 -6.769  1.00 34.20  ? 64   GLU A N   1 
ATOM   503  C  CA  . GLU A 1 64  ? -22.280 -12.696 -6.045  1.00 34.80  ? 64   GLU A CA  1 
ATOM   504  C  C   . GLU A 1 64  ? -23.444 -13.040 -6.961  1.00 36.43  ? 64   GLU A C   1 
ATOM   505  O  O   . GLU A 1 64  ? -24.383 -13.734 -6.529  1.00 35.30  ? 64   GLU A O   1 
ATOM   506  C  CB  . GLU A 1 64  ? -22.762 -11.676 -5.017  1.00 35.16  ? 64   GLU A CB  1 
ATOM   507  C  CG  . GLU A 1 64  ? -21.731 -11.262 -4.016  1.00 35.23  ? 64   GLU A CG  1 
ATOM   508  C  CD  . GLU A 1 64  ? -22.293 -10.310 -2.988  1.00 40.53  ? 64   GLU A CD  1 
ATOM   509  O  OE1 . GLU A 1 64  ? -22.311 -9.086  -3.244  1.00 43.11  ? 64   GLU A OE1 1 
ATOM   510  O  OE2 . GLU A 1 64  ? -22.723 -10.786 -1.922  1.00 36.30  ? 64   GLU A OE2 1 
ATOM   511  N  N   . SER A 1 65  ? -23.437 -12.537 -8.194  1.00 35.22  ? 65   SER A N   1 
ATOM   512  C  CA  . SER A 1 65  ? -24.445 -12.973 -9.138  1.00 37.02  ? 65   SER A CA  1 
ATOM   513  C  C   . SER A 1 65  ? -24.201 -14.404 -9.582  1.00 36.12  ? 65   SER A C   1 
ATOM   514  O  O   . SER A 1 65  ? -25.130 -15.061 -10.059 1.00 39.45  ? 65   SER A O   1 
ATOM   515  C  CB  . SER A 1 65  ? -24.480 -12.036 -10.359 1.00 37.34  ? 65   SER A CB  1 
ATOM   516  O  OG  . SER A 1 65  ? -23.408 -12.317 -11.237 1.00 38.25  ? 65   SER A OG  1 
ATOM   517  N  N   . ARG A 1 66  ? -22.975 -14.902 -9.438  1.00 35.10  ? 66   ARG A N   1 
ATOM   518  C  CA  . ARG A 1 66  ? -22.628 -16.237 -9.911  1.00 36.18  ? 66   ARG A CA  1 
ATOM   519  C  C   . ARG A 1 66  ? -22.425 -17.254 -8.799  1.00 36.94  ? 66   ARG A C   1 
ATOM   520  O  O   . ARG A 1 66  ? -22.669 -18.439 -9.024  1.00 36.00  ? 66   ARG A O   1 
ATOM   521  C  CB  . ARG A 1 66  ? -21.353 -16.187 -10.768 1.00 38.95  ? 66   ARG A CB  1 
ATOM   522  C  CG  . ARG A 1 66  ? -21.491 -15.397 -12.080 1.00 40.50  ? 66   ARG A CG  1 
ATOM   523  C  CD  . ARG A 1 66  ? -20.110 -15.024 -12.650 1.00 41.87  ? 66   ARG A CD  1 
ATOM   524  N  NE  . ARG A 1 66  ? -19.426 -16.185 -13.198 1.00 41.69  ? 66   ARG A NE  1 
ATOM   525  C  CZ  . ARG A 1 66  ? -18.141 -16.226 -13.526 1.00 42.98  ? 66   ARG A CZ  1 
ATOM   526  N  NH1 . ARG A 1 66  ? -17.346 -15.176 -13.363 1.00 44.11  ? 66   ARG A NH1 1 
ATOM   527  N  NH2 . ARG A 1 66  ? -17.639 -17.350 -14.029 1.00 47.06  ? 66   ARG A NH2 1 
ATOM   528  N  N   . PHE A 1 67  ? -21.969 -16.824 -7.621  1.00 36.34  ? 67   PHE A N   1 
ATOM   529  C  CA  . PHE A 1 67  ? -21.625 -17.715 -6.522  1.00 35.22  ? 67   PHE A CA  1 
ATOM   530  C  C   . PHE A 1 67  ? -22.164 -17.152 -5.215  1.00 33.57  ? 67   PHE A C   1 
ATOM   531  O  O   . PHE A 1 67  ? -22.092 -15.947 -4.966  1.00 33.00  ? 67   PHE A O   1 
ATOM   532  C  CB  . PHE A 1 67  ? -20.105 -17.908 -6.410  1.00 35.07  ? 67   PHE A CB  1 
ATOM   533  C  CG  . PHE A 1 67  ? -19.474 -18.449 -7.666  1.00 38.86  ? 67   PHE A CG  1 
ATOM   534  C  CD1 . PHE A 1 67  ? -19.417 -19.819 -7.891  1.00 36.44  ? 67   PHE A CD1 1 
ATOM   535  C  CD2 . PHE A 1 67  ? -18.954 -17.591 -8.623  1.00 37.12  ? 67   PHE A CD2 1 
ATOM   536  C  CE1 . PHE A 1 67  ? -18.852 -20.326 -9.052  1.00 38.93  ? 67   PHE A CE1 1 
ATOM   537  C  CE2 . PHE A 1 67  ? -18.381 -18.093 -9.791  1.00 39.39  ? 67   PHE A CE2 1 
ATOM   538  C  CZ  . PHE A 1 67  ? -18.326 -19.461 -10.000 1.00 39.90  ? 67   PHE A CZ  1 
ATOM   539  N  N   . ASP A 1 68  ? -22.677 -18.042 -4.379  1.00 33.79  ? 68   ASP A N   1 
ATOM   540  C  CA  . ASP A 1 68  ? -23.204 -17.708 -3.064  1.00 33.16  ? 68   ASP A CA  1 
ATOM   541  C  C   . ASP A 1 68  ? -22.383 -18.451 -2.013  1.00 34.91  ? 68   ASP A C   1 
ATOM   542  O  O   . ASP A 1 68  ? -21.664 -19.405 -2.324  1.00 31.03  ? 68   ASP A O   1 
ATOM   543  C  CB  . ASP A 1 68  ? -24.695 -18.087 -3.004  1.00 33.03  ? 68   ASP A CB  1 
ATOM   544  C  CG  . ASP A 1 68  ? -25.352 -17.771 -1.662  1.00 33.68  ? 68   ASP A CG  1 
ATOM   545  O  OD1 . ASP A 1 68  ? -24.927 -16.837 -0.947  1.00 35.64  ? 68   ASP A OD1 1 
ATOM   546  O  OD2 . ASP A 1 68  ? -26.322 -18.481 -1.347  1.00 34.34  ? 68   ASP A OD2 1 
ATOM   547  N  N   . LYS A 1 69  ? -22.493 -18.019 -0.753  1.00 32.86  ? 69   LYS A N   1 
ATOM   548  C  CA  . LYS A 1 69  ? -21.786 -18.706 0.320   1.00 33.07  ? 69   LYS A CA  1 
ATOM   549  C  C   . LYS A 1 69  ? -22.269 -20.146 0.464   1.00 32.79  ? 69   LYS A C   1 
ATOM   550  O  O   . LYS A 1 69  ? -23.476 -20.418 0.491   1.00 33.30  ? 69   LYS A O   1 
ATOM   551  C  CB  . LYS A 1 69  ? -21.969 -17.962 1.650   1.00 29.55  ? 69   LYS A CB  1 
ATOM   552  C  CG  . LYS A 1 69  ? -21.569 -18.811 2.874   1.00 31.19  ? 69   LYS A CG  1 
ATOM   553  C  CD  . LYS A 1 69  ? -21.282 -17.947 4.113   1.00 30.47  ? 69   LYS A CD  1 
ATOM   554  C  CE  . LYS A 1 69  ? -21.124 -18.842 5.349   1.00 30.32  ? 69   LYS A CE  1 
ATOM   555  N  NZ  . LYS A 1 69  ? -20.364 -18.171 6.459   1.00 29.90  ? 69   LYS A NZ  1 
ATOM   556  N  N   . ASN A 1 70  ? -21.321 -21.063 0.589   1.00 30.25  ? 70   ASN A N   1 
ATOM   557  C  CA  . ASN A 1 70  ? -21.598 -22.467 0.836   1.00 32.70  ? 70   ASN A CA  1 
ATOM   558  C  C   . ASN A 1 70  ? -21.151 -22.829 2.245   1.00 33.65  ? 70   ASN A C   1 
ATOM   559  O  O   . ASN A 1 70  ? -20.192 -22.257 2.769   1.00 32.00  ? 70   ASN A O   1 
ATOM   560  C  CB  . ASN A 1 70  ? -20.863 -23.348 -0.184  1.00 33.00  ? 70   ASN A CB  1 
ATOM   561  C  CG  . ASN A 1 70  ? -21.082 -24.825 0.061   1.00 37.41  ? 70   ASN A CG  1 
ATOM   562  O  OD1 . ASN A 1 70  ? -22.220 -25.290 0.073   1.00 37.15  ? 70   ASN A OD1 1 
ATOM   563  N  ND2 . ASN A 1 70  ? -20.004 -25.566 0.256   1.00 38.06  ? 70   ASN A ND2 1 
ATOM   564  N  N   . LEU A 1 71  ? -21.852 -23.774 2.871   1.00 33.05  ? 71   LEU A N   1 
ATOM   565  C  CA  . LEU A 1 71  ? -21.371 -24.320 4.137   1.00 32.68  ? 71   LEU A CA  1 
ATOM   566  C  C   . LEU A 1 71  ? -20.364 -25.420 3.827   1.00 36.05  ? 71   LEU A C   1 
ATOM   567  O  O   . LEU A 1 71  ? -20.726 -26.475 3.295   1.00 35.93  ? 71   LEU A O   1 
ATOM   568  C  CB  . LEU A 1 71  ? -22.524 -24.844 4.993   1.00 32.77  ? 71   LEU A CB  1 
ATOM   569  C  CG  . LEU A 1 71  ? -23.580 -23.823 5.392   1.00 33.09  ? 71   LEU A CG  1 
ATOM   570  C  CD1 . LEU A 1 71  ? -24.530 -24.407 6.418   1.00 35.35  ? 71   LEU A CD1 1 
ATOM   571  C  CD2 . LEU A 1 71  ? -22.952 -22.522 5.919   1.00 32.81  ? 71   LEU A CD2 1 
ATOM   572  N  N   . SER A 1 72  ? -19.094 -25.157 4.118   1.00 32.29  ? 72   SER A N   1 
ATOM   573  C  CA  . SER A 1 72  ? -18.089 -26.201 4.066   1.00 33.91  ? 72   SER A CA  1 
ATOM   574  C  C   . SER A 1 72  ? -18.450 -27.303 5.061   1.00 36.28  ? 72   SER A C   1 
ATOM   575  O  O   . SER A 1 72  ? -19.302 -27.136 5.940   1.00 33.61  ? 72   SER A O   1 
ATOM   576  C  CB  . SER A 1 72  ? -16.714 -25.624 4.391   1.00 34.85  ? 72   SER A CB  1 
ATOM   577  O  OG  . SER A 1 72  ? -16.713 -25.041 5.686   1.00 36.06  ? 72   SER A OG  1 
ATOM   578  N  N   . GLN A 1 73  ? -17.787 -28.448 4.924   1.00 34.39  ? 73   GLN A N   1 
ATOM   579  C  CA  . GLN A 1 73  ? -18.002 -29.509 5.904   1.00 36.09  ? 73   GLN A CA  1 
ATOM   580  C  C   . GLN A 1 73  ? -17.710 -29.010 7.312   1.00 35.88  ? 73   GLN A C   1 
ATOM   581  O  O   . GLN A 1 73  ? -18.435 -29.334 8.260   1.00 35.36  ? 73   GLN A O   1 
ATOM   582  C  CB  . GLN A 1 73  ? -17.132 -30.722 5.578   1.00 35.47  ? 73   GLN A CB  1 
ATOM   583  C  CG  . GLN A 1 73  ? -17.566 -31.943 6.345   1.00 42.29  ? 73   GLN A CG  1 
ATOM   584  C  CD  . GLN A 1 73  ? -19.012 -32.281 6.042   1.00 48.17  ? 73   GLN A CD  1 
ATOM   585  O  OE1 . GLN A 1 73  ? -19.409 -32.371 4.878   1.00 49.03  ? 73   GLN A OE1 1 
ATOM   586  N  NE2 . GLN A 1 73  ? -19.821 -32.408 7.086   1.00 46.44  ? 73   GLN A NE2 1 
ATOM   587  N  N   . ALA A 1 74  ? -16.644 -28.226 7.466   1.00 34.05  ? 74   ALA A N   1 
ATOM   588  C  CA  . ALA A 1 74  ? -16.311 -27.668 8.769   1.00 35.07  ? 74   ALA A CA  1 
ATOM   589  C  C   . ALA A 1 74  ? -17.465 -26.843 9.330   1.00 32.85  ? 74   ALA A C   1 
ATOM   590  O  O   . ALA A 1 74  ? -17.803 -26.968 10.514  1.00 34.87  ? 74   ALA A O   1 
ATOM   591  C  CB  . ALA A 1 74  ? -15.041 -26.822 8.654   1.00 34.30  ? 74   ALA A CB  1 
ATOM   592  N  N   . LEU A 1 75  ? -18.084 -25.993 8.504   1.00 34.33  ? 75   LEU A N   1 
ATOM   593  C  CA  . LEU A 1 75  ? -19.206 -25.189 8.998   1.00 33.10  ? 75   LEU A CA  1 
ATOM   594  C  C   . LEU A 1 75  ? -20.439 -26.042 9.259   1.00 35.12  ? 75   LEU A C   1 
ATOM   595  O  O   . LEU A 1 75  ? -21.221 -25.732 10.163  1.00 34.05  ? 75   LEU A O   1 
ATOM   596  C  CB  . LEU A 1 75  ? -19.546 -24.058 8.021   1.00 31.83  ? 75   LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 75  ? -18.512 -22.938 7.818   1.00 31.61  ? 75   LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 75  ? -19.109 -21.738 7.045   1.00 31.75  ? 75   LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 75  ? -17.923 -22.465 9.138   1.00 33.14  ? 75   LEU A CD2 1 
ATOM   600  N  N   . LYS A 1 76  ? -20.650 -27.108 8.482   1.00 33.75  ? 76   LYS A N   1 
ATOM   601  C  CA  . LYS A 1 76  ? -21.738 -28.029 8.808   1.00 33.92  ? 76   LYS A CA  1 
ATOM   602  C  C   . LYS A 1 76  ? -21.536 -28.666 10.179  1.00 36.47  ? 76   LYS A C   1 
ATOM   603  O  O   . LYS A 1 76  ? -22.505 -28.894 10.915  1.00 34.97  ? 76   LYS A O   1 
ATOM   604  C  CB  . LYS A 1 76  ? -21.862 -29.096 7.724   1.00 34.96  ? 76   LYS A CB  1 
ATOM   605  C  CG  . LYS A 1 76  ? -22.371 -28.493 6.421   1.00 39.11  ? 76   LYS A CG  1 
ATOM   606  C  CD  . LYS A 1 76  ? -22.548 -29.514 5.329   1.00 46.42  ? 76   LYS A CD  1 
ATOM   607  C  CE  . LYS A 1 76  ? -22.920 -28.813 4.028   1.00 46.16  ? 76   LYS A CE  1 
ATOM   608  N  NZ  . LYS A 1 76  ? -23.036 -29.779 2.913   1.00 55.75  ? 76   LYS A NZ  1 
ATOM   609  N  N   . PHE A 1 77  ? -20.287 -28.961 10.544  1.00 34.55  ? 77   PHE A N   1 
ATOM   610  C  CA  . PHE A 1 77  ? -20.036 -29.530 11.864  1.00 35.05  ? 77   PHE A CA  1 
ATOM   611  C  C   . PHE A 1 77  ? -20.214 -28.475 12.944  1.00 37.29  ? 77   PHE A C   1 
ATOM   612  O  O   . PHE A 1 77  ? -20.813 -28.742 13.994  1.00 39.69  ? 77   PHE A O   1 
ATOM   613  C  CB  . PHE A 1 77  ? -18.630 -30.131 11.931  1.00 37.08  ? 77   PHE A CB  1 
ATOM   614  C  CG  . PHE A 1 77  ? -18.430 -31.333 11.045  1.00 40.14  ? 77   PHE A CG  1 
ATOM   615  C  CD1 . PHE A 1 77  ? -19.501 -32.104 10.646  1.00 43.85  ? 77   PHE A CD1 1 
ATOM   616  C  CD2 . PHE A 1 77  ? -17.154 -31.702 10.635  1.00 38.76  ? 77   PHE A CD2 1 
ATOM   617  C  CE1 . PHE A 1 77  ? -19.312 -33.215 9.836   1.00 46.71  ? 77   PHE A CE1 1 
ATOM   618  C  CE2 . PHE A 1 77  ? -16.963 -32.806 9.819   1.00 43.57  ? 77   PHE A CE2 1 
ATOM   619  C  CZ  . PHE A 1 77  ? -18.044 -33.559 9.421   1.00 42.33  ? 77   PHE A CZ  1 
ATOM   620  N  N   . VAL A 1 78  ? -19.714 -27.266 12.696  1.00 35.44  ? 78   VAL A N   1 
ATOM   621  C  CA  . VAL A 1 78  ? -19.864 -26.203 13.681  1.00 34.72  ? 78   VAL A CA  1 
ATOM   622  C  C   . VAL A 1 78  ? -21.330 -25.840 13.844  1.00 33.07  ? 78   VAL A C   1 
ATOM   623  O  O   . VAL A 1 78  ? -21.755 -25.410 14.927  1.00 38.57  ? 78   VAL A O   1 
ATOM   624  C  CB  . VAL A 1 78  ? -19.005 -24.996 13.267  1.00 38.00  ? 78   VAL A CB  1 
ATOM   625  C  CG1 . VAL A 1 78  ? -19.504 -23.722 13.942  1.00 45.00  ? 78   VAL A CG1 1 
ATOM   626  C  CG2 . VAL A 1 78  ? -17.549 -25.285 13.586  1.00 41.01  ? 78   VAL A CG2 1 
ATOM   627  N  N   . ARG A 1 79  ? -22.129 -26.001 12.781  1.00 33.79  ? 79   ARG A N   1 
ATOM   628  C  CA  . ARG A 1 79  ? -23.557 -25.730 12.891  1.00 34.13  ? 79   ARG A CA  1 
ATOM   629  C  C   . ARG A 1 79  ? -24.219 -26.606 13.941  1.00 36.50  ? 79   ARG A C   1 
ATOM   630  O  O   . ARG A 1 79  ? -25.297 -26.256 14.426  1.00 35.04  ? 79   ARG A O   1 
ATOM   631  C  CB  . ARG A 1 79  ? -24.252 -25.913 11.538  1.00 35.42  ? 79   ARG A CB  1 
ATOM   632  C  CG  . ARG A 1 79  ? -25.758 -25.668 11.564  1.00 35.34  ? 79   ARG A CG  1 
ATOM   633  C  CD  . ARG A 1 79  ? -26.306 -25.399 10.169  1.00 33.40  ? 79   ARG A CD  1 
ATOM   634  N  NE  . ARG A 1 79  ? -27.767 -25.300 10.170  1.00 38.20  ? 79   ARG A NE  1 
ATOM   635  C  CZ  . ARG A 1 79  ? -28.467 -24.413 9.472   1.00 39.63  ? 79   ARG A CZ  1 
ATOM   636  N  NH1 . ARG A 1 79  ? -27.872 -23.509 8.711   1.00 35.83  ? 79   ARG A NH1 1 
ATOM   637  N  NH2 . ARG A 1 79  ? -29.799 -24.426 9.551   1.00 39.64  ? 79   ARG A NH2 1 
ATOM   638  N  N   . ASP A 1 80  ? -23.605 -27.734 14.307  1.00 35.86  ? 80   ASP A N   1 
ATOM   639  C  CA  . ASP A 1 80  ? -24.168 -28.544 15.387  1.00 39.73  ? 80   ASP A CA  1 
ATOM   640  C  C   . ASP A 1 80  ? -24.327 -27.752 16.678  1.00 39.06  ? 80   ASP A C   1 
ATOM   641  O  O   . ASP A 1 80  ? -25.232 -28.049 17.466  1.00 39.62  ? 80   ASP A O   1 
ATOM   642  C  CB  . ASP A 1 80  ? -23.317 -29.785 15.634  1.00 39.09  ? 80   ASP A CB  1 
ATOM   643  C  CG  . ASP A 1 80  ? -23.572 -30.872 14.602  1.00 44.43  ? 80   ASP A CG  1 
ATOM   644  O  OD1 . ASP A 1 80  ? -24.591 -30.778 13.887  1.00 42.54  ? 80   ASP A OD1 1 
ATOM   645  O  OD2 . ASP A 1 80  ? -22.762 -31.817 14.516  1.00 52.15  ? 80   ASP A OD2 1 
ATOM   646  N  N   . PHE A 1 81  ? -23.482 -26.742 16.924  1.00 36.71  ? 81   PHE A N   1 
ATOM   647  C  CA  . PHE A 1 81  ? -23.723 -25.882 18.073  1.00 37.08  ? 81   PHE A CA  1 
ATOM   648  C  C   . PHE A 1 81  ? -24.044 -24.434 17.720  1.00 34.25  ? 81   PHE A C   1 
ATOM   649  O  O   . PHE A 1 81  ? -24.662 -23.754 18.542  1.00 37.62  ? 81   PHE A O   1 
ATOM   650  C  CB  . PHE A 1 81  ? -22.547 -25.926 19.079  1.00 35.95  ? 81   PHE A CB  1 
ATOM   651  C  CG  . PHE A 1 81  ? -21.172 -25.672 18.490  1.00 36.54  ? 81   PHE A CG  1 
ATOM   652  C  CD1 . PHE A 1 81  ? -20.659 -24.385 18.408  1.00 37.46  ? 81   PHE A CD1 1 
ATOM   653  C  CD2 . PHE A 1 81  ? -20.373 -26.729 18.069  1.00 38.75  ? 81   PHE A CD2 1 
ATOM   654  C  CE1 . PHE A 1 81  ? -19.389 -24.151 17.894  1.00 38.62  ? 81   PHE A CE1 1 
ATOM   655  C  CE2 . PHE A 1 81  ? -19.104 -26.500 17.559  1.00 40.80  ? 81   PHE A CE2 1 
ATOM   656  C  CZ  . PHE A 1 81  ? -18.608 -25.212 17.469  1.00 37.56  ? 81   PHE A CZ  1 
ATOM   657  N  N   . ALA A 1 82  ? -23.708 -23.961 16.514  1.00 35.07  ? 82   ALA A N   1 
ATOM   658  C  CA  . ALA A 1 82  ? -24.004 -22.583 16.119  1.00 33.62  ? 82   ALA A CA  1 
ATOM   659  C  C   . ALA A 1 82  ? -25.294 -22.436 15.312  1.00 32.91  ? 82   ALA A C   1 
ATOM   660  O  O   . ALA A 1 82  ? -25.693 -21.306 15.019  1.00 32.36  ? 82   ALA A O   1 
ATOM   661  C  CB  . ALA A 1 82  ? -22.838 -22.001 15.312  1.00 33.59  ? 82   ALA A CB  1 
ATOM   662  N  N   . GLY A 1 83  ? -25.947 -23.540 14.949  1.00 34.75  ? 83   GLY A N   1 
ATOM   663  C  CA  . GLY A 1 83  ? -27.280 -23.488 14.364  1.00 34.72  ? 83   GLY A CA  1 
ATOM   664  C  C   . GLY A 1 83  ? -27.385 -22.602 13.138  1.00 35.52  ? 83   GLY A C   1 
ATOM   665  O  O   . GLY A 1 83  ? -26.495 -22.572 12.279  1.00 33.75  ? 83   GLY A O   1 
ATOM   666  N  N   . ASP A 1 84  ? -28.498 -21.876 13.033  1.00 32.13  ? 84   ASP A N   1 
ATOM   667  C  CA  . ASP A 1 84  ? -28.671 -20.895 11.963  1.00 32.61  ? 84   ASP A CA  1 
ATOM   668  C  C   . ASP A 1 84  ? -28.345 -19.490 12.451  1.00 33.32  ? 84   ASP A C   1 
ATOM   669  O  O   . ASP A 1 84  ? -28.996 -18.524 12.069  1.00 33.80  ? 84   ASP A O   1 
ATOM   670  C  CB  . ASP A 1 84  ? -30.079 -20.970 11.357  1.00 35.35  ? 84   ASP A CB  1 
ATOM   671  C  CG  . ASP A 1 84  ? -31.187 -20.753 12.376  1.00 38.71  ? 84   ASP A CG  1 
ATOM   672  O  OD1 . ASP A 1 84  ? -30.905 -20.715 13.583  1.00 37.05  ? 84   ASP A OD1 1 
ATOM   673  O  OD2 . ASP A 1 84  ? -32.362 -20.630 11.955  1.00 37.68  ? 84   ASP A OD2 1 
ATOM   674  N  N   . GLY A 1 85  ? -27.336 -19.362 13.323  1.00 31.36  ? 85   GLY A N   1 
ATOM   675  C  CA  . GLY A 1 85  ? -26.711 -18.070 13.554  1.00 33.00  ? 85   GLY A CA  1 
ATOM   676  C  C   . GLY A 1 85  ? -26.066 -17.544 12.275  1.00 33.24  ? 85   GLY A C   1 
ATOM   677  O  O   . GLY A 1 85  ? -26.026 -18.213 11.243  1.00 31.30  ? 85   GLY A O   1 
ATOM   678  N  N   . LEU A 1 86  ? -25.545 -16.311 12.344  1.00 29.18  ? 86   LEU A N   1 
ATOM   679  C  CA  . LEU A 1 86  ? -25.144 -15.633 11.106  1.00 29.94  ? 86   LEU A CA  1 
ATOM   680  C  C   . LEU A 1 86  ? -24.033 -16.381 10.380  1.00 31.02  ? 86   LEU A C   1 
ATOM   681  O  O   . LEU A 1 86  ? -23.999 -16.396 9.143   1.00 31.17  ? 86   LEU A O   1 
ATOM   682  C  CB  . LEU A 1 86  ? -24.708 -14.187 11.397  1.00 31.38  ? 86   LEU A CB  1 
ATOM   683  C  CG  . LEU A 1 86  ? -25.866 -13.186 11.566  1.00 32.02  ? 86   LEU A CG  1 
ATOM   684  C  CD1 . LEU A 1 86  ? -25.333 -11.827 11.987  1.00 35.42  ? 86   LEU A CD1 1 
ATOM   685  C  CD2 . LEU A 1 86  ? -26.665 -13.053 10.267  1.00 30.69  ? 86   LEU A CD2 1 
ATOM   686  N  N   . PHE A 1 87  ? -23.105 -16.997 11.123  1.00 32.11  ? 87   PHE A N   1 
ATOM   687  C  CA  . PHE A 1 87  ? -21.919 -17.575 10.476  1.00 30.17  ? 87   PHE A CA  1 
ATOM   688  C  C   . PHE A 1 87  ? -22.256 -18.880 9.753   1.00 32.61  ? 87   PHE A C   1 
ATOM   689  O  O   . PHE A 1 87  ? -21.647 -19.201 8.726   1.00 29.76  ? 87   PHE A O   1 
ATOM   690  C  CB  . PHE A 1 87  ? -20.815 -17.824 11.520  1.00 29.93  ? 87   PHE A CB  1 
ATOM   691  C  CG  . PHE A 1 87  ? -19.399 -17.817 10.967  1.00 30.71  ? 87   PHE A CG  1 
ATOM   692  C  CD1 . PHE A 1 87  ? -18.932 -18.869 10.172  1.00 31.59  ? 87   PHE A CD1 1 
ATOM   693  C  CD2 . PHE A 1 87  ? -18.537 -16.769 11.263  1.00 31.09  ? 87   PHE A CD2 1 
ATOM   694  C  CE1 . PHE A 1 87  ? -17.634 -18.865 9.674   1.00 32.72  ? 87   PHE A CE1 1 
ATOM   695  C  CE2 . PHE A 1 87  ? -17.221 -16.751 10.758  1.00 34.65  ? 87   PHE A CE2 1 
ATOM   696  C  CZ  . PHE A 1 87  ? -16.780 -17.808 9.963   1.00 32.20  ? 87   PHE A CZ  1 
ATOM   697  N  N   . THR A 1 88  ? -23.229 -19.635 10.253  1.00 31.14  ? 88   THR A N   1 
ATOM   698  C  CA  . THR A 1 88  ? -23.474 -20.976 9.740   1.00 33.97  ? 88   THR A CA  1 
ATOM   699  C  C   . THR A 1 88  ? -24.846 -21.114 9.090   1.00 32.49  ? 88   THR A C   1 
ATOM   700  O  O   . THR A 1 88  ? -25.292 -22.241 8.850   1.00 34.56  ? 88   THR A O   1 
ATOM   701  C  CB  . THR A 1 88  ? -23.313 -22.026 10.849  1.00 31.89  ? 88   THR A CB  1 
ATOM   702  O  OG1 . THR A 1 88  ? -24.058 -21.630 12.008  1.00 32.25  ? 88   THR A OG1 1 
ATOM   703  C  CG2 . THR A 1 88  ? -21.843 -22.179 11.230  1.00 30.27  ? 88   THR A CG2 1 
ATOM   704  N  N   . SER A 1 89  ? -25.518 -20.012 8.790   1.00 33.53  ? 89   SER A N   1 
ATOM   705  C  CA  . SER A 1 89  ? -26.766 -20.073 8.048   1.00 33.77  ? 89   SER A CA  1 
ATOM   706  C  C   . SER A 1 89  ? -26.500 -19.935 6.549   1.00 33.94  ? 89   SER A C   1 
ATOM   707  O  O   . SER A 1 89  ? -25.504 -19.335 6.121   1.00 32.11  ? 89   SER A O   1 
ATOM   708  C  CB  . SER A 1 89  ? -27.731 -18.990 8.532   1.00 37.36  ? 89   SER A CB  1 
ATOM   709  O  OG  . SER A 1 89  ? -27.116 -17.719 8.523   1.00 38.32  ? 89   SER A OG  1 
ATOM   710  N  N   . TRP A 1 90  ? -27.385 -20.533 5.749   1.00 33.63  ? 90   TRP A N   1 
ATOM   711  C  CA  . TRP A 1 90  ? -27.394 -20.276 4.315   1.00 35.00  ? 90   TRP A CA  1 
ATOM   712  C  C   . TRP A 1 90  ? -28.011 -18.911 4.030   1.00 33.79  ? 90   TRP A C   1 
ATOM   713  O  O   . TRP A 1 90  ? -28.924 -18.461 4.728   1.00 33.15  ? 90   TRP A O   1 
ATOM   714  C  CB  . TRP A 1 90  ? -28.200 -21.345 3.571   1.00 34.22  ? 90   TRP A CB  1 
ATOM   715  C  CG  . TRP A 1 90  ? -27.726 -22.736 3.809   1.00 35.61  ? 90   TRP A CG  1 
ATOM   716  C  CD1 . TRP A 1 90  ? -28.151 -23.584 4.776   1.00 33.11  ? 90   TRP A CD1 1 
ATOM   717  C  CD2 . TRP A 1 90  ? -26.738 -23.439 3.057   1.00 33.90  ? 90   TRP A CD2 1 
ATOM   718  N  NE1 . TRP A 1 90  ? -27.494 -24.795 4.673   1.00 34.87  ? 90   TRP A NE1 1 
ATOM   719  C  CE2 . TRP A 1 90  ? -26.616 -24.725 3.624   1.00 33.61  ? 90   TRP A CE2 1 
ATOM   720  C  CE3 . TRP A 1 90  ? -25.947 -23.110 1.951   1.00 31.80  ? 90   TRP A CE3 1 
ATOM   721  C  CZ2 . TRP A 1 90  ? -25.730 -25.685 3.123   1.00 38.24  ? 90   TRP A CZ2 1 
ATOM   722  C  CZ3 . TRP A 1 90  ? -25.062 -24.064 1.456   1.00 36.27  ? 90   TRP A CZ3 1 
ATOM   723  C  CH2 . TRP A 1 90  ? -24.961 -25.334 2.044   1.00 36.01  ? 90   TRP A CH2 1 
ATOM   724  N  N   . THR A 1 91  ? -27.538 -18.269 2.961   1.00 32.97  ? 91   THR A N   1 
ATOM   725  C  CA  . THR A 1 91  ? -28.063 -16.952 2.614   1.00 32.38  ? 91   THR A CA  1 
ATOM   726  C  C   . THR A 1 91  ? -29.572 -16.979 2.406   1.00 33.50  ? 91   THR A C   1 
ATOM   727  O  O   . THR A 1 91  ? -30.243 -15.967 2.622   1.00 34.44  ? 91   THR A O   1 
ATOM   728  C  CB  . THR A 1 91  ? -27.357 -16.447 1.356   1.00 29.51  ? 91   THR A CB  1 
ATOM   729  O  OG1 . THR A 1 91  ? -25.946 -16.556 1.552   1.00 30.82  ? 91   THR A OG1 1 
ATOM   730  C  CG2 . THR A 1 91  ? -27.724 -14.999 1.043   1.00 33.82  ? 91   THR A CG2 1 
ATOM   731  N  N   . HIS A 1 92  ? -30.113 -18.104 1.959   1.00 34.66  ? 92   HIS A N   1 
ATOM   732  C  CA  . HIS A 1 92  ? -31.537 -18.191 1.656   1.00 33.73  ? 92   HIS A CA  1 
ATOM   733  C  C   . HIS A 1 92  ? -32.388 -18.620 2.847   1.00 33.41  ? 92   HIS A C   1 
ATOM   734  O  O   . HIS A 1 92  ? -33.616 -18.659 2.717   1.00 34.96  ? 92   HIS A O   1 
ATOM   735  C  CB  . HIS A 1 92  ? -31.771 -19.151 0.488   1.00 34.59  ? 92   HIS A CB  1 
ATOM   736  C  CG  . HIS A 1 92  ? -31.085 -20.469 0.650   1.00 35.04  ? 92   HIS A CG  1 
ATOM   737  N  ND1 . HIS A 1 92  ? -31.543 -21.445 1.510   1.00 37.22  ? 92   HIS A ND1 1 
ATOM   738  C  CD2 . HIS A 1 92  ? -29.972 -20.972 0.066   1.00 38.03  ? 92   HIS A CD2 1 
ATOM   739  C  CE1 . HIS A 1 92  ? -30.740 -22.492 1.446   1.00 35.26  ? 92   HIS A CE1 1 
ATOM   740  N  NE2 . HIS A 1 92  ? -29.779 -22.230 0.582   1.00 37.88  ? 92   HIS A NE2 1 
ATOM   741  N  N   . GLU A 1 93  ? -31.792 -18.949 3.992   1.00 33.13  ? 93   GLU A N   1 
ATOM   742  C  CA  . GLU A 1 93  ? -32.616 -19.201 5.170   1.00 33.96  ? 93   GLU A CA  1 
ATOM   743  C  C   . GLU A 1 93  ? -33.147 -17.884 5.712   1.00 34.86  ? 93   GLU A C   1 
ATOM   744  O  O   . GLU A 1 93  ? -32.428 -16.878 5.756   1.00 37.31  ? 93   GLU A O   1 
ATOM   745  C  CB  . GLU A 1 93  ? -31.825 -19.922 6.260   1.00 34.31  ? 93   GLU A CB  1 
ATOM   746  C  CG  . GLU A 1 93  ? -31.494 -21.397 5.957   1.00 36.13  ? 93   GLU A CG  1 
ATOM   747  C  CD  . GLU A 1 93  ? -30.670 -22.030 7.068   1.00 40.86  ? 93   GLU A CD  1 
ATOM   748  O  OE1 . GLU A 1 93  ? -29.441 -21.779 7.116   1.00 37.38  ? 93   GLU A OE1 1 
ATOM   749  O  OE2 . GLU A 1 93  ? -31.245 -22.780 7.892   1.00 39.68  ? 93   GLU A OE2 1 
ATOM   750  N  N   . LYS A 1 94  ? -34.415 -17.885 6.135   1.00 36.13  ? 94   LYS A N   1 
ATOM   751  C  CA  . LYS A 1 94  ? -35.019 -16.624 6.547   1.00 33.13  ? 94   LYS A CA  1 
ATOM   752  C  C   . LYS A 1 94  ? -34.205 -15.971 7.663   1.00 34.37  ? 94   LYS A C   1 
ATOM   753  O  O   . LYS A 1 94  ? -34.024 -14.750 7.674   1.00 36.26  ? 94   LYS A O   1 
ATOM   754  C  CB  . LYS A 1 94  ? -36.475 -16.841 6.977   1.00 38.77  ? 94   LYS A CB  1 
ATOM   755  C  CG  . LYS A 1 94  ? -37.055 -15.731 7.837   1.00 39.89  ? 94   LYS A CG  1 
ATOM   756  C  CD  . LYS A 1 94  ? -38.510 -16.029 8.197   1.00 42.17  ? 94   LYS A CD  1 
ATOM   757  C  CE  . LYS A 1 94  ? -38.992 -15.127 9.305   1.00 50.79  ? 94   LYS A CE  1 
ATOM   758  N  NZ  . LYS A 1 94  ? -40.132 -15.728 10.052  1.00 61.01  ? 94   LYS A NZ  1 
ATOM   759  N  N   . ASN A 1 95  ? -33.644 -16.771 8.568   1.00 33.66  ? 95   ASN A N   1 
ATOM   760  C  CA  . ASN A 1 95  ? -32.961 -16.157 9.697   1.00 34.05  ? 95   ASN A CA  1 
ATOM   761  C  C   . ASN A 1 95  ? -31.633 -15.501 9.315   1.00 35.22  ? 95   ASN A C   1 
ATOM   762  O  O   . ASN A 1 95  ? -31.111 -14.722 10.122  1.00 32.93  ? 95   ASN A O   1 
ATOM   763  C  CB  . ASN A 1 95  ? -32.760 -17.187 10.810  1.00 34.00  ? 95   ASN A CB  1 
ATOM   764  C  CG  . ASN A 1 95  ? -33.984 -17.317 11.691  1.00 35.70  ? 95   ASN A CG  1 
ATOM   765  O  OD1 . ASN A 1 95  ? -34.759 -16.368 11.823  1.00 39.55  ? 95   ASN A OD1 1 
ATOM   766  N  ND2 . ASN A 1 95  ? -34.162 -18.484 12.298  1.00 36.50  ? 95   ASN A ND2 1 
ATOM   767  N  N   . TRP A 1 96  ? -31.082 -15.741 8.116   1.00 32.49  ? 96   TRP A N   1 
ATOM   768  C  CA  . TRP A 1 96  ? -29.848 -15.029 7.787   1.00 32.73  ? 96   TRP A CA  1 
ATOM   769  C  C   . TRP A 1 96  ? -30.116 -13.540 7.597   1.00 32.91  ? 96   TRP A C   1 
ATOM   770  O  O   . TRP A 1 96  ? -29.589 -12.709 8.338   1.00 34.58  ? 96   TRP A O   1 
ATOM   771  C  CB  . TRP A 1 96  ? -29.125 -15.599 6.551   1.00 34.56  ? 96   TRP A CB  1 
ATOM   772  C  CG  . TRP A 1 96  ? -27.945 -14.697 6.336   1.00 32.41  ? 96   TRP A CG  1 
ATOM   773  C  CD1 . TRP A 1 96  ? -26.828 -14.616 7.131   1.00 32.00  ? 96   TRP A CD1 1 
ATOM   774  C  CD2 . TRP A 1 96  ? -27.846 -13.621 5.401   1.00 36.39  ? 96   TRP A CD2 1 
ATOM   775  N  NE1 . TRP A 1 96  ? -26.017 -13.589 6.703   1.00 33.09  ? 96   TRP A NE1 1 
ATOM   776  C  CE2 . TRP A 1 96  ? -26.619 -12.963 5.646   1.00 31.15  ? 96   TRP A CE2 1 
ATOM   777  C  CE3 . TRP A 1 96  ? -28.660 -13.165 4.356   1.00 35.33  ? 96   TRP A CE3 1 
ATOM   778  C  CZ2 . TRP A 1 96  ? -26.184 -11.881 4.871   1.00 37.72  ? 96   TRP A CZ2 1 
ATOM   779  C  CZ3 . TRP A 1 96  ? -28.236 -12.076 3.598   1.00 35.63  ? 96   TRP A CZ3 1 
ATOM   780  C  CH2 . TRP A 1 96  ? -27.002 -11.456 3.852   1.00 36.77  ? 96   TRP A CH2 1 
ATOM   781  N  N   . LYS A 1 97  ? -30.930 -13.169 6.596   1.00 31.58  ? 97   LYS A N   1 
ATOM   782  C  CA  . LYS A 1 97  ? -31.145 -11.746 6.353   1.00 34.61  ? 97   LYS A CA  1 
ATOM   783  C  C   . LYS A 1 97  ? -31.846 -11.086 7.531   1.00 34.85  ? 97   LYS A C   1 
ATOM   784  O  O   . LYS A 1 97  ? -31.575 -9.924  7.839   1.00 33.63  ? 97   LYS A O   1 
ATOM   785  C  CB  . LYS A 1 97  ? -31.935 -11.538 5.057   1.00 37.76  ? 97   LYS A CB  1 
ATOM   786  C  CG  . LYS A 1 97  ? -32.160 -10.064 4.678   1.00 39.38  ? 97   LYS A CG  1 
ATOM   787  C  CD  . LYS A 1 97  ? -30.867 -9.266  4.614   1.00 42.23  ? 97   LYS A CD  1 
ATOM   788  C  CE  . LYS A 1 97  ? -31.007 -8.061  3.692   1.00 47.82  ? 97   LYS A CE  1 
ATOM   789  N  NZ  . LYS A 1 97  ? -29.692 -7.431  3.379   1.00 52.74  ? 97   LYS A NZ  1 
ATOM   790  N  N   . LYS A 1 98  ? -32.723 -11.815 8.227   1.00 32.81  ? 98   LYS A N   1 
ATOM   791  C  CA  . LYS A 1 98  ? -33.422 -11.218 9.358   1.00 34.77  ? 98   LYS A CA  1 
ATOM   792  C  C   . LYS A 1 98  ? -32.435 -10.813 10.457  1.00 33.79  ? 98   LYS A C   1 
ATOM   793  O  O   . LYS A 1 98  ? -32.441 -9.669  10.928  1.00 33.34  ? 98   LYS A O   1 
ATOM   794  C  CB  . LYS A 1 98  ? -34.478 -12.196 9.875   1.00 37.92  ? 98   LYS A CB  1 
ATOM   795  C  CG  . LYS A 1 98  ? -35.274 -11.717 11.083  1.00 39.15  ? 98   LYS A CG  1 
ATOM   796  C  CD  . LYS A 1 98  ? -36.310 -12.790 11.447  1.00 39.78  ? 98   LYS A CD  1 
ATOM   797  C  CE  . LYS A 1 98  ? -36.891 -12.574 12.830  1.00 41.89  ? 98   LYS A CE  1 
ATOM   798  N  NZ  . LYS A 1 98  ? -37.935 -13.609 13.071  1.00 41.37  ? 98   LYS A NZ  1 
ATOM   799  N  N   . ALA A 1 99  ? -31.542 -11.728 10.846  1.00 31.60  ? 99   ALA A N   1 
ATOM   800  C  CA  . ALA A 1 99  ? -30.555 -11.395 11.873  1.00 31.44  ? 99   ALA A CA  1 
ATOM   801  C  C   . ALA A 1 99  ? -29.525 -10.403 11.362  1.00 32.84  ? 99   ALA A C   1 
ATOM   802  O  O   . ALA A 1 99  ? -29.027 -9.574  12.135  1.00 32.32  ? 99   ALA A O   1 
ATOM   803  C  CB  . ALA A 1 99  ? -29.848 -12.655 12.370  1.00 30.45  ? 99   ALA A CB  1 
ATOM   804  N  N   . HIS A 1 100 ? -29.179 -10.479 10.075  1.00 34.23  ? 100  HIS A N   1 
ATOM   805  C  CA  . HIS A 1 100 ? -28.279 -9.484  9.505   1.00 33.41  ? 100  HIS A CA  1 
ATOM   806  C  C   . HIS A 1 100 ? -28.861 -8.081  9.656   1.00 34.68  ? 100  HIS A C   1 
ATOM   807  O  O   . HIS A 1 100 ? -28.188 -7.159  10.135  1.00 34.00  ? 100  HIS A O   1 
ATOM   808  C  CB  . HIS A 1 100 ? -28.009 -9.813  8.034   1.00 33.84  ? 100  HIS A CB  1 
ATOM   809  C  CG  . HIS A 1 100 ? -27.211 -8.769  7.323   1.00 40.40  ? 100  HIS A CG  1 
ATOM   810  N  ND1 . HIS A 1 100 ? -25.833 -8.783  7.298   1.00 46.02  ? 100  HIS A ND1 1 
ATOM   811  C  CD2 . HIS A 1 100 ? -27.591 -7.682  6.611   1.00 46.57  ? 100  HIS A CD2 1 
ATOM   812  C  CE1 . HIS A 1 100 ? -25.398 -7.748  6.600   1.00 45.37  ? 100  HIS A CE1 1 
ATOM   813  N  NE2 . HIS A 1 100 ? -26.444 -7.065  6.171   1.00 48.97  ? 100  HIS A NE2 1 
ATOM   814  N  N   . ASN A 1 101 ? -30.140 -7.910  9.302   1.00 34.62  ? 101  ASN A N   1 
ATOM   815  C  CA  . ASN A 1 101 ? -30.757 -6.589  9.412   1.00 34.45  ? 101  ASN A CA  1 
ATOM   816  C  C   . ASN A 1 101 ? -30.810 -6.116  10.857  1.00 34.79  ? 101  ASN A C   1 
ATOM   817  O  O   . ASN A 1 101 ? -30.628 -4.924  11.135  1.00 35.38  ? 101  ASN A O   1 
ATOM   818  C  CB  . ASN A 1 101 ? -32.175 -6.607  8.827   1.00 35.95  ? 101  ASN A CB  1 
ATOM   819  C  CG  . ASN A 1 101 ? -32.184 -6.651  7.312   1.00 38.03  ? 101  ASN A CG  1 
ATOM   820  O  OD1 . ASN A 1 101 ? -31.180 -6.362  6.666   1.00 36.96  ? 101  ASN A OD1 1 
ATOM   821  N  ND2 . ASN A 1 101 ? -33.335 -7.001  6.736   1.00 37.26  ? 101  ASN A ND2 1 
ATOM   822  N  N   . ILE A 1 102 ? -31.096 -7.030  11.784  1.00 32.45  ? 102  ILE A N   1 
ATOM   823  C  CA  . ILE A 1 102 ? -31.278 -6.647  13.175  1.00 34.30  ? 102  ILE A CA  1 
ATOM   824  C  C   . ILE A 1 102 ? -29.941 -6.337  13.827  1.00 34.61  ? 102  ILE A C   1 
ATOM   825  O  O   . ILE A 1 102 ? -29.861 -5.439  14.661  1.00 32.38  ? 102  ILE A O   1 
ATOM   826  C  CB  . ILE A 1 102 ? -32.025 -7.755  13.933  1.00 33.29  ? 102  ILE A CB  1 
ATOM   827  C  CG1 . ILE A 1 102 ? -33.484 -7.838  13.465  1.00 37.74  ? 102  ILE A CG1 1 
ATOM   828  C  CG2 . ILE A 1 102 ? -31.890 -7.574  15.453  1.00 38.32  ? 102  ILE A CG2 1 
ATOM   829  C  CD1 . ILE A 1 102 ? -34.203 -9.100  13.919  1.00 34.46  ? 102  ILE A CD1 1 
ATOM   830  N  N   . LEU A 1 103 ? -28.868 -7.025  13.427  1.00 33.82  ? 103  LEU A N   1 
ATOM   831  C  CA  . LEU A 1 103 ? -27.594 -6.885  14.133  1.00 34.01  ? 103  LEU A CA  1 
ATOM   832  C  C   . LEU A 1 103 ? -26.600 -5.962  13.434  1.00 32.74  ? 103  LEU A C   1 
ATOM   833  O  O   . LEU A 1 103 ? -25.660 -5.484  14.079  1.00 32.06  ? 103  LEU A O   1 
ATOM   834  C  CB  . LEU A 1 103 ? -26.968 -8.274  14.360  1.00 31.72  ? 103  LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 103 ? -27.850 -9.223  15.183  1.00 32.11  ? 103  LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 103 ? -27.187 -10.583 15.325  1.00 30.16  ? 103  LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 103 ? -28.157 -8.631  16.578  1.00 33.76  ? 103  LEU A CD2 1 
ATOM   838  N  N   . LEU A 1 104 ? -26.801 -5.644  12.166  1.00 33.83  ? 104  LEU A N   1 
ATOM   839  C  CA  . LEU A 1 104 ? -25.911 -4.688  11.512  1.00 36.20  ? 104  LEU A CA  1 
ATOM   840  C  C   . LEU A 1 104 ? -25.774 -3.373  12.280  1.00 36.90  ? 104  LEU A C   1 
ATOM   841  O  O   . LEU A 1 104 ? -24.646 -2.853  12.369  1.00 34.92  ? 104  LEU A O   1 
ATOM   842  C  CB  . LEU A 1 104 ? -26.402 -4.444  10.081  1.00 34.28  ? 104  LEU A CB  1 
ATOM   843  C  CG  . LEU A 1 104 ? -25.435 -3.679  9.181   1.00 41.96  ? 104  LEU A CG  1 
ATOM   844  C  CD1 . LEU A 1 104 ? -24.140 -4.482  9.045   1.00 44.12  ? 104  LEU A CD1 1 
ATOM   845  C  CD2 . LEU A 1 104 ? -26.080 -3.418  7.817   1.00 44.37  ? 104  LEU A CD2 1 
ATOM   846  N  N   . PRO A 1 105 ? -26.830 -2.801  12.861  1.00 35.44  ? 105  PRO A N   1 
ATOM   847  C  CA  . PRO A 1 105 ? -26.664 -1.545  13.616  1.00 38.87  ? 105  PRO A CA  1 
ATOM   848  C  C   . PRO A 1 105 ? -25.744 -1.672  14.821  1.00 36.29  ? 105  PRO A C   1 
ATOM   849  O  O   . PRO A 1 105 ? -25.199 -0.659  15.271  1.00 38.20  ? 105  PRO A O   1 
ATOM   850  C  CB  . PRO A 1 105 ? -28.097 -1.200  14.045  1.00 37.34  ? 105  PRO A CB  1 
ATOM   851  C  CG  . PRO A 1 105 ? -28.954 -1.835  12.980  1.00 39.74  ? 105  PRO A CG  1 
ATOM   852  C  CD  . PRO A 1 105 ? -28.250 -3.140  12.662  1.00 34.46  ? 105  PRO A CD  1 
ATOM   853  N  N   . SER A 1 106 ? -25.546 -2.879  15.348  1.00 33.37  ? 106  SER A N   1 
ATOM   854  C  CA  . SER A 1 106 ? -24.623 -3.107  16.456  1.00 33.62  ? 106  SER A CA  1 
ATOM   855  C  C   . SER A 1 106 ? -23.166 -2.948  16.052  1.00 34.82  ? 106  SER A C   1 
ATOM   856  O  O   . SER A 1 106 ? -22.283 -3.080  16.908  1.00 36.90  ? 106  SER A O   1 
ATOM   857  C  CB  . SER A 1 106 ? -24.832 -4.510  17.028  1.00 36.85  ? 106  SER A CB  1 
ATOM   858  O  OG  . SER A 1 106 ? -26.079 -4.580  17.680  1.00 41.78  ? 106  SER A OG  1 
ATOM   859  N  N   . PHE A 1 107 ? -22.892 -2.692  14.773  1.00 35.33  ? 107  PHE A N   1 
ATOM   860  C  CA  . PHE A 1 107 ? -21.527 -2.463  14.308  1.00 36.03  ? 107  PHE A CA  1 
ATOM   861  C  C   . PHE A 1 107 ? -21.397 -1.150  13.540  1.00 40.07  ? 107  PHE A C   1 
ATOM   862  O  O   . PHE A 1 107 ? -20.409 -0.944  12.836  1.00 38.43  ? 107  PHE A O   1 
ATOM   863  C  CB  . PHE A 1 107 ? -21.056 -3.666  13.482  1.00 34.62  ? 107  PHE A CB  1 
ATOM   864  C  CG  . PHE A 1 107 ? -21.056 -4.921  14.279  1.00 34.36  ? 107  PHE A CG  1 
ATOM   865  C  CD1 . PHE A 1 107 ? -20.008 -5.191  15.147  1.00 35.97  ? 107  PHE A CD1 1 
ATOM   866  C  CD2 . PHE A 1 107 ? -22.145 -5.777  14.262  1.00 35.30  ? 107  PHE A CD2 1 
ATOM   867  C  CE1 . PHE A 1 107 ? -20.026 -6.322  15.943  1.00 38.19  ? 107  PHE A CE1 1 
ATOM   868  C  CE2 . PHE A 1 107 ? -22.174 -6.904  15.056  1.00 35.85  ? 107  PHE A CE2 1 
ATOM   869  C  CZ  . PHE A 1 107 ? -21.113 -7.185  15.896  1.00 36.00  ? 107  PHE A CZ  1 
ATOM   870  N  N   . SER A 1 108 ? -22.355 -0.242  13.703  1.00 40.22  ? 108  SER A N   1 
ATOM   871  C  CA  . SER A 1 108 ? -22.247 1.103   13.158  1.00 40.58  ? 108  SER A CA  1 
ATOM   872  C  C   . SER A 1 108 ? -21.130 1.884   13.859  1.00 45.82  ? 108  SER A C   1 
ATOM   873  O  O   . SER A 1 108 ? -20.591 1.471   14.895  1.00 40.22  ? 108  SER A O   1 
ATOM   874  C  CB  . SER A 1 108 ? -23.567 1.841   13.325  1.00 44.22  ? 108  SER A CB  1 
ATOM   875  O  OG  . SER A 1 108 ? -23.839 2.050   14.703  1.00 44.93  ? 108  SER A OG  1 
ATOM   876  N  N   . GLN A 1 109 ? -20.779 3.038   13.277  1.00 44.10  ? 109  GLN A N   1 
ATOM   877  C  CA  . GLN A 1 109 ? -19.834 3.934   13.942  1.00 44.75  ? 109  GLN A CA  1 
ATOM   878  C  C   . GLN A 1 109 ? -20.314 4.294   15.341  1.00 42.15  ? 109  GLN A C   1 
ATOM   879  O  O   . GLN A 1 109 ? -19.544 4.247   16.309  1.00 44.67  ? 109  GLN A O   1 
ATOM   880  C  CB  . GLN A 1 109 ? -19.605 5.215   13.121  1.00 47.38  ? 109  GLN A CB  1 
ATOM   881  C  CG  . GLN A 1 109 ? -18.783 5.062   11.843  1.00 55.90  ? 109  GLN A CG  1 
ATOM   882  C  CD  . GLN A 1 109 ? -19.107 6.130   10.793  1.00 54.43  ? 109  GLN A CD  1 
ATOM   883  O  OE1 . GLN A 1 109 ? -19.625 7.200   11.116  1.00 52.71  ? 109  GLN A OE1 1 
ATOM   884  N  NE2 . GLN A 1 109 ? -18.772 5.850   9.540   1.00 55.86  ? 109  GLN A NE2 1 
ATOM   885  N  N   . GLN A 1 110 ? -21.588 4.668   15.469  1.00 41.11  ? 110  GLN A N   1 
ATOM   886  C  CA  . GLN A 1 110 ? -22.094 5.072   16.772  1.00 43.61  ? 110  GLN A CA  1 
ATOM   887  C  C   . GLN A 1 110 ? -22.003 3.920   17.767  1.00 42.79  ? 110  GLN A C   1 
ATOM   888  O  O   . GLN A 1 110 ? -21.704 4.127   18.952  1.00 41.26  ? 110  GLN A O   1 
ATOM   889  C  CB  . GLN A 1 110 ? -23.532 5.570   16.644  1.00 48.23  ? 110  GLN A CB  1 
ATOM   890  C  CG  . GLN A 1 110 ? -24.183 5.805   17.972  1.00 53.17  ? 110  GLN A CG  1 
ATOM   891  C  CD  . GLN A 1 110 ? -23.601 7.031   18.646  1.00 65.56  ? 110  GLN A CD  1 
ATOM   892  O  OE1 . GLN A 1 110 ? -23.197 6.984   19.812  1.00 69.48  ? 110  GLN A OE1 1 
ATOM   893  N  NE2 . GLN A 1 110 ? -23.525 8.133   17.902  1.00 63.95  ? 110  GLN A NE2 1 
ATOM   894  N  N   . ALA A 1 111 ? -22.256 2.697   17.297  1.00 41.36  ? 111  ALA A N   1 
ATOM   895  C  CA  . ALA A 1 111 ? -22.136 1.520   18.151  1.00 40.47  ? 111  ALA A CA  1 
ATOM   896  C  C   . ALA A 1 111 ? -20.695 1.310   18.603  1.00 37.88  ? 111  ALA A C   1 
ATOM   897  O  O   . ALA A 1 111 ? -20.448 1.008   19.777  1.00 39.95  ? 111  ALA A O   1 
ATOM   898  C  CB  . ALA A 1 111 ? -22.659 0.282   17.416  1.00 40.24  ? 111  ALA A CB  1 
ATOM   899  N  N   . MET A 1 112 ? -19.731 1.419   17.676  1.00 37.47  ? 112  MET A N   1 
ATOM   900  C  CA  . MET A 1 112 ? -18.322 1.299   18.061  1.00 38.01  ? 112  MET A CA  1 
ATOM   901  C  C   . MET A 1 112 ? -17.890 2.375   19.040  1.00 38.96  ? 112  MET A C   1 
ATOM   902  O  O   . MET A 1 112 ? -17.105 2.101   19.958  1.00 36.67  ? 112  MET A O   1 
ATOM   903  C  CB  . MET A 1 112 ? -17.399 1.291   16.841  1.00 38.53  ? 112  MET A CB  1 
ATOM   904  C  CG  . MET A 1 112 ? -17.757 0.272   15.793  1.00 44.50  ? 112  MET A CG  1 
ATOM   905  S  SD  . MET A 1 112 ? -17.102 -1.283  16.522  1.00 41.44  ? 112  MET A SD  1 
ATOM   906  C  CE  . MET A 1 112 ? -15.587 -0.730  17.231  1.00 43.60  ? 112  MET A CE  1 
ATOM   907  N  N   . LYS A 1 113 ? -18.344 3.612   18.846  1.00 37.67  ? 113  LYS A N   1 
ATOM   908  C  CA  . LYS A 1 113 ? -18.034 4.626   19.846  1.00 38.60  ? 113  LYS A CA  1 
ATOM   909  C  C   . LYS A 1 113 ? -18.552 4.208   21.216  1.00 38.42  ? 113  LYS A C   1 
ATOM   910  O  O   . LYS A 1 113 ? -17.898 4.458   22.236  1.00 40.73  ? 113  LYS A O   1 
ATOM   911  C  CB  . LYS A 1 113 ? -18.611 5.976   19.422  1.00 36.58  ? 113  LYS A CB  1 
ATOM   912  C  CG  . LYS A 1 113 ? -17.945 6.527   18.167  1.00 42.67  ? 113  LYS A CG  1 
ATOM   913  C  CD  . LYS A 1 113 ? -18.590 7.833   17.713  1.00 44.00  ? 113  LYS A CD  1 
ATOM   914  C  CE  . LYS A 1 113 ? -17.967 8.333   16.408  1.00 46.24  ? 113  LYS A CE  1 
ATOM   915  N  NZ  . LYS A 1 113 ? -18.847 9.324   15.712  1.00 49.80  ? 113  LYS A NZ  1 
ATOM   916  N  N   . GLY A 1 114 ? -19.707 3.535   21.252  1.00 37.43  ? 114  GLY A N   1 
ATOM   917  C  CA  . GLY A 1 114 ? -20.265 3.080   22.514  1.00 41.94  ? 114  GLY A CA  1 
ATOM   918  C  C   . GLY A 1 114 ? -19.537 1.890   23.117  1.00 40.31  ? 114  GLY A C   1 
ATOM   919  O  O   . GLY A 1 114 ? -19.585 1.683   24.335  1.00 41.35  ? 114  GLY A O   1 
ATOM   920  N  N   . TYR A 1 115 ? -18.872 1.084   22.285  1.00 37.02  ? 115  TYR A N   1 
ATOM   921  C  CA  . TYR A 1 115 ? -18.077 -0.032  22.795  1.00 35.79  ? 115  TYR A CA  1 
ATOM   922  C  C   . TYR A 1 115 ? -16.729 0.407   23.332  1.00 36.00  ? 115  TYR A C   1 
ATOM   923  O  O   . TYR A 1 115 ? -16.120 -0.334  24.112  1.00 34.14  ? 115  TYR A O   1 
ATOM   924  C  CB  . TYR A 1 115 ? -17.802 -1.064  21.700  1.00 33.68  ? 115  TYR A CB  1 
ATOM   925  C  CG  . TYR A 1 115 ? -19.017 -1.729  21.130  1.00 32.21  ? 115  TYR A CG  1 
ATOM   926  C  CD1 . TYR A 1 115 ? -20.051 -2.144  21.951  1.00 35.80  ? 115  TYR A CD1 1 
ATOM   927  C  CD2 . TYR A 1 115 ? -19.114 -1.962  19.752  1.00 36.11  ? 115  TYR A CD2 1 
ATOM   928  C  CE1 . TYR A 1 115 ? -21.153 -2.775  21.420  1.00 37.00  ? 115  TYR A CE1 1 
ATOM   929  C  CE2 . TYR A 1 115 ? -20.206 -2.573  19.215  1.00 34.08  ? 115  TYR A CE2 1 
ATOM   930  C  CZ  . TYR A 1 115 ? -21.224 -2.976  20.047  1.00 35.91  ? 115  TYR A CZ  1 
ATOM   931  O  OH  . TYR A 1 115 ? -22.316 -3.598  19.507  1.00 38.86  ? 115  TYR A OH  1 
ATOM   932  N  N   . HIS A 1 116 ? -16.242 1.572   22.908  1.00 35.97  ? 116  HIS A N   1 
ATOM   933  C  CA  . HIS A 1 116 ? -14.833 1.905   23.086  1.00 36.65  ? 116  HIS A CA  1 
ATOM   934  C  C   . HIS A 1 116 ? -14.399 1.852   24.553  1.00 36.23  ? 116  HIS A C   1 
ATOM   935  O  O   . HIS A 1 116 ? -13.344 1.297   24.878  1.00 36.20  ? 116  HIS A O   1 
ATOM   936  C  CB  . HIS A 1 116 ? -14.551 3.287   22.501  1.00 35.14  ? 116  HIS A CB  1 
ATOM   937  C  CG  . HIS A 1 116 ? -13.122 3.694   22.626  1.00 37.14  ? 116  HIS A CG  1 
ATOM   938  N  ND1 . HIS A 1 116 ? -12.175 3.391   21.669  1.00 36.64  ? 116  HIS A ND1 1 
ATOM   939  C  CD2 . HIS A 1 116 ? -12.470 4.357   23.610  1.00 40.40  ? 116  HIS A CD2 1 
ATOM   940  C  CE1 . HIS A 1 116 ? -11.002 3.863   22.054  1.00 41.10  ? 116  HIS A CE1 1 
ATOM   941  N  NE2 . HIS A 1 116 ? -11.154 4.454   23.228  1.00 37.86  ? 116  HIS A NE2 1 
ATOM   942  N  N   . ALA A 1 117 ? -15.175 2.459   25.447  1.00 34.45  ? 117  ALA A N   1 
ATOM   943  C  CA  . ALA A 1 117 ? -14.787 2.487   26.860  1.00 38.72  ? 117  ALA A CA  1 
ATOM   944  C  C   . ALA A 1 117 ? -14.589 1.082   27.432  1.00 37.20  ? 117  ALA A C   1 
ATOM   945  O  O   . ALA A 1 117 ? -13.664 0.856   28.222  1.00 34.88  ? 117  ALA A O   1 
ATOM   946  C  CB  . ALA A 1 117 ? -15.825 3.247   27.683  1.00 40.81  ? 117  ALA A CB  1 
ATOM   947  N  N   . MET A 1 118 ? -15.466 0.128   27.084  1.00 34.99  ? 118  MET A N   1 
ATOM   948  C  CA  . MET A 1 118 ? -15.280 -1.216  27.632  1.00 34.75  ? 118  MET A CA  1 
ATOM   949  C  C   . MET A 1 118 ? -14.120 -1.941  26.965  1.00 33.23  ? 118  MET A C   1 
ATOM   950  O  O   . MET A 1 118 ? -13.518 -2.836  27.569  1.00 33.24  ? 118  MET A O   1 
ATOM   951  C  CB  . MET A 1 118 ? -16.550 -2.064  27.521  1.00 35.35  ? 118  MET A CB  1 
ATOM   952  C  CG  . MET A 1 118 ? -17.627 -1.781  28.582  1.00 38.49  ? 118  MET A CG  1 
ATOM   953  S  SD  . MET A 1 118 ? -19.273 -2.286  28.018  1.00 49.53  ? 118  MET A SD  1 
ATOM   954  C  CE  . MET A 1 118 ? -20.125 -2.357  29.606  1.00 45.59  ? 118  MET A CE  1 
ATOM   955  N  N   . MET A 1 119 ? -13.798 -1.581  25.726  1.00 32.72  ? 119  MET A N   1 
ATOM   956  C  CA  . MET A 1 119 ? -12.611 -2.142  25.121  1.00 30.57  ? 119  MET A CA  1 
ATOM   957  C  C   . MET A 1 119 ? -11.393 -1.686  25.906  1.00 34.65  ? 119  MET A C   1 
ATOM   958  O  O   . MET A 1 119 ? -10.456 -2.456  26.135  1.00 33.67  ? 119  MET A O   1 
ATOM   959  C  CB  . MET A 1 119 ? -12.496 -1.683  23.672  1.00 34.38  ? 119  MET A CB  1 
ATOM   960  C  CG  . MET A 1 119 ? -13.303 -2.535  22.697  1.00 36.02  ? 119  MET A CG  1 
ATOM   961  S  SD  . MET A 1 119 ? -12.926 -2.131  20.991  1.00 33.58  ? 119  MET A SD  1 
ATOM   962  C  CE  . MET A 1 119 ? -14.393 -2.776  20.177  1.00 33.76  ? 119  MET A CE  1 
ATOM   963  N  N   . VAL A 1 120 ? -11.398 -0.419  26.323  1.00 32.34  ? 120  VAL A N   1 
ATOM   964  C  CA  . VAL A 1 120 ? -10.270 0.112   27.072  1.00 34.13  ? 120  VAL A CA  1 
ATOM   965  C  C   . VAL A 1 120 ? -10.175 -0.579  28.421  1.00 33.59  ? 120  VAL A C   1 
ATOM   966  O  O   . VAL A 1 120 ? -9.079  -0.897  28.888  1.00 35.87  ? 120  VAL A O   1 
ATOM   967  C  CB  . VAL A 1 120 ? -10.395 1.643   27.205  1.00 37.98  ? 120  VAL A CB  1 
ATOM   968  C  CG1 . VAL A 1 120 ? -9.346  2.186   28.161  1.00 37.47  ? 120  VAL A CG1 1 
ATOM   969  C  CG2 . VAL A 1 120 ? -10.228 2.301   25.834  1.00 34.58  ? 120  VAL A CG2 1 
ATOM   970  N  N   . ASP A 1 121 ? -11.319 -0.828  29.067  1.00 32.86  ? 121  ASP A N   1 
ATOM   971  C  CA  . ASP A 1 121 ? -11.322 -1.576  30.319  1.00 34.28  ? 121  ASP A CA  1 
ATOM   972  C  C   . ASP A 1 121 ? -10.460 -2.833  30.203  1.00 34.37  ? 121  ASP A C   1 
ATOM   973  O  O   . ASP A 1 121 ? -9.540  -3.052  31.002  1.00 34.07  ? 121  ASP A O   1 
ATOM   974  C  CB  . ASP A 1 121 ? -12.766 -1.931  30.695  1.00 33.51  ? 121  ASP A CB  1 
ATOM   975  C  CG  . ASP A 1 121 ? -12.890 -2.578  32.063  1.00 34.88  ? 121  ASP A CG  1 
ATOM   976  O  OD1 . ASP A 1 121 ? -12.332 -3.675  32.283  1.00 33.70  ? 121  ASP A OD1 1 
ATOM   977  O  OD2 . ASP A 1 121 ? -13.601 -2.007  32.914  1.00 35.87  ? 121  ASP A OD2 1 
ATOM   978  N  N   . ILE A 1 122 ? -10.719 -3.654  29.184  1.00 31.62  ? 122  ILE A N   1 
ATOM   979  C  CA  . ILE A 1 122 ? -9.996  -4.917  29.063  1.00 33.17  ? 122  ILE A CA  1 
ATOM   980  C  C   . ILE A 1 122 ? -8.548  -4.668  28.654  1.00 34.75  ? 122  ILE A C   1 
ATOM   981  O  O   . ILE A 1 122 ? -7.629  -5.357  29.118  1.00 32.90  ? 122  ILE A O   1 
ATOM   982  C  CB  . ILE A 1 122 ? -10.704 -5.859  28.072  1.00 33.18  ? 122  ILE A CB  1 
ATOM   983  C  CG1 . ILE A 1 122 ? -12.187 -6.019  28.430  1.00 29.27  ? 122  ILE A CG1 1 
ATOM   984  C  CG2 . ILE A 1 122 ? -10.006 -7.211  28.061  1.00 30.69  ? 122  ILE A CG2 1 
ATOM   985  C  CD1 . ILE A 1 122 ? -12.417 -6.446  29.882  1.00 30.80  ? 122  ILE A CD1 1 
ATOM   986  N  N   . ALA A 1 123 ? -8.323  -3.687  27.779  1.00 32.18  ? 123  ALA A N   1 
ATOM   987  C  CA  . ALA A 1 123 ? -6.968  -3.397  27.320  1.00 32.99  ? 123  ALA A CA  1 
ATOM   988  C  C   . ALA A 1 123 ? -6.088  -2.954  28.478  1.00 34.29  ? 123  ALA A C   1 
ATOM   989  O  O   . ALA A 1 123 ? -4.913  -3.333  28.563  1.00 33.92  ? 123  ALA A O   1 
ATOM   990  C  CB  . ALA A 1 123 ? -6.997  -2.308  26.244  1.00 35.33  ? 123  ALA A CB  1 
ATOM   991  N  N   . VAL A 1 124 ? -6.638  -2.133  29.365  1.00 32.76  ? 124  VAL A N   1 
ATOM   992  C  CA  . VAL A 1 124 ? -5.881  -1.705  30.543  1.00 35.19  ? 124  VAL A CA  1 
ATOM   993  C  C   . VAL A 1 124 ? -5.555  -2.906  31.435  1.00 34.68  ? 124  VAL A C   1 
ATOM   994  O  O   . VAL A 1 124 ? -4.450  -3.011  31.976  1.00 36.48  ? 124  VAL A O   1 
ATOM   995  C  CB  . VAL A 1 124 ? -6.663  -0.611  31.295  1.00 36.35  ? 124  VAL A CB  1 
ATOM   996  C  CG1 . VAL A 1 124 ? -6.101  -0.403  32.710  1.00 38.20  ? 124  VAL A CG1 1 
ATOM   997  C  CG2 . VAL A 1 124 ? -6.630  0.711   30.508  1.00 32.31  ? 124  VAL A CG2 1 
ATOM   998  N  N   . GLN A 1 125 ? -6.486  -3.855  31.568  1.00 33.25  ? 125  GLN A N   1 
ATOM   999  C  CA  . GLN A 1 125 ? -6.176  -5.067  32.326  1.00 33.45  ? 125  GLN A CA  1 
ATOM   1000 C  C   . GLN A 1 125 ? -4.995  -5.817  31.716  1.00 35.19  ? 125  GLN A C   1 
ATOM   1001 O  O   . GLN A 1 125 ? -4.162  -6.373  32.445  1.00 34.11  ? 125  GLN A O   1 
ATOM   1002 C  CB  . GLN A 1 125 ? -7.405  -5.979  32.420  1.00 34.91  ? 125  GLN A CB  1 
ATOM   1003 C  CG  . GLN A 1 125 ? -8.539  -5.418  33.276  1.00 34.21  ? 125  GLN A CG  1 
ATOM   1004 C  CD  . GLN A 1 125 ? -9.610  -6.451  33.570  1.00 32.02  ? 125  GLN A CD  1 
ATOM   1005 O  OE1 . GLN A 1 125 ? -9.312  -7.579  33.997  1.00 32.53  ? 125  GLN A OE1 1 
ATOM   1006 N  NE2 . GLN A 1 125 ? -10.876 -6.073  33.347  1.00 32.60  ? 125  GLN A NE2 1 
ATOM   1007 N  N   . LEU A 1 126 ? -4.909  -5.856  30.381  1.00 31.70  ? 126  LEU A N   1 
ATOM   1008 C  CA  . LEU A 1 126 ? -3.776  -6.511  29.740  1.00 29.09  ? 126  LEU A CA  1 
ATOM   1009 C  C   . LEU A 1 126 ? -2.478  -5.770  30.049  1.00 33.57  ? 126  LEU A C   1 
ATOM   1010 O  O   . LEU A 1 126 ? -1.475  -6.380  30.454  1.00 34.30  ? 126  LEU A O   1 
ATOM   1011 C  CB  . LEU A 1 126 ? -3.999  -6.605  28.223  1.00 33.90  ? 126  LEU A CB  1 
ATOM   1012 C  CG  . LEU A 1 126 ? -2.758  -7.093  27.459  1.00 35.36  ? 126  LEU A CG  1 
ATOM   1013 C  CD1 . LEU A 1 126 ? -2.562  -8.596  27.650  1.00 34.24  ? 126  LEU A CD1 1 
ATOM   1014 C  CD2 . LEU A 1 126 ? -2.841  -6.745  25.972  1.00 41.52  ? 126  LEU A CD2 1 
ATOM   1015 N  N   . VAL A 1 127 ? -2.477  -4.448  29.864  1.00 33.71  ? 127  VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 127 ? -1.258  -3.676  30.103  1.00 35.63  ? 127  VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 127 ? -0.806  -3.838  31.551  1.00 36.68  ? 127  VAL A C   1 
ATOM   1018 O  O   . VAL A 1 127 ? 0.381   -4.047  31.826  1.00 35.67  ? 127  VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 127 ? -1.474  -2.194  29.740  1.00 36.03  ? 127  VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 127 ? -0.242  -1.363  30.145  1.00 38.07  ? 127  VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 127 ? -1.766  -2.042  28.240  1.00 35.40  ? 127  VAL A CG2 1 
ATOM   1022 N  N   . GLN A 1 128 ? -1.749  -3.759  32.495  1.00 34.75  ? 128  GLN A N   1 
ATOM   1023 C  CA  . GLN A 1 128 ? -1.422  -3.935  33.911  1.00 35.41  ? 128  GLN A CA  1 
ATOM   1024 C  C   . GLN A 1 128 ? -0.840  -5.320  34.190  1.00 34.92  ? 128  GLN A C   1 
ATOM   1025 O  O   . GLN A 1 128 ? 0.124   -5.446  34.957  1.00 35.45  ? 128  GLN A O   1 
ATOM   1026 C  CB  . GLN A 1 128 ? -2.683  -3.671  34.734  1.00 34.18  ? 128  GLN A CB  1 
ATOM   1027 C  CG  . GLN A 1 128 ? -3.047  -2.188  34.761  1.00 35.06  ? 128  GLN A CG  1 
ATOM   1028 C  CD  . GLN A 1 128 ? -4.165  -1.873  35.717  1.00 48.92  ? 128  GLN A CD  1 
ATOM   1029 O  OE1 . GLN A 1 128 ? -5.124  -2.643  35.822  1.00 51.64  ? 128  GLN A OE1 1 
ATOM   1030 N  NE2 . GLN A 1 128 ? -4.072  -0.736  36.411  1.00 52.19  ? 128  GLN A NE2 1 
ATOM   1031 N  N   . LYS A 1 129 ? -1.407  -6.375  33.594  1.00 33.38  ? 129  LYS A N   1 
ATOM   1032 C  CA  . LYS A 1 129 ? -0.836  -7.705  33.794  1.00 31.47  ? 129  LYS A CA  1 
ATOM   1033 C  C   . LYS A 1 129 ? 0.645   -7.711  33.428  1.00 34.36  ? 129  LYS A C   1 
ATOM   1034 O  O   . LYS A 1 129 ? 1.491   -8.216  34.179  1.00 33.90  ? 129  LYS A O   1 
ATOM   1035 C  CB  . LYS A 1 129 ? -1.566  -8.766  32.966  1.00 34.45  ? 129  LYS A CB  1 
ATOM   1036 C  CG  . LYS A 1 129 ? -0.917  -10.146 33.145  1.00 35.94  ? 129  LYS A CG  1 
ATOM   1037 C  CD  . LYS A 1 129 ? -1.658  -11.250 32.413  1.00 35.03  ? 129  LYS A CD  1 
ATOM   1038 C  CE  . LYS A 1 129 ? -0.933  -12.593 32.597  1.00 37.29  ? 129  LYS A CE  1 
ATOM   1039 N  NZ  . LYS A 1 129 ? -1.654  -13.756 31.995  1.00 36.70  ? 129  LYS A NZ  1 
ATOM   1040 N  N   . TRP A 1 130 ? 0.971   -7.123  32.280  1.00 33.76  ? 130  TRP A N   1 
ATOM   1041 C  CA  . TRP A 1 130 ? 2.347   -7.166  31.799  1.00 33.79  ? 130  TRP A CA  1 
ATOM   1042 C  C   . TRP A 1 130 ? 3.255   -6.238  32.597  1.00 36.77  ? 130  TRP A C   1 
ATOM   1043 O  O   . TRP A 1 130 ? 4.432   -6.569  32.822  1.00 36.65  ? 130  TRP A O   1 
ATOM   1044 C  CB  . TRP A 1 130 ? 2.366   -6.829  30.304  1.00 32.81  ? 130  TRP A CB  1 
ATOM   1045 C  CG  . TRP A 1 130 ? 1.749   -7.906  29.434  1.00 32.82  ? 130  TRP A CG  1 
ATOM   1046 C  CD1 . TRP A 1 130 ? 1.204   -9.106  29.839  1.00 32.93  ? 130  TRP A CD1 1 
ATOM   1047 C  CD2 . TRP A 1 130 ? 1.604   -7.859  28.017  1.00 32.96  ? 130  TRP A CD2 1 
ATOM   1048 N  NE1 . TRP A 1 130 ? 0.745   -9.811  28.742  1.00 33.27  ? 130  TRP A NE1 1 
ATOM   1049 C  CE2 . TRP A 1 130 ? 0.983   -9.062  27.613  1.00 31.64  ? 130  TRP A CE2 1 
ATOM   1050 C  CE3 . TRP A 1 130 ? 1.960   -6.918  27.043  1.00 33.99  ? 130  TRP A CE3 1 
ATOM   1051 C  CZ2 . TRP A 1 130 ? 0.713   -9.349  26.276  1.00 33.89  ? 130  TRP A CZ2 1 
ATOM   1052 C  CZ3 . TRP A 1 130 ? 1.679   -7.209  25.700  1.00 30.09  ? 130  TRP A CZ3 1 
ATOM   1053 C  CH2 . TRP A 1 130 ? 1.071   -8.414  25.341  1.00 33.09  ? 130  TRP A CH2 1 
ATOM   1054 N  N   . GLU A 1 131 ? 2.740   -5.084  33.034  1.00 33.23  ? 131  GLU A N   1 
ATOM   1055 C  CA  . GLU A 1 131 ? 3.513   -4.220  33.928  1.00 36.83  ? 131  GLU A CA  1 
ATOM   1056 C  C   . GLU A 1 131 ? 3.869   -4.929  35.227  1.00 38.63  ? 131  GLU A C   1 
ATOM   1057 O  O   . GLU A 1 131 ? 4.888   -4.610  35.858  1.00 35.09  ? 131  GLU A O   1 
ATOM   1058 C  CB  . GLU A 1 131 ? 2.738   -2.939  34.244  1.00 36.87  ? 131  GLU A CB  1 
ATOM   1059 C  CG  . GLU A 1 131 ? 2.432   -2.032  33.038  1.00 37.31  ? 131  GLU A CG  1 
ATOM   1060 C  CD  . GLU A 1 131 ? 3.590   -1.109  32.694  1.00 43.85  ? 131  GLU A CD  1 
ATOM   1061 O  OE1 . GLU A 1 131 ? 4.757   -1.470  32.984  1.00 41.56  ? 131  GLU A OE1 1 
ATOM   1062 O  OE2 . GLU A 1 131 ? 3.335   -0.020  32.138  1.00 46.66  ? 131  GLU A OE2 1 
ATOM   1063 N  N   . ARG A 1 132 ? 3.055   -5.892  35.639  1.00 34.49  ? 132  ARG A N   1 
ATOM   1064 C  CA  . ARG A 1 132 ? 3.220   -6.529  36.937  1.00 35.74  ? 132  ARG A CA  1 
ATOM   1065 C  C   . ARG A 1 132 ? 4.044   -7.808  36.887  1.00 36.94  ? 132  ARG A C   1 
ATOM   1066 O  O   . ARG A 1 132 ? 4.193   -8.468  37.927  1.00 35.72  ? 132  ARG A O   1 
ATOM   1067 C  CB  . ARG A 1 132 ? 1.842   -6.818  37.549  1.00 32.84  ? 132  ARG A CB  1 
ATOM   1068 C  CG  . ARG A 1 132 ? 1.170   -5.568  38.083  1.00 31.72  ? 132  ARG A CG  1 
ATOM   1069 C  CD  . ARG A 1 132 ? -0.310  -5.780  38.415  1.00 33.81  ? 132  ARG A CD  1 
ATOM   1070 N  NE  . ARG A 1 132 ? -0.901  -4.511  38.826  1.00 34.63  ? 132  ARG A NE  1 
ATOM   1071 C  CZ  . ARG A 1 132 ? -2.203  -4.274  38.897  1.00 36.79  ? 132  ARG A CZ  1 
ATOM   1072 N  NH1 . ARG A 1 132 ? -3.092  -5.182  38.529  1.00 35.13  ? 132  ARG A NH1 1 
ATOM   1073 N  NH2 . ARG A 1 132 ? -2.622  -3.098  39.355  1.00 38.36  ? 132  ARG A NH2 1 
ATOM   1074 N  N   . LEU A 1 133 ? 4.593   -8.163  35.724  1.00 36.86  ? 133  LEU A N   1 
ATOM   1075 C  CA  . LEU A 1 133 ? 5.452   -9.331  35.615  1.00 32.50  ? 133  LEU A CA  1 
ATOM   1076 C  C   . LEU A 1 133 ? 6.792   -9.064  36.289  1.00 37.88  ? 133  LEU A C   1 
ATOM   1077 O  O   . LEU A 1 133 ? 7.275   -7.928  36.330  1.00 38.96  ? 133  LEU A O   1 
ATOM   1078 C  CB  . LEU A 1 133 ? 5.671   -9.695  34.145  1.00 36.70  ? 133  LEU A CB  1 
ATOM   1079 C  CG  . LEU A 1 133 ? 4.415   -10.247 33.466  1.00 36.64  ? 133  LEU A CG  1 
ATOM   1080 C  CD1 . LEU A 1 133 ? 4.737   -10.668 32.020  1.00 37.05  ? 133  LEU A CD1 1 
ATOM   1081 C  CD2 . LEU A 1 133 ? 3.846   -11.423 34.248  1.00 36.34  ? 133  LEU A CD2 1 
ATOM   1082 N  N   . ASN A 1 134 ? 7.385   -10.120 36.835  1.00 35.31  ? 134  ASN A N   1 
ATOM   1083 C  CA  . ASN A 1 134 ? 8.709   -9.959  37.411  1.00 40.84  ? 134  ASN A CA  1 
ATOM   1084 C  C   . ASN A 1 134 ? 9.758   -10.025 36.312  1.00 42.95  ? 134  ASN A C   1 
ATOM   1085 O  O   . ASN A 1 134 ? 9.473   -10.387 35.167  1.00 42.88  ? 134  ASN A O   1 
ATOM   1086 C  CB  . ASN A 1 134 ? 8.984   -11.025 38.464  1.00 37.78  ? 134  ASN A CB  1 
ATOM   1087 C  CG  . ASN A 1 134 ? 7.991   -10.975 39.594  1.00 37.82  ? 134  ASN A CG  1 
ATOM   1088 O  OD1 . ASN A 1 134 ? 7.932   -9.994  40.335  1.00 36.52  ? 134  ASN A OD1 1 
ATOM   1089 N  ND2 . ASN A 1 134 ? 7.190   -12.019 39.715  1.00 38.29  ? 134  ASN A ND2 1 
ATOM   1090 N  N   . ALA A 1 135 ? 10.989  -9.672  36.678  1.00 48.72  ? 135  ALA A N   1 
ATOM   1091 C  CA  . ALA A 1 135 ? 12.085  -9.676  35.716  1.00 51.58  ? 135  ALA A CA  1 
ATOM   1092 C  C   . ALA A 1 135 ? 12.295  -11.072 35.144  1.00 46.54  ? 135  ALA A C   1 
ATOM   1093 O  O   . ALA A 1 135 ? 12.279  -12.072 35.866  1.00 51.37  ? 135  ALA A O   1 
ATOM   1094 C  CB  . ALA A 1 135 ? 13.371  -9.179  36.379  1.00 51.56  ? 135  ALA A CB  1 
ATOM   1095 N  N   . ASP A 1 136 ? 12.485  -11.142 33.829  1.00 52.34  ? 136  ASP A N   1 
ATOM   1096 C  CA  . ASP A 1 136 ? 12.745  -12.387 33.115  1.00 53.65  ? 136  ASP A CA  1 
ATOM   1097 C  C   . ASP A 1 136 ? 11.566  -13.356 33.110  1.00 54.83  ? 136  ASP A C   1 
ATOM   1098 O  O   . ASP A 1 136 ? 11.684  -14.433 32.505  1.00 56.75  ? 136  ASP A O   1 
ATOM   1099 C  CB  . ASP A 1 136 ? 13.985  -13.117 33.650  1.00 60.51  ? 136  ASP A CB  1 
ATOM   1100 C  CG  . ASP A 1 136 ? 15.279  -12.409 33.285  1.00 64.86  ? 136  ASP A CG  1 
ATOM   1101 O  OD1 . ASP A 1 136 ? 15.234  -11.462 32.463  1.00 66.22  ? 136  ASP A OD1 1 
ATOM   1102 O  OD2 . ASP A 1 136 ? 16.337  -12.792 33.825  1.00 67.60  ? 136  ASP A OD2 1 
ATOM   1103 N  N   . GLU A 1 137 ? 10.442  -13.031 33.757  1.00 47.40  ? 137  GLU A N   1 
ATOM   1104 C  CA  . GLU A 1 137 ? 9.211   -13.712 33.388  1.00 38.24  ? 137  GLU A CA  1 
ATOM   1105 C  C   . GLU A 1 137 ? 8.858   -13.321 31.957  1.00 38.97  ? 137  GLU A C   1 
ATOM   1106 O  O   . GLU A 1 137 ? 9.343   -12.325 31.423  1.00 44.48  ? 137  GLU A O   1 
ATOM   1107 C  CB  . GLU A 1 137 ? 8.060   -13.356 34.340  1.00 40.45  ? 137  GLU A CB  1 
ATOM   1108 C  CG  . GLU A 1 137 ? 8.261   -13.947 35.732  1.00 43.60  ? 137  GLU A CG  1 
ATOM   1109 C  CD  . GLU A 1 137 ? 7.163   -13.605 36.725  1.00 46.25  ? 137  GLU A CD  1 
ATOM   1110 O  OE1 . GLU A 1 137 ? 6.264   -12.787 36.420  1.00 39.02  ? 137  GLU A OE1 1 
ATOM   1111 O  OE2 . GLU A 1 137 ? 7.220   -14.164 37.840  1.00 50.06  ? 137  GLU A OE2 1 
ATOM   1112 N  N   . HIS A 1 138 ? 8.006   -14.110 31.333  1.00 36.17  ? 138  HIS A N   1 
ATOM   1113 C  CA  . HIS A 1 138 ? 7.661   -13.823 29.952  1.00 40.99  ? 138  HIS A CA  1 
ATOM   1114 C  C   . HIS A 1 138 ? 6.153   -13.829 29.776  1.00 38.73  ? 138  HIS A C   1 
ATOM   1115 O  O   . HIS A 1 138 ? 5.388   -14.178 30.682  1.00 38.00  ? 138  HIS A O   1 
ATOM   1116 C  CB  . HIS A 1 138 ? 8.311   -14.818 28.990  1.00 38.88  ? 138  HIS A CB  1 
ATOM   1117 C  CG  . HIS A 1 138 ? 7.900   -16.232 29.219  1.00 42.33  ? 138  HIS A CG  1 
ATOM   1118 N  ND1 . HIS A 1 138 ? 8.676   -17.124 29.927  1.00 46.45  ? 138  HIS A ND1 1 
ATOM   1119 C  CD2 . HIS A 1 138 ? 6.789   -16.908 28.851  1.00 40.64  ? 138  HIS A CD2 1 
ATOM   1120 C  CE1 . HIS A 1 138 ? 8.066   -18.293 29.973  1.00 47.46  ? 138  HIS A CE1 1 
ATOM   1121 N  NE2 . HIS A 1 138 ? 6.917   -18.189 29.329  1.00 45.23  ? 138  HIS A NE2 1 
ATOM   1122 N  N   . ILE A 1 139 ? 5.752   -13.449 28.567  1.00 35.34  ? 139  ILE A N   1 
ATOM   1123 C  CA  . ILE A 1 139 ? 4.352   -13.375 28.164  1.00 35.76  ? 139  ILE A CA  1 
ATOM   1124 C  C   . ILE A 1 139 ? 4.039   -14.561 27.270  1.00 37.57  ? 139  ILE A C   1 
ATOM   1125 O  O   . ILE A 1 139 ? 4.778   -14.843 26.316  1.00 38.49  ? 139  ILE A O   1 
ATOM   1126 C  CB  . ILE A 1 139 ? 4.072   -12.058 27.429  1.00 34.07  ? 139  ILE A CB  1 
ATOM   1127 C  CG1 . ILE A 1 139 ? 4.203   -10.896 28.406  1.00 35.63  ? 139  ILE A CG1 1 
ATOM   1128 C  CG2 . ILE A 1 139 ? 2.707   -12.098 26.729  1.00 36.09  ? 139  ILE A CG2 1 
ATOM   1129 C  CD1 . ILE A 1 139 ? 4.549   -9.598  27.744  1.00 35.70  ? 139  ILE A CD1 1 
ATOM   1130 N  N   . GLU A 1 140 ? 2.940   -15.255 27.572  1.00 33.26  ? 140  GLU A N   1 
ATOM   1131 C  CA  . GLU A 1 140 ? 2.397   -16.296 26.705  1.00 31.01  ? 140  GLU A CA  1 
ATOM   1132 C  C   . GLU A 1 140 ? 1.404   -15.613 25.771  1.00 35.70  ? 140  GLU A C   1 
ATOM   1133 O  O   . GLU A 1 140 ? 0.267   -15.334 26.158  1.00 33.95  ? 140  GLU A O   1 
ATOM   1134 C  CB  . GLU A 1 140 ? 1.734   -17.385 27.540  1.00 35.16  ? 140  GLU A CB  1 
ATOM   1135 C  CG  . GLU A 1 140 ? 2.711   -18.161 28.426  1.00 40.73  ? 140  GLU A CG  1 
ATOM   1136 C  CD  . GLU A 1 140 ? 2.004   -19.197 29.275  1.00 50.07  ? 140  GLU A CD  1 
ATOM   1137 O  OE1 . GLU A 1 140 ? 0.805   -19.001 29.568  1.00 48.03  ? 140  GLU A OE1 1 
ATOM   1138 O  OE2 . GLU A 1 140 ? 2.644   -20.200 29.655  1.00 52.00  ? 140  GLU A OE2 1 
ATOM   1139 N  N   . VAL A 1 141 ? 1.830   -15.332 24.544  1.00 36.12  ? 141  VAL A N   1 
ATOM   1140 C  CA  . VAL A 1 141 ? 1.149   -14.345 23.702  1.00 32.14  ? 141  VAL A CA  1 
ATOM   1141 C  C   . VAL A 1 141 ? -0.251  -14.797 23.281  1.00 32.70  ? 141  VAL A C   1 
ATOM   1142 O  O   . VAL A 1 141 ? -1.223  -14.071 23.548  1.00 34.64  ? 141  VAL A O   1 
ATOM   1143 C  CB  . VAL A 1 141 ? 1.997   -14.002 22.466  1.00 35.67  ? 141  VAL A CB  1 
ATOM   1144 C  CG1 . VAL A 1 141 ? 1.207   -13.093 21.534  1.00 33.95  ? 141  VAL A CG1 1 
ATOM   1145 C  CG2 . VAL A 1 141 ? 3.288   -13.327 22.897  1.00 34.41  ? 141  VAL A CG2 1 
ATOM   1146 N  N   . PRO A 1 142 ? -0.420  -15.928 22.582  1.00 35.54  ? 142  PRO A N   1 
ATOM   1147 C  CA  . PRO A 1 142 ? -1.786  -16.305 22.186  1.00 33.32  ? 142  PRO A CA  1 
ATOM   1148 C  C   . PRO A 1 142 ? -2.687  -16.498 23.382  1.00 35.10  ? 142  PRO A C   1 
ATOM   1149 O  O   . PRO A 1 142 ? -3.887  -16.182 23.325  1.00 32.03  ? 142  PRO A O   1 
ATOM   1150 C  CB  . PRO A 1 142 ? -1.587  -17.602 21.384  1.00 35.01  ? 142  PRO A CB  1 
ATOM   1151 C  CG  . PRO A 1 142 ? -0.206  -18.086 21.758  1.00 37.14  ? 142  PRO A CG  1 
ATOM   1152 C  CD  . PRO A 1 142 ? 0.576   -16.837 21.993  1.00 35.25  ? 142  PRO A CD  1 
ATOM   1153 N  N   . GLU A 1 143 ? -2.129  -16.965 24.491  1.00 33.75  ? 143  GLU A N   1 
ATOM   1154 C  CA  . GLU A 1 143 ? -2.938  -17.138 25.687  1.00 32.91  ? 143  GLU A CA  1 
ATOM   1155 C  C   . GLU A 1 143 ? -3.470  -15.798 26.176  1.00 35.50  ? 143  GLU A C   1 
ATOM   1156 O  O   . GLU A 1 143 ? -4.669  -15.648 26.445  1.00 31.44  ? 143  GLU A O   1 
ATOM   1157 C  CB  . GLU A 1 143 ? -2.104  -17.832 26.760  1.00 32.49  ? 143  GLU A CB  1 
ATOM   1158 C  CG  . GLU A 1 143 ? -1.835  -19.316 26.467  1.00 36.43  ? 143  GLU A CG  1 
ATOM   1159 C  CD  . GLU A 1 143 ? -0.715  -19.587 25.450  1.00 39.45  ? 143  GLU A CD  1 
ATOM   1160 O  OE1 . GLU A 1 143 ? 0.009   -18.661 25.011  1.00 34.55  ? 143  GLU A OE1 1 
ATOM   1161 O  OE2 . GLU A 1 143 ? -0.567  -20.765 25.080  1.00 43.56  ? 143  GLU A OE2 1 
ATOM   1162 N  N   . ASP A 1 144 ? -2.595  -14.800 26.288  1.00 30.32  ? 144  ASP A N   1 
ATOM   1163 C  CA  . ASP A 1 144 ? -3.056  -13.500 26.739  1.00 30.24  ? 144  ASP A CA  1 
ATOM   1164 C  C   . ASP A 1 144 ? -3.923  -12.802 25.692  1.00 31.88  ? 144  ASP A C   1 
ATOM   1165 O  O   . ASP A 1 144 ? -4.830  -12.035 26.057  1.00 31.65  ? 144  ASP A O   1 
ATOM   1166 C  CB  . ASP A 1 144 ? -1.865  -12.616 27.123  1.00 32.79  ? 144  ASP A CB  1 
ATOM   1167 C  CG  . ASP A 1 144 ? -1.433  -12.822 28.566  1.00 38.58  ? 144  ASP A CG  1 
ATOM   1168 O  OD1 . ASP A 1 144 ? -2.219  -13.427 29.329  1.00 32.86  ? 144  ASP A OD1 1 
ATOM   1169 O  OD2 . ASP A 1 144 ? -0.318  -12.382 28.938  1.00 34.82  ? 144  ASP A OD2 1 
ATOM   1170 N  N   . MET A 1 145 ? -3.677  -13.017 24.396  1.00 32.60  ? 145  MET A N   1 
ATOM   1171 C  CA  . MET A 1 145 ? -4.579  -12.333 23.473  1.00 31.39  ? 145  MET A CA  1 
ATOM   1172 C  C   . MET A 1 145 ? -5.952  -12.979 23.454  1.00 30.00  ? 145  MET A C   1 
ATOM   1173 O  O   . MET A 1 145 ? -6.943  -12.290 23.209  1.00 32.37  ? 145  MET A O   1 
ATOM   1174 C  CB  . MET A 1 145 ? -3.997  -12.216 22.059  1.00 32.75  ? 145  MET A CB  1 
ATOM   1175 C  CG  . MET A 1 145 ? -2.566  -11.761 22.178  1.00 33.87  ? 145  MET A CG  1 
ATOM   1176 S  SD  . MET A 1 145 ? -2.657  -9.983  22.196  1.00 35.05  ? 145  MET A SD  1 
ATOM   1177 C  CE  . MET A 1 145 ? -2.168  -9.749  23.927  1.00 37.99  ? 145  MET A CE  1 
ATOM   1178 N  N   . THR A 1 146 ? -6.039  -14.272 23.754  1.00 30.19  ? 146  THR A N   1 
ATOM   1179 C  CA  . THR A 1 146 ? -7.350  -14.893 23.925  1.00 30.24  ? 146  THR A CA  1 
ATOM   1180 C  C   . THR A 1 146 ? -8.058  -14.373 25.165  1.00 32.23  ? 146  THR A C   1 
ATOM   1181 O  O   . THR A 1 146 ? -9.267  -14.103 25.125  1.00 30.44  ? 146  THR A O   1 
ATOM   1182 C  CB  . THR A 1 146 ? -7.203  -16.415 23.979  1.00 33.17  ? 146  THR A CB  1 
ATOM   1183 O  OG1 . THR A 1 146 ? -6.725  -16.865 22.706  1.00 39.73  ? 146  THR A OG1 1 
ATOM   1184 C  CG2 . THR A 1 146 ? -8.546  -17.095 24.301  1.00 34.00  ? 146  THR A CG2 1 
ATOM   1185 N  N   . ARG A 1 147 ? -7.337  -14.234 26.287  1.00 30.37  ? 147  ARG A N   1 
ATOM   1186 C  CA  . ARG A 1 147 ? -7.924  -13.578 27.451  1.00 29.92  ? 147  ARG A CA  1 
ATOM   1187 C  C   . ARG A 1 147 ? -8.509  -12.233 27.074  1.00 31.71  ? 147  ARG A C   1 
ATOM   1188 O  O   . ARG A 1 147 ? -9.655  -11.922 27.412  1.00 32.18  ? 147  ARG A O   1 
ATOM   1189 C  CB  . ARG A 1 147 ? -6.876  -13.387 28.551  1.00 31.73  ? 147  ARG A CB  1 
ATOM   1190 C  CG  . ARG A 1 147 ? -6.423  -14.665 29.200  1.00 33.10  ? 147  ARG A CG  1 
ATOM   1191 C  CD  . ARG A 1 147 ? -5.490  -14.327 30.361  1.00 34.79  ? 147  ARG A CD  1 
ATOM   1192 N  NE  . ARG A 1 147 ? -5.200  -15.504 31.166  1.00 34.24  ? 147  ARG A NE  1 
ATOM   1193 C  CZ  . ARG A 1 147 ? -4.173  -16.318 30.977  1.00 39.56  ? 147  ARG A CZ  1 
ATOM   1194 N  NH1 . ARG A 1 147 ? -3.282  -16.106 30.013  1.00 34.36  ? 147  ARG A NH1 1 
ATOM   1195 N  NH2 . ARG A 1 147 ? -4.033  -17.372 31.778  1.00 41.78  ? 147  ARG A NH2 1 
ATOM   1196 N  N   . LEU A 1 148 ? -7.733  -11.427 26.344  1.00 28.87  ? 148  LEU A N   1 
ATOM   1197 C  CA  . LEU A 1 148 ? -8.176  -10.083 26.000  1.00 31.57  ? 148  LEU A CA  1 
ATOM   1198 C  C   . LEU A 1 148 ? -9.391  -10.111 25.080  1.00 31.36  ? 148  LEU A C   1 
ATOM   1199 O  O   . LEU A 1 148 ? -10.391 -9.426  25.341  1.00 32.75  ? 148  LEU A O   1 
ATOM   1200 C  CB  . LEU A 1 148 ? -7.030  -9.298  25.356  1.00 33.16  ? 148  LEU A CB  1 
ATOM   1201 C  CG  . LEU A 1 148 ? -7.581  -7.965  24.828  1.00 30.76  ? 148  LEU A CG  1 
ATOM   1202 C  CD1 . LEU A 1 148 ? -7.034  -6.799  25.605  1.00 34.01  ? 148  LEU A CD1 1 
ATOM   1203 C  CD2 . LEU A 1 148 ? -7.318  -7.819  23.339  1.00 37.98  ? 148  LEU A CD2 1 
ATOM   1204 N  N   . THR A 1 149 ? -9.320  -10.867 23.986  1.00 30.17  ? 149  THR A N   1 
ATOM   1205 C  CA  . THR A 1 149 ? -10.406 -10.776 23.001  1.00 27.15  ? 149  THR A CA  1 
ATOM   1206 C  C   . THR A 1 149 ? -11.694 -11.407 23.519  1.00 29.89  ? 149  THR A C   1 
ATOM   1207 O  O   . THR A 1 149 ? -12.787 -10.895 23.249  1.00 30.75  ? 149  THR A O   1 
ATOM   1208 C  CB  . THR A 1 149 ? -10.015 -11.402 21.668  1.00 29.22  ? 149  THR A CB  1 
ATOM   1209 O  OG1 . THR A 1 149 ? -9.718  -12.791 21.842  1.00 29.34  ? 149  THR A OG1 1 
ATOM   1210 C  CG2 . THR A 1 149 ? -8.824  -10.638 21.026  1.00 28.13  ? 149  THR A CG2 1 
ATOM   1211 N  N   . LEU A 1 150 ? -11.597 -12.521 24.243  1.00 30.99  ? 150  LEU A N   1 
ATOM   1212 C  CA  . LEU A 1 150 ? -12.796 -13.095 24.852  1.00 30.64  ? 150  LEU A CA  1 
ATOM   1213 C  C   . LEU A 1 150 ? -13.433 -12.104 25.817  1.00 32.00  ? 150  LEU A C   1 
ATOM   1214 O  O   . LEU A 1 150 ? -14.656 -11.909 25.816  1.00 30.52  ? 150  LEU A O   1 
ATOM   1215 C  CB  . LEU A 1 150 ? -12.452 -14.407 25.578  1.00 32.35  ? 150  LEU A CB  1 
ATOM   1216 C  CG  . LEU A 1 150 ? -13.665 -15.011 26.291  1.00 33.41  ? 150  LEU A CG  1 
ATOM   1217 C  CD1 . LEU A 1 150 ? -14.615 -15.636 25.240  1.00 30.93  ? 150  LEU A CD1 1 
ATOM   1218 C  CD2 . LEU A 1 150 ? -13.243 -16.040 27.354  1.00 33.28  ? 150  LEU A CD2 1 
ATOM   1219 N  N   . ASP A 1 151 ? -12.622 -11.464 26.663  1.00 29.39  ? 151  ASP A N   1 
ATOM   1220 C  CA  . ASP A 1 151 ? -13.214 -10.558 27.632  1.00 30.37  ? 151  ASP A CA  1 
ATOM   1221 C  C   . ASP A 1 151 ? -13.840 -9.360  26.943  1.00 28.75  ? 151  ASP A C   1 
ATOM   1222 O  O   . ASP A 1 151 ? -14.865 -8.841  27.405  1.00 31.80  ? 151  ASP A O   1 
ATOM   1223 C  CB  . ASP A 1 151 ? -12.168 -10.126 28.662  1.00 32.29  ? 151  ASP A CB  1 
ATOM   1224 C  CG  . ASP A 1 151 ? -12.003 -11.158 29.787  1.00 29.57  ? 151  ASP A CG  1 
ATOM   1225 O  OD1 . ASP A 1 151 ? -12.216 -12.361 29.537  1.00 35.42  ? 151  ASP A OD1 1 
ATOM   1226 O  OD2 . ASP A 1 151 ? -11.654 -10.774 30.909  1.00 34.22  ? 151  ASP A OD2 1 
ATOM   1227 N  N   . THR A 1 152 ? -13.244 -8.915  25.843  1.00 29.06  ? 152  THR A N   1 
ATOM   1228 C  CA  . THR A 1 152 ? -13.764 -7.760  25.132  1.00 30.18  ? 152  THR A CA  1 
ATOM   1229 C  C   . THR A 1 152 ? -15.122 -8.066  24.499  1.00 32.07  ? 152  THR A C   1 
ATOM   1230 O  O   . THR A 1 152 ? -16.058 -7.274  24.627  1.00 32.14  ? 152  THR A O   1 
ATOM   1231 C  CB  . THR A 1 152 ? -12.738 -7.293  24.094  1.00 30.44  ? 152  THR A CB  1 
ATOM   1232 O  OG1 . THR A 1 152 ? -11.559 -6.873  24.797  1.00 30.84  ? 152  THR A OG1 1 
ATOM   1233 C  CG2 . THR A 1 152 ? -13.262 -6.094  23.302  1.00 32.38  ? 152  THR A CG2 1 
ATOM   1234 N  N   . ILE A 1 153 ? -15.273 -9.222  23.847  1.00 29.63  ? 153  ILE A N   1 
ATOM   1235 C  CA  . ILE A 1 153 ? -16.589 -9.471  23.258  1.00 30.19  ? 153  ILE A CA  1 
ATOM   1236 C  C   . ILE A 1 153 ? -17.608 -9.742  24.357  1.00 28.94  ? 153  ILE A C   1 
ATOM   1237 O  O   . ILE A 1 153 ? -18.772 -9.326  24.247  1.00 29.93  ? 153  ILE A O   1 
ATOM   1238 C  CB  . ILE A 1 153 ? -16.552 -10.600 22.203  1.00 29.95  ? 153  ILE A CB  1 
ATOM   1239 C  CG1 . ILE A 1 153 ? -17.904 -10.681 21.455  1.00 30.90  ? 153  ILE A CG1 1 
ATOM   1240 C  CG2 . ILE A 1 153 ? -16.195 -11.951 22.814  1.00 31.31  ? 153  ILE A CG2 1 
ATOM   1241 C  CD1 . ILE A 1 153 ? -18.208 -9.433  20.612  1.00 33.76  ? 153  ILE A CD1 1 
ATOM   1242 N  N   . GLY A 1 154 ? -17.195 -10.381 25.457  1.00 28.36  ? 154  GLY A N   1 
ATOM   1243 C  CA  . GLY A 1 154 ? -18.137 -10.601 26.554  1.00 31.96  ? 154  GLY A CA  1 
ATOM   1244 C  C   . GLY A 1 154 ? -18.655 -9.293  27.130  1.00 33.66  ? 154  GLY A C   1 
ATOM   1245 O  O   . GLY A 1 154 ? -19.863 -9.109  27.321  1.00 33.21  ? 154  GLY A O   1 
ATOM   1246 N  N   . LEU A 1 155 ? -17.744 -8.367  27.421  1.00 31.81  ? 155  LEU A N   1 
ATOM   1247 C  CA  . LEU A 1 155 ? -18.134 -7.116  28.075  1.00 31.84  ? 155  LEU A CA  1 
ATOM   1248 C  C   . LEU A 1 155 ? -18.854 -6.183  27.105  1.00 32.35  ? 155  LEU A C   1 
ATOM   1249 O  O   . LEU A 1 155 ? -19.971 -5.729  27.385  1.00 32.91  ? 155  LEU A O   1 
ATOM   1250 C  CB  . LEU A 1 155 ? -16.897 -6.438  28.672  1.00 31.68  ? 155  LEU A CB  1 
ATOM   1251 C  CG  . LEU A 1 155 ? -17.135 -5.173  29.491  1.00 31.88  ? 155  LEU A CG  1 
ATOM   1252 C  CD1 . LEU A 1 155 ? -18.060 -5.471  30.668  1.00 34.23  ? 155  LEU A CD1 1 
ATOM   1253 C  CD2 . LEU A 1 155 ? -15.792 -4.608  29.982  1.00 32.95  ? 155  LEU A CD2 1 
ATOM   1254 N  N   . CYS A 1 156 ? -18.243 -5.905  25.945  1.00 32.15  ? 156  CYS A N   1 
ATOM   1255 C  CA  . CYS A 1 156 ? -18.851 -4.997  24.976  1.00 32.39  ? 156  CYS A CA  1 
ATOM   1256 C  C   . CYS A 1 156 ? -20.158 -5.552  24.431  1.00 33.56  ? 156  CYS A C   1 
ATOM   1257 O  O   . CYS A 1 156 ? -21.123 -4.803  24.238  1.00 34.42  ? 156  CYS A O   1 
ATOM   1258 C  CB  . CYS A 1 156 ? -17.893 -4.730  23.817  1.00 32.88  ? 156  CYS A CB  1 
ATOM   1259 S  SG  . CYS A 1 156 ? -16.326 -3.942  24.296  1.00 36.21  ? 156  CYS A SG  1 
ATOM   1260 N  N   . GLY A 1 157 ? -20.187 -6.847  24.111  1.00 33.34  ? 157  GLY A N   1 
ATOM   1261 C  CA  . GLY A 1 157 ? -21.360 -7.418  23.465  1.00 32.64  ? 157  GLY A CA  1 
ATOM   1262 C  C   . GLY A 1 157 ? -22.478 -7.767  24.422  1.00 35.17  ? 157  GLY A C   1 
ATOM   1263 O  O   . GLY A 1 157 ? -23.653 -7.617  24.077  1.00 32.56  ? 157  GLY A O   1 
ATOM   1264 N  N   . PHE A 1 158 ? -22.146 -8.210  25.641  1.00 30.32  ? 158  PHE A N   1 
ATOM   1265 C  CA  . PHE A 1 158 ? -23.137 -8.844  26.508  1.00 29.98  ? 158  PHE A CA  1 
ATOM   1266 C  C   . PHE A 1 158 ? -23.106 -8.343  27.944  1.00 33.45  ? 158  PHE A C   1 
ATOM   1267 O  O   . PHE A 1 158 ? -23.846 -8.875  28.788  1.00 35.90  ? 158  PHE A O   1 
ATOM   1268 C  CB  . PHE A 1 158 ? -22.950 -10.373 26.474  1.00 32.45  ? 158  PHE A CB  1 
ATOM   1269 C  CG  . PHE A 1 158 ? -22.971 -10.925 25.073  1.00 34.15  ? 158  PHE A CG  1 
ATOM   1270 C  CD1 . PHE A 1 158 ? -24.176 -11.240 24.466  1.00 30.69  ? 158  PHE A CD1 1 
ATOM   1271 C  CD2 . PHE A 1 158 ? -21.807 -11.041 24.337  1.00 33.68  ? 158  PHE A CD2 1 
ATOM   1272 C  CE1 . PHE A 1 158 ? -24.227 -11.699 23.172  1.00 30.01  ? 158  PHE A CE1 1 
ATOM   1273 C  CE2 . PHE A 1 158 ? -21.844 -11.500 23.013  1.00 30.61  ? 158  PHE A CE2 1 
ATOM   1274 C  CZ  . PHE A 1 158 ? -23.059 -11.833 22.433  1.00 32.80  ? 158  PHE A CZ  1 
ATOM   1275 N  N   . ASN A 1 159 ? -22.290 -7.332  28.238  1.00 32.45  ? 159  ASN A N   1 
ATOM   1276 C  CA  . ASN A 1 159 ? -22.104 -6.841  29.600  1.00 35.03  ? 159  ASN A CA  1 
ATOM   1277 C  C   . ASN A 1 159 ? -21.827 -7.979  30.576  1.00 38.08  ? 159  ASN A C   1 
ATOM   1278 O  O   . ASN A 1 159 ? -22.351 -8.010  31.695  1.00 33.52  ? 159  ASN A O   1 
ATOM   1279 C  CB  . ASN A 1 159 ? -23.311 -6.013  30.058  1.00 38.15  ? 159  ASN A CB  1 
ATOM   1280 C  CG  . ASN A 1 159 ? -22.953 -5.074  31.177  1.00 46.32  ? 159  ASN A CG  1 
ATOM   1281 O  OD1 . ASN A 1 159 ? -21.778 -4.748  31.364  1.00 39.28  ? 159  ASN A OD1 1 
ATOM   1282 N  ND2 . ASN A 1 159 ? -23.947 -4.662  31.954  1.00 48.76  ? 159  ASN A ND2 1 
ATOM   1283 N  N   . TYR A 1 160 ? -20.973 -8.919  30.163  1.00 33.50  ? 160  TYR A N   1 
ATOM   1284 C  CA  . TYR A 1 160 ? -20.616 -10.060 30.993  1.00 33.78  ? 160  TYR A CA  1 
ATOM   1285 C  C   . TYR A 1 160 ? -19.100 -10.116 31.113  1.00 34.88  ? 160  TYR A C   1 
ATOM   1286 O  O   . TYR A 1 160 ? -18.383 -9.930  30.120  1.00 33.03  ? 160  TYR A O   1 
ATOM   1287 C  CB  . TYR A 1 160 ? -21.146 -11.368 30.404  1.00 34.44  ? 160  TYR A CB  1 
ATOM   1288 C  CG  . TYR A 1 160 ? -20.892 -12.582 31.253  1.00 34.88  ? 160  TYR A CG  1 
ATOM   1289 C  CD1 . TYR A 1 160 ? -21.725 -12.882 32.313  1.00 36.94  ? 160  TYR A CD1 1 
ATOM   1290 C  CD2 . TYR A 1 160 ? -19.822 -13.443 30.986  1.00 34.93  ? 160  TYR A CD2 1 
ATOM   1291 C  CE1 . TYR A 1 160 ? -21.521 -13.989 33.091  1.00 40.58  ? 160  TYR A CE1 1 
ATOM   1292 C  CE2 . TYR A 1 160 ? -19.602 -14.568 31.775  1.00 38.60  ? 160  TYR A CE2 1 
ATOM   1293 C  CZ  . TYR A 1 160 ? -20.466 -14.825 32.832  1.00 40.58  ? 160  TYR A CZ  1 
ATOM   1294 O  OH  . TYR A 1 160 ? -20.290 -15.923 33.635  1.00 42.93  ? 160  TYR A OH  1 
ATOM   1295 N  N   . ARG A 1 161 ? -18.610 -10.362 32.329  1.00 32.46  ? 161  ARG A N   1 
ATOM   1296 C  CA  . ARG A 1 161 ? -17.173 -10.350 32.599  1.00 34.31  ? 161  ARG A CA  1 
ATOM   1297 C  C   . ARG A 1 161 ? -16.684 -11.788 32.721  1.00 31.51  ? 161  ARG A C   1 
ATOM   1298 O  O   . ARG A 1 161 ? -16.981 -12.473 33.701  1.00 33.30  ? 161  ARG A O   1 
ATOM   1299 C  CB  . ARG A 1 161 ? -16.869 -9.530  33.849  1.00 35.59  ? 161  ARG A CB  1 
ATOM   1300 C  CG  . ARG A 1 161 ? -16.988 -8.023  33.565  1.00 31.82  ? 161  ARG A CG  1 
ATOM   1301 C  CD  . ARG A 1 161 ? -16.454 -7.147  34.664  1.00 35.26  ? 161  ARG A CD  1 
ATOM   1302 N  NE  . ARG A 1 161 ? -16.619 -5.738  34.316  1.00 33.40  ? 161  ARG A NE  1 
ATOM   1303 C  CZ  . ARG A 1 161 ? -15.666 -4.969  33.814  1.00 35.35  ? 161  ARG A CZ  1 
ATOM   1304 N  NH1 . ARG A 1 161 ? -14.448 -5.440  33.587  1.00 32.79  ? 161  ARG A NH1 1 
ATOM   1305 N  NH2 . ARG A 1 161 ? -15.933 -3.689  33.558  1.00 34.05  ? 161  ARG A NH2 1 
ATOM   1306 N  N   . PHE A 1 162 ? -15.973 -12.261 31.692  1.00 30.99  ? 162  PHE A N   1 
ATOM   1307 C  CA  . PHE A 1 162 ? -15.320 -13.559 31.776  1.00 31.16  ? 162  PHE A CA  1 
ATOM   1308 C  C   . PHE A 1 162 ? -14.161 -13.536 32.769  1.00 33.22  ? 162  PHE A C   1 
ATOM   1309 O  O   . PHE A 1 162 ? -13.768 -14.591 33.283  1.00 34.11  ? 162  PHE A O   1 
ATOM   1310 C  CB  . PHE A 1 162 ? -14.805 -13.971 30.391  1.00 32.32  ? 162  PHE A CB  1 
ATOM   1311 C  CG  . PHE A 1 162 ? -15.888 -14.461 29.450  1.00 33.80  ? 162  PHE A CG  1 
ATOM   1312 C  CD1 . PHE A 1 162 ? -16.374 -15.755 29.540  1.00 38.36  ? 162  PHE A CD1 1 
ATOM   1313 C  CD2 . PHE A 1 162 ? -16.388 -13.625 28.463  1.00 33.71  ? 162  PHE A CD2 1 
ATOM   1314 C  CE1 . PHE A 1 162 ? -17.365 -16.203 28.661  1.00 38.17  ? 162  PHE A CE1 1 
ATOM   1315 C  CE2 . PHE A 1 162 ? -17.380 -14.062 27.583  1.00 32.87  ? 162  PHE A CE2 1 
ATOM   1316 C  CZ  . PHE A 1 162 ? -17.865 -15.363 27.693  1.00 36.52  ? 162  PHE A CZ  1 
ATOM   1317 N  N   . ASN A 1 163 ? -13.617 -12.353 33.044  1.00 31.33  ? 163  ASN A N   1 
ATOM   1318 C  CA  . ASN A 1 163 ? -12.564 -12.188 34.045  1.00 31.44  ? 163  ASN A CA  1 
ATOM   1319 C  C   . ASN A 1 163 ? -11.376 -13.095 33.747  1.00 31.32  ? 163  ASN A C   1 
ATOM   1320 O  O   . ASN A 1 163 ? -10.777 -13.706 34.639  1.00 32.11  ? 163  ASN A O   1 
ATOM   1321 C  CB  . ASN A 1 163 ? -13.128 -12.392 35.448  1.00 33.08  ? 163  ASN A CB  1 
ATOM   1322 C  CG  . ASN A 1 163 ? -13.910 -11.173 35.904  1.00 31.73  ? 163  ASN A CG  1 
ATOM   1323 O  OD1 . ASN A 1 163 ? -13.439 -10.047 35.733  1.00 33.18  ? 163  ASN A OD1 1 
ATOM   1324 N  ND2 . ASN A 1 163 ? -15.128 -11.376 36.439  1.00 30.01  ? 163  ASN A ND2 1 
ATOM   1325 N  N   . SER A 1 164 ? -10.996 -13.124 32.464  1.00 31.85  ? 164  SER A N   1 
ATOM   1326 C  CA  . SER A 1 164 ? -9.961  -14.041 32.021  1.00 33.21  ? 164  SER A CA  1 
ATOM   1327 C  C   . SER A 1 164 ? -8.617  -13.722 32.646  1.00 33.18  ? 164  SER A C   1 
ATOM   1328 O  O   . SER A 1 164 ? -7.797  -14.629 32.813  1.00 31.15  ? 164  SER A O   1 
ATOM   1329 C  CB  . SER A 1 164 ? -9.847  -14.014 30.498  1.00 32.78  ? 164  SER A CB  1 
ATOM   1330 O  OG  . SER A 1 164 ? -11.042 -14.514 29.898  1.00 30.91  ? 164  SER A OG  1 
ATOM   1331 N  N   . PHE A 1 165 ? -8.360  -12.455 32.968  1.00 32.01  ? 165  PHE A N   1 
ATOM   1332 C  CA  . PHE A 1 165 ? -7.077  -12.111 33.571  1.00 34.27  ? 165  PHE A CA  1 
ATOM   1333 C  C   . PHE A 1 165 ? -7.024  -12.452 35.050  1.00 35.15  ? 165  PHE A C   1 
ATOM   1334 O  O   . PHE A 1 165 ? -5.976  -12.258 35.680  1.00 34.86  ? 165  PHE A O   1 
ATOM   1335 C  CB  . PHE A 1 165 ? -6.764  -10.627 33.356  1.00 31.60  ? 165  PHE A CB  1 
ATOM   1336 C  CG  . PHE A 1 165 ? -6.454  -10.290 31.919  1.00 32.63  ? 165  PHE A CG  1 
ATOM   1337 C  CD1 . PHE A 1 165 ? -5.277  -10.744 31.327  1.00 32.30  ? 165  PHE A CD1 1 
ATOM   1338 C  CD2 . PHE A 1 165 ? -7.361  -9.588  31.141  1.00 33.83  ? 165  PHE A CD2 1 
ATOM   1339 C  CE1 . PHE A 1 165 ? -4.993  -10.461 29.995  1.00 33.81  ? 165  PHE A CE1 1 
ATOM   1340 C  CE2 . PHE A 1 165 ? -7.078  -9.307  29.791  1.00 34.01  ? 165  PHE A CE2 1 
ATOM   1341 C  CZ  . PHE A 1 165 ? -5.895  -9.747  29.230  1.00 33.51  ? 165  PHE A CZ  1 
ATOM   1342 N  N   . TYR A 1 166 ? -8.123  -12.944 35.618  1.00 33.08  ? 166  TYR A N   1 
ATOM   1343 C  CA  . TYR A 1 166 ? -8.122  -13.485 36.971  1.00 35.81  ? 166  TYR A CA  1 
ATOM   1344 C  C   . TYR A 1 166 ? -7.945  -14.994 36.973  1.00 35.72  ? 166  TYR A C   1 
ATOM   1345 O  O   . TYR A 1 166 ? -8.111  -15.630 38.015  1.00 38.33  ? 166  TYR A O   1 
ATOM   1346 C  CB  . TYR A 1 166 ? -9.413  -13.080 37.700  1.00 30.81  ? 166  TYR A CB  1 
ATOM   1347 C  CG  . TYR A 1 166 ? -9.490  -11.588 37.905  1.00 34.77  ? 166  TYR A CG  1 
ATOM   1348 C  CD1 . TYR A 1 166 ? -9.984  -10.748 36.903  1.00 30.72  ? 166  TYR A CD1 1 
ATOM   1349 C  CD2 . TYR A 1 166 ? -9.006  -11.009 39.076  1.00 31.95  ? 166  TYR A CD2 1 
ATOM   1350 C  CE1 . TYR A 1 166 ? -10.032 -9.368  37.087  1.00 30.59  ? 166  TYR A CE1 1 
ATOM   1351 C  CE2 . TYR A 1 166 ? -9.025  -9.634  39.259  1.00 31.37  ? 166  TYR A CE2 1 
ATOM   1352 C  CZ  . TYR A 1 166 ? -9.547  -8.821  38.264  1.00 29.50  ? 166  TYR A CZ  1 
ATOM   1353 O  OH  . TYR A 1 166 ? -9.572  -7.476  38.441  1.00 31.99  ? 166  TYR A OH  1 
ATOM   1354 N  N   . ARG A 1 167 ? -7.572  -15.576 35.831  1.00 35.65  ? 167  ARG A N   1 
ATOM   1355 C  CA  . ARG A 1 167 ? -7.472  -17.015 35.678  1.00 37.44  ? 167  ARG A CA  1 
ATOM   1356 C  C   . ARG A 1 167 ? -6.097  -17.359 35.128  1.00 40.40  ? 167  ARG A C   1 
ATOM   1357 O  O   . ARG A 1 167 ? -5.626  -16.725 34.179  1.00 40.99  ? 167  ARG A O   1 
ATOM   1358 C  CB  . ARG A 1 167 ? -8.532  -17.552 34.719  1.00 36.31  ? 167  ARG A CB  1 
ATOM   1359 C  CG  . ARG A 1 167 ? -9.960  -17.479 35.235  1.00 39.76  ? 167  ARG A CG  1 
ATOM   1360 C  CD  . ARG A 1 167 ? -10.918 -17.585 34.055  1.00 41.42  ? 167  ARG A CD  1 
ATOM   1361 N  NE  . ARG A 1 167 ? -12.248 -17.080 34.370  1.00 46.91  ? 167  ARG A NE  1 
ATOM   1362 C  CZ  . ARG A 1 167 ? -13.170 -17.756 35.042  1.00 47.34  ? 167  ARG A CZ  1 
ATOM   1363 N  NH1 . ARG A 1 167 ? -12.991 -19.028 35.375  1.00 47.78  ? 167  ARG A NH1 1 
ATOM   1364 N  NH2 . ARG A 1 167 ? -14.307 -17.145 35.369  1.00 50.26  ? 167  ARG A NH2 1 
ATOM   1365 N  N   . ASP A 1 168 ? -5.470  -18.378 35.705  1.00 41.59  ? 168  ASP A N   1 
ATOM   1366 C  CA  . ASP A 1 168 ? -4.237  -18.894 35.130  1.00 42.73  ? 168  ASP A CA  1 
ATOM   1367 C  C   . ASP A 1 168 ? -4.500  -20.017 34.137  1.00 46.39  ? 168  ASP A C   1 
ATOM   1368 O  O   . ASP A 1 168 ? -3.630  -20.314 33.312  1.00 50.36  ? 168  ASP A O   1 
ATOM   1369 C  CB  . ASP A 1 168 ? -3.271  -19.330 36.252  1.00 45.69  ? 168  ASP A CB  1 
ATOM   1370 C  CG  . ASP A 1 168 ? -3.874  -20.367 37.194  1.00 53.17  ? 168  ASP A CG  1 
ATOM   1371 O  OD1 . ASP A 1 168 ? -4.682  -20.004 38.086  1.00 50.25  ? 168  ASP A OD1 1 
ATOM   1372 O  OD2 . ASP A 1 168 ? -3.532  -21.558 37.049  1.00 62.68  ? 168  ASP A OD2 1 
ATOM   1373 N  N   . GLN A 1 169 ? -5.696  -20.605 34.169  1.00 45.48  ? 169  GLN A N   1 
ATOM   1374 C  CA  . GLN A 1 169 ? -6.179  -21.572 33.202  1.00 50.40  ? 169  GLN A CA  1 
ATOM   1375 C  C   . GLN A 1 169 ? -7.294  -20.965 32.357  1.00 48.74  ? 169  GLN A C   1 
ATOM   1376 O  O   . GLN A 1 169 ? -7.964  -20.017 32.780  1.00 47.81  ? 169  GLN A O   1 
ATOM   1377 C  CB  . GLN A 1 169 ? -6.699  -22.825 33.916  1.00 54.08  ? 169  GLN A CB  1 
ATOM   1378 C  CG  . GLN A 1 169 ? -5.741  -23.366 34.973  1.00 58.99  ? 169  GLN A CG  1 
ATOM   1379 C  CD  . GLN A 1 169 ? -6.252  -24.638 35.620  1.00 69.57  ? 169  GLN A CD  1 
ATOM   1380 O  OE1 . GLN A 1 169 ? -6.951  -24.591 36.634  1.00 71.53  ? 169  GLN A OE1 1 
ATOM   1381 N  NE2 . GLN A 1 169 ? -5.927  -25.781 35.025  1.00 72.72  ? 169  GLN A NE2 1 
ATOM   1382 N  N   . PRO A 1 170 ? -7.533  -21.494 31.160  1.00 50.54  ? 170  PRO A N   1 
ATOM   1383 C  CA  . PRO A 1 170 ? -8.570  -20.915 30.298  1.00 49.01  ? 170  PRO A CA  1 
ATOM   1384 C  C   . PRO A 1 170 ? -9.945  -20.991 30.946  1.00 50.50  ? 170  PRO A C   1 
ATOM   1385 O  O   . PRO A 1 170 ? -10.256 -21.921 31.698  1.00 47.81  ? 170  PRO A O   1 
ATOM   1386 C  CB  . PRO A 1 170 ? -8.501  -21.780 29.030  1.00 50.41  ? 170  PRO A CB  1 
ATOM   1387 C  CG  . PRO A 1 170 ? -7.131  -22.370 29.050  1.00 50.95  ? 170  PRO A CG  1 
ATOM   1388 C  CD  . PRO A 1 170 ? -6.820  -22.601 30.500  1.00 48.38  ? 170  PRO A CD  1 
ATOM   1389 N  N   . HIS A 1 171 ? -10.772 -19.993 30.651  1.00 46.78  ? 171  HIS A N   1 
ATOM   1390 C  CA  . HIS A 1 171 ? -12.162 -20.068 31.060  1.00 47.28  ? 171  HIS A CA  1 
ATOM   1391 C  C   . HIS A 1 171 ? -12.760 -21.382 30.560  1.00 47.97  ? 171  HIS A C   1 
ATOM   1392 O  O   . HIS A 1 171 ? -12.436 -21.825 29.447  1.00 48.40  ? 171  HIS A O   1 
ATOM   1393 C  CB  . HIS A 1 171 ? -12.951 -18.873 30.511  1.00 42.74  ? 171  HIS A CB  1 
ATOM   1394 C  CG  . HIS A 1 171 ? -14.313 -18.718 31.113  1.00 45.62  ? 171  HIS A CG  1 
ATOM   1395 N  ND1 . HIS A 1 171 ? -15.371 -19.531 30.773  1.00 46.25  ? 171  HIS A ND1 1 
ATOM   1396 C  CD2 . HIS A 1 171 ? -14.788 -17.847 32.035  1.00 40.95  ? 171  HIS A CD2 1 
ATOM   1397 C  CE1 . HIS A 1 171 ? -16.440 -19.173 31.462  1.00 50.54  ? 171  HIS A CE1 1 
ATOM   1398 N  NE2 . HIS A 1 171 ? -16.113 -18.155 32.237  1.00 46.66  ? 171  HIS A NE2 1 
ATOM   1399 N  N   . PRO A 1 172 ? -13.611 -22.039 31.350  1.00 50.41  ? 172  PRO A N   1 
ATOM   1400 C  CA  . PRO A 1 172 ? -14.266 -23.269 30.868  1.00 48.16  ? 172  PRO A CA  1 
ATOM   1401 C  C   . PRO A 1 172 ? -14.873 -23.132 29.478  1.00 46.78  ? 172  PRO A C   1 
ATOM   1402 O  O   . PRO A 1 172 ? -14.877 -24.101 28.704  1.00 42.02  ? 172  PRO A O   1 
ATOM   1403 C  CB  . PRO A 1 172 ? -15.346 -23.519 31.928  1.00 52.65  ? 172  PRO A CB  1 
ATOM   1404 C  CG  . PRO A 1 172 ? -14.828 -22.855 33.159  1.00 53.46  ? 172  PRO A CG  1 
ATOM   1405 C  CD  . PRO A 1 172 ? -14.035 -21.667 32.712  1.00 49.56  ? 172  PRO A CD  1 
ATOM   1406 N  N   . PHE A 1 173 ? -15.410 -21.956 29.146  1.00 44.62  ? 173  PHE A N   1 
ATOM   1407 C  CA  . PHE A 1 173 ? -15.960 -21.762 27.809  1.00 41.83  ? 173  PHE A CA  1 
ATOM   1408 C  C   . PHE A 1 173 ? -14.890 -21.992 26.754  1.00 41.61  ? 173  PHE A C   1 
ATOM   1409 O  O   . PHE A 1 173 ? -15.142 -22.647 25.737  1.00 45.61  ? 173  PHE A O   1 
ATOM   1410 C  CB  . PHE A 1 173 ? -16.557 -20.358 27.669  1.00 44.10  ? 173  PHE A CB  1 
ATOM   1411 C  CG  . PHE A 1 173 ? -17.287 -20.131 26.360  1.00 41.22  ? 173  PHE A CG  1 
ATOM   1412 C  CD1 . PHE A 1 173 ? -18.631 -20.445 26.237  1.00 43.10  ? 173  PHE A CD1 1 
ATOM   1413 C  CD2 . PHE A 1 173 ? -16.622 -19.610 25.261  1.00 44.16  ? 173  PHE A CD2 1 
ATOM   1414 C  CE1 . PHE A 1 173 ? -19.302 -20.241 25.047  1.00 43.34  ? 173  PHE A CE1 1 
ATOM   1415 C  CE2 . PHE A 1 173 ? -17.289 -19.403 24.056  1.00 38.92  ? 173  PHE A CE2 1 
ATOM   1416 C  CZ  . PHE A 1 173 ? -18.624 -19.718 23.949  1.00 42.77  ? 173  PHE A CZ  1 
ATOM   1417 N  N   . ILE A 1 174 ? -13.687 -21.467 26.984  1.00 40.16  ? 174  ILE A N   1 
ATOM   1418 C  CA  . ILE A 1 174 ? -12.605 -21.637 26.022  1.00 42.23  ? 174  ILE A CA  1 
ATOM   1419 C  C   . ILE A 1 174 ? -12.209 -23.102 25.912  1.00 41.85  ? 174  ILE A C   1 
ATOM   1420 O  O   . ILE A 1 174 ? -11.954 -23.611 24.815  1.00 40.35  ? 174  ILE A O   1 
ATOM   1421 C  CB  . ILE A 1 174 ? -11.396 -20.772 26.411  1.00 40.43  ? 174  ILE A CB  1 
ATOM   1422 C  CG1 . ILE A 1 174 ? -11.705 -19.277 26.260  1.00 39.67  ? 174  ILE A CG1 1 
ATOM   1423 C  CG2 . ILE A 1 174 ? -10.183 -21.195 25.582  1.00 40.23  ? 174  ILE A CG2 1 
ATOM   1424 C  CD1 . ILE A 1 174 ? -12.142 -18.854 24.834  1.00 32.99  ? 174  ILE A CD1 1 
ATOM   1425 N  N   . THR A 1 175 ? -12.101 -23.791 27.047  1.00 42.31  ? 175  THR A N   1 
ATOM   1426 C  CA  . THR A 1 175 ? -11.700 -25.192 27.016  1.00 41.02  ? 175  THR A CA  1 
ATOM   1427 C  C   . THR A 1 175 ? -12.651 -26.007 26.155  1.00 41.72  ? 175  THR A C   1 
ATOM   1428 O  O   . THR A 1 175 ? -12.222 -26.778 25.289  1.00 40.11  ? 175  THR A O   1 
ATOM   1429 C  CB  . THR A 1 175 ? -11.666 -25.755 28.432  1.00 43.30  ? 175  THR A CB  1 
ATOM   1430 O  OG1 . THR A 1 175 ? -10.655 -25.076 29.181  1.00 46.67  ? 175  THR A OG1 1 
ATOM   1431 C  CG2 . THR A 1 175 ? -11.378 -27.256 28.399  1.00 45.06  ? 175  THR A CG2 1 
ATOM   1432 N  N   . SER A 1 176 ? -13.954 -25.848 26.390  1.00 38.16  ? 176  SER A N   1 
ATOM   1433 C  CA  . SER A 1 176 ? -14.942 -26.599 25.632  1.00 39.73  ? 176  SER A CA  1 
ATOM   1434 C  C   . SER A 1 176 ? -14.996 -26.130 24.181  1.00 40.39  ? 176  SER A C   1 
ATOM   1435 O  O   . SER A 1 176 ? -15.189 -26.943 23.273  1.00 38.90  ? 176  SER A O   1 
ATOM   1436 C  CB  . SER A 1 176 ? -16.312 -26.472 26.299  1.00 40.91  ? 176  SER A CB  1 
ATOM   1437 O  OG  . SER A 1 176 ? -16.337 -27.166 27.538  1.00 45.88  ? 176  SER A OG  1 
ATOM   1438 N  N   . MET A 1 177 ? -14.826 -24.825 23.947  1.00 38.62  ? 177  MET A N   1 
ATOM   1439 C  CA  . MET A 1 177 ? -14.859 -24.294 22.587  1.00 36.99  ? 177  MET A CA  1 
ATOM   1440 C  C   . MET A 1 177 ? -13.700 -24.836 21.760  1.00 36.68  ? 177  MET A C   1 
ATOM   1441 O  O   . MET A 1 177 ? -13.894 -25.302 20.625  1.00 37.60  ? 177  MET A O   1 
ATOM   1442 C  CB  . MET A 1 177 ? -14.849 -22.763 22.633  1.00 42.01  ? 177  MET A CB  1 
ATOM   1443 C  CG  . MET A 1 177 ? -15.038 -22.072 21.289  1.00 41.53  ? 177  MET A CG  1 
ATOM   1444 S  SD  . MET A 1 177 ? -14.064 -20.589 20.972  1.00 38.20  ? 177  MET A SD  1 
ATOM   1445 C  CE  . MET A 1 177 ? -12.377 -21.024 21.399  1.00 37.07  ? 177  MET A CE  1 
ATOM   1446 N  N   . VAL A 1 178 ? -12.490 -24.818 22.320  1.00 37.70  ? 178  VAL A N   1 
ATOM   1447 C  CA  . VAL A 1 178 ? -11.351 -25.373 21.595  1.00 38.85  ? 178  VAL A CA  1 
ATOM   1448 C  C   . VAL A 1 178 ? -11.556 -26.860 21.326  1.00 42.59  ? 178  VAL A C   1 
ATOM   1449 O  O   . VAL A 1 178 ? -11.275 -27.353 20.227  1.00 41.75  ? 178  VAL A O   1 
ATOM   1450 C  CB  . VAL A 1 178 ? -10.040 -25.108 22.353  1.00 40.06  ? 178  VAL A CB  1 
ATOM   1451 C  CG1 . VAL A 1 178 ? -8.870  -25.794 21.635  1.00 42.86  ? 178  VAL A CG1 1 
ATOM   1452 C  CG2 . VAL A 1 178 ? -9.802  -23.617 22.470  1.00 39.54  ? 178  VAL A CG2 1 
ATOM   1453 N  N   . ARG A 1 179 ? -12.057 -27.601 22.319  1.00 41.16  ? 179  ARG A N   1 
ATOM   1454 C  CA  . ARG A 1 179 ? -12.251 -29.036 22.126  1.00 39.21  ? 179  ARG A CA  1 
ATOM   1455 C  C   . ARG A 1 179 ? -13.318 -29.315 21.074  1.00 43.98  ? 179  ARG A C   1 
ATOM   1456 O  O   . ARG A 1 179 ? -13.210 -30.286 20.314  1.00 40.13  ? 179  ARG A O   1 
ATOM   1457 C  CB  . ARG A 1 179 ? -12.611 -29.695 23.460  1.00 44.75  ? 179  ARG A CB  1 
ATOM   1458 C  CG  . ARG A 1 179 ? -12.248 -31.168 23.555  1.00 50.46  ? 179  ARG A CG  1 
ATOM   1459 C  CD  . ARG A 1 179 ? -11.927 -31.536 25.007  1.00 54.43  ? 179  ARG A CD  1 
ATOM   1460 N  NE  . ARG A 1 179 ? -12.974 -31.100 25.928  1.00 55.81  ? 179  ARG A NE  1 
ATOM   1461 C  CZ  . ARG A 1 179 ? -12.762 -30.727 27.184  1.00 54.34  ? 179  ARG A CZ  1 
ATOM   1462 N  NH1 . ARG A 1 179 ? -11.547 -30.723 27.710  1.00 58.47  ? 179  ARG A NH1 1 
ATOM   1463 N  NH2 . ARG A 1 179 ? -13.796 -30.343 27.930  1.00 51.59  ? 179  ARG A NH2 1 
ATOM   1464 N  N   . ALA A 1 180 ? -14.356 -28.475 21.013  1.00 36.26  ? 180  ALA A N   1 
ATOM   1465 C  CA  . ALA A 1 180 ? -15.375 -28.640 19.984  1.00 38.40  ? 180  ALA A CA  1 
ATOM   1466 C  C   . ALA A 1 180 ? -14.810 -28.336 18.602  1.00 40.42  ? 180  ALA A C   1 
ATOM   1467 O  O   . ALA A 1 180 ? -15.095 -29.055 17.639  1.00 37.86  ? 180  ALA A O   1 
ATOM   1468 C  CB  . ALA A 1 180 ? -16.580 -27.749 20.279  1.00 39.60  ? 180  ALA A CB  1 
ATOM   1469 N  N   . LEU A 1 181 ? -13.999 -27.279 18.491  1.00 38.09  ? 181  LEU A N   1 
ATOM   1470 C  CA  . LEU A 1 181 ? -13.383 -26.950 17.208  1.00 38.21  ? 181  LEU A CA  1 
ATOM   1471 C  C   . LEU A 1 181 ? -12.385 -28.026 16.795  1.00 41.29  ? 181  LEU A C   1 
ATOM   1472 O  O   . LEU A 1 181 ? -12.330 -28.409 15.616  1.00 38.69  ? 181  LEU A O   1 
ATOM   1473 C  CB  . LEU A 1 181 ? -12.702 -25.580 17.286  1.00 38.96  ? 181  LEU A CB  1 
ATOM   1474 C  CG  . LEU A 1 181 ? -13.637 -24.383 17.498  1.00 38.72  ? 181  LEU A CG  1 
ATOM   1475 C  CD1 . LEU A 1 181 ? -12.825 -23.122 17.689  1.00 41.22  ? 181  LEU A CD1 1 
ATOM   1476 C  CD2 . LEU A 1 181 ? -14.575 -24.260 16.274  1.00 35.16  ? 181  LEU A CD2 1 
ATOM   1477 N  N   . ASP A 1 182 ? -11.577 -28.507 17.748  1.00 38.66  ? 182  ASP A N   1 
ATOM   1478 C  CA  . ASP A 1 182 ? -10.683 -29.635 17.485  1.00 44.31  ? 182  ASP A CA  1 
ATOM   1479 C  C   . ASP A 1 182 ? -11.454 -30.818 16.928  1.00 42.45  ? 182  ASP A C   1 
ATOM   1480 O  O   . ASP A 1 182 ? -11.033 -31.451 15.953  1.00 45.08  ? 182  ASP A O   1 
ATOM   1481 C  CB  . ASP A 1 182 ? -9.963  -30.077 18.761  1.00 46.02  ? 182  ASP A CB  1 
ATOM   1482 C  CG  . ASP A 1 182 ? -8.829  -29.172 19.144  1.00 51.54  ? 182  ASP A CG  1 
ATOM   1483 O  OD1 . ASP A 1 182 ? -8.274  -28.497 18.254  1.00 55.28  ? 182  ASP A OD1 1 
ATOM   1484 O  OD2 . ASP A 1 182 ? -8.458  -29.179 20.341  1.00 55.07  ? 182  ASP A OD2 1 
ATOM   1485 N  N   . GLU A 1 183 ? -12.575 -31.156 17.567  1.00 43.43  ? 183  GLU A N   1 
ATOM   1486 C  CA  . GLU A 1 183 ? -13.363 -32.299 17.123  1.00 42.75  ? 183  GLU A CA  1 
ATOM   1487 C  C   . GLU A 1 183 ? -13.893 -32.079 15.711  1.00 41.94  ? 183  GLU A C   1 
ATOM   1488 O  O   . GLU A 1 183 ? -13.836 -32.981 14.867  1.00 43.84  ? 183  GLU A O   1 
ATOM   1489 C  CB  . GLU A 1 183 ? -14.506 -32.560 18.105  1.00 42.03  ? 183  GLU A CB  1 
ATOM   1490 C  CG  . GLU A 1 183 ? -15.609 -33.456 17.568  1.00 46.01  ? 183  GLU A CG  1 
ATOM   1491 C  CD  . GLU A 1 183 ? -15.188 -34.915 17.403  1.00 49.50  ? 183  GLU A CD  1 
ATOM   1492 O  OE1 . GLU A 1 183 ? -14.020 -35.248 17.702  1.00 44.84  ? 183  GLU A OE1 1 
ATOM   1493 O  OE2 . GLU A 1 183 ? -16.033 -35.721 16.956  1.00 45.30  ? 183  GLU A OE2 1 
ATOM   1494 N  N   . ALA A 1 184 ? -14.432 -30.887 15.440  1.00 40.89  ? 184  ALA A N   1 
ATOM   1495 C  CA  . ALA A 1 184 ? -14.935 -30.608 14.099  1.00 39.74  ? 184  ALA A CA  1 
ATOM   1496 C  C   . ALA A 1 184 ? -13.829 -30.741 13.059  1.00 38.18  ? 184  ALA A C   1 
ATOM   1497 O  O   . ALA A 1 184 ? -14.062 -31.259 11.958  1.00 38.42  ? 184  ALA A O   1 
ATOM   1498 C  CB  . ALA A 1 184 ? -15.557 -29.208 14.044  1.00 36.98  ? 184  ALA A CB  1 
ATOM   1499 N  N   . MET A 1 185 ? -12.624 -30.266 13.381  1.00 38.88  ? 185  MET A N   1 
ATOM   1500 C  CA  . MET A 1 185 ? -11.519 -30.349 12.426  1.00 39.10  ? 185  MET A CA  1 
ATOM   1501 C  C   . MET A 1 185 ? -11.072 -31.791 12.217  1.00 42.46  ? 185  MET A C   1 
ATOM   1502 O  O   . MET A 1 185 ? -10.812 -32.214 11.084  1.00 39.91  ? 185  MET A O   1 
ATOM   1503 C  CB  . MET A 1 185 ? -10.342 -29.490 12.893  1.00 37.83  ? 185  MET A CB  1 
ATOM   1504 C  CG  . MET A 1 185 ? -9.255  -29.313 11.815  1.00 35.90  ? 185  MET A CG  1 
ATOM   1505 S  SD  . MET A 1 185 ? -7.789  -28.415 12.373  1.00 40.51  ? 185  MET A SD  1 
ATOM   1506 C  CE  . MET A 1 185 ? -7.022  -29.629 13.452  1.00 44.75  ? 185  MET A CE  1 
ATOM   1507 N  N   . ASN A 1 186 ? -10.967 -32.560 13.301  1.00 40.56  ? 186  ASN A N   1 
ATOM   1508 C  CA  . ASN A 1 186 ? -10.580 -33.960 13.172  1.00 42.46  ? 186  ASN A CA  1 
ATOM   1509 C  C   . ASN A 1 186 ? -11.655 -34.766 12.465  1.00 42.18  ? 186  ASN A C   1 
ATOM   1510 O  O   . ASN A 1 186 ? -11.342 -35.712 11.735  1.00 45.46  ? 186  ASN A O   1 
ATOM   1511 C  CB  . ASN A 1 186 ? -10.297 -34.547 14.558  1.00 43.39  ? 186  ASN A CB  1 
ATOM   1512 C  CG  . ASN A 1 186 ? -9.678  -35.942 14.494  1.00 52.48  ? 186  ASN A CG  1 
ATOM   1513 O  OD1 . ASN A 1 186 ? -10.367 -36.949 14.678  1.00 53.01  ? 186  ASN A OD1 1 
ATOM   1514 N  ND2 . ASN A 1 186 ? -8.371  -36.000 14.248  1.00 46.54  ? 186  ASN A ND2 1 
ATOM   1515 N  N   . LYS A 1 187 ? -12.925 -34.416 12.669  1.00 42.70  ? 187  LYS A N   1 
ATOM   1516 C  CA  . LYS A 1 187 ? -14.001 -35.139 12.009  1.00 43.51  ? 187  LYS A CA  1 
ATOM   1517 C  C   . LYS A 1 187 ? -13.956 -34.989 10.484  1.00 42.50  ? 187  LYS A C   1 
ATOM   1518 O  O   . LYS A 1 187 ? -14.501 -35.840 9.774   1.00 43.95  ? 187  LYS A O   1 
ATOM   1519 C  CB  . LYS A 1 187 ? -15.344 -34.661 12.567  1.00 44.59  ? 187  LYS A CB  1 
ATOM   1520 C  CG  . LYS A 1 187 ? -16.476 -35.666 12.442  1.00 48.64  ? 187  LYS A CG  1 
ATOM   1521 C  CD  . LYS A 1 187 ? -17.754 -35.155 13.105  1.00 49.83  ? 187  LYS A CD  1 
ATOM   1522 C  CE  . LYS A 1 187 ? -18.988 -35.584 12.311  1.00 55.20  ? 187  LYS A CE  1 
ATOM   1523 N  NZ  . LYS A 1 187 ? -20.236 -34.855 12.698  1.00 60.82  ? 187  LYS A NZ  1 
ATOM   1524 N  N   . LEU A 1 188 ? -13.303 -33.946 9.967   1.00 39.85  ? 188  LEU A N   1 
ATOM   1525 C  CA  . LEU A 1 188 ? -13.253 -33.727 8.523   1.00 41.14  ? 188  LEU A CA  1 
ATOM   1526 C  C   . LEU A 1 188 ? -12.737 -34.952 7.768   1.00 43.93  ? 188  LEU A C   1 
ATOM   1527 O  O   . LEU A 1 188 ? -13.196 -35.242 6.660   1.00 45.35  ? 188  LEU A O   1 
ATOM   1528 C  CB  . LEU A 1 188 ? -12.373 -32.520 8.201   1.00 37.57  ? 188  LEU A CB  1 
ATOM   1529 C  CG  . LEU A 1 188 ? -12.939 -31.177 8.662   1.00 41.80  ? 188  LEU A CG  1 
ATOM   1530 C  CD1 . LEU A 1 188 ? -11.973 -30.043 8.359   1.00 42.08  ? 188  LEU A CD1 1 
ATOM   1531 C  CD2 . LEU A 1 188 ? -14.296 -30.943 8.007   1.00 35.70  ? 188  LEU A CD2 1 
ATOM   1532 N  N   . GLN A 1 189 ? -11.775 -35.671 8.337   1.00 47.93  ? 189  GLN A N   1 
ATOM   1533 C  CA  . GLN A 1 189 ? -11.165 -36.802 7.646   1.00 48.49  ? 189  GLN A CA  1 
ATOM   1534 C  C   . GLN A 1 189 ? -11.755 -38.156 8.034   1.00 51.14  ? 189  GLN A C   1 
ATOM   1535 O  O   . GLN A 1 189 ? -11.298 -39.184 7.519   1.00 53.23  ? 189  GLN A O   1 
ATOM   1536 C  CB  . GLN A 1 189 ? -9.639  -36.784 7.866   1.00 47.66  ? 189  GLN A CB  1 
ATOM   1537 C  CG  . GLN A 1 189 ? -9.184  -36.721 9.326   1.00 47.96  ? 189  GLN A CG  1 
ATOM   1538 C  CD  . GLN A 1 189 ? -9.271  -38.051 10.056  1.00 53.76  ? 189  GLN A CD  1 
ATOM   1539 O  OE1 . GLN A 1 189 ? -8.421  -38.927 9.883   1.00 55.22  ? 189  GLN A OE1 1 
ATOM   1540 N  NE2 . GLN A 1 189 ? -10.292 -38.197 10.901  1.00 54.68  ? 189  GLN A NE2 1 
ATOM   1541 N  N   . ARG A 1 190 ? -12.779 -38.189 8.890   1.00 48.96  ? 190  ARG A N   1 
ATOM   1542 C  CA  . ARG A 1 190 ? -13.380 -39.450 9.328   1.00 52.37  ? 190  ARG A CA  1 
ATOM   1543 C  C   . ARG A 1 190 ? -14.259 -40.024 8.227   1.00 56.60  ? 190  ARG A C   1 
ATOM   1544 O  O   . ARG A 1 190 ? -15.324 -39.477 7.921   1.00 53.25  ? 190  ARG A O   1 
ATOM   1545 C  CB  . ARG A 1 190 ? -14.198 -39.247 10.596  1.00 54.68  ? 190  ARG A CB  1 
ATOM   1546 C  CG  . ARG A 1 190 ? -13.464 -39.590 11.841  1.00 55.14  ? 190  ARG A CG  1 
ATOM   1547 C  CD  . ARG A 1 190 ? -14.294 -39.240 13.051  1.00 52.24  ? 190  ARG A CD  1 
ATOM   1548 N  NE  . ARG A 1 190 ? -13.477 -38.471 13.977  1.00 51.32  ? 190  ARG A NE  1 
ATOM   1549 C  CZ  . ARG A 1 190 ? -13.958 -37.765 14.986  1.00 50.09  ? 190  ARG A CZ  1 
ATOM   1550 N  NH1 . ARG A 1 190 ? -15.254 -37.742 15.255  1.00 45.98  ? 190  ARG A NH1 1 
ATOM   1551 N  NH2 . ARG A 1 190 ? -13.118 -37.065 15.740  1.00 48.13  ? 190  ARG A NH2 1 
ATOM   1552 N  N   . ALA A 1 191 ? -13.838 -41.153 7.653   1.00 58.16  ? 191  ALA A N   1 
ATOM   1553 C  CA  . ALA A 1 191 ? -14.625 -41.761 6.585   1.00 58.29  ? 191  ALA A CA  1 
ATOM   1554 C  C   . ALA A 1 191 ? -15.909 -42.384 7.126   1.00 61.16  ? 191  ALA A C   1 
ATOM   1555 O  O   . ALA A 1 191 ? -16.952 -42.345 6.461   1.00 58.94  ? 191  ALA A O   1 
ATOM   1556 C  CB  . ALA A 1 191 ? -13.784 -42.798 5.838   1.00 61.66  ? 191  ALA A CB  1 
ATOM   1557 N  N   . ASN A 1 192 ? -15.861 -42.961 8.331   1.00 58.38  ? 192  ASN A N   1 
ATOM   1558 C  CA  . ASN A 1 192 ? -17.036 -43.548 8.977   1.00 63.50  ? 192  ASN A CA  1 
ATOM   1559 C  C   . ASN A 1 192 ? -17.245 -42.877 10.330  1.00 56.87  ? 192  ASN A C   1 
ATOM   1560 O  O   . ASN A 1 192 ? -16.851 -43.412 11.377  1.00 57.82  ? 192  ASN A O   1 
ATOM   1561 C  CB  . ASN A 1 192 ? -16.902 -45.065 9.109   1.00 64.49  ? 192  ASN A CB  1 
ATOM   1562 C  CG  . ASN A 1 192 ? -16.218 -45.694 7.904   1.00 65.79  ? 192  ASN A CG  1 
ATOM   1563 O  OD1 . ASN A 1 192 ? -15.069 -46.132 7.976   1.00 72.38  ? 192  ASN A OD1 1 
ATOM   1564 N  ND2 . ASN A 1 192 ? -16.924 -45.720 6.779   1.00 66.13  ? 192  ASN A ND2 1 
ATOM   1565 N  N   . PRO A 1 193 ? -17.885 -41.706 10.347  1.00 59.04  ? 193  PRO A N   1 
ATOM   1566 C  CA  . PRO A 1 193 ? -18.041 -40.979 11.614  1.00 59.40  ? 193  PRO A CA  1 
ATOM   1567 C  C   . PRO A 1 193 ? -18.994 -41.651 12.577  1.00 61.72  ? 193  PRO A C   1 
ATOM   1568 O  O   . PRO A 1 193 ? -18.961 -41.334 13.771  1.00 60.89  ? 193  PRO A O   1 
ATOM   1569 C  CB  . PRO A 1 193 ? -18.575 -39.608 11.179  1.00 55.85  ? 193  PRO A CB  1 
ATOM   1570 C  CG  . PRO A 1 193 ? -19.132 -39.811 9.789   1.00 59.33  ? 193  PRO A CG  1 
ATOM   1571 C  CD  . PRO A 1 193 ? -18.755 -41.176 9.285   1.00 59.25  ? 193  PRO A CD  1 
ATOM   1572 N  N   . ASP A 1 194 ? -19.847 -42.557 12.105  1.00 61.61  ? 194  ASP A N   1 
ATOM   1573 C  CA  . ASP A 1 194 ? -20.770 -43.262 12.982  1.00 63.61  ? 194  ASP A CA  1 
ATOM   1574 C  C   . ASP A 1 194 ? -20.208 -44.584 13.485  1.00 65.93  ? 194  ASP A C   1 
ATOM   1575 O  O   . ASP A 1 194 ? -20.933 -45.341 14.141  1.00 65.93  ? 194  ASP A O   1 
ATOM   1576 C  CB  . ASP A 1 194 ? -22.106 -43.483 12.271  1.00 65.20  ? 194  ASP A CB  1 
ATOM   1577 C  CG  . ASP A 1 194 ? -22.894 -42.199 12.119  1.00 70.96  ? 194  ASP A CG  1 
ATOM   1578 O  OD1 . ASP A 1 194 ? -22.706 -41.290 12.958  1.00 68.81  ? 194  ASP A OD1 1 
ATOM   1579 O  OD2 . ASP A 1 194 ? -23.690 -42.091 11.164  1.00 76.61  ? 194  ASP A OD2 1 
ATOM   1580 N  N   . ASP A 1 195 ? -18.939 -44.872 13.205  1.00 62.44  ? 195  ASP A N   1 
ATOM   1581 C  CA  . ASP A 1 195 ? -18.300 -46.044 13.784  1.00 66.34  ? 195  ASP A CA  1 
ATOM   1582 C  C   . ASP A 1 195 ? -18.247 -45.900 15.303  1.00 67.37  ? 195  ASP A C   1 
ATOM   1583 O  O   . ASP A 1 195 ? -17.802 -44.858 15.806  1.00 65.36  ? 195  ASP A O   1 
ATOM   1584 C  CB  . ASP A 1 195 ? -16.888 -46.216 13.225  1.00 67.62  ? 195  ASP A CB  1 
ATOM   1585 C  CG  . ASP A 1 195 ? -16.196 -47.461 13.758  1.00 72.23  ? 195  ASP A CG  1 
ATOM   1586 O  OD1 . ASP A 1 195 ? -16.726 -48.571 13.539  1.00 76.29  ? 195  ASP A OD1 1 
ATOM   1587 O  OD2 . ASP A 1 195 ? -15.123 -47.336 14.390  1.00 68.61  ? 195  ASP A OD2 1 
ATOM   1588 N  N   . PRO A 1 196 ? -18.665 -46.917 16.066  1.00 69.25  ? 196  PRO A N   1 
ATOM   1589 C  CA  . PRO A 1 196 ? -18.679 -46.786 17.533  1.00 67.17  ? 196  PRO A CA  1 
ATOM   1590 C  C   . PRO A 1 196 ? -17.334 -46.382 18.126  1.00 66.20  ? 196  PRO A C   1 
ATOM   1591 O  O   . PRO A 1 196 ? -17.263 -46.001 19.299  1.00 66.60  ? 196  PRO A O   1 
ATOM   1592 C  CB  . PRO A 1 196 ? -19.103 -48.184 18.004  1.00 69.45  ? 196  PRO A CB  1 
ATOM   1593 C  CG  . PRO A 1 196 ? -19.866 -48.752 16.855  1.00 71.21  ? 196  PRO A CG  1 
ATOM   1594 C  CD  . PRO A 1 196 ? -19.188 -48.220 15.620  1.00 71.11  ? 196  PRO A CD  1 
ATOM   1595 N  N   . ALA A 1 197 ? -16.260 -46.455 17.335  1.00 64.34  ? 197  ALA A N   1 
ATOM   1596 C  CA  . ALA A 1 197 ? -14.966 -45.968 17.800  1.00 64.91  ? 197  ALA A CA  1 
ATOM   1597 C  C   . ALA A 1 197 ? -15.000 -44.488 18.162  1.00 63.13  ? 197  ALA A C   1 
ATOM   1598 O  O   . ALA A 1 197 ? -14.105 -44.014 18.867  1.00 62.19  ? 197  ALA A O   1 
ATOM   1599 C  CB  . ALA A 1 197 ? -13.894 -46.212 16.736  1.00 63.09  ? 197  ALA A CB  1 
ATOM   1600 N  N   . TYR A 1 198 ? -16.003 -43.746 17.691  1.00 61.73  ? 198  TYR A N   1 
ATOM   1601 C  CA  . TYR A 1 198 ? -16.125 -42.322 17.977  1.00 59.66  ? 198  TYR A CA  1 
ATOM   1602 C  C   . TYR A 1 198 ? -17.257 -42.027 18.952  1.00 59.72  ? 198  TYR A C   1 
ATOM   1603 O  O   . TYR A 1 198 ? -17.722 -40.884 19.035  1.00 56.63  ? 198  TYR A O   1 
ATOM   1604 C  CB  . TYR A 1 198 ? -16.320 -41.546 16.676  1.00 57.93  ? 198  TYR A CB  1 
ATOM   1605 C  CG  . TYR A 1 198 ? -15.228 -41.808 15.669  1.00 54.89  ? 198  TYR A CG  1 
ATOM   1606 C  CD1 . TYR A 1 198 ? -15.504 -42.451 14.473  1.00 57.89  ? 198  TYR A CD1 1 
ATOM   1607 C  CD2 . TYR A 1 198 ? -13.917 -41.428 15.923  1.00 56.17  ? 198  TYR A CD2 1 
ATOM   1608 C  CE1 . TYR A 1 198 ? -14.509 -42.703 13.550  1.00 59.54  ? 198  TYR A CE1 1 
ATOM   1609 C  CE2 . TYR A 1 198 ? -12.910 -41.675 15.005  1.00 60.06  ? 198  TYR A CE2 1 
ATOM   1610 C  CZ  . TYR A 1 198 ? -13.215 -42.316 13.820  1.00 58.92  ? 198  TYR A CZ  1 
ATOM   1611 O  OH  . TYR A 1 198 ? -12.227 -42.565 12.895  1.00 68.29  ? 198  TYR A OH  1 
ATOM   1612 N  N   . ASP A 1 199 ? -17.728 -43.042 19.678  1.00 60.41  ? 199  ASP A N   1 
ATOM   1613 C  CA  . ASP A 1 199 ? -18.761 -42.802 20.676  1.00 59.78  ? 199  ASP A CA  1 
ATOM   1614 C  C   . ASP A 1 199 ? -18.290 -41.789 21.704  1.00 56.91  ? 199  ASP A C   1 
ATOM   1615 O  O   . ASP A 1 199 ? -19.033 -40.870 22.065  1.00 52.83  ? 199  ASP A O   1 
ATOM   1616 C  CB  . ASP A 1 199 ? -19.154 -44.111 21.359  1.00 63.72  ? 199  ASP A CB  1 
ATOM   1617 C  CG  . ASP A 1 199 ? -19.994 -45.001 20.473  1.00 67.17  ? 199  ASP A CG  1 
ATOM   1618 O  OD1 . ASP A 1 199 ? -20.627 -44.477 19.529  1.00 63.89  ? 199  ASP A OD1 1 
ATOM   1619 O  OD2 . ASP A 1 199 ? -20.031 -46.223 20.735  1.00 69.03  ? 199  ASP A OD2 1 
ATOM   1620 N  N   . GLU A 1 200 ? -17.049 -41.932 22.173  1.00 56.98  ? 200  GLU A N   1 
ATOM   1621 C  CA  . GLU A 1 200 ? -16.513 -41.015 23.173  1.00 58.88  ? 200  GLU A CA  1 
ATOM   1622 C  C   . GLU A 1 200 ? -16.340 -39.611 22.602  1.00 56.36  ? 200  GLU A C   1 
ATOM   1623 O  O   . GLU A 1 200 ? -16.658 -38.623 23.274  1.00 53.46  ? 200  GLU A O   1 
ATOM   1624 C  CB  . GLU A 1 200 ? -15.187 -41.557 23.710  1.00 59.16  ? 200  GLU A CB  1 
ATOM   1625 C  CG  . GLU A 1 200 ? -14.481 -40.653 24.701  1.00 59.08  ? 200  GLU A CG  1 
ATOM   1626 C  CD  . GLU A 1 200 ? -15.331 -40.312 25.914  1.00 66.12  ? 200  GLU A CD  1 
ATOM   1627 O  OE1 . GLU A 1 200 ? -16.326 -41.026 26.175  1.00 67.95  ? 200  GLU A OE1 1 
ATOM   1628 O  OE2 . GLU A 1 200 ? -14.994 -39.330 26.613  1.00 67.43  ? 200  GLU A OE2 1 
ATOM   1629 N  N   . ASN A 1 201 ? -15.830 -39.502 21.370  1.00 57.22  ? 201  ASN A N   1 
ATOM   1630 C  CA  . ASN A 1 201 ? -15.810 -38.212 20.682  1.00 52.01  ? 201  ASN A CA  1 
ATOM   1631 C  C   . ASN A 1 201 ? -17.186 -37.565 20.723  1.00 52.60  ? 201  ASN A C   1 
ATOM   1632 O  O   . ASN A 1 201 ? -17.327 -36.378 21.039  1.00 52.41  ? 201  ASN A O   1 
ATOM   1633 C  CB  . ASN A 1 201 ? -15.372 -38.391 19.226  1.00 55.94  ? 201  ASN A CB  1 
ATOM   1634 C  CG  . ASN A 1 201 ? -14.021 -39.053 19.094  1.00 57.73  ? 201  ASN A CG  1 
ATOM   1635 O  OD1 . ASN A 1 201 ? -13.923 -40.279 19.067  1.00 62.90  ? 201  ASN A OD1 1 
ATOM   1636 N  ND2 . ASN A 1 201 ? -12.972 -38.247 18.974  1.00 56.90  ? 201  ASN A ND2 1 
ATOM   1637 N  N   . LYS A 1 202 ? -18.216 -38.347 20.395  1.00 50.91  ? 202  LYS A N   1 
ATOM   1638 C  CA  . LYS A 1 202 ? -19.578 -37.833 20.373  1.00 50.91  ? 202  LYS A CA  1 
ATOM   1639 C  C   . LYS A 1 202 ? -19.998 -37.358 21.760  1.00 51.63  ? 202  LYS A C   1 
ATOM   1640 O  O   . LYS A 1 202 ? -20.571 -36.271 21.915  1.00 48.17  ? 202  LYS A O   1 
ATOM   1641 C  CB  . LYS A 1 202 ? -20.527 -38.920 19.864  1.00 53.02  ? 202  LYS A CB  1 
ATOM   1642 C  CG  . LYS A 1 202 ? -21.007 -38.747 18.428  1.00 56.81  ? 202  LYS A CG  1 
ATOM   1643 C  CD  . LYS A 1 202 ? -21.344 -40.104 17.809  1.00 58.62  ? 202  LYS A CD  1 
ATOM   1644 C  CE  . LYS A 1 202 ? -20.974 -40.180 16.328  1.00 61.40  ? 202  LYS A CE  1 
ATOM   1645 N  NZ  . LYS A 1 202 ? -21.169 -41.561 15.802  1.00 64.42  ? 202  LYS A NZ  1 
ATOM   1646 N  N   . ARG A 1 203 ? -19.720 -38.167 22.787  1.00 53.03  ? 203  ARG A N   1 
ATOM   1647 C  CA  . ARG A 1 203 ? -20.106 -37.794 24.143  1.00 50.73  ? 203  ARG A CA  1 
ATOM   1648 C  C   . ARG A 1 203 ? -19.397 -36.514 24.574  1.00 49.45  ? 203  ARG A C   1 
ATOM   1649 O  O   . ARG A 1 203 ? -20.015 -35.602 25.137  1.00 49.78  ? 203  ARG A O   1 
ATOM   1650 C  CB  . ARG A 1 203 ? -19.785 -38.932 25.114  1.00 55.25  ? 203  ARG A CB  1 
ATOM   1651 C  CG  . ARG A 1 203 ? -20.147 -38.598 26.557  1.00 60.56  ? 203  ARG A CG  1 
ATOM   1652 C  CD  . ARG A 1 203 ? -19.401 -39.447 27.573  1.00 59.57  ? 203  ARG A CD  1 
ATOM   1653 N  NE  . ARG A 1 203 ? -18.006 -39.032 27.672  1.00 63.46  ? 203  ARG A NE  1 
ATOM   1654 C  CZ  . ARG A 1 203 ? -17.606 -37.890 28.217  1.00 64.16  ? 203  ARG A CZ  1 
ATOM   1655 N  NH1 . ARG A 1 203 ? -18.470 -37.032 28.739  1.00 63.11  ? 203  ARG A NH1 1 
ATOM   1656 N  NH2 . ARG A 1 203 ? -16.307 -37.599 28.234  1.00 66.43  ? 203  ARG A NH2 1 
ATOM   1657 N  N   . GLN A 1 204 ? -18.088 -36.440 24.324  1.00 47.55  ? 204  GLN A N   1 
ATOM   1658 C  CA  . GLN A 1 204 ? -17.320 -35.250 24.672  1.00 48.37  ? 204  GLN A CA  1 
ATOM   1659 C  C   . GLN A 1 204 ? -17.864 -34.021 23.950  1.00 48.62  ? 204  GLN A C   1 
ATOM   1660 O  O   . GLN A 1 204 ? -18.059 -32.962 24.559  1.00 48.32  ? 204  GLN A O   1 
ATOM   1661 C  CB  . GLN A 1 204 ? -15.845 -35.467 24.335  1.00 49.69  ? 204  GLN A CB  1 
ATOM   1662 C  CG  . GLN A 1 204 ? -14.947 -34.304 24.711  1.00 51.14  ? 204  GLN A CG  1 
ATOM   1663 C  CD  . GLN A 1 204 ? -14.984 -34.028 26.197  1.00 56.56  ? 204  GLN A CD  1 
ATOM   1664 O  OE1 . GLN A 1 204 ? -15.606 -33.063 26.655  1.00 54.01  ? 204  GLN A OE1 1 
ATOM   1665 N  NE2 . GLN A 1 204 ? -14.339 -34.896 26.966  1.00 57.91  ? 204  GLN A NE2 1 
ATOM   1666 N  N   . PHE A 1 205 ? -18.108 -34.149 22.642  1.00 46.11  ? 205  PHE A N   1 
ATOM   1667 C  CA  . PHE A 1 205 ? -18.717 -33.066 21.874  1.00 48.84  ? 205  PHE A CA  1 
ATOM   1668 C  C   . PHE A 1 205 ? -19.994 -32.568 22.543  1.00 46.84  ? 205  PHE A C   1 
ATOM   1669 O  O   . PHE A 1 205 ? -20.156 -31.367 22.792  1.00 45.50  ? 205  PHE A O   1 
ATOM   1670 C  CB  . PHE A 1 205 ? -18.992 -33.551 20.446  1.00 46.32  ? 205  PHE A CB  1 
ATOM   1671 C  CG  . PHE A 1 205 ? -19.181 -32.446 19.434  1.00 45.79  ? 205  PHE A CG  1 
ATOM   1672 C  CD1 . PHE A 1 205 ? -18.180 -31.517 19.197  1.00 44.75  ? 205  PHE A CD1 1 
ATOM   1673 C  CD2 . PHE A 1 205 ? -20.340 -32.383 18.672  1.00 46.33  ? 205  PHE A CD2 1 
ATOM   1674 C  CE1 . PHE A 1 205 ? -18.349 -30.517 18.238  1.00 44.50  ? 205  PHE A CE1 1 
ATOM   1675 C  CE2 . PHE A 1 205 ? -20.515 -31.391 17.712  1.00 44.10  ? 205  PHE A CE2 1 
ATOM   1676 C  CZ  . PHE A 1 205 ? -19.521 -30.456 17.499  1.00 45.47  ? 205  PHE A CZ  1 
ATOM   1677 N  N   . GLN A 1 206 ? -20.906 -33.486 22.866  1.00 47.45  ? 206  GLN A N   1 
ATOM   1678 C  CA  . GLN A 1 206 ? -22.151 -33.087 23.513  1.00 50.48  ? 206  GLN A CA  1 
ATOM   1679 C  C   . GLN A 1 206 ? -21.870 -32.358 24.822  1.00 49.85  ? 206  GLN A C   1 
ATOM   1680 O  O   . GLN A 1 206 ? -22.503 -31.341 25.132  1.00 48.23  ? 206  GLN A O   1 
ATOM   1681 C  CB  . GLN A 1 206 ? -23.020 -34.320 23.758  1.00 51.23  ? 206  GLN A CB  1 
ATOM   1682 C  CG  . GLN A 1 206 ? -23.847 -34.719 22.547  1.00 61.12  ? 206  GLN A CG  1 
ATOM   1683 C  CD  . GLN A 1 206 ? -24.279 -33.520 21.724  1.00 61.82  ? 206  GLN A CD  1 
ATOM   1684 O  OE1 . GLN A 1 206 ? -24.932 -32.606 22.233  1.00 64.92  ? 206  GLN A OE1 1 
ATOM   1685 N  NE2 . GLN A 1 206 ? -23.894 -33.504 20.450  1.00 59.03  ? 206  GLN A NE2 1 
ATOM   1686 N  N   . GLU A 1 207 ? -20.906 -32.861 25.593  1.00 49.15  ? 207  GLU A N   1 
ATOM   1687 C  CA  . GLU A 1 207 ? -20.549 -32.247 26.868  1.00 49.55  ? 207  GLU A CA  1 
ATOM   1688 C  C   . GLU A 1 207 ? -20.034 -30.826 26.668  1.00 49.96  ? 207  GLU A C   1 
ATOM   1689 O  O   . GLU A 1 207 ? -20.377 -29.913 27.431  1.00 43.66  ? 207  GLU A O   1 
ATOM   1690 C  CB  . GLU A 1 207 ? -19.493 -33.112 27.555  1.00 51.89  ? 207  GLU A CB  1 
ATOM   1691 C  CG  . GLU A 1 207 ? -18.974 -32.608 28.879  1.00 56.22  ? 207  GLU A CG  1 
ATOM   1692 C  CD  . GLU A 1 207 ? -17.957 -33.568 29.471  1.00 66.61  ? 207  GLU A CD  1 
ATOM   1693 O  OE1 . GLU A 1 207 ? -18.355 -34.676 29.900  1.00 68.43  ? 207  GLU A OE1 1 
ATOM   1694 O  OE2 . GLU A 1 207 ? -16.755 -33.212 29.496  1.00 66.06  ? 207  GLU A OE2 1 
ATOM   1695 N  N   . ASP A 1 208 ? -19.197 -30.625 25.650  1.00 45.56  ? 208  ASP A N   1 
ATOM   1696 C  CA  . ASP A 1 208 ? -18.648 -29.302 25.393  1.00 43.86  ? 208  ASP A CA  1 
ATOM   1697 C  C   . ASP A 1 208 ? -19.715 -28.339 24.892  1.00 44.56  ? 208  ASP A C   1 
ATOM   1698 O  O   . ASP A 1 208 ? -19.639 -27.137 25.170  1.00 45.72  ? 208  ASP A O   1 
ATOM   1699 C  CB  . ASP A 1 208 ? -17.497 -29.407 24.395  1.00 45.59  ? 208  ASP A CB  1 
ATOM   1700 C  CG  . ASP A 1 208 ? -16.271 -30.051 24.997  1.00 47.76  ? 208  ASP A CG  1 
ATOM   1701 O  OD1 . ASP A 1 208 ? -16.016 -29.806 26.191  1.00 48.82  ? 208  ASP A OD1 1 
ATOM   1702 O  OD2 . ASP A 1 208 ? -15.564 -30.794 24.283  1.00 45.85  ? 208  ASP A OD2 1 
ATOM   1703 N  N   . ILE A 1 209 ? -20.707 -28.843 24.158  1.00 44.74  ? 209  ILE A N   1 
ATOM   1704 C  CA  . ILE A 1 209 ? -21.812 -27.999 23.715  1.00 45.34  ? 209  ILE A CA  1 
ATOM   1705 C  C   . ILE A 1 209 ? -22.680 -27.586 24.900  1.00 46.91  ? 209  ILE A C   1 
ATOM   1706 O  O   . ILE A 1 209 ? -23.158 -26.447 24.972  1.00 45.97  ? 209  ILE A O   1 
ATOM   1707 C  CB  . ILE A 1 209 ? -22.626 -28.723 22.626  1.00 46.89  ? 209  ILE A CB  1 
ATOM   1708 C  CG1 . ILE A 1 209 ? -21.781 -28.865 21.347  1.00 45.03  ? 209  ILE A CG1 1 
ATOM   1709 C  CG2 . ILE A 1 209 ? -23.911 -27.976 22.345  1.00 48.06  ? 209  ILE A CG2 1 
ATOM   1710 C  CD1 . ILE A 1 209 ? -22.378 -29.784 20.292  1.00 43.64  ? 209  ILE A CD1 1 
ATOM   1711 N  N   . LYS A 1 210 ? -22.898 -28.500 25.849  1.00 46.00  ? 210  LYS A N   1 
ATOM   1712 C  CA  . LYS A 1 210 ? -23.641 -28.147 27.055  1.00 44.19  ? 210  LYS A CA  1 
ATOM   1713 C  C   . LYS A 1 210 ? -22.934 -27.042 27.831  1.00 43.92  ? 210  LYS A C   1 
ATOM   1714 O  O   . LYS A 1 210 ? -23.568 -26.084 28.284  1.00 47.49  ? 210  LYS A O   1 
ATOM   1715 C  CB  . LYS A 1 210 ? -23.828 -29.385 27.938  1.00 47.51  ? 210  LYS A CB  1 
ATOM   1716 C  CG  . LYS A 1 210 ? -24.444 -29.107 29.322  1.00 52.35  ? 210  LYS A CG  1 
ATOM   1717 C  CD  . LYS A 1 210 ? -25.969 -29.044 29.278  1.00 57.28  ? 210  LYS A CD  1 
ATOM   1718 C  CE  . LYS A 1 210 ? -26.560 -28.548 30.602  1.00 57.54  ? 210  LYS A CE  1 
ATOM   1719 N  NZ  . LYS A 1 210 ? -25.669 -28.825 31.769  1.00 56.26  ? 210  LYS A NZ  1 
ATOM   1720 N  N   . VAL A 1 211 ? -21.617 -27.178 28.022  1.00 42.29  ? 211  VAL A N   1 
ATOM   1721 C  CA  . VAL A 1 211 ? -20.864 -26.161 28.755  1.00 44.44  ? 211  VAL A CA  1 
ATOM   1722 C  C   . VAL A 1 211 ? -21.064 -24.810 28.101  1.00 46.09  ? 211  VAL A C   1 
ATOM   1723 O  O   . VAL A 1 211 ? -21.233 -23.780 28.768  1.00 42.59  ? 211  VAL A O   1 
ATOM   1724 C  CB  . VAL A 1 211 ? -19.369 -26.539 28.810  1.00 47.07  ? 211  VAL A CB  1 
ATOM   1725 C  CG1 . VAL A 1 211 ? -18.529 -25.358 29.277  1.00 46.57  ? 211  VAL A CG1 1 
ATOM   1726 C  CG2 . VAL A 1 211 ? -19.141 -27.744 29.714  1.00 45.01  ? 211  VAL A CG2 1 
ATOM   1727 N  N   . MET A 1 212 ? -21.082 -24.807 26.773  1.00 40.15  ? 212  MET A N   1 
ATOM   1728 C  CA  . MET A 1 212 ? -21.144 -23.571 26.027  1.00 42.70  ? 212  MET A CA  1 
ATOM   1729 C  C   . MET A 1 212 ? -22.531 -22.959 26.189  1.00 43.26  ? 212  MET A C   1 
ATOM   1730 O  O   . MET A 1 212 ? -22.667 -21.754 26.424  1.00 43.26  ? 212  MET A O   1 
ATOM   1731 C  CB  . MET A 1 212 ? -20.787 -23.927 24.578  1.00 44.09  ? 212  MET A CB  1 
ATOM   1732 C  CG  . MET A 1 212 ? -19.285 -23.764 24.319  1.00 40.51  ? 212  MET A CG  1 
ATOM   1733 S  SD  . MET A 1 212 ? -18.714 -23.589 22.615  1.00 46.09  ? 212  MET A SD  1 
ATOM   1734 C  CE  . MET A 1 212 ? -19.108 -25.206 21.938  1.00 41.31  ? 212  MET A CE  1 
ATOM   1735 N  N   . ASN A 1 213 ? -23.562 -23.807 26.170  1.00 43.41  ? 213  ASN A N   1 
ATOM   1736 C  CA  . ASN A 1 213 ? -24.942 -23.353 26.302  1.00 46.44  ? 213  ASN A CA  1 
ATOM   1737 C  C   . ASN A 1 213 ? -25.282 -22.939 27.729  1.00 47.10  ? 213  ASN A C   1 
ATOM   1738 O  O   . ASN A 1 213 ? -26.166 -22.098 27.934  1.00 49.14  ? 213  ASN A O   1 
ATOM   1739 C  CB  . ASN A 1 213 ? -25.894 -24.450 25.837  1.00 47.24  ? 213  ASN A CB  1 
ATOM   1740 C  CG  . ASN A 1 213 ? -26.252 -24.314 24.385  1.00 50.40  ? 213  ASN A CG  1 
ATOM   1741 O  OD1 . ASN A 1 213 ? -27.201 -23.614 24.042  1.00 56.28  ? 213  ASN A OD1 1 
ATOM   1742 N  ND2 . ASN A 1 213 ? -25.490 -24.969 23.517  1.00 47.17  ? 213  ASN A ND2 1 
ATOM   1743 N  N   . ASP A 1 214 ? -24.612 -23.524 28.722  1.00 45.23  ? 214  ASP A N   1 
ATOM   1744 C  CA  . ASP A 1 214 ? -24.832 -23.103 30.102  1.00 47.75  ? 214  ASP A CA  1 
ATOM   1745 C  C   . ASP A 1 214 ? -24.431 -21.646 30.301  1.00 45.69  ? 214  ASP A C   1 
ATOM   1746 O  O   . ASP A 1 214 ? -25.131 -20.889 30.979  1.00 44.29  ? 214  ASP A O   1 
ATOM   1747 C  CB  . ASP A 1 214 ? -24.053 -24.003 31.056  1.00 45.84  ? 214  ASP A CB  1 
ATOM   1748 C  CG  . ASP A 1 214 ? -24.695 -25.375 31.227  1.00 47.24  ? 214  ASP A CG  1 
ATOM   1749 O  OD1 . ASP A 1 214 ? -25.867 -25.539 30.841  1.00 51.61  ? 214  ASP A OD1 1 
ATOM   1750 O  OD2 . ASP A 1 214 ? -24.019 -26.288 31.741  1.00 55.10  ? 214  ASP A OD2 1 
ATOM   1751 N  N   . LEU A 1 215 ? -23.301 -21.239 29.718  1.00 45.32  ? 215  LEU A N   1 
ATOM   1752 C  CA  . LEU A 1 215 ? -22.883 -19.844 29.800  1.00 43.01  ? 215  LEU A CA  1 
ATOM   1753 C  C   . LEU A 1 215 ? -23.870 -18.942 29.075  1.00 44.08  ? 215  LEU A C   1 
ATOM   1754 O  O   . LEU A 1 215 ? -24.195 -17.842 29.549  1.00 44.05  ? 215  LEU A O   1 
ATOM   1755 C  CB  . LEU A 1 215 ? -21.484 -19.685 29.211  1.00 45.15  ? 215  LEU A CB  1 
ATOM   1756 C  CG  . LEU A 1 215 ? -21.022 -18.237 29.347  1.00 47.78  ? 215  LEU A CG  1 
ATOM   1757 C  CD1 . LEU A 1 215 ? -20.322 -18.089 30.687  1.00 48.90  ? 215  LEU A CD1 1 
ATOM   1758 C  CD2 . LEU A 1 215 ? -20.123 -17.829 28.211  1.00 45.25  ? 215  LEU A CD2 1 
ATOM   1759 N  N   . VAL A 1 216 ? -24.354 -19.387 27.913  1.00 42.83  ? 216  VAL A N   1 
ATOM   1760 C  CA  . VAL A 1 216 ? -25.382 -18.633 27.202  1.00 41.73  ? 216  VAL A CA  1 
ATOM   1761 C  C   . VAL A 1 216 ? -26.600 -18.413 28.096  1.00 46.54  ? 216  VAL A C   1 
ATOM   1762 O  O   . VAL A 1 216 ? -27.132 -17.299 28.185  1.00 46.01  ? 216  VAL A O   1 
ATOM   1763 C  CB  . VAL A 1 216 ? -25.750 -19.347 25.891  1.00 43.11  ? 216  VAL A CB  1 
ATOM   1764 C  CG1 . VAL A 1 216 ? -27.011 -18.757 25.294  1.00 46.41  ? 216  VAL A CG1 1 
ATOM   1765 C  CG2 . VAL A 1 216 ? -24.589 -19.247 24.923  1.00 41.98  ? 216  VAL A CG2 1 
ATOM   1766 N  N   . ASP A 1 217 ? -27.063 -19.468 28.775  1.00 47.77  ? 217  ASP A N   1 
ATOM   1767 C  CA  . ASP A 1 217 ? -28.206 -19.315 29.674  1.00 48.41  ? 217  ASP A CA  1 
ATOM   1768 C  C   . ASP A 1 217 ? -27.953 -18.221 30.707  1.00 48.48  ? 217  ASP A C   1 
ATOM   1769 O  O   . ASP A 1 217 ? -28.819 -17.376 30.966  1.00 45.05  ? 217  ASP A O   1 
ATOM   1770 C  CB  . ASP A 1 217 ? -28.511 -20.640 30.383  1.00 51.57  ? 217  ASP A CB  1 
ATOM   1771 C  CG  . ASP A 1 217 ? -28.985 -21.715 29.437  1.00 53.21  ? 217  ASP A CG  1 
ATOM   1772 O  OD1 . ASP A 1 217 ? -29.534 -21.372 28.373  1.00 54.64  ? 217  ASP A OD1 1 
ATOM   1773 O  OD2 . ASP A 1 217 ? -28.807 -22.906 29.768  1.00 61.82  ? 217  ASP A OD2 1 
ATOM   1774 N  N   . LYS A 1 218 ? -26.771 -18.238 31.322  1.00 43.67  ? 218  LYS A N   1 
ATOM   1775 C  CA  . LYS A 1 218 ? -26.445 -17.257 32.354  1.00 47.40  ? 218  LYS A CA  1 
ATOM   1776 C  C   . LYS A 1 218 ? -26.453 -15.845 31.786  1.00 46.51  ? 218  LYS A C   1 
ATOM   1777 O  O   . LYS A 1 218 ? -26.984 -14.913 32.400  1.00 46.19  ? 218  LYS A O   1 
ATOM   1778 C  CB  . LYS A 1 218 ? -25.077 -17.584 32.954  1.00 45.36  ? 218  LYS A CB  1 
ATOM   1779 C  CG  . LYS A 1 218 ? -24.539 -16.593 34.000  1.00 48.55  ? 218  LYS A CG  1 
ATOM   1780 C  CD  . LYS A 1 218 ? -25.154 -16.770 35.385  1.00 57.73  ? 218  LYS A CD  1 
ATOM   1781 C  CE  . LYS A 1 218 ? -25.159 -15.454 36.167  1.00 57.84  ? 218  LYS A CE  1 
ATOM   1782 N  NZ  . LYS A 1 218 ? -23.793 -14.930 36.546  1.00 50.60  ? 218  LYS A NZ  1 
ATOM   1783 N  N   . ILE A 1 219 ? -25.843 -15.665 30.616  1.00 39.63  ? 219  ILE A N   1 
ATOM   1784 C  CA  . ILE A 1 219 ? -25.811 -14.343 30.003  1.00 38.33  ? 219  ILE A CA  1 
ATOM   1785 C  C   . ILE A 1 219 ? -27.226 -13.832 29.777  1.00 41.31  ? 219  ILE A C   1 
ATOM   1786 O  O   . ILE A 1 219 ? -27.527 -12.657 30.021  1.00 42.60  ? 219  ILE A O   1 
ATOM   1787 C  CB  . ILE A 1 219 ? -25.015 -14.381 28.682  1.00 37.85  ? 219  ILE A CB  1 
ATOM   1788 C  CG1 . ILE A 1 219 ? -23.513 -14.542 28.954  1.00 37.04  ? 219  ILE A CG1 1 
ATOM   1789 C  CG2 . ILE A 1 219 ? -25.341 -13.139 27.859  1.00 35.49  ? 219  ILE A CG2 1 
ATOM   1790 C  CD1 . ILE A 1 219 ? -22.679 -14.794 27.695  1.00 39.07  ? 219  ILE A CD1 1 
ATOM   1791 N  N   . ILE A 1 220 ? -28.120 -14.704 29.304  1.00 40.71  ? 220  ILE A N   1 
ATOM   1792 C  CA  . ILE A 1 220 ? -29.483 -14.264 29.034  1.00 42.84  ? 220  ILE A CA  1 
ATOM   1793 C  C   . ILE A 1 220 ? -30.212 -13.968 30.337  1.00 46.74  ? 220  ILE A C   1 
ATOM   1794 O  O   . ILE A 1 220 ? -30.884 -12.940 30.467  1.00 45.53  ? 220  ILE A O   1 
ATOM   1795 C  CB  . ILE A 1 220 ? -30.239 -15.306 28.195  1.00 46.97  ? 220  ILE A CB  1 
ATOM   1796 C  CG1 . ILE A 1 220 ? -29.725 -15.302 26.753  1.00 42.92  ? 220  ILE A CG1 1 
ATOM   1797 C  CG2 . ILE A 1 220 ? -31.729 -15.000 28.221  1.00 49.19  ? 220  ILE A CG2 1 
ATOM   1798 C  CD1 . ILE A 1 220 ? -30.162 -16.508 25.943  1.00 44.57  ? 220  ILE A CD1 1 
ATOM   1799 N  N   . ALA A 1 221 ? -30.081 -14.859 31.322  1.00 46.74  ? 221  ALA A N   1 
ATOM   1800 C  CA  . ALA A 1 221 ? -30.785 -14.672 32.590  1.00 52.52  ? 221  ALA A CA  1 
ATOM   1801 C  C   . ALA A 1 221 ? -30.342 -13.389 33.282  1.00 50.85  ? 221  ALA A C   1 
ATOM   1802 O  O   . ALA A 1 221 ? -31.174 -12.611 33.764  1.00 52.87  ? 221  ALA A O   1 
ATOM   1803 C  CB  . ALA A 1 221 ? -30.561 -15.879 33.503  1.00 51.26  ? 221  ALA A CB  1 
ATOM   1804 N  N   . ASP A 1 222 ? -29.028 -13.152 33.350  1.00 49.34  ? 222  ASP A N   1 
ATOM   1805 C  CA  . ASP A 1 222 ? -28.534 -11.927 33.972  1.00 50.04  ? 222  ASP A CA  1 
ATOM   1806 C  C   . ASP A 1 222 ? -29.099 -10.681 33.306  1.00 50.63  ? 222  ASP A C   1 
ATOM   1807 O  O   . ASP A 1 222 ? -29.446 -9.712  33.990  1.00 50.43  ? 222  ASP A O   1 
ATOM   1808 C  CB  . ASP A 1 222 ? -27.008 -11.890 33.948  1.00 45.92  ? 222  ASP A CB  1 
ATOM   1809 C  CG  . ASP A 1 222 ? -26.389 -12.973 34.794  1.00 52.18  ? 222  ASP A CG  1 
ATOM   1810 O  OD1 . ASP A 1 222 ? -25.148 -13.110 34.754  1.00 52.43  ? 222  ASP A OD1 1 
ATOM   1811 O  OD2 . ASP A 1 222 ? -27.138 -13.658 35.527  1.00 51.67  ? 222  ASP A OD2 1 
ATOM   1812 N  N   . ARG A 1 223 ? -29.180 -10.669 31.973  1.00 44.77  ? 223  ARG A N   1 
ATOM   1813 C  CA  . ARG A 1 223 ? -29.660 -9.468  31.300  1.00 43.21  ? 223  ARG A CA  1 
ATOM   1814 C  C   . ARG A 1 223 ? -31.138 -9.230  31.590  1.00 48.89  ? 223  ARG A C   1 
ATOM   1815 O  O   . ARG A 1 223 ? -31.552 -8.097  31.854  1.00 47.72  ? 223  ARG A O   1 
ATOM   1816 C  CB  . ARG A 1 223 ? -29.441 -9.566  29.787  1.00 44.87  ? 223  ARG A CB  1 
ATOM   1817 C  CG  . ARG A 1 223 ? -30.087 -8.414  29.020  1.00 38.69  ? 223  ARG A CG  1 
ATOM   1818 C  CD  . ARG A 1 223 ? -29.481 -7.066  29.406  1.00 42.72  ? 223  ARG A CD  1 
ATOM   1819 N  NE  . ARG A 1 223 ? -28.034 -7.066  29.211  1.00 42.31  ? 223  ARG A NE  1 
ATOM   1820 C  CZ  . ARG A 1 223 ? -27.421 -6.593  28.132  1.00 42.88  ? 223  ARG A CZ  1 
ATOM   1821 N  NH1 . ARG A 1 223 ? -28.095 -6.027  27.140  1.00 36.48  ? 223  ARG A NH1 1 
ATOM   1822 N  NH2 . ARG A 1 223 ? -26.099 -6.706  28.038  1.00 38.94  ? 223  ARG A NH2 1 
ATOM   1823 N  N   . LYS A 1 224 ? -31.960 -10.279 31.509  1.00 44.80  ? 224  LYS A N   1 
ATOM   1824 C  CA  . LYS A 1 224 ? -33.398 -10.051 31.644  1.00 54.40  ? 224  LYS A CA  1 
ATOM   1825 C  C   . LYS A 1 224 ? -33.804 -9.754  33.081  1.00 58.14  ? 224  LYS A C   1 
ATOM   1826 O  O   . LYS A 1 224 ? -34.888 -9.205  33.306  1.00 58.63  ? 224  LYS A O   1 
ATOM   1827 C  CB  . LYS A 1 224 ? -34.196 -11.238 31.093  1.00 57.05  ? 224  LYS A CB  1 
ATOM   1828 C  CG  . LYS A 1 224 ? -33.891 -12.595 31.693  1.00 59.23  ? 224  LYS A CG  1 
ATOM   1829 C  CD  . LYS A 1 224 ? -34.705 -13.672 30.963  1.00 64.46  ? 224  LYS A CD  1 
ATOM   1830 C  CE  . LYS A 1 224 ? -34.043 -15.047 30.989  1.00 61.89  ? 224  LYS A CE  1 
ATOM   1831 N  NZ  . LYS A 1 224 ? -34.463 -15.857 29.805  1.00 65.56  ? 224  LYS A NZ  1 
ATOM   1832 N  N   . ALA A 1 225 ? -32.958 -10.086 34.047  1.00 54.71  ? 225  ALA A N   1 
ATOM   1833 C  CA  . ALA A 1 225 ? -33.181 -9.730  35.440  1.00 58.95  ? 225  ALA A CA  1 
ATOM   1834 C  C   . ALA A 1 225 ? -32.471 -8.442  35.834  1.00 64.26  ? 225  ALA A C   1 
ATOM   1835 O  O   . ALA A 1 225 ? -32.615 -7.995  36.975  1.00 71.23  ? 225  ALA A O   1 
ATOM   1836 C  CB  . ALA A 1 225 ? -32.719 -10.872 36.349  1.00 58.61  ? 225  ALA A CB  1 
ATOM   1837 N  N   . SER A 1 226 ? -31.716 -7.838  34.920  1.00 61.14  ? 226  SER A N   1 
ATOM   1838 C  CA  . SER A 1 226 ? -30.869 -6.704  35.257  1.00 69.40  ? 226  SER A CA  1 
ATOM   1839 C  C   . SER A 1 226 ? -31.695 -5.448  35.498  1.00 79.06  ? 226  SER A C   1 
ATOM   1840 O  O   . SER A 1 226 ? -32.793 -5.284  34.959  1.00 75.31  ? 226  SER A O   1 
ATOM   1841 C  CB  . SER A 1 226 ? -29.857 -6.441  34.139  1.00 70.10  ? 226  SER A CB  1 
ATOM   1842 O  OG  . SER A 1 226 ? -29.170 -5.220  34.350  1.00 77.57  ? 226  SER A OG  1 
ATOM   1843 N  N   . GLY A 1 227 ? -31.142 -4.552  36.315  1.00 83.34  ? 227  GLY A N   1 
ATOM   1844 C  CA  . GLY A 1 227 ? -31.733 -3.251  36.562  1.00 86.14  ? 227  GLY A CA  1 
ATOM   1845 C  C   . GLY A 1 227 ? -30.900 -2.120  35.990  1.00 92.45  ? 227  GLY A C   1 
ATOM   1846 O  O   . GLY A 1 227 ? -31.034 -0.965  36.408  1.00 94.00  ? 227  GLY A O   1 
ATOM   1847 N  N   . GLU A 1 228 ? -30.026 -2.449  35.039  1.00 91.81  ? 228  GLU A N   1 
ATOM   1848 C  CA  . GLU A 1 228 ? -29.208 -1.477  34.323  1.00 91.98  ? 228  GLU A CA  1 
ATOM   1849 C  C   . GLU A 1 228 ? -29.630 -1.453  32.861  1.00 89.58  ? 228  GLU A C   1 
ATOM   1850 O  O   . GLU A 1 228 ? -29.761 -2.508  32.230  1.00 89.01  ? 228  GLU A O   1 
ATOM   1851 C  CB  . GLU A 1 228 ? -27.718 -1.815  34.432  1.00 93.97  ? 228  GLU A CB  1 
ATOM   1852 C  CG  . GLU A 1 228 ? -27.236 -2.176  35.835  1.00 96.90  ? 228  GLU A CG  1 
ATOM   1853 C  CD  . GLU A 1 228 ? -27.343 -1.019  36.815  1.00 100.87 ? 228  GLU A CD  1 
ATOM   1854 O  OE1 . GLU A 1 228 ? -27.106 0.137   36.403  1.00 100.72 ? 228  GLU A OE1 1 
ATOM   1855 O  OE2 . GLU A 1 228 ? -27.659 -1.267  38.000  1.00 103.05 ? 228  GLU A OE2 1 
ATOM   1856 N  N   . GLN A 1 229 ? -29.841 -0.254  32.324  1.00 90.36  ? 229  GLN A N   1 
ATOM   1857 C  CA  . GLN A 1 229 ? -30.263 -0.101  30.935  1.00 85.32  ? 229  GLN A CA  1 
ATOM   1858 C  C   . GLN A 1 229 ? -29.043 -0.170  30.026  1.00 80.58  ? 229  GLN A C   1 
ATOM   1859 O  O   . GLN A 1 229 ? -28.240 0.768   29.978  1.00 80.29  ? 229  GLN A O   1 
ATOM   1860 C  CB  . GLN A 1 229 ? -31.015 1.212   30.746  1.00 88.63  ? 229  GLN A CB  1 
ATOM   1861 C  CG  . GLN A 1 229 ? -32.345 1.252   31.467  1.00 93.80  ? 229  GLN A CG  1 
ATOM   1862 C  CD  . GLN A 1 229 ? -33.440 0.572   30.674  1.00 96.80  ? 229  GLN A CD  1 
ATOM   1863 O  OE1 . GLN A 1 229 ? -33.867 -0.534  31.004  1.00 97.29  ? 229  GLN A OE1 1 
ATOM   1864 N  NE2 . GLN A 1 229 ? -33.897 1.230   29.614  1.00 102.66 ? 229  GLN A NE2 1 
ATOM   1865 N  N   . SER A 1 230 ? -28.904 -1.276  29.304  1.00 72.98  ? 230  SER A N   1 
ATOM   1866 C  CA  . SER A 1 230 ? -27.819 -1.456  28.353  1.00 61.97  ? 230  SER A CA  1 
ATOM   1867 C  C   . SER A 1 230 ? -28.300 -1.152  26.938  1.00 58.30  ? 230  SER A C   1 
ATOM   1868 O  O   . SER A 1 230 ? -29.499 -1.147  26.644  1.00 54.12  ? 230  SER A O   1 
ATOM   1869 C  CB  . SER A 1 230 ? -27.262 -2.884  28.422  1.00 59.66  ? 230  SER A CB  1 
ATOM   1870 O  OG  . SER A 1 230 ? -26.454 -3.081  29.576  1.00 62.21  ? 230  SER A OG  1 
ATOM   1871 N  N   . ASP A 1 231 ? -27.333 -0.880  26.059  1.00 52.00  ? 231  ASP A N   1 
ATOM   1872 C  CA  . ASP A 1 231 ? -27.579 -0.704  24.642  1.00 52.11  ? 231  ASP A CA  1 
ATOM   1873 C  C   . ASP A 1 231 ? -26.413 -1.376  23.917  1.00 51.42  ? 231  ASP A C   1 
ATOM   1874 O  O   . ASP A 1 231 ? -25.517 -0.728  23.380  1.00 55.37  ? 231  ASP A O   1 
ATOM   1875 C  CB  . ASP A 1 231 ? -27.696 0.773   24.261  1.00 54.65  ? 231  ASP A CB  1 
ATOM   1876 C  CG  . ASP A 1 231 ? -28.070 0.976   22.798  1.00 60.37  ? 231  ASP A CG  1 
ATOM   1877 O  OD1 . ASP A 1 231 ? -28.613 0.036   22.173  1.00 61.19  ? 231  ASP A OD1 1 
ATOM   1878 O  OD2 . ASP A 1 231 ? -27.821 2.080   22.271  1.00 68.02  ? 231  ASP A OD2 1 
ATOM   1879 N  N   . ASP A 1 232 ? -26.399 -2.708  23.919  1.00 41.49  ? 232  ASP A N   1 
ATOM   1880 C  CA  . ASP A 1 232 ? -25.278 -3.395  23.289  1.00 40.97  ? 232  ASP A CA  1 
ATOM   1881 C  C   . ASP A 1 232 ? -25.757 -4.445  22.297  1.00 42.13  ? 232  ASP A C   1 
ATOM   1882 O  O   . ASP A 1 232 ? -26.925 -4.445  21.884  1.00 38.23  ? 232  ASP A O   1 
ATOM   1883 C  CB  . ASP A 1 232 ? -24.360 -4.010  24.360  1.00 37.23  ? 232  ASP A CB  1 
ATOM   1884 C  CG  . ASP A 1 232 ? -25.090 -4.949  25.325  1.00 40.92  ? 232  ASP A CG  1 
ATOM   1885 O  OD1 . ASP A 1 232 ? -26.213 -5.412  25.023  1.00 38.56  ? 232  ASP A OD1 1 
ATOM   1886 O  OD2 . ASP A 1 232 ? -24.515 -5.245  26.404  1.00 39.07  ? 232  ASP A OD2 1 
ATOM   1887 N  N   . LEU A 1 233 ? -24.853 -5.332  21.891  1.00 40.00  ? 233  LEU A N   1 
ATOM   1888 C  CA  . LEU A 1 233 ? -25.207 -6.376  20.939  1.00 36.02  ? 233  LEU A CA  1 
ATOM   1889 C  C   . LEU A 1 233 ? -26.372 -7.215  21.454  1.00 37.27  ? 233  LEU A C   1 
ATOM   1890 O  O   . LEU A 1 233 ? -27.333 -7.490  20.723  1.00 35.91  ? 233  LEU A O   1 
ATOM   1891 C  CB  . LEU A 1 233 ? -23.978 -7.247  20.676  1.00 34.28  ? 233  LEU A CB  1 
ATOM   1892 C  CG  . LEU A 1 233 ? -24.073 -8.414  19.702  1.00 34.42  ? 233  LEU A CG  1 
ATOM   1893 C  CD1 . LEU A 1 233 ? -24.455 -7.970  18.281  1.00 36.72  ? 233  LEU A CD1 1 
ATOM   1894 C  CD2 . LEU A 1 233 ? -22.713 -9.125  19.678  1.00 38.67  ? 233  LEU A CD2 1 
ATOM   1895 N  N   . LEU A 1 234 ? -26.307 -7.623  22.722  1.00 33.54  ? 234  LEU A N   1 
ATOM   1896 C  CA  . LEU A 1 234 ? -27.391 -8.413  23.299  1.00 32.14  ? 234  LEU A CA  1 
ATOM   1897 C  C   . LEU A 1 234 ? -28.706 -7.636  23.296  1.00 36.55  ? 234  LEU A C   1 
ATOM   1898 O  O   . LEU A 1 234 ? -29.776 -8.214  23.068  1.00 36.63  ? 234  LEU A O   1 
ATOM   1899 C  CB  . LEU A 1 234 ? -27.022 -8.843  24.722  1.00 35.60  ? 234  LEU A CB  1 
ATOM   1900 C  CG  . LEU A 1 234 ? -28.006 -9.782  25.424  1.00 34.11  ? 234  LEU A CG  1 
ATOM   1901 C  CD1 . LEU A 1 234 ? -28.263 -11.020 24.605  1.00 35.10  ? 234  LEU A CD1 1 
ATOM   1902 C  CD2 . LEU A 1 234 ? -27.469 -10.158 26.819  1.00 36.48  ? 234  LEU A CD2 1 
ATOM   1903 N  N   . THR A 1 235 ? -28.652 -6.329  23.567  1.00 36.97  ? 235  THR A N   1 
ATOM   1904 C  CA  . THR A 1 235 ? -29.871 -5.522  23.498  1.00 38.86  ? 235  THR A CA  1 
ATOM   1905 C  C   . THR A 1 235 ? -30.520 -5.665  22.139  1.00 39.54  ? 235  THR A C   1 
ATOM   1906 O  O   . THR A 1 235 ? -31.742 -5.834  22.029  1.00 37.45  ? 235  THR A O   1 
ATOM   1907 C  CB  . THR A 1 235 ? -29.565 -4.049  23.764  1.00 37.71  ? 235  THR A CB  1 
ATOM   1908 O  OG1 . THR A 1 235 ? -28.878 -3.927  25.015  1.00 38.05  ? 235  THR A OG1 1 
ATOM   1909 C  CG2 . THR A 1 235 ? -30.878 -3.242  23.802  1.00 38.92  ? 235  THR A CG2 1 
ATOM   1910 N  N   . HIS A 1 236 ? -29.706 -5.632  21.088  1.00 35.97  ? 236  HIS A N   1 
ATOM   1911 C  CA  . HIS A 1 236 ? -30.252 -5.709  19.744  1.00 38.81  ? 236  HIS A CA  1 
ATOM   1912 C  C   . HIS A 1 236 ? -30.808 -7.103  19.477  1.00 40.51  ? 236  HIS A C   1 
ATOM   1913 O  O   . HIS A 1 236 ? -31.869 -7.245  18.851  1.00 36.96  ? 236  HIS A O   1 
ATOM   1914 C  CB  . HIS A 1 236 ? -29.163 -5.379  18.734  1.00 37.02  ? 236  HIS A CB  1 
ATOM   1915 C  CG  . HIS A 1 236 ? -28.971 -3.914  18.514  1.00 44.58  ? 236  HIS A CG  1 
ATOM   1916 N  ND1 . HIS A 1 236 ? -28.263 -3.136  19.408  1.00 43.39  ? 236  HIS A ND1 1 
ATOM   1917 C  CD2 . HIS A 1 236 ? -29.402 -3.073  17.541  1.00 45.67  ? 236  HIS A CD2 1 
ATOM   1918 C  CE1 . HIS A 1 236 ? -28.238 -1.886  18.978  1.00 45.19  ? 236  HIS A CE1 1 
ATOM   1919 N  NE2 . HIS A 1 236 ? -28.923 -1.819  17.851  1.00 43.78  ? 236  HIS A NE2 1 
ATOM   1920 N  N   . MET A 1 237 ? -30.111 -8.157  19.930  1.00 35.39  ? 237  MET A N   1 
ATOM   1921 C  CA  . MET A 1 237 ? -30.671 -9.496  19.743  1.00 37.25  ? 237  MET A CA  1 
ATOM   1922 C  C   . MET A 1 237 ? -32.030 -9.629  20.408  1.00 39.27  ? 237  MET A C   1 
ATOM   1923 O  O   . MET A 1 237 ? -32.936 -10.266 19.857  1.00 38.34  ? 237  MET A O   1 
ATOM   1924 C  CB  . MET A 1 237 ? -29.792 -10.651 20.258  1.00 37.79  ? 237  MET A CB  1 
ATOM   1925 C  CG  . MET A 1 237 ? -28.548 -11.011 19.469  1.00 38.91  ? 237  MET A CG  1 
ATOM   1926 S  SD  . MET A 1 237 ? -27.344 -11.871 20.489  1.00 35.65  ? 237  MET A SD  1 
ATOM   1927 C  CE  . MET A 1 237 ? -25.860 -11.877 19.471  1.00 31.91  ? 237  MET A CE  1 
ATOM   1928 N  N   . LEU A 1 238 ? -32.175 -9.072  21.608  1.00 37.28  ? 238  LEU A N   1 
ATOM   1929 C  CA  . LEU A 1 238 ? -33.391 -9.302  22.376  1.00 38.07  ? 238  LEU A CA  1 
ATOM   1930 C  C   . LEU A 1 238 ? -34.510 -8.371  21.947  1.00 43.54  ? 238  LEU A C   1 
ATOM   1931 O  O   . LEU A 1 238 ? -35.685 -8.712  22.104  1.00 42.93  ? 238  LEU A O   1 
ATOM   1932 C  CB  . LEU A 1 238 ? -33.117 -9.136  23.880  1.00 37.11  ? 238  LEU A CB  1 
ATOM   1933 C  CG  . LEU A 1 238 ? -32.067 -10.044 24.539  1.00 40.74  ? 238  LEU A CG  1 
ATOM   1934 C  CD1 . LEU A 1 238 ? -31.809 -9.644  26.013  1.00 34.14  ? 238  LEU A CD1 1 
ATOM   1935 C  CD2 . LEU A 1 238 ? -32.498 -11.491 24.451  1.00 41.97  ? 238  LEU A CD2 1 
ATOM   1936 N  N   . ASN A 1 239 ? -34.185 -7.202  21.405  1.00 39.41  ? 239  ASN A N   1 
ATOM   1937 C  CA  . ASN A 1 239 ? -35.208 -6.197  21.158  1.00 41.35  ? 239  ASN A CA  1 
ATOM   1938 C  C   . ASN A 1 239 ? -35.297 -5.727  19.716  1.00 46.28  ? 239  ASN A C   1 
ATOM   1939 O  O   . ASN A 1 239 ? -36.360 -5.235  19.309  1.00 42.98  ? 239  ASN A O   1 
ATOM   1940 C  CB  . ASN A 1 239 ? -34.969 -4.987  22.067  1.00 43.59  ? 239  ASN A CB  1 
ATOM   1941 C  CG  . ASN A 1 239 ? -34.966 -5.373  23.528  1.00 46.84  ? 239  ASN A CG  1 
ATOM   1942 O  OD1 . ASN A 1 239 ? -33.929 -5.332  24.189  1.00 50.20  ? 239  ASN A OD1 1 
ATOM   1943 N  ND2 . ASN A 1 239 ? -36.123 -5.784  24.036  1.00 50.19  ? 239  ASN A ND2 1 
ATOM   1944 N  N   . GLY A 1 240 ? -34.242 -5.889  18.924  1.00 39.32  ? 240  GLY A N   1 
ATOM   1945 C  CA  . GLY A 1 240 ? -34.253 -5.329  17.589  1.00 37.89  ? 240  GLY A CA  1 
ATOM   1946 C  C   . GLY A 1 240 ? -35.300 -5.979  16.707  1.00 41.11  ? 240  GLY A C   1 
ATOM   1947 O  O   . GLY A 1 240 ? -35.587 -7.174  16.811  1.00 40.86  ? 240  GLY A O   1 
ATOM   1948 N  N   . LYS A 1 241 ? -35.855 -5.179  15.801  1.00 40.07  ? 241  LYS A N   1 
ATOM   1949 C  CA  . LYS A 1 241 ? -36.907 -5.619  14.900  1.00 42.01  ? 241  LYS A CA  1 
ATOM   1950 C  C   . LYS A 1 241 ? -36.403 -5.519  13.472  1.00 41.59  ? 241  LYS A C   1 
ATOM   1951 O  O   . LYS A 1 241 ? -35.839 -4.490  13.084  1.00 41.91  ? 241  LYS A O   1 
ATOM   1952 C  CB  . LYS A 1 241 ? -38.165 -4.767  15.067  1.00 47.68  ? 241  LYS A CB  1 
ATOM   1953 C  CG  . LYS A 1 241 ? -38.715 -4.756  16.482  1.00 51.65  ? 241  LYS A CG  1 
ATOM   1954 C  CD  . LYS A 1 241 ? -39.032 -6.157  16.961  1.00 49.59  ? 241  LYS A CD  1 
ATOM   1955 C  CE  . LYS A 1 241 ? -39.994 -6.119  18.148  1.00 59.43  ? 241  LYS A CE  1 
ATOM   1956 N  NZ  . LYS A 1 241 ? -39.370 -6.684  19.386  1.00 57.06  ? 241  LYS A NZ  1 
ATOM   1957 N  N   . ASP A 1 242 ? -36.603 -6.577  12.707  1.00 41.25  ? 242  ASP A N   1 
ATOM   1958 C  CA  . ASP A 1 242 ? -36.184 -6.591  11.307  1.00 44.19  ? 242  ASP A CA  1 
ATOM   1959 C  C   . ASP A 1 242 ? -37.119 -5.680  10.520  1.00 50.74  ? 242  ASP A C   1 
ATOM   1960 O  O   . ASP A 1 242 ? -38.343 -5.870  10.572  1.00 51.75  ? 242  ASP A O   1 
ATOM   1961 C  CB  . ASP A 1 242 ? -36.199 -8.031  10.767  1.00 42.16  ? 242  ASP A CB  1 
ATOM   1962 C  CG  . ASP A 1 242 ? -36.018 -8.117  9.243   1.00 44.67  ? 242  ASP A CG  1 
ATOM   1963 O  OD1 . ASP A 1 242 ? -35.534 -7.153  8.626   1.00 45.17  ? 242  ASP A OD1 1 
ATOM   1964 O  OD2 . ASP A 1 242 ? -36.303 -9.191  8.672   1.00 42.33  ? 242  ASP A OD2 1 
ATOM   1965 N  N   . PRO A 1 243 ? -36.613 -4.654  9.840   1.00 51.41  ? 243  PRO A N   1 
ATOM   1966 C  CA  . PRO A 1 243 ? -37.516 -3.825  9.026   1.00 55.87  ? 243  PRO A CA  1 
ATOM   1967 C  C   . PRO A 1 243 ? -38.243 -4.603  7.937   1.00 51.84  ? 243  PRO A C   1 
ATOM   1968 O  O   . PRO A 1 243 ? -39.372 -4.238  7.588   1.00 65.96  ? 243  PRO A O   1 
ATOM   1969 C  CB  . PRO A 1 243 ? -36.581 -2.748  8.454   1.00 58.75  ? 243  PRO A CB  1 
ATOM   1970 C  CG  . PRO A 1 243 ? -35.197 -3.327  8.566   1.00 56.99  ? 243  PRO A CG  1 
ATOM   1971 C  CD  . PRO A 1 243 ? -35.217 -4.182  9.790   1.00 50.20  ? 243  PRO A CD  1 
ATOM   1972 N  N   . GLU A 1 244 ? -37.656 -5.680  7.407   1.00 57.50  ? 244  GLU A N   1 
ATOM   1973 C  CA  . GLU A 1 244 ? -38.297 -6.420  6.314   1.00 52.85  ? 244  GLU A CA  1 
ATOM   1974 C  C   . GLU A 1 244 ? -39.436 -7.307  6.821   1.00 62.63  ? 244  GLU A C   1 
ATOM   1975 O  O   . GLU A 1 244 ? -40.610 -7.059  6.524   1.00 65.69  ? 244  GLU A O   1 
ATOM   1976 C  CB  . GLU A 1 244 ? -37.254 -7.240  5.541   1.00 55.12  ? 244  GLU A CB  1 
ATOM   1977 C  CG  . GLU A 1 244 ? -37.870 -8.317  4.652   1.00 59.53  ? 244  GLU A CG  1 
ATOM   1978 C  CD  . GLU A 1 244 ? -36.843 -9.185  3.938   1.00 66.21  ? 244  GLU A CD  1 
ATOM   1979 O  OE1 . GLU A 1 244 ? -35.631 -9.080  4.237   1.00 61.52  ? 244  GLU A OE1 1 
ATOM   1980 O  OE2 . GLU A 1 244 ? -37.261 -9.992  3.077   1.00 72.93  ? 244  GLU A OE2 1 
ATOM   1981 N  N   . THR A 1 245 ? -39.109 -8.358  7.585   1.00 60.35  ? 245  THR A N   1 
ATOM   1982 C  CA  . THR A 1 245 ? -40.136 -9.246  8.130   1.00 54.75  ? 245  THR A CA  1 
ATOM   1983 C  C   . THR A 1 245 ? -40.904 -8.628  9.297   1.00 56.47  ? 245  THR A C   1 
ATOM   1984 O  O   . THR A 1 245 ? -41.972 -9.142  9.644   1.00 63.25  ? 245  THR A O   1 
ATOM   1985 C  CB  . THR A 1 245 ? -39.520 -10.587 8.572   1.00 56.61  ? 245  THR A CB  1 
ATOM   1986 O  OG1 . THR A 1 245 ? -38.573 -10.386 9.639   1.00 45.83  ? 245  THR A OG1 1 
ATOM   1987 C  CG2 . THR A 1 245 ? -38.820 -11.282 7.391   1.00 56.93  ? 245  THR A CG2 1 
ATOM   1988 N  N   . GLY A 1 246 ? -40.400 -7.549  9.900   1.00 57.03  ? 246  GLY A N   1 
ATOM   1989 C  CA  . GLY A 1 246 ? -41.077 -6.858  10.985  1.00 53.83  ? 246  GLY A CA  1 
ATOM   1990 C  C   . GLY A 1 246 ? -40.904 -7.477  12.359  1.00 57.45  ? 246  GLY A C   1 
ATOM   1991 O  O   . GLY A 1 246 ? -41.144 -6.795  13.367  1.00 52.60  ? 246  GLY A O   1 
ATOM   1992 N  N   . GLU A 1 247 ? -40.454 -8.797  12.438  1.00 57.03  ? 247  GLU A N   1 
ATOM   1993 C  CA  . GLU A 1 247 ? -40.281 -9.703  13.561  1.00 46.97  ? 247  GLU A CA  1 
ATOM   1994 C  C   . GLU A 1 247 ? -38.937 -9.486  14.261  1.00 46.74  ? 247  GLU A C   1 
ATOM   1995 O  O   . GLU A 1 247 ? -37.957 -9.068  13.636  1.00 41.33  ? 247  GLU A O   1 
ATOM   1996 C  CB  . GLU A 1 247 ? -40.373 -11.158 13.092  1.00 52.25  ? 247  GLU A CB  1 
ATOM   1997 C  CG  . GLU A 1 247 ? -41.378 -11.417 11.954  1.00 53.98  ? 247  GLU A CG  1 
ATOM   1998 C  CD  . GLU A 1 247 ? -41.234 -12.806 11.342  1.00 59.37  ? 247  GLU A CD  1 
ATOM   1999 O  OE1 . GLU A 1 247 ? -40.183 -13.452 11.549  1.00 54.80  ? 247  GLU A OE1 1 
ATOM   2000 O  OE2 . GLU A 1 247 ? -42.176 -13.261 10.654  1.00 60.58  ? 247  GLU A OE2 1 
ATOM   2001 N  N   . PRO A 1 248 ? -38.880 -9.759  15.557  1.00 45.59  ? 248  PRO A N   1 
ATOM   2002 C  CA  . PRO A 1 248 ? -37.595 -9.889  16.244  1.00 38.14  ? 248  PRO A CA  1 
ATOM   2003 C  C   . PRO A 1 248 ? -37.106 -11.324 16.088  1.00 40.19  ? 248  PRO A C   1 
ATOM   2004 O  O   . PRO A 1 248 ? -37.825 -12.206 15.609  1.00 39.60  ? 248  PRO A O   1 
ATOM   2005 C  CB  . PRO A 1 248 ? -37.953 -9.564  17.698  1.00 42.93  ? 248  PRO A CB  1 
ATOM   2006 C  CG  . PRO A 1 248 ? -39.326 -10.148 17.837  1.00 46.43  ? 248  PRO A CG  1 
ATOM   2007 C  CD  . PRO A 1 248 ? -40.014 -9.895  16.492  1.00 48.94  ? 248  PRO A CD  1 
ATOM   2008 N  N   . LEU A 1 249 ? -35.844 -11.537 16.447  1.00 33.55  ? 249  LEU A N   1 
ATOM   2009 C  CA  . LEU A 1 249 ? -35.344 -12.906 16.497  1.00 37.54  ? 249  LEU A CA  1 
ATOM   2010 C  C   . LEU A 1 249 ? -36.119 -13.688 17.543  1.00 39.37  ? 249  LEU A C   1 
ATOM   2011 O  O   . LEU A 1 249 ? -36.535 -13.139 18.562  1.00 38.70  ? 249  LEU A O   1 
ATOM   2012 C  CB  . LEU A 1 249 ? -33.856 -12.939 16.850  1.00 36.32  ? 249  LEU A CB  1 
ATOM   2013 C  CG  . LEU A 1 249 ? -32.954 -12.149 15.908  1.00 34.89  ? 249  LEU A CG  1 
ATOM   2014 C  CD1 . LEU A 1 249 ? -31.501 -12.345 16.341  1.00 36.93  ? 249  LEU A CD1 1 
ATOM   2015 C  CD2 . LEU A 1 249 ? -33.158 -12.601 14.474  1.00 35.02  ? 249  LEU A CD2 1 
ATOM   2016 N  N   . ASP A 1 250 ? -36.311 -14.983 17.299  1.00 40.09  ? 250  ASP A N   1 
ATOM   2017 C  CA  . ASP A 1 250 ? -36.936 -15.801 18.330  1.00 43.70  ? 250  ASP A CA  1 
ATOM   2018 C  C   . ASP A 1 250 ? -35.870 -16.364 19.271  1.00 43.43  ? 250  ASP A C   1 
ATOM   2019 O  O   . ASP A 1 250 ? -34.666 -16.255 19.028  1.00 40.22  ? 250  ASP A O   1 
ATOM   2020 C  CB  . ASP A 1 250 ? -37.818 -16.892 17.699  1.00 47.91  ? 250  ASP A CB  1 
ATOM   2021 C  CG  . ASP A 1 250 ? -37.037 -17.985 16.983  1.00 49.24  ? 250  ASP A CG  1 
ATOM   2022 O  OD1 . ASP A 1 250 ? -35.819 -18.165 17.198  1.00 46.10  ? 250  ASP A OD1 1 
ATOM   2023 O  OD2 . ASP A 1 250 ? -37.665 -18.657 16.141  1.00 59.70  ? 250  ASP A OD2 1 
ATOM   2024 N  N   . ASP A 1 251 ? -36.335 -16.936 20.384  1.00 42.06  ? 251  ASP A N   1 
ATOM   2025 C  CA  . ASP A 1 251 ? -35.433 -17.366 21.448  1.00 45.08  ? 251  ASP A CA  1 
ATOM   2026 C  C   . ASP A 1 251 ? -34.405 -18.370 20.944  1.00 43.10  ? 251  ASP A C   1 
ATOM   2027 O  O   . ASP A 1 251 ? -33.226 -18.307 21.322  1.00 39.88  ? 251  ASP A O   1 
ATOM   2028 C  CB  . ASP A 1 251 ? -36.256 -17.963 22.588  1.00 45.46  ? 251  ASP A CB  1 
ATOM   2029 C  CG  . ASP A 1 251 ? -36.783 -16.904 23.528  1.00 52.79  ? 251  ASP A CG  1 
ATOM   2030 O  OD1 . ASP A 1 251 ? -37.175 -17.257 24.657  1.00 62.11  ? 251  ASP A OD1 1 
ATOM   2031 O  OD2 . ASP A 1 251 ? -36.771 -15.712 23.151  1.00 56.78  ? 251  ASP A OD2 1 
ATOM   2032 N  N   . GLU A 1 252 ? -34.824 -19.312 20.094  1.00 39.50  ? 252  GLU A N   1 
ATOM   2033 C  CA  . GLU A 1 252 ? -33.876 -20.337 19.651  1.00 40.78  ? 252  GLU A CA  1 
ATOM   2034 C  C   . GLU A 1 252 ? -32.750 -19.720 18.822  1.00 37.61  ? 252  GLU A C   1 
ATOM   2035 O  O   . GLU A 1 252 ? -31.569 -20.040 19.021  1.00 36.74  ? 252  GLU A O   1 
ATOM   2036 C  CB  . GLU A 1 252 ? -34.589 -21.432 18.848  1.00 41.44  ? 252  GLU A CB  1 
ATOM   2037 C  CG  . GLU A 1 252 ? -33.616 -22.491 18.318  1.00 40.85  ? 252  GLU A CG  1 
ATOM   2038 C  CD  . GLU A 1 252 ? -34.245 -23.518 17.377  1.00 51.67  ? 252  GLU A CD  1 
ATOM   2039 O  OE1 . GLU A 1 252 ? -34.401 -23.217 16.172  1.00 56.56  ? 252  GLU A OE1 1 
ATOM   2040 O  OE2 . GLU A 1 252 ? -34.581 -24.628 17.840  1.00 57.75  ? 252  GLU A OE2 1 
ATOM   2041 N  N   . ASN A 1 253 ? -33.089 -18.818 17.905  1.00 33.95  ? 253  ASN A N   1 
ATOM   2042 C  CA  . ASN A 1 253 ? -32.042 -18.185 17.105  1.00 32.17  ? 253  ASN A CA  1 
ATOM   2043 C  C   . ASN A 1 253 ? -31.153 -17.263 17.945  1.00 36.56  ? 253  ASN A C   1 
ATOM   2044 O  O   . ASN A 1 253 ? -29.939 -17.175 17.704  1.00 34.54  ? 253  ASN A O   1 
ATOM   2045 C  CB  . ASN A 1 253 ? -32.658 -17.415 15.943  1.00 34.09  ? 253  ASN A CB  1 
ATOM   2046 C  CG  . ASN A 1 253 ? -31.605 -16.897 14.990  1.00 32.49  ? 253  ASN A CG  1 
ATOM   2047 O  OD1 . ASN A 1 253 ? -31.312 -15.706 14.971  1.00 35.22  ? 253  ASN A OD1 1 
ATOM   2048 N  ND2 . ASN A 1 253 ? -31.029 -17.792 14.202  1.00 31.80  ? 253  ASN A ND2 1 
ATOM   2049 N  N   . ILE A 1 254 ? -31.730 -16.546 18.915  1.00 34.50  ? 254  ILE A N   1 
ATOM   2050 C  CA  . ILE A 1 254 ? -30.913 -15.708 19.795  1.00 33.30  ? 254  ILE A CA  1 
ATOM   2051 C  C   . ILE A 1 254 ? -29.797 -16.526 20.430  1.00 33.35  ? 254  ILE A C   1 
ATOM   2052 O  O   . ILE A 1 254 ? -28.635 -16.096 20.473  1.00 33.31  ? 254  ILE A O   1 
ATOM   2053 C  CB  . ILE A 1 254 ? -31.789 -15.028 20.866  1.00 36.65  ? 254  ILE A CB  1 
ATOM   2054 C  CG1 . ILE A 1 254 ? -32.609 -13.902 20.236  1.00 39.20  ? 254  ILE A CG1 1 
ATOM   2055 C  CG2 . ILE A 1 254 ? -30.901 -14.525 22.044  1.00 35.66  ? 254  ILE A CG2 1 
ATOM   2056 C  CD1 . ILE A 1 254 ? -33.774 -13.393 21.100  1.00 40.43  ? 254  ILE A CD1 1 
ATOM   2057 N  N   . ARG A 1 255 ? -30.127 -17.712 20.956  1.00 32.67  ? 255  ARG A N   1 
ATOM   2058 C  CA  . ARG A 1 255 ? -29.094 -18.519 21.603  1.00 34.06  ? 255  ARG A CA  1 
ATOM   2059 C  C   . ARG A 1 255 ? -28.006 -18.907 20.613  1.00 34.70  ? 255  ARG A C   1 
ATOM   2060 O  O   . ARG A 1 255 ? -26.819 -18.911 20.960  1.00 33.41  ? 255  ARG A O   1 
ATOM   2061 C  CB  . ARG A 1 255 ? -29.683 -19.769 22.267  1.00 39.67  ? 255  ARG A CB  1 
ATOM   2062 C  CG  . ARG A 1 255 ? -30.866 -19.512 23.196  1.00 44.56  ? 255  ARG A CG  1 
ATOM   2063 C  CD  . ARG A 1 255 ? -31.432 -20.836 23.710  1.00 50.31  ? 255  ARG A CD  1 
ATOM   2064 N  NE  . ARG A 1 255 ? -30.393 -21.658 24.317  1.00 52.54  ? 255  ARG A NE  1 
ATOM   2065 C  CZ  . ARG A 1 255 ? -29.885 -21.475 25.532  1.00 56.78  ? 255  ARG A CZ  1 
ATOM   2066 N  NH1 . ARG A 1 255 ? -30.424 -20.617 26.391  1.00 52.84  ? 255  ARG A NH1 1 
ATOM   2067 N  NH2 . ARG A 1 255 ? -28.821 -22.184 25.902  1.00 53.38  ? 255  ARG A NH2 1 
ATOM   2068 N  N   . TYR A 1 256 ? -28.388 -19.235 19.375  1.00 33.41  ? 256  TYR A N   1 
ATOM   2069 C  CA  . TYR A 1 256 ? -27.382 -19.500 18.347  1.00 30.89  ? 256  TYR A CA  1 
ATOM   2070 C  C   . TYR A 1 256 ? -26.513 -18.270 18.097  1.00 32.33  ? 256  TYR A C   1 
ATOM   2071 O  O   . TYR A 1 256 ? -25.294 -18.390 17.898  1.00 33.23  ? 256  TYR A O   1 
ATOM   2072 C  CB  . TYR A 1 256 ? -28.063 -19.939 17.045  1.00 31.84  ? 256  TYR A CB  1 
ATOM   2073 C  CG  . TYR A 1 256 ? -28.569 -21.366 17.083  1.00 34.46  ? 256  TYR A CG  1 
ATOM   2074 C  CD1 . TYR A 1 256 ? -27.796 -22.380 17.629  1.00 37.60  ? 256  TYR A CD1 1 
ATOM   2075 C  CD2 . TYR A 1 256 ? -29.825 -21.693 16.578  1.00 37.22  ? 256  TYR A CD2 1 
ATOM   2076 C  CE1 . TYR A 1 256 ? -28.254 -23.698 17.669  1.00 40.53  ? 256  TYR A CE1 1 
ATOM   2077 C  CE2 . TYR A 1 256 ? -30.290 -23.004 16.613  1.00 40.14  ? 256  TYR A CE2 1 
ATOM   2078 C  CZ  . TYR A 1 256 ? -29.503 -23.997 17.158  1.00 38.13  ? 256  TYR A CZ  1 
ATOM   2079 O  OH  . TYR A 1 256 ? -29.947 -25.302 17.190  1.00 44.36  ? 256  TYR A OH  1 
ATOM   2080 N  N   . GLN A 1 257 ? -27.126 -17.082 18.042  1.00 30.94  ? 257  GLN A N   1 
ATOM   2081 C  CA  . GLN A 1 257 ? -26.327 -15.883 17.781  1.00 30.83  ? 257  GLN A CA  1 
ATOM   2082 C  C   . GLN A 1 257 ? -25.357 -15.611 18.927  1.00 31.68  ? 257  GLN A C   1 
ATOM   2083 O  O   . GLN A 1 257 ? -24.214 -15.194 18.697  1.00 31.62  ? 257  GLN A O   1 
ATOM   2084 C  CB  . GLN A 1 257 ? -27.214 -14.658 17.549  1.00 33.79  ? 257  GLN A CB  1 
ATOM   2085 C  CG  . GLN A 1 257 ? -28.260 -14.794 16.438  1.00 31.48  ? 257  GLN A CG  1 
ATOM   2086 C  CD  . GLN A 1 257 ? -27.689 -14.928 15.031  1.00 34.22  ? 257  GLN A CD  1 
ATOM   2087 O  OE1 . GLN A 1 257 ? -26.463 -14.840 14.800  1.00 30.09  ? 257  GLN A OE1 1 
ATOM   2088 N  NE2 . GLN A 1 257 ? -28.588 -15.127 14.066  1.00 29.53  ? 257  GLN A NE2 1 
ATOM   2089 N  N   . ILE A 1 258 ? -25.784 -15.825 20.175  1.00 32.93  ? 258  ILE A N   1 
ATOM   2090 C  CA  . ILE A 1 258 ? -24.867 -15.576 21.290  1.00 31.40  ? 258  ILE A CA  1 
ATOM   2091 C  C   . ILE A 1 258 ? -23.659 -16.498 21.188  1.00 32.39  ? 258  ILE A C   1 
ATOM   2092 O  O   . ILE A 1 258 ? -22.506 -16.055 21.282  1.00 32.26  ? 258  ILE A O   1 
ATOM   2093 C  CB  . ILE A 1 258 ? -25.579 -15.736 22.646  1.00 30.12  ? 258  ILE A CB  1 
ATOM   2094 C  CG1 . ILE A 1 258 ? -26.718 -14.728 22.764  1.00 36.73  ? 258  ILE A CG1 1 
ATOM   2095 C  CG2 . ILE A 1 258 ? -24.571 -15.493 23.790  1.00 34.73  ? 258  ILE A CG2 1 
ATOM   2096 C  CD1 . ILE A 1 258 ? -27.550 -14.892 24.037  1.00 35.60  ? 258  ILE A CD1 1 
ATOM   2097 N  N   . ILE A 1 259 ? -23.904 -17.793 20.990  1.00 33.67  ? 259  ILE A N   1 
ATOM   2098 C  CA  . ILE A 1 259 ? -22.804 -18.738 20.791  1.00 29.85  ? 259  ILE A CA  1 
ATOM   2099 C  C   . ILE A 1 259 ? -21.925 -18.282 19.634  1.00 31.86  ? 259  ILE A C   1 
ATOM   2100 O  O   . ILE A 1 259 ? -20.694 -18.237 19.740  1.00 31.59  ? 259  ILE A O   1 
ATOM   2101 C  CB  . ILE A 1 259 ? -23.353 -20.153 20.535  1.00 35.87  ? 259  ILE A CB  1 
ATOM   2102 C  CG1 . ILE A 1 259 ? -23.932 -20.729 21.828  1.00 40.63  ? 259  ILE A CG1 1 
ATOM   2103 C  CG2 . ILE A 1 259 ? -22.257 -21.053 19.957  1.00 42.23  ? 259  ILE A CG2 1 
ATOM   2104 C  CD1 . ILE A 1 259 ? -24.753 -21.972 21.630  1.00 47.29  ? 259  ILE A CD1 1 
ATOM   2105 N  N   . THR A 1 260 ? -22.555 -17.949 18.505  1.00 30.78  ? 260  THR A N   1 
ATOM   2106 C  CA  . THR A 1 260 ? -21.812 -17.503 17.326  1.00 31.27  ? 260  THR A CA  1 
ATOM   2107 C  C   . THR A 1 260 ? -20.940 -16.292 17.642  1.00 33.03  ? 260  THR A C   1 
ATOM   2108 O  O   . THR A 1 260 ? -19.754 -16.249 17.279  1.00 32.73  ? 260  THR A O   1 
ATOM   2109 C  CB  . THR A 1 260 ? -22.788 -17.160 16.196  1.00 30.44  ? 260  THR A CB  1 
ATOM   2110 O  OG1 . THR A 1 260 ? -23.507 -18.338 15.811  1.00 31.52  ? 260  THR A OG1 1 
ATOM   2111 C  CG2 . THR A 1 260 ? -22.048 -16.598 14.987  1.00 31.68  ? 260  THR A CG2 1 
ATOM   2112 N  N   . PHE A 1 261 ? -21.520 -15.269 18.269  1.00 30.19  ? 261  PHE A N   1 
ATOM   2113 C  CA  . PHE A 1 261 ? -20.743 -14.049 18.463  1.00 32.15  ? 261  PHE A CA  1 
ATOM   2114 C  C   . PHE A 1 261 ? -19.703 -14.208 19.562  1.00 31.16  ? 261  PHE A C   1 
ATOM   2115 O  O   . PHE A 1 261 ? -18.643 -13.582 19.484  1.00 30.76  ? 261  PHE A O   1 
ATOM   2116 C  CB  . PHE A 1 261 ? -21.671 -12.848 18.720  1.00 32.83  ? 261  PHE A CB  1 
ATOM   2117 C  CG  . PHE A 1 261 ? -22.198 -12.231 17.447  1.00 29.52  ? 261  PHE A CG  1 
ATOM   2118 C  CD1 . PHE A 1 261 ? -23.350 -12.708 16.841  1.00 31.31  ? 261  PHE A CD1 1 
ATOM   2119 C  CD2 . PHE A 1 261 ? -21.505 -11.196 16.832  1.00 28.79  ? 261  PHE A CD2 1 
ATOM   2120 C  CE1 . PHE A 1 261 ? -23.808 -12.145 15.660  1.00 30.05  ? 261  PHE A CE1 1 
ATOM   2121 C  CE2 . PHE A 1 261 ? -21.936 -10.632 15.676  1.00 28.06  ? 261  PHE A CE2 1 
ATOM   2122 C  CZ  . PHE A 1 261 ? -23.105 -11.090 15.070  1.00 30.56  ? 261  PHE A CZ  1 
ATOM   2123 N  N   . LEU A 1 262 ? -19.947 -15.051 20.572  1.00 30.20  ? 262  LEU A N   1 
ATOM   2124 C  CA  . LEU A 1 262 ? -18.878 -15.276 21.553  1.00 32.18  ? 262  LEU A CA  1 
ATOM   2125 C  C   . LEU A 1 262 ? -17.653 -15.917 20.907  1.00 33.25  ? 262  LEU A C   1 
ATOM   2126 O  O   . LEU A 1 262 ? -16.512 -15.638 21.307  1.00 33.30  ? 262  LEU A O   1 
ATOM   2127 C  CB  . LEU A 1 262 ? -19.357 -16.152 22.701  1.00 30.99  ? 262  LEU A CB  1 
ATOM   2128 C  CG  . LEU A 1 262 ? -20.309 -15.479 23.691  1.00 33.88  ? 262  LEU A CG  1 
ATOM   2129 C  CD1 . LEU A 1 262 ? -20.814 -16.497 24.698  1.00 33.68  ? 262  LEU A CD1 1 
ATOM   2130 C  CD2 . LEU A 1 262 ? -19.608 -14.312 24.362  1.00 31.32  ? 262  LEU A CD2 1 
ATOM   2131 N  N   . ILE A 1 263 ? -17.867 -16.808 19.938  1.00 31.92  ? 263  ILE A N   1 
ATOM   2132 C  CA  . ILE A 1 263 ? -16.771 -17.551 19.319  1.00 29.94  ? 263  ILE A CA  1 
ATOM   2133 C  C   . ILE A 1 263 ? -16.175 -16.723 18.186  1.00 32.46  ? 263  ILE A C   1 
ATOM   2134 O  O   . ILE A 1 263 ? -14.987 -16.384 18.210  1.00 31.54  ? 263  ILE A O   1 
ATOM   2135 C  CB  . ILE A 1 263 ? -17.246 -18.927 18.808  1.00 30.84  ? 263  ILE A CB  1 
ATOM   2136 C  CG1 . ILE A 1 263 ? -17.710 -19.801 19.986  1.00 32.74  ? 263  ILE A CG1 1 
ATOM   2137 C  CG2 . ILE A 1 263 ? -16.129 -19.600 17.996  1.00 33.47  ? 263  ILE A CG2 1 
ATOM   2138 C  CD1 . ILE A 1 263 ? -18.314 -21.150 19.553  1.00 35.26  ? 263  ILE A CD1 1 
ATOM   2139 N  N   . ALA A 1 264 ? -16.993 -16.387 17.180  1.00 28.44  ? 264  ALA A N   1 
ATOM   2140 C  CA  . ALA A 1 264 ? -16.491 -15.565 16.080  1.00 30.75  ? 264  ALA A CA  1 
ATOM   2141 C  C   . ALA A 1 264 ? -16.003 -14.206 16.562  1.00 31.56  ? 264  ALA A C   1 
ATOM   2142 O  O   . ALA A 1 264 ? -15.088 -13.635 15.967  1.00 30.03  ? 264  ALA A O   1 
ATOM   2143 C  CB  . ALA A 1 264 ? -17.578 -15.376 15.019  1.00 31.04  ? 264  ALA A CB  1 
ATOM   2144 N  N   . GLY A 1 265 ? -16.601 -13.665 17.618  1.00 30.08  ? 265  GLY A N   1 
ATOM   2145 C  CA  . GLY A 1 265 ? -16.245 -12.333 18.078  1.00 29.59  ? 265  GLY A CA  1 
ATOM   2146 C  C   . GLY A 1 265 ? -14.959 -12.238 18.868  1.00 30.63  ? 265  GLY A C   1 
ATOM   2147 O  O   . GLY A 1 265 ? -14.617 -11.133 19.297  1.00 29.96  ? 265  GLY A O   1 
ATOM   2148 N  N   . HIS A 1 266 ? -14.253 -13.352 19.085  1.00 31.61  ? 266  HIS A N   1 
ATOM   2149 C  CA  . HIS A 1 266 ? -12.949 -13.281 19.757  1.00 30.85  ? 266  HIS A CA  1 
ATOM   2150 C  C   . HIS A 1 266 ? -11.866 -14.174 19.164  1.00 32.41  ? 266  HIS A C   1 
ATOM   2151 O  O   . HIS A 1 266 ? -10.695 -13.780 19.202  1.00 31.61  ? 266  HIS A O   1 
ATOM   2152 C  CB  . HIS A 1 266 ? -13.084 -13.616 21.256  1.00 30.51  ? 266  HIS A CB  1 
ATOM   2153 C  CG  . HIS A 1 266 ? -12.815 -15.053 21.580  1.00 31.68  ? 266  HIS A CG  1 
ATOM   2154 N  ND1 . HIS A 1 266 ? -13.789 -16.027 21.516  1.00 32.34  ? 266  HIS A ND1 1 
ATOM   2155 C  CD2 . HIS A 1 266 ? -11.678 -15.685 21.964  1.00 31.91  ? 266  HIS A CD2 1 
ATOM   2156 C  CE1 . HIS A 1 266 ? -13.265 -17.197 21.838  1.00 30.41  ? 266  HIS A CE1 1 
ATOM   2157 N  NE2 . HIS A 1 266 ? -11.984 -17.017 22.110  1.00 30.83  ? 266  HIS A NE2 1 
ATOM   2158 N  N   . GLU A 1 267 ? -12.182 -15.360 18.638  1.00 31.29  ? 267  GLU A N   1 
ATOM   2159 C  CA  . GLU A 1 267 ? -11.123 -16.318 18.330  1.00 30.07  ? 267  GLU A CA  1 
ATOM   2160 C  C   . GLU A 1 267 ? -10.206 -15.776 17.236  1.00 33.44  ? 267  GLU A C   1 
ATOM   2161 O  O   . GLU A 1 267 ? -8.976  -15.762 17.381  1.00 33.22  ? 267  GLU A O   1 
ATOM   2162 C  CB  . GLU A 1 267 ? -11.737 -17.659 17.929  1.00 32.14  ? 267  GLU A CB  1 
ATOM   2163 C  CG  . GLU A 1 267 ? -10.839 -18.557 17.098  1.00 33.42  ? 267  GLU A CG  1 
ATOM   2164 C  CD  . GLU A 1 267 ? -9.591  -19.000 17.821  1.00 37.54  ? 267  GLU A CD  1 
ATOM   2165 O  OE1 . GLU A 1 267 ? -9.635  -19.132 19.058  1.00 38.42  ? 267  GLU A OE1 1 
ATOM   2166 O  OE2 . GLU A 1 267 ? -8.557  -19.218 17.139  1.00 43.03  ? 267  GLU A OE2 1 
ATOM   2167 N  N   . THR A 1 268 ? -10.787 -15.286 16.151  1.00 30.95  ? 268  THR A N   1 
ATOM   2168 C  CA  . THR A 1 268 ? -9.952  -14.843 15.033  1.00 32.55  ? 268  THR A CA  1 
ATOM   2169 C  C   . THR A 1 268 ? -9.199  -13.559 15.357  1.00 32.93  ? 268  THR A C   1 
ATOM   2170 O  O   . THR A 1 268 ? -8.133  -13.305 14.775  1.00 33.08  ? 268  THR A O   1 
ATOM   2171 C  CB  . THR A 1 268 ? -10.812 -14.658 13.792  1.00 32.53  ? 268  THR A CB  1 
ATOM   2172 O  OG1 . THR A 1 268 ? -12.029 -13.994 14.160  1.00 30.59  ? 268  THR A OG1 1 
ATOM   2173 C  CG2 . THR A 1 268 ? -11.150 -16.017 13.189  1.00 30.22  ? 268  THR A CG2 1 
ATOM   2174 N  N   . THR A 1 269 ? -9.732  -12.732 16.258  1.00 29.42  ? 269  THR A N   1 
ATOM   2175 C  CA  . THR A 1 269 ? -9.026  -11.509 16.629  1.00 31.32  ? 269  THR A CA  1 
ATOM   2176 C  C   . THR A 1 269 ? -7.839  -11.825 17.532  1.00 30.48  ? 269  THR A C   1 
ATOM   2177 O  O   . THR A 1 269 ? -6.813  -11.128 17.482  1.00 31.46  ? 269  THR A O   1 
ATOM   2178 C  CB  . THR A 1 269 ? -9.982  -10.523 17.316  1.00 30.43  ? 269  THR A CB  1 
ATOM   2179 O  OG1 . THR A 1 269 ? -11.077 -10.233 16.420  1.00 29.33  ? 269  THR A OG1 1 
ATOM   2180 C  CG2 . THR A 1 269 ? -9.265  -9.209  17.678  1.00 29.41  ? 269  THR A CG2 1 
ATOM   2181 N  N   A SER A 1 270 ? -7.947  -12.868 18.357  0.58 29.79  ? 270  SER A N   1 
ATOM   2182 N  N   B SER A 1 270 ? -7.960  -12.851 18.377  0.42 29.82  ? 270  SER A N   1 
ATOM   2183 C  CA  A SER A 1 270 ? -6.787  -13.269 19.151  0.58 28.90  ? 270  SER A CA  1 
ATOM   2184 C  CA  B SER A 1 270 ? -6.797  -13.288 19.147  0.42 28.94  ? 270  SER A CA  1 
ATOM   2185 C  C   A SER A 1 270 ? -5.685  -13.825 18.252  0.58 30.96  ? 270  SER A C   1 
ATOM   2186 C  C   B SER A 1 270 ? -5.694  -13.776 18.218  0.42 30.96  ? 270  SER A C   1 
ATOM   2187 O  O   A SER A 1 270 ? -4.494  -13.587 18.499  0.58 31.97  ? 270  SER A O   1 
ATOM   2188 O  O   B SER A 1 270 ? -4.514  -13.455 18.414  0.42 31.97  ? 270  SER A O   1 
ATOM   2189 C  CB  A SER A 1 270 ? -7.199  -14.288 20.222  0.58 32.73  ? 270  SER A CB  1 
ATOM   2190 C  CB  B SER A 1 270 ? -7.193  -14.391 20.131  0.42 32.66  ? 270  SER A CB  1 
ATOM   2191 O  OG  A SER A 1 270 ? -7.523  -15.553 19.669  0.58 31.12  ? 270  SER A OG  1 
ATOM   2192 O  OG  B SER A 1 270 ? -6.048  -15.098 20.587  0.42 31.60  ? 270  SER A OG  1 
ATOM   2193 N  N   . GLY A 1 271 ? -6.061  -14.560 17.204  1.00 32.34  ? 271  GLY A N   1 
ATOM   2194 C  CA  . GLY A 1 271 ? -5.074  -14.995 16.228  1.00 30.19  ? 271  GLY A CA  1 
ATOM   2195 C  C   . GLY A 1 271 ? -4.412  -13.819 15.544  1.00 33.78  ? 271  GLY A C   1 
ATOM   2196 O  O   . GLY A 1 271 ? -3.185  -13.781 15.384  1.00 32.23  ? 271  GLY A O   1 
ATOM   2197 N  N   . LEU A 1 272 ? -5.208  -12.828 15.147  1.00 31.26  ? 272  LEU A N   1 
ATOM   2198 C  CA  . LEU A 1 272 ? -4.641  -11.669 14.464  1.00 33.26  ? 272  LEU A CA  1 
ATOM   2199 C  C   . LEU A 1 272 ? -3.620  -10.953 15.340  1.00 33.35  ? 272  LEU A C   1 
ATOM   2200 O  O   . LEU A 1 272 ? -2.514  -10.614 14.889  1.00 32.70  ? 272  LEU A O   1 
ATOM   2201 C  CB  . LEU A 1 272 ? -5.753  -10.706 14.062  1.00 32.66  ? 272  LEU A CB  1 
ATOM   2202 C  CG  . LEU A 1 272 ? -5.280  -9.322  13.624  1.00 33.66  ? 272  LEU A CG  1 
ATOM   2203 C  CD1 . LEU A 1 272 ? -4.287  -9.413  12.438  1.00 31.11  ? 272  LEU A CD1 1 
ATOM   2204 C  CD2 . LEU A 1 272 ? -6.498  -8.444  13.259  1.00 33.22  ? 272  LEU A CD2 1 
ATOM   2205 N  N   . LEU A 1 273 ? -3.977  -10.696 16.596  1.00 30.84  ? 273  LEU A N   1 
ATOM   2206 C  CA  . LEU A 1 273 ? -3.058  -9.967  17.464  1.00 31.44  ? 273  LEU A CA  1 
ATOM   2207 C  C   . LEU A 1 273 ? -1.792  -10.775 17.709  1.00 31.68  ? 273  LEU A C   1 
ATOM   2208 O  O   . LEU A 1 273 ? -0.697  -10.206 17.799  1.00 33.52  ? 273  LEU A O   1 
ATOM   2209 C  CB  . LEU A 1 273 ? -3.731  -9.611  18.792  1.00 32.52  ? 273  LEU A CB  1 
ATOM   2210 C  CG  . LEU A 1 273 ? -4.669  -8.409  18.743  1.00 29.93  ? 273  LEU A CG  1 
ATOM   2211 C  CD1 . LEU A 1 273 ? -5.610  -8.403  19.963  1.00 30.61  ? 273  LEU A CD1 1 
ATOM   2212 C  CD2 . LEU A 1 273 ? -3.876  -7.109  18.688  1.00 33.82  ? 273  LEU A CD2 1 
ATOM   2213 N  N   . SER A 1 274 ? -1.928  -12.098 17.828  1.00 31.17  ? 274  SER A N   1 
ATOM   2214 C  CA  . SER A 1 274 ? -0.768  -12.967 18.022  1.00 33.08  ? 274  SER A CA  1 
ATOM   2215 C  C   . SER A 1 274 ? 0.156   -12.909 16.814  1.00 35.70  ? 274  SER A C   1 
ATOM   2216 O  O   . SER A 1 274 ? 1.370   -12.708 16.957  1.00 33.10  ? 274  SER A O   1 
ATOM   2217 C  CB  . SER A 1 274 ? -1.215  -14.409 18.280  1.00 32.86  ? 274  SER A CB  1 
ATOM   2218 O  OG  . SER A 1 274 ? -2.072  -14.478 19.420  1.00 32.23  ? 274  SER A OG  1 
ATOM   2219 N  N   . PHE A 1 275 ? -0.402  -13.090 15.611  1.00 32.14  ? 275  PHE A N   1 
ATOM   2220 C  CA  . PHE A 1 275 ? 0.426   -12.983 14.406  1.00 33.41  ? 275  PHE A CA  1 
ATOM   2221 C  C   . PHE A 1 275 ? 1.023   -11.583 14.263  1.00 34.70  ? 275  PHE A C   1 
ATOM   2222 O  O   . PHE A 1 275 ? 2.172   -11.434 13.818  1.00 36.92  ? 275  PHE A O   1 
ATOM   2223 C  CB  . PHE A 1 275 ? -0.390  -13.338 13.157  1.00 30.12  ? 275  PHE A CB  1 
ATOM   2224 C  CG  . PHE A 1 275 ? -0.581  -14.811 12.936  1.00 32.09  ? 275  PHE A CG  1 
ATOM   2225 C  CD1 . PHE A 1 275 ? 0.503   -15.641 12.671  1.00 35.02  ? 275  PHE A CD1 1 
ATOM   2226 C  CD2 . PHE A 1 275 ? -1.854  -15.367 12.986  1.00 29.30  ? 275  PHE A CD2 1 
ATOM   2227 C  CE1 . PHE A 1 275 ? 0.325   -16.999 12.435  1.00 34.34  ? 275  PHE A CE1 1 
ATOM   2228 C  CE2 . PHE A 1 275 ? -2.045  -16.712 12.773  1.00 32.39  ? 275  PHE A CE2 1 
ATOM   2229 C  CZ  . PHE A 1 275 ? -0.954  -17.546 12.492  1.00 35.85  ? 275  PHE A CZ  1 
ATOM   2230 N  N   . ALA A 1 276 ? 0.260   -10.541 14.609  1.00 33.20  ? 276  ALA A N   1 
ATOM   2231 C  CA  . ALA A 1 276 ? 0.766   -9.180  14.451  1.00 33.32  ? 276  ALA A CA  1 
ATOM   2232 C  C   . ALA A 1 276 ? 1.969   -8.942  15.350  1.00 38.28  ? 276  ALA A C   1 
ATOM   2233 O  O   . ALA A 1 276 ? 2.977   -8.362  14.921  1.00 36.09  ? 276  ALA A O   1 
ATOM   2234 C  CB  . ALA A 1 276 ? -0.326  -8.153  14.746  1.00 34.33  ? 276  ALA A CB  1 
ATOM   2235 N  N   . LEU A 1 277 ? 1.886   -9.383  16.605  1.00 36.01  ? 277  LEU A N   1 
ATOM   2236 C  CA  . LEU A 1 277 ? 3.027   -9.207  17.501  1.00 32.47  ? 277  LEU A CA  1 
ATOM   2237 C  C   . LEU A 1 277 ? 4.209   -10.043 17.034  1.00 38.16  ? 277  LEU A C   1 
ATOM   2238 O  O   . LEU A 1 277 ? 5.363   -9.603  17.115  1.00 35.55  ? 277  LEU A O   1 
ATOM   2239 C  CB  . LEU A 1 277 ? 2.643   -9.579  18.933  1.00 36.18  ? 277  LEU A CB  1 
ATOM   2240 C  CG  . LEU A 1 277 ? 3.769   -9.373  19.954  1.00 37.07  ? 277  LEU A CG  1 
ATOM   2241 C  CD1 . LEU A 1 277 ? 4.212   -7.918  19.950  1.00 34.69  ? 277  LEU A CD1 1 
ATOM   2242 C  CD2 . LEU A 1 277 ? 3.289   -9.765  21.344  1.00 34.62  ? 277  LEU A CD2 1 
ATOM   2243 N  N   . TYR A 1 278 ? 3.939   -11.250 16.540  1.00 33.37  ? 278  TYR A N   1 
ATOM   2244 C  CA  . TYR A 1 278 ? 5.002   -12.080 15.983  1.00 35.34  ? 278  TYR A CA  1 
ATOM   2245 C  C   . TYR A 1 278 ? 5.737   -11.343 14.868  1.00 40.09  ? 278  TYR A C   1 
ATOM   2246 O  O   . TYR A 1 278 ? 6.970   -11.236 14.883  1.00 38.44  ? 278  TYR A O   1 
ATOM   2247 C  CB  . TYR A 1 278 ? 4.426   -13.404 15.471  1.00 34.93  ? 278  TYR A CB  1 
ATOM   2248 C  CG  . TYR A 1 278 ? 5.377   -14.166 14.587  1.00 39.91  ? 278  TYR A CG  1 
ATOM   2249 C  CD1 . TYR A 1 278 ? 6.342   -15.002 15.135  1.00 38.72  ? 278  TYR A CD1 1 
ATOM   2250 C  CD2 . TYR A 1 278 ? 5.326   -14.035 13.199  1.00 38.38  ? 278  TYR A CD2 1 
ATOM   2251 C  CE1 . TYR A 1 278 ? 7.235   -15.698 14.322  1.00 41.20  ? 278  TYR A CE1 1 
ATOM   2252 C  CE2 . TYR A 1 278 ? 6.211   -14.725 12.381  1.00 38.85  ? 278  TYR A CE2 1 
ATOM   2253 C  CZ  . TYR A 1 278 ? 7.169   -15.551 12.951  1.00 42.62  ? 278  TYR A CZ  1 
ATOM   2254 O  OH  . TYR A 1 278 ? 8.054   -16.251 12.144  1.00 41.07  ? 278  TYR A OH  1 
ATOM   2255 N  N   . PHE A 1 279 ? 4.998   -10.822 13.887  1.00 37.69  ? 279  PHE A N   1 
ATOM   2256 C  CA  . PHE A 1 279 ? 5.676   -10.142 12.787  1.00 36.91  ? 279  PHE A CA  1 
ATOM   2257 C  C   . PHE A 1 279 ? 6.385   -8.880  13.260  1.00 37.86  ? 279  PHE A C   1 
ATOM   2258 O  O   . PHE A 1 279 ? 7.442   -8.530  12.725  1.00 42.65  ? 279  PHE A O   1 
ATOM   2259 C  CB  . PHE A 1 279 ? 4.683   -9.829  11.658  1.00 34.07  ? 279  PHE A CB  1 
ATOM   2260 C  CG  . PHE A 1 279 ? 4.323   -11.026 10.827  1.00 36.90  ? 279  PHE A CG  1 
ATOM   2261 C  CD1 . PHE A 1 279 ? 5.280   -11.669 10.064  1.00 37.38  ? 279  PHE A CD1 1 
ATOM   2262 C  CD2 . PHE A 1 279 ? 3.025   -11.504 10.790  1.00 36.50  ? 279  PHE A CD2 1 
ATOM   2263 C  CE1 . PHE A 1 279 ? 4.966   -12.779 9.310   1.00 36.93  ? 279  PHE A CE1 1 
ATOM   2264 C  CE2 . PHE A 1 279 ? 2.704   -12.618 10.037  1.00 35.79  ? 279  PHE A CE2 1 
ATOM   2265 C  CZ  . PHE A 1 279 ? 3.670   -13.246 9.284   1.00 41.27  ? 279  PHE A CZ  1 
ATOM   2266 N  N   . LEU A 1 280 ? 5.853   -8.203  14.278  1.00 35.95  ? 280  LEU A N   1 
ATOM   2267 C  CA  . LEU A 1 280 ? 6.489   -6.978  14.752  1.00 38.52  ? 280  LEU A CA  1 
ATOM   2268 C  C   . LEU A 1 280 ? 7.842   -7.274  15.405  1.00 40.95  ? 280  LEU A C   1 
ATOM   2269 O  O   . LEU A 1 280 ? 8.830   -6.566  15.151  1.00 39.41  ? 280  LEU A O   1 
ATOM   2270 C  CB  . LEU A 1 280 ? 5.572   -6.240  15.724  1.00 38.01  ? 280  LEU A CB  1 
ATOM   2271 C  CG  . LEU A 1 280 ? 4.426   -5.445  15.087  1.00 37.03  ? 280  LEU A CG  1 
ATOM   2272 C  CD1 . LEU A 1 280 ? 3.641   -4.643  16.133  1.00 43.40  ? 280  LEU A CD1 1 
ATOM   2273 C  CD2 . LEU A 1 280 ? 4.960   -4.539  13.969  1.00 39.17  ? 280  LEU A CD2 1 
ATOM   2274 N  N   . VAL A 1 281 ? 7.913   -8.314  16.248  1.00 38.42  ? 281  VAL A N   1 
ATOM   2275 C  CA  . VAL A 1 281 ? 9.211   -8.626  16.864  1.00 41.14  ? 281  VAL A CA  1 
ATOM   2276 C  C   . VAL A 1 281 ? 10.168  -9.233  15.851  1.00 44.66  ? 281  VAL A C   1 
ATOM   2277 O  O   . VAL A 1 281 ? 11.393  -9.138  16.015  1.00 42.38  ? 281  VAL A O   1 
ATOM   2278 C  CB  . VAL A 1 281 ? 9.074   -9.542  18.099  1.00 41.14  ? 281  VAL A CB  1 
ATOM   2279 C  CG1 . VAL A 1 281 ? 8.291   -8.835  19.187  1.00 42.03  ? 281  VAL A CG1 1 
ATOM   2280 C  CG2 . VAL A 1 281 ? 8.475   -10.904 17.731  1.00 37.23  ? 281  VAL A CG2 1 
ATOM   2281 N  N   . LYS A 1 282 ? 9.651   -9.865  14.798  1.00 38.75  ? 282  LYS A N   1 
ATOM   2282 C  CA  . LYS A 1 282 ? 10.533  -10.356 13.748  1.00 41.57  ? 282  LYS A CA  1 
ATOM   2283 C  C   . LYS A 1 282 ? 10.941  -9.269  12.761  1.00 43.17  ? 282  LYS A C   1 
ATOM   2284 O  O   . LYS A 1 282 ? 11.769  -9.536  11.879  1.00 47.24  ? 282  LYS A O   1 
ATOM   2285 C  CB  . LYS A 1 282 ? 9.877   -11.506 12.986  1.00 43.72  ? 282  LYS A CB  1 
ATOM   2286 C  CG  . LYS A 1 282 ? 9.639   -12.791 13.790  1.00 42.03  ? 282  LYS A CG  1 
ATOM   2287 C  CD  . LYS A 1 282 ? 10.910  -13.333 14.485  1.00 40.93  ? 282  LYS A CD  1 
ATOM   2288 C  CE  . LYS A 1 282 ? 10.729  -14.815 14.833  1.00 41.02  ? 282  LYS A CE  1 
ATOM   2289 N  NZ  . LYS A 1 282 ? 11.886  -15.420 15.598  1.00 40.47  ? 282  LYS A NZ  1 
ATOM   2290 N  N   . ASN A 1 283 ? 10.397  -8.060  12.882  1.00 41.28  ? 283  ASN A N   1 
ATOM   2291 C  CA  . ASN A 1 283 ? 10.669  -6.972  11.940  1.00 40.16  ? 283  ASN A CA  1 
ATOM   2292 C  C   . ASN A 1 283 ? 10.828  -5.684  12.724  1.00 43.88  ? 283  ASN A C   1 
ATOM   2293 O  O   . ASN A 1 283 ? 9.971   -4.794  12.682  1.00 42.41  ? 283  ASN A O   1 
ATOM   2294 C  CB  . ASN A 1 283 ? 9.559   -6.874  10.888  1.00 39.01  ? 283  ASN A CB  1 
ATOM   2295 C  CG  . ASN A 1 283 ? 9.549   -8.060  9.953   1.00 40.92  ? 283  ASN A CG  1 
ATOM   2296 O  OD1 . ASN A 1 283 ? 10.269  -8.079  8.948   1.00 42.12  ? 283  ASN A OD1 1 
ATOM   2297 N  ND2 . ASN A 1 283 ? 8.737   -9.062  10.268  1.00 38.66  ? 283  ASN A ND2 1 
ATOM   2298 N  N   . PRO A 1 284 ? 11.948  -5.542  13.445  1.00 43.79  ? 284  PRO A N   1 
ATOM   2299 C  CA  . PRO A 1 284 ? 12.075  -4.435  14.409  1.00 45.58  ? 284  PRO A CA  1 
ATOM   2300 C  C   . PRO A 1 284 ? 11.917  -3.063  13.791  1.00 41.07  ? 284  PRO A C   1 
ATOM   2301 O  O   . PRO A 1 284 ? 11.499  -2.124  14.485  1.00 48.65  ? 284  PRO A O   1 
ATOM   2302 C  CB  . PRO A 1 284 ? 13.492  -4.623  14.976  1.00 49.34  ? 284  PRO A CB  1 
ATOM   2303 C  CG  . PRO A 1 284 ? 13.862  -6.039  14.657  1.00 44.03  ? 284  PRO A CG  1 
ATOM   2304 C  CD  . PRO A 1 284 ? 13.154  -6.384  13.388  1.00 46.52  ? 284  PRO A CD  1 
ATOM   2305 N  N   . HIS A 1 285 ? 12.259  -2.909  12.511  1.00 47.26  ? 285  HIS A N   1 
ATOM   2306 C  CA  . HIS A 1 285 ? 12.097  -1.614  11.859  1.00 46.88  ? 285  HIS A CA  1 
ATOM   2307 C  C   . HIS A 1 285 ? 10.622  -1.251  11.750  1.00 43.34  ? 285  HIS A C   1 
ATOM   2308 O  O   . HIS A 1 285 ? 10.238  -0.090  11.945  1.00 44.73  ? 285  HIS A O   1 
ATOM   2309 C  CB  . HIS A 1 285 ? 12.744  -1.635  10.470  1.00 48.68  ? 285  HIS A CB  1 
ATOM   2310 C  CG  . HIS A 1 285 ? 14.233  -1.827  10.494  1.00 60.12  ? 285  HIS A CG  1 
ATOM   2311 N  ND1 . HIS A 1 285 ? 14.879  -2.748  9.694   1.00 61.69  ? 285  HIS A ND1 1 
ATOM   2312 C  CD2 . HIS A 1 285 ? 15.197  -1.243  11.246  1.00 62.09  ? 285  HIS A CD2 1 
ATOM   2313 C  CE1 . HIS A 1 285 ? 16.179  -2.701  9.930   1.00 60.83  ? 285  HIS A CE1 1 
ATOM   2314 N  NE2 . HIS A 1 285 ? 16.397  -1.801  10.872  1.00 63.03  ? 285  HIS A NE2 1 
ATOM   2315 N  N   . VAL A 1 286 ? 9.787   -2.248  11.462  1.00 45.88  ? 286  VAL A N   1 
ATOM   2316 C  CA  . VAL A 1 286 ? 8.337   -2.054  11.437  1.00 42.14  ? 286  VAL A CA  1 
ATOM   2317 C  C   . VAL A 1 286 ? 7.814   -1.757  12.838  1.00 38.84  ? 286  VAL A C   1 
ATOM   2318 O  O   . VAL A 1 286 ? 7.037   -0.814  13.054  1.00 42.19  ? 286  VAL A O   1 
ATOM   2319 C  CB  . VAL A 1 286 ? 7.664   -3.296  10.825  1.00 40.78  ? 286  VAL A CB  1 
ATOM   2320 C  CG1 . VAL A 1 286 ? 6.139   -3.106  10.751  1.00 41.02  ? 286  VAL A CG1 1 
ATOM   2321 C  CG2 . VAL A 1 286 ? 8.253   -3.600  9.438   1.00 45.46  ? 286  VAL A CG2 1 
ATOM   2322 N  N   . LEU A 1 287 ? 8.254   -2.544  13.824  1.00 43.16  ? 287  LEU A N   1 
ATOM   2323 C  CA  . LEU A 1 287 ? 7.878   -2.267  15.206  1.00 41.58  ? 287  LEU A CA  1 
ATOM   2324 C  C   . LEU A 1 287 ? 8.178   -0.819  15.577  1.00 40.01  ? 287  LEU A C   1 
ATOM   2325 O  O   . LEU A 1 287 ? 7.330   -0.118  16.144  1.00 41.58  ? 287  LEU A O   1 
ATOM   2326 C  CB  . LEU A 1 287 ? 8.600   -3.238  16.144  1.00 43.63  ? 287  LEU A CB  1 
ATOM   2327 C  CG  . LEU A 1 287 ? 7.909   -3.392  17.504  1.00 43.92  ? 287  LEU A CG  1 
ATOM   2328 C  CD1 . LEU A 1 287 ? 8.349   -4.687  18.175  1.00 45.98  ? 287  LEU A CD1 1 
ATOM   2329 C  CD2 . LEU A 1 287 ? 8.182   -2.188  18.411  1.00 44.38  ? 287  LEU A CD2 1 
ATOM   2330 N  N   . GLN A 1 288 ? 9.374   -0.335  15.223  1.00 44.97  ? 288  GLN A N   1 
ATOM   2331 C  CA  . GLN A 1 288 ? 9.733   1.034   15.579  1.00 42.40  ? 288  GLN A CA  1 
ATOM   2332 C  C   . GLN A 1 288 ? 8.781   2.039   14.948  1.00 42.88  ? 288  GLN A C   1 
ATOM   2333 O  O   . GLN A 1 288 ? 8.319   2.975   15.608  1.00 47.03  ? 288  GLN A O   1 
ATOM   2334 C  CB  . GLN A 1 288 ? 11.170  1.349   15.160  1.00 51.91  ? 288  GLN A CB  1 
ATOM   2335 C  CG  . GLN A 1 288 ? 11.610  2.709   15.675  1.00 51.73  ? 288  GLN A CG  1 
ATOM   2336 C  CD  . GLN A 1 288 ? 12.948  3.138   15.126  1.00 62.57  ? 288  GLN A CD  1 
ATOM   2337 O  OE1 . GLN A 1 288 ? 13.818  2.311   14.846  1.00 67.10  ? 288  GLN A OE1 1 
ATOM   2338 N  NE2 . GLN A 1 288 ? 13.121  4.445   14.960  1.00 65.01  ? 288  GLN A NE2 1 
ATOM   2339 N  N   . LYS A 1 289 ? 8.485   1.873   13.659  1.00 44.14  ? 289  LYS A N   1 
ATOM   2340 C  CA  . LYS A 1 289 ? 7.587   2.812   12.999  1.00 41.75  ? 289  LYS A CA  1 
ATOM   2341 C  C   . LYS A 1 289 ? 6.216   2.810   13.662  1.00 39.96  ? 289  LYS A C   1 
ATOM   2342 O  O   . LYS A 1 289 ? 5.634   3.871   13.927  1.00 36.68  ? 289  LYS A O   1 
ATOM   2343 C  CB  . LYS A 1 289 ? 7.478   2.461   11.516  1.00 40.88  ? 289  LYS A CB  1 
ATOM   2344 C  CG  . LYS A 1 289 ? 6.797   3.525   10.669  1.00 44.63  ? 289  LYS A CG  1 
ATOM   2345 C  CD  . LYS A 1 289 ? 6.982   3.223   9.185   1.00 45.87  ? 289  LYS A CD  1 
ATOM   2346 C  CE  . LYS A 1 289 ? 6.096   4.093   8.307   1.00 50.55  ? 289  LYS A CE  1 
ATOM   2347 N  NZ  . LYS A 1 289 ? 6.229   3.687   6.874   1.00 50.92  ? 289  LYS A NZ  1 
ATOM   2348 N  N   . ALA A 1 290 ? 5.696   1.620   13.965  1.00 44.14  ? 290  ALA A N   1 
ATOM   2349 C  CA  . ALA A 1 290 ? 4.408   1.535   14.640  1.00 43.35  ? 290  ALA A CA  1 
ATOM   2350 C  C   . ALA A 1 290 ? 4.479   2.119   16.049  1.00 38.88  ? 290  ALA A C   1 
ATOM   2351 O  O   . ALA A 1 290 ? 3.562   2.830   16.478  1.00 42.18  ? 290  ALA A O   1 
ATOM   2352 C  CB  . ALA A 1 290 ? 3.938   0.080   14.659  1.00 41.06  ? 290  ALA A CB  1 
ATOM   2353 N  N   . ALA A 1 291 ? 5.559   1.844   16.783  1.00 41.83  ? 291  ALA A N   1 
ATOM   2354 C  CA  . ALA A 1 291 ? 5.696   2.420   18.121  1.00 42.50  ? 291  ALA A CA  1 
ATOM   2355 C  C   . ALA A 1 291 ? 5.765   3.940   18.062  1.00 41.34  ? 291  ALA A C   1 
ATOM   2356 O  O   . ALA A 1 291 ? 5.221   4.633   18.930  1.00 41.89  ? 291  ALA A O   1 
ATOM   2357 C  CB  . ALA A 1 291 ? 6.937   1.856   18.819  1.00 41.48  ? 291  ALA A CB  1 
ATOM   2358 N  N   . GLU A 1 292 ? 6.438   4.480   17.046  1.00 44.09  ? 292  GLU A N   1 
ATOM   2359 C  CA  . GLU A 1 292 ? 6.516   5.931   16.917  1.00 41.03  ? 292  GLU A CA  1 
ATOM   2360 C  C   . GLU A 1 292 ? 5.141   6.535   16.700  1.00 43.67  ? 292  GLU A C   1 
ATOM   2361 O  O   . GLU A 1 292 ? 4.811   7.576   17.283  1.00 45.03  ? 292  GLU A O   1 
ATOM   2362 C  CB  . GLU A 1 292 ? 7.470   6.284   15.777  1.00 47.16  ? 292  GLU A CB  1 
ATOM   2363 C  CG  . GLU A 1 292 ? 8.865   5.713   16.020  1.00 51.39  ? 292  GLU A CG  1 
ATOM   2364 C  CD  . GLU A 1 292 ? 9.880   6.191   15.007  1.00 58.46  ? 292  GLU A CD  1 
ATOM   2365 O  OE1 . GLU A 1 292 ? 9.570   7.154   14.280  1.00 62.90  ? 292  GLU A OE1 1 
ATOM   2366 O  OE2 . GLU A 1 292 ? 10.987  5.611   14.948  1.00 60.78  ? 292  GLU A OE2 1 
ATOM   2367 N  N   . GLU A 1 293 ? 4.310   5.884   15.881  1.00 43.54  ? 293  GLU A N   1 
ATOM   2368 C  CA  . GLU A 1 293 ? 2.940   6.354   15.721  1.00 44.58  ? 293  GLU A CA  1 
ATOM   2369 C  C   . GLU A 1 293 ? 2.197   6.307   17.049  1.00 40.51  ? 293  GLU A C   1 
ATOM   2370 O  O   . GLU A 1 293 ? 1.534   7.275   17.442  1.00 43.74  ? 293  GLU A O   1 
ATOM   2371 C  CB  . GLU A 1 293 ? 2.207   5.520   14.668  1.00 40.23  ? 293  GLU A CB  1 
ATOM   2372 C  CG  . GLU A 1 293 ? 0.762   5.967   14.478  1.00 41.22  ? 293  GLU A CG  1 
ATOM   2373 C  CD  . GLU A 1 293 ? 0.052   5.162   13.414  1.00 42.30  ? 293  GLU A CD  1 
ATOM   2374 O  OE1 . GLU A 1 293 ? -0.294  3.993   13.692  1.00 40.47  ? 293  GLU A OE1 1 
ATOM   2375 O  OE2 . GLU A 1 293 ? -0.131  5.685   12.294  1.00 41.40  ? 293  GLU A OE2 1 
ATOM   2376 N  N   . ALA A 1 294 ? 2.290   5.176   17.752  1.00 45.89  ? 294  ALA A N   1 
ATOM   2377 C  CA  . ALA A 1 294 ? 1.574   5.036   19.016  1.00 42.61  ? 294  ALA A CA  1 
ATOM   2378 C  C   . ALA A 1 294 ? 1.942   6.154   19.987  1.00 39.60  ? 294  ALA A C   1 
ATOM   2379 O  O   . ALA A 1 294 ? 1.064   6.746   20.625  1.00 41.92  ? 294  ALA A O   1 
ATOM   2380 C  CB  . ALA A 1 294 ? 1.861   3.662   19.624  1.00 41.29  ? 294  ALA A CB  1 
ATOM   2381 N  N   . ALA A 1 295 ? 3.232   6.486   20.084  1.00 47.80  ? 295  ALA A N   1 
ATOM   2382 C  CA  . ALA A 1 295 ? 3.651   7.544   21.001  1.00 44.72  ? 295  ALA A CA  1 
ATOM   2383 C  C   . ALA A 1 295 ? 3.099   8.902   20.580  1.00 46.73  ? 295  ALA A C   1 
ATOM   2384 O  O   . ALA A 1 295 ? 2.665   9.696   21.424  1.00 47.70  ? 295  ALA A O   1 
ATOM   2385 C  CB  . ALA A 1 295 ? 5.177   7.585   21.088  1.00 49.95  ? 295  ALA A CB  1 
ATOM   2386 N  N   . ARG A 1 296 ? 3.075   9.177   19.276  1.00 49.23  ? 296  ARG A N   1 
ATOM   2387 C  CA  . ARG A 1 296 ? 2.608   10.477  18.803  1.00 44.05  ? 296  ARG A CA  1 
ATOM   2388 C  C   . ARG A 1 296 ? 1.099   10.633  18.965  1.00 46.78  ? 296  ARG A C   1 
ATOM   2389 O  O   . ARG A 1 296 ? 0.609   11.730  19.259  1.00 46.14  ? 296  ARG A O   1 
ATOM   2390 C  CB  . ARG A 1 296 ? 3.003   10.663  17.342  1.00 51.70  ? 296  ARG A CB  1 
ATOM   2391 C  CG  . ARG A 1 296 ? 2.147   11.678  16.621  1.00 47.14  ? 296  ARG A CG  1 
ATOM   2392 C  CD  . ARG A 1 296 ? 2.832   12.158  15.368  1.00 57.84  ? 296  ARG A CD  1 
ATOM   2393 N  NE  . ARG A 1 296 ? 3.362   11.022  14.627  1.00 52.78  ? 296  ARG A NE  1 
ATOM   2394 C  CZ  . ARG A 1 296 ? 2.639   10.240  13.836  1.00 57.75  ? 296  ARG A CZ  1 
ATOM   2395 N  NH1 . ARG A 1 296 ? 1.328   10.410  13.705  1.00 53.90  ? 296  ARG A NH1 1 
ATOM   2396 N  NH2 . ARG A 1 296 ? 3.244   9.256   13.171  1.00 56.06  ? 296  ARG A NH2 1 
ATOM   2397 N  N   . VAL A 1 297 ? 0.340   9.561   18.758  1.00 43.35  ? 297  VAL A N   1 
ATOM   2398 C  CA  . VAL A 1 297 ? -1.116  9.670   18.763  1.00 42.95  ? 297  VAL A CA  1 
ATOM   2399 C  C   . VAL A 1 297 ? -1.694  9.476   20.155  1.00 39.59  ? 297  VAL A C   1 
ATOM   2400 O  O   . VAL A 1 297 ? -2.640  10.166  20.541  1.00 41.88  ? 297  VAL A O   1 
ATOM   2401 C  CB  . VAL A 1 297 ? -1.713  8.663   17.759  1.00 39.51  ? 297  VAL A CB  1 
ATOM   2402 C  CG1 . VAL A 1 297 ? -3.222  8.542   17.949  1.00 42.44  ? 297  VAL A CG1 1 
ATOM   2403 C  CG2 . VAL A 1 297 ? -1.370  9.079   16.331  1.00 43.66  ? 297  VAL A CG2 1 
ATOM   2404 N  N   . LEU A 1 298 ? -1.163  8.527   20.927  1.00 45.04  ? 298  LEU A N   1 
ATOM   2405 C  CA  . LEU A 1 298 ? -1.779  8.154   22.201  1.00 40.19  ? 298  LEU A CA  1 
ATOM   2406 C  C   . LEU A 1 298 ? -1.200  9.018   23.324  1.00 47.25  ? 298  LEU A C   1 
ATOM   2407 O  O   . LEU A 1 298 ? -0.428  8.572   24.173  1.00 48.47  ? 298  LEU A O   1 
ATOM   2408 C  CB  . LEU A 1 298 ? -1.591  6.664   22.467  1.00 41.47  ? 298  LEU A CB  1 
ATOM   2409 C  CG  . LEU A 1 298 ? -2.181  5.760   21.372  1.00 41.64  ? 298  LEU A CG  1 
ATOM   2410 C  CD1 . LEU A 1 298 ? -1.943  4.273   21.665  1.00 40.17  ? 298  LEU A CD1 1 
ATOM   2411 C  CD2 . LEU A 1 298 ? -3.652  6.057   21.206  1.00 41.19  ? 298  LEU A CD2 1 
ATOM   2412 N  N   . VAL A 1 299 ? -1.619  10.290  23.315  1.00 47.92  ? 299  VAL A N   1 
ATOM   2413 C  CA  . VAL A 1 299 ? -1.063  11.297  24.218  1.00 47.01  ? 299  VAL A CA  1 
ATOM   2414 C  C   . VAL A 1 299 ? -1.799  11.365  25.547  1.00 49.97  ? 299  VAL A C   1 
ATOM   2415 O  O   . VAL A 1 299 ? -1.399  12.136  26.430  1.00 49.41  ? 299  VAL A O   1 
ATOM   2416 C  CB  . VAL A 1 299 ? -1.068  12.691  23.551  1.00 45.70  ? 299  VAL A CB  1 
ATOM   2417 C  CG1 . VAL A 1 299 ? -0.240  12.670  22.254  1.00 46.86  ? 299  VAL A CG1 1 
ATOM   2418 C  CG2 . VAL A 1 299 ? -2.502  13.165  23.296  1.00 46.89  ? 299  VAL A CG2 1 
ATOM   2419 N  N   . ASP A 1 300 ? -2.863  10.594  25.723  1.00 46.06  ? 300  ASP A N   1 
ATOM   2420 C  CA  . ASP A 1 300 ? -3.576  10.555  26.985  1.00 48.26  ? 300  ASP A CA  1 
ATOM   2421 C  C   . ASP A 1 300 ? -3.347  9.219   27.692  1.00 47.60  ? 300  ASP A C   1 
ATOM   2422 O  O   . ASP A 1 300 ? -2.948  8.229   27.067  1.00 47.48  ? 300  ASP A O   1 
ATOM   2423 C  CB  . ASP A 1 300 ? -5.074  10.789  26.755  1.00 50.45  ? 300  ASP A CB  1 
ATOM   2424 C  CG  . ASP A 1 300 ? -5.369  12.155  26.148  1.00 53.95  ? 300  ASP A CG  1 
ATOM   2425 O  OD1 . ASP A 1 300 ? -4.681  13.131  26.521  1.00 50.78  ? 300  ASP A OD1 1 
ATOM   2426 O  OD2 . ASP A 1 300 ? -6.288  12.256  25.301  1.00 52.59  ? 300  ASP A OD2 1 
ATOM   2427 N  N   . PRO A 1 301 ? -3.567  9.159   29.006  1.00 49.75  ? 301  PRO A N   1 
ATOM   2428 C  CA  . PRO A 1 301 ? -3.404  7.869   29.701  1.00 49.04  ? 301  PRO A CA  1 
ATOM   2429 C  C   . PRO A 1 301 ? -4.331  6.796   29.164  1.00 48.09  ? 301  PRO A C   1 
ATOM   2430 O  O   . PRO A 1 301 ? -3.948  5.621   29.132  1.00 49.13  ? 301  PRO A O   1 
ATOM   2431 C  CB  . PRO A 1 301 ? -3.710  8.199   31.172  1.00 50.27  ? 301  PRO A CB  1 
ATOM   2432 C  CG  . PRO A 1 301 ? -3.974  9.668   31.246  1.00 53.23  ? 301  PRO A CG  1 
ATOM   2433 C  CD  . PRO A 1 301 ? -4.092  10.230  29.869  1.00 52.31  ? 301  PRO A CD  1 
ATOM   2434 N  N   . VAL A 1 302 ? -5.526  7.179   28.726  1.00 43.69  ? 302  VAL A N   1 
ATOM   2435 C  CA  . VAL A 1 302 ? -6.521  6.270   28.172  1.00 49.45  ? 302  VAL A CA  1 
ATOM   2436 C  C   . VAL A 1 302 ? -6.743  6.663   26.718  1.00 46.39  ? 302  VAL A C   1 
ATOM   2437 O  O   . VAL A 1 302 ? -7.045  7.827   26.446  1.00 46.60  ? 302  VAL A O   1 
ATOM   2438 C  CB  . VAL A 1 302 ? -7.850  6.339   28.946  1.00 50.96  ? 302  VAL A CB  1 
ATOM   2439 C  CG1 . VAL A 1 302 ? -8.858  5.375   28.371  1.00 56.59  ? 302  VAL A CG1 1 
ATOM   2440 C  CG2 . VAL A 1 302 ? -7.622  6.099   30.447  1.00 58.19  ? 302  VAL A CG2 1 
ATOM   2441 N  N   . PRO A 1 303 ? -6.620  5.747   25.754  1.00 45.60  ? 303  PRO A N   1 
ATOM   2442 C  CA  . PRO A 1 303 ? -6.907  6.113   24.358  1.00 39.80  ? 303  PRO A CA  1 
ATOM   2443 C  C   . PRO A 1 303 ? -8.375  6.447   24.149  1.00 41.69  ? 303  PRO A C   1 
ATOM   2444 O  O   . PRO A 1 303 ? -9.263  5.868   24.780  1.00 40.15  ? 303  PRO A O   1 
ATOM   2445 C  CB  . PRO A 1 303 ? -6.503  4.861   23.570  1.00 48.76  ? 303  PRO A CB  1 
ATOM   2446 C  CG  . PRO A 1 303 ? -5.546  4.139   24.474  1.00 44.56  ? 303  PRO A CG  1 
ATOM   2447 C  CD  . PRO A 1 303 ? -6.049  4.394   25.859  1.00 44.16  ? 303  PRO A CD  1 
ATOM   2448 N  N   . SER A 1 304 ? -8.627  7.409   23.265  1.00 39.60  ? 304  SER A N   1 
ATOM   2449 C  CA  . SER A 1 304 ? -9.986  7.735   22.865  1.00 39.16  ? 304  SER A CA  1 
ATOM   2450 C  C   . SER A 1 304 ? -10.323 7.069   21.529  1.00 37.90  ? 304  SER A C   1 
ATOM   2451 O  O   . SER A 1 304 ? -9.444  6.651   20.774  1.00 35.75  ? 304  SER A O   1 
ATOM   2452 C  CB  . SER A 1 304 ? -10.167 9.249   22.752  1.00 42.34  ? 304  SER A CB  1 
ATOM   2453 O  OG  . SER A 1 304 ? -9.483  9.721   21.611  1.00 40.36  ? 304  SER A OG  1 
ATOM   2454 N  N   . TYR A 1 305 ? -11.624 6.976   21.251  1.00 37.90  ? 305  TYR A N   1 
ATOM   2455 C  CA  . TYR A 1 305 ? -12.073 6.479   19.952  1.00 39.44  ? 305  TYR A CA  1 
ATOM   2456 C  C   . TYR A 1 305 ? -11.380 7.221   18.814  1.00 40.47  ? 305  TYR A C   1 
ATOM   2457 O  O   . TYR A 1 305 ? -10.869 6.606   17.871  1.00 40.53  ? 305  TYR A O   1 
ATOM   2458 C  CB  . TYR A 1 305 ? -13.591 6.628   19.837  1.00 40.96  ? 305  TYR A CB  1 
ATOM   2459 C  CG  . TYR A 1 305 ? -14.136 6.153   18.509  1.00 42.97  ? 305  TYR A CG  1 
ATOM   2460 C  CD1 . TYR A 1 305 ? -14.436 4.813   18.308  1.00 41.66  ? 305  TYR A CD1 1 
ATOM   2461 C  CD2 . TYR A 1 305 ? -14.348 7.043   17.457  1.00 44.81  ? 305  TYR A CD2 1 
ATOM   2462 C  CE1 . TYR A 1 305 ? -14.928 4.364   17.093  1.00 45.60  ? 305  TYR A CE1 1 
ATOM   2463 C  CE2 . TYR A 1 305 ? -14.842 6.598   16.237  1.00 44.40  ? 305  TYR A CE2 1 
ATOM   2464 C  CZ  . TYR A 1 305 ? -15.128 5.254   16.069  1.00 46.39  ? 305  TYR A CZ  1 
ATOM   2465 O  OH  . TYR A 1 305 ? -15.624 4.787   14.871  1.00 55.93  ? 305  TYR A OH  1 
ATOM   2466 N  N   . LYS A 1 306 ? -11.351 8.558   18.897  1.00 40.95  ? 306  LYS A N   1 
ATOM   2467 C  CA  . LYS A 1 306 ? -10.775 9.362   17.826  1.00 40.88  ? 306  LYS A CA  1 
ATOM   2468 C  C   . LYS A 1 306 ? -9.296  9.070   17.653  1.00 40.98  ? 306  LYS A C   1 
ATOM   2469 O  O   . LYS A 1 306 ? -8.789  9.041   16.529  1.00 42.72  ? 306  LYS A O   1 
ATOM   2470 C  CB  . LYS A 1 306 ? -10.988 10.852  18.108  1.00 46.91  ? 306  LYS A CB  1 
ATOM   2471 C  CG  . LYS A 1 306 ? -12.273 11.425  17.557  1.00 52.93  ? 306  LYS A CG  1 
ATOM   2472 C  CD  . LYS A 1 306 ? -12.437 12.869  18.012  1.00 57.02  ? 306  LYS A CD  1 
ATOM   2473 C  CE  . LYS A 1 306 ? -13.887 13.196  18.312  1.00 64.91  ? 306  LYS A CE  1 
ATOM   2474 N  NZ  . LYS A 1 306 ? -14.020 14.450  19.108  1.00 73.48  ? 306  LYS A NZ  1 
ATOM   2475 N  N   . GLN A 1 307 ? -8.582  8.844   18.755  1.00 39.10  ? 307  GLN A N   1 
ATOM   2476 C  CA  . GLN A 1 307 ? -7.153  8.577   18.638  1.00 38.61  ? 307  GLN A CA  1 
ATOM   2477 C  C   . GLN A 1 307 ? -6.894  7.231   17.967  1.00 37.62  ? 307  GLN A C   1 
ATOM   2478 O  O   . GLN A 1 307 ? -5.952  7.092   17.179  1.00 39.49  ? 307  GLN A O   1 
ATOM   2479 C  CB  . GLN A 1 307 ? -6.502  8.641   20.023  1.00 37.14  ? 307  GLN A CB  1 
ATOM   2480 C  CG  . GLN A 1 307 ? -6.563  10.044  20.609  1.00 43.09  ? 307  GLN A CG  1 
ATOM   2481 C  CD  . GLN A 1 307 ? -6.239  10.097  22.091  1.00 47.12  ? 307  GLN A CD  1 
ATOM   2482 O  OE1 . GLN A 1 307 ? -6.285  9.085   22.787  1.00 42.54  ? 307  GLN A OE1 1 
ATOM   2483 N  NE2 . GLN A 1 307 ? -5.915  11.292  22.584  1.00 47.97  ? 307  GLN A NE2 1 
ATOM   2484 N  N   . VAL A 1 308 ? -7.708  6.219   18.281  1.00 38.99  ? 308  VAL A N   1 
ATOM   2485 C  CA  . VAL A 1 308 ? -7.504  4.907   17.669  1.00 37.36  ? 308  VAL A CA  1 
ATOM   2486 C  C   . VAL A 1 308 ? -7.693  5.003   16.161  1.00 36.39  ? 308  VAL A C   1 
ATOM   2487 O  O   . VAL A 1 308 ? -6.989  4.347   15.388  1.00 37.36  ? 308  VAL A O   1 
ATOM   2488 C  CB  . VAL A 1 308 ? -8.453  3.868   18.299  1.00 38.22  ? 308  VAL A CB  1 
ATOM   2489 C  CG1 . VAL A 1 308 ? -8.405  2.538   17.515  1.00 37.06  ? 308  VAL A CG1 1 
ATOM   2490 C  CG2 . VAL A 1 308 ? -8.126  3.674   19.779  1.00 39.33  ? 308  VAL A CG2 1 
ATOM   2491 N  N   . LYS A 1 309 ? -8.640  5.836   15.723  1.00 39.12  ? 309  LYS A N   1 
ATOM   2492 C  CA  . LYS A 1 309 ? -8.861  6.046   14.299  1.00 42.95  ? 309  LYS A CA  1 
ATOM   2493 C  C   . LYS A 1 309 ? -7.664  6.690   13.622  1.00 42.54  ? 309  LYS A C   1 
ATOM   2494 O  O   . LYS A 1 309 ? -7.542  6.609   12.400  1.00 41.13  ? 309  LYS A O   1 
ATOM   2495 C  CB  . LYS A 1 309 ? -10.098 6.911   14.081  1.00 41.96  ? 309  LYS A CB  1 
ATOM   2496 C  CG  . LYS A 1 309 ? -11.407 6.209   14.402  1.00 45.84  ? 309  LYS A CG  1 
ATOM   2497 C  CD  . LYS A 1 309 ? -11.535 4.932   13.578  1.00 46.63  ? 309  LYS A CD  1 
ATOM   2498 C  CE  . LYS A 1 309 ? -12.888 4.277   13.765  1.00 52.42  ? 309  LYS A CE  1 
ATOM   2499 N  NZ  . LYS A 1 309 ? -12.956 2.963   13.061  1.00 57.07  ? 309  LYS A NZ  1 
ATOM   2500 N  N   . GLN A 1 310 ? -6.783  7.332   14.380  1.00 41.46  ? 310  GLN A N   1 
ATOM   2501 C  CA  . GLN A 1 310 ? -5.595  7.931   13.797  1.00 41.36  ? 310  GLN A CA  1 
ATOM   2502 C  C   . GLN A 1 310 ? -4.389  7.006   13.829  1.00 40.39  ? 310  GLN A C   1 
ATOM   2503 O  O   . GLN A 1 310 ? -3.315  7.397   13.359  1.00 41.25  ? 310  GLN A O   1 
ATOM   2504 C  CB  . GLN A 1 310 ? -5.276  9.259   14.496  1.00 45.03  ? 310  GLN A CB  1 
ATOM   2505 C  CG  . GLN A 1 310 ? -6.291  10.362  14.190  1.00 48.49  ? 310  GLN A CG  1 
ATOM   2506 C  CD  . GLN A 1 310 ? -6.551  10.513  12.687  1.00 52.97  ? 310  GLN A CD  1 
ATOM   2507 O  OE1 . GLN A 1 310 ? -5.612  10.546  11.891  1.00 53.83  ? 310  GLN A OE1 1 
ATOM   2508 N  NE2 . GLN A 1 310 ? -7.820  10.604  12.298  1.00 45.66  ? 310  GLN A NE2 1 
ATOM   2509 N  N   . LEU A 1 311 ? -4.536  5.778   14.333  1.00 37.64  ? 311  LEU A N   1 
ATOM   2510 C  CA  . LEU A 1 311 ? -3.422  4.824   14.340  1.00 36.17  ? 311  LEU A CA  1 
ATOM   2511 C  C   . LEU A 1 311 ? -3.374  4.099   12.992  1.00 43.86  ? 311  LEU A C   1 
ATOM   2512 O  O   . LEU A 1 311 ? -3.588  2.889   12.870  1.00 38.30  ? 311  LEU A O   1 
ATOM   2513 C  CB  . LEU A 1 311 ? -3.556  3.849   15.506  1.00 34.86  ? 311  LEU A CB  1 
ATOM   2514 C  CG  . LEU A 1 311 ? -3.391  4.477   16.899  1.00 38.04  ? 311  LEU A CG  1 
ATOM   2515 C  CD1 . LEU A 1 311 ? -3.727  3.450   17.967  1.00 34.40  ? 311  LEU A CD1 1 
ATOM   2516 C  CD2 . LEU A 1 311 ? -1.967  4.986   17.080  1.00 43.45  ? 311  LEU A CD2 1 
ATOM   2517 N  N   . LYS A 1 312 ? -3.043  4.873   11.959  1.00 39.95  ? 312  LYS A N   1 
ATOM   2518 C  CA  . LYS A 1 312 ? -3.220  4.386   10.602  1.00 42.88  ? 312  LYS A CA  1 
ATOM   2519 C  C   . LYS A 1 312 ? -2.144  3.372   10.223  1.00 39.63  ? 312  LYS A C   1 
ATOM   2520 O  O   . LYS A 1 312 ? -2.447  2.361   9.585   1.00 38.61  ? 312  LYS A O   1 
ATOM   2521 C  CB  . LYS A 1 312 ? -3.278  5.590   9.662   1.00 42.10  ? 312  LYS A CB  1 
ATOM   2522 C  CG  . LYS A 1 312 ? -4.672  6.209   9.722   1.00 48.50  ? 312  LYS A CG  1 
ATOM   2523 C  CD  . LYS A 1 312 ? -4.824  7.522   8.990   1.00 58.00  ? 312  LYS A CD  1 
ATOM   2524 C  CE  . LYS A 1 312 ? -6.291  7.947   9.011   1.00 55.08  ? 312  LYS A CE  1 
ATOM   2525 N  NZ  . LYS A 1 312 ? -6.444  9.428   9.019   1.00 64.97  ? 312  LYS A NZ  1 
ATOM   2526 N  N   . TYR A 1 313 ? -0.893  3.588   10.649  1.00 37.68  ? 313  TYR A N   1 
ATOM   2527 C  CA  . TYR A 1 313 ? 0.143   2.606   10.373  1.00 37.72  ? 313  TYR A CA  1 
ATOM   2528 C  C   . TYR A 1 313 ? -0.092  1.308   11.146  1.00 35.38  ? 313  TYR A C   1 
ATOM   2529 O  O   . TYR A 1 313 ? 0.150   0.218   10.619  1.00 36.95  ? 313  TYR A O   1 
ATOM   2530 C  CB  . TYR A 1 313 ? 1.519   3.177   10.702  1.00 43.46  ? 313  TYR A CB  1 
ATOM   2531 C  CG  . TYR A 1 313 ? 2.611   2.292   10.193  1.00 38.68  ? 313  TYR A CG  1 
ATOM   2532 C  CD1 . TYR A 1 313 ? 2.913   2.252   8.836   1.00 41.90  ? 313  TYR A CD1 1 
ATOM   2533 C  CD2 . TYR A 1 313 ? 3.322   1.467   11.050  1.00 38.12  ? 313  TYR A CD2 1 
ATOM   2534 C  CE1 . TYR A 1 313 ? 3.904   1.431   8.349   1.00 42.79  ? 313  TYR A CE1 1 
ATOM   2535 C  CE2 . TYR A 1 313 ? 4.308   0.627   10.571  1.00 38.96  ? 313  TYR A CE2 1 
ATOM   2536 C  CZ  . TYR A 1 313 ? 4.607   0.629   9.219   1.00 42.49  ? 313  TYR A CZ  1 
ATOM   2537 O  OH  . TYR A 1 313 ? 5.581   -0.192  8.726   1.00 39.94  ? 313  TYR A OH  1 
ATOM   2538 N  N   . VAL A 1 314 ? -0.534  1.404   12.406  1.00 37.43  ? 314  VAL A N   1 
ATOM   2539 C  CA  . VAL A 1 314 ? -0.934  0.201   13.140  1.00 37.33  ? 314  VAL A CA  1 
ATOM   2540 C  C   . VAL A 1 314 ? -1.997  -0.559  12.350  1.00 35.20  ? 314  VAL A C   1 
ATOM   2541 O  O   . VAL A 1 314 ? -1.970  -1.792  12.255  1.00 35.90  ? 314  VAL A O   1 
ATOM   2542 C  CB  . VAL A 1 314 ? -1.436  0.578   14.548  1.00 37.05  ? 314  VAL A CB  1 
ATOM   2543 C  CG1 . VAL A 1 314 ? -1.983  -0.662  15.292  1.00 38.82  ? 314  VAL A CG1 1 
ATOM   2544 C  CG2 . VAL A 1 314 ? -0.323  1.275   15.373  1.00 38.14  ? 314  VAL A CG2 1 
ATOM   2545 N  N   . GLY A 1 315 ? -2.937  0.173   11.759  1.00 35.17  ? 315  GLY A N   1 
ATOM   2546 C  CA  . GLY A 1 315 ? -3.941  -0.462  10.915  1.00 37.09  ? 315  GLY A CA  1 
ATOM   2547 C  C   . GLY A 1 315 ? -3.347  -1.242  9.751   1.00 38.74  ? 315  GLY A C   1 
ATOM   2548 O  O   . GLY A 1 315 ? -3.823  -2.332  9.414   1.00 33.03  ? 315  GLY A O   1 
ATOM   2549 N  N   . MET A 1 316 ? -2.318  -0.683  9.097   1.00 35.73  ? 316  MET A N   1 
ATOM   2550 C  CA  . MET A 1 316 ? -1.658  -1.408  8.009   1.00 33.27  ? 316  MET A CA  1 
ATOM   2551 C  C   . MET A 1 316 ? -0.859  -2.598  8.516   1.00 33.68  ? 316  MET A C   1 
ATOM   2552 O  O   . MET A 1 316 ? -0.753  -3.608  7.813   1.00 33.38  ? 316  MET A O   1 
ATOM   2553 C  CB  . MET A 1 316 ? -0.751  -0.469  7.186   1.00 36.91  ? 316  MET A CB  1 
ATOM   2554 C  CG  . MET A 1 316 ? -1.470  0.798   6.708   1.00 40.04  ? 316  MET A CG  1 
ATOM   2555 S  SD  . MET A 1 316 ? -0.417  2.090   5.961   1.00 49.26  ? 316  MET A SD  1 
ATOM   2556 C  CE  . MET A 1 316 ? 0.872   1.126   5.231   1.00 46.38  ? 316  MET A CE  1 
ATOM   2557 N  N   . VAL A 1 317 ? -0.268  -2.498  9.710   1.00 33.68  ? 317  VAL A N   1 
ATOM   2558 C  CA  . VAL A 1 317 ? 0.388   -3.658  10.310  1.00 35.40  ? 317  VAL A CA  1 
ATOM   2559 C  C   . VAL A 1 317 ? -0.595  -4.813  10.436  1.00 33.43  ? 317  VAL A C   1 
ATOM   2560 O  O   . VAL A 1 317 ? -0.291  -5.958  10.085  1.00 33.13  ? 317  VAL A O   1 
ATOM   2561 C  CB  . VAL A 1 317 ? 0.987   -3.284  11.679  1.00 36.17  ? 317  VAL A CB  1 
ATOM   2562 C  CG1 . VAL A 1 317 ? 1.344   -4.545  12.478  1.00 31.48  ? 317  VAL A CG1 1 
ATOM   2563 C  CG2 . VAL A 1 317 ? 2.210   -2.389  11.493  1.00 35.43  ? 317  VAL A CG2 1 
ATOM   2564 N  N   . LEU A 1 318 ? -1.801  -4.519  10.916  1.00 35.26  ? 318  LEU A N   1 
ATOM   2565 C  CA  . LEU A 1 318 ? -2.787  -5.573  11.100  1.00 35.65  ? 318  LEU A CA  1 
ATOM   2566 C  C   . LEU A 1 318 ? -3.254  -6.131  9.759   1.00 32.76  ? 318  LEU A C   1 
ATOM   2567 O  O   . LEU A 1 318 ? -3.449  -7.341  9.620   1.00 32.17  ? 318  LEU A O   1 
ATOM   2568 C  CB  . LEU A 1 318 ? -3.962  -5.036  11.922  1.00 35.04  ? 318  LEU A CB  1 
ATOM   2569 C  CG  . LEU A 1 318 ? -3.631  -4.669  13.374  1.00 34.60  ? 318  LEU A CG  1 
ATOM   2570 C  CD1 . LEU A 1 318 ? -4.732  -3.770  13.966  1.00 36.06  ? 318  LEU A CD1 1 
ATOM   2571 C  CD2 . LEU A 1 318 ? -3.467  -5.950  14.182  1.00 33.71  ? 318  LEU A CD2 1 
ATOM   2572 N  N   . ASN A 1 319 ? -3.429  -5.273  8.750   1.00 32.74  ? 319  ASN A N   1 
ATOM   2573 C  CA  . ASN A 1 319 ? -3.812  -5.787  7.439   1.00 34.64  ? 319  ASN A CA  1 
ATOM   2574 C  C   . ASN A 1 319 ? -2.727  -6.679  6.860   1.00 33.49  ? 319  ASN A C   1 
ATOM   2575 O  O   . ASN A 1 319 ? -3.020  -7.689  6.214   1.00 32.37  ? 319  ASN A O   1 
ATOM   2576 C  CB  . ASN A 1 319 ? -4.146  -4.630  6.504   1.00 35.36  ? 319  ASN A CB  1 
ATOM   2577 C  CG  . ASN A 1 319 ? -5.564  -4.149  6.700   1.00 42.26  ? 319  ASN A CG  1 
ATOM   2578 O  OD1 . ASN A 1 319 ? -6.450  -4.949  7.002   1.00 38.81  ? 319  ASN A OD1 1 
ATOM   2579 N  ND2 . ASN A 1 319 ? -5.785  -2.848  6.575   1.00 43.05  ? 319  ASN A ND2 1 
ATOM   2580 N  N   . GLU A 1 320 ? -1.463  -6.317  7.072   1.00 33.20  ? 320  GLU A N   1 
ATOM   2581 C  CA  . GLU A 1 320 ? -0.377  -7.129  6.544   1.00 33.76  ? 320  GLU A CA  1 
ATOM   2582 C  C   . GLU A 1 320 ? -0.295  -8.466  7.278   1.00 33.40  ? 320  GLU A C   1 
ATOM   2583 O  O   . GLU A 1 320 ? -0.001  -9.495  6.665   1.00 32.30  ? 320  GLU A O   1 
ATOM   2584 C  CB  . GLU A 1 320 ? 0.926   -6.326  6.636   1.00 33.11  ? 320  GLU A CB  1 
ATOM   2585 C  CG  . GLU A 1 320 ? 2.192   -7.023  6.111   1.00 37.66  ? 320  GLU A CG  1 
ATOM   2586 C  CD  . GLU A 1 320 ? 2.199   -7.249  4.601   1.00 40.50  ? 320  GLU A CD  1 
ATOM   2587 O  OE1 . GLU A 1 320 ? 1.131   -7.149  3.942   1.00 36.18  ? 320  GLU A OE1 1 
ATOM   2588 O  OE2 . GLU A 1 320 ? 3.284   -7.563  4.062   1.00 37.40  ? 320  GLU A OE2 1 
ATOM   2589 N  N   . ALA A 1 321 ? -0.584  -8.476  8.589   1.00 32.34  ? 321  ALA A N   1 
ATOM   2590 C  CA  . ALA A 1 321 ? -0.669  -9.742  9.321   1.00 33.87  ? 321  ALA A CA  1 
ATOM   2591 C  C   . ALA A 1 321 ? -1.844  -10.582 8.834   1.00 29.96  ? 321  ALA A C   1 
ATOM   2592 O  O   . ALA A 1 321 ? -1.735  -11.806 8.730   1.00 31.05  ? 321  ALA A O   1 
ATOM   2593 C  CB  . ALA A 1 321 ? -0.779  -9.481  10.837  1.00 32.03  ? 321  ALA A CB  1 
ATOM   2594 N  N   . LEU A 1 322 ? -2.981  -9.940  8.515   1.00 32.40  ? 322  LEU A N   1 
ATOM   2595 C  CA  . LEU A 1 322 ? -4.082  -10.680 7.899   1.00 33.00  ? 322  LEU A CA  1 
ATOM   2596 C  C   . LEU A 1 322 ? -3.728  -11.166 6.495   1.00 33.61  ? 322  LEU A C   1 
ATOM   2597 O  O   . LEU A 1 322 ? -4.268  -12.182 6.035   1.00 32.46  ? 322  LEU A O   1 
ATOM   2598 C  CB  . LEU A 1 322 ? -5.342  -9.811  7.839   1.00 31.92  ? 322  LEU A CB  1 
ATOM   2599 C  CG  . LEU A 1 322 ? -6.045  -9.635  9.184   1.00 36.37  ? 322  LEU A CG  1 
ATOM   2600 C  CD1 . LEU A 1 322 ? -7.184  -8.614  9.037   1.00 38.52  ? 322  LEU A CD1 1 
ATOM   2601 C  CD2 . LEU A 1 322 ? -6.552  -10.966 9.733   1.00 33.84  ? 322  LEU A CD2 1 
ATOM   2602 N  N   . ARG A 1 323 ? -2.843  -10.458 5.786   1.00 33.59  ? 323  ARG A N   1 
ATOM   2603 C  CA  . ARG A 1 323 ? -2.424  -10.959 4.481   1.00 32.61  ? 323  ARG A CA  1 
ATOM   2604 C  C   . ARG A 1 323 ? -1.683  -12.281 4.624   1.00 30.50  ? 323  ARG A C   1 
ATOM   2605 O  O   . ARG A 1 323 ? -2.038  -13.276 3.995   1.00 33.90  ? 323  ARG A O   1 
ATOM   2606 C  CB  . ARG A 1 323 ? -1.549  -9.936  3.748   1.00 32.31  ? 323  ARG A CB  1 
ATOM   2607 C  CG  . ARG A 1 323 ? -1.292  -10.377 2.299   1.00 35.21  ? 323  ARG A CG  1 
ATOM   2608 C  CD  . ARG A 1 323 ? -0.334  -9.437  1.550   1.00 34.90  ? 323  ARG A CD  1 
ATOM   2609 N  NE  . ARG A 1 323 ? 0.990   -9.363  2.160   1.00 36.79  ? 323  ARG A NE  1 
ATOM   2610 C  CZ  . ARG A 1 323 ? 1.966   -10.241 1.943   1.00 35.93  ? 323  ARG A CZ  1 
ATOM   2611 N  NH1 . ARG A 1 323 ? 1.797   -11.277 1.148   1.00 38.50  ? 323  ARG A NH1 1 
ATOM   2612 N  NH2 . ARG A 1 323 ? 3.134   -10.081 2.560   1.00 38.70  ? 323  ARG A NH2 1 
ATOM   2613 N  N   . LEU A 1 324 ? -0.666  -12.324 5.485   1.00 33.04  ? 324  LEU A N   1 
ATOM   2614 C  CA  . LEU A 1 324 ? 0.168   -13.521 5.535   1.00 33.68  ? 324  LEU A CA  1 
ATOM   2615 C  C   . LEU A 1 324 ? -0.536  -14.681 6.233   1.00 34.18  ? 324  LEU A C   1 
ATOM   2616 O  O   . LEU A 1 324 ? -0.397  -15.837 5.822   1.00 35.08  ? 324  LEU A O   1 
ATOM   2617 C  CB  . LEU A 1 324 ? 1.490   -13.180 6.211   1.00 38.34  ? 324  LEU A CB  1 
ATOM   2618 C  CG  . LEU A 1 324 ? 2.358   -12.388 5.228   1.00 39.24  ? 324  LEU A CG  1 
ATOM   2619 C  CD1 . LEU A 1 324 ? 3.552   -11.739 5.938   1.00 43.57  ? 324  LEU A CD1 1 
ATOM   2620 C  CD2 . LEU A 1 324 ? 2.801   -13.297 4.078   1.00 42.55  ? 324  LEU A CD2 1 
ATOM   2621 N  N   . TRP A 1 325 ? -1.318  -14.410 7.272   1.00 33.29  ? 325  TRP A N   1 
ATOM   2622 C  CA  . TRP A 1 325 ? -1.963  -15.480 8.034   1.00 31.44  ? 325  TRP A CA  1 
ATOM   2623 C  C   . TRP A 1 325 ? -3.380  -15.074 8.402   1.00 31.92  ? 325  TRP A C   1 
ATOM   2624 O  O   . TRP A 1 325 ? -3.680  -14.778 9.563   1.00 33.71  ? 325  TRP A O   1 
ATOM   2625 C  CB  . TRP A 1 325 ? -1.136  -15.834 9.273   1.00 33.11  ? 325  TRP A CB  1 
ATOM   2626 C  CG  . TRP A 1 325 ? 0.049   -16.592 8.850   1.00 33.39  ? 325  TRP A CG  1 
ATOM   2627 C  CD1 . TRP A 1 325 ? 1.346   -16.196 8.944   1.00 36.30  ? 325  TRP A CD1 1 
ATOM   2628 C  CD2 . TRP A 1 325 ? 0.053   -17.853 8.186   1.00 33.55  ? 325  TRP A CD2 1 
ATOM   2629 N  NE1 . TRP A 1 325 ? 2.167   -17.147 8.389   1.00 35.86  ? 325  TRP A NE1 1 
ATOM   2630 C  CE2 . TRP A 1 325 ? 1.395   -18.182 7.926   1.00 35.77  ? 325  TRP A CE2 1 
ATOM   2631 C  CE3 . TRP A 1 325 ? -0.948  -18.752 7.804   1.00 34.96  ? 325  TRP A CE3 1 
ATOM   2632 C  CZ2 . TRP A 1 325 ? 1.763   -19.366 7.287   1.00 36.18  ? 325  TRP A CZ2 1 
ATOM   2633 C  CZ3 . TRP A 1 325 ? -0.580  -19.936 7.166   1.00 39.06  ? 325  TRP A CZ3 1 
ATOM   2634 C  CH2 . TRP A 1 325 ? 0.769   -20.228 6.918   1.00 39.97  ? 325  TRP A CH2 1 
ATOM   2635 N  N   . PRO A 1 326 ? -4.289  -15.075 7.426   1.00 32.34  ? 326  PRO A N   1 
ATOM   2636 C  CA  . PRO A 1 326 ? -5.705  -14.818 7.737   1.00 31.21  ? 326  PRO A CA  1 
ATOM   2637 C  C   . PRO A 1 326 ? -6.245  -15.914 8.639   1.00 31.05  ? 326  PRO A C   1 
ATOM   2638 O  O   . PRO A 1 326 ? -6.167  -17.098 8.303   1.00 31.62  ? 326  PRO A O   1 
ATOM   2639 C  CB  . PRO A 1 326 ? -6.376  -14.841 6.358   1.00 31.69  ? 326  PRO A CB  1 
ATOM   2640 C  CG  . PRO A 1 326 ? -5.482  -15.714 5.529   1.00 33.25  ? 326  PRO A CG  1 
ATOM   2641 C  CD  . PRO A 1 326 ? -4.082  -15.398 6.003   1.00 31.69  ? 326  PRO A CD  1 
ATOM   2642 N  N   . THR A 1 327 ? -6.849  -15.508 9.765   1.00 32.00  ? 327  THR A N   1 
ATOM   2643 C  CA  . THR A 1 327 ? -7.070  -16.440 10.866  1.00 32.29  ? 327  THR A CA  1 
ATOM   2644 C  C   . THR A 1 327 ? -8.345  -17.260 10.709  1.00 33.01  ? 327  THR A C   1 
ATOM   2645 O  O   . THR A 1 327 ? -8.489  -18.280 11.388  1.00 31.90  ? 327  THR A O   1 
ATOM   2646 C  CB  . THR A 1 327 ? -7.066  -15.675 12.198  1.00 32.92  ? 327  THR A CB  1 
ATOM   2647 O  OG1 . THR A 1 327 ? -7.893  -14.516 12.092  1.00 31.55  ? 327  THR A OG1 1 
ATOM   2648 C  CG2 . THR A 1 327 ? -5.647  -15.186 12.510  1.00 31.15  ? 327  THR A CG2 1 
ATOM   2649 N  N   . ALA A 1 328 ? -9.273  -16.841 9.838   1.00 30.83  ? 328  ALA A N   1 
ATOM   2650 C  CA  . ALA A 1 328 ? -10.290 -17.754 9.338   1.00 30.20  ? 328  ALA A CA  1 
ATOM   2651 C  C   . ALA A 1 328 ? -9.918  -18.084 7.898   1.00 32.68  ? 328  ALA A C   1 
ATOM   2652 O  O   . ALA A 1 328 ? -10.307 -17.360 6.976   1.00 34.06  ? 328  ALA A O   1 
ATOM   2653 C  CB  . ALA A 1 328 ? -11.688 -17.133 9.437   1.00 33.87  ? 328  ALA A CB  1 
ATOM   2654 N  N   . PRO A 1 329 ? -9.167  -19.166 7.667   1.00 31.77  ? 329  PRO A N   1 
ATOM   2655 C  CA  . PRO A 1 329 ? -8.306  -19.236 6.475   1.00 30.40  ? 329  PRO A CA  1 
ATOM   2656 C  C   . PRO A 1 329 ? -8.988  -19.693 5.199   1.00 32.77  ? 329  PRO A C   1 
ATOM   2657 O  O   . PRO A 1 329 ? -8.313  -19.818 4.168   1.00 34.34  ? 329  PRO A O   1 
ATOM   2658 C  CB  . PRO A 1 329 ? -7.223  -20.240 6.903   1.00 31.45  ? 329  PRO A CB  1 
ATOM   2659 C  CG  . PRO A 1 329 ? -7.943  -21.170 7.876   1.00 32.18  ? 329  PRO A CG  1 
ATOM   2660 C  CD  . PRO A 1 329 ? -8.859  -20.226 8.655   1.00 30.93  ? 329  PRO A CD  1 
ATOM   2661 N  N   . ALA A 1 330 ? -10.286 -19.950 5.204   1.00 30.84  ? 330  ALA A N   1 
ATOM   2662 C  CA  . ALA A 1 330 ? -10.942 -20.325 3.959   1.00 30.80  ? 330  ALA A CA  1 
ATOM   2663 C  C   . ALA A 1 330 ? -12.414 -19.993 4.084   1.00 31.48  ? 330  ALA A C   1 
ATOM   2664 O  O   . ALA A 1 330 ? -12.955 -19.866 5.187   1.00 34.72  ? 330  ALA A O   1 
ATOM   2665 C  CB  . ALA A 1 330 ? -10.758 -21.809 3.640   1.00 32.19  ? 330  ALA A CB  1 
ATOM   2666 N  N   . PHE A 1 331 ? -13.039 -19.810 2.935   1.00 32.51  ? 331  PHE A N   1 
ATOM   2667 C  CA  . PHE A 1 331 ? -14.481 -19.807 2.871   1.00 30.07  ? 331  PHE A CA  1 
ATOM   2668 C  C   . PHE A 1 331 ? -14.877 -20.558 1.614   1.00 33.51  ? 331  PHE A C   1 
ATOM   2669 O  O   . PHE A 1 331 ? -14.054 -20.801 0.723   1.00 34.35  ? 331  PHE A O   1 
ATOM   2670 C  CB  . PHE A 1 331 ? -15.071 -18.382 2.944   1.00 32.58  ? 331  PHE A CB  1 
ATOM   2671 C  CG  . PHE A 1 331 ? -14.580 -17.430 1.874   1.00 31.54  ? 331  PHE A CG  1 
ATOM   2672 C  CD1 . PHE A 1 331 ? -13.421 -16.693 2.068   1.00 34.49  ? 331  PHE A CD1 1 
ATOM   2673 C  CD2 . PHE A 1 331 ? -15.315 -17.226 0.713   1.00 32.73  ? 331  PHE A CD2 1 
ATOM   2674 C  CE1 . PHE A 1 331 ? -12.986 -15.778 1.125   1.00 34.89  ? 331  PHE A CE1 1 
ATOM   2675 C  CE2 . PHE A 1 331 ? -14.875 -16.305 -0.253  1.00 34.42  ? 331  PHE A CE2 1 
ATOM   2676 C  CZ  . PHE A 1 331 ? -13.720 -15.582 -0.040  1.00 31.16  ? 331  PHE A CZ  1 
ATOM   2677 N  N   . SER A 1 332 ? -16.144 -20.962 1.572   1.00 34.62  ? 332  SER A N   1 
ATOM   2678 C  CA  . SER A 1 332 ? -16.660 -21.866 0.560   1.00 35.06  ? 332  SER A CA  1 
ATOM   2679 C  C   . SER A 1 332 ? -17.781 -21.178 -0.207  1.00 33.93  ? 332  SER A C   1 
ATOM   2680 O  O   . SER A 1 332 ? -18.499 -20.327 0.332   1.00 34.65  ? 332  SER A O   1 
ATOM   2681 C  CB  . SER A 1 332 ? -17.170 -23.168 1.202   1.00 33.11  ? 332  SER A CB  1 
ATOM   2682 O  OG  . SER A 1 332 ? -17.535 -24.139 0.233   1.00 36.25  ? 332  SER A OG  1 
ATOM   2683 N  N   . LEU A 1 333 ? -17.907 -21.542 -1.475  1.00 32.95  ? 333  LEU A N   1 
ATOM   2684 C  CA  . LEU A 1 333 ? -18.904 -20.981 -2.373  1.00 35.00  ? 333  LEU A CA  1 
ATOM   2685 C  C   . LEU A 1 333 ? -19.522 -22.110 -3.185  1.00 34.27  ? 333  LEU A C   1 
ATOM   2686 O  O   . LEU A 1 333 ? -18.931 -23.183 -3.326  1.00 35.50  ? 333  LEU A O   1 
ATOM   2687 C  CB  . LEU A 1 333 ? -18.279 -19.938 -3.316  1.00 31.07  ? 333  LEU A CB  1 
ATOM   2688 C  CG  . LEU A 1 333 ? -17.513 -18.807 -2.624  1.00 35.01  ? 333  LEU A CG  1 
ATOM   2689 C  CD1 . LEU A 1 333 ? -16.537 -18.125 -3.580  1.00 36.24  ? 333  LEU A CD1 1 
ATOM   2690 C  CD2 . LEU A 1 333 ? -18.516 -17.794 -2.037  1.00 34.32  ? 333  LEU A CD2 1 
ATOM   2691 N  N   . TYR A 1 334 ? -20.732 -21.881 -3.690  1.00 32.57  ? 334  TYR A N   1 
ATOM   2692 C  CA  . TYR A 1 334 ? -21.323 -22.777 -4.679  1.00 33.90  ? 334  TYR A CA  1 
ATOM   2693 C  C   . TYR A 1 334 ? -21.826 -21.963 -5.861  1.00 36.26  ? 334  TYR A C   1 
ATOM   2694 O  O   . TYR A 1 334 ? -22.236 -20.804 -5.719  1.00 33.80  ? 334  TYR A O   1 
ATOM   2695 C  CB  . TYR A 1 334 ? -22.469 -23.637 -4.094  1.00 36.88  ? 334  TYR A CB  1 
ATOM   2696 C  CG  . TYR A 1 334 ? -23.702 -22.841 -3.723  1.00 35.78  ? 334  TYR A CG  1 
ATOM   2697 C  CD1 . TYR A 1 334 ? -23.825 -22.241 -2.465  1.00 34.12  ? 334  TYR A CD1 1 
ATOM   2698 C  CD2 . TYR A 1 334 ? -24.745 -22.677 -4.638  1.00 35.57  ? 334  TYR A CD2 1 
ATOM   2699 C  CE1 . TYR A 1 334 ? -24.955 -21.496 -2.134  1.00 33.05  ? 334  TYR A CE1 1 
ATOM   2700 C  CE2 . TYR A 1 334 ? -25.872 -21.937 -4.322  1.00 39.47  ? 334  TYR A CE2 1 
ATOM   2701 C  CZ  . TYR A 1 334 ? -25.978 -21.351 -3.072  1.00 36.82  ? 334  TYR A CZ  1 
ATOM   2702 O  OH  . TYR A 1 334 ? -27.100 -20.608 -2.771  1.00 38.69  ? 334  TYR A OH  1 
ATOM   2703 N  N   . ALA A 1 335 ? -21.789 -22.580 -7.039  1.00 35.27  ? 335  ALA A N   1 
ATOM   2704 C  CA  . ALA A 1 335 ? -22.246 -21.909 -8.251  1.00 36.27  ? 335  ALA A CA  1 
ATOM   2705 C  C   . ALA A 1 335 ? -23.766 -21.792 -8.261  1.00 37.77  ? 335  ALA A C   1 
ATOM   2706 O  O   . ALA A 1 335 ? -24.481 -22.789 -8.126  1.00 37.22  ? 335  ALA A O   1 
ATOM   2707 C  CB  . ALA A 1 335 ? -21.763 -22.666 -9.489  1.00 40.29  ? 335  ALA A CB  1 
ATOM   2708 N  N   . LYS A 1 336 ? -24.266 -20.566 -8.418  1.00 35.56  ? 336  LYS A N   1 
ATOM   2709 C  CA  . LYS A 1 336 ? -25.713 -20.378 -8.486  1.00 38.10  ? 336  LYS A CA  1 
ATOM   2710 C  C   . LYS A 1 336 ? -26.296 -20.915 -9.789  1.00 42.61  ? 336  LYS A C   1 
ATOM   2711 O  O   . LYS A 1 336 ? -27.471 -21.306 -9.825  1.00 45.59  ? 336  LYS A O   1 
ATOM   2712 C  CB  . LYS A 1 336 ? -26.048 -18.895 -8.326  1.00 40.02  ? 336  LYS A CB  1 
ATOM   2713 C  CG  . LYS A 1 336 ? -25.862 -18.394 -6.887  1.00 38.54  ? 336  LYS A CG  1 
ATOM   2714 C  CD  . LYS A 1 336 ? -25.740 -16.878 -6.839  1.00 41.46  ? 336  LYS A CD  1 
ATOM   2715 C  CE  . LYS A 1 336 ? -27.018 -16.216 -7.309  1.00 42.06  ? 336  LYS A CE  1 
ATOM   2716 N  NZ  . LYS A 1 336 ? -28.174 -16.566 -6.431  1.00 44.20  ? 336  LYS A NZ  1 
ATOM   2717 N  N   . GLU A 1 337 ? -25.499 -20.941 -10.853 1.00 39.28  ? 337  GLU A N   1 
ATOM   2718 C  CA  . GLU A 1 337 ? -25.927 -21.432 -12.158 1.00 41.07  ? 337  GLU A CA  1 
ATOM   2719 C  C   . GLU A 1 337 ? -24.715 -22.044 -12.847 1.00 43.01  ? 337  GLU A C   1 
ATOM   2720 O  O   . GLU A 1 337 ? -23.578 -21.839 -12.424 1.00 38.96  ? 337  GLU A O   1 
ATOM   2721 C  CB  . GLU A 1 337 ? -26.494 -20.296 -13.019 1.00 41.88  ? 337  GLU A CB  1 
ATOM   2722 C  CG  . GLU A 1 337 ? -27.842 -19.768 -12.561 1.00 50.64  ? 337  GLU A CG  1 
ATOM   2723 C  CD  . GLU A 1 337 ? -28.931 -20.822 -12.540 1.00 54.36  ? 337  GLU A CD  1 
ATOM   2724 O  OE1 . GLU A 1 337 ? -28.838 -21.813 -13.296 1.00 59.65  ? 337  GLU A OE1 1 
ATOM   2725 O  OE2 . GLU A 1 337 ? -29.883 -20.660 -11.746 1.00 59.42  ? 337  GLU A OE2 1 
ATOM   2726 N  N   . ASP A 1 338 ? -24.953 -22.772 -13.941 1.00 45.61  ? 338  ASP A N   1 
ATOM   2727 C  CA  . ASP A 1 338 ? -23.839 -23.189 -14.783 1.00 43.31  ? 338  ASP A CA  1 
ATOM   2728 C  C   . ASP A 1 338 ? -22.997 -21.974 -15.146 1.00 42.54  ? 338  ASP A C   1 
ATOM   2729 O  O   . ASP A 1 338 ? -23.525 -20.917 -15.495 1.00 46.02  ? 338  ASP A O   1 
ATOM   2730 C  CB  . ASP A 1 338 ? -24.344 -23.877 -16.062 1.00 48.91  ? 338  ASP A CB  1 
ATOM   2731 C  CG  . ASP A 1 338 ? -25.155 -25.139 -15.786 1.00 47.65  ? 338  ASP A CG  1 
ATOM   2732 O  OD1 . ASP A 1 338 ? -25.179 -25.620 -14.635 1.00 46.80  ? 338  ASP A OD1 1 
ATOM   2733 O  OD2 . ASP A 1 338 ? -25.778 -25.660 -16.739 1.00 48.57  ? 338  ASP A OD2 1 
ATOM   2734 N  N   . THR A 1 339 ? -21.680 -22.123 -15.078 1.00 41.71  ? 339  THR A N   1 
ATOM   2735 C  CA  . THR A 1 339 ? -20.818 -20.999 -15.405 1.00 44.08  ? 339  THR A CA  1 
ATOM   2736 C  C   . THR A 1 339 ? -19.409 -21.524 -15.631 1.00 46.09  ? 339  THR A C   1 
ATOM   2737 O  O   . THR A 1 339 ? -19.078 -22.639 -15.224 1.00 49.15  ? 339  THR A O   1 
ATOM   2738 C  CB  . THR A 1 339 ? -20.853 -19.934 -14.296 1.00 44.84  ? 339  THR A CB  1 
ATOM   2739 O  OG1 . THR A 1 339 ? -20.340 -18.694 -14.799 1.00 46.68  ? 339  THR A OG1 1 
ATOM   2740 C  CG2 . THR A 1 339 ? -20.050 -20.395 -13.068 1.00 43.96  ? 339  THR A CG2 1 
ATOM   2741 N  N   . VAL A 1 340 ? -18.583 -20.708 -16.285 1.00 40.67  ? 340  VAL A N   1 
ATOM   2742 C  CA  . VAL A 1 340 ? -17.213 -21.074 -16.628 1.00 44.84  ? 340  VAL A CA  1 
ATOM   2743 C  C   . VAL A 1 340 ? -16.258 -20.172 -15.863 1.00 44.74  ? 340  VAL A C   1 
ATOM   2744 O  O   . VAL A 1 340 ? -16.377 -18.941 -15.915 1.00 44.02  ? 340  VAL A O   1 
ATOM   2745 C  CB  . VAL A 1 340 ? -16.956 -20.980 -18.146 1.00 44.04  ? 340  VAL A CB  1 
ATOM   2746 C  CG1 . VAL A 1 340 ? -15.480 -21.190 -18.446 1.00 46.17  ? 340  VAL A CG1 1 
ATOM   2747 C  CG2 . VAL A 1 340 ? -17.792 -22.009 -18.881 1.00 41.66  ? 340  VAL A CG2 1 
ATOM   2748 N  N   . LEU A 1 341 ? -15.307 -20.783 -15.164 1.00 44.34  ? 341  LEU A N   1 
ATOM   2749 C  CA  . LEU A 1 341 ? -14.334 -20.047 -14.369 1.00 44.92  ? 341  LEU A CA  1 
ATOM   2750 C  C   . LEU A 1 341 ? -13.081 -19.792 -15.199 1.00 45.19  ? 341  LEU A C   1 
ATOM   2751 O  O   . LEU A 1 341 ? -12.523 -20.725 -15.783 1.00 46.06  ? 341  LEU A O   1 
ATOM   2752 C  CB  . LEU A 1 341 ? -13.980 -20.844 -13.110 1.00 46.19  ? 341  LEU A CB  1 
ATOM   2753 C  CG  . LEU A 1 341 ? -13.665 -20.071 -11.842 1.00 49.74  ? 341  LEU A CG  1 
ATOM   2754 C  CD1 . LEU A 1 341 ? -14.838 -19.160 -11.508 1.00 43.05  ? 341  LEU A CD1 1 
ATOM   2755 C  CD2 . LEU A 1 341 ? -13.372 -21.042 -10.695 1.00 46.07  ? 341  LEU A CD2 1 
ATOM   2756 N  N   . GLY A 1 342 ? -12.640 -18.534 -15.247 1.00 45.70  ? 342  GLY A N   1 
ATOM   2757 C  CA  . GLY A 1 342 ? -11.381 -18.212 -15.898 1.00 43.34  ? 342  GLY A CA  1 
ATOM   2758 C  C   . GLY A 1 342 ? -11.310 -18.589 -17.363 1.00 50.28  ? 342  GLY A C   1 
ATOM   2759 O  O   . GLY A 1 342 ? -10.209 -18.772 -17.894 1.00 48.79  ? 342  GLY A O   1 
ATOM   2760 N  N   . GLY A 1 343 ? -12.454 -18.726 -18.029 1.00 48.68  ? 343  GLY A N   1 
ATOM   2761 C  CA  . GLY A 1 343 ? -12.469 -19.159 -19.414 1.00 48.60  ? 343  GLY A CA  1 
ATOM   2762 C  C   . GLY A 1 343 ? -11.994 -20.574 -19.654 1.00 53.66  ? 343  GLY A C   1 
ATOM   2763 O  O   . GLY A 1 343 ? -11.840 -20.967 -20.812 1.00 48.95  ? 343  GLY A O   1 
ATOM   2764 N  N   . GLU A 1 344 ? -11.762 -21.359 -18.600 1.00 46.47  ? 344  GLU A N   1 
ATOM   2765 C  CA  . GLU A 1 344 ? -11.160 -22.682 -18.745 1.00 49.59  ? 344  GLU A CA  1 
ATOM   2766 C  C   . GLU A 1 344 ? -11.821 -23.782 -17.936 1.00 50.88  ? 344  GLU A C   1 
ATOM   2767 O  O   . GLU A 1 344 ? -11.647 -24.956 -18.284 1.00 51.48  ? 344  GLU A O   1 
ATOM   2768 C  CB  . GLU A 1 344 ? -9.668  -22.636 -18.367 1.00 51.59  ? 344  GLU A CB  1 
ATOM   2769 C  CG  . GLU A 1 344 ? -8.943  -21.372 -18.819 1.00 54.19  ? 344  GLU A CG  1 
ATOM   2770 C  CD  . GLU A 1 344 ? -7.442  -21.412 -18.575 1.00 59.60  ? 344  GLU A CD  1 
ATOM   2771 O  OE1 . GLU A 1 344 ? -7.024  -21.393 -17.397 1.00 56.01  ? 344  GLU A OE1 1 
ATOM   2772 O  OE2 . GLU A 1 344 ? -6.675  -21.460 -19.560 1.00 66.98  ? 344  GLU A OE2 1 
ATOM   2773 N  N   . TYR A 1 345 ? -12.558 -23.466 -16.872 1.00 44.39  ? 345  TYR A N   1 
ATOM   2774 C  CA  . TYR A 1 345 ? -13.058 -24.486 -15.953 1.00 46.52  ? 345  TYR A CA  1 
ATOM   2775 C  C   . TYR A 1 345 ? -14.574 -24.411 -15.860 1.00 48.44  ? 345  TYR A C   1 
ATOM   2776 O  O   . TYR A 1 345 ? -15.123 -23.635 -15.061 1.00 44.27  ? 345  TYR A O   1 
ATOM   2777 C  CB  . TYR A 1 345 ? -12.407 -24.333 -14.584 1.00 42.99  ? 345  TYR A CB  1 
ATOM   2778 C  CG  . TYR A 1 345 ? -10.909 -24.422 -14.664 1.00 40.72  ? 345  TYR A CG  1 
ATOM   2779 C  CD1 . TYR A 1 345 ? -10.287 -25.642 -14.870 1.00 47.05  ? 345  TYR A CD1 1 
ATOM   2780 C  CD2 . TYR A 1 345 ? -10.115 -23.296 -14.537 1.00 43.74  ? 345  TYR A CD2 1 
ATOM   2781 C  CE1 . TYR A 1 345 ? -8.922  -25.740 -14.954 1.00 43.99  ? 345  TYR A CE1 1 
ATOM   2782 C  CE2 . TYR A 1 345 ? -8.732  -23.382 -14.614 1.00 42.50  ? 345  TYR A CE2 1 
ATOM   2783 C  CZ  . TYR A 1 345 ? -8.144  -24.616 -14.827 1.00 48.88  ? 345  TYR A CZ  1 
ATOM   2784 O  OH  . TYR A 1 345 ? -6.770  -24.737 -14.907 1.00 49.51  ? 345  TYR A OH  1 
ATOM   2785 N  N   . PRO A 1 346 ? -15.291 -25.203 -16.654 1.00 45.70  ? 346  PRO A N   1 
ATOM   2786 C  CA  . PRO A 1 346 ? -16.753 -25.175 -16.585 1.00 48.14  ? 346  PRO A CA  1 
ATOM   2787 C  C   . PRO A 1 346 ? -17.251 -25.766 -15.278 1.00 49.17  ? 346  PRO A C   1 
ATOM   2788 O  O   . PRO A 1 346 ? -16.724 -26.766 -14.782 1.00 46.44  ? 346  PRO A O   1 
ATOM   2789 C  CB  . PRO A 1 346 ? -17.180 -26.031 -17.785 1.00 48.82  ? 346  PRO A CB  1 
ATOM   2790 C  CG  . PRO A 1 346 ? -16.036 -26.959 -17.983 1.00 53.60  ? 346  PRO A CG  1 
ATOM   2791 C  CD  . PRO A 1 346 ? -14.811 -26.141 -17.683 1.00 47.70  ? 346  PRO A CD  1 
ATOM   2792 N  N   . LEU A 1 347 ? -18.282 -25.127 -14.728 1.00 44.79  ? 347  LEU A N   1 
ATOM   2793 C  CA  . LEU A 1 347 ? -18.951 -25.577 -13.520 1.00 44.09  ? 347  LEU A CA  1 
ATOM   2794 C  C   . LEU A 1 347 ? -20.446 -25.673 -13.775 1.00 42.32  ? 347  LEU A C   1 
ATOM   2795 O  O   . LEU A 1 347 ? -21.022 -24.883 -14.532 1.00 46.63  ? 347  LEU A O   1 
ATOM   2796 C  CB  . LEU A 1 347 ? -18.693 -24.619 -12.344 1.00 42.54  ? 347  LEU A CB  1 
ATOM   2797 C  CG  . LEU A 1 347 ? -17.234 -24.293 -12.026 1.00 42.95  ? 347  LEU A CG  1 
ATOM   2798 C  CD1 . LEU A 1 347 ? -17.158 -23.143 -11.020 1.00 42.74  ? 347  LEU A CD1 1 
ATOM   2799 C  CD2 . LEU A 1 347 ? -16.506 -25.526 -11.503 1.00 43.22  ? 347  LEU A CD2 1 
ATOM   2800 N  N   . GLU A 1 348 ? -21.069 -26.641 -13.117 1.00 40.72  ? 348  GLU A N   1 
ATOM   2801 C  CA  . GLU A 1 348 ? -22.510 -26.813 -13.116 1.00 43.35  ? 348  GLU A CA  1 
ATOM   2802 C  C   . GLU A 1 348 ? -23.105 -26.168 -11.870 1.00 44.73  ? 348  GLU A C   1 
ATOM   2803 O  O   . GLU A 1 348 ? -22.467 -26.107 -10.813 1.00 41.98  ? 348  GLU A O   1 
ATOM   2804 C  CB  . GLU A 1 348 ? -22.870 -28.297 -13.143 1.00 47.75  ? 348  GLU A CB  1 
ATOM   2805 C  CG  . GLU A 1 348 ? -22.425 -28.996 -14.419 1.00 50.98  ? 348  GLU A CG  1 
ATOM   2806 C  CD  . GLU A 1 348 ? -22.782 -30.469 -14.425 1.00 63.02  ? 348  GLU A CD  1 
ATOM   2807 O  OE1 . GLU A 1 348 ? -22.402 -31.161 -15.389 1.00 71.44  ? 348  GLU A OE1 1 
ATOM   2808 O  OE2 . GLU A 1 348 ? -23.458 -30.930 -13.481 1.00 70.45  ? 348  GLU A OE2 1 
ATOM   2809 N  N   . LYS A 1 349 ? -24.342 -25.697 -12.000 1.00 43.22  ? 349  LYS A N   1 
ATOM   2810 C  CA  . LYS A 1 349 ? -25.088 -25.186 -10.857 1.00 43.04  ? 349  LYS A CA  1 
ATOM   2811 C  C   . LYS A 1 349 ? -24.925 -26.117 -9.664  1.00 47.80  ? 349  LYS A C   1 
ATOM   2812 O  O   . LYS A 1 349 ? -25.077 -27.336 -9.782  1.00 47.28  ? 349  LYS A O   1 
ATOM   2813 C  CB  . LYS A 1 349 ? -26.566 -25.048 -11.228 1.00 45.47  ? 349  LYS A CB  1 
ATOM   2814 C  CG  . LYS A 1 349 ? -27.538 -24.973 -10.067 1.00 49.26  ? 349  LYS A CG  1 
ATOM   2815 C  CD  . LYS A 1 349 ? -28.915 -24.604 -10.598 1.00 48.73  ? 349  LYS A CD  1 
ATOM   2816 C  CE  . LYS A 1 349 ? -29.896 -24.265 -9.495  1.00 55.53  ? 349  LYS A CE  1 
ATOM   2817 N  NZ  . LYS A 1 349 ? -30.456 -22.896 -9.718  1.00 62.25  ? 349  LYS A NZ  1 
ATOM   2818 N  N   . GLY A 1 350 ? -24.578 -25.547 -8.517  1.00 40.33  ? 350  GLY A N   1 
ATOM   2819 C  CA  . GLY A 1 350 ? -24.384 -26.338 -7.326  1.00 40.79  ? 350  GLY A CA  1 
ATOM   2820 C  C   . GLY A 1 350 ? -22.954 -26.744 -7.052  1.00 41.56  ? 350  GLY A C   1 
ATOM   2821 O  O   . GLY A 1 350 ? -22.635 -27.087 -5.903  1.00 40.05  ? 350  GLY A O   1 
ATOM   2822 N  N   . ASP A 1 351 ? -22.084 -26.706 -8.067  1.00 40.45  ? 351  ASP A N   1 
ATOM   2823 C  CA  . ASP A 1 351 ? -20.676 -27.033 -7.869  1.00 38.42  ? 351  ASP A CA  1 
ATOM   2824 C  C   . ASP A 1 351 ? -20.050 -26.116 -6.823  1.00 38.17  ? 351  ASP A C   1 
ATOM   2825 O  O   . ASP A 1 351 ? -20.333 -24.916 -6.779  1.00 37.78  ? 351  ASP A O   1 
ATOM   2826 C  CB  . ASP A 1 351 ? -19.898 -26.900 -9.179  1.00 37.27  ? 351  ASP A CB  1 
ATOM   2827 C  CG  . ASP A 1 351 ? -20.070 -28.107 -10.098 1.00 42.47  ? 351  ASP A CG  1 
ATOM   2828 O  OD1 . ASP A 1 351 ? -20.788 -29.055 -9.713  1.00 41.28  ? 351  ASP A OD1 1 
ATOM   2829 O  OD2 . ASP A 1 351 ? -19.478 -28.090 -11.203 1.00 41.39  ? 351  ASP A OD2 1 
ATOM   2830 N  N   . GLU A 1 352 ? -19.143 -26.687 -6.027  1.00 38.43  ? 352  GLU A N   1 
ATOM   2831 C  CA  . GLU A 1 352 ? -18.558 -26.070 -4.845  1.00 40.54  ? 352  GLU A CA  1 
ATOM   2832 C  C   . GLU A 1 352 ? -17.128 -25.614 -5.107  1.00 41.34  ? 352  GLU A C   1 
ATOM   2833 O  O   . GLU A 1 352 ? -16.380 -26.247 -5.862  1.00 39.40  ? 352  GLU A O   1 
ATOM   2834 C  CB  . GLU A 1 352 ? -18.559 -27.094 -3.712  1.00 38.60  ? 352  GLU A CB  1 
ATOM   2835 C  CG  . GLU A 1 352 ? -19.850 -27.135 -2.985  1.00 46.19  ? 352  GLU A CG  1 
ATOM   2836 C  CD  . GLU A 1 352 ? -19.833 -28.138 -1.845  1.00 50.69  ? 352  GLU A CD  1 
ATOM   2837 O  OE1 . GLU A 1 352 ? -20.872 -28.814 -1.703  1.00 55.55  ? 352  GLU A OE1 1 
ATOM   2838 O  OE2 . GLU A 1 352 ? -18.801 -28.299 -1.157  1.00 49.17  ? 352  GLU A OE2 1 
ATOM   2839 N  N   . LEU A 1 353 ? -16.741 -24.531 -4.433  1.00 36.47  ? 353  LEU A N   1 
ATOM   2840 C  CA  . LEU A 1 353 ? -15.382 -24.020 -4.431  1.00 36.24  ? 353  LEU A CA  1 
ATOM   2841 C  C   . LEU A 1 353 ? -14.944 -23.781 -2.993  1.00 36.75  ? 353  LEU A C   1 
ATOM   2842 O  O   . LEU A 1 353 ? -15.759 -23.435 -2.137  1.00 36.37  ? 353  LEU A O   1 
ATOM   2843 C  CB  . LEU A 1 353 ? -15.280 -22.693 -5.204  1.00 33.41  ? 353  LEU A CB  1 
ATOM   2844 C  CG  . LEU A 1 353 ? -15.805 -22.680 -6.633  1.00 40.34  ? 353  LEU A CG  1 
ATOM   2845 C  CD1 . LEU A 1 353 ? -15.960 -21.231 -7.113  1.00 35.58  ? 353  LEU A CD1 1 
ATOM   2846 C  CD2 . LEU A 1 353 ? -14.839 -23.455 -7.515  1.00 38.58  ? 353  LEU A CD2 1 
ATOM   2847 N  N   . MET A 1 354 ? -13.651 -23.959 -2.738  1.00 35.65  ? 354  MET A N   1 
ATOM   2848 C  CA  . MET A 1 354 ? -12.990 -23.452 -1.537  1.00 39.20  ? 354  MET A CA  1 
ATOM   2849 C  C   . MET A 1 354 ? -12.003 -22.358 -1.902  1.00 35.48  ? 354  MET A C   1 
ATOM   2850 O  O   . MET A 1 354 ? -11.155 -22.547 -2.777  1.00 37.95  ? 354  MET A O   1 
ATOM   2851 C  CB  . MET A 1 354 ? -12.262 -24.557 -0.755  1.00 34.15  ? 354  MET A CB  1 
ATOM   2852 C  CG  . MET A 1 354 ? -13.106 -25.761 -0.338  1.00 34.80  ? 354  MET A CG  1 
ATOM   2853 S  SD  . MET A 1 354 ? -14.315 -25.267 0.956   1.00 36.92  ? 354  MET A SD  1 
ATOM   2854 C  CE  . MET A 1 354 ? -13.240 -24.615 2.208   1.00 37.73  ? 354  MET A CE  1 
ATOM   2855 N  N   . VAL A 1 355 ? -12.098 -21.225 -1.219  1.00 35.34  ? 355  VAL A N   1 
ATOM   2856 C  CA  . VAL A 1 355 ? -11.133 -20.142 -1.375  1.00 30.84  ? 355  VAL A CA  1 
ATOM   2857 C  C   . VAL A 1 355 ? -10.055 -20.301 -0.311  1.00 34.08  ? 355  VAL A C   1 
ATOM   2858 O  O   . VAL A 1 355 ? -10.328 -20.201 0.891   1.00 33.15  ? 355  VAL A O   1 
ATOM   2859 C  CB  . VAL A 1 355 ? -11.814 -18.769 -1.266  1.00 32.87  ? 355  VAL A CB  1 
ATOM   2860 C  CG1 . VAL A 1 355 ? -10.780 -17.658 -1.393  1.00 33.60  ? 355  VAL A CG1 1 
ATOM   2861 C  CG2 . VAL A 1 355 ? -12.897 -18.619 -2.325  1.00 31.36  ? 355  VAL A CG2 1 
ATOM   2862 N  N   . LEU A 1 356 ? -8.821  -20.552 -0.746  1.00 30.39  ? 356  LEU A N   1 
ATOM   2863 C  CA  . LEU A 1 356 ? -7.727  -20.825 0.187   1.00 34.42  ? 356  LEU A CA  1 
ATOM   2864 C  C   . LEU A 1 356 ? -7.010  -19.514 0.456   1.00 32.75  ? 356  LEU A C   1 
ATOM   2865 O  O   . LEU A 1 356 ? -6.056  -19.156 -0.230  1.00 34.32  ? 356  LEU A O   1 
ATOM   2866 C  CB  . LEU A 1 356 ? -6.784  -21.871 -0.394  1.00 34.15  ? 356  LEU A CB  1 
ATOM   2867 C  CG  . LEU A 1 356 ? -5.704  -22.433 0.532   1.00 38.01  ? 356  LEU A CG  1 
ATOM   2868 C  CD1 . LEU A 1 356 ? -6.358  -23.137 1.708   1.00 36.33  ? 356  LEU A CD1 1 
ATOM   2869 C  CD2 . LEU A 1 356 ? -4.792  -23.413 -0.216  1.00 38.00  ? 356  LEU A CD2 1 
ATOM   2870 N  N   . ILE A 1 357 ? -7.452  -18.794 1.493   1.00 31.75  ? 357  ILE A N   1 
ATOM   2871 C  CA  . ILE A 1 357 ? -7.080  -17.381 1.616   1.00 33.21  ? 357  ILE A CA  1 
ATOM   2872 C  C   . ILE A 1 357 ? -5.579  -17.178 1.785   1.00 32.58  ? 357  ILE A C   1 
ATOM   2873 O  O   . ILE A 1 357 ? -5.028  -16.260 1.150   1.00 33.34  ? 357  ILE A O   1 
ATOM   2874 C  CB  . ILE A 1 357 ? -7.879  -16.715 2.750   1.00 33.11  ? 357  ILE A CB  1 
ATOM   2875 C  CG1 . ILE A 1 357 ? -9.382  -16.959 2.606   1.00 31.24  ? 357  ILE A CG1 1 
ATOM   2876 C  CG2 . ILE A 1 357 ? -7.639  -15.221 2.694   1.00 33.33  ? 357  ILE A CG2 1 
ATOM   2877 C  CD1 . ILE A 1 357 ? -10.175 -16.441 3.858   1.00 29.81  ? 357  ILE A CD1 1 
ATOM   2878 N  N   . PRO A 1 358 ? -4.870  -17.936 2.621   1.00 33.95  ? 358  PRO A N   1 
ATOM   2879 C  CA  . PRO A 1 358 ? -3.431  -17.670 2.767   1.00 32.04  ? 358  PRO A CA  1 
ATOM   2880 C  C   . PRO A 1 358 ? -2.674  -17.846 1.466   1.00 34.09  ? 358  PRO A C   1 
ATOM   2881 O  O   . PRO A 1 358 ? -1.662  -17.168 1.247   1.00 35.38  ? 358  PRO A O   1 
ATOM   2882 C  CB  . PRO A 1 358 ? -2.982  -18.687 3.827   1.00 35.06  ? 358  PRO A CB  1 
ATOM   2883 C  CG  . PRO A 1 358 ? -4.282  -19.065 4.565   1.00 34.63  ? 358  PRO A CG  1 
ATOM   2884 C  CD  . PRO A 1 358 ? -5.314  -19.053 3.477   1.00 33.95  ? 358  PRO A CD  1 
ATOM   2885 N  N   . GLN A 1 359 ? -3.153  -18.722 0.587   1.00 34.25  ? 359  GLN A N   1 
ATOM   2886 C  CA  . GLN A 1 359 ? -2.495  -18.909 -0.702  1.00 35.15  ? 359  GLN A CA  1 
ATOM   2887 C  C   . GLN A 1 359 ? -2.852  -17.780 -1.676  1.00 36.95  ? 359  GLN A C   1 
ATOM   2888 O  O   . GLN A 1 359 ? -1.976  -17.256 -2.372  1.00 36.09  ? 359  GLN A O   1 
ATOM   2889 C  CB  . GLN A 1 359 ? -2.861  -20.283 -1.262  1.00 38.88  ? 359  GLN A CB  1 
ATOM   2890 C  CG  . GLN A 1 359 ? -1.865  -20.840 -2.268  1.00 40.65  ? 359  GLN A CG  1 
ATOM   2891 C  CD  . GLN A 1 359 ? -0.519  -21.175 -1.648  1.00 43.36  ? 359  GLN A CD  1 
ATOM   2892 O  OE1 . GLN A 1 359 ? -0.349  -21.194 -0.414  1.00 38.74  ? 359  GLN A OE1 1 
ATOM   2893 N  NE2 . GLN A 1 359 ? 0.461   -21.430 -2.511  1.00 45.91  ? 359  GLN A NE2 1 
ATOM   2894 N  N   . LEU A 1 360 ? -4.123  -17.369 -1.725  1.00 34.59  ? 360  LEU A N   1 
ATOM   2895 C  CA  . LEU A 1 360 ? -4.479  -16.156 -2.465  1.00 33.45  ? 360  LEU A CA  1 
ATOM   2896 C  C   . LEU A 1 360 ? -3.563  -14.995 -2.094  1.00 32.91  ? 360  LEU A C   1 
ATOM   2897 O  O   . LEU A 1 360 ? -3.068  -14.264 -2.964  1.00 37.58  ? 360  LEU A O   1 
ATOM   2898 C  CB  . LEU A 1 360 ? -5.938  -15.762 -2.194  1.00 33.32  ? 360  LEU A CB  1 
ATOM   2899 C  CG  . LEU A 1 360 ? -6.298  -14.313 -2.600  1.00 32.70  ? 360  LEU A CG  1 
ATOM   2900 C  CD1 . LEU A 1 360 ? -6.408  -14.184 -4.123  1.00 33.18  ? 360  LEU A CD1 1 
ATOM   2901 C  CD2 . LEU A 1 360 ? -7.624  -13.909 -1.946  1.00 32.95  ? 360  LEU A CD2 1 
ATOM   2902 N  N   . HIS A 1 361 ? -3.331  -14.803 -0.801  1.00 31.31  ? 361  HIS A N   1 
ATOM   2903 C  CA  . HIS A 1 361 ? -2.552  -13.674 -0.336  1.00 31.45  ? 361  HIS A CA  1 
ATOM   2904 C  C   . HIS A 1 361 ? -1.062  -13.815 -0.632  1.00 32.77  ? 361  HIS A C   1 
ATOM   2905 O  O   . HIS A 1 361 ? -0.298  -12.925 -0.257  1.00 34.16  ? 361  HIS A O   1 
ATOM   2906 C  CB  . HIS A 1 361 ? -2.766  -13.487 1.165   1.00 33.59  ? 361  HIS A CB  1 
ATOM   2907 C  CG  . HIS A 1 361 ? -4.149  -13.030 1.519   1.00 30.47  ? 361  HIS A CG  1 
ATOM   2908 N  ND1 . HIS A 1 361 ? -4.606  -12.972 2.815   1.00 35.65  ? 361  HIS A ND1 1 
ATOM   2909 C  CD2 . HIS A 1 361 ? -5.171  -12.602 0.736   1.00 32.22  ? 361  HIS A CD2 1 
ATOM   2910 C  CE1 . HIS A 1 361 ? -5.851  -12.518 2.823   1.00 33.54  ? 361  HIS A CE1 1 
ATOM   2911 N  NE2 . HIS A 1 361 ? -6.221  -12.297 1.573   1.00 31.44  ? 361  HIS A NE2 1 
ATOM   2912 N  N   . ARG A 1 362 ? -0.645  -14.928 -1.226  1.00 35.77  ? 362  ARG A N   1 
ATOM   2913 C  CA  . ARG A 1 362 ? 0.741   -15.134 -1.638  1.00 35.92  ? 362  ARG A CA  1 
ATOM   2914 C  C   . ARG A 1 362 ? 0.883   -15.126 -3.156  1.00 39.82  ? 362  ARG A C   1 
ATOM   2915 O  O   . ARG A 1 362 ? 1.928   -15.529 -3.682  1.00 39.65  ? 362  ARG A O   1 
ATOM   2916 C  CB  . ARG A 1 362 ? 1.277   -16.442 -1.048  1.00 35.36  ? 362  ARG A CB  1 
ATOM   2917 C  CG  . ARG A 1 362 ? 1.675   -16.335 0.432   1.00 37.31  ? 362  ARG A CG  1 
ATOM   2918 C  CD  . ARG A 1 362 ? 1.825   -17.713 1.131   1.00 35.51  ? 362  ARG A CD  1 
ATOM   2919 N  NE  . ARG A 1 362 ? 2.312   -17.553 2.502   1.00 39.06  ? 362  ARG A NE  1 
ATOM   2920 C  CZ  . ARG A 1 362 ? 1.553   -17.139 3.509   1.00 40.65  ? 362  ARG A CZ  1 
ATOM   2921 N  NH1 . ARG A 1 362 ? 0.264   -16.898 3.340   1.00 32.32  ? 362  ARG A NH1 1 
ATOM   2922 N  NH2 . ARG A 1 362 ? 2.100   -16.956 4.707   1.00 38.21  ? 362  ARG A NH2 1 
ATOM   2923 N  N   . ASP A 1 363 ? -0.134  -14.654 -3.868  1.00 35.95  ? 363  ASP A N   1 
ATOM   2924 C  CA  . ASP A 1 363 ? -0.126  -14.598 -5.332  1.00 37.38  ? 363  ASP A CA  1 
ATOM   2925 C  C   . ASP A 1 363 ? 0.942   -13.618 -5.800  1.00 37.32  ? 363  ASP A C   1 
ATOM   2926 O  O   . ASP A 1 363 ? 0.783   -12.395 -5.682  1.00 36.72  ? 363  ASP A O   1 
ATOM   2927 C  CB  . ASP A 1 363 ? -1.514  -14.188 -5.825  1.00 38.02  ? 363  ASP A CB  1 
ATOM   2928 C  CG  . ASP A 1 363 ? -1.684  -14.306 -7.334  1.00 40.02  ? 363  ASP A CG  1 
ATOM   2929 O  OD1 . ASP A 1 363 ? -0.673  -14.218 -8.075  1.00 39.40  ? 363  ASP A OD1 1 
ATOM   2930 O  OD2 . ASP A 1 363 ? -2.842  -14.470 -7.784  1.00 38.33  ? 363  ASP A OD2 1 
ATOM   2931 N  N   . LYS A 1 364 ? 2.037   -14.139 -6.353  1.00 38.89  ? 364  LYS A N   1 
ATOM   2932 C  CA  . LYS A 1 364 ? 3.121   -13.235 -6.725  1.00 41.48  ? 364  LYS A CA  1 
ATOM   2933 C  C   . LYS A 1 364 ? 2.726   -12.266 -7.831  1.00 39.96  ? 364  LYS A C   1 
ATOM   2934 O  O   . LYS A 1 364 ? 3.330   -11.192 -7.939  1.00 38.39  ? 364  LYS A O   1 
ATOM   2935 C  CB  . LYS A 1 364 ? 4.358   -14.027 -7.143  1.00 42.46  ? 364  LYS A CB  1 
ATOM   2936 C  CG  . LYS A 1 364 ? 5.125   -14.585 -5.952  1.00 47.42  ? 364  LYS A CG  1 
ATOM   2937 C  CD  . LYS A 1 364 ? 6.337   -15.388 -6.396  1.00 51.46  ? 364  LYS A CD  1 
ATOM   2938 C  CE  . LYS A 1 364 ? 6.972   -16.094 -5.206  1.00 57.03  ? 364  LYS A CE  1 
ATOM   2939 N  NZ  . LYS A 1 364 ? 7.971   -17.109 -5.642  1.00 59.19  ? 364  LYS A NZ  1 
ATOM   2940 N  N   . THR A 1 365 ? 1.744   -12.612 -8.661  1.00 38.71  ? 365  THR A N   1 
ATOM   2941 C  CA  . THR A 1 365 ? 1.367   -11.675 -9.712  1.00 40.62  ? 365  THR A CA  1 
ATOM   2942 C  C   . THR A 1 365 ? 0.708   -10.429 -9.142  1.00 45.13  ? 365  THR A C   1 
ATOM   2943 O  O   . THR A 1 365 ? 0.652   -9.401  -9.826  1.00 40.09  ? 365  THR A O   1 
ATOM   2944 C  CB  . THR A 1 365 ? 0.450   -12.343 -10.739 1.00 42.80  ? 365  THR A CB  1 
ATOM   2945 O  OG1 . THR A 1 365 ? -0.866  -12.506 -10.192 1.00 41.99  ? 365  THR A OG1 1 
ATOM   2946 C  CG2 . THR A 1 365 ? 1.003   -13.694 -11.150 1.00 43.74  ? 365  THR A CG2 1 
ATOM   2947 N  N   . ILE A 1 366 ? 0.228   -10.495 -7.900  1.00 38.47  ? 366  ILE A N   1 
ATOM   2948 C  CA  . ILE A 1 366 ? -0.401  -9.353  -7.247  1.00 35.52  ? 366  ILE A CA  1 
ATOM   2949 C  C   . ILE A 1 366 ? 0.593   -8.579  -6.398  1.00 37.71  ? 366  ILE A C   1 
ATOM   2950 O  O   . ILE A 1 366 ? 0.749   -7.367  -6.552  1.00 41.20  ? 366  ILE A O   1 
ATOM   2951 C  CB  . ILE A 1 366 ? -1.588  -9.838  -6.384  1.00 35.73  ? 366  ILE A CB  1 
ATOM   2952 C  CG1 . ILE A 1 366 ? -2.677  -10.455 -7.263  1.00 36.07  ? 366  ILE A CG1 1 
ATOM   2953 C  CG2 . ILE A 1 366 ? -2.096  -8.701  -5.522  1.00 37.16  ? 366  ILE A CG2 1 
ATOM   2954 C  CD1 . ILE A 1 366 ? -3.265  -9.515  -8.280  1.00 39.44  ? 366  ILE A CD1 1 
ATOM   2955 N  N   . TRP A 1 367 ? 1.285   -9.273  -5.491  1.00 36.57  ? 367  TRP A N   1 
ATOM   2956 C  CA  . TRP A 1 367 ? 2.069   -8.610  -4.462  1.00 39.67  ? 367  TRP A CA  1 
ATOM   2957 C  C   . TRP A 1 367 ? 3.532   -8.439  -4.838  1.00 41.93  ? 367  TRP A C   1 
ATOM   2958 O  O   . TRP A 1 367 ? 4.222   -7.615  -4.224  1.00 48.90  ? 367  TRP A O   1 
ATOM   2959 C  CB  . TRP A 1 367 ? 1.939   -9.381  -3.143  1.00 41.21  ? 367  TRP A CB  1 
ATOM   2960 C  CG  . TRP A 1 367 ? 0.495   -9.574  -2.763  1.00 36.92  ? 367  TRP A CG  1 
ATOM   2961 C  CD1 . TRP A 1 367 ? -0.268  -10.686 -2.959  1.00 36.25  ? 367  TRP A CD1 1 
ATOM   2962 C  CD2 . TRP A 1 367 ? -0.358  -8.604  -2.141  1.00 36.93  ? 367  TRP A CD2 1 
ATOM   2963 N  NE1 . TRP A 1 367 ? -1.551  -10.462 -2.508  1.00 37.78  ? 367  TRP A NE1 1 
ATOM   2964 C  CE2 . TRP A 1 367 ? -1.626  -9.193  -1.999  1.00 36.31  ? 367  TRP A CE2 1 
ATOM   2965 C  CE3 . TRP A 1 367 ? -0.171  -7.289  -1.709  1.00 35.97  ? 367  TRP A CE3 1 
ATOM   2966 C  CZ2 . TRP A 1 367 ? -2.706  -8.514  -1.415  1.00 34.30  ? 367  TRP A CZ2 1 
ATOM   2967 C  CZ3 . TRP A 1 367 ? -1.236  -6.616  -1.137  1.00 38.18  ? 367  TRP A CZ3 1 
ATOM   2968 C  CH2 . TRP A 1 367 ? -2.485  -7.232  -0.992  1.00 33.14  ? 367  TRP A CH2 1 
ATOM   2969 N  N   . GLY A 1 368 ? 4.012   -9.166  -5.834  1.00 42.85  ? 368  GLY A N   1 
ATOM   2970 C  CA  . GLY A 1 368 ? 5.397   -9.059  -6.244  1.00 44.85  ? 368  GLY A CA  1 
ATOM   2971 C  C   . GLY A 1 368 ? 6.232   -10.188 -5.681  1.00 53.99  ? 368  GLY A C   1 
ATOM   2972 O  O   . GLY A 1 368 ? 5.750   -11.090 -4.986  1.00 48.36  ? 368  GLY A O   1 
ATOM   2973 N  N   . ASP A 1 369 ? 7.529   -10.124 -5.988  1.00 50.28  ? 369  ASP A N   1 
ATOM   2974 C  CA  . ASP A 1 369 ? 8.421   -11.200 -5.572  1.00 57.77  ? 369  ASP A CA  1 
ATOM   2975 C  C   . ASP A 1 369 ? 8.543   -11.269 -4.051  1.00 51.98  ? 369  ASP A C   1 
ATOM   2976 O  O   . ASP A 1 369 ? 8.603   -12.364 -3.482  1.00 58.26  ? 369  ASP A O   1 
ATOM   2977 C  CB  . ASP A 1 369 ? 9.788   -11.014 -6.231  1.00 57.30  ? 369  ASP A CB  1 
ATOM   2978 C  CG  . ASP A 1 369 ? 9.785   -11.419 -7.706  1.00 66.65  ? 369  ASP A CG  1 
ATOM   2979 O  OD1 . ASP A 1 369 ? 8.848   -12.136 -8.137  1.00 60.18  ? 369  ASP A OD1 1 
ATOM   2980 O  OD2 . ASP A 1 369 ? 10.708  -10.999 -8.439  1.00 69.48  ? 369  ASP A OD2 1 
ATOM   2981 N  N   . ASP A 1 370 ? 8.564   -10.117 -3.380  1.00 50.86  ? 370  ASP A N   1 
ATOM   2982 C  CA  . ASP A 1 370 ? 8.769   -10.031 -1.936  1.00 50.77  ? 370  ASP A CA  1 
ATOM   2983 C  C   . ASP A 1 370 ? 7.544   -10.469 -1.127  1.00 50.48  ? 370  ASP A C   1 
ATOM   2984 O  O   . ASP A 1 370 ? 7.320   -9.960  -0.021  1.00 48.18  ? 370  ASP A O   1 
ATOM   2985 C  CB  . ASP A 1 370 ? 9.158   -8.593  -1.553  1.00 48.42  ? 370  ASP A CB  1 
ATOM   2986 C  CG  . ASP A 1 370 ? 7.983   -7.618  -1.633  1.00 53.97  ? 370  ASP A CG  1 
ATOM   2987 O  OD1 . ASP A 1 370 ? 6.953   -7.981  -2.235  1.00 54.24  ? 370  ASP A OD1 1 
ATOM   2988 O  OD2 . ASP A 1 370 ? 8.089   -6.485  -1.108  1.00 54.00  ? 370  ASP A OD2 1 
ATOM   2989 N  N   . VAL A 1 371 ? 6.782   -11.441 -1.636  1.00 47.98  ? 371  VAL A N   1 
ATOM   2990 C  CA  . VAL A 1 371 ? 5.461   -11.735 -1.070  1.00 49.54  ? 371  VAL A CA  1 
ATOM   2991 C  C   . VAL A 1 371 ? 5.542   -12.239 0.373   1.00 49.46  ? 371  VAL A C   1 
ATOM   2992 O  O   . VAL A 1 371 ? 4.606   -12.024 1.166   1.00 44.67  ? 371  VAL A O   1 
ATOM   2993 C  CB  . VAL A 1 371 ? 4.713   -12.735 -1.970  1.00 47.17  ? 371  VAL A CB  1 
ATOM   2994 C  CG1 . VAL A 1 371 ? 5.327   -14.128 -1.860  1.00 49.41  ? 371  VAL A CG1 1 
ATOM   2995 C  CG2 . VAL A 1 371 ? 3.247   -12.767 -1.591  1.00 44.53  ? 371  VAL A CG2 1 
ATOM   2996 N  N   . GLU A 1 372 ? 6.628   -12.922 0.742   1.00 46.78  ? 372  GLU A N   1 
ATOM   2997 C  CA  . GLU A 1 372 ? 6.750   -13.446 2.095   1.00 47.67  ? 372  GLU A CA  1 
ATOM   2998 C  C   . GLU A 1 372 ? 7.238   -12.405 3.088   1.00 47.66  ? 372  GLU A C   1 
ATOM   2999 O  O   . GLU A 1 372 ? 7.254   -12.682 4.292   1.00 47.77  ? 372  GLU A O   1 
ATOM   3000 C  CB  . GLU A 1 372 ? 7.687   -14.656 2.114   1.00 48.66  ? 372  GLU A CB  1 
ATOM   3001 C  CG  . GLU A 1 372 ? 7.093   -15.902 1.479   1.00 46.50  ? 372  GLU A CG  1 
ATOM   3002 C  CD  . GLU A 1 372 ? 6.051   -16.583 2.362   1.00 51.64  ? 372  GLU A CD  1 
ATOM   3003 O  OE1 . GLU A 1 372 ? 6.135   -16.470 3.608   1.00 55.40  ? 372  GLU A OE1 1 
ATOM   3004 O  OE2 . GLU A 1 372 ? 5.150   -17.244 1.808   1.00 52.05  ? 372  GLU A OE2 1 
ATOM   3005 N  N   A GLU A 1 373 ? 7.627   -11.225 2.618   0.56 43.85  ? 373  GLU A N   1 
ATOM   3006 N  N   B GLU A 1 373 ? 7.624   -11.223 2.622   0.44 43.89  ? 373  GLU A N   1 
ATOM   3007 C  CA  A GLU A 1 373 ? 8.091   -10.157 3.486   0.56 45.35  ? 373  GLU A CA  1 
ATOM   3008 C  CA  B GLU A 1 373 ? 8.106   -10.171 3.502   0.44 45.35  ? 373  GLU A CA  1 
ATOM   3009 C  C   A GLU A 1 373 ? 6.916   -9.503  4.201   0.56 44.78  ? 373  GLU A C   1 
ATOM   3010 C  C   B GLU A 1 373 ? 6.943   -9.454  4.177   0.44 44.77  ? 373  GLU A C   1 
ATOM   3011 O  O   A GLU A 1 373 ? 5.808   -9.408  3.663   0.56 42.02  ? 373  GLU A O   1 
ATOM   3012 O  O   B GLU A 1 373 ? 5.868   -9.275  3.595   0.44 42.03  ? 373  GLU A O   1 
ATOM   3013 C  CB  A GLU A 1 373 ? 8.848   -9.102  2.678   0.56 46.15  ? 373  GLU A CB  1 
ATOM   3014 C  CB  B GLU A 1 373 ? 8.951   -9.167  2.718   0.44 46.20  ? 373  GLU A CB  1 
ATOM   3015 C  CG  A GLU A 1 373 ? 10.326  -9.392  2.495   0.56 48.50  ? 373  GLU A CG  1 
ATOM   3016 C  CG  B GLU A 1 373 ? 10.267  -9.735  2.203   0.44 47.96  ? 373  GLU A CG  1 
ATOM   3017 C  CD  A GLU A 1 373 ? 11.035  -8.296  1.724   0.56 48.64  ? 373  GLU A CD  1 
ATOM   3018 C  CD  B GLU A 1 373 ? 11.090  -10.374 3.301   0.44 47.78  ? 373  GLU A CD  1 
ATOM   3019 O  OE1 A GLU A 1 373 ? 10.974  -7.122  2.148   0.56 52.56  ? 373  GLU A OE1 1 
ATOM   3020 O  OE1 B GLU A 1 373 ? 11.501  -9.644  4.231   0.44 48.80  ? 373  GLU A OE1 1 
ATOM   3021 O  OE2 A GLU A 1 373 ? 11.641  -8.611  0.683   0.56 51.38  ? 373  GLU A OE2 1 
ATOM   3022 O  OE2 B GLU A 1 373 ? 11.344  -11.595 3.229   0.44 47.96  ? 373  GLU A OE2 1 
ATOM   3023 N  N   . PHE A 1 374 ? 7.175   -9.034  5.418   1.00 42.07  ? 374  PHE A N   1 
ATOM   3024 C  CA  . PHE A 1 374 ? 6.187   -8.290  6.191   1.00 40.80  ? 374  PHE A CA  1 
ATOM   3025 C  C   . PHE A 1 374 ? 6.394   -6.805  5.926   1.00 41.97  ? 374  PHE A C   1 
ATOM   3026 O  O   . PHE A 1 374 ? 7.267   -6.165  6.523   1.00 40.64  ? 374  PHE A O   1 
ATOM   3027 C  CB  . PHE A 1 374 ? 6.301   -8.607  7.681   1.00 39.07  ? 374  PHE A CB  1 
ATOM   3028 C  CG  . PHE A 1 374 ? 5.156   -8.075  8.492   1.00 36.24  ? 374  PHE A CG  1 
ATOM   3029 C  CD1 . PHE A 1 374 ? 3.943   -8.745  8.511   1.00 39.20  ? 374  PHE A CD1 1 
ATOM   3030 C  CD2 . PHE A 1 374 ? 5.273   -6.893  9.196   1.00 37.89  ? 374  PHE A CD2 1 
ATOM   3031 C  CE1 . PHE A 1 374 ? 2.875   -8.253  9.248   1.00 32.07  ? 374  PHE A CE1 1 
ATOM   3032 C  CE2 . PHE A 1 374 ? 4.209   -6.399  9.935   1.00 43.07  ? 374  PHE A CE2 1 
ATOM   3033 C  CZ  . PHE A 1 374 ? 2.998   -7.084  9.946   1.00 36.31  ? 374  PHE A CZ  1 
ATOM   3034 N  N   . ARG A 1 375 ? 5.579   -6.238  5.040   1.00 39.61  ? 375  ARG A N   1 
ATOM   3035 C  CA  . ARG A 1 375 ? 5.720   -4.839  4.642   1.00 36.31  ? 375  ARG A CA  1 
ATOM   3036 C  C   . ARG A 1 375 ? 4.355   -4.172  4.679   1.00 39.95  ? 375  ARG A C   1 
ATOM   3037 O  O   . ARG A 1 375 ? 3.610   -4.209  3.691   1.00 39.52  ? 375  ARG A O   1 
ATOM   3038 C  CB  . ARG A 1 375 ? 6.346   -4.730  3.250   1.00 44.95  ? 375  ARG A CB  1 
ATOM   3039 C  CG  . ARG A 1 375 ? 6.651   -3.310  2.844   1.00 46.29  ? 375  ARG A CG  1 
ATOM   3040 C  CD  . ARG A 1 375 ? 7.668   -3.263  1.703   1.00 54.48  ? 375  ARG A CD  1 
ATOM   3041 N  NE  . ARG A 1 375 ? 7.121   -3.869  0.497   1.00 52.89  ? 375  ARG A NE  1 
ATOM   3042 C  CZ  . ARG A 1 375 ? 6.296   -3.249  -0.336  1.00 55.84  ? 375  ARG A CZ  1 
ATOM   3043 N  NH1 . ARG A 1 375 ? 5.874   -2.015  -0.099  1.00 53.30  ? 375  ARG A NH1 1 
ATOM   3044 N  NH2 . ARG A 1 375 ? 5.863   -3.891  -1.420  1.00 56.36  ? 375  ARG A NH2 1 
ATOM   3045 N  N   . PRO A 1 376 ? 3.988   -3.560  5.808   1.00 39.15  ? 376  PRO A N   1 
ATOM   3046 C  CA  . PRO A 1 376 ? 2.653   -2.943  5.909   1.00 37.97  ? 376  PRO A CA  1 
ATOM   3047 C  C   . PRO A 1 376 ? 2.406   -1.879  4.869   1.00 42.19  ? 376  PRO A C   1 
ATOM   3048 O  O   . PRO A 1 376 ? 1.242   -1.590  4.564   1.00 37.66  ? 376  PRO A O   1 
ATOM   3049 C  CB  . PRO A 1 376 ? 2.657   -2.330  7.314   1.00 39.45  ? 376  PRO A CB  1 
ATOM   3050 C  CG  . PRO A 1 376 ? 3.665   -3.137  8.086   1.00 38.17  ? 376  PRO A CG  1 
ATOM   3051 C  CD  . PRO A 1 376 ? 4.740   -3.473  7.070   1.00 39.26  ? 376  PRO A CD  1 
ATOM   3052 N  N   . GLU A 1 377 ? 3.471   -1.266  4.340   1.00 38.71  ? 377  GLU A N   1 
ATOM   3053 C  CA  . GLU A 1 377 ? 3.337   -0.226  3.328   1.00 42.43  ? 377  GLU A CA  1 
ATOM   3054 C  C   . GLU A 1 377 ? 2.610   -0.708  2.075   1.00 39.71  ? 377  GLU A C   1 
ATOM   3055 O  O   . GLU A 1 377 ? 2.116   0.129   1.308   1.00 40.25  ? 377  GLU A O   1 
ATOM   3056 C  CB  . GLU A 1 377 ? 4.733   0.317   2.991   1.00 44.38  ? 377  GLU A CB  1 
ATOM   3057 C  CG  . GLU A 1 377 ? 5.323   1.190   4.115   1.00 43.19  ? 377  GLU A CG  1 
ATOM   3058 C  CD  . GLU A 1 377 ? 5.931   0.396   5.287   1.00 44.88  ? 377  GLU A CD  1 
ATOM   3059 O  OE1 . GLU A 1 377 ? 6.132   -0.831  5.160   1.00 43.68  ? 377  GLU A OE1 1 
ATOM   3060 O  OE2 . GLU A 1 377 ? 6.201   1.020   6.337   1.00 44.11  ? 377  GLU A OE2 1 
ATOM   3061 N  N   . ARG A 1 378 ? 2.543   -2.024  1.840   1.00 39.26  ? 378  ARG A N   1 
ATOM   3062 C  CA  . ARG A 1 378 ? 1.734   -2.555  0.746   1.00 41.06  ? 378  ARG A CA  1 
ATOM   3063 C  C   . ARG A 1 378 ? 0.321   -2.018  0.750   1.00 38.86  ? 378  ARG A C   1 
ATOM   3064 O  O   . ARG A 1 378 ? -0.341  -2.056  -0.296  1.00 37.93  ? 378  ARG A O   1 
ATOM   3065 C  CB  . ARG A 1 378 ? 1.589   -4.075  0.823   1.00 42.82  ? 378  ARG A CB  1 
ATOM   3066 C  CG  . ARG A 1 378 ? 2.814   -4.867  0.662   1.00 47.41  ? 378  ARG A CG  1 
ATOM   3067 C  CD  . ARG A 1 378 ? 2.496   -6.295  0.999   1.00 41.36  ? 378  ARG A CD  1 
ATOM   3068 N  NE  . ARG A 1 378 ? 3.706   -7.008  1.369   1.00 40.48  ? 378  ARG A NE  1 
ATOM   3069 C  CZ  . ARG A 1 378 ? 4.580   -7.495  0.505   1.00 45.61  ? 378  ARG A CZ  1 
ATOM   3070 N  NH1 . ARG A 1 378 ? 4.426   -7.332  -0.803  1.00 48.60  ? 378  ARG A NH1 1 
ATOM   3071 N  NH2 . ARG A 1 378 ? 5.629   -8.174  0.961   1.00 46.76  ? 378  ARG A NH2 1 
ATOM   3072 N  N   . PHE A 1 379 ? -0.175  -1.576  1.907   1.00 36.31  ? 379  PHE A N   1 
ATOM   3073 C  CA  . PHE A 1 379 ? -1.569  -1.190  2.063   1.00 36.44  ? 379  PHE A CA  1 
ATOM   3074 C  C   . PHE A 1 379 ? -1.752  0.316   2.050   1.00 38.62  ? 379  PHE A C   1 
ATOM   3075 O  O   . PHE A 1 379 ? -2.824  0.811   2.400   1.00 37.58  ? 379  PHE A O   1 
ATOM   3076 C  CB  . PHE A 1 379 ? -2.146  -1.820  3.341   1.00 36.81  ? 379  PHE A CB  1 
ATOM   3077 C  CG  . PHE A 1 379 ? -2.387  -3.294  3.193   1.00 37.20  ? 379  PHE A CG  1 
ATOM   3078 C  CD1 . PHE A 1 379 ? -3.560  -3.763  2.604   1.00 36.45  ? 379  PHE A CD1 1 
ATOM   3079 C  CD2 . PHE A 1 379 ? -1.411  -4.206  3.542   1.00 39.28  ? 379  PHE A CD2 1 
ATOM   3080 C  CE1 . PHE A 1 379 ? -3.772  -5.130  2.420   1.00 35.59  ? 379  PHE A CE1 1 
ATOM   3081 C  CE2 . PHE A 1 379 ? -1.605  -5.565  3.353   1.00 36.13  ? 379  PHE A CE2 1 
ATOM   3082 C  CZ  . PHE A 1 379 ? -2.788  -6.034  2.801   1.00 37.06  ? 379  PHE A CZ  1 
ATOM   3083 N  N   . GLU A 1 380 ? -0.746  1.054   1.589   1.00 35.82  ? 380  GLU A N   1 
ATOM   3084 C  CA  . GLU A 1 380 ? -0.835  2.500   1.677   1.00 36.65  ? 380  GLU A CA  1 
ATOM   3085 C  C   . GLU A 1 380 ? -1.945  3.037   0.780   1.00 39.14  ? 380  GLU A C   1 
ATOM   3086 O  O   . GLU A 1 380 ? -2.563  4.053   1.105   1.00 40.67  ? 380  GLU A O   1 
ATOM   3087 C  CB  . GLU A 1 380 ? 0.521   3.092   1.314   1.00 44.65  ? 380  GLU A CB  1 
ATOM   3088 C  CG  . GLU A 1 380 ? 0.953   4.210   2.251   1.00 57.07  ? 380  GLU A CG  1 
ATOM   3089 C  CD  . GLU A 1 380 ? 2.463   4.283   2.330   1.00 61.21  ? 380  GLU A CD  1 
ATOM   3090 O  OE1 . GLU A 1 380 ? 3.102   4.306   1.256   1.00 64.87  ? 380  GLU A OE1 1 
ATOM   3091 O  OE2 . GLU A 1 380 ? 3.013   4.229   3.453   1.00 56.59  ? 380  GLU A OE2 1 
ATOM   3092 N  N   . ASN A 1 381 ? -2.231  2.355   -0.328  1.00 38.12  ? 381  ASN A N   1 
ATOM   3093 C  CA  . ASN A 1 381 ? -3.206  2.817   -1.316  1.00 36.57  ? 381  ASN A CA  1 
ATOM   3094 C  C   . ASN A 1 381 ? -4.105  1.665   -1.755  1.00 36.56  ? 381  ASN A C   1 
ATOM   3095 O  O   . ASN A 1 381 ? -3.749  0.916   -2.676  1.00 35.10  ? 381  ASN A O   1 
ATOM   3096 C  CB  . ASN A 1 381 ? -2.511  3.420   -2.536  1.00 39.12  ? 381  ASN A CB  1 
ATOM   3097 C  CG  . ASN A 1 381 ? -3.492  4.070   -3.494  1.00 42.15  ? 381  ASN A CG  1 
ATOM   3098 O  OD1 . ASN A 1 381 ? -4.707  4.012   -3.283  1.00 39.68  ? 381  ASN A OD1 1 
ATOM   3099 N  ND2 . ASN A 1 381 ? -2.976  4.643   -4.585  1.00 41.23  ? 381  ASN A ND2 1 
ATOM   3100 N  N   . PRO A 1 382 ? -5.288  1.512   -1.153  1.00 37.88  ? 382  PRO A N   1 
ATOM   3101 C  CA  . PRO A 1 382 ? -6.195  0.437   -1.591  1.00 35.92  ? 382  PRO A CA  1 
ATOM   3102 C  C   . PRO A 1 382 ? -6.530  0.486   -3.068  1.00 35.14  ? 382  PRO A C   1 
ATOM   3103 O  O   . PRO A 1 382 ? -6.845  -0.560  -3.645  1.00 35.74  ? 382  PRO A O   1 
ATOM   3104 C  CB  . PRO A 1 382 ? -7.446  0.658   -0.728  1.00 38.58  ? 382  PRO A CB  1 
ATOM   3105 C  CG  . PRO A 1 382 ? -6.919  1.359   0.505   1.00 45.00  ? 382  PRO A CG  1 
ATOM   3106 C  CD  . PRO A 1 382 ? -5.832  2.275   -0.018  1.00 38.40  ? 382  PRO A CD  1 
ATOM   3107 N  N   . SER A 1 383 ? -6.477  1.663   -3.702  1.00 34.65  ? 383  SER A N   1 
ATOM   3108 C  CA  . SER A 1 383 ? -6.794  1.733   -5.122  1.00 35.14  ? 383  SER A CA  1 
ATOM   3109 C  C   . SER A 1 383 ? -5.722  1.086   -5.993  1.00 33.78  ? 383  SER A C   1 
ATOM   3110 O  O   . SER A 1 383 ? -5.982  0.804   -7.166  1.00 37.45  ? 383  SER A O   1 
ATOM   3111 C  CB  . SER A 1 383 ? -6.994  3.187   -5.555  1.00 39.03  ? 383  SER A CB  1 
ATOM   3112 O  OG  . SER A 1 383 ? -8.049  3.799   -4.825  1.00 38.50  ? 383  SER A OG  1 
ATOM   3113 N  N   . ALA A 1 384 ? -4.527  0.885   -5.465  1.00 33.97  ? 384  ALA A N   1 
ATOM   3114 C  CA  . ALA A 1 384 ? -3.459  0.224   -6.203  1.00 36.80  ? 384  ALA A CA  1 
ATOM   3115 C  C   . ALA A 1 384 ? -3.478  -1.287  -6.032  1.00 38.17  ? 384  ALA A C   1 
ATOM   3116 O  O   . ALA A 1 384 ? -2.638  -1.980  -6.616  1.00 39.86  ? 384  ALA A O   1 
ATOM   3117 C  CB  . ALA A 1 384 ? -2.100  0.783   -5.768  1.00 39.59  ? 384  ALA A CB  1 
ATOM   3118 N  N   . ILE A 1 385 ? -4.407  -1.818  -5.249  1.00 32.99  ? 385  ILE A N   1 
ATOM   3119 C  CA  . ILE A 1 385 ? -4.530  -3.257  -5.041  1.00 35.65  ? 385  ILE A CA  1 
ATOM   3120 C  C   . ILE A 1 385 ? -5.652  -3.777  -5.936  1.00 33.41  ? 385  ILE A C   1 
ATOM   3121 O  O   . ILE A 1 385 ? -6.786  -3.286  -5.828  1.00 35.65  ? 385  ILE A O   1 
ATOM   3122 C  CB  . ILE A 1 385 ? -4.807  -3.582  -3.570  1.00 35.85  ? 385  ILE A CB  1 
ATOM   3123 C  CG1 . ILE A 1 385 ? -3.686  -3.014  -2.689  1.00 37.06  ? 385  ILE A CG1 1 
ATOM   3124 C  CG2 . ILE A 1 385 ? -5.000  -5.096  -3.396  1.00 36.22  ? 385  ILE A CG2 1 
ATOM   3125 C  CD1 . ILE A 1 385 ? -3.969  -3.144  -1.204  1.00 38.58  ? 385  ILE A CD1 1 
ATOM   3126 N  N   . PRO A 1 386 ? -5.398  -4.768  -6.795  1.00 34.83  ? 386  PRO A N   1 
ATOM   3127 C  CA  . PRO A 1 386 ? -6.456  -5.289  -7.676  1.00 33.70  ? 386  PRO A CA  1 
ATOM   3128 C  C   . PRO A 1 386 ? -7.657  -5.832  -6.901  1.00 33.37  ? 386  PRO A C   1 
ATOM   3129 O  O   . PRO A 1 386 ? -7.566  -6.235  -5.741  1.00 33.93  ? 386  PRO A O   1 
ATOM   3130 C  CB  . PRO A 1 386 ? -5.753  -6.418  -8.446  1.00 36.66  ? 386  PRO A CB  1 
ATOM   3131 C  CG  . PRO A 1 386 ? -4.305  -6.034  -8.423  1.00 36.20  ? 386  PRO A CG  1 
ATOM   3132 C  CD  . PRO A 1 386 ? -4.082  -5.361  -7.094  1.00 37.79  ? 386  PRO A CD  1 
ATOM   3133 N  N   . GLN A 1 387 ? -8.796  -5.892  -7.589  1.00 34.39  ? 387  GLN A N   1 
ATOM   3134 C  CA  . GLN A 1 387 ? -10.017 -6.374  -6.953  1.00 34.32  ? 387  GLN A CA  1 
ATOM   3135 C  C   . GLN A 1 387 ? -9.849  -7.798  -6.433  1.00 32.61  ? 387  GLN A C   1 
ATOM   3136 O  O   . GLN A 1 387 ? -9.300  -8.669  -7.115  1.00 34.32  ? 387  GLN A O   1 
ATOM   3137 C  CB  . GLN A 1 387 ? -11.180 -6.334  -7.948  1.00 33.23  ? 387  GLN A CB  1 
ATOM   3138 C  CG  . GLN A 1 387 ? -11.654 -4.947  -8.290  1.00 36.22  ? 387  GLN A CG  1 
ATOM   3139 C  CD  . GLN A 1 387 ? -13.077 -4.971  -8.778  1.00 35.04  ? 387  GLN A CD  1 
ATOM   3140 O  OE1 . GLN A 1 387 ? -14.016 -4.942  -7.973  1.00 35.21  ? 387  GLN A OE1 1 
ATOM   3141 N  NE2 . GLN A 1 387 ? -13.251 -5.062  -10.103 1.00 35.55  ? 387  GLN A NE2 1 
ATOM   3142 N  N   . HIS A 1 388 ? -10.340 -8.025  -5.213  1.00 32.84  ? 388  HIS A N   1 
ATOM   3143 C  CA  . HIS A 1 388 ? -10.443 -9.341  -4.582  1.00 34.04  ? 388  HIS A CA  1 
ATOM   3144 C  C   . HIS A 1 388 ? -9.096  -10.002 -4.369  1.00 32.92  ? 388  HIS A C   1 
ATOM   3145 O  O   . HIS A 1 388 ? -9.017  -11.223 -4.184  1.00 33.10  ? 388  HIS A O   1 
ATOM   3146 C  CB  . HIS A 1 388 ? -11.385 -10.252 -5.369  1.00 32.87  ? 388  HIS A CB  1 
ATOM   3147 C  CG  . HIS A 1 388 ? -12.731 -9.634  -5.558  1.00 34.92  ? 388  HIS A CG  1 
ATOM   3148 N  ND1 . HIS A 1 388 ? -13.530 -9.294  -4.486  1.00 35.74  ? 388  HIS A ND1 1 
ATOM   3149 C  CD2 . HIS A 1 388 ? -13.392 -9.236  -6.669  1.00 37.16  ? 388  HIS A CD2 1 
ATOM   3150 C  CE1 . HIS A 1 388 ? -14.647 -8.748  -4.933  1.00 39.75  ? 388  HIS A CE1 1 
ATOM   3151 N  NE2 . HIS A 1 388 ? -14.589 -8.697  -6.252  1.00 35.45  ? 388  HIS A NE2 1 
ATOM   3152 N  N   . ALA A 1 389 ? -8.039  -9.206  -4.352  1.00 31.29  ? 389  ALA A N   1 
ATOM   3153 C  CA  . ALA A 1 389 ? -6.731  -9.726  -3.973  1.00 34.32  ? 389  ALA A CA  1 
ATOM   3154 C  C   . ALA A 1 389 ? -6.612  -10.015 -2.481  1.00 34.33  ? 389  ALA A C   1 
ATOM   3155 O  O   . ALA A 1 389 ? -5.740  -10.796 -2.086  1.00 32.19  ? 389  ALA A O   1 
ATOM   3156 C  CB  . ALA A 1 389 ? -5.642  -8.733  -4.363  1.00 33.77  ? 389  ALA A CB  1 
ATOM   3157 N  N   . PHE A 1 390 ? -7.455  -9.412  -1.640  1.00 30.02  ? 390  PHE A N   1 
ATOM   3158 C  CA  . PHE A 1 390 ? -7.238  -9.403  -0.188  1.00 29.61  ? 390  PHE A CA  1 
ATOM   3159 C  C   . PHE A 1 390 ? -8.591  -9.687  0.460   1.00 32.09  ? 390  PHE A C   1 
ATOM   3160 O  O   . PHE A 1 390 ? -9.457  -8.814  0.464   1.00 33.65  ? 390  PHE A O   1 
ATOM   3161 C  CB  . PHE A 1 390 ? -6.658  -8.057  0.238   1.00 33.38  ? 390  PHE A CB  1 
ATOM   3162 C  CG  . PHE A 1 390 ? -6.429  -7.899  1.724   1.00 35.17  ? 390  PHE A CG  1 
ATOM   3163 C  CD1 . PHE A 1 390 ? -5.466  -8.654  2.395   1.00 32.47  ? 390  PHE A CD1 1 
ATOM   3164 C  CD2 . PHE A 1 390 ? -7.145  -6.946  2.440   1.00 35.08  ? 390  PHE A CD2 1 
ATOM   3165 C  CE1 . PHE A 1 390 ? -5.256  -8.475  3.763   1.00 31.55  ? 390  PHE A CE1 1 
ATOM   3166 C  CE2 . PHE A 1 390 ? -6.936  -6.759  3.805   1.00 33.10  ? 390  PHE A CE2 1 
ATOM   3167 C  CZ  . PHE A 1 390 ? -5.986  -7.516  4.467   1.00 34.59  ? 390  PHE A CZ  1 
ATOM   3168 N  N   . LYS A 1 391 ? -8.783  -10.929 0.973   1.00 32.05  ? 391  LYS A N   1 
ATOM   3169 C  CA  . LYS A 1 391 ? -10.117 -11.370 1.391   1.00 29.99  ? 391  LYS A CA  1 
ATOM   3170 C  C   . LYS A 1 391 ? -10.149 -11.963 2.799   1.00 29.63  ? 391  LYS A C   1 
ATOM   3171 O  O   . LYS A 1 391 ? -10.806 -12.985 3.014   1.00 31.74  ? 391  LYS A O   1 
ATOM   3172 C  CB  . LYS A 1 391 ? -10.659 -12.414 0.410   1.00 32.86  ? 391  LYS A CB  1 
ATOM   3173 C  CG  . LYS A 1 391 ? -10.625 -12.030 -1.078  1.00 34.43  ? 391  LYS A CG  1 
ATOM   3174 C  CD  . LYS A 1 391 ? -11.487 -10.809 -1.373  1.00 33.56  ? 391  LYS A CD  1 
ATOM   3175 C  CE  . LYS A 1 391 ? -12.967 -11.116 -1.132  1.00 35.44  ? 391  LYS A CE  1 
ATOM   3176 N  NZ  . LYS A 1 391 ? -13.857 -10.029 -1.656  1.00 37.89  ? 391  LYS A NZ  1 
ATOM   3177 N  N   . PRO A 1 392 ? -9.476  -11.366 3.785   1.00 30.47  ? 392  PRO A N   1 
ATOM   3178 C  CA  . PRO A 1 392 ? -9.429  -11.989 5.119   1.00 29.87  ? 392  PRO A CA  1 
ATOM   3179 C  C   . PRO A 1 392 ? -10.754 -11.946 5.854   1.00 33.68  ? 392  PRO A C   1 
ATOM   3180 O  O   . PRO A 1 392 ? -10.908 -12.638 6.871   1.00 32.75  ? 392  PRO A O   1 
ATOM   3181 C  CB  . PRO A 1 392 ? -8.380  -11.149 5.844   1.00 31.23  ? 392  PRO A CB  1 
ATOM   3182 C  CG  . PRO A 1 392 ? -8.565  -9.799  5.251   1.00 33.62  ? 392  PRO A CG  1 
ATOM   3183 C  CD  . PRO A 1 392 ? -8.804  -10.057 3.780   1.00 33.05  ? 392  PRO A CD  1 
ATOM   3184 N  N   . HIS A 1 393 ? -11.703 -11.155 5.368   1.00 30.61  ? 393  HIS A N   1 
ATOM   3185 C  CA  . HIS A 1 393 ? -13.023 -11.041 5.981   1.00 33.10  ? 393  HIS A CA  1 
ATOM   3186 C  C   . HIS A 1 393 ? -14.125 -11.586 5.077   1.00 32.45  ? 393  HIS A C   1 
ATOM   3187 O  O   . HIS A 1 393 ? -15.305 -11.242 5.243   1.00 32.32  ? 393  HIS A O   1 
ATOM   3188 C  CB  . HIS A 1 393 ? -13.235 -9.580  6.390   1.00 36.26  ? 393  HIS A CB  1 
ATOM   3189 C  CG  . HIS A 1 393 ? -12.403 -9.181  7.583   1.00 37.48  ? 393  HIS A CG  1 
ATOM   3190 N  ND1 . HIS A 1 393 ? -11.397 -8.243  7.523   1.00 39.75  ? 393  HIS A ND1 1 
ATOM   3191 C  CD2 . HIS A 1 393 ? -12.476 -9.565  8.884   1.00 44.47  ? 393  HIS A CD2 1 
ATOM   3192 C  CE1 . HIS A 1 393 ? -10.857 -8.095  8.718   1.00 39.86  ? 393  HIS A CE1 1 
ATOM   3193 N  NE2 . HIS A 1 393 ? -11.494 -8.887  9.566   1.00 45.63  ? 393  HIS A NE2 1 
ATOM   3194 N  N   . GLY A 1 394 ? -13.769 -12.447 4.121   1.00 31.51  ? 394  GLY A N   1 
ATOM   3195 C  CA  . GLY A 1 394 ? -14.795 -13.046 3.287   1.00 31.57  ? 394  GLY A CA  1 
ATOM   3196 C  C   . GLY A 1 394 ? -15.254 -12.105 2.187   1.00 31.37  ? 394  GLY A C   1 
ATOM   3197 O  O   . GLY A 1 394 ? -14.530 -11.187 1.782   1.00 31.70  ? 394  GLY A O   1 
ATOM   3198 N  N   . ASN A 1 395 ? -16.476 -12.337 1.693   1.00 30.95  ? 395  ASN A N   1 
ATOM   3199 C  CA  . ASN A 1 395 ? -16.911 -11.671 0.472   1.00 32.10  ? 395  ASN A CA  1 
ATOM   3200 C  C   . ASN A 1 395 ? -18.376 -11.252 0.498   1.00 32.31  ? 395  ASN A C   1 
ATOM   3201 O  O   . ASN A 1 395 ? -19.240 -12.006 0.952   1.00 31.01  ? 395  ASN A O   1 
ATOM   3202 C  CB  . ASN A 1 395 ? -16.721 -12.572 -0.740  1.00 30.13  ? 395  ASN A CB  1 
ATOM   3203 C  CG  . ASN A 1 395 ? -17.027 -11.844 -2.051  1.00 32.49  ? 395  ASN A CG  1 
ATOM   3204 O  OD1 . ASN A 1 395 ? -16.325 -10.898 -2.418  1.00 32.53  ? 395  ASN A OD1 1 
ATOM   3205 N  ND2 . ASN A 1 395 ? -18.072 -12.272 -2.748  1.00 31.93  ? 395  ASN A ND2 1 
ATOM   3206 N  N   . GLY A 1 396 ? -18.642 -10.045 -0.017  1.00 32.09  ? 396  GLY A N   1 
ATOM   3207 C  CA  . GLY A 1 396 ? -19.997 -9.665  -0.388  1.00 31.83  ? 396  GLY A CA  1 
ATOM   3208 C  C   . GLY A 1 396 ? -20.897 -9.512  0.822   1.00 32.02  ? 396  GLY A C   1 
ATOM   3209 O  O   . GLY A 1 396 ? -20.455 -9.167  1.917   1.00 31.49  ? 396  GLY A O   1 
ATOM   3210 N  N   . GLN A 1 397 ? -22.191 -9.764  0.609   1.00 30.61  ? 397  GLN A N   1 
ATOM   3211 C  CA  . GLN A 1 397 ? -23.132 -9.632  1.711   1.00 32.87  ? 397  GLN A CA  1 
ATOM   3212 C  C   . GLN A 1 397 ? -22.860 -10.643 2.816   1.00 34.26  ? 397  GLN A C   1 
ATOM   3213 O  O   . GLN A 1 397 ? -23.330 -10.449 3.946   1.00 31.10  ? 397  GLN A O   1 
ATOM   3214 C  CB  . GLN A 1 397 ? -24.568 -9.777  1.202   1.00 32.51  ? 397  GLN A CB  1 
ATOM   3215 C  CG  . GLN A 1 397 ? -24.923 -11.157 0.687   1.00 33.22  ? 397  GLN A CG  1 
ATOM   3216 C  CD  . GLN A 1 397 ? -26.325 -11.191 0.104   1.00 39.76  ? 397  GLN A CD  1 
ATOM   3217 O  OE1 . GLN A 1 397 ? -27.162 -10.354 0.448   1.00 37.49  ? 397  GLN A OE1 1 
ATOM   3218 N  NE2 . GLN A 1 397 ? -26.581 -12.140 -0.794  1.00 36.40  ? 397  GLN A NE2 1 
ATOM   3219 N  N   . ARG A 1 398 ? -22.109 -11.711 2.521   1.00 32.67  ? 398  ARG A N   1 
ATOM   3220 C  CA  . ARG A 1 398 ? -21.710 -12.674 3.540   1.00 31.17  ? 398  ARG A CA  1 
ATOM   3221 C  C   . ARG A 1 398 ? -20.311 -12.395 4.096   1.00 30.54  ? 398  ARG A C   1 
ATOM   3222 O  O   . ARG A 1 398 ? -19.709 -13.278 4.710   1.00 30.36  ? 398  ARG A O   1 
ATOM   3223 C  CB  . ARG A 1 398 ? -21.789 -14.099 2.987   1.00 32.69  ? 398  ARG A CB  1 
ATOM   3224 C  CG  . ARG A 1 398 ? -23.184 -14.528 2.522   1.00 30.24  ? 398  ARG A CG  1 
ATOM   3225 C  CD  . ARG A 1 398 ? -24.259 -14.327 3.602   1.00 29.19  ? 398  ARG A CD  1 
ATOM   3226 N  NE  . ARG A 1 398 ? -23.965 -15.025 4.850   1.00 30.29  ? 398  ARG A NE  1 
ATOM   3227 C  CZ  . ARG A 1 398 ? -24.315 -16.277 5.112   1.00 32.27  ? 398  ARG A CZ  1 
ATOM   3228 N  NH1 . ARG A 1 398 ? -24.958 -17.020 4.217   1.00 31.18  ? 398  ARG A NH1 1 
ATOM   3229 N  NH2 . ARG A 1 398 ? -24.010 -16.797 6.299   1.00 31.22  ? 398  ARG A NH2 1 
ATOM   3230 N  N   . ALA A 1 399 ? -19.784 -11.191 3.892   1.00 31.37  ? 399  ALA A N   1 
ATOM   3231 C  CA  . ALA A 1 399 ? -18.519 -10.844 4.523   1.00 30.46  ? 399  ALA A CA  1 
ATOM   3232 C  C   . ALA A 1 399 ? -18.716 -10.672 6.029   1.00 32.22  ? 399  ALA A C   1 
ATOM   3233 O  O   . ALA A 1 399 ? -19.837 -10.607 6.544   1.00 33.22  ? 399  ALA A O   1 
ATOM   3234 C  CB  . ALA A 1 399 ? -17.915 -9.572  3.904   1.00 32.51  ? 399  ALA A CB  1 
ATOM   3235 N  N   . CYS A 1 400 ? -17.594 -10.577 6.734   1.00 28.74  ? 400  CYS A N   1 
ATOM   3236 C  CA  . CYS A 1 400 ? -17.588 -10.528 8.190   1.00 30.90  ? 400  CYS A CA  1 
ATOM   3237 C  C   . CYS A 1 400 ? -18.339 -9.301  8.704   1.00 31.90  ? 400  CYS A C   1 
ATOM   3238 O  O   . CYS A 1 400 ? -17.976 -8.164  8.393   1.00 35.57  ? 400  CYS A O   1 
ATOM   3239 C  CB  . CYS A 1 400 ? -16.143 -10.517 8.675   1.00 30.56  ? 400  CYS A CB  1 
ATOM   3240 S  SG  . CYS A 1 400 ? -15.984 -10.334 10.452  1.00 32.04  ? 400  CYS A SG  1 
ATOM   3241 N  N   . ILE A 1 401 ? -19.401 -9.533  9.485   1.00 31.29  ? 401  ILE A N   1 
ATOM   3242 C  CA  . ILE A 1 401 ? -20.141 -8.426  10.071  1.00 30.89  ? 401  ILE A CA  1 
ATOM   3243 C  C   . ILE A 1 401 ? -19.340 -7.723  11.164  1.00 34.06  ? 401  ILE A C   1 
ATOM   3244 O  O   . ILE A 1 401 ? -19.603 -6.550  11.453  1.00 32.92  ? 401  ILE A O   1 
ATOM   3245 C  CB  . ILE A 1 401 ? -21.491 -8.915  10.641  1.00 29.19  ? 401  ILE A CB  1 
ATOM   3246 C  CG1 . ILE A 1 401 ? -22.459 -7.733  10.805  1.00 35.07  ? 401  ILE A CG1 1 
ATOM   3247 C  CG2 . ILE A 1 401 ? -21.275 -9.620  11.976  1.00 30.75  ? 401  ILE A CG2 1 
ATOM   3248 C  CD1 . ILE A 1 401 ? -23.854 -8.154  11.317  1.00 34.96  ? 401  ILE A CD1 1 
ATOM   3249 N  N   . GLY A 1 402 ? -18.363 -8.402  11.765  1.00 30.68  ? 402  GLY A N   1 
ATOM   3250 C  CA  . GLY A 1 402 ? -17.593 -7.889  12.882  1.00 34.48  ? 402  GLY A CA  1 
ATOM   3251 C  C   . GLY A 1 402 ? -16.258 -7.267  12.526  1.00 32.77  ? 402  GLY A C   1 
ATOM   3252 O  O   . GLY A 1 402 ? -15.481 -6.950  13.436  1.00 33.55  ? 402  GLY A O   1 
ATOM   3253 N  N   . GLN A 1 403 ? -15.997 -7.023  11.243  1.00 31.01  ? 403  GLN A N   1 
ATOM   3254 C  CA  . GLN A 1 403 ? -14.688 -6.549  10.800  1.00 31.49  ? 403  GLN A CA  1 
ATOM   3255 C  C   . GLN A 1 403 ? -14.273 -5.267  11.511  1.00 33.64  ? 403  GLN A C   1 
ATOM   3256 O  O   . GLN A 1 403 ? -13.116 -5.122  11.928  1.00 33.59  ? 403  GLN A O   1 
ATOM   3257 C  CB  . GLN A 1 403 ? -14.713 -6.328  9.283   1.00 36.24  ? 403  GLN A CB  1 
ATOM   3258 C  CG  . GLN A 1 403 ? -13.461 -5.671  8.752   1.00 43.06  ? 403  GLN A CG  1 
ATOM   3259 C  CD  . GLN A 1 403 ? -13.641 -5.133  7.348   1.00 47.84  ? 403  GLN A CD  1 
ATOM   3260 O  OE1 . GLN A 1 403 ? -14.488 -5.612  6.592   1.00 41.73  ? 403  GLN A OE1 1 
ATOM   3261 N  NE2 . GLN A 1 403 ? -12.827 -4.146  6.983   1.00 54.63  ? 403  GLN A NE2 1 
ATOM   3262 N  N   . GLN A 1 404 ? -15.182 -4.296  11.618  1.00 37.02  ? 404  GLN A N   1 
ATOM   3263 C  CA  . GLN A 1 404 ? -14.798 -3.028  12.245  1.00 36.09  ? 404  GLN A CA  1 
ATOM   3264 C  C   . GLN A 1 404 ? -14.552 -3.200  13.735  1.00 35.61  ? 404  GLN A C   1 
ATOM   3265 O  O   . GLN A 1 404 ? -13.643 -2.576  14.300  1.00 36.10  ? 404  GLN A O   1 
ATOM   3266 C  CB  . GLN A 1 404 ? -15.859 -1.957  11.999  1.00 37.13  ? 404  GLN A CB  1 
ATOM   3267 C  CG  . GLN A 1 404 ? -16.110 -1.747  10.515  1.00 43.99  ? 404  GLN A CG  1 
ATOM   3268 C  CD  . GLN A 1 404 ? -14.950 -1.040  9.871   1.00 51.60  ? 404  GLN A CD  1 
ATOM   3269 O  OE1 . GLN A 1 404 ? -14.321 -1.575  8.957   1.00 56.98  ? 404  GLN A OE1 1 
ATOM   3270 N  NE2 . GLN A 1 404 ? -14.627 0.157   10.367  1.00 59.07  ? 404  GLN A NE2 1 
ATOM   3271 N  N   . PHE A 1 405 ? -15.350 -4.042  14.385  1.00 31.92  ? 405  PHE A N   1 
ATOM   3272 C  CA  . PHE A 1 405 ? -15.129 -4.351  15.797  1.00 32.37  ? 405  PHE A CA  1 
ATOM   3273 C  C   . PHE A 1 405 ? -13.733 -4.927  16.002  1.00 33.60  ? 405  PHE A C   1 
ATOM   3274 O  O   . PHE A 1 405 ? -12.972 -4.469  16.868  1.00 34.92  ? 405  PHE A O   1 
ATOM   3275 C  CB  . PHE A 1 405 ? -16.202 -5.344  16.277  1.00 31.71  ? 405  PHE A CB  1 
ATOM   3276 C  CG  . PHE A 1 405 ? -16.241 -5.556  17.776  1.00 33.51  ? 405  PHE A CG  1 
ATOM   3277 C  CD1 . PHE A 1 405 ? -15.373 -6.452  18.386  1.00 33.94  ? 405  PHE A CD1 1 
ATOM   3278 C  CD2 . PHE A 1 405 ? -17.182 -4.899  18.572  1.00 34.11  ? 405  PHE A CD2 1 
ATOM   3279 C  CE1 . PHE A 1 405 ? -15.416 -6.672  19.760  1.00 33.81  ? 405  PHE A CE1 1 
ATOM   3280 C  CE2 . PHE A 1 405 ? -17.235 -5.121  19.949  1.00 35.43  ? 405  PHE A CE2 1 
ATOM   3281 C  CZ  . PHE A 1 405 ? -16.341 -6.001  20.544  1.00 32.64  ? 405  PHE A CZ  1 
ATOM   3282 N  N   . ALA A 1 406 ? -13.396 -5.960  15.219  1.00 31.36  ? 406  ALA A N   1 
ATOM   3283 C  CA  . ALA A 1 406 ? -12.086 -6.606  15.323  1.00 33.31  ? 406  ALA A CA  1 
ATOM   3284 C  C   . ALA A 1 406 ? -10.959 -5.605  15.116  1.00 31.26  ? 406  ALA A C   1 
ATOM   3285 O  O   . ALA A 1 406 ? -9.967  -5.595  15.862  1.00 30.59  ? 406  ALA A O   1 
ATOM   3286 C  CB  . ALA A 1 406 ? -11.968 -7.741  14.294  1.00 31.45  ? 406  ALA A CB  1 
ATOM   3287 N  N   . LEU A 1 407 ? -11.060 -4.796  14.071  1.00 33.91  ? 407  LEU A N   1 
ATOM   3288 C  CA  . LEU A 1 407 ? -9.922  -3.941  13.765  1.00 34.95  ? 407  LEU A CA  1 
ATOM   3289 C  C   . LEU A 1 407 ? -9.831  -2.779  14.740  1.00 34.32  ? 407  LEU A C   1 
ATOM   3290 O  O   . LEU A 1 407 ? -8.724  -2.349  15.072  1.00 33.68  ? 407  LEU A O   1 
ATOM   3291 C  CB  . LEU A 1 407 ? -9.987  -3.469  12.312  1.00 34.82  ? 407  LEU A CB  1 
ATOM   3292 C  CG  . LEU A 1 407 ? -9.747  -4.585  11.278  1.00 39.41  ? 407  LEU A CG  1 
ATOM   3293 C  CD1 . LEU A 1 407 ? -10.089 -4.122  9.848   1.00 42.67  ? 407  LEU A CD1 1 
ATOM   3294 C  CD2 . LEU A 1 407 ? -8.332  -5.123  11.342  1.00 42.36  ? 407  LEU A CD2 1 
ATOM   3295 N  N   . HIS A 1 408 ? -10.952 -2.304  15.283  1.00 32.88  ? 408  HIS A N   1 
ATOM   3296 C  CA  . HIS A 1 408 ? -10.842 -1.256  16.288  1.00 35.38  ? 408  HIS A CA  1 
ATOM   3297 C  C   . HIS A 1 408 ? -10.208 -1.801  17.563  1.00 34.65  ? 408  HIS A C   1 
ATOM   3298 O  O   . HIS A 1 408 ? -9.305  -1.179  18.139  1.00 35.67  ? 408  HIS A O   1 
ATOM   3299 C  CB  . HIS A 1 408 ? -12.213 -0.652  16.580  1.00 35.54  ? 408  HIS A CB  1 
ATOM   3300 C  CG  . HIS A 1 408 ? -12.159 0.576   17.435  1.00 35.84  ? 408  HIS A CG  1 
ATOM   3301 N  ND1 . HIS A 1 408 ? -11.957 1.837   16.909  1.00 35.01  ? 408  HIS A ND1 1 
ATOM   3302 C  CD2 . HIS A 1 408 ? -12.284 0.742   18.772  1.00 39.56  ? 408  HIS A CD2 1 
ATOM   3303 C  CE1 . HIS A 1 408 ? -11.967 2.724   17.887  1.00 38.21  ? 408  HIS A CE1 1 
ATOM   3304 N  NE2 . HIS A 1 408 ? -12.161 2.087   19.027  1.00 37.31  ? 408  HIS A NE2 1 
ATOM   3305 N  N   . GLU A 1 409 ? -10.673 -2.967  18.017  1.00 32.39  ? 409  GLU A N   1 
ATOM   3306 C  CA  . GLU A 1 409 ? -10.082 -3.610  19.186  1.00 32.60  ? 409  GLU A CA  1 
ATOM   3307 C  C   . GLU A 1 409 ? -8.593  -3.860  18.985  1.00 33.24  ? 409  GLU A C   1 
ATOM   3308 O  O   . GLU A 1 409 ? -7.763  -3.503  19.834  1.00 32.65  ? 409  GLU A O   1 
ATOM   3309 C  CB  . GLU A 1 409 ? -10.807 -4.925  19.467  1.00 33.19  ? 409  GLU A CB  1 
ATOM   3310 C  CG  . GLU A 1 409 ? -10.181 -5.714  20.617  1.00 33.16  ? 409  GLU A CG  1 
ATOM   3311 C  CD  . GLU A 1 409 ? -10.893 -7.025  20.876  1.00 32.65  ? 409  GLU A CD  1 
ATOM   3312 O  OE1 . GLU A 1 409 ? -11.824 -7.371  20.105  1.00 32.27  ? 409  GLU A OE1 1 
ATOM   3313 O  OE2 . GLU A 1 409 ? -10.529 -7.702  21.849  1.00 32.15  ? 409  GLU A OE2 1 
ATOM   3314 N  N   . ALA A 1 410 ? -8.233  -4.472  17.857  1.00 31.57  ? 410  ALA A N   1 
ATOM   3315 C  CA  . ALA A 1 410 ? -6.835  -4.837  17.647  1.00 31.11  ? 410  ALA A CA  1 
ATOM   3316 C  C   . ALA A 1 410 ? -5.967  -3.597  17.488  1.00 35.07  ? 410  ALA A C   1 
ATOM   3317 O  O   . ALA A 1 410 ? -4.817  -3.568  17.949  1.00 35.44  ? 410  ALA A O   1 
ATOM   3318 C  CB  . ALA A 1 410 ? -6.707  -5.756  16.430  1.00 32.02  ? 410  ALA A CB  1 
ATOM   3319 N  N   . THR A 1 411 ? -6.497  -2.557  16.850  1.00 32.53  ? 411  THR A N   1 
ATOM   3320 C  CA  . THR A 1 411 ? -5.717  -1.332  16.708  1.00 34.86  ? 411  THR A CA  1 
ATOM   3321 C  C   . THR A 1 411 ? -5.490  -0.675  18.073  1.00 34.93  ? 411  THR A C   1 
ATOM   3322 O  O   . THR A 1 411 ? -4.354  -0.310  18.423  1.00 34.80  ? 411  THR A O   1 
ATOM   3323 C  CB  . THR A 1 411 ? -6.423  -0.392  15.731  1.00 35.59  ? 411  THR A CB  1 
ATOM   3324 O  OG1 . THR A 1 411 ? -6.539  -1.047  14.450  1.00 33.89  ? 411  THR A OG1 1 
ATOM   3325 C  CG2 . THR A 1 411 ? -5.607  0.890   15.560  1.00 35.99  ? 411  THR A CG2 1 
ATOM   3326 N  N   . LEU A 1 412 ? -6.555  -0.565  18.879  1.00 33.34  ? 412  LEU A N   1 
ATOM   3327 C  CA  . LEU A 1 412 ? -6.436  -0.012  20.231  1.00 34.39  ? 412  LEU A CA  1 
ATOM   3328 C  C   . LEU A 1 412 ? -5.408  -0.780  21.052  1.00 35.09  ? 412  LEU A C   1 
ATOM   3329 O  O   . LEU A 1 412 ? -4.501  -0.186  21.656  1.00 37.47  ? 412  LEU A O   1 
ATOM   3330 C  CB  . LEU A 1 412 ? -7.798  -0.038  20.934  1.00 32.28  ? 412  LEU A CB  1 
ATOM   3331 C  CG  . LEU A 1 412 ? -7.776  0.060   22.466  1.00 36.50  ? 412  LEU A CG  1 
ATOM   3332 C  CD1 . LEU A 1 412 ? -7.363  1.459   22.873  1.00 37.93  ? 412  LEU A CD1 1 
ATOM   3333 C  CD2 . LEU A 1 412 ? -9.147  -0.284  23.046  1.00 38.30  ? 412  LEU A CD2 1 
ATOM   3334 N  N   . VAL A 1 413 ? -5.531  -2.108  21.076  1.00 34.37  ? 413  VAL A N   1 
ATOM   3335 C  CA  . VAL A 1 413 ? -4.700  -2.935  21.952  1.00 34.38  ? 413  VAL A CA  1 
ATOM   3336 C  C   . VAL A 1 413 ? -3.247  -2.913  21.494  1.00 35.30  ? 413  VAL A C   1 
ATOM   3337 O  O   . VAL A 1 413 ? -2.322  -2.758  22.306  1.00 35.75  ? 413  VAL A O   1 
ATOM   3338 C  CB  . VAL A 1 413 ? -5.266  -4.366  22.000  1.00 36.53  ? 413  VAL A CB  1 
ATOM   3339 C  CG1 . VAL A 1 413 ? -4.333  -5.293  22.743  1.00 42.04  ? 413  VAL A CG1 1 
ATOM   3340 C  CG2 . VAL A 1 413 ? -6.643  -4.345  22.680  1.00 33.22  ? 413  VAL A CG2 1 
ATOM   3341 N  N   . LEU A 1 414 ? -3.015  -3.060  20.189  1.00 32.89  ? 414  LEU A N   1 
ATOM   3342 C  CA  . LEU A 1 414 ? -1.634  -3.048  19.711  1.00 35.67  ? 414  LEU A CA  1 
ATOM   3343 C  C   . LEU A 1 414 ? -1.012  -1.672  19.913  1.00 37.47  ? 414  LEU A C   1 
ATOM   3344 O  O   . LEU A 1 414 ? 0.188   -1.566  20.204  1.00 36.13  ? 414  LEU A O   1 
ATOM   3345 C  CB  . LEU A 1 414 ? -1.570  -3.473  18.235  1.00 34.13  ? 414  LEU A CB  1 
ATOM   3346 C  CG  . LEU A 1 414 ? -0.224  -3.762  17.553  1.00 39.33  ? 414  LEU A CG  1 
ATOM   3347 C  CD1 . LEU A 1 414 ? 0.619   -4.760  18.375  1.00 37.94  ? 414  LEU A CD1 1 
ATOM   3348 C  CD2 . LEU A 1 414 ? -0.417  -4.277  16.123  1.00 35.24  ? 414  LEU A CD2 1 
ATOM   3349 N  N   . GLY A 1 415 ? -1.810  -0.610  19.767  1.00 35.01  ? 415  GLY A N   1 
ATOM   3350 C  CA  . GLY A 1 415 ? -1.304  0.732   20.027  1.00 35.19  ? 415  GLY A CA  1 
ATOM   3351 C  C   . GLY A 1 415 ? -0.872  0.917   21.472  1.00 41.21  ? 415  GLY A C   1 
ATOM   3352 O  O   . GLY A 1 415 ? 0.199   1.460   21.749  1.00 42.18  ? 415  GLY A O   1 
ATOM   3353 N  N   . MET A 1 416 ? -1.698  0.470   22.424  1.00 35.59  ? 416  MET A N   1 
ATOM   3354 C  CA  . MET A 1 416 ? -1.279  0.596   23.822  1.00 35.47  ? 416  MET A CA  1 
ATOM   3355 C  C   . MET A 1 416 ? -0.083  -0.295  24.124  1.00 37.00  ? 416  MET A C   1 
ATOM   3356 O  O   . MET A 1 416 ? 0.813   0.082   24.892  1.00 39.97  ? 416  MET A O   1 
ATOM   3357 C  CB  . MET A 1 416 ? -2.434  0.288   24.774  1.00 35.72  ? 416  MET A CB  1 
ATOM   3358 C  CG  . MET A 1 416 ? -3.641  1.189   24.631  1.00 35.93  ? 416  MET A CG  1 
ATOM   3359 S  SD  . MET A 1 416 ? -4.966  0.752   25.761  1.00 41.49  ? 416  MET A SD  1 
ATOM   3360 C  CE  . MET A 1 416 ? -4.151  1.103   27.321  1.00 40.62  ? 416  MET A CE  1 
ATOM   3361 N  N   . MET A 1 417 ? -0.061  -1.479  23.528  1.00 35.02  ? 417  MET A N   1 
ATOM   3362 C  CA  . MET A 1 417 ? 1.055   -2.403  23.660  1.00 36.62  ? 417  MET A CA  1 
ATOM   3363 C  C   . MET A 1 417 ? 2.360   -1.729  23.235  1.00 40.42  ? 417  MET A C   1 
ATOM   3364 O  O   . MET A 1 417 ? 3.369   -1.763  23.956  1.00 39.36  ? 417  MET A O   1 
ATOM   3365 C  CB  . MET A 1 417 ? 0.689   -3.591  22.791  1.00 39.46  ? 417  MET A CB  1 
ATOM   3366 C  CG  . MET A 1 417 ? -0.081  -4.666  23.545  1.00 38.01  ? 417  MET A CG  1 
ATOM   3367 S  SD  . MET A 1 417 ? -0.560  -5.967  22.398  1.00 37.84  ? 417  MET A SD  1 
ATOM   3368 C  CE  . MET A 1 417 ? 0.996   -6.713  21.974  1.00 40.22  ? 417  MET A CE  1 
ATOM   3369 N  N   . LEU A 1 418 ? 2.337   -1.058  22.088  1.00 37.52  ? 418  LEU A N   1 
ATOM   3370 C  CA  . LEU A 1 418 ? 3.524   -0.380  21.588  1.00 38.83  ? 418  LEU A CA  1 
ATOM   3371 C  C   . LEU A 1 418 ? 3.808   0.934   22.307  1.00 37.02  ? 418  LEU A C   1 
ATOM   3372 O  O   . LEU A 1 418 ? 4.956   1.388   22.300  1.00 42.62  ? 418  LEU A O   1 
ATOM   3373 C  CB  . LEU A 1 418 ? 3.366   -0.138  20.085  1.00 38.18  ? 418  LEU A CB  1 
ATOM   3374 C  CG  . LEU A 1 418 ? 3.223   -1.435  19.282  1.00 42.84  ? 418  LEU A CG  1 
ATOM   3375 C  CD1 . LEU A 1 418 ? 2.800   -1.149  17.844  1.00 41.57  ? 418  LEU A CD1 1 
ATOM   3376 C  CD2 . LEU A 1 418 ? 4.513   -2.246  19.298  1.00 40.93  ? 418  LEU A CD2 1 
ATOM   3377 N  N   . LYS A 1 419 ? 2.791   1.572   22.894  1.00 36.97  ? 419  LYS A N   1 
ATOM   3378 C  CA  . LYS A 1 419 ? 3.031   2.768   23.695  1.00 36.80  ? 419  LYS A CA  1 
ATOM   3379 C  C   . LYS A 1 419 ? 3.751   2.420   24.989  1.00 42.94  ? 419  LYS A C   1 
ATOM   3380 O  O   . LYS A 1 419 ? 4.661   3.140   25.416  1.00 39.84  ? 419  LYS A O   1 
ATOM   3381 C  CB  . LYS A 1 419 ? 1.718   3.481   24.017  1.00 40.27  ? 419  LYS A CB  1 
ATOM   3382 C  CG  . LYS A 1 419 ? 1.873   4.657   25.008  1.00 43.68  ? 419  LYS A CG  1 
ATOM   3383 C  CD  . LYS A 1 419 ? 0.529   5.276   25.363  1.00 42.10  ? 419  LYS A CD  1 
ATOM   3384 C  CE  . LYS A 1 419 ? 0.666   6.423   26.353  1.00 43.60  ? 419  LYS A CE  1 
ATOM   3385 N  NZ  . LYS A 1 419 ? -0.627  7.138   26.550  1.00 46.24  ? 419  LYS A NZ  1 
ATOM   3386 N  N   . HIS A 1 420 ? 3.381   1.306   25.611  1.00 40.02  ? 420  HIS A N   1 
ATOM   3387 C  CA  . HIS A 1 420 ? 3.797   1.055   26.984  1.00 40.51  ? 420  HIS A CA  1 
ATOM   3388 C  C   . HIS A 1 420 ? 4.987   0.116   27.130  1.00 37.57  ? 420  HIS A C   1 
ATOM   3389 O  O   . HIS A 1 420 ? 5.579   0.083   28.212  1.00 42.05  ? 420  HIS A O   1 
ATOM   3390 C  CB  . HIS A 1 420 ? 2.612   0.515   27.791  1.00 37.36  ? 420  HIS A CB  1 
ATOM   3391 C  CG  . HIS A 1 420 ? 1.610   1.566   28.134  1.00 39.88  ? 420  HIS A CG  1 
ATOM   3392 N  ND1 . HIS A 1 420 ? 1.776   2.423   29.197  1.00 38.18  ? 420  HIS A ND1 1 
ATOM   3393 C  CD2 . HIS A 1 420 ? 0.446   1.921   27.541  1.00 38.15  ? 420  HIS A CD2 1 
ATOM   3394 C  CE1 . HIS A 1 420 ? 0.758   3.262   29.248  1.00 38.37  ? 420  HIS A CE1 1 
ATOM   3395 N  NE2 . HIS A 1 420 ? -0.067  2.976   28.256  1.00 41.03  ? 420  HIS A NE2 1 
ATOM   3396 N  N   . PHE A 1 421 ? 5.367   -0.638  26.102  1.00 38.23  ? 421  PHE A N   1 
ATOM   3397 C  CA  . PHE A 1 421 ? 6.390   -1.663  26.269  1.00 39.29  ? 421  PHE A CA  1 
ATOM   3398 C  C   . PHE A 1 421 ? 7.329   -1.715  25.076  1.00 45.44  ? 421  PHE A C   1 
ATOM   3399 O  O   . PHE A 1 421 ? 6.925   -1.489  23.931  1.00 42.60  ? 421  PHE A O   1 
ATOM   3400 C  CB  . PHE A 1 421 ? 5.798   -3.073  26.431  1.00 41.89  ? 421  PHE A CB  1 
ATOM   3401 C  CG  . PHE A 1 421 ? 4.819   -3.197  27.553  1.00 38.21  ? 421  PHE A CG  1 
ATOM   3402 C  CD1 . PHE A 1 421 ? 5.263   -3.416  28.848  1.00 37.79  ? 421  PHE A CD1 1 
ATOM   3403 C  CD2 . PHE A 1 421 ? 3.458   -3.084  27.320  1.00 41.29  ? 421  PHE A CD2 1 
ATOM   3404 C  CE1 . PHE A 1 421 ? 4.371   -3.532  29.892  1.00 38.02  ? 421  PHE A CE1 1 
ATOM   3405 C  CE2 . PHE A 1 421 ? 2.546   -3.190  28.365  1.00 37.98  ? 421  PHE A CE2 1 
ATOM   3406 C  CZ  . PHE A 1 421 ? 3.006   -3.409  29.655  1.00 39.58  ? 421  PHE A CZ  1 
ATOM   3407 N  N   . ASP A 1 422 ? 8.583   -2.054  25.361  1.00 43.12  ? 422  ASP A N   1 
ATOM   3408 C  CA  . ASP A 1 422 ? 9.464   -2.649  24.367  1.00 43.94  ? 422  ASP A CA  1 
ATOM   3409 C  C   . ASP A 1 422 ? 9.337   -4.162  24.448  1.00 45.26  ? 422  ASP A C   1 
ATOM   3410 O  O   . ASP A 1 422 ? 9.026   -4.716  25.507  1.00 45.71  ? 422  ASP A O   1 
ATOM   3411 C  CB  . ASP A 1 422 ? 10.923  -2.237  24.587  1.00 46.29  ? 422  ASP A CB  1 
ATOM   3412 C  CG  . ASP A 1 422 ? 11.158  -0.777  24.314  1.00 49.26  ? 422  ASP A CG  1 
ATOM   3413 O  OD1 . ASP A 1 422 ? 10.884  -0.340  23.178  1.00 52.21  ? 422  ASP A OD1 1 
ATOM   3414 O  OD2 . ASP A 1 422 ? 11.630  -0.069  25.221  1.00 51.58  ? 422  ASP A OD2 1 
ATOM   3415 N  N   . PHE A 1 423 ? 9.567   -4.833  23.324  1.00 37.18  ? 423  PHE A N   1 
ATOM   3416 C  CA  . PHE A 1 423 ? 9.381   -6.274  23.244  1.00 40.63  ? 423  PHE A CA  1 
ATOM   3417 C  C   . PHE A 1 423 ? 10.650  -6.958  22.772  1.00 45.53  ? 423  PHE A C   1 
ATOM   3418 O  O   . PHE A 1 423 ? 11.379  -6.443  21.915  1.00 46.58  ? 423  PHE A O   1 
ATOM   3419 C  CB  . PHE A 1 423 ? 8.213   -6.645  22.315  1.00 39.25  ? 423  PHE A CB  1 
ATOM   3420 C  CG  . PHE A 1 423 ? 6.880   -6.187  22.824  1.00 40.10  ? 423  PHE A CG  1 
ATOM   3421 C  CD1 . PHE A 1 423 ? 6.134   -6.990  23.679  1.00 45.27  ? 423  PHE A CD1 1 
ATOM   3422 C  CD2 . PHE A 1 423 ? 6.385   -4.939  22.476  1.00 42.00  ? 423  PHE A CD2 1 
ATOM   3423 C  CE1 . PHE A 1 423 ? 4.897   -6.561  24.169  1.00 38.40  ? 423  PHE A CE1 1 
ATOM   3424 C  CE2 . PHE A 1 423 ? 5.169   -4.498  22.959  1.00 39.92  ? 423  PHE A CE2 1 
ATOM   3425 C  CZ  . PHE A 1 423 ? 4.419   -5.312  23.816  1.00 41.31  ? 423  PHE A CZ  1 
ATOM   3426 N  N   . GLU A 1 424 ? 10.895  -8.134  23.333  1.00 41.93  ? 424  GLU A N   1 
ATOM   3427 C  CA  . GLU A 1 424 ? 12.083  -8.915  23.039  1.00 41.94  ? 424  GLU A CA  1 
ATOM   3428 C  C   . GLU A 1 424 ? 11.649  -10.313 22.636  1.00 43.04  ? 424  GLU A C   1 
ATOM   3429 O  O   . GLU A 1 424 ? 10.917  -10.975 23.377  1.00 42.86  ? 424  GLU A O   1 
ATOM   3430 C  CB  . GLU A 1 424 ? 13.024  -8.962  24.250  1.00 41.72  ? 424  GLU A CB  1 
ATOM   3431 C  CG  . GLU A 1 424 ? 14.282  -9.750  23.984  1.00 47.07  ? 424  GLU A CG  1 
ATOM   3432 C  CD  . GLU A 1 424 ? 15.074  -10.018 25.243  1.00 53.01  ? 424  GLU A CD  1 
ATOM   3433 O  OE1 . GLU A 1 424 ? 14.684  -9.508  26.317  1.00 50.34  ? 424  GLU A OE1 1 
ATOM   3434 O  OE2 . GLU A 1 424 ? 16.088  -10.737 25.148  1.00 57.45  ? 424  GLU A OE2 1 
ATOM   3435 N  N   . ASP A 1 425 ? 12.088  -10.753 21.456  1.00 40.26  ? 425  ASP A N   1 
ATOM   3436 C  CA  . ASP A 1 425 ? 11.914  -12.138 21.014  1.00 38.49  ? 425  ASP A CA  1 
ATOM   3437 C  C   . ASP A 1 425 ? 13.047  -12.967 21.620  1.00 42.11  ? 425  ASP A C   1 
ATOM   3438 O  O   . ASP A 1 425 ? 13.976  -13.416 20.942  1.00 41.63  ? 425  ASP A O   1 
ATOM   3439 C  CB  . ASP A 1 425 ? 11.901  -12.193 19.489  1.00 41.66  ? 425  ASP A CB  1 
ATOM   3440 C  CG  . ASP A 1 425 ? 11.846  -13.603 18.932  1.00 41.30  ? 425  ASP A CG  1 
ATOM   3441 O  OD1 . ASP A 1 425 ? 11.367  -14.526 19.621  1.00 41.42  ? 425  ASP A OD1 1 
ATOM   3442 O  OD2 . ASP A 1 425 ? 12.295  -13.793 17.778  1.00 43.30  ? 425  ASP A OD2 1 
ATOM   3443 N  N   . HIS A 1 426 ? 12.957  -13.168 22.941  1.00 42.16  ? 426  HIS A N   1 
ATOM   3444 C  CA  . HIS A 1 426 ? 14.105  -13.673 23.698  1.00 43.95  ? 426  HIS A CA  1 
ATOM   3445 C  C   . HIS A 1 426 ? 14.434  -15.131 23.397  1.00 44.02  ? 426  HIS A C   1 
ATOM   3446 O  O   . HIS A 1 426 ? 15.563  -15.559 23.665  1.00 43.74  ? 426  HIS A O   1 
ATOM   3447 C  CB  . HIS A 1 426 ? 13.858  -13.501 25.199  1.00 42.46  ? 426  HIS A CB  1 
ATOM   3448 C  CG  . HIS A 1 426 ? 12.719  -14.322 25.714  1.00 45.46  ? 426  HIS A CG  1 
ATOM   3449 N  ND1 . HIS A 1 426 ? 11.405  -14.053 25.391  1.00 42.09  ? 426  HIS A ND1 1 
ATOM   3450 C  CD2 . HIS A 1 426 ? 12.693  -15.406 26.529  1.00 45.49  ? 426  HIS A CD2 1 
ATOM   3451 C  CE1 . HIS A 1 426 ? 10.620  -14.940 25.980  1.00 45.20  ? 426  HIS A CE1 1 
ATOM   3452 N  NE2 . HIS A 1 426 ? 11.375  -15.770 26.680  1.00 46.63  ? 426  HIS A NE2 1 
ATOM   3453 N  N   . THR A 1 427 ? 13.493  -15.912 22.863  1.00 42.60  ? 427  THR A N   1 
ATOM   3454 C  CA  . THR A 1 427 ? 13.754  -17.308 22.519  1.00 39.82  ? 427  THR A CA  1 
ATOM   3455 C  C   . THR A 1 427 ? 14.016  -17.530 21.032  1.00 40.24  ? 427  THR A C   1 
ATOM   3456 O  O   . THR A 1 427 ? 14.157  -18.682 20.613  1.00 40.72  ? 427  THR A O   1 
ATOM   3457 C  CB  . THR A 1 427 ? 12.585  -18.210 22.941  1.00 41.06  ? 427  THR A CB  1 
ATOM   3458 O  OG1 . THR A 1 427 ? 11.481  -18.033 22.032  1.00 43.55  ? 427  THR A OG1 1 
ATOM   3459 C  CG2 . THR A 1 427 ? 12.133  -17.891 24.350  1.00 39.67  ? 427  THR A CG2 1 
ATOM   3460 N  N   . ASN A 1 428 ? 14.061  -16.474 20.227  1.00 40.86  ? 428  ASN A N   1 
ATOM   3461 C  CA  . ASN A 1 428 ? 14.115  -16.618 18.774  1.00 44.23  ? 428  ASN A CA  1 
ATOM   3462 C  C   . ASN A 1 428 ? 13.055  -17.615 18.305  1.00 43.20  ? 428  ASN A C   1 
ATOM   3463 O  O   . ASN A 1 428 ? 13.338  -18.648 17.689  1.00 42.15  ? 428  ASN A O   1 
ATOM   3464 C  CB  . ASN A 1 428 ? 15.516  -17.033 18.305  1.00 44.43  ? 428  ASN A CB  1 
ATOM   3465 C  CG  . ASN A 1 428 ? 15.760  -16.668 16.853  1.00 49.98  ? 428  ASN A CG  1 
ATOM   3466 O  OD1 . ASN A 1 428 ? 15.093  -15.781 16.314  1.00 47.91  ? 428  ASN A OD1 1 
ATOM   3467 N  ND2 . ASN A 1 428 ? 16.707  -17.353 16.207  1.00 51.23  ? 428  ASN A ND2 1 
ATOM   3468 N  N   . TYR A 1 429 ? 11.802  -17.272 18.603  1.00 40.95  ? 429  TYR A N   1 
ATOM   3469 C  CA  . TYR A 1 429 ? 10.702  -18.210 18.444  1.00 39.87  ? 429  TYR A CA  1 
ATOM   3470 C  C   . TYR A 1 429 ? 10.554  -18.660 16.997  1.00 41.29  ? 429  TYR A C   1 
ATOM   3471 O  O   . TYR A 1 429 ? 10.593  -17.846 16.073  1.00 42.21  ? 429  TYR A O   1 
ATOM   3472 C  CB  . TYR A 1 429 ? 9.412   -17.547 18.932  1.00 39.26  ? 429  TYR A CB  1 
ATOM   3473 C  CG  . TYR A 1 429 ? 8.140   -18.239 18.509  1.00 41.40  ? 429  TYR A CG  1 
ATOM   3474 C  CD1 . TYR A 1 429 ? 7.756   -19.440 19.087  1.00 37.92  ? 429  TYR A CD1 1 
ATOM   3475 C  CD2 . TYR A 1 429 ? 7.308   -17.673 17.545  1.00 40.88  ? 429  TYR A CD2 1 
ATOM   3476 C  CE1 . TYR A 1 429 ? 6.575   -20.069 18.714  1.00 40.25  ? 429  TYR A CE1 1 
ATOM   3477 C  CE2 . TYR A 1 429 ? 6.143   -18.292 17.158  1.00 37.35  ? 429  TYR A CE2 1 
ATOM   3478 C  CZ  . TYR A 1 429 ? 5.775   -19.477 17.745  1.00 38.65  ? 429  TYR A CZ  1 
ATOM   3479 O  OH  . TYR A 1 429 ? 4.616   -20.091 17.353  1.00 35.23  ? 429  TYR A OH  1 
ATOM   3480 N  N   . GLU A 1 430 ? 10.371  -19.961 16.805  1.00 41.73  ? 430  GLU A N   1 
ATOM   3481 C  CA  . GLU A 1 430 ? 10.096  -20.511 15.486  1.00 45.05  ? 430  GLU A CA  1 
ATOM   3482 C  C   . GLU A 1 430 ? 8.588   -20.617 15.310  1.00 42.79  ? 430  GLU A C   1 
ATOM   3483 O  O   . GLU A 1 430 ? 7.925   -21.357 16.047  1.00 42.28  ? 430  GLU A O   1 
ATOM   3484 C  CB  . GLU A 1 430 ? 10.753  -21.877 15.305  1.00 48.54  ? 430  GLU A CB  1 
ATOM   3485 C  CG  . GLU A 1 430 ? 10.988  -22.249 13.853  1.00 57.24  ? 430  GLU A CG  1 
ATOM   3486 C  CD  . GLU A 1 430 ? 11.702  -23.581 13.698  1.00 69.18  ? 430  GLU A CD  1 
ATOM   3487 O  OE1 . GLU A 1 430 ? 12.651  -23.845 14.467  1.00 74.66  ? 430  GLU A OE1 1 
ATOM   3488 O  OE2 . GLU A 1 430 ? 11.319  -24.359 12.797  1.00 75.04  ? 430  GLU A OE2 1 
ATOM   3489 N  N   . LEU A 1 431 ? 8.050   -19.891 14.329  1.00 39.91  ? 431  LEU A N   1 
ATOM   3490 C  CA  . LEU A 1 431 ? 6.603   -19.874 14.149  1.00 40.60  ? 431  LEU A CA  1 
ATOM   3491 C  C   . LEU A 1 431 ? 6.060   -21.292 14.004  1.00 38.25  ? 431  LEU A C   1 
ATOM   3492 O  O   . LEU A 1 431 ? 6.542   -22.092 13.198  1.00 41.59  ? 431  LEU A O   1 
ATOM   3493 C  CB  . LEU A 1 431 ? 6.220   -19.025 12.939  1.00 38.98  ? 431  LEU A CB  1 
ATOM   3494 C  CG  . LEU A 1 431 ? 4.707   -18.918 12.711  1.00 39.56  ? 431  LEU A CG  1 
ATOM   3495 C  CD1 . LEU A 1 431 ? 4.071   -18.141 13.849  1.00 38.93  ? 431  LEU A CD1 1 
ATOM   3496 C  CD2 . LEU A 1 431 ? 4.420   -18.265 11.362  1.00 42.03  ? 431  LEU A CD2 1 
ATOM   3497 N  N   . ASP A 1 432 ? 5.045   -21.598 14.804  1.00 35.57  ? 432  ASP A N   1 
ATOM   3498 C  CA  . ASP A 1 432 ? 4.375   -22.891 14.821  1.00 36.65  ? 432  ASP A CA  1 
ATOM   3499 C  C   . ASP A 1 432 ? 2.885   -22.573 14.846  1.00 36.42  ? 432  ASP A C   1 
ATOM   3500 O  O   . ASP A 1 432 ? 2.403   -21.986 15.819  1.00 37.18  ? 432  ASP A O   1 
ATOM   3501 C  CB  . ASP A 1 432 ? 4.815   -23.683 16.063  1.00 38.53  ? 432  ASP A CB  1 
ATOM   3502 C  CG  . ASP A 1 432 ? 4.186   -25.053 16.162  1.00 43.48  ? 432  ASP A CG  1 
ATOM   3503 O  OD1 . ASP A 1 432 ? 3.454   -25.469 15.253  1.00 45.12  ? 432  ASP A OD1 1 
ATOM   3504 O  OD2 . ASP A 1 432 ? 4.423   -25.721 17.191  1.00 50.63  ? 432  ASP A OD2 1 
ATOM   3505 N  N   . ILE A 1 433 ? 2.169   -22.897 13.774  1.00 35.80  ? 433  ILE A N   1 
ATOM   3506 C  CA  . ILE A 1 433 ? 0.780   -22.472 13.621  1.00 34.71  ? 433  ILE A CA  1 
ATOM   3507 C  C   . ILE A 1 433 ? -0.125  -23.644 13.955  1.00 33.27  ? 433  ILE A C   1 
ATOM   3508 O  O   . ILE A 1 433 ? -0.146  -24.657 13.244  1.00 35.88  ? 433  ILE A O   1 
ATOM   3509 C  CB  . ILE A 1 433 ? 0.505   -21.925 12.214  1.00 34.55  ? 433  ILE A CB  1 
ATOM   3510 C  CG1 . ILE A 1 433 ? 1.316   -20.650 12.005  1.00 36.72  ? 433  ILE A CG1 1 
ATOM   3511 C  CG2 . ILE A 1 433 ? -1.003  -21.625 12.059  1.00 32.92  ? 433  ILE A CG2 1 
ATOM   3512 C  CD1 . ILE A 1 433 ? 1.370   -20.163 10.575  1.00 38.65  ? 433  ILE A CD1 1 
ATOM   3513 N  N   . LYS A 1 434 ? -0.897  -23.487 15.037  1.00 34.86  ? 434  LYS A N   1 
ATOM   3514 C  CA  . LYS A 1 434 ? -1.879  -24.470 15.457  1.00 35.56  ? 434  LYS A CA  1 
ATOM   3515 C  C   . LYS A 1 434 ? -3.194  -24.250 14.724  1.00 31.97  ? 434  LYS A C   1 
ATOM   3516 O  O   . LYS A 1 434 ? -3.624  -23.110 14.516  1.00 36.71  ? 434  LYS A O   1 
ATOM   3517 C  CB  . LYS A 1 434 ? -2.111  -24.364 16.967  1.00 35.20  ? 434  LYS A CB  1 
ATOM   3518 C  CG  . LYS A 1 434 ? -3.157  -25.315 17.542  1.00 36.51  ? 434  LYS A CG  1 
ATOM   3519 C  CD  . LYS A 1 434 ? -3.185  -25.159 19.072  1.00 42.03  ? 434  LYS A CD  1 
ATOM   3520 C  CE  . LYS A 1 434 ? -4.316  -25.947 19.723  1.00 47.69  ? 434  LYS A CE  1 
ATOM   3521 N  NZ  . LYS A 1 434 ? -4.191  -27.408 19.467  1.00 47.66  ? 434  LYS A NZ  1 
ATOM   3522 N  N   . GLU A 1 435 ? -3.844  -25.345 14.355  1.00 32.41  ? 435  GLU A N   1 
ATOM   3523 C  CA  . GLU A 1 435 ? -5.085  -25.282 13.594  1.00 33.57  ? 435  GLU A CA  1 
ATOM   3524 C  C   . GLU A 1 435 ? -6.241  -25.797 14.443  1.00 36.13  ? 435  GLU A C   1 
ATOM   3525 O  O   . GLU A 1 435 ? -6.176  -26.901 14.999  1.00 34.61  ? 435  GLU A O   1 
ATOM   3526 C  CB  . GLU A 1 435 ? -4.962  -26.080 12.295  1.00 33.34  ? 435  GLU A CB  1 
ATOM   3527 C  CG  . GLU A 1 435 ? -3.829  -25.553 11.413  1.00 33.23  ? 435  GLU A CG  1 
ATOM   3528 C  CD  . GLU A 1 435 ? -4.034  -25.844 9.930   1.00 36.35  ? 435  GLU A CD  1 
ATOM   3529 O  OE1 . GLU A 1 435 ? -5.176  -26.169 9.530   1.00 36.61  ? 435  GLU A OE1 1 
ATOM   3530 O  OE2 . GLU A 1 435 ? -3.040  -25.766 9.169   1.00 35.69  ? 435  GLU A OE2 1 
ATOM   3531 N  N   . THR A 1 436 ? -7.286  -24.983 14.544  1.00 34.75  ? 436  THR A N   1 
ATOM   3532 C  CA  . THR A 1 436 ? -8.570  -25.352 15.128  1.00 34.59  ? 436  THR A CA  1 
ATOM   3533 C  C   . THR A 1 436 ? -9.683  -24.872 14.210  1.00 38.13  ? 436  THR A C   1 
ATOM   3534 O  O   . THR A 1 436 ? -10.618 -24.180 14.623  1.00 34.49  ? 436  THR A O   1 
ATOM   3535 C  CB  . THR A 1 436 ? -8.718  -24.767 16.534  1.00 35.39  ? 436  THR A CB  1 
ATOM   3536 O  OG1 . THR A 1 436 ? -8.566  -23.341 16.480  1.00 35.56  ? 436  THR A OG1 1 
ATOM   3537 C  CG2 . THR A 1 436 ? -7.658  -25.336 17.469  1.00 37.38  ? 436  THR A CG2 1 
ATOM   3538 N  N   . LEU A 1 437 ? -9.569  -25.242 12.929  1.00 34.73  ? 437  LEU A N   1 
ATOM   3539 C  CA  . LEU A 1 437 ? -10.264 -24.597 11.818  1.00 31.94  ? 437  LEU A CA  1 
ATOM   3540 C  C   . LEU A 1 437 ? -9.626  -23.228 11.609  1.00 35.99  ? 437  LEU A C   1 
ATOM   3541 O  O   . LEU A 1 437 ? -9.042  -22.957 10.551  1.00 33.18  ? 437  LEU A O   1 
ATOM   3542 C  CB  . LEU A 1 437 ? -11.781 -24.481 12.062  1.00 32.68  ? 437  LEU A CB  1 
ATOM   3543 C  CG  . LEU A 1 437 ? -12.539 -25.795 12.325  1.00 34.28  ? 437  LEU A CG  1 
ATOM   3544 C  CD1 . LEU A 1 437 ? -14.045 -25.558 12.413  1.00 34.55  ? 437  LEU A CD1 1 
ATOM   3545 C  CD2 . LEU A 1 437 ? -12.246 -26.810 11.229  1.00 34.47  ? 437  LEU A CD2 1 
ATOM   3546 N  N   . THR A 1 438 ? -9.720  -22.366 12.619  1.00 31.22  ? 438  THR A N   1 
ATOM   3547 C  CA  . THR A 1 438 ? -8.962  -21.126 12.641  1.00 33.14  ? 438  THR A CA  1 
ATOM   3548 C  C   . THR A 1 438 ? -7.467  -21.404 12.882  1.00 34.14  ? 438  THR A C   1 
ATOM   3549 O  O   . THR A 1 438 ? -7.055  -22.526 13.196  1.00 34.78  ? 438  THR A O   1 
ATOM   3550 C  CB  . THR A 1 438 ? -9.507  -20.196 13.731  1.00 33.70  ? 438  THR A CB  1 
ATOM   3551 O  OG1 . THR A 1 438 ? -9.495  -20.884 14.985  1.00 35.82  ? 438  THR A OG1 1 
ATOM   3552 C  CG2 . THR A 1 438 ? -10.966 -19.782 13.403  1.00 32.43  ? 438  THR A CG2 1 
ATOM   3553 N  N   . LEU A 1 439 ? -6.653  -20.354 12.731  1.00 31.44  ? 439  LEU A N   1 
ATOM   3554 C  CA  . LEU A 1 439 ? -5.192  -20.429 12.819  1.00 31.77  ? 439  LEU A CA  1 
ATOM   3555 C  C   . LEU A 1 439 ? -4.649  -19.508 13.905  1.00 32.83  ? 439  LEU A C   1 
ATOM   3556 O  O   . LEU A 1 439 ? -5.077  -18.355 14.032  1.00 32.07  ? 439  LEU A O   1 
ATOM   3557 C  CB  . LEU A 1 439 ? -4.551  -20.023 11.490  1.00 31.22  ? 439  LEU A CB  1 
ATOM   3558 C  CG  . LEU A 1 439 ? -4.983  -20.743 10.217  1.00 32.24  ? 439  LEU A CG  1 
ATOM   3559 C  CD1 . LEU A 1 439 ? -4.197  -20.177 9.010   1.00 33.40  ? 439  LEU A CD1 1 
ATOM   3560 C  CD2 . LEU A 1 439 ? -4.756  -22.251 10.352  1.00 33.43  ? 439  LEU A CD2 1 
ATOM   3561 N  N   . LYS A 1 440 ? -3.650  -19.994 14.659  1.00 33.75  ? 440  LYS A N   1 
ATOM   3562 C  CA  . LYS A 1 440 ? -3.075  -19.162 15.705  1.00 32.96  ? 440  LYS A CA  1 
ATOM   3563 C  C   . LYS A 1 440 ? -1.682  -19.675 16.019  1.00 34.89  ? 440  LYS A C   1 
ATOM   3564 O  O   . LYS A 1 440 ? -1.482  -20.896 16.014  1.00 35.08  ? 440  LYS A O   1 
ATOM   3565 C  CB  . LYS A 1 440 ? -3.948  -19.188 16.975  1.00 34.50  ? 440  LYS A CB  1 
ATOM   3566 C  CG  . LYS A 1 440 ? -3.610  -18.097 17.977  1.00 36.07  ? 440  LYS A CG  1 
ATOM   3567 C  CD  . LYS A 1 440 ? -4.456  -18.198 19.257  1.00 38.68  ? 440  LYS A CD  1 
ATOM   3568 C  CE  . LYS A 1 440 ? -5.906  -18.518 18.984  1.00 39.99  ? 440  LYS A CE  1 
ATOM   3569 N  NZ  . LYS A 1 440 ? -6.666  -18.456 20.271  1.00 44.03  ? 440  LYS A NZ  1 
ATOM   3570 N  N   . PRO A 1 441 ? -0.712  -18.798 16.298  1.00 34.94  ? 441  PRO A N   1 
ATOM   3571 C  CA  . PRO A 1 441 ? 0.592   -19.270 16.786  1.00 36.03  ? 441  PRO A CA  1 
ATOM   3572 C  C   . PRO A 1 441 ? 0.436   -20.068 18.070  1.00 39.23  ? 441  PRO A C   1 
ATOM   3573 O  O   . PRO A 1 441 ? -0.452  -19.808 18.884  1.00 35.81  ? 441  PRO A O   1 
ATOM   3574 C  CB  . PRO A 1 441 ? 1.372   -17.976 17.038  1.00 34.45  ? 441  PRO A CB  1 
ATOM   3575 C  CG  . PRO A 1 441 ? 0.685   -16.930 16.228  1.00 35.66  ? 441  PRO A CG  1 
ATOM   3576 C  CD  . PRO A 1 441 ? -0.763  -17.328 16.197  1.00 32.89  ? 441  PRO A CD  1 
ATOM   3577 N  N   . GLU A 1 442 ? 1.313   -21.053 18.242  1.00 36.29  ? 442  GLU A N   1 
ATOM   3578 C  CA  . GLU A 1 442 ? 1.357   -21.870 19.444  1.00 35.62  ? 442  GLU A CA  1 
ATOM   3579 C  C   . GLU A 1 442 ? 2.759   -21.778 20.016  1.00 41.07  ? 442  GLU A C   1 
ATOM   3580 O  O   . GLU A 1 442 ? 3.745   -21.841 19.271  1.00 38.30  ? 442  GLU A O   1 
ATOM   3581 C  CB  . GLU A 1 442 ? 0.998   -23.334 19.174  1.00 41.90  ? 442  GLU A CB  1 
ATOM   3582 C  CG  . GLU A 1 442 ? 1.117   -24.208 20.426  1.00 44.44  ? 442  GLU A CG  1 
ATOM   3583 C  CD  . GLU A 1 442 ? 0.665   -25.655 20.242  1.00 49.23  ? 442  GLU A CD  1 
ATOM   3584 O  OE1 . GLU A 1 442 ? 0.665   -26.177 19.107  1.00 46.40  ? 442  GLU A OE1 1 
ATOM   3585 O  OE2 . GLU A 1 442 ? 0.307   -26.283 21.263  1.00 56.23  ? 442  GLU A OE2 1 
ATOM   3586 N  N   . GLY A 1 443 ? 2.840   -21.606 21.328  1.00 38.27  ? 443  GLY A N   1 
ATOM   3587 C  CA  . GLY A 1 443 ? 4.130   -21.543 21.984  1.00 41.23  ? 443  GLY A CA  1 
ATOM   3588 C  C   . GLY A 1 443 ? 4.874   -20.249 21.797  1.00 38.04  ? 443  GLY A C   1 
ATOM   3589 O  O   . GLY A 1 443 ? 6.065   -20.186 22.123  1.00 41.53  ? 443  GLY A O   1 
ATOM   3590 N  N   . PHE A 1 444 ? 4.223   -19.218 21.265  1.00 38.56  ? 444  PHE A N   1 
ATOM   3591 C  CA  . PHE A 1 444 ? 4.864   -17.931 21.024  1.00 36.27  ? 444  PHE A CA  1 
ATOM   3592 C  C   . PHE A 1 444 ? 4.953   -17.154 22.335  1.00 40.23  ? 444  PHE A C   1 
ATOM   3593 O  O   . PHE A 1 444 ? 3.926   -16.830 22.942  1.00 36.65  ? 444  PHE A O   1 
ATOM   3594 C  CB  . PHE A 1 444 ? 4.074   -17.156 19.961  1.00 35.49  ? 444  PHE A CB  1 
ATOM   3595 C  CG  . PHE A 1 444 ? 4.555   -15.739 19.723  1.00 40.26  ? 444  PHE A CG  1 
ATOM   3596 C  CD1 . PHE A 1 444 ? 5.907   -15.421 19.745  1.00 37.10  ? 444  PHE A CD1 1 
ATOM   3597 C  CD2 . PHE A 1 444 ? 3.650   -14.732 19.436  1.00 35.23  ? 444  PHE A CD2 1 
ATOM   3598 C  CE1 . PHE A 1 444 ? 6.331   -14.114 19.533  1.00 36.21  ? 444  PHE A CE1 1 
ATOM   3599 C  CE2 . PHE A 1 444 ? 4.061   -13.424 19.213  1.00 35.90  ? 444  PHE A CE2 1 
ATOM   3600 C  CZ  . PHE A 1 444 ? 5.411   -13.110 19.252  1.00 36.47  ? 444  PHE A CZ  1 
ATOM   3601 N  N   . VAL A 1 445 ? 6.184   -16.865 22.778  1.00 36.07  ? 445  VAL A N   1 
ATOM   3602 C  CA  . VAL A 1 445 ? 6.447   -16.139 24.010  1.00 37.22  ? 445  VAL A CA  1 
ATOM   3603 C  C   . VAL A 1 445 ? 7.390   -14.986 23.694  1.00 38.32  ? 445  VAL A C   1 
ATOM   3604 O  O   . VAL A 1 445 ? 8.208   -15.062 22.769  1.00 39.05  ? 445  VAL A O   1 
ATOM   3605 C  CB  . VAL A 1 445 ? 7.058   -17.055 25.099  1.00 40.00  ? 445  VAL A CB  1 
ATOM   3606 C  CG1 . VAL A 1 445 ? 6.079   -18.149 25.490  1.00 37.80  ? 445  VAL A CG1 1 
ATOM   3607 C  CG2 . VAL A 1 445 ? 8.362   -17.662 24.598  1.00 40.41  ? 445  VAL A CG2 1 
ATOM   3608 N  N   . VAL A 1 446 ? 7.261   -13.906 24.459  1.00 36.47  ? 446  VAL A N   1 
ATOM   3609 C  CA  . VAL A 1 446 ? 8.144   -12.752 24.360  1.00 40.98  ? 446  VAL A CA  1 
ATOM   3610 C  C   . VAL A 1 446 ? 8.381   -12.212 25.766  1.00 40.51  ? 446  VAL A C   1 
ATOM   3611 O  O   . VAL A 1 446 ? 7.683   -12.562 26.718  1.00 38.18  ? 446  VAL A O   1 
ATOM   3612 C  CB  . VAL A 1 446 ? 7.570   -11.637 23.458  1.00 39.73  ? 446  VAL A CB  1 
ATOM   3613 C  CG1 . VAL A 1 446 ? 7.319   -12.157 22.036  1.00 36.51  ? 446  VAL A CG1 1 
ATOM   3614 C  CG2 . VAL A 1 446 ? 6.302   -11.038 24.072  1.00 39.42  ? 446  VAL A CG2 1 
ATOM   3615 N  N   . LYS A 1 447 ? 9.369   -11.335 25.883  1.00 39.97  ? 447  LYS A N   1 
ATOM   3616 C  CA  . LYS A 1 447 ? 9.550   -10.514 27.068  1.00 38.82  ? 447  LYS A CA  1 
ATOM   3617 C  C   . LYS A 1 447 ? 9.188   -9.073  26.751  1.00 44.57  ? 447  LYS A C   1 
ATOM   3618 O  O   . LYS A 1 447 ? 9.482   -8.571  25.660  1.00 45.72  ? 447  LYS A O   1 
ATOM   3619 C  CB  . LYS A 1 447 ? 10.988  -10.578 27.588  1.00 43.32  ? 447  LYS A CB  1 
ATOM   3620 C  CG  . LYS A 1 447 ? 11.304  -11.826 28.383  1.00 47.21  ? 447  LYS A CG  1 
ATOM   3621 C  CD  . LYS A 1 447 ? 12.794  -11.880 28.710  1.00 50.74  ? 447  LYS A CD  1 
ATOM   3622 C  CE  . LYS A 1 447 ? 13.054  -12.690 29.962  1.00 59.94  ? 447  LYS A CE  1 
ATOM   3623 N  NZ  . LYS A 1 447 ? 13.337  -14.114 29.626  1.00 58.20  ? 447  LYS A NZ  1 
ATOM   3624 N  N   . ALA A 1 448 ? 8.556   -8.405  27.707  1.00 39.42  ? 448  ALA A N   1 
ATOM   3625 C  CA  . ALA A 1 448 ? 8.205   -7.001  27.567  1.00 44.28  ? 448  ALA A CA  1 
ATOM   3626 C  C   . ALA A 1 448 ? 8.987   -6.191  28.587  1.00 51.92  ? 448  ALA A C   1 
ATOM   3627 O  O   . ALA A 1 448 ? 9.081   -6.580  29.758  1.00 51.81  ? 448  ALA A O   1 
ATOM   3628 C  CB  . ALA A 1 448 ? 6.700   -6.788  27.745  1.00 42.21  ? 448  ALA A CB  1 
ATOM   3629 N  N   . LYS A 1 449 ? 9.552   -5.075  28.146  1.00 45.83  ? 449  LYS A N   1 
ATOM   3630 C  CA  . LYS A 1 449 ? 10.248  -4.153  29.034  1.00 46.13  ? 449  LYS A CA  1 
ATOM   3631 C  C   . LYS A 1 449 ? 9.432   -2.872  29.112  1.00 44.35  ? 449  LYS A C   1 
ATOM   3632 O  O   . LYS A 1 449 ? 9.280   -2.158  28.115  1.00 46.43  ? 449  LYS A O   1 
ATOM   3633 C  CB  . LYS A 1 449 ? 11.678  -3.894  28.557  1.00 48.85  ? 449  LYS A CB  1 
ATOM   3634 C  CG  . LYS A 1 449 ? 12.572  -5.128  28.595  1.00 54.65  ? 449  LYS A CG  1 
ATOM   3635 C  CD  . LYS A 1 449 ? 12.191  -6.156  27.531  1.00 53.43  ? 449  LYS A CD  1 
ATOM   3636 C  CE  . LYS A 1 449 ? 13.309  -7.180  27.289  1.00 50.70  ? 449  LYS A CE  1 
ATOM   3637 N  NZ  . LYS A 1 449 ? 13.632  -8.017  28.471  1.00 61.88  ? 449  LYS A NZ  1 
ATOM   3638 N  N   . SER A 1 450 ? 8.899   -2.593  30.296  1.00 42.42  ? 450  SER A N   1 
ATOM   3639 C  CA  . SER A 1 450 ? 8.060   -1.423  30.487  1.00 44.84  ? 450  SER A CA  1 
ATOM   3640 C  C   . SER A 1 450 ? 8.799   -0.140  30.124  1.00 45.21  ? 450  SER A C   1 
ATOM   3641 O  O   . SER A 1 450 ? 9.977   0.035   30.444  1.00 47.62  ? 450  SER A O   1 
ATOM   3642 C  CB  . SER A 1 450 ? 7.585   -1.364  31.934  1.00 42.50  ? 450  SER A CB  1 
ATOM   3643 O  OG  . SER A 1 450 ? 6.722   -0.264  32.135  1.00 46.32  ? 450  SER A OG  1 
ATOM   3644 N  N   . LYS A 1 451 ? 8.097   0.755   29.430  1.00 41.71  ? 451  LYS A N   1 
ATOM   3645 C  CA  . LYS A 1 451 ? 8.539   2.131   29.260  1.00 47.88  ? 451  LYS A CA  1 
ATOM   3646 C  C   . LYS A 1 451 ? 8.143   3.001   30.441  1.00 49.70  ? 451  LYS A C   1 
ATOM   3647 O  O   . LYS A 1 451 ? 8.400   4.209   30.418  1.00 51.43  ? 451  LYS A O   1 
ATOM   3648 C  CB  . LYS A 1 451 ? 7.978   2.719   27.954  1.00 46.56  ? 451  LYS A CB  1 
ATOM   3649 C  CG  . LYS A 1 451 ? 8.515   2.049   26.690  1.00 46.40  ? 451  LYS A CG  1 
ATOM   3650 C  CD  . LYS A 1 451 ? 7.968   2.719   25.425  1.00 47.63  ? 451  LYS A CD  1 
ATOM   3651 C  CE  . LYS A 1 451 ? 8.511   2.083   24.156  1.00 48.37  ? 451  LYS A CE  1 
ATOM   3652 N  NZ  . LYS A 1 451 ? 9.916   2.498   23.865  1.00 52.84  ? 451  LYS A NZ  1 
ATOM   3653 N  N   . LYS A 1 452 ? 7.523   2.402   31.462  1.00 44.23  ? 452  LYS A N   1 
ATOM   3654 C  CA  . LYS A 1 452 ? 7.121   3.076   32.695  1.00 48.57  ? 452  LYS A CA  1 
ATOM   3655 C  C   . LYS A 1 452 ? 6.295   4.332   32.419  1.00 52.53  ? 452  LYS A C   1 
ATOM   3656 O  O   . LYS A 1 452 ? 6.546   5.408   32.966  1.00 51.32  ? 452  LYS A O   1 
ATOM   3657 C  CB  . LYS A 1 452 ? 8.342   3.397   33.565  1.00 52.18  ? 452  LYS A CB  1 
ATOM   3658 C  CG  . LYS A 1 452 ? 8.874   2.201   34.357  1.00 55.47  ? 452  LYS A CG  1 
ATOM   3659 C  CD  . LYS A 1 452 ? 10.336  2.407   34.777  1.00 61.74  ? 452  LYS A CD  1 
ATOM   3660 C  CE  . LYS A 1 452 ? 10.825  1.320   35.733  1.00 66.85  ? 452  LYS A CE  1 
ATOM   3661 N  NZ  . LYS A 1 452 ? 11.692  0.309   35.064  1.00 72.44  ? 452  LYS A NZ  1 
ATOM   3662 N  N   . ILE A 1 453 ? 5.271   4.186   31.588  1.00 48.73  ? 453  ILE A N   1 
ATOM   3663 C  CA  . ILE A 1 453 ? 4.376   5.295   31.276  1.00 46.04  ? 453  ILE A CA  1 
ATOM   3664 C  C   . ILE A 1 453 ? 3.053   5.051   31.995  1.00 51.72  ? 453  ILE A C   1 
ATOM   3665 O  O   . ILE A 1 453 ? 2.405   4.024   31.757  1.00 50.65  ? 453  ILE A O   1 
ATOM   3666 C  CB  . ILE A 1 453 ? 4.168   5.454   29.764  1.00 47.36  ? 453  ILE A CB  1 
ATOM   3667 C  CG1 . ILE A 1 453 ? 5.506   5.792   29.097  1.00 47.64  ? 453  ILE A CG1 1 
ATOM   3668 C  CG2 . ILE A 1 453 ? 3.146   6.546   29.505  1.00 47.28  ? 453  ILE A CG2 1 
ATOM   3669 C  CD1 . ILE A 1 453 ? 5.459   5.781   27.603  1.00 48.82  ? 453  ILE A CD1 1 
ATOM   3670 N  N   . PRO A 1 454 ? 2.616   5.958   32.868  1.00 54.51  ? 454  PRO A N   1 
ATOM   3671 C  CA  . PRO A 1 454 ? 1.443   5.677   33.704  1.00 53.93  ? 454  PRO A CA  1 
ATOM   3672 C  C   . PRO A 1 454 ? 0.158   5.589   32.900  1.00 53.24  ? 454  PRO A C   1 
ATOM   3673 O  O   . PRO A 1 454 ? 0.008   6.208   31.842  1.00 53.06  ? 454  PRO A O   1 
ATOM   3674 C  CB  . PRO A 1 454 ? 1.397   6.869   34.672  1.00 55.43  ? 454  PRO A CB  1 
ATOM   3675 C  CG  . PRO A 1 454 ? 2.771   7.487   34.610  1.00 59.97  ? 454  PRO A CG  1 
ATOM   3676 C  CD  . PRO A 1 454 ? 3.271   7.229   33.225  1.00 54.41  ? 454  PRO A CD  1 
ATOM   3677 N  N   . LEU A 1 455 ? -0.787  4.817   33.441  1.00 52.46  ? 455  LEU A N   1 
ATOM   3678 C  CA  . LEU A 1 455 ? -2.131  4.691   32.886  1.00 51.21  ? 455  LEU A CA  1 
ATOM   3679 C  C   . LEU A 1 455 ? -3.123  5.633   33.580  1.00 56.94  ? 455  LEU A C   1 
ATOM   3680 O  O   . LEU A 1 455 ? -2.767  6.354   34.521  1.00 57.18  ? 455  LEU A O   1 
ATOM   3681 C  CB  . LEU A 1 455 ? -2.617  3.244   33.009  1.00 48.76  ? 455  LEU A CB  1 
ATOM   3682 C  CG  . LEU A 1 455 ? -1.887  2.242   32.120  1.00 46.85  ? 455  LEU A CG  1 
ATOM   3683 C  CD1 . LEU A 1 455 ? -2.068  0.834   32.655  1.00 46.75  ? 455  LEU A CD1 1 
ATOM   3684 C  CD2 . LEU A 1 455 ? -2.412  2.346   30.703  1.00 43.15  ? 455  LEU A CD2 1 
ATOM   3685 O  OXT . LEU A 1 455 ? -4.306  5.698   33.219  1.00 52.12  ? 455  LEU A OXT 1 
ATOM   3686 N  N   . THR B 1 1   ? -1.428  -25.330 99.868  1.00 78.23  ? 1    THR B N   1 
ATOM   3687 C  CA  . THR B 1 1   ? -0.590  -24.404 99.109  1.00 78.27  ? 1    THR B CA  1 
ATOM   3688 C  C   . THR B 1 1   ? -0.240  -24.986 97.745  1.00 68.13  ? 1    THR B C   1 
ATOM   3689 O  O   . THR B 1 1   ? -0.680  -24.478 96.712  1.00 65.56  ? 1    THR B O   1 
ATOM   3690 C  CB  . THR B 1 1   ? 0.713   -24.065 99.864  1.00 81.46  ? 1    THR B CB  1 
ATOM   3691 O  OG1 . THR B 1 1   ? 0.456   -24.035 101.275 1.00 87.78  ? 1    THR B OG1 1 
ATOM   3692 C  CG2 . THR B 1 1   ? 1.261   -22.711 99.414  1.00 75.63  ? 1    THR B CG2 1 
ATOM   3693 N  N   . ILE B 1 2   ? 0.551   -26.055 97.755  1.00 68.67  ? 2    ILE B N   1 
ATOM   3694 C  CA  . ILE B 1 2   ? 0.952   -26.745 96.532  1.00 65.54  ? 2    ILE B CA  1 
ATOM   3695 C  C   . ILE B 1 2   ? -0.244  -27.559 96.038  1.00 68.95  ? 2    ILE B C   1 
ATOM   3696 O  O   . ILE B 1 2   ? -0.621  -28.561 96.651  1.00 72.37  ? 2    ILE B O   1 
ATOM   3697 C  CB  . ILE B 1 2   ? 2.173   -27.639 96.773  1.00 66.44  ? 2    ILE B CB  1 
ATOM   3698 C  CG1 . ILE B 1 2   ? 3.332   -26.819 97.360  1.00 68.58  ? 2    ILE B CG1 1 
ATOM   3699 C  CG2 . ILE B 1 2   ? 2.583   -28.348 95.485  1.00 64.76  ? 2    ILE B CG2 1 
ATOM   3700 C  CD1 . ILE B 1 2   ? 3.728   -25.606 96.535  1.00 66.79  ? 2    ILE B CD1 1 
ATOM   3701 N  N   . LYS B 1 3   ? -0.846  -27.125 94.932  1.00 62.76  ? 3    LYS B N   1 
ATOM   3702 C  CA  . LYS B 1 3   ? -2.008  -27.789 94.356  1.00 61.52  ? 3    LYS B CA  1 
ATOM   3703 C  C   . LYS B 1 3   ? -1.581  -28.812 93.309  1.00 59.82  ? 3    LYS B C   1 
ATOM   3704 O  O   . LYS B 1 3   ? -0.589  -28.629 92.597  1.00 59.28  ? 3    LYS B O   1 
ATOM   3705 C  CB  . LYS B 1 3   ? -2.950  -26.767 93.709  1.00 60.07  ? 3    LYS B CB  1 
ATOM   3706 C  CG  . LYS B 1 3   ? -3.291  -25.588 94.598  1.00 61.18  ? 3    LYS B CG  1 
ATOM   3707 C  CD  . LYS B 1 3   ? -4.784  -25.298 94.607  1.00 66.21  ? 3    LYS B CD  1 
ATOM   3708 C  CE  . LYS B 1 3   ? -5.317  -25.053 93.205  1.00 63.49  ? 3    LYS B CE  1 
ATOM   3709 N  NZ  . LYS B 1 3   ? -6.753  -24.650 93.246  1.00 65.64  ? 3    LYS B NZ  1 
ATOM   3710 N  N   . GLU B 1 4   ? -2.350  -29.891 93.213  1.00 58.55  ? 4    GLU B N   1 
ATOM   3711 C  CA  . GLU B 1 4   ? -2.160  -30.851 92.142  1.00 55.17  ? 4    GLU B CA  1 
ATOM   3712 C  C   . GLU B 1 4   ? -2.953  -30.404 90.921  1.00 49.19  ? 4    GLU B C   1 
ATOM   3713 O  O   . GLU B 1 4   ? -4.098  -29.963 91.027  1.00 52.22  ? 4    GLU B O   1 
ATOM   3714 C  CB  . GLU B 1 4   ? -2.584  -32.254 92.563  1.00 55.77  ? 4    GLU B CB  1 
ATOM   3715 C  CG  . GLU B 1 4   ? -2.181  -33.300 91.539  1.00 64.83  ? 4    GLU B CG  1 
ATOM   3716 C  CD  . GLU B 1 4   ? -2.578  -34.704 91.935  1.00 72.45  ? 4    GLU B CD  1 
ATOM   3717 O  OE1 . GLU B 1 4   ? -2.895  -35.505 91.026  1.00 72.89  ? 4    GLU B OE1 1 
ATOM   3718 O  OE2 . GLU B 1 4   ? -2.571  -35.004 93.149  1.00 76.34  ? 4    GLU B OE2 1 
ATOM   3719 N  N   . MET B 1 5   ? -2.332  -30.516 89.774  1.00 49.01  ? 5    MET B N   1 
ATOM   3720 C  CA  . MET B 1 5   ? -2.822  -29.988 88.519  1.00 45.89  ? 5    MET B CA  1 
ATOM   3721 C  C   . MET B 1 5   ? -3.718  -31.018 87.836  1.00 40.28  ? 5    MET B C   1 
ATOM   3722 O  O   . MET B 1 5   ? -3.353  -32.191 87.756  1.00 40.84  ? 5    MET B O   1 
ATOM   3723 C  CB  . MET B 1 5   ? -1.622  -29.660 87.640  1.00 48.93  ? 5    MET B CB  1 
ATOM   3724 C  CG  . MET B 1 5   ? -1.840  -28.874 86.420  1.00 46.87  ? 5    MET B CG  1 
ATOM   3725 S  SD  . MET B 1 5   ? -0.216  -28.903 85.634  1.00 41.50  ? 5    MET B SD  1 
ATOM   3726 C  CE  . MET B 1 5   ? 0.719   -27.880 86.784  1.00 41.69  ? 5    MET B CE  1 
ATOM   3727 N  N   . PRO B 1 6   ? -4.897  -30.666 87.328  1.00 36.33  ? 6    PRO B N   1 
ATOM   3728 C  CA  . PRO B 1 6   ? -5.713  -31.663 86.625  1.00 38.80  ? 6    PRO B CA  1 
ATOM   3729 C  C   . PRO B 1 6   ? -5.060  -32.089 85.316  1.00 39.66  ? 6    PRO B C   1 
ATOM   3730 O  O   . PRO B 1 6   ? -4.126  -31.463 84.816  1.00 36.51  ? 6    PRO B O   1 
ATOM   3731 C  CB  . PRO B 1 6   ? -7.036  -30.937 86.370  1.00 40.28  ? 6    PRO B CB  1 
ATOM   3732 C  CG  . PRO B 1 6   ? -6.674  -29.513 86.367  1.00 39.62  ? 6    PRO B CG  1 
ATOM   3733 C  CD  . PRO B 1 6   ? -5.588  -29.366 87.406  1.00 39.41  ? 6    PRO B CD  1 
ATOM   3734 N  N   . GLN B 1 7   ? -5.583  -33.180 84.755  1.00 37.44  ? 7    GLN B N   1 
ATOM   3735 C  CA  . GLN B 1 7   ? -5.048  -33.762 83.533  1.00 35.33  ? 7    GLN B CA  1 
ATOM   3736 C  C   . GLN B 1 7   ? -6.195  -34.385 82.756  1.00 38.00  ? 7    GLN B C   1 
ATOM   3737 O  O   . GLN B 1 7   ? -7.041  -35.066 83.359  1.00 38.75  ? 7    GLN B O   1 
ATOM   3738 C  CB  . GLN B 1 7   ? -3.978  -34.821 83.834  1.00 38.00  ? 7    GLN B CB  1 
ATOM   3739 C  CG  . GLN B 1 7   ? -3.323  -35.439 82.602  1.00 36.60  ? 7    GLN B CG  1 
ATOM   3740 C  CD  . GLN B 1 7   ? -2.270  -36.476 82.959  1.00 42.78  ? 7    GLN B CD  1 
ATOM   3741 O  OE1 . GLN B 1 7   ? -2.115  -36.845 84.125  1.00 45.96  ? 7    GLN B OE1 1 
ATOM   3742 N  NE2 . GLN B 1 7   ? -1.553  -36.963 81.951  1.00 38.90  ? 7    GLN B NE2 1 
ATOM   3743 N  N   . PRO B 1 8   ? -6.264  -34.169 81.448  1.00 36.50  ? 8    PRO B N   1 
ATOM   3744 C  CA  . PRO B 1 8   ? -7.335  -34.784 80.654  1.00 34.14  ? 8    PRO B CA  1 
ATOM   3745 C  C   . PRO B 1 8   ? -7.157  -36.287 80.504  1.00 33.69  ? 8    PRO B C   1 
ATOM   3746 O  O   . PRO B 1 8   ? -6.181  -36.863 80.986  1.00 35.02  ? 8    PRO B O   1 
ATOM   3747 C  CB  . PRO B 1 8   ? -7.232  -34.066 79.301  1.00 33.85  ? 8    PRO B CB  1 
ATOM   3748 C  CG  . PRO B 1 8   ? -5.771  -33.638 79.218  1.00 34.17  ? 8    PRO B CG  1 
ATOM   3749 C  CD  . PRO B 1 8   ? -5.407  -33.277 80.644  1.00 33.92  ? 8    PRO B CD  1 
ATOM   3750 N  N   . LYS B 1 9   ? -8.090  -36.932 79.817  1.00 32.24  ? 9    LYS B N   1 
ATOM   3751 C  CA  . LYS B 1 9   ? -8.144  -38.385 79.797  1.00 33.24  ? 9    LYS B CA  1 
ATOM   3752 C  C   . LYS B 1 9   ? -6.932  -38.981 79.087  1.00 35.83  ? 9    LYS B C   1 
ATOM   3753 O  O   . LYS B 1 9   ? -6.360  -38.387 78.164  1.00 34.79  ? 9    LYS B O   1 
ATOM   3754 C  CB  . LYS B 1 9   ? -9.437  -38.840 79.121  1.00 33.80  ? 9    LYS B CB  1 
ATOM   3755 C  CG  . LYS B 1 9   ? -9.523  -38.479 77.646  1.00 31.40  ? 9    LYS B CG  1 
ATOM   3756 C  CD  . LYS B 1 9   ? -10.945 -38.629 77.159  1.00 37.06  ? 9    LYS B CD  1 
ATOM   3757 C  CE  . LYS B 1 9   ? -11.086 -38.121 75.741  1.00 44.15  ? 9    LYS B CE  1 
ATOM   3758 N  NZ  . LYS B 1 9   ? -12.447 -38.407 75.219  1.00 47.02  ? 9    LYS B NZ  1 
ATOM   3759 N  N   . THR B 1 10  ? -6.556  -40.188 79.508  1.00 35.84  ? 10   THR B N   1 
ATOM   3760 C  CA  . THR B 1 10  ? -5.349  -40.848 79.038  1.00 32.99  ? 10   THR B CA  1 
ATOM   3761 C  C   . THR B 1 10  ? -5.677  -42.106 78.242  1.00 36.11  ? 10   THR B C   1 
ATOM   3762 O  O   . THR B 1 10  ? -6.778  -42.666 78.320  1.00 34.75  ? 10   THR B O   1 
ATOM   3763 C  CB  . THR B 1 10  ? -4.424  -41.210 80.206  1.00 37.36  ? 10   THR B CB  1 
ATOM   3764 O  OG1 . THR B 1 10  ? -5.139  -42.016 81.160  1.00 34.10  ? 10   THR B OG1 1 
ATOM   3765 C  CG2 . THR B 1 10  ? -3.925  -39.945 80.895  1.00 38.59  ? 10   THR B CG2 1 
ATOM   3766 N  N   . PHE B 1 11  ? -4.672  -42.547 77.487  1.00 32.36  ? 11   PHE B N   1 
ATOM   3767 C  CA  . PHE B 1 11  ? -4.769  -43.650 76.544  1.00 33.58  ? 11   PHE B CA  1 
ATOM   3768 C  C   . PHE B 1 11  ? -3.622  -44.645 76.800  1.00 37.57  ? 11   PHE B C   1 
ATOM   3769 O  O   . PHE B 1 11  ? -2.813  -44.935 75.920  1.00 36.34  ? 11   PHE B O   1 
ATOM   3770 C  CB  . PHE B 1 11  ? -4.714  -43.133 75.100  1.00 35.11  ? 11   PHE B CB  1 
ATOM   3771 C  CG  . PHE B 1 11  ? -5.869  -42.245 74.718  1.00 33.33  ? 11   PHE B CG  1 
ATOM   3772 C  CD1 . PHE B 1 11  ? -5.939  -40.932 75.176  1.00 33.35  ? 11   PHE B CD1 1 
ATOM   3773 C  CD2 . PHE B 1 11  ? -6.879  -42.722 73.887  1.00 32.90  ? 11   PHE B CD2 1 
ATOM   3774 C  CE1 . PHE B 1 11  ? -7.014  -40.109 74.824  1.00 35.41  ? 11   PHE B CE1 1 
ATOM   3775 C  CE2 . PHE B 1 11  ? -7.939  -41.903 73.518  1.00 34.57  ? 11   PHE B CE2 1 
ATOM   3776 C  CZ  . PHE B 1 11  ? -8.008  -40.594 73.989  1.00 35.46  ? 11   PHE B CZ  1 
ATOM   3777 N  N   . GLY B 1 12  ? -3.560  -45.177 78.020  1.00 36.75  ? 12   GLY B N   1 
ATOM   3778 C  CA  . GLY B 1 12  ? -2.500  -46.128 78.331  1.00 37.79  ? 12   GLY B CA  1 
ATOM   3779 C  C   . GLY B 1 12  ? -1.134  -45.499 78.136  1.00 41.51  ? 12   GLY B C   1 
ATOM   3780 O  O   . GLY B 1 12  ? -0.899  -44.339 78.490  1.00 35.97  ? 12   GLY B O   1 
ATOM   3781 N  N   . GLU B 1 13  ? -0.221  -46.260 77.530  1.00 40.84  ? 13   GLU B N   1 
ATOM   3782 C  CA  . GLU B 1 13  ? 1.138   -45.762 77.366  1.00 43.85  ? 13   GLU B CA  1 
ATOM   3783 C  C   . GLU B 1 13  ? 1.243   -44.594 76.387  1.00 43.01  ? 13   GLU B C   1 
ATOM   3784 O  O   . GLU B 1 13  ? 2.283   -43.931 76.370  1.00 42.90  ? 13   GLU B O   1 
ATOM   3785 C  CB  . GLU B 1 13  ? 2.059   -46.904 76.938  1.00 46.57  ? 13   GLU B CB  1 
ATOM   3786 C  CG  . GLU B 1 13  ? 2.079   -48.061 77.947  1.00 52.30  ? 13   GLU B CG  1 
ATOM   3787 C  CD  . GLU B 1 13  ? 2.846   -47.743 79.223  1.00 62.76  ? 13   GLU B CD  1 
ATOM   3788 O  OE1 . GLU B 1 13  ? 3.307   -46.589 79.398  1.00 66.18  ? 13   GLU B OE1 1 
ATOM   3789 O  OE2 . GLU B 1 13  ? 2.985   -48.659 80.065  1.00 69.89  ? 13   GLU B OE2 1 
ATOM   3790 N  N   . LEU B 1 14  ? 0.209   -44.310 75.583  1.00 38.74  ? 14   LEU B N   1 
ATOM   3791 C  CA  . LEU B 1 14  ? 0.260   -43.096 74.766  1.00 37.78  ? 14   LEU B CA  1 
ATOM   3792 C  C   . LEU B 1 14  ? -0.105  -41.835 75.555  1.00 38.95  ? 14   LEU B C   1 
ATOM   3793 O  O   . LEU B 1 14  ? -0.003  -40.724 75.012  1.00 39.05  ? 14   LEU B O   1 
ATOM   3794 C  CB  . LEU B 1 14  ? -0.644  -43.237 73.545  1.00 36.43  ? 14   LEU B CB  1 
ATOM   3795 C  CG  . LEU B 1 14  ? -0.326  -44.437 72.640  1.00 41.28  ? 14   LEU B CG  1 
ATOM   3796 C  CD1 . LEU B 1 14  ? -1.309  -44.522 71.495  1.00 42.32  ? 14   LEU B CD1 1 
ATOM   3797 C  CD2 . LEU B 1 14  ? 1.097   -44.353 72.125  1.00 45.53  ? 14   LEU B CD2 1 
ATOM   3798 N  N   . LYS B 1 15  ? -0.515  -41.987 76.811  1.00 38.24  ? 15   LYS B N   1 
ATOM   3799 C  CA  . LYS B 1 15  ? -0.805  -40.893 77.748  1.00 37.16  ? 15   LYS B CA  1 
ATOM   3800 C  C   . LYS B 1 15  ? -1.850  -39.989 77.096  1.00 35.70  ? 15   LYS B C   1 
ATOM   3801 O  O   . LYS B 1 15  ? -2.919  -40.493 76.708  1.00 35.60  ? 15   LYS B O   1 
ATOM   3802 C  CB  . LYS B 1 15  ? 0.502   -40.224 78.163  1.00 38.04  ? 15   LYS B CB  1 
ATOM   3803 C  CG  . LYS B 1 15  ? 1.434   -41.223 78.864  1.00 42.49  ? 15   LYS B CG  1 
ATOM   3804 C  CD  . LYS B 1 15  ? 2.732   -40.583 79.297  1.00 46.35  ? 15   LYS B CD  1 
ATOM   3805 C  CE  . LYS B 1 15  ? 3.566   -41.563 80.106  1.00 51.69  ? 15   LYS B CE  1 
ATOM   3806 N  NZ  . LYS B 1 15  ? 4.869   -40.962 80.482  1.00 58.02  ? 15   LYS B NZ  1 
ATOM   3807 N  N   . ASN B 1 16  ? -1.615  -38.681 76.968  1.00 35.23  ? 16   ASN B N   1 
ATOM   3808 C  CA  . ASN B 1 16  ? -2.618  -37.802 76.362  1.00 35.16  ? 16   ASN B CA  1 
ATOM   3809 C  C   . ASN B 1 16  ? -2.470  -37.636 74.856  1.00 37.26  ? 16   ASN B C   1 
ATOM   3810 O  O   . ASN B 1 16  ? -3.261  -36.898 74.262  1.00 35.88  ? 16   ASN B O   1 
ATOM   3811 C  CB  . ASN B 1 16  ? -2.574  -36.408 76.998  1.00 34.78  ? 16   ASN B CB  1 
ATOM   3812 C  CG  . ASN B 1 16  ? -2.903  -36.424 78.470  1.00 37.24  ? 16   ASN B CG  1 
ATOM   3813 O  OD1 . ASN B 1 16  ? -2.089  -36.030 79.300  1.00 36.61  ? 16   ASN B OD1 1 
ATOM   3814 N  ND2 . ASN B 1 16  ? -4.127  -36.864 78.806  1.00 35.39  ? 16   ASN B ND2 1 
ATOM   3815 N  N   . LEU B 1 17  ? -1.487  -38.281 74.225  1.00 33.73  ? 17   LEU B N   1 
ATOM   3816 C  CA  . LEU B 1 17  ? -1.184  -37.959 72.830  1.00 34.06  ? 17   LEU B CA  1 
ATOM   3817 C  C   . LEU B 1 17  ? -2.371  -38.124 71.890  1.00 37.44  ? 17   LEU B C   1 
ATOM   3818 O  O   . LEU B 1 17  ? -2.544  -37.272 71.001  1.00 36.91  ? 17   LEU B O   1 
ATOM   3819 C  CB  . LEU B 1 17  ? -0.004  -38.812 72.346  1.00 37.20  ? 17   LEU B CB  1 
ATOM   3820 C  CG  . LEU B 1 17  ? 0.580   -38.360 70.998  1.00 37.44  ? 17   LEU B CG  1 
ATOM   3821 C  CD1 . LEU B 1 17  ? 1.203   -36.975 71.095  1.00 40.25  ? 17   LEU B CD1 1 
ATOM   3822 C  CD2 . LEU B 1 17  ? 1.583   -39.387 70.476  1.00 42.82  ? 17   LEU B CD2 1 
ATOM   3823 N  N   . PRO B 1 18  ? -3.197  -39.164 71.996  1.00 36.05  ? 18   PRO B N   1 
ATOM   3824 C  CA  . PRO B 1 18  ? -4.308  -39.304 71.045  1.00 36.62  ? 18   PRO B CA  1 
ATOM   3825 C  C   . PRO B 1 18  ? -5.332  -38.179 71.108  1.00 33.73  ? 18   PRO B C   1 
ATOM   3826 O  O   . PRO B 1 18  ? -6.155  -38.085 70.192  1.00 33.60  ? 18   PRO B O   1 
ATOM   3827 C  CB  . PRO B 1 18  ? -4.928  -40.657 71.425  1.00 35.97  ? 18   PRO B CB  1 
ATOM   3828 C  CG  . PRO B 1 18  ? -3.760  -41.423 72.067  1.00 36.71  ? 18   PRO B CG  1 
ATOM   3829 C  CD  . PRO B 1 18  ? -3.057  -40.354 72.860  1.00 36.12  ? 18   PRO B CD  1 
ATOM   3830 N  N   . LEU B 1 19  ? -5.332  -37.347 72.150  1.00 33.59  ? 19   LEU B N   1 
ATOM   3831 C  CA  . LEU B 1 19  ? -6.209  -36.178 72.149  1.00 35.74  ? 19   LEU B CA  1 
ATOM   3832 C  C   . LEU B 1 19  ? -5.875  -35.220 71.015  1.00 36.01  ? 19   LEU B C   1 
ATOM   3833 O  O   . LEU B 1 19  ? -6.728  -34.418 70.624  1.00 36.15  ? 19   LEU B O   1 
ATOM   3834 C  CB  . LEU B 1 19  ? -6.124  -35.442 73.482  1.00 34.73  ? 19   LEU B CB  1 
ATOM   3835 C  CG  . LEU B 1 19  ? -6.628  -36.240 74.690  1.00 33.32  ? 19   LEU B CG  1 
ATOM   3836 C  CD1 . LEU B 1 19  ? -6.445  -35.438 75.943  1.00 34.95  ? 19   LEU B CD1 1 
ATOM   3837 C  CD2 . LEU B 1 19  ? -8.093  -36.611 74.504  1.00 37.29  ? 19   LEU B CD2 1 
ATOM   3838 N  N   . LEU B 1 20  ? -4.662  -35.299 70.475  1.00 35.30  ? 20   LEU B N   1 
ATOM   3839 C  CA  . LEU B 1 20  ? -4.259  -34.493 69.335  1.00 35.07  ? 20   LEU B CA  1 
ATOM   3840 C  C   . LEU B 1 20  ? -4.595  -35.149 68.005  1.00 35.96  ? 20   LEU B C   1 
ATOM   3841 O  O   . LEU B 1 20  ? -4.324  -34.557 66.962  1.00 36.79  ? 20   LEU B O   1 
ATOM   3842 C  CB  . LEU B 1 20  ? -2.749  -34.216 69.402  1.00 34.99  ? 20   LEU B CB  1 
ATOM   3843 C  CG  . LEU B 1 20  ? -2.282  -33.517 70.673  1.00 33.93  ? 20   LEU B CG  1 
ATOM   3844 C  CD1 . LEU B 1 20  ? -0.776  -33.297 70.600  1.00 36.13  ? 20   LEU B CD1 1 
ATOM   3845 C  CD2 . LEU B 1 20  ? -3.008  -32.204 70.849  1.00 36.53  ? 20   LEU B CD2 1 
ATOM   3846 N  N   . ASN B 1 21  ? -5.154  -36.362 68.012  1.00 33.60  ? 21   ASN B N   1 
ATOM   3847 C  CA  . ASN B 1 21  ? -5.505  -37.050 66.768  1.00 36.58  ? 21   ASN B CA  1 
ATOM   3848 C  C   . ASN B 1 21  ? -6.850  -36.513 66.283  1.00 39.30  ? 21   ASN B C   1 
ATOM   3849 O  O   . ASN B 1 21  ? -7.900  -37.156 66.383  1.00 37.29  ? 21   ASN B O   1 
ATOM   3850 C  CB  . ASN B 1 21  ? -5.544  -38.560 66.961  1.00 38.49  ? 21   ASN B CB  1 
ATOM   3851 C  CG  . ASN B 1 21  ? -5.727  -39.313 65.643  1.00 46.69  ? 21   ASN B CG  1 
ATOM   3852 O  OD1 . ASN B 1 21  ? -5.794  -38.705 64.567  1.00 46.34  ? 21   ASN B OD1 1 
ATOM   3853 N  ND2 . ASN B 1 21  ? -5.781  -40.639 65.719  1.00 48.72  ? 21   ASN B ND2 1 
ATOM   3854 N  N   . THR B 1 22  ? -6.794  -35.287 65.777  1.00 36.17  ? 22   THR B N   1 
ATOM   3855 C  CA  . THR B 1 22  ? -7.967  -34.568 65.302  1.00 34.04  ? 22   THR B CA  1 
ATOM   3856 C  C   . THR B 1 22  ? -7.490  -33.524 64.306  1.00 35.70  ? 22   THR B C   1 
ATOM   3857 O  O   . THR B 1 22  ? -6.342  -33.082 64.362  1.00 36.23  ? 22   THR B O   1 
ATOM   3858 C  CB  . THR B 1 22  ? -8.734  -33.910 66.450  1.00 38.18  ? 22   THR B CB  1 
ATOM   3859 O  OG1 . THR B 1 22  ? -9.710  -33.009 65.913  1.00 39.95  ? 22   THR B OG1 1 
ATOM   3860 C  CG2 . THR B 1 22  ? -7.783  -33.114 67.375  1.00 36.26  ? 22   THR B CG2 1 
ATOM   3861 N  N   . ASP B 1 23  ? -8.387  -33.131 63.388  1.00 38.58  ? 23   ASP B N   1 
ATOM   3862 C  CA  . ASP B 1 23  ? -8.040  -32.060 62.465  1.00 42.67  ? 23   ASP B CA  1 
ATOM   3863 C  C   . ASP B 1 23  ? -8.080  -30.698 63.141  1.00 34.41  ? 23   ASP B C   1 
ATOM   3864 O  O   . ASP B 1 23  ? -7.693  -29.707 62.513  1.00 33.87  ? 23   ASP B O   1 
ATOM   3865 C  CB  . ASP B 1 23  ? -8.993  -32.008 61.261  1.00 40.74  ? 23   ASP B CB  1 
ATOM   3866 C  CG  . ASP B 1 23  ? -10.459 -32.082 61.662  1.00 45.54  ? 23   ASP B CG  1 
ATOM   3867 O  OD1 . ASP B 1 23  ? -10.766 -32.449 62.810  1.00 52.97  ? 23   ASP B OD1 1 
ATOM   3868 O  OD2 . ASP B 1 23  ? -11.329 -31.762 60.820  1.00 57.90  ? 23   ASP B OD2 1 
ATOM   3869 N  N   . LYS B 1 24  ? -8.562  -30.628 64.383  1.00 34.43  ? 24   LYS B N   1 
ATOM   3870 C  CA  . LYS B 1 24  ? -8.782  -29.363 65.085  1.00 33.04  ? 24   LYS B CA  1 
ATOM   3871 C  C   . LYS B 1 24  ? -8.229  -29.457 66.502  1.00 31.99  ? 24   LYS B C   1 
ATOM   3872 O  O   . LYS B 1 24  ? -8.977  -29.392 67.487  1.00 33.96  ? 24   LYS B O   1 
ATOM   3873 C  CB  . LYS B 1 24  ? -10.269 -29.007 65.087  1.00 35.81  ? 24   LYS B CB  1 
ATOM   3874 C  CG  . LYS B 1 24  ? -10.807 -28.755 63.670  1.00 36.38  ? 24   LYS B CG  1 
ATOM   3875 C  CD  . LYS B 1 24  ? -12.295 -28.410 63.677  1.00 40.95  ? 24   LYS B CD  1 
ATOM   3876 C  CE  . LYS B 1 24  ? -12.766 -28.028 62.276  1.00 38.20  ? 24   LYS B CE  1 
ATOM   3877 N  NZ  . LYS B 1 24  ? -14.219 -27.685 62.268  1.00 38.05  ? 24   LYS B NZ  1 
ATOM   3878 N  N   . PRO B 1 25  ? -6.903  -29.594 66.636  1.00 31.83  ? 25   PRO B N   1 
ATOM   3879 C  CA  . PRO B 1 25  ? -6.323  -29.831 67.970  1.00 33.03  ? 25   PRO B CA  1 
ATOM   3880 C  C   . PRO B 1 25  ? -6.397  -28.631 68.899  1.00 31.69  ? 25   PRO B C   1 
ATOM   3881 O  O   . PRO B 1 25  ? -6.615  -28.806 70.105  1.00 30.06  ? 25   PRO B O   1 
ATOM   3882 C  CB  . PRO B 1 25  ? -4.872  -30.224 67.651  1.00 30.80  ? 25   PRO B CB  1 
ATOM   3883 C  CG  . PRO B 1 25  ? -4.608  -29.636 66.273  1.00 32.80  ? 25   PRO B CG  1 
ATOM   3884 C  CD  . PRO B 1 25  ? -5.913  -29.746 65.555  1.00 33.36  ? 25   PRO B CD  1 
ATOM   3885 N  N   . VAL B 1 26  ? -6.223  -27.411 68.386  1.00 32.06  ? 26   VAL B N   1 
ATOM   3886 C  CA  . VAL B 1 26  ? -6.318  -26.249 69.264  1.00 30.03  ? 26   VAL B CA  1 
ATOM   3887 C  C   . VAL B 1 26  ? -7.719  -26.140 69.827  1.00 30.79  ? 26   VAL B C   1 
ATOM   3888 O  O   . VAL B 1 26  ? -7.906  -25.910 71.021  1.00 33.09  ? 26   VAL B O   1 
ATOM   3889 C  CB  . VAL B 1 26  ? -5.919  -24.962 68.527  1.00 33.19  ? 26   VAL B CB  1 
ATOM   3890 C  CG1 . VAL B 1 26  ? -6.207  -23.749 69.435  1.00 31.43  ? 26   VAL B CG1 1 
ATOM   3891 C  CG2 . VAL B 1 26  ? -4.428  -25.028 68.113  1.00 31.75  ? 26   VAL B CG2 1 
ATOM   3892 N  N   . GLN B 1 27  ? -8.730  -26.299 68.966  1.00 31.40  ? 27   GLN B N   1 
ATOM   3893 C  CA  . GLN B 1 27  ? -10.108 -26.236 69.442  1.00 32.23  ? 27   GLN B CA  1 
ATOM   3894 C  C   . GLN B 1 27  ? -10.397 -27.349 70.443  1.00 33.65  ? 27   GLN B C   1 
ATOM   3895 O  O   . GLN B 1 27  ? -11.125 -27.137 71.421  1.00 31.84  ? 27   GLN B O   1 
ATOM   3896 C  CB  . GLN B 1 27  ? -11.064 -26.276 68.251  1.00 33.90  ? 27   GLN B CB  1 
ATOM   3897 C  CG  . GLN B 1 27  ? -11.020 -24.975 67.455  1.00 32.00  ? 27   GLN B CG  1 
ATOM   3898 C  CD  . GLN B 1 27  ? -11.608 -25.093 66.062  1.00 33.60  ? 27   GLN B CD  1 
ATOM   3899 O  OE1 . GLN B 1 27  ? -12.825 -24.911 65.861  1.00 34.71  ? 27   GLN B OE1 1 
ATOM   3900 N  NE2 . GLN B 1 27  ? -10.756 -25.372 65.089  1.00 33.47  ? 27   GLN B NE2 1 
ATOM   3901 N  N   . ALA B 1 28  ? -9.800  -28.532 70.247  1.00 34.32  ? 28   ALA B N   1 
ATOM   3902 C  CA  . ALA B 1 28  ? -9.943  -29.594 71.244  1.00 32.34  ? 28   ALA B CA  1 
ATOM   3903 C  C   . ALA B 1 28  ? -9.308  -29.190 72.561  1.00 36.46  ? 28   ALA B C   1 
ATOM   3904 O  O   . ALA B 1 28  ? -9.877  -29.419 73.635  1.00 33.64  ? 28   ALA B O   1 
ATOM   3905 C  CB  . ALA B 1 28  ? -9.312  -30.895 70.731  1.00 33.85  ? 28   ALA B CB  1 
ATOM   3906 N  N   . LEU B 1 29  ? -8.127  -28.573 72.497  1.00 33.24  ? 29   LEU B N   1 
ATOM   3907 C  CA  . LEU B 1 29  ? -7.469  -28.134 73.720  1.00 32.21  ? 29   LEU B CA  1 
ATOM   3908 C  C   . LEU B 1 29  ? -8.263  -27.034 74.417  1.00 36.72  ? 29   LEU B C   1 
ATOM   3909 O  O   . LEU B 1 29  ? -8.314  -26.998 75.654  1.00 34.95  ? 29   LEU B O   1 
ATOM   3910 C  CB  . LEU B 1 29  ? -6.042  -27.681 73.408  1.00 34.44  ? 29   LEU B CB  1 
ATOM   3911 C  CG  . LEU B 1 29  ? -5.105  -28.838 73.042  1.00 34.06  ? 29   LEU B CG  1 
ATOM   3912 C  CD1 . LEU B 1 29  ? -3.946  -28.327 72.196  1.00 31.27  ? 29   LEU B CD1 1 
ATOM   3913 C  CD2 . LEU B 1 29  ? -4.604  -29.526 74.313  1.00 35.45  ? 29   LEU B CD2 1 
ATOM   3914 N  N   . MET B 1 30  ? -8.897  -26.128 73.662  1.00 32.03  ? 30   MET B N   1 
ATOM   3915 C  CA  . MET B 1 30  ? -9.753  -25.162 74.345  1.00 33.42  ? 30   MET B CA  1 
ATOM   3916 C  C   . MET B 1 30  ? -10.910 -25.839 75.070  1.00 34.75  ? 30   MET B C   1 
ATOM   3917 O  O   . MET B 1 30  ? -11.245 -25.443 76.191  1.00 35.55  ? 30   MET B O   1 
ATOM   3918 C  CB  . MET B 1 30  ? -10.258 -24.018 73.441  1.00 37.86  ? 30   MET B CB  1 
ATOM   3919 C  CG  . MET B 1 30  ? -9.246  -23.364 72.485  1.00 32.41  ? 30   MET B CG  1 
ATOM   3920 S  SD  . MET B 1 30  ? -9.927  -22.437 71.105  1.00 34.43  ? 30   MET B SD  1 
ATOM   3921 C  CE  . MET B 1 30  ? -11.134 -21.397 71.965  1.00 36.85  ? 30   MET B CE  1 
ATOM   3922 N  N   . LYS B 1 31  ? -11.515 -26.869 74.472  1.00 33.51  ? 31   LYS B N   1 
ATOM   3923 C  CA  . LYS B 1 31  ? -12.595 -27.563 75.179  1.00 34.87  ? 31   LYS B CA  1 
ATOM   3924 C  C   . LYS B 1 31  ? -12.084 -28.224 76.458  1.00 36.91  ? 31   LYS B C   1 
ATOM   3925 O  O   . LYS B 1 31  ? -12.758 -28.196 77.492  1.00 35.15  ? 31   LYS B O   1 
ATOM   3926 C  CB  . LYS B 1 31  ? -13.251 -28.602 74.275  1.00 35.48  ? 31   LYS B CB  1 
ATOM   3927 C  CG  . LYS B 1 31  ? -14.544 -28.130 73.642  1.00 51.96  ? 31   LYS B CG  1 
ATOM   3928 C  CD  . LYS B 1 31  ? -14.557 -28.498 72.167  1.00 53.68  ? 31   LYS B CD  1 
ATOM   3929 C  CE  . LYS B 1 31  ? -15.701 -27.827 71.422  1.00 55.63  ? 31   LYS B CE  1 
ATOM   3930 N  NZ  . LYS B 1 31  ? -15.227 -27.437 70.060  1.00 56.97  ? 31   LYS B NZ  1 
ATOM   3931 N  N   . ILE B 1 32  ? -10.895 -28.829 76.409  1.00 34.03  ? 32   ILE B N   1 
ATOM   3932 C  CA  . ILE B 1 32  ? -10.301 -29.384 77.624  1.00 33.72  ? 32   ILE B CA  1 
ATOM   3933 C  C   . ILE B 1 32  ? -10.073 -28.284 78.655  1.00 32.69  ? 32   ILE B C   1 
ATOM   3934 O  O   . ILE B 1 32  ? -10.379 -28.456 79.843  1.00 34.79  ? 32   ILE B O   1 
ATOM   3935 C  CB  . ILE B 1 32  ? -8.995  -30.135 77.291  1.00 34.62  ? 32   ILE B CB  1 
ATOM   3936 C  CG1 . ILE B 1 32  ? -9.309  -31.367 76.434  1.00 34.90  ? 32   ILE B CG1 1 
ATOM   3937 C  CG2 . ILE B 1 32  ? -8.236  -30.523 78.579  1.00 30.72  ? 32   ILE B CG2 1 
ATOM   3938 C  CD1 . ILE B 1 32  ? -8.106  -31.948 75.700  1.00 34.43  ? 32   ILE B CD1 1 
ATOM   3939 N  N   . ALA B 1 33  ? -9.572  -27.124 78.216  1.00 33.89  ? 33   ALA B N   1 
ATOM   3940 C  CA  . ALA B 1 33  ? -9.360  -26.018 79.142  1.00 32.40  ? 33   ALA B CA  1 
ATOM   3941 C  C   . ALA B 1 33  ? -10.677 -25.565 79.758  1.00 34.94  ? 33   ALA B C   1 
ATOM   3942 O  O   . ALA B 1 33  ? -10.734 -25.221 80.944  1.00 35.71  ? 33   ALA B O   1 
ATOM   3943 C  CB  . ALA B 1 33  ? -8.672  -24.848 78.432  1.00 35.14  ? 33   ALA B CB  1 
ATOM   3944 N  N   . ASP B 1 34  ? -11.744 -25.549 78.965  1.00 35.50  ? 34   ASP B N   1 
ATOM   3945 C  CA  . ASP B 1 34  ? -13.037 -25.167 79.513  1.00 37.88  ? 34   ASP B CA  1 
ATOM   3946 C  C   . ASP B 1 34  ? -13.469 -26.129 80.601  1.00 39.09  ? 34   ASP B C   1 
ATOM   3947 O  O   . ASP B 1 34  ? -14.091 -25.717 81.588  1.00 42.21  ? 34   ASP B O   1 
ATOM   3948 C  CB  . ASP B 1 34  ? -14.094 -25.126 78.412  1.00 40.88  ? 34   ASP B CB  1 
ATOM   3949 C  CG  . ASP B 1 34  ? -14.087 -23.817 77.654  1.00 46.03  ? 34   ASP B CG  1 
ATOM   3950 O  OD1 . ASP B 1 34  ? -13.528 -22.820 78.173  1.00 51.48  ? 34   ASP B OD1 1 
ATOM   3951 O  OD2 . ASP B 1 34  ? -14.673 -23.776 76.554  1.00 45.35  ? 34   ASP B OD2 1 
ATOM   3952 N  N   . GLU B 1 35  ? -13.139 -27.407 80.446  1.00 33.10  ? 35   GLU B N   1 
ATOM   3953 C  CA  . GLU B 1 35  ? -13.537 -28.400 81.433  1.00 35.16  ? 35   GLU B CA  1 
ATOM   3954 C  C   . GLU B 1 35  ? -12.612 -28.400 82.648  1.00 38.71  ? 35   GLU B C   1 
ATOM   3955 O  O   . GLU B 1 35  ? -13.076 -28.571 83.782  1.00 36.95  ? 35   GLU B O   1 
ATOM   3956 C  CB  . GLU B 1 35  ? -13.593 -29.782 80.778  1.00 41.06  ? 35   GLU B CB  1 
ATOM   3957 C  CG  . GLU B 1 35  ? -13.626 -30.931 81.764  1.00 48.09  ? 35   GLU B CG  1 
ATOM   3958 C  CD  . GLU B 1 35  ? -13.650 -32.296 81.083  1.00 58.29  ? 35   GLU B CD  1 
ATOM   3959 O  OE1 . GLU B 1 35  ? -13.668 -32.359 79.830  1.00 54.46  ? 35   GLU B OE1 1 
ATOM   3960 O  OE2 . GLU B 1 35  ? -13.648 -33.308 81.818  1.00 64.17  ? 35   GLU B OE2 1 
ATOM   3961 N  N   . LEU B 1 36  ? -11.310 -28.191 82.445  1.00 34.12  ? 36   LEU B N   1 
ATOM   3962 C  CA  . LEU B 1 36  ? -10.361 -28.413 83.526  1.00 35.64  ? 36   LEU B CA  1 
ATOM   3963 C  C   . LEU B 1 36  ? -9.898  -27.144 84.223  1.00 32.90  ? 36   LEU B C   1 
ATOM   3964 O  O   . LEU B 1 36  ? -9.461  -27.226 85.377  1.00 36.54  ? 36   LEU B O   1 
ATOM   3965 C  CB  . LEU B 1 36  ? -9.129  -29.166 83.012  1.00 33.85  ? 36   LEU B CB  1 
ATOM   3966 C  CG  . LEU B 1 36  ? -9.380  -30.579 82.491  1.00 38.73  ? 36   LEU B CG  1 
ATOM   3967 C  CD1 . LEU B 1 36  ? -8.037  -31.266 82.181  1.00 34.34  ? 36   LEU B CD1 1 
ATOM   3968 C  CD2 . LEU B 1 36  ? -10.188 -31.383 83.493  1.00 38.25  ? 36   LEU B CD2 1 
ATOM   3969 N  N   . GLY B 1 37  ? -9.973  -25.994 83.572  1.00 32.76  ? 37   GLY B N   1 
ATOM   3970 C  CA  . GLY B 1 37  ? -9.658  -24.736 84.210  1.00 34.34  ? 37   GLY B CA  1 
ATOM   3971 C  C   . GLY B 1 37  ? -8.358  -24.123 83.720  1.00 35.62  ? 37   GLY B C   1 
ATOM   3972 O  O   . GLY B 1 37  ? -7.890  -24.367 82.602  1.00 35.47  ? 37   GLY B O   1 
ATOM   3973 N  N   . GLU B 1 38  ? -7.776  -23.296 84.582  1.00 33.90  ? 38   GLU B N   1 
ATOM   3974 C  CA  . GLU B 1 38  ? -6.715  -22.387 84.164  1.00 37.99  ? 38   GLU B CA  1 
ATOM   3975 C  C   . GLU B 1 38  ? -5.399  -23.091 83.875  1.00 37.13  ? 38   GLU B C   1 
ATOM   3976 O  O   . GLU B 1 38  ? -4.526  -22.489 83.238  1.00 33.47  ? 38   GLU B O   1 
ATOM   3977 C  CB  . GLU B 1 38  ? -6.503  -21.316 85.230  1.00 36.66  ? 38   GLU B CB  1 
ATOM   3978 C  CG  . GLU B 1 38  ? -5.926  -21.866 86.518  1.00 38.84  ? 38   GLU B CG  1 
ATOM   3979 C  CD  . GLU B 1 38  ? -5.707  -20.808 87.588  1.00 45.11  ? 38   GLU B CD  1 
ATOM   3980 O  OE1 . GLU B 1 38  ? -5.650  -19.595 87.264  1.00 38.34  ? 38   GLU B OE1 1 
ATOM   3981 O  OE2 . GLU B 1 38  ? -5.586  -21.211 88.769  1.00 41.04  ? 38   GLU B OE2 1 
ATOM   3982 N  N   . ILE B 1 39  ? -5.221  -24.328 84.333  1.00 35.49  ? 39   ILE B N   1 
ATOM   3983 C  CA  . ILE B 1 39  ? -3.977  -25.056 84.079  1.00 32.28  ? 39   ILE B CA  1 
ATOM   3984 C  C   . ILE B 1 39  ? -4.282  -26.546 84.028  1.00 36.47  ? 39   ILE B C   1 
ATOM   3985 O  O   . ILE B 1 39  ? -5.058  -27.062 84.840  1.00 34.46  ? 39   ILE B O   1 
ATOM   3986 C  CB  . ILE B 1 39  ? -2.906  -24.739 85.148  1.00 33.95  ? 39   ILE B CB  1 
ATOM   3987 C  CG1 . ILE B 1 39  ? -1.594  -25.452 84.818  1.00 36.76  ? 39   ILE B CG1 1 
ATOM   3988 C  CG2 . ILE B 1 39  ? -3.399  -25.105 86.575  1.00 36.78  ? 39   ILE B CG2 1 
ATOM   3989 C  CD1 . ILE B 1 39  ? -0.400  -24.926 85.639  1.00 38.86  ? 39   ILE B CD1 1 
ATOM   3990 N  N   . PHE B 1 40  ? -3.688  -27.242 83.058  1.00 32.88  ? 40   PHE B N   1 
ATOM   3991 C  CA  . PHE B 1 40  ? -3.738  -28.697 83.078  1.00 34.67  ? 40   PHE B CA  1 
ATOM   3992 C  C   . PHE B 1 40  ? -2.435  -29.258 82.538  1.00 35.51  ? 40   PHE B C   1 
ATOM   3993 O  O   . PHE B 1 40  ? -1.745  -28.627 81.731  1.00 34.25  ? 40   PHE B O   1 
ATOM   3994 C  CB  . PHE B 1 40  ? -4.960  -29.289 82.321  1.00 34.30  ? 40   PHE B CB  1 
ATOM   3995 C  CG  . PHE B 1 40  ? -5.040  -28.952 80.834  1.00 34.84  ? 40   PHE B CG  1 
ATOM   3996 C  CD1 . PHE B 1 40  ? -5.794  -27.861 80.396  1.00 33.04  ? 40   PHE B CD1 1 
ATOM   3997 C  CD2 . PHE B 1 40  ? -4.441  -29.765 79.879  1.00 32.79  ? 40   PHE B CD2 1 
ATOM   3998 C  CE1 . PHE B 1 40  ? -5.901  -27.548 79.046  1.00 35.07  ? 40   PHE B CE1 1 
ATOM   3999 C  CE2 . PHE B 1 40  ? -4.546  -29.474 78.524  1.00 32.01  ? 40   PHE B CE2 1 
ATOM   4000 C  CZ  . PHE B 1 40  ? -5.277  -28.371 78.094  1.00 34.74  ? 40   PHE B CZ  1 
ATOM   4001 N  N   . LYS B 1 41  ? -2.078  -30.422 83.065  1.00 35.07  ? 41   LYS B N   1 
ATOM   4002 C  CA  . LYS B 1 41  ? -0.923  -31.166 82.593  1.00 36.45  ? 41   LYS B CA  1 
ATOM   4003 C  C   . LYS B 1 41  ? -1.296  -31.962 81.355  1.00 38.17  ? 41   LYS B C   1 
ATOM   4004 O  O   . LYS B 1 41  ? -2.405  -32.496 81.250  1.00 37.35  ? 41   LYS B O   1 
ATOM   4005 C  CB  . LYS B 1 41  ? -0.421  -32.104 83.692  1.00 36.94  ? 41   LYS B CB  1 
ATOM   4006 C  CG  . LYS B 1 41  ? 0.736   -32.992 83.256  1.00 40.83  ? 41   LYS B CG  1 
ATOM   4007 C  CD  . LYS B 1 41  ? 1.521   -33.488 84.464  1.00 50.62  ? 41   LYS B CD  1 
ATOM   4008 C  CE  . LYS B 1 41  ? 1.486   -34.995 84.579  1.00 53.70  ? 41   LYS B CE  1 
ATOM   4009 N  NZ  . LYS B 1 41  ? 2.564   -35.510 85.489  1.00 55.62  ? 41   LYS B NZ  1 
ATOM   4010 N  N   . PHE B 1 42  ? -0.371  -32.021 80.402  1.00 33.62  ? 42   PHE B N   1 
ATOM   4011 C  CA  . PHE B 1 42  ? -0.550  -32.784 79.178  1.00 33.17  ? 42   PHE B CA  1 
ATOM   4012 C  C   . PHE B 1 42  ? 0.719   -33.589 78.944  1.00 36.77  ? 42   PHE B C   1 
ATOM   4013 O  O   . PHE B 1 42  ? 1.809   -33.016 78.858  1.00 35.48  ? 42   PHE B O   1 
ATOM   4014 C  CB  . PHE B 1 42  ? -0.846  -31.853 77.997  1.00 32.86  ? 42   PHE B CB  1 
ATOM   4015 C  CG  . PHE B 1 42  ? -1.238  -32.573 76.733  1.00 34.94  ? 42   PHE B CG  1 
ATOM   4016 C  CD1 . PHE B 1 42  ? -0.272  -33.143 75.918  1.00 37.72  ? 42   PHE B CD1 1 
ATOM   4017 C  CD2 . PHE B 1 42  ? -2.572  -32.690 76.363  1.00 36.78  ? 42   PHE B CD2 1 
ATOM   4018 C  CE1 . PHE B 1 42  ? -0.626  -33.819 74.759  1.00 39.96  ? 42   PHE B CE1 1 
ATOM   4019 C  CE2 . PHE B 1 42  ? -2.930  -33.352 75.191  1.00 35.34  ? 42   PHE B CE2 1 
ATOM   4020 C  CZ  . PHE B 1 42  ? -1.955  -33.915 74.394  1.00 37.70  ? 42   PHE B CZ  1 
ATOM   4021 N  N   . GLU B 1 43  ? 0.575   -34.905 78.821  1.00 35.21  ? 43   GLU B N   1 
ATOM   4022 C  CA  . GLU B 1 43  ? 1.712   -35.818 78.712  1.00 39.07  ? 43   GLU B CA  1 
ATOM   4023 C  C   . GLU B 1 43  ? 1.657   -36.591 77.406  1.00 38.81  ? 43   GLU B C   1 
ATOM   4024 O  O   . GLU B 1 43  ? 0.587   -37.012 76.967  1.00 38.43  ? 43   GLU B O   1 
ATOM   4025 C  CB  . GLU B 1 43  ? 1.737   -36.833 79.856  1.00 36.92  ? 43   GLU B CB  1 
ATOM   4026 C  CG  . GLU B 1 43  ? 2.057   -36.262 81.212  1.00 42.31  ? 43   GLU B CG  1 
ATOM   4027 C  CD  . GLU B 1 43  ? 2.153   -37.355 82.257  1.00 49.94  ? 43   GLU B CD  1 
ATOM   4028 O  OE1 . GLU B 1 43  ? 1.196   -38.144 82.372  1.00 50.28  ? 43   GLU B OE1 1 
ATOM   4029 O  OE2 . GLU B 1 43  ? 3.179   -37.435 82.952  1.00 55.11  ? 43   GLU B OE2 1 
ATOM   4030 N  N   . ALA B 1 44  ? 2.817   -36.797 76.803  1.00 39.14  ? 44   ALA B N   1 
ATOM   4031 C  CA  . ALA B 1 44  ? 3.005   -37.709 75.690  1.00 36.43  ? 44   ALA B CA  1 
ATOM   4032 C  C   . ALA B 1 44  ? 4.196   -38.584 76.035  1.00 34.36  ? 44   ALA B C   1 
ATOM   4033 O  O   . ALA B 1 44  ? 4.943   -38.273 76.967  1.00 36.59  ? 44   ALA B O   1 
ATOM   4034 C  CB  . ALA B 1 44  ? 3.254   -36.954 74.378  1.00 37.38  ? 44   ALA B CB  1 
ATOM   4035 N  N   . PRO B 1 45  ? 4.384   -39.704 75.344  1.00 36.25  ? 45   PRO B N   1 
ATOM   4036 C  CA  . PRO B 1 45  ? 5.564   -40.522 75.655  1.00 38.74  ? 45   PRO B CA  1 
ATOM   4037 C  C   . PRO B 1 45  ? 6.805   -39.656 75.586  1.00 40.60  ? 45   PRO B C   1 
ATOM   4038 O  O   . PRO B 1 45  ? 7.082   -39.048 74.548  1.00 44.92  ? 45   PRO B O   1 
ATOM   4039 C  CB  . PRO B 1 45  ? 5.548   -41.608 74.571  1.00 38.73  ? 45   PRO B CB  1 
ATOM   4040 C  CG  . PRO B 1 45  ? 4.085   -41.732 74.202  1.00 39.74  ? 45   PRO B CG  1 
ATOM   4041 C  CD  . PRO B 1 45  ? 3.550   -40.314 74.292  1.00 38.64  ? 45   PRO B CD  1 
ATOM   4042 N  N   . GLY B 1 46  ? 7.523   -39.558 76.701  1.00 45.05  ? 46   GLY B N   1 
ATOM   4043 C  CA  . GLY B 1 46  ? 8.750   -38.791 76.771  1.00 47.15  ? 46   GLY B CA  1 
ATOM   4044 C  C   . GLY B 1 46  ? 8.606   -37.286 76.841  1.00 46.62  ? 46   GLY B C   1 
ATOM   4045 O  O   . GLY B 1 46  ? 9.600   -36.584 76.637  1.00 46.63  ? 46   GLY B O   1 
ATOM   4046 N  N   . ARG B 1 47  ? 7.417   -36.753 77.114  1.00 40.91  ? 47   ARG B N   1 
ATOM   4047 C  CA  . ARG B 1 47  ? 7.313   -35.304 77.200  1.00 41.02  ? 47   ARG B CA  1 
ATOM   4048 C  C   . ARG B 1 47  ? 6.131   -34.911 78.073  1.00 41.68  ? 47   ARG B C   1 
ATOM   4049 O  O   . ARG B 1 47  ? 5.108   -35.599 78.114  1.00 38.53  ? 47   ARG B O   1 
ATOM   4050 C  CB  . ARG B 1 47  ? 7.193   -34.662 75.810  1.00 43.32  ? 47   ARG B CB  1 
ATOM   4051 C  CG  . ARG B 1 47  ? 6.461   -33.326 75.826  1.00 49.84  ? 47   ARG B CG  1 
ATOM   4052 C  CD  . ARG B 1 47  ? 6.593   -32.559 74.515  1.00 49.29  ? 47   ARG B CD  1 
ATOM   4053 N  NE  . ARG B 1 47  ? 6.232   -31.148 74.644  1.00 45.87  ? 47   ARG B NE  1 
ATOM   4054 C  CZ  . ARG B 1 47  ? 5.622   -30.468 73.680  1.00 45.61  ? 47   ARG B CZ  1 
ATOM   4055 N  NH1 . ARG B 1 47  ? 5.351   -31.030 72.512  1.00 45.94  ? 47   ARG B NH1 1 
ATOM   4056 N  NH2 . ARG B 1 47  ? 5.236   -29.211 73.904  1.00 35.12  ? 47   ARG B NH2 1 
ATOM   4057 N  N   . VAL B 1 48  ? 6.283   -33.781 78.755  1.00 42.15  ? 48   VAL B N   1 
ATOM   4058 C  CA  . VAL B 1 48  ? 5.206   -33.189 79.536  1.00 35.07  ? 48   VAL B CA  1 
ATOM   4059 C  C   . VAL B 1 48  ? 5.197   -31.690 79.277  1.00 38.41  ? 48   VAL B C   1 
ATOM   4060 O  O   . VAL B 1 48  ? 6.253   -31.060 79.138  1.00 39.63  ? 48   VAL B O   1 
ATOM   4061 C  CB  . VAL B 1 48  ? 5.357   -33.494 81.041  1.00 44.03  ? 48   VAL B CB  1 
ATOM   4062 C  CG1 . VAL B 1 48  ? 6.693   -33.009 81.544  1.00 45.10  ? 48   VAL B CG1 1 
ATOM   4063 C  CG2 . VAL B 1 48  ? 4.225   -32.857 81.832  1.00 42.82  ? 48   VAL B CG2 1 
ATOM   4064 N  N   . THR B 1 49  ? 4.001   -31.119 79.191  1.00 33.77  ? 49   THR B N   1 
ATOM   4065 C  CA  . THR B 1 49  ? 3.853   -29.671 79.184  1.00 34.19  ? 49   THR B CA  1 
ATOM   4066 C  C   . THR B 1 49  ? 2.614   -29.317 79.998  1.00 35.97  ? 49   THR B C   1 
ATOM   4067 O  O   . THR B 1 49  ? 1.872   -30.194 80.451  1.00 35.34  ? 49   THR B O   1 
ATOM   4068 C  CB  . THR B 1 49  ? 3.801   -29.125 77.745  1.00 34.13  ? 49   THR B CB  1 
ATOM   4069 O  OG1 . THR B 1 49  ? 3.920   -27.694 77.758  1.00 33.02  ? 49   THR B OG1 1 
ATOM   4070 C  CG2 . THR B 1 49  ? 2.473   -29.520 77.063  1.00 35.40  ? 49   THR B CG2 1 
ATOM   4071 N  N   . ARG B 1 50  ? 2.430   -28.023 80.239  1.00 33.82  ? 50   ARG B N   1 
ATOM   4072 C  CA  . ARG B 1 50  ? 1.309   -27.518 81.033  1.00 34.71  ? 50   ARG B CA  1 
ATOM   4073 C  C   . ARG B 1 50  ? 0.621   -26.412 80.246  1.00 34.97  ? 50   ARG B C   1 
ATOM   4074 O  O   . ARG B 1 50  ? 1.262   -25.427 79.871  1.00 33.98  ? 50   ARG B O   1 
ATOM   4075 C  CB  . ARG B 1 50  ? 1.796   -27.004 82.386  1.00 36.70  ? 50   ARG B CB  1 
ATOM   4076 C  CG  . ARG B 1 50  ? 2.529   -28.060 83.183  1.00 36.45  ? 50   ARG B CG  1 
ATOM   4077 C  CD  . ARG B 1 50  ? 3.835   -27.510 83.711  1.00 40.08  ? 50   ARG B CD  1 
ATOM   4078 N  NE  . ARG B 1 50  ? 4.632   -28.574 84.301  1.00 44.83  ? 50   ARG B NE  1 
ATOM   4079 C  CZ  . ARG B 1 50  ? 5.621   -29.205 83.684  1.00 44.58  ? 50   ARG B CZ  1 
ATOM   4080 N  NH1 . ARG B 1 50  ? 6.026   -28.847 82.466  1.00 38.74  ? 50   ARG B NH1 1 
ATOM   4081 N  NH2 . ARG B 1 50  ? 6.216   -30.226 84.298  1.00 39.65  ? 50   ARG B NH2 1 
ATOM   4082 N  N   . TYR B 1 51  ? -0.675  -26.573 79.995  1.00 31.36  ? 51   TYR B N   1 
ATOM   4083 C  CA  . TYR B 1 51  ? -1.451  -25.591 79.237  1.00 32.61  ? 51   TYR B CA  1 
ATOM   4084 C  C   . TYR B 1 51  ? -2.068  -24.565 80.174  1.00 31.95  ? 51   TYR B C   1 
ATOM   4085 O  O   . TYR B 1 51  ? -2.785  -24.929 81.113  1.00 33.89  ? 51   TYR B O   1 
ATOM   4086 C  CB  . TYR B 1 51  ? -2.561  -26.266 78.433  1.00 31.91  ? 51   TYR B CB  1 
ATOM   4087 C  CG  . TYR B 1 51  ? -2.035  -26.972 77.195  1.00 31.60  ? 51   TYR B CG  1 
ATOM   4088 C  CD1 . TYR B 1 51  ? -1.514  -28.254 77.285  1.00 32.46  ? 51   TYR B CD1 1 
ATOM   4089 C  CD2 . TYR B 1 51  ? -2.016  -26.333 75.953  1.00 32.99  ? 51   TYR B CD2 1 
ATOM   4090 C  CE1 . TYR B 1 51  ? -1.002  -28.901 76.168  1.00 33.76  ? 51   TYR B CE1 1 
ATOM   4091 C  CE2 . TYR B 1 51  ? -1.498  -26.968 74.832  1.00 33.84  ? 51   TYR B CE2 1 
ATOM   4092 C  CZ  . TYR B 1 51  ? -1.002  -28.257 74.947  1.00 33.10  ? 51   TYR B CZ  1 
ATOM   4093 O  OH  . TYR B 1 51  ? -0.491  -28.901 73.840  1.00 32.33  ? 51   TYR B OH  1 
ATOM   4094 N  N   . LEU B 1 52  ? -1.809  -23.289 79.903  1.00 31.69  ? 52   LEU B N   1 
ATOM   4095 C  CA  . LEU B 1 52  ? -2.258  -22.190 80.743  1.00 31.92  ? 52   LEU B CA  1 
ATOM   4096 C  C   . LEU B 1 52  ? -3.352  -21.401 80.040  1.00 34.07  ? 52   LEU B C   1 
ATOM   4097 O  O   . LEU B 1 52  ? -3.243  -21.098 78.848  1.00 32.55  ? 52   LEU B O   1 
ATOM   4098 C  CB  . LEU B 1 52  ? -1.105  -21.243 81.084  1.00 32.67  ? 52   LEU B CB  1 
ATOM   4099 C  CG  . LEU B 1 52  ? 0.147   -21.848 81.716  1.00 34.06  ? 52   LEU B CG  1 
ATOM   4100 C  CD1 . LEU B 1 52  ? 1.096   -20.713 82.089  1.00 38.08  ? 52   LEU B CD1 1 
ATOM   4101 C  CD2 . LEU B 1 52  ? -0.209  -22.663 82.933  1.00 37.33  ? 52   LEU B CD2 1 
ATOM   4102 N  N   . SER B 1 53  ? -4.387  -21.027 80.793  1.00 34.23  ? 53   SER B N   1 
ATOM   4103 C  CA  . SER B 1 53  ? -5.543  -20.361 80.219  1.00 33.19  ? 53   SER B CA  1 
ATOM   4104 C  C   . SER B 1 53  ? -5.993  -19.101 80.953  1.00 33.86  ? 53   SER B C   1 
ATOM   4105 O  O   . SER B 1 53  ? -6.829  -18.383 80.400  1.00 34.81  ? 53   SER B O   1 
ATOM   4106 C  CB  . SER B 1 53  ? -6.740  -21.329 80.146  1.00 35.05  ? 53   SER B CB  1 
ATOM   4107 O  OG  . SER B 1 53  ? -6.503  -22.346 79.201  1.00 37.59  ? 53   SER B OG  1 
ATOM   4108 N  N   . SER B 1 54  ? -5.497  -18.808 82.165  1.00 31.93  ? 54   SER B N   1 
ATOM   4109 C  CA  . SER B 1 54  ? -5.928  -17.622 82.913  1.00 30.78  ? 54   SER B CA  1 
ATOM   4110 C  C   . SER B 1 54  ? -4.898  -16.501 82.817  1.00 32.88  ? 54   SER B C   1 
ATOM   4111 O  O   . SER B 1 54  ? -3.694  -16.741 82.708  1.00 35.28  ? 54   SER B O   1 
ATOM   4112 C  CB  . SER B 1 54  ? -6.175  -17.944 84.395  1.00 32.58  ? 54   SER B CB  1 
ATOM   4113 O  OG  . SER B 1 54  ? -4.949  -18.290 85.009  1.00 34.41  ? 54   SER B OG  1 
ATOM   4114 N  N   . GLN B 1 55  ? -5.388  -15.263 82.855  1.00 34.68  ? 55   GLN B N   1 
ATOM   4115 C  CA  . GLN B 1 55  ? -4.480  -14.124 82.915  1.00 35.39  ? 55   GLN B CA  1 
ATOM   4116 C  C   . GLN B 1 55  ? -3.608  -14.190 84.163  1.00 34.76  ? 55   GLN B C   1 
ATOM   4117 O  O   . GLN B 1 55  ? -2.436  -13.799 84.128  1.00 34.65  ? 55   GLN B O   1 
ATOM   4118 C  CB  . GLN B 1 55  ? -5.292  -12.833 82.867  1.00 35.36  ? 55   GLN B CB  1 
ATOM   4119 C  CG  . GLN B 1 55  ? -4.479  -11.560 82.700  1.00 37.04  ? 55   GLN B CG  1 
ATOM   4120 C  CD  . GLN B 1 55  ? -4.046  -10.986 84.040  1.00 38.77  ? 55   GLN B CD  1 
ATOM   4121 O  OE1 . GLN B 1 55  ? -4.446  -11.482 85.099  1.00 37.51  ? 55   GLN B OE1 1 
ATOM   4122 N  NE2 . GLN B 1 55  ? -3.239  -9.928  84.002  1.00 41.85  ? 55   GLN B NE2 1 
ATOM   4123 N  N   . ARG B 1 56  ? -4.152  -14.727 85.256  1.00 35.17  ? 56   ARG B N   1 
ATOM   4124 C  CA  . ARG B 1 56  ? -3.409  -14.841 86.510  1.00 34.15  ? 56   ARG B CA  1 
ATOM   4125 C  C   . ARG B 1 56  ? -2.096  -15.585 86.318  1.00 37.86  ? 56   ARG B C   1 
ATOM   4126 O  O   . ARG B 1 56  ? -1.038  -15.124 86.757  1.00 38.63  ? 56   ARG B O   1 
ATOM   4127 C  CB  . ARG B 1 56  ? -4.270  -15.563 87.556  1.00 37.34  ? 56   ARG B CB  1 
ATOM   4128 C  CG  . ARG B 1 56  ? -3.547  -15.853 88.868  1.00 45.45  ? 56   ARG B CG  1 
ATOM   4129 C  CD  . ARG B 1 56  ? -4.450  -16.600 89.859  1.00 44.79  ? 56   ARG B CD  1 
ATOM   4130 N  NE  . ARG B 1 56  ? -4.330  -18.053 89.762  1.00 45.71  ? 56   ARG B NE  1 
ATOM   4131 C  CZ  . ARG B 1 56  ? -3.552  -18.796 90.541  1.00 46.27  ? 56   ARG B CZ  1 
ATOM   4132 N  NH1 . ARG B 1 56  ? -2.776  -18.249 91.462  1.00 44.38  ? 56   ARG B NH1 1 
ATOM   4133 N  NH2 . ARG B 1 56  ? -3.566  -20.122 90.404  1.00 44.48  ? 56   ARG B NH2 1 
ATOM   4134 N  N   . LEU B 1 57  ? -2.157  -16.762 85.689  1.00 35.27  ? 57   LEU B N   1 
ATOM   4135 C  CA  . LEU B 1 57  ? -0.952  -17.549 85.473  1.00 32.20  ? 57   LEU B CA  1 
ATOM   4136 C  C   . LEU B 1 57  ? -0.161  -17.065 84.270  1.00 35.65  ? 57   LEU B C   1 
ATOM   4137 O  O   . LEU B 1 57  ? 1.074   -17.122 84.282  1.00 32.65  ? 57   LEU B O   1 
ATOM   4138 C  CB  . LEU B 1 57  ? -1.309  -19.018 85.298  1.00 33.92  ? 57   LEU B CB  1 
ATOM   4139 C  CG  . LEU B 1 57  ? -2.001  -19.646 86.515  1.00 34.01  ? 57   LEU B CG  1 
ATOM   4140 C  CD1 . LEU B 1 57  ? -2.271  -21.116 86.250  1.00 35.44  ? 57   LEU B CD1 1 
ATOM   4141 C  CD2 . LEU B 1 57  ? -1.151  -19.446 87.775  1.00 39.62  ? 57   LEU B CD2 1 
ATOM   4142 N  N   . ILE B 1 58  ? -0.839  -16.600 83.221  1.00 32.67  ? 58   ILE B N   1 
ATOM   4143 C  CA  . ILE B 1 58  ? -0.104  -16.234 82.010  1.00 33.31  ? 58   ILE B CA  1 
ATOM   4144 C  C   . ILE B 1 58  ? 0.713   -14.966 82.233  1.00 33.70  ? 58   ILE B C   1 
ATOM   4145 O  O   . ILE B 1 58  ? 1.801   -14.812 81.662  1.00 35.92  ? 58   ILE B O   1 
ATOM   4146 C  CB  . ILE B 1 58  ? -1.090  -16.130 80.826  1.00 32.66  ? 58   ILE B CB  1 
ATOM   4147 C  CG1 . ILE B 1 58  ? -1.515  -17.540 80.390  1.00 33.15  ? 58   ILE B CG1 1 
ATOM   4148 C  CG2 . ILE B 1 58  ? -0.476  -15.376 79.628  1.00 31.93  ? 58   ILE B CG2 1 
ATOM   4149 C  CD1 . ILE B 1 58  ? -2.779  -17.585 79.502  1.00 30.52  ? 58   ILE B CD1 1 
ATOM   4150 N  N   . LYS B 1 59  ? 0.255   -14.065 83.101  1.00 32.70  ? 59   LYS B N   1 
ATOM   4151 C  CA  . LYS B 1 59  ? 1.062   -12.879 83.369  1.00 35.72  ? 59   LYS B CA  1 
ATOM   4152 C  C   . LYS B 1 59  ? 2.391   -13.256 84.012  1.00 36.01  ? 59   LYS B C   1 
ATOM   4153 O  O   . LYS B 1 59  ? 3.410   -12.598 83.768  1.00 36.21  ? 59   LYS B O   1 
ATOM   4154 C  CB  . LYS B 1 59  ? 0.299   -11.896 84.262  1.00 36.58  ? 59   LYS B CB  1 
ATOM   4155 C  CG  . LYS B 1 59  ? 0.128   -12.337 85.691  1.00 42.64  ? 59   LYS B CG  1 
ATOM   4156 C  CD  . LYS B 1 59  ? -0.568  -11.253 86.495  1.00 43.77  ? 59   LYS B CD  1 
ATOM   4157 C  CE  . LYS B 1 59  ? -0.718  -11.658 87.950  1.00 46.94  ? 59   LYS B CE  1 
ATOM   4158 N  NZ  . LYS B 1 59  ? -1.531  -10.645 88.685  1.00 53.27  ? 59   LYS B NZ  1 
ATOM   4159 N  N   . GLU B 1 60  ? 2.405   -14.308 84.833  1.00 34.79  ? 60   GLU B N   1 
ATOM   4160 C  CA  . GLU B 1 60  ? 3.671   -14.791 85.383  1.00 37.22  ? 60   GLU B CA  1 
ATOM   4161 C  C   . GLU B 1 60  ? 4.508   -15.477 84.319  1.00 38.09  ? 60   GLU B C   1 
ATOM   4162 O  O   . GLU B 1 60  ? 5.736   -15.315 84.281  1.00 37.74  ? 60   GLU B O   1 
ATOM   4163 C  CB  . GLU B 1 60  ? 3.421   -15.744 86.554  1.00 35.40  ? 60   GLU B CB  1 
ATOM   4164 C  CG  . GLU B 1 60  ? 2.922   -15.048 87.809  1.00 39.13  ? 60   GLU B CG  1 
ATOM   4165 C  CD  . GLU B 1 60  ? 2.839   -15.988 89.003  1.00 45.53  ? 60   GLU B CD  1 
ATOM   4166 O  OE1 . GLU B 1 60  ? 3.699   -16.887 89.144  1.00 40.09  ? 60   GLU B OE1 1 
ATOM   4167 O  OE2 . GLU B 1 60  ? 1.916   -15.802 89.817  1.00 43.38  ? 60   GLU B OE2 1 
ATOM   4168 N  N   . ALA B 1 61  ? 3.870   -16.261 83.451  1.00 33.98  ? 61   ALA B N   1 
ATOM   4169 C  CA  . ALA B 1 61  ? 4.619   -16.907 82.385  1.00 35.58  ? 61   ALA B CA  1 
ATOM   4170 C  C   . ALA B 1 61  ? 5.289   -15.885 81.480  1.00 33.73  ? 61   ALA B C   1 
ATOM   4171 O  O   . ALA B 1 61  ? 6.307   -16.198 80.849  1.00 35.89  ? 61   ALA B O   1 
ATOM   4172 C  CB  . ALA B 1 61  ? 3.699   -17.807 81.558  1.00 36.96  ? 61   ALA B CB  1 
ATOM   4173 N  N   . CYS B 1 62  ? 4.731   -14.672 81.396  1.00 35.47  ? 62   CYS B N   1 
ATOM   4174 C  CA  . CYS B 1 62  ? 5.245   -13.606 80.541  1.00 34.44  ? 62   CYS B CA  1 
ATOM   4175 C  C   . CYS B 1 62  ? 6.338   -12.788 81.216  1.00 35.25  ? 62   CYS B C   1 
ATOM   4176 O  O   . CYS B 1 62  ? 6.799   -11.794 80.646  1.00 36.13  ? 62   CYS B O   1 
ATOM   4177 C  CB  . CYS B 1 62  ? 4.111   -12.685 80.096  1.00 35.26  ? 62   CYS B CB  1 
ATOM   4178 S  SG  . CYS B 1 62  ? 3.018   -13.446 78.864  1.00 36.64  ? 62   CYS B SG  1 
ATOM   4179 N  N   . ASP B 1 63  ? 6.761   -13.191 82.408  1.00 33.80  ? 63   ASP B N   1 
ATOM   4180 C  CA  . ASP B 1 63  ? 7.889   -12.569 83.089  1.00 36.45  ? 63   ASP B CA  1 
ATOM   4181 C  C   . ASP B 1 63  ? 9.166   -13.115 82.471  1.00 33.57  ? 63   ASP B C   1 
ATOM   4182 O  O   . ASP B 1 63  ? 9.513   -14.279 82.689  1.00 35.44  ? 63   ASP B O   1 
ATOM   4183 C  CB  . ASP B 1 63  ? 7.800   -12.873 84.583  1.00 37.99  ? 63   ASP B CB  1 
ATOM   4184 C  CG  . ASP B 1 63  ? 8.906   -12.232 85.396  1.00 39.64  ? 63   ASP B CG  1 
ATOM   4185 O  OD1 . ASP B 1 63  ? 9.936   -11.782 84.836  1.00 37.02  ? 63   ASP B OD1 1 
ATOM   4186 O  OD2 . ASP B 1 63  ? 8.731   -12.220 86.632  1.00 41.40  ? 63   ASP B OD2 1 
ATOM   4187 N  N   . GLU B 1 64  ? 9.849   -12.284 81.677  1.00 33.35  ? 64   GLU B N   1 
ATOM   4188 C  CA  . GLU B 1 64  ? 11.033  -12.721 80.946  1.00 36.12  ? 64   GLU B CA  1 
ATOM   4189 C  C   . GLU B 1 64  ? 12.219  -13.007 81.857  1.00 37.29  ? 64   GLU B C   1 
ATOM   4190 O  O   . GLU B 1 64  ? 13.173  -13.658 81.413  1.00 36.95  ? 64   GLU B O   1 
ATOM   4191 C  CB  . GLU B 1 64  ? 11.429  -11.669 79.909  1.00 37.81  ? 64   GLU B CB  1 
ATOM   4192 C  CG  . GLU B 1 64  ? 10.387  -11.464 78.820  1.00 35.70  ? 64   GLU B CG  1 
ATOM   4193 C  CD  . GLU B 1 64  ? 10.772  -10.366 77.844  1.00 41.00  ? 64   GLU B CD  1 
ATOM   4194 O  OE1 . GLU B 1 64  ? 10.623  -9.176  78.179  1.00 47.16  ? 64   GLU B OE1 1 
ATOM   4195 O  OE2 . GLU B 1 64  ? 11.210  -10.696 76.732  1.00 36.00  ? 64   GLU B OE2 1 
ATOM   4196 N  N   . SER B 1 65  ? 12.195  -12.526 83.108  1.00 36.13  ? 65   SER B N   1 
ATOM   4197 C  CA  . SER B 1 65  ? 13.250  -12.916 84.034  1.00 38.00  ? 65   SER B CA  1 
ATOM   4198 C  C   . SER B 1 65  ? 13.074  -14.352 84.487  1.00 39.05  ? 65   SER B C   1 
ATOM   4199 O  O   . SER B 1 65  ? 14.032  -14.960 84.978  1.00 38.07  ? 65   SER B O   1 
ATOM   4200 C  CB  . SER B 1 65  ? 13.289  -11.982 85.256  1.00 41.86  ? 65   SER B CB  1 
ATOM   4201 O  OG  . SER B 1 65  ? 12.217  -12.261 86.149  1.00 41.50  ? 65   SER B OG  1 
ATOM   4202 N  N   . ARG B 1 66  ? 11.873  -14.910 84.323  1.00 35.04  ? 66   ARG B N   1 
ATOM   4203 C  CA  . ARG B 1 66  ? 11.588  -16.256 84.790  1.00 36.77  ? 66   ARG B CA  1 
ATOM   4204 C  C   . ARG B 1 66  ? 11.373  -17.267 83.678  1.00 33.88  ? 66   ARG B C   1 
ATOM   4205 O  O   . ARG B 1 66  ? 11.655  -18.445 83.888  1.00 36.01  ? 66   ARG B O   1 
ATOM   4206 C  CB  . ARG B 1 66  ? 10.350  -16.252 85.693  1.00 36.75  ? 66   ARG B CB  1 
ATOM   4207 C  CG  . ARG B 1 66  ? 10.495  -15.366 86.921  1.00 37.15  ? 66   ARG B CG  1 
ATOM   4208 C  CD  . ARG B 1 66  ? 9.137   -15.201 87.605  1.00 40.13  ? 66   ARG B CD  1 
ATOM   4209 N  NE  . ARG B 1 66  ? 8.657   -16.467 88.138  1.00 41.08  ? 66   ARG B NE  1 
ATOM   4210 C  CZ  . ARG B 1 66  ? 7.408   -16.691 88.522  1.00 38.52  ? 66   ARG B CZ  1 
ATOM   4211 N  NH1 . ARG B 1 66  ? 6.464   -15.772 88.378  1.00 38.15  ? 66   ARG B NH1 1 
ATOM   4212 N  NH2 . ARG B 1 66  ? 7.100   -17.866 89.063  1.00 43.43  ? 66   ARG B NH2 1 
ATOM   4213 N  N   . PHE B 1 67  ? 10.879  -16.838 82.516  1.00 32.96  ? 67   PHE B N   1 
ATOM   4214 C  CA  . PHE B 1 67  ? 10.552  -17.741 81.425  1.00 31.09  ? 67   PHE B CA  1 
ATOM   4215 C  C   . PHE B 1 67  ? 11.030  -17.149 80.107  1.00 32.58  ? 67   PHE B C   1 
ATOM   4216 O  O   . PHE B 1 67  ? 10.889  -15.945 79.873  1.00 33.91  ? 67   PHE B O   1 
ATOM   4217 C  CB  . PHE B 1 67  ? 9.027   -18.002 81.345  1.00 35.49  ? 67   PHE B CB  1 
ATOM   4218 C  CG  . PHE B 1 67  ? 8.451   -18.567 82.606  1.00 34.44  ? 67   PHE B CG  1 
ATOM   4219 C  CD1 . PHE B 1 67  ? 8.440   -19.934 82.816  1.00 35.39  ? 67   PHE B CD1 1 
ATOM   4220 C  CD2 . PHE B 1 67  ? 7.944   -17.733 83.584  1.00 33.92  ? 67   PHE B CD2 1 
ATOM   4221 C  CE1 . PHE B 1 67  ? 7.924   -20.478 83.986  1.00 38.13  ? 67   PHE B CE1 1 
ATOM   4222 C  CE2 . PHE B 1 67  ? 7.420   -18.266 84.781  1.00 36.44  ? 67   PHE B CE2 1 
ATOM   4223 C  CZ  . PHE B 1 67  ? 7.414   -19.649 84.966  1.00 33.67  ? 67   PHE B CZ  1 
ATOM   4224 N  N   . ASP B 1 68  ? 11.561  -18.014 79.245  1.00 32.95  ? 68   ASP B N   1 
ATOM   4225 C  CA  . ASP B 1 68  ? 11.997  -17.672 77.898  1.00 32.02  ? 68   ASP B CA  1 
ATOM   4226 C  C   . ASP B 1 68  ? 11.154  -18.429 76.874  1.00 34.55  ? 68   ASP B C   1 
ATOM   4227 O  O   . ASP B 1 68  ? 10.499  -19.425 77.189  1.00 30.55  ? 68   ASP B O   1 
ATOM   4228 C  CB  . ASP B 1 68  ? 13.496  -18.013 77.746  1.00 32.55  ? 68   ASP B CB  1 
ATOM   4229 C  CG  . ASP B 1 68  ? 14.079  -17.619 76.410  1.00 35.21  ? 68   ASP B CG  1 
ATOM   4230 O  OD1 . ASP B 1 68  ? 13.573  -16.688 75.734  1.00 33.77  ? 68   ASP B OD1 1 
ATOM   4231 O  OD2 . ASP B 1 68  ? 15.089  -18.264 76.035  1.00 34.98  ? 68   ASP B OD2 1 
ATOM   4232 N  N   . LYS B 1 69  ? 11.176  -17.950 75.632  1.00 33.12  ? 69   LYS B N   1 
ATOM   4233 C  CA  . LYS B 1 69  ? 10.474  -18.642 74.550  1.00 31.30  ? 69   LYS B CA  1 
ATOM   4234 C  C   . LYS B 1 69  ? 10.986  -20.072 74.381  1.00 34.61  ? 69   LYS B C   1 
ATOM   4235 O  O   . LYS B 1 69  ? 12.196  -20.312 74.302  1.00 33.01  ? 69   LYS B O   1 
ATOM   4236 C  CB  . LYS B 1 69  ? 10.643  -17.883 73.227  1.00 31.41  ? 69   LYS B CB  1 
ATOM   4237 C  CG  . LYS B 1 69  ? 10.316  -18.751 71.989  1.00 33.08  ? 69   LYS B CG  1 
ATOM   4238 C  CD  . LYS B 1 69  ? 9.874   -17.892 70.787  1.00 29.76  ? 69   LYS B CD  1 
ATOM   4239 C  CE  . LYS B 1 69  ? 9.714   -18.758 69.508  1.00 30.19  ? 69   LYS B CE  1 
ATOM   4240 N  NZ  . LYS B 1 69  ? 8.846   -18.094 68.425  1.00 30.10  ? 69   LYS B NZ  1 
ATOM   4241 N  N   . ASN B 1 70  ? 10.056  -21.019 74.285  1.00 30.36  ? 70   ASN B N   1 
ATOM   4242 C  CA  . ASN B 1 70  ? 10.354  -22.404 73.971  1.00 29.29  ? 70   ASN B CA  1 
ATOM   4243 C  C   . ASN B 1 70  ? 9.890   -22.717 72.551  1.00 30.97  ? 70   ASN B C   1 
ATOM   4244 O  O   . ASN B 1 70  ? 8.909   -22.141 72.062  1.00 32.22  ? 70   ASN B O   1 
ATOM   4245 C  CB  . ASN B 1 70  ? 9.668   -23.352 74.972  1.00 31.38  ? 70   ASN B CB  1 
ATOM   4246 C  CG  . ASN B 1 70  ? 9.968   -24.796 74.689  1.00 35.66  ? 70   ASN B CG  1 
ATOM   4247 O  OD1 . ASN B 1 70  ? 11.135  -25.191 74.580  1.00 34.47  ? 70   ASN B OD1 1 
ATOM   4248 N  ND2 . ASN B 1 70  ? 8.921   -25.603 74.550  1.00 34.15  ? 70   ASN B ND2 1 
ATOM   4249 N  N   . LEU B 1 71  ? 10.586  -23.641 71.884  1.00 30.39  ? 71   LEU B N   1 
ATOM   4250 C  CA  . LEU B 1 71  ? 10.086  -24.213 70.633  1.00 30.42  ? 71   LEU B CA  1 
ATOM   4251 C  C   . LEU B 1 71  ? 9.180   -25.389 70.989  1.00 32.76  ? 71   LEU B C   1 
ATOM   4252 O  O   . LEU B 1 71  ? 9.652   -26.443 71.431  1.00 33.39  ? 71   LEU B O   1 
ATOM   4253 C  CB  . LEU B 1 71  ? 11.228  -24.649 69.709  1.00 31.44  ? 71   LEU B CB  1 
ATOM   4254 C  CG  . LEU B 1 71  ? 12.237  -23.568 69.295  1.00 30.77  ? 71   LEU B CG  1 
ATOM   4255 C  CD1 . LEU B 1 71  ? 13.233  -24.134 68.268  1.00 33.00  ? 71   LEU B CD1 1 
ATOM   4256 C  CD2 . LEU B 1 71  ? 11.573  -22.305 68.729  1.00 32.11  ? 71   LEU B CD2 1 
ATOM   4257 N  N   . SER B 1 72  ? 7.871   -25.198 70.816  1.00 31.41  ? 72   SER B N   1 
ATOM   4258 C  CA  . SER B 1 72  ? 6.933   -26.310 70.846  1.00 34.40  ? 72   SER B CA  1 
ATOM   4259 C  C   . SER B 1 72  ? 7.322   -27.352 69.797  1.00 32.79  ? 72   SER B C   1 
ATOM   4260 O  O   . SER B 1 72  ? 8.121   -27.100 68.898  1.00 32.88  ? 72   SER B O   1 
ATOM   4261 C  CB  . SER B 1 72  ? 5.523   -25.807 70.547  1.00 30.29  ? 72   SER B CB  1 
ATOM   4262 O  OG  . SER B 1 72  ? 5.527   -25.096 69.307  1.00 32.52  ? 72   SER B OG  1 
ATOM   4263 N  N   . GLN B 1 73  ? 6.721   -28.536 69.895  1.00 33.38  ? 73   GLN B N   1 
ATOM   4264 C  CA  . GLN B 1 73  ? 6.937   -29.520 68.840  1.00 32.04  ? 73   GLN B CA  1 
ATOM   4265 C  C   . GLN B 1 73  ? 6.542   -28.949 67.490  1.00 31.81  ? 73   GLN B C   1 
ATOM   4266 O  O   . GLN B 1 73  ? 7.227   -29.176 66.481  1.00 33.91  ? 73   GLN B O   1 
ATOM   4267 C  CB  . GLN B 1 73  ? 6.151   -30.798 69.133  1.00 35.11  ? 73   GLN B CB  1 
ATOM   4268 C  CG  . GLN B 1 73  ? 6.583   -31.978 68.299  1.00 41.15  ? 73   GLN B CG  1 
ATOM   4269 C  CD  . GLN B 1 73  ? 8.015   -32.362 68.568  1.00 45.61  ? 73   GLN B CD  1 
ATOM   4270 O  OE1 . GLN B 1 73  ? 8.341   -32.850 69.649  1.00 43.26  ? 73   GLN B OE1 1 
ATOM   4271 N  NE2 . GLN B 1 73  ? 8.884   -32.142 67.579  1.00 42.54  ? 73   GLN B NE2 1 
ATOM   4272 N  N   . ALA B 1 74  ? 5.449   -28.185 67.450  1.00 33.87  ? 74   ALA B N   1 
ATOM   4273 C  CA  . ALA B 1 74  ? 5.032   -27.570 66.194  1.00 33.77  ? 74   ALA B CA  1 
ATOM   4274 C  C   . ALA B 1 74  ? 6.164   -26.739 65.594  1.00 32.11  ? 74   ALA B C   1 
ATOM   4275 O  O   . ALA B 1 74  ? 6.468   -26.848 64.400  1.00 31.15  ? 74   ALA B O   1 
ATOM   4276 C  CB  . ALA B 1 74  ? 3.787   -26.707 66.412  1.00 33.63  ? 74   ALA B CB  1 
ATOM   4277 N  N   . LEU B 1 75  ? 6.797   -25.892 66.414  1.00 31.46  ? 75   LEU B N   1 
ATOM   4278 C  CA  . LEU B 1 75  ? 7.856   -25.039 65.880  1.00 29.45  ? 75   LEU B CA  1 
ATOM   4279 C  C   . LEU B 1 75  ? 9.110   -25.842 65.572  1.00 29.84  ? 75   LEU B C   1 
ATOM   4280 O  O   . LEU B 1 75  ? 9.841   -25.493 64.639  1.00 30.59  ? 75   LEU B O   1 
ATOM   4281 C  CB  . LEU B 1 75  ? 8.187   -23.899 66.841  1.00 30.63  ? 75   LEU B CB  1 
ATOM   4282 C  CG  . LEU B 1 75  ? 7.106   -22.829 67.069  1.00 34.47  ? 75   LEU B CG  1 
ATOM   4283 C  CD1 . LEU B 1 75  ? 7.705   -21.603 67.773  1.00 32.43  ? 75   LEU B CD1 1 
ATOM   4284 C  CD2 . LEU B 1 75  ? 6.412   -22.434 65.778  1.00 35.21  ? 75   LEU B CD2 1 
ATOM   4285 N  N   . LYS B 1 76  ? 9.377   -26.915 66.330  1.00 31.72  ? 76   LYS B N   1 
ATOM   4286 C  CA  . LYS B 1 76  ? 10.512  -27.766 65.966  1.00 33.41  ? 76   LYS B CA  1 
ATOM   4287 C  C   . LYS B 1 76  ? 10.299  -28.376 64.587  1.00 34.90  ? 76   LYS B C   1 
ATOM   4288 O  O   . LYS B 1 76  ? 11.237  -28.465 63.780  1.00 32.99  ? 76   LYS B O   1 
ATOM   4289 C  CB  . LYS B 1 76  ? 10.738  -28.853 67.016  1.00 33.04  ? 76   LYS B CB  1 
ATOM   4290 C  CG  . LYS B 1 76  ? 11.258  -28.285 68.346  1.00 34.30  ? 76   LYS B CG  1 
ATOM   4291 C  CD  . LYS B 1 76  ? 11.577  -29.380 69.335  1.00 39.26  ? 76   LYS B CD  1 
ATOM   4292 C  CE  . LYS B 1 76  ? 12.080  -28.776 70.640  1.00 44.51  ? 76   LYS B CE  1 
ATOM   4293 N  NZ  . LYS B 1 76  ? 12.179  -29.800 71.707  1.00 52.16  ? 76   LYS B NZ  1 
ATOM   4294 N  N   . PHE B 1 77  ? 9.057   -28.762 64.279  1.00 34.63  ? 77   PHE B N   1 
ATOM   4295 C  CA  . PHE B 1 77  ? 8.763   -29.310 62.960  1.00 34.49  ? 77   PHE B CA  1 
ATOM   4296 C  C   . PHE B 1 77  ? 8.842   -28.242 61.874  1.00 35.71  ? 77   PHE B C   1 
ATOM   4297 O  O   . PHE B 1 77  ? 9.359   -28.502 60.782  1.00 35.78  ? 77   PHE B O   1 
ATOM   4298 C  CB  . PHE B 1 77  ? 7.379   -29.960 62.973  1.00 35.25  ? 77   PHE B CB  1 
ATOM   4299 C  CG  . PHE B 1 77  ? 7.319   -31.245 63.764  1.00 37.18  ? 77   PHE B CG  1 
ATOM   4300 C  CD1 . PHE B 1 77  ? 8.470   -31.985 64.002  1.00 42.47  ? 77   PHE B CD1 1 
ATOM   4301 C  CD2 . PHE B 1 77  ? 6.117   -31.718 64.246  1.00 34.97  ? 77   PHE B CD2 1 
ATOM   4302 C  CE1 . PHE B 1 77  ? 8.413   -33.171 64.705  1.00 42.73  ? 77   PHE B CE1 1 
ATOM   4303 C  CE2 . PHE B 1 77  ? 6.046   -32.901 64.963  1.00 39.37  ? 77   PHE B CE2 1 
ATOM   4304 C  CZ  . PHE B 1 77  ? 7.201   -33.629 65.192  1.00 43.63  ? 77   PHE B CZ  1 
ATOM   4305 N  N   . VAL B 1 78  ? 8.309   -27.045 62.142  1.00 32.23  ? 78   VAL B N   1 
ATOM   4306 C  CA  . VAL B 1 78  ? 8.391   -25.949 61.180  1.00 32.41  ? 78   VAL B CA  1 
ATOM   4307 C  C   . VAL B 1 78  ? 9.842   -25.558 60.951  1.00 33.98  ? 78   VAL B C   1 
ATOM   4308 O  O   . VAL B 1 78  ? 10.209  -25.097 59.866  1.00 33.16  ? 78   VAL B O   1 
ATOM   4309 C  CB  . VAL B 1 78  ? 7.552   -24.761 61.700  1.00 36.82  ? 78   VAL B CB  1 
ATOM   4310 C  CG1 . VAL B 1 78  ? 7.949   -23.455 61.024  1.00 40.22  ? 78   VAL B CG1 1 
ATOM   4311 C  CG2 . VAL B 1 78  ? 6.069   -25.059 61.514  1.00 41.71  ? 78   VAL B CG2 1 
ATOM   4312 N  N   . ARG B 1 79  ? 10.683  -25.734 61.968  1.00 32.98  ? 79   ARG B N   1 
ATOM   4313 C  CA  . ARG B 1 79  ? 12.102  -25.402 61.834  1.00 33.80  ? 79   ARG B CA  1 
ATOM   4314 C  C   . ARG B 1 79  ? 12.798  -26.241 60.769  1.00 37.75  ? 79   ARG B C   1 
ATOM   4315 O  O   . ARG B 1 79  ? 13.880  -25.857 60.296  1.00 34.75  ? 79   ARG B O   1 
ATOM   4316 C  CB  . ARG B 1 79  ? 12.798  -25.572 63.193  1.00 32.23  ? 79   ARG B CB  1 
ATOM   4317 C  CG  . ARG B 1 79  ? 14.296  -25.300 63.124  1.00 33.49  ? 79   ARG B CG  1 
ATOM   4318 C  CD  . ARG B 1 79  ? 14.866  -25.006 64.487  1.00 31.88  ? 79   ARG B CD  1 
ATOM   4319 N  NE  . ARG B 1 79  ? 16.325  -24.931 64.446  1.00 36.66  ? 79   ARG B NE  1 
ATOM   4320 C  CZ  . ARG B 1 79  ? 17.045  -24.028 65.098  1.00 39.17  ? 79   ARG B CZ  1 
ATOM   4321 N  NH1 . ARG B 1 79  ? 16.471  -23.101 65.844  1.00 32.92  ? 79   ARG B NH1 1 
ATOM   4322 N  NH2 . ARG B 1 79  ? 18.380  -24.052 64.991  1.00 36.39  ? 79   ARG B NH2 1 
ATOM   4323 N  N   . ASP B 1 80  ? 12.209  -27.374 60.367  1.00 34.84  ? 80   ASP B N   1 
ATOM   4324 C  CA  . ASP B 1 80  ? 12.813  -28.142 59.285  1.00 35.65  ? 80   ASP B CA  1 
ATOM   4325 C  C   . ASP B 1 80  ? 12.886  -27.333 57.998  1.00 37.40  ? 80   ASP B C   1 
ATOM   4326 O  O   . ASP B 1 80  ? 13.756  -27.595 57.160  1.00 38.77  ? 80   ASP B O   1 
ATOM   4327 C  CB  . ASP B 1 80  ? 12.052  -29.453 59.042  1.00 37.06  ? 80   ASP B CB  1 
ATOM   4328 C  CG  . ASP B 1 80  ? 12.325  -30.498 60.107  1.00 45.56  ? 80   ASP B CG  1 
ATOM   4329 O  OD1 . ASP B 1 80  ? 13.288  -30.337 60.874  1.00 43.91  ? 80   ASP B OD1 1 
ATOM   4330 O  OD2 . ASP B 1 80  ? 11.561  -31.484 60.187  1.00 48.59  ? 80   ASP B OD2 1 
ATOM   4331 N  N   . PHE B 1 81  ? 11.986  -26.360 57.801  1.00 34.52  ? 81   PHE B N   1 
ATOM   4332 C  CA  . PHE B 1 81  ? 12.154  -25.456 56.672  1.00 33.85  ? 81   PHE B CA  1 
ATOM   4333 C  C   . PHE B 1 81  ? 12.417  -24.000 57.058  1.00 33.31  ? 81   PHE B C   1 
ATOM   4334 O  O   . PHE B 1 81  ? 12.947  -23.254 56.228  1.00 35.14  ? 81   PHE B O   1 
ATOM   4335 C  CB  . PHE B 1 81  ? 10.947  -25.540 55.708  1.00 33.85  ? 81   PHE B CB  1 
ATOM   4336 C  CG  . PHE B 1 81  ? 9.599   -25.360 56.355  1.00 34.21  ? 81   PHE B CG  1 
ATOM   4337 C  CD1 . PHE B 1 81  ? 8.867   -26.463 56.788  1.00 37.12  ? 81   PHE B CD1 1 
ATOM   4338 C  CD2 . PHE B 1 81  ? 9.027   -24.097 56.462  1.00 32.93  ? 81   PHE B CD2 1 
ATOM   4339 C  CE1 . PHE B 1 81  ? 7.597   -26.298 57.361  1.00 36.76  ? 81   PHE B CE1 1 
ATOM   4340 C  CE2 . PHE B 1 81  ? 7.756   -23.925 57.029  1.00 37.29  ? 81   PHE B CE2 1 
ATOM   4341 C  CZ  . PHE B 1 81  ? 7.042   -25.029 57.475  1.00 37.69  ? 81   PHE B CZ  1 
ATOM   4342 N  N   . ALA B 1 82  ? 12.125  -23.585 58.295  1.00 34.11  ? 82   ALA B N   1 
ATOM   4343 C  CA  . ALA B 1 82  ? 12.365  -22.203 58.702  1.00 33.67  ? 82   ALA B CA  1 
ATOM   4344 C  C   . ALA B 1 82  ? 13.668  -22.011 59.474  1.00 32.63  ? 82   ALA B C   1 
ATOM   4345 O  O   . ALA B 1 82  ? 14.032  -20.863 59.746  1.00 33.20  ? 82   ALA B O   1 
ATOM   4346 C  CB  . ALA B 1 82  ? 11.186  -21.674 59.551  1.00 32.04  ? 82   ALA B CB  1 
ATOM   4347 N  N   . GLY B 1 83  ? 14.355  -23.093 59.842  1.00 33.74  ? 83   GLY B N   1 
ATOM   4348 C  CA  . GLY B 1 83  ? 15.704  -23.015 60.380  1.00 34.05  ? 83   GLY B CA  1 
ATOM   4349 C  C   . GLY B 1 83  ? 15.835  -22.105 61.584  1.00 34.21  ? 83   GLY B C   1 
ATOM   4350 O  O   . GLY B 1 83  ? 14.971  -22.065 62.475  1.00 31.73  ? 83   GLY B O   1 
ATOM   4351 N  N   . ASP B 1 84  ? 16.933  -21.347 61.626  1.00 33.65  ? 84   ASP B N   1 
ATOM   4352 C  CA  . ASP B 1 84  ? 17.112  -20.376 62.702  1.00 33.71  ? 84   ASP B CA  1 
ATOM   4353 C  C   . ASP B 1 84  ? 16.712  -18.973 62.261  1.00 35.38  ? 84   ASP B C   1 
ATOM   4354 O  O   . ASP B 1 84  ? 17.353  -17.981 62.626  1.00 31.44  ? 84   ASP B O   1 
ATOM   4355 C  CB  . ASP B 1 84  ? 18.543  -20.421 63.245  1.00 32.37  ? 84   ASP B CB  1 
ATOM   4356 C  CG  . ASP B 1 84  ? 19.593  -20.128 62.194  1.00 36.32  ? 84   ASP B CG  1 
ATOM   4357 O  OD1 . ASP B 1 84  ? 19.278  -20.054 60.986  1.00 33.50  ? 84   ASP B OD1 1 
ATOM   4358 O  OD2 . ASP B 1 84  ? 20.774  -19.992 62.590  1.00 37.52  ? 84   ASP B OD2 1 
ATOM   4359 N  N   . GLY B 1 85  ? 15.624  -18.875 61.479  1.00 32.93  ? 85   GLY B N   1 
ATOM   4360 C  CA  . GLY B 1 85  ? 14.971  -17.607 61.223  1.00 31.50  ? 85   GLY B CA  1 
ATOM   4361 C  C   . GLY B 1 85  ? 14.342  -17.090 62.505  1.00 33.93  ? 85   GLY B C   1 
ATOM   4362 O  O   . GLY B 1 85  ? 14.373  -17.784 63.526  1.00 32.00  ? 85   GLY B O   1 
ATOM   4363 N  N   . LEU B 1 86  ? 13.757  -15.890 62.476  1.00 30.56  ? 86   LEU B N   1 
ATOM   4364 C  CA  . LEU B 1 86  ? 13.380  -15.239 63.732  1.00 28.16  ? 86   LEU B CA  1 
ATOM   4365 C  C   . LEU B 1 86  ? 12.308  -16.021 64.480  1.00 30.49  ? 86   LEU B C   1 
ATOM   4366 O  O   . LEU B 1 86  ? 12.276  -16.010 65.717  1.00 29.81  ? 86   LEU B O   1 
ATOM   4367 C  CB  . LEU B 1 86  ? 12.888  -13.812 63.467  1.00 30.26  ? 86   LEU B CB  1 
ATOM   4368 C  CG  . LEU B 1 86  ? 14.003  -12.786 63.258  1.00 31.85  ? 86   LEU B CG  1 
ATOM   4369 C  CD1 . LEU B 1 86  ? 13.346  -11.469 62.918  1.00 35.23  ? 86   LEU B CD1 1 
ATOM   4370 C  CD2 . LEU B 1 86  ? 14.828  -12.658 64.553  1.00 31.45  ? 86   LEU B CD2 1 
ATOM   4371 N  N   . PHE B 1 87  ? 11.391  -16.672 63.756  1.00 31.79  ? 87   PHE B N   1 
ATOM   4372 C  CA  . PHE B 1 87  ? 10.265  -17.336 64.428  1.00 31.93  ? 87   PHE B CA  1 
ATOM   4373 C  C   . PHE B 1 87  ? 10.687  -18.642 65.109  1.00 31.41  ? 87   PHE B C   1 
ATOM   4374 O  O   . PHE B 1 87  ? 10.122  -19.027 66.149  1.00 31.46  ? 87   PHE B O   1 
ATOM   4375 C  CB  . PHE B 1 87  ? 9.153   -17.589 63.397  1.00 30.51  ? 87   PHE B CB  1 
ATOM   4376 C  CG  . PHE B 1 87  ? 7.748   -17.659 63.990  1.00 32.17  ? 87   PHE B CG  1 
ATOM   4377 C  CD1 . PHE B 1 87  ? 7.336   -18.772 64.685  1.00 32.79  ? 87   PHE B CD1 1 
ATOM   4378 C  CD2 . PHE B 1 87  ? 6.857   -16.609 63.820  1.00 32.76  ? 87   PHE B CD2 1 
ATOM   4379 C  CE1 . PHE B 1 87  ? 6.041   -18.843 65.223  1.00 34.14  ? 87   PHE B CE1 1 
ATOM   4380 C  CE2 . PHE B 1 87  ? 5.551   -16.673 64.345  1.00 31.93  ? 87   PHE B CE2 1 
ATOM   4381 C  CZ  . PHE B 1 87  ? 5.161   -17.779 65.050  1.00 32.45  ? 87   PHE B CZ  1 
ATOM   4382 N  N   . THR B 1 88  ? 11.685  -19.335 64.564  1.00 30.62  ? 88   THR B N   1 
ATOM   4383 C  CA  . THR B 1 88  ? 12.005  -20.679 65.036  1.00 29.02  ? 88   THR B CA  1 
ATOM   4384 C  C   . THR B 1 88  ? 13.408  -20.788 65.630  1.00 29.80  ? 88   THR B C   1 
ATOM   4385 O  O   . THR B 1 88  ? 13.899  -21.903 65.841  1.00 33.34  ? 88   THR B O   1 
ATOM   4386 C  CB  . THR B 1 88  ? 11.828  -21.710 63.913  1.00 32.02  ? 88   THR B CB  1 
ATOM   4387 O  OG1 . THR B 1 88  ? 12.468  -21.253 62.702  1.00 32.12  ? 88   THR B OG1 1 
ATOM   4388 C  CG2 . THR B 1 88  ? 10.341  -21.906 63.637  1.00 33.89  ? 88   THR B CG2 1 
ATOM   4389 N  N   . SER B 1 89  ? 14.056  -19.673 65.912  1.00 32.79  ? 89   SER B N   1 
ATOM   4390 C  CA  . SER B 1 89  ? 15.328  -19.706 66.630  1.00 30.44  ? 89   SER B CA  1 
ATOM   4391 C  C   . SER B 1 89  ? 15.121  -19.598 68.138  1.00 32.30  ? 89   SER B C   1 
ATOM   4392 O  O   . SER B 1 89  ? 14.134  -19.035 68.615  1.00 32.26  ? 89   SER B O   1 
ATOM   4393 C  CB  . SER B 1 89  ? 16.236  -18.576 66.135  1.00 34.17  ? 89   SER B CB  1 
ATOM   4394 O  OG  . SER B 1 89  ? 15.534  -17.340 66.123  1.00 36.22  ? 89   SER B OG  1 
ATOM   4395 N  N   . TRP B 1 90  ? 16.055  -20.182 68.891  1.00 31.53  ? 90   TRP B N   1 
ATOM   4396 C  CA  . TRP B 1 90  ? 16.109  -19.983 70.332  1.00 30.57  ? 90   TRP B CA  1 
ATOM   4397 C  C   . TRP B 1 90  ? 16.688  -18.606 70.624  1.00 32.39  ? 90   TRP B C   1 
ATOM   4398 O  O   . TRP B 1 90  ? 17.506  -18.085 69.857  1.00 31.73  ? 90   TRP B O   1 
ATOM   4399 C  CB  . TRP B 1 90  ? 16.977  -21.055 70.997  1.00 31.52  ? 90   TRP B CB  1 
ATOM   4400 C  CG  . TRP B 1 90  ? 16.501  -22.455 70.752  1.00 32.39  ? 90   TRP B CG  1 
ATOM   4401 C  CD1 . TRP B 1 90  ? 16.853  -23.275 69.724  1.00 31.60  ? 90   TRP B CD1 1 
ATOM   4402 C  CD2 . TRP B 1 90  ? 15.563  -23.188 71.551  1.00 33.10  ? 90   TRP B CD2 1 
ATOM   4403 N  NE1 . TRP B 1 90  ? 16.213  -24.484 69.838  1.00 33.17  ? 90   TRP B NE1 1 
ATOM   4404 C  CE2 . TRP B 1 90  ? 15.403  -24.451 70.949  1.00 33.88  ? 90   TRP B CE2 1 
ATOM   4405 C  CE3 . TRP B 1 90  ? 14.842  -22.896 72.720  1.00 35.23  ? 90   TRP B CE3 1 
ATOM   4406 C  CZ2 . TRP B 1 90  ? 14.562  -25.434 71.483  1.00 35.04  ? 90   TRP B CZ2 1 
ATOM   4407 C  CZ3 . TRP B 1 90  ? 13.993  -23.873 73.245  1.00 34.30  ? 90   TRP B CZ3 1 
ATOM   4408 C  CH2 . TRP B 1 90  ? 13.865  -25.125 72.622  1.00 34.58  ? 90   TRP B CH2 1 
ATOM   4409 N  N   . THR B 1 91  ? 16.238  -18.007 71.726  1.00 30.52  ? 91   THR B N   1 
ATOM   4410 C  CA  . THR B 1 91  ? 16.716  -16.680 72.088  1.00 31.90  ? 91   THR B CA  1 
ATOM   4411 C  C   . THR B 1 91  ? 18.232  -16.652 72.261  1.00 36.05  ? 91   THR B C   1 
ATOM   4412 O  O   . THR B 1 91  ? 18.866  -15.629 71.974  1.00 34.38  ? 91   THR B O   1 
ATOM   4413 C  CB  . THR B 1 91  ? 16.017  -16.194 73.364  1.00 32.32  ? 91   THR B CB  1 
ATOM   4414 O  OG1 . THR B 1 91  ? 14.593  -16.313 73.206  1.00 34.03  ? 91   THR B OG1 1 
ATOM   4415 C  CG2 . THR B 1 91  ? 16.400  -14.742 73.685  1.00 34.37  ? 91   THR B CG2 1 
ATOM   4416 N  N   . HIS B 1 92  ? 18.829  -17.765 72.697  1.00 32.11  ? 92   HIS B N   1 
ATOM   4417 C  CA  . HIS B 1 92  ? 20.268  -17.829 72.938  1.00 31.85  ? 92   HIS B CA  1 
ATOM   4418 C  C   . HIS B 1 92  ? 21.092  -18.154 71.697  1.00 34.33  ? 92   HIS B C   1 
ATOM   4419 O  O   . HIS B 1 92  ? 22.327  -18.076 71.761  1.00 32.60  ? 92   HIS B O   1 
ATOM   4420 C  CB  . HIS B 1 92  ? 20.554  -18.869 74.022  1.00 33.50  ? 92   HIS B CB  1 
ATOM   4421 C  CG  . HIS B 1 92  ? 19.915  -20.197 73.764  1.00 34.52  ? 92   HIS B CG  1 
ATOM   4422 N  ND1 . HIS B 1 92  ? 20.437  -21.109 72.873  1.00 33.86  ? 92   HIS B ND1 1 
ATOM   4423 C  CD2 . HIS B 1 92  ? 18.806  -20.776 74.289  1.00 33.70  ? 92   HIS B CD2 1 
ATOM   4424 C  CE1 . HIS B 1 92  ? 19.673  -22.188 72.851  1.00 33.80  ? 92   HIS B CE1 1 
ATOM   4425 N  NE2 . HIS B 1 92  ? 18.686  -22.018 73.714  1.00 33.96  ? 92   HIS B NE2 1 
ATOM   4426 N  N   . GLU B 1 93  ? 20.471  -18.521 70.577  1.00 32.54  ? 93   GLU B N   1 
ATOM   4427 C  CA  . GLU B 1 93  ? 21.234  -18.679 69.346  1.00 30.06  ? 93   GLU B CA  1 
ATOM   4428 C  C   . GLU B 1 93  ? 21.705  -17.321 68.834  1.00 32.40  ? 93   GLU B C   1 
ATOM   4429 O  O   . GLU B 1 93  ? 20.941  -16.358 68.790  1.00 31.37  ? 93   GLU B O   1 
ATOM   4430 C  CB  . GLU B 1 93  ? 20.393  -19.364 68.267  1.00 32.33  ? 93   GLU B CB  1 
ATOM   4431 C  CG  . GLU B 1 93  ? 20.152  -20.852 68.540  1.00 33.72  ? 93   GLU B CG  1 
ATOM   4432 C  CD  . GLU B 1 93  ? 19.338  -21.481 67.439  1.00 34.81  ? 93   GLU B CD  1 
ATOM   4433 O  OE1 . GLU B 1 93  ? 18.106  -21.255 67.407  1.00 35.29  ? 93   GLU B OE1 1 
ATOM   4434 O  OE2 . GLU B 1 93  ? 19.927  -22.191 66.600  1.00 37.72  ? 93   GLU B OE2 1 
ATOM   4435 N  N   . LYS B 1 94  ? 22.970  -17.254 68.409  1.00 33.61  ? 94   LYS B N   1 
ATOM   4436 C  CA  . LYS B 1 94  ? 23.527  -15.984 67.943  1.00 33.45  ? 94   LYS B CA  1 
ATOM   4437 C  C   . LYS B 1 94  ? 22.642  -15.322 66.880  1.00 31.42  ? 94   LYS B C   1 
ATOM   4438 O  O   . LYS B 1 94  ? 22.449  -14.102 66.897  1.00 32.91  ? 94   LYS B O   1 
ATOM   4439 C  CB  . LYS B 1 94  ? 24.949  -16.215 67.409  1.00 34.89  ? 94   LYS B CB  1 
ATOM   4440 C  CG  . LYS B 1 94  ? 25.587  -14.989 66.746  1.00 34.27  ? 94   LYS B CG  1 
ATOM   4441 C  CD  . LYS B 1 94  ? 27.046  -15.275 66.329  1.00 33.20  ? 94   LYS B CD  1 
ATOM   4442 C  CE  . LYS B 1 94  ? 27.654  -14.058 65.675  1.00 38.29  ? 94   LYS B CE  1 
ATOM   4443 N  NZ  . LYS B 1 94  ? 29.054  -14.307 65.189  1.00 42.36  ? 94   LYS B NZ  1 
ATOM   4444 N  N   . ASN B 1 95  ? 22.083  -16.108 65.956  1.00 30.92  ? 95   ASN B N   1 
ATOM   4445 C  CA  . ASN B 1 95  ? 21.342  -15.498 64.859  1.00 33.04  ? 95   ASN B CA  1 
ATOM   4446 C  C   . ASN B 1 95  ? 20.002  -14.905 65.291  1.00 34.20  ? 95   ASN B C   1 
ATOM   4447 O  O   . ASN B 1 95  ? 19.402  -14.165 64.496  1.00 33.66  ? 95   ASN B O   1 
ATOM   4448 C  CB  . ASN B 1 95  ? 21.110  -16.506 63.738  1.00 32.67  ? 95   ASN B CB  1 
ATOM   4449 C  CG  . ASN B 1 95  ? 22.284  -16.589 62.763  1.00 33.54  ? 95   ASN B CG  1 
ATOM   4450 O  OD1 . ASN B 1 95  ? 23.054  -15.639 62.616  1.00 37.44  ? 95   ASN B OD1 1 
ATOM   4451 N  ND2 . ASN B 1 95  ? 22.424  -17.734 62.104  1.00 32.71  ? 95   ASN B ND2 1 
ATOM   4452 N  N   . TRP B 1 96  ? 19.506  -15.185 66.503  1.00 32.92  ? 96   TRP B N   1 
ATOM   4453 C  CA  . TRP B 1 96  ? 18.249  -14.540 66.897  1.00 31.87  ? 96   TRP B CA  1 
ATOM   4454 C  C   . TRP B 1 96  ? 18.449  -13.041 67.114  1.00 32.21  ? 96   TRP B C   1 
ATOM   4455 O  O   . TRP B 1 96  ? 17.874  -12.213 66.395  1.00 32.18  ? 96   TRP B O   1 
ATOM   4456 C  CB  . TRP B 1 96  ? 17.603  -15.170 68.150  1.00 31.71  ? 96   TRP B CB  1 
ATOM   4457 C  CG  . TRP B 1 96  ? 16.384  -14.340 68.399  1.00 30.88  ? 96   TRP B CG  1 
ATOM   4458 C  CD1 . TRP B 1 96  ? 15.242  -14.320 67.621  1.00 34.45  ? 96   TRP B CD1 1 
ATOM   4459 C  CD2 . TRP B 1 96  ? 16.233  -13.276 69.349  1.00 32.69  ? 96   TRP B CD2 1 
ATOM   4460 N  NE1 . TRP B 1 96  ? 14.390  -13.344 68.065  1.00 31.38  ? 96   TRP B NE1 1 
ATOM   4461 C  CE2 . TRP B 1 96  ? 14.968  -12.686 69.121  1.00 31.63  ? 96   TRP B CE2 1 
ATOM   4462 C  CE3 . TRP B 1 96  ? 17.031  -12.781 70.392  1.00 34.47  ? 96   TRP B CE3 1 
ATOM   4463 C  CZ2 . TRP B 1 96  ? 14.475  -11.629 69.907  1.00 36.14  ? 96   TRP B CZ2 1 
ATOM   4464 C  CZ3 . TRP B 1 96  ? 16.549  -11.728 71.163  1.00 35.27  ? 96   TRP B CZ3 1 
ATOM   4465 C  CH2 . TRP B 1 96  ? 15.271  -11.165 70.916  1.00 36.05  ? 96   TRP B CH2 1 
ATOM   4466 N  N   . LYS B 1 97  ? 19.290  -12.663 68.085  1.00 31.70  ? 97   LYS B N   1 
ATOM   4467 C  CA  . LYS B 1 97  ? 19.454  -11.237 68.380  1.00 32.66  ? 97   LYS B CA  1 
ATOM   4468 C  C   . LYS B 1 97  ? 20.061  -10.505 67.195  1.00 30.27  ? 97   LYS B C   1 
ATOM   4469 O  O   . LYS B 1 97  ? 19.734  -9.341  66.926  1.00 32.41  ? 97   LYS B O   1 
ATOM   4470 C  CB  . LYS B 1 97  ? 20.323  -11.053 69.633  1.00 31.57  ? 97   LYS B CB  1 
ATOM   4471 C  CG  . LYS B 1 97  ? 20.359  -9.623  70.184  1.00 36.32  ? 97   LYS B CG  1 
ATOM   4472 C  CD  . LYS B 1 97  ? 18.949  -9.114  70.485  1.00 39.25  ? 97   LYS B CD  1 
ATOM   4473 C  CE  . LYS B 1 97  ? 18.944  -7.689  71.051  1.00 46.00  ? 97   LYS B CE  1 
ATOM   4474 N  NZ  . LYS B 1 97  ? 19.727  -7.615  72.312  1.00 51.80  ? 97   LYS B NZ  1 
ATOM   4475 N  N   . LYS B 1 98  ? 20.958  -11.170 66.478  1.00 30.97  ? 98   LYS B N   1 
ATOM   4476 C  CA  . LYS B 1 98  ? 21.578  -10.550 65.317  1.00 31.05  ? 98   LYS B CA  1 
ATOM   4477 C  C   . LYS B 1 98  ? 20.534  -10.174 64.274  1.00 35.03  ? 98   LYS B C   1 
ATOM   4478 O  O   . LYS B 1 98  ? 20.492  -9.030  63.801  1.00 34.30  ? 98   LYS B O   1 
ATOM   4479 C  CB  . LYS B 1 98  ? 22.618  -11.518 64.752  1.00 35.10  ? 98   LYS B CB  1 
ATOM   4480 C  CG  . LYS B 1 98  ? 23.357  -11.032 63.568  1.00 36.60  ? 98   LYS B CG  1 
ATOM   4481 C  CD  . LYS B 1 98  ? 24.375  -12.079 63.135  1.00 36.34  ? 98   LYS B CD  1 
ATOM   4482 C  CE  . LYS B 1 98  ? 24.960  -11.733 61.795  1.00 34.88  ? 98   LYS B CE  1 
ATOM   4483 N  NZ  . LYS B 1 98  ? 26.029  -12.705 61.448  1.00 35.13  ? 98   LYS B NZ  1 
ATOM   4484 N  N   . ALA B 1 99  ? 19.681  -11.132 63.896  1.00 32.87  ? 99   ALA B N   1 
ATOM   4485 C  CA  . ALA B 1 99  ? 18.643  -10.841 62.909  1.00 32.72  ? 99   ALA B CA  1 
ATOM   4486 C  C   . ALA B 1 99  ? 17.609  -9.864  63.456  1.00 31.83  ? 99   ALA B C   1 
ATOM   4487 O  O   . ALA B 1 99  ? 17.089  -9.017  62.709  1.00 34.67  ? 99   ALA B O   1 
ATOM   4488 C  CB  . ALA B 1 99  ? 17.969  -12.138 62.451  1.00 31.42  ? 99   ALA B CB  1 
ATOM   4489 N  N   . HIS B 1 100 ? 17.280  -9.980  64.742  1.00 33.46  ? 100  HIS B N   1 
ATOM   4490 C  CA  . HIS B 1 100 ? 16.355  -9.041  65.358  1.00 33.89  ? 100  HIS B CA  1 
ATOM   4491 C  C   . HIS B 1 100 ? 16.873  -7.612  65.219  1.00 35.43  ? 100  HIS B C   1 
ATOM   4492 O  O   . HIS B 1 100 ? 16.152  -6.721  64.764  1.00 34.50  ? 100  HIS B O   1 
ATOM   4493 C  CB  . HIS B 1 100 ? 16.134  -9.420  66.828  1.00 31.62  ? 100  HIS B CB  1 
ATOM   4494 C  CG  . HIS B 1 100 ? 15.368  -8.403  67.611  1.00 37.70  ? 100  HIS B CG  1 
ATOM   4495 N  ND1 . HIS B 1 100 ? 13.990  -8.344  67.600  1.00 39.73  ? 100  HIS B ND1 1 
ATOM   4496 C  CD2 . HIS B 1 100 ? 15.781  -7.413  68.439  1.00 43.42  ? 100  HIS B CD2 1 
ATOM   4497 C  CE1 . HIS B 1 100 ? 13.587  -7.364  68.389  1.00 43.86  ? 100  HIS B CE1 1 
ATOM   4498 N  NE2 . HIS B 1 100 ? 14.653  -6.785  68.913  1.00 46.55  ? 100  HIS B NE2 1 
ATOM   4499 N  N   . ASN B 1 101 ? 18.147  -7.384  65.564  1.00 33.28  ? 101  ASN B N   1 
ATOM   4500 C  CA  . ASN B 1 101 ? 18.705  -6.035  65.463  1.00 35.75  ? 101  ASN B CA  1 
ATOM   4501 C  C   . ASN B 1 101 ? 18.709  -5.538  64.021  1.00 32.81  ? 101  ASN B C   1 
ATOM   4502 O  O   . ASN B 1 101 ? 18.492  -4.345  63.769  1.00 35.86  ? 101  ASN B O   1 
ATOM   4503 C  CB  . ASN B 1 101 ? 20.134  -6.000  66.035  1.00 31.30  ? 101  ASN B CB  1 
ATOM   4504 C  CG  . ASN B 1 101 ? 20.163  -6.096  67.556  1.00 36.80  ? 101  ASN B CG  1 
ATOM   4505 O  OD1 . ASN B 1 101 ? 19.163  -5.832  68.222  1.00 35.63  ? 101  ASN B OD1 1 
ATOM   4506 N  ND2 . ASN B 1 101 ? 21.320  -6.465  68.116  1.00 36.17  ? 101  ASN B ND2 1 
ATOM   4507 N  N   . ILE B 1 102 ? 18.974  -6.431  63.066  1.00 34.34  ? 102  ILE B N   1 
ATOM   4508 C  CA  . ILE B 1 102 ? 19.116  -6.035  61.669  1.00 34.23  ? 102  ILE B CA  1 
ATOM   4509 C  C   . ILE B 1 102 ? 17.760  -5.701  61.066  1.00 35.51  ? 102  ILE B C   1 
ATOM   4510 O  O   . ILE B 1 102 ? 17.634  -4.767  60.264  1.00 34.54  ? 102  ILE B O   1 
ATOM   4511 C  CB  . ILE B 1 102 ? 19.842  -7.145  60.875  1.00 33.70  ? 102  ILE B CB  1 
ATOM   4512 C  CG1 . ILE B 1 102 ? 21.344  -7.144  61.216  1.00 33.88  ? 102  ILE B CG1 1 
ATOM   4513 C  CG2 . ILE B 1 102 ? 19.634  -7.002  59.366  1.00 36.31  ? 102  ILE B CG2 1 
ATOM   4514 C  CD1 . ILE B 1 102 ? 22.086  -8.366  60.709  1.00 34.33  ? 102  ILE B CD1 1 
ATOM   4515 N  N   . LEU B 1 103 ? 16.724  -6.442  61.451  1.00 35.99  ? 103  LEU B N   1 
ATOM   4516 C  CA  . LEU B 1 103 ? 15.443  -6.340  60.768  1.00 31.76  ? 103  LEU B CA  1 
ATOM   4517 C  C   . LEU B 1 103 ? 14.416  -5.485  61.498  1.00 36.32  ? 103  LEU B C   1 
ATOM   4518 O  O   . LEU B 1 103 ? 13.458  -5.035  60.860  1.00 35.20  ? 103  LEU B O   1 
ATOM   4519 C  CB  . LEU B 1 103 ? 14.874  -7.747  60.518  1.00 33.65  ? 103  LEU B CB  1 
ATOM   4520 C  CG  . LEU B 1 103 ? 15.745  -8.653  59.635  1.00 33.63  ? 103  LEU B CG  1 
ATOM   4521 C  CD1 . LEU B 1 103 ? 15.110  -10.042 59.459  1.00 34.86  ? 103  LEU B CD1 1 
ATOM   4522 C  CD2 . LEU B 1 103 ? 16.014  -8.014  58.254  1.00 36.34  ? 103  LEU B CD2 1 
ATOM   4523 N  N   . LEU B 1 104 ? 14.579  -5.236  62.794  1.00 34.06  ? 104  LEU B N   1 
ATOM   4524 C  CA  . LEU B 1 104 ? 13.668  -4.335  63.498  1.00 36.63  ? 104  LEU B CA  1 
ATOM   4525 C  C   . LEU B 1 104 ? 13.453  -3.008  62.785  1.00 42.09  ? 104  LEU B C   1 
ATOM   4526 O  O   . LEU B 1 104 ? 12.304  -2.530  62.765  1.00 40.59  ? 104  LEU B O   1 
ATOM   4527 C  CB  . LEU B 1 104 ? 14.185  -4.052  64.917  1.00 38.77  ? 104  LEU B CB  1 
ATOM   4528 C  CG  . LEU B 1 104 ? 13.182  -3.535  65.956  1.00 44.49  ? 104  LEU B CG  1 
ATOM   4529 C  CD1 . LEU B 1 104 ? 11.827  -4.256  65.936  1.00 43.78  ? 104  LEU B CD1 1 
ATOM   4530 C  CD2 . LEU B 1 104 ? 13.793  -3.501  67.364  1.00 45.73  ? 104  LEU B CD2 1 
ATOM   4531 N  N   . PRO B 1 105 ? 14.474  -2.363  62.213  1.00 41.72  ? 105  PRO B N   1 
ATOM   4532 C  CA  . PRO B 1 105 ? 14.238  -1.083  61.522  1.00 42.71  ? 105  PRO B CA  1 
ATOM   4533 C  C   . PRO B 1 105 ? 13.300  -1.190  60.331  1.00 44.40  ? 105  PRO B C   1 
ATOM   4534 O  O   . PRO B 1 105 ? 12.757  -0.163  59.910  1.00 45.25  ? 105  PRO B O   1 
ATOM   4535 C  CB  . PRO B 1 105 ? 15.645  -0.658  61.075  1.00 43.52  ? 105  PRO B CB  1 
ATOM   4536 C  CG  . PRO B 1 105 ? 16.558  -1.311  62.076  1.00 43.48  ? 105  PRO B CG  1 
ATOM   4537 C  CD  . PRO B 1 105 ? 15.915  -2.665  62.325  1.00 42.11  ? 105  PRO B CD  1 
ATOM   4538 N  N   . SER B 1 106 ? 13.118  -2.385  59.761  1.00 37.42  ? 106  SER B N   1 
ATOM   4539 C  CA  . SER B 1 106 ? 12.210  -2.584  58.637  1.00 37.17  ? 106  SER B CA  1 
ATOM   4540 C  C   . SER B 1 106 ? 10.757  -2.426  59.034  1.00 39.83  ? 106  SER B C   1 
ATOM   4541 O  O   . SER B 1 106 ? 9.877   -2.494  58.166  1.00 38.93  ? 106  SER B O   1 
ATOM   4542 C  CB  . SER B 1 106 ? 12.396  -3.973  58.043  1.00 38.96  ? 106  SER B CB  1 
ATOM   4543 O  OG  . SER B 1 106 ? 13.661  -4.064  57.434  1.00 46.55  ? 106  SER B OG  1 
ATOM   4544 N  N   . PHE B 1 107 ? 10.495  -2.258  60.322  1.00 36.41  ? 107  PHE B N   1 
ATOM   4545 C  CA  . PHE B 1 107 ? 9.144   -2.125  60.841  1.00 41.29  ? 107  PHE B CA  1 
ATOM   4546 C  C   . PHE B 1 107 ? 9.010   -0.852  61.665  1.00 43.55  ? 107  PHE B C   1 
ATOM   4547 O  O   . PHE B 1 107 ? 8.105   -0.741  62.485  1.00 46.87  ? 107  PHE B O   1 
ATOM   4548 C  CB  . PHE B 1 107 ? 8.773   -3.381  61.630  1.00 41.20  ? 107  PHE B CB  1 
ATOM   4549 C  CG  . PHE B 1 107 ? 8.806   -4.615  60.788  1.00 40.92  ? 107  PHE B CG  1 
ATOM   4550 C  CD1 . PHE B 1 107 ? 7.723   -4.930  59.971  1.00 38.52  ? 107  PHE B CD1 1 
ATOM   4551 C  CD2 . PHE B 1 107 ? 9.936   -5.408  60.722  1.00 38.09  ? 107  PHE B CD2 1 
ATOM   4552 C  CE1 . PHE B 1 107 ? 7.760   -6.041  59.152  1.00 36.84  ? 107  PHE B CE1 1 
ATOM   4553 C  CE2 . PHE B 1 107 ? 9.983   -6.525  59.891  1.00 36.89  ? 107  PHE B CE2 1 
ATOM   4554 C  CZ  . PHE B 1 107 ? 8.886   -6.844  59.112  1.00 39.52  ? 107  PHE B CZ  1 
ATOM   4555 N  N   . SER B 1 108 ? 9.879   0.124   61.422  1.00 44.83  ? 108  SER B N   1 
ATOM   4556 C  CA  . SER B 1 108 ? 9.717   1.445   62.013  1.00 46.24  ? 108  SER B CA  1 
ATOM   4557 C  C   . SER B 1 108 ? 8.561   2.186   61.340  1.00 51.68  ? 108  SER B C   1 
ATOM   4558 O  O   . SER B 1 108 ? 8.051   1.787   60.285  1.00 49.05  ? 108  SER B O   1 
ATOM   4559 C  CB  . SER B 1 108 ? 11.000  2.257   61.872  1.00 48.89  ? 108  SER B CB  1 
ATOM   4560 O  OG  . SER B 1 108 ? 11.258  2.546   60.513  1.00 49.30  ? 108  SER B OG  1 
ATOM   4561 N  N   . GLN B 1 109 ? 8.152   3.297   61.957  1.00 53.35  ? 109  GLN B N   1 
ATOM   4562 C  CA  . GLN B 1 109 ? 7.043   4.060   61.392  1.00 54.33  ? 109  GLN B CA  1 
ATOM   4563 C  C   . GLN B 1 109 ? 7.406   4.586   60.013  1.00 49.75  ? 109  GLN B C   1 
ATOM   4564 O  O   . GLN B 1 109 ? 6.588   4.541   59.086  1.00 48.87  ? 109  GLN B O   1 
ATOM   4565 C  CB  . GLN B 1 109 ? 6.653   5.203   62.329  1.00 59.15  ? 109  GLN B CB  1 
ATOM   4566 C  CG  . GLN B 1 109 ? 5.933   4.754   63.609  1.00 64.43  ? 109  GLN B CG  1 
ATOM   4567 C  CD  . GLN B 1 109 ? 4.841   3.707   63.385  1.00 70.57  ? 109  GLN B CD  1 
ATOM   4568 O  OE1 . GLN B 1 109 ? 4.928   2.864   62.489  1.00 70.64  ? 109  GLN B OE1 1 
ATOM   4569 N  NE2 . GLN B 1 109 ? 3.803   3.759   64.218  1.00 73.52  ? 109  GLN B NE2 1 
ATOM   4570 N  N   . GLN B 1 110 ? 8.636   5.071   59.848  1.00 50.02  ? 110  GLN B N   1 
ATOM   4571 C  CA  . GLN B 1 110 ? 9.048   5.543   58.534  1.00 52.14  ? 110  GLN B CA  1 
ATOM   4572 C  C   . GLN B 1 110 ? 9.104   4.411   57.519  1.00 50.42  ? 110  GLN B C   1 
ATOM   4573 O  O   . GLN B 1 110 ? 8.802   4.628   56.342  1.00 46.18  ? 110  GLN B O   1 
ATOM   4574 C  CB  . GLN B 1 110 ? 10.382  6.280   58.637  1.00 58.82  ? 110  GLN B CB  1 
ATOM   4575 C  CG  . GLN B 1 110 ? 10.323  7.429   59.647  1.00 66.49  ? 110  GLN B CG  1 
ATOM   4576 C  CD  . GLN B 1 110 ? 9.116   8.354   59.421  1.00 62.75  ? 110  GLN B CD  1 
ATOM   4577 O  OE1 . GLN B 1 110 ? 8.223   8.474   60.273  1.00 62.38  ? 110  GLN B OE1 1 
ATOM   4578 N  NE2 . GLN B 1 110 ? 9.100   9.021   58.273  1.00 63.61  ? 110  GLN B NE2 1 
ATOM   4579 N  N   . ALA B 1 111 ? 9.474   3.200   57.945  1.00 47.67  ? 111  ALA B N   1 
ATOM   4580 C  CA  . ALA B 1 111 ? 9.371   2.060   57.040  1.00 43.35  ? 111  ALA B CA  1 
ATOM   4581 C  C   . ALA B 1 111 ? 7.917   1.808   56.651  1.00 38.91  ? 111  ALA B C   1 
ATOM   4582 O  O   . ALA B 1 111 ? 7.617   1.538   55.482  1.00 43.22  ? 111  ALA B O   1 
ATOM   4583 C  CB  . ALA B 1 111 ? 9.980   0.814   57.683  1.00 44.07  ? 111  ALA B CB  1 
ATOM   4584 N  N   . MET B 1 112 ? 7.004   1.910   57.610  1.00 39.07  ? 112  MET B N   1 
ATOM   4585 C  CA  . MET B 1 112 ? 5.605   1.627   57.308  1.00 42.67  ? 112  MET B CA  1 
ATOM   4586 C  C   . MET B 1 112 ? 5.008   2.669   56.374  1.00 41.58  ? 112  MET B C   1 
ATOM   4587 O  O   . MET B 1 112 ? 4.213   2.333   55.485  1.00 39.26  ? 112  MET B O   1 
ATOM   4588 C  CB  . MET B 1 112 ? 4.805   1.533   58.595  1.00 45.82  ? 112  MET B CB  1 
ATOM   4589 C  CG  . MET B 1 112 ? 5.295   0.374   59.423  1.00 52.48  ? 112  MET B CG  1 
ATOM   4590 S  SD  . MET B 1 112 ? 4.465   -1.130  58.881  1.00 43.03  ? 112  MET B SD  1 
ATOM   4591 C  CE  . MET B 1 112 ? 3.019   -0.459  58.087  1.00 44.95  ? 112  MET B CE  1 
ATOM   4592 N  N   . LYS B 1 113 ? 5.364   3.942   56.562  1.00 38.51  ? 113  LYS B N   1 
ATOM   4593 C  CA  . LYS B 1 113 ? 4.962   4.948   55.586  1.00 38.88  ? 113  LYS B CA  1 
ATOM   4594 C  C   . LYS B 1 113 ? 5.458   4.581   54.197  1.00 41.62  ? 113  LYS B C   1 
ATOM   4595 O  O   . LYS B 1 113 ? 4.765   4.817   53.199  1.00 42.23  ? 113  LYS B O   1 
ATOM   4596 C  CB  . LYS B 1 113 ? 5.462   6.333   56.008  1.00 40.67  ? 113  LYS B CB  1 
ATOM   4597 C  CG  . LYS B 1 113 ? 4.863   6.789   57.319  1.00 41.04  ? 113  LYS B CG  1 
ATOM   4598 C  CD  . LYS B 1 113 ? 5.501   8.073   57.843  1.00 42.63  ? 113  LYS B CD  1 
ATOM   4599 C  CE  . LYS B 1 113 ? 4.816   8.517   59.138  1.00 50.22  ? 113  LYS B CE  1 
ATOM   4600 N  NZ  . LYS B 1 113 ? 5.490   9.682   59.779  1.00 56.15  ? 113  LYS B NZ  1 
ATOM   4601 N  N   . GLY B 1 114 ? 6.643   3.974   54.114  1.00 38.15  ? 114  GLY B N   1 
ATOM   4602 C  CA  . GLY B 1 114 ? 7.176   3.591   52.822  1.00 39.33  ? 114  GLY B CA  1 
ATOM   4603 C  C   . GLY B 1 114 ? 6.531   2.352   52.235  1.00 41.02  ? 114  GLY B C   1 
ATOM   4604 O  O   . GLY B 1 114 ? 6.542   2.173   51.012  1.00 44.57  ? 114  GLY B O   1 
ATOM   4605 N  N   . TYR B 1 115 ? 5.975   1.476   53.082  1.00 38.86  ? 115  TYR B N   1 
ATOM   4606 C  CA  . TYR B 1 115 ? 5.258   0.304   52.579  1.00 40.12  ? 115  TYR B CA  1 
ATOM   4607 C  C   . TYR B 1 115 ? 3.872   0.657   52.081  1.00 35.67  ? 115  TYR B C   1 
ATOM   4608 O  O   . TYR B 1 115 ? 3.296   -0.100  51.289  1.00 34.91  ? 115  TYR B O   1 
ATOM   4609 C  CB  . TYR B 1 115 ? 5.095   -0.775  53.663  1.00 35.02  ? 115  TYR B CB  1 
ATOM   4610 C  CG  . TYR B 1 115 ? 6.383   -1.389  54.167  1.00 36.79  ? 115  TYR B CG  1 
ATOM   4611 C  CD1 . TYR B 1 115 ? 7.436   -1.651  53.304  1.00 37.67  ? 115  TYR B CD1 1 
ATOM   4612 C  CD2 . TYR B 1 115 ? 6.541   -1.698  55.510  1.00 36.71  ? 115  TYR B CD2 1 
ATOM   4613 C  CE1 . TYR B 1 115 ? 8.609   -2.218  53.768  1.00 39.47  ? 115  TYR B CE1 1 
ATOM   4614 C  CE2 . TYR B 1 115 ? 7.705   -2.256  55.986  1.00 37.64  ? 115  TYR B CE2 1 
ATOM   4615 C  CZ  . TYR B 1 115 ? 8.737   -2.516  55.112  1.00 39.11  ? 115  TYR B CZ  1 
ATOM   4616 O  OH  . TYR B 1 115 ? 9.903   -3.074  55.597  1.00 43.39  ? 115  TYR B OH  1 
ATOM   4617 N  N   . HIS B 1 116 ? 3.342   1.795   52.517  1.00 35.47  ? 116  HIS B N   1 
ATOM   4618 C  CA  . HIS B 1 116 ? 1.918   2.070   52.358  1.00 35.19  ? 116  HIS B CA  1 
ATOM   4619 C  C   . HIS B 1 116 ? 1.471   1.998   50.898  1.00 36.24  ? 116  HIS B C   1 
ATOM   4620 O  O   . HIS B 1 116 ? 0.420   1.421   50.592  1.00 36.28  ? 116  HIS B O   1 
ATOM   4621 C  CB  . HIS B 1 116 ? 1.588   3.434   52.951  1.00 34.72  ? 116  HIS B CB  1 
ATOM   4622 C  CG  . HIS B 1 116 ? 0.151   3.794   52.802  1.00 35.37  ? 116  HIS B CG  1 
ATOM   4623 N  ND1 . HIS B 1 116 ? -0.803  3.421   53.720  1.00 33.89  ? 116  HIS B ND1 1 
ATOM   4624 C  CD2 . HIS B 1 116 ? -0.505  4.434   51.806  1.00 33.90  ? 116  HIS B CD2 1 
ATOM   4625 C  CE1 . HIS B 1 116 ? -1.988  3.835   53.306  1.00 34.38  ? 116  HIS B CE1 1 
ATOM   4626 N  NE2 . HIS B 1 116 ? -1.833  4.448   52.146  1.00 35.08  ? 116  HIS B NE2 1 
ATOM   4627 N  N   . ALA B 1 117 ? 2.217   2.622   49.984  1.00 32.44  ? 117  ALA B N   1 
ATOM   4628 C  CA  . ALA B 1 117 ? 1.729   2.663   48.602  1.00 37.10  ? 117  ALA B CA  1 
ATOM   4629 C  C   . ALA B 1 117 ? 1.646   1.267   47.995  1.00 36.02  ? 117  ALA B C   1 
ATOM   4630 O  O   . ALA B 1 117 ? 0.740   0.988   47.196  1.00 34.71  ? 117  ALA B O   1 
ATOM   4631 C  CB  . ALA B 1 117 ? 2.623   3.556   47.738  1.00 39.14  ? 117  ALA B CB  1 
ATOM   4632 N  N   A MET B 1 118 ? 2.578   0.375   48.344  0.60 35.28  ? 118  MET B N   1 
ATOM   4633 N  N   B MET B 1 118 ? 2.599   0.397   48.328  0.40 35.28  ? 118  MET B N   1 
ATOM   4634 C  CA  A MET B 1 118 ? 2.531   -0.975  47.797  0.60 34.92  ? 118  MET B CA  1 
ATOM   4635 C  CA  B MET B 1 118 ? 2.547   -0.969  47.828  0.40 34.93  ? 118  MET B CA  1 
ATOM   4636 C  C   A MET B 1 118 ? 1.430   -1.807  48.450  0.60 33.66  ? 118  MET B C   1 
ATOM   4637 C  C   B MET B 1 118 ? 1.353   -1.709  48.412  0.40 33.63  ? 118  MET B C   1 
ATOM   4638 O  O   A MET B 1 118 ? 0.907   -2.729  47.823  0.60 32.46  ? 118  MET B O   1 
ATOM   4639 O  O   B MET B 1 118 ? 0.673   -2.455  47.701  0.40 32.67  ? 118  MET B O   1 
ATOM   4640 C  CB  A MET B 1 118 ? 3.893   -1.654  47.960  0.60 36.61  ? 118  MET B CB  1 
ATOM   4641 C  CB  B MET B 1 118 ? 3.852   -1.692  48.156  0.40 36.59  ? 118  MET B CB  1 
ATOM   4642 C  CG  A MET B 1 118 ? 4.935   -1.227  46.931  0.60 36.24  ? 118  MET B CG  1 
ATOM   4643 C  CG  B MET B 1 118 ? 5.064   -1.156  47.416  0.40 37.34  ? 118  MET B CG  1 
ATOM   4644 S  SD  A MET B 1 118 ? 6.577   -1.893  47.318  0.60 39.59  ? 118  MET B SD  1 
ATOM   4645 S  SD  B MET B 1 118 ? 6.560   -1.378  48.406  0.40 38.51  ? 118  MET B SD  1 
ATOM   4646 C  CE  A MET B 1 118 ? 7.458   -1.531  45.793  0.60 41.49  ? 118  MET B CE  1 
ATOM   4647 C  CE  B MET B 1 118 ? 7.837   -1.221  47.157  0.40 41.27  ? 118  MET B CE  1 
ATOM   4648 N  N   . MET B 1 119 ? 1.076   -1.513  49.703  1.00 32.16  ? 119  MET B N   1 
ATOM   4649 C  CA  . MET B 1 119 ? -0.120  -2.112  50.280  1.00 29.79  ? 119  MET B CA  1 
ATOM   4650 C  C   . MET B 1 119 ? -1.354  -1.684  49.495  1.00 32.64  ? 119  MET B C   1 
ATOM   4651 O  O   . MET B 1 119 ? -2.221  -2.507  49.173  1.00 31.09  ? 119  MET B O   1 
ATOM   4652 C  CB  . MET B 1 119 ? -0.243  -1.675  51.733  1.00 29.14  ? 119  MET B CB  1 
ATOM   4653 C  CG  . MET B 1 119 ? 0.899   -2.158  52.639  1.00 31.95  ? 119  MET B CG  1 
ATOM   4654 S  SD  . MET B 1 119 ? 0.339   -2.112  54.339  1.00 32.57  ? 119  MET B SD  1 
ATOM   4655 C  CE  . MET B 1 119 ? 1.792   -2.800  55.140  1.00 33.26  ? 119  MET B CE  1 
ATOM   4656 N  N   . VAL B 1 120 ? -1.441  -0.397  49.166  1.00 32.01  ? 120  VAL B N   1 
ATOM   4657 C  CA  . VAL B 1 120 ? -2.604  0.082   48.421  1.00 31.86  ? 120  VAL B CA  1 
ATOM   4658 C  C   . VAL B 1 120 ? -2.667  -0.592  47.061  1.00 30.66  ? 120  VAL B C   1 
ATOM   4659 O  O   . VAL B 1 120 ? -3.753  -0.904  46.560  1.00 35.20  ? 120  VAL B O   1 
ATOM   4660 C  CB  . VAL B 1 120 ? -2.579  1.621   48.298  1.00 36.19  ? 120  VAL B CB  1 
ATOM   4661 C  CG1 . VAL B 1 120 ? -3.706  2.103   47.373  1.00 35.00  ? 120  VAL B CG1 1 
ATOM   4662 C  CG2 . VAL B 1 120 ? -2.716  2.279   49.672  1.00 34.44  ? 120  VAL B CG2 1 
ATOM   4663 N  N   . ASP B 1 121 ? -1.503  -0.816  46.434  1.00 31.25  ? 121  ASP B N   1 
ATOM   4664 C  CA  . ASP B 1 121 ? -1.460  -1.452  45.118  1.00 33.41  ? 121  ASP B CA  1 
ATOM   4665 C  C   . ASP B 1 121 ? -2.204  -2.789  45.128  1.00 32.75  ? 121  ASP B C   1 
ATOM   4666 O  O   . ASP B 1 121 ? -3.075  -3.041  44.283  1.00 32.98  ? 121  ASP B O   1 
ATOM   4667 C  CB  . ASP B 1 121 ? 0.007   -1.629  44.694  1.00 32.88  ? 121  ASP B CB  1 
ATOM   4668 C  CG  . ASP B 1 121 ? 0.163   -2.260  43.307  1.00 37.83  ? 121  ASP B CG  1 
ATOM   4669 O  OD1 . ASP B 1 121 ? -0.345  -3.386  43.086  1.00 33.30  ? 121  ASP B OD1 1 
ATOM   4670 O  OD2 . ASP B 1 121 ? 0.836   -1.646  42.440  1.00 35.53  ? 121  ASP B OD2 1 
ATOM   4671 N  N   . ILE B 1 122 ? -1.917  -3.639  46.123  1.00 31.47  ? 122  ILE B N   1 
ATOM   4672 C  CA  . ILE B 1 122 ? -2.561  -4.947  46.197  1.00 31.05  ? 122  ILE B CA  1 
ATOM   4673 C  C   . ILE B 1 122 ? -4.014  -4.801  46.644  1.00 33.94  ? 122  ILE B C   1 
ATOM   4674 O  O   . ILE B 1 122 ? -4.904  -5.525  46.166  1.00 31.63  ? 122  ILE B O   1 
ATOM   4675 C  CB  . ILE B 1 122 ? -1.773  -5.883  47.138  1.00 30.84  ? 122  ILE B CB  1 
ATOM   4676 C  CG1 . ILE B 1 122 ? -0.281  -5.955  46.763  1.00 29.96  ? 122  ILE B CG1 1 
ATOM   4677 C  CG2 . ILE B 1 122 ? -2.391  -7.277  47.179  1.00 30.46  ? 122  ILE B CG2 1 
ATOM   4678 C  CD1 . ILE B 1 122 ? 0.014   -6.333  45.299  1.00 32.63  ? 122  ILE B CD1 1 
ATOM   4679 N  N   . ALA B 1 123 ? -4.279  -3.876  47.571  1.00 31.75  ? 123  ALA B N   1 
ATOM   4680 C  CA  . ALA B 1 123 ? -5.648  -3.674  48.046  1.00 32.22  ? 123  ALA B CA  1 
ATOM   4681 C  C   . ALA B 1 123 ? -6.557  -3.255  46.902  1.00 31.24  ? 123  ALA B C   1 
ATOM   4682 O  O   . ALA B 1 123 ? -7.704  -3.713  46.806  1.00 32.26  ? 123  ALA B O   1 
ATOM   4683 C  CB  . ALA B 1 123 ? -5.681  -2.634  49.175  1.00 33.83  ? 123  ALA B CB  1 
ATOM   4684 N  N   . VAL B 1 124 ? -6.067  -2.383  46.026  1.00 33.01  ? 124  VAL B N   1 
ATOM   4685 C  CA  . VAL B 1 124 ? -6.848  -1.980  44.853  1.00 31.60  ? 124  VAL B CA  1 
ATOM   4686 C  C   . VAL B 1 124 ? -7.114  -3.176  43.942  1.00 32.41  ? 124  VAL B C   1 
ATOM   4687 O  O   . VAL B 1 124 ? -8.229  -3.343  43.425  1.00 32.18  ? 124  VAL B O   1 
ATOM   4688 C  CB  . VAL B 1 124 ? -6.135  -0.838  44.111  1.00 34.32  ? 124  VAL B CB  1 
ATOM   4689 C  CG1 . VAL B 1 124 ? -6.784  -0.598  42.744  1.00 34.76  ? 124  VAL B CG1 1 
ATOM   4690 C  CG2 . VAL B 1 124 ? -6.159  0.433   44.956  1.00 36.42  ? 124  VAL B CG2 1 
ATOM   4691 N  N   . GLN B 1 125 ? -6.116  -4.047  43.746  1.00 30.59  ? 125  GLN B N   1 
ATOM   4692 C  CA  . GLN B 1 125 ? -6.371  -5.263  42.972  1.00 32.24  ? 125  GLN B CA  1 
ATOM   4693 C  C   . GLN B 1 125 ? -7.500  -6.092  43.577  1.00 35.05  ? 125  GLN B C   1 
ATOM   4694 O  O   . GLN B 1 125 ? -8.292  -6.699  42.843  1.00 31.80  ? 125  GLN B O   1 
ATOM   4695 C  CB  . GLN B 1 125 ? -5.102  -6.106  42.858  1.00 31.07  ? 125  GLN B CB  1 
ATOM   4696 C  CG  . GLN B 1 125 ? -3.995  -5.426  42.056  1.00 31.93  ? 125  GLN B CG  1 
ATOM   4697 C  CD  . GLN B 1 125 ? -2.865  -6.400  41.756  1.00 32.59  ? 125  GLN B CD  1 
ATOM   4698 O  OE1 . GLN B 1 125 ? -3.105  -7.530  41.320  1.00 31.36  ? 125  GLN B OE1 1 
ATOM   4699 N  NE2 . GLN B 1 125 ? -1.628  -5.967  41.982  1.00 31.82  ? 125  GLN B NE2 1 
ATOM   4700 N  N   . LEU B 1 126 ? -7.585  -6.144  44.915  1.00 33.16  ? 126  LEU B N   1 
ATOM   4701 C  CA  . LEU B 1 126 ? -8.664  -6.890  45.563  1.00 31.74  ? 126  LEU B CA  1 
ATOM   4702 C  C   . LEU B 1 126 ? -10.018 -6.255  45.273  1.00 34.36  ? 126  LEU B C   1 
ATOM   4703 O  O   . LEU B 1 126 ? -10.971 -6.945  44.896  1.00 32.55  ? 126  LEU B O   1 
ATOM   4704 C  CB  . LEU B 1 126 ? -8.441  -6.968  47.079  1.00 29.68  ? 126  LEU B CB  1 
ATOM   4705 C  CG  . LEU B 1 126 ? -9.609  -7.620  47.849  1.00 32.01  ? 126  LEU B CG  1 
ATOM   4706 C  CD1 . LEU B 1 126 ? -9.693  -9.127  47.568  1.00 31.03  ? 126  LEU B CD1 1 
ATOM   4707 C  CD2 . LEU B 1 126 ? -9.529  -7.350  49.349  1.00 35.01  ? 126  LEU B CD2 1 
ATOM   4708 N  N   . VAL B 1 127 ? -10.132 -4.943  45.488  1.00 31.21  ? 127  VAL B N   1 
ATOM   4709 C  CA  . VAL B 1 127 ? -11.403 -4.257  45.255  1.00 32.85  ? 127  VAL B CA  1 
ATOM   4710 C  C   . VAL B 1 127 ? -11.817 -4.398  43.791  1.00 33.56  ? 127  VAL B C   1 
ATOM   4711 O  O   . VAL B 1 127 ? -13.000 -4.605  43.474  1.00 33.16  ? 127  VAL B O   1 
ATOM   4712 C  CB  . VAL B 1 127 ? -11.284 -2.781  45.683  1.00 32.42  ? 127  VAL B CB  1 
ATOM   4713 C  CG1 . VAL B 1 127 ? -12.512 -1.973  45.239  1.00 33.69  ? 127  VAL B CG1 1 
ATOM   4714 C  CG2 . VAL B 1 127 ? -11.081 -2.686  47.206  1.00 34.50  ? 127  VAL B CG2 1 
ATOM   4715 N  N   . GLN B 1 128 ? -10.843 -4.320  42.877  1.00 31.89  ? 128  GLN B N   1 
ATOM   4716 C  CA  . GLN B 1 128 ? -11.166 -4.399  41.455  1.00 32.76  ? 128  GLN B CA  1 
ATOM   4717 C  C   . GLN B 1 128 ? -11.661 -5.797  41.093  1.00 32.89  ? 128  GLN B C   1 
ATOM   4718 O  O   . GLN B 1 128 ? -12.585 -5.946  40.281  1.00 34.12  ? 128  GLN B O   1 
ATOM   4719 C  CB  . GLN B 1 128 ? -9.935  -4.007  40.623  1.00 32.68  ? 128  GLN B CB  1 
ATOM   4720 C  CG  . GLN B 1 128 ? -9.894  -2.509  40.349  1.00 40.79  ? 128  GLN B CG  1 
ATOM   4721 C  CD  . GLN B 1 128 ? -8.680  -2.035  39.573  1.00 48.37  ? 128  GLN B CD  1 
ATOM   4722 O  OE1 . GLN B 1 128 ? -7.623  -2.671  39.575  1.00 48.74  ? 128  GLN B OE1 1 
ATOM   4723 N  NE2 . GLN B 1 128 ? -8.830  -0.900  38.896  1.00 53.47  ? 128  GLN B NE2 1 
ATOM   4724 N  N   . LYS B 1 129 ? -11.071 -6.838  41.689  1.00 30.07  ? 129  LYS B N   1 
ATOM   4725 C  CA  . LYS B 1 129 ? -11.572 -8.187  41.450  1.00 32.42  ? 129  LYS B CA  1 
ATOM   4726 C  C   . LYS B 1 129 ? -13.044 -8.286  41.825  1.00 31.78  ? 129  LYS B C   1 
ATOM   4727 O  O   . LYS B 1 129 ? -13.861 -8.837  41.075  1.00 34.13  ? 129  LYS B O   1 
ATOM   4728 C  CB  . LYS B 1 129 ? -10.757 -9.218  42.236  1.00 32.15  ? 129  LYS B CB  1 
ATOM   4729 C  CG  . LYS B 1 129 ? -11.382 -10.620 42.178  1.00 34.57  ? 129  LYS B CG  1 
ATOM   4730 C  CD  . LYS B 1 129 ? -10.476 -11.707 42.718  1.00 36.15  ? 129  LYS B CD  1 
ATOM   4731 C  CE  . LYS B 1 129 ? -11.148 -13.083 42.664  1.00 37.63  ? 129  LYS B CE  1 
ATOM   4732 N  NZ  . LYS B 1 129 ? -10.243 -14.208 43.117  1.00 35.87  ? 129  LYS B NZ  1 
ATOM   4733 N  N   . TRP B 1 130 ? -13.398 -7.761  42.990  1.00 31.04  ? 130  TRP B N   1 
ATOM   4734 C  CA  . TRP B 1 130 ? -14.776 -7.879  43.466  1.00 29.27  ? 130  TRP B CA  1 
ATOM   4735 C  C   . TRP B 1 130 ? -15.724 -6.972  42.689  1.00 32.07  ? 130  TRP B C   1 
ATOM   4736 O  O   . TRP B 1 130 ? -16.894 -7.332  42.477  1.00 31.06  ? 130  TRP B O   1 
ATOM   4737 C  CB  . TRP B 1 130 ? -14.826 -7.569  44.964  1.00 32.20  ? 130  TRP B CB  1 
ATOM   4738 C  CG  . TRP B 1 130 ? -14.128 -8.598  45.793  1.00 34.00  ? 130  TRP B CG  1 
ATOM   4739 C  CD1 . TRP B 1 130 ? -13.504 -9.742  45.348  1.00 33.10  ? 130  TRP B CD1 1 
ATOM   4740 C  CD2 . TRP B 1 130 ? -13.953 -8.575  47.215  1.00 30.87  ? 130  TRP B CD2 1 
ATOM   4741 N  NE1 . TRP B 1 130 ? -12.980 -10.435 46.417  1.00 32.03  ? 130  TRP B NE1 1 
ATOM   4742 C  CE2 . TRP B 1 130 ? -13.236 -9.736  47.569  1.00 31.88  ? 130  TRP B CE2 1 
ATOM   4743 C  CE3 . TRP B 1 130 ? -14.341 -7.686  48.222  1.00 31.10  ? 130  TRP B CE3 1 
ATOM   4744 C  CZ2 . TRP B 1 130 ? -12.897 -10.029 48.891  1.00 33.13  ? 130  TRP B CZ2 1 
ATOM   4745 C  CZ3 . TRP B 1 130 ? -13.996 -7.982  49.537  1.00 31.54  ? 130  TRP B CZ3 1 
ATOM   4746 C  CH2 . TRP B 1 130 ? -13.287 -9.137  49.854  1.00 33.62  ? 130  TRP B CH2 1 
ATOM   4747 N  N   . GLU B 1 131 ? -15.266 -5.776  42.296  1.00 30.79  ? 131  GLU B N   1 
ATOM   4748 C  CA  . GLU B 1 131 ? -16.093 -4.925  41.434  1.00 33.92  ? 131  GLU B CA  1 
ATOM   4749 C  C   . GLU B 1 131 ? -16.451 -5.634  40.139  1.00 36.30  ? 131  GLU B C   1 
ATOM   4750 O  O   . GLU B 1 131 ? -17.494 -5.344  39.535  1.00 32.42  ? 131  GLU B O   1 
ATOM   4751 C  CB  . GLU B 1 131 ? -15.386 -3.616  41.072  1.00 35.74  ? 131  GLU B CB  1 
ATOM   4752 C  CG  . GLU B 1 131 ? -15.120 -2.653  42.244  1.00 37.71  ? 131  GLU B CG  1 
ATOM   4753 C  CD  . GLU B 1 131 ? -16.359 -1.894  42.685  1.00 38.88  ? 131  GLU B CD  1 
ATOM   4754 O  OE1 . GLU B 1 131 ? -17.484 -2.328  42.344  1.00 39.80  ? 131  GLU B OE1 1 
ATOM   4755 O  OE2 . GLU B 1 131 ? -16.209 -0.871  43.383  1.00 41.88  ? 131  GLU B OE2 1 
ATOM   4756 N  N   . ARG B 1 132 ? -15.592 -6.532  39.683  1.00 30.77  ? 132  ARG B N   1 
ATOM   4757 C  CA  . ARG B 1 132 ? -15.742 -7.116  38.357  1.00 32.42  ? 132  ARG B CA  1 
ATOM   4758 C  C   . ARG B 1 132 ? -16.505 -8.430  38.353  1.00 34.10  ? 132  ARG B C   1 
ATOM   4759 O  O   . ARG B 1 132 ? -16.669 -9.032  37.282  1.00 35.51  ? 132  ARG B O   1 
ATOM   4760 C  CB  . ARG B 1 132 ? -14.364 -7.297  37.722  1.00 32.15  ? 132  ARG B CB  1 
ATOM   4761 C  CG  . ARG B 1 132 ? -13.767 -5.954  37.368  1.00 32.36  ? 132  ARG B CG  1 
ATOM   4762 C  CD  . ARG B 1 132 ? -12.284 -6.037  37.006  1.00 32.63  ? 132  ARG B CD  1 
ATOM   4763 N  NE  . ARG B 1 132 ? -11.828 -4.728  36.556  1.00 31.76  ? 132  ARG B NE  1 
ATOM   4764 C  CZ  . ARG B 1 132 ? -10.554 -4.376  36.421  1.00 36.07  ? 132  ARG B CZ  1 
ATOM   4765 N  NH1 . ARG B 1 132 ? -9.575  -5.190  36.763  1.00 32.10  ? 132  ARG B NH1 1 
ATOM   4766 N  NH2 . ARG B 1 132 ? -10.260 -3.175  35.928  1.00 36.04  ? 132  ARG B NH2 1 
ATOM   4767 N  N   . LEU B 1 133 ? -16.999 -8.879  39.501  1.00 32.64  ? 133  LEU B N   1 
ATOM   4768 C  CA  . LEU B 1 133 ? -17.780 -10.105 39.533  1.00 30.36  ? 133  LEU B CA  1 
ATOM   4769 C  C   . LEU B 1 133 ? -19.145 -9.874  38.890  1.00 36.62  ? 133  LEU B C   1 
ATOM   4770 O  O   . LEU B 1 133 ? -19.684 -8.763  38.903  1.00 36.96  ? 133  LEU B O   1 
ATOM   4771 C  CB  . LEU B 1 133 ? -17.959 -10.597 40.970  1.00 35.61  ? 133  LEU B CB  1 
ATOM   4772 C  CG  . LEU B 1 133 ? -16.674 -10.939 41.720  1.00 33.51  ? 133  LEU B CG  1 
ATOM   4773 C  CD1 . LEU B 1 133 ? -17.011 -11.354 43.152  1.00 38.77  ? 133  LEU B CD1 1 
ATOM   4774 C  CD2 . LEU B 1 133 ? -15.883 -12.044 40.989  1.00 35.17  ? 133  LEU B CD2 1 
ATOM   4775 N  N   . ASN B 1 134 ? -19.692 -10.939 38.315  1.00 33.00  ? 134  ASN B N   1 
ATOM   4776 C  CA  . ASN B 1 134 ? -20.994 -10.891 37.670  1.00 33.32  ? 134  ASN B CA  1 
ATOM   4777 C  C   . ASN B 1 134 ? -22.108 -11.098 38.684  1.00 40.04  ? 134  ASN B C   1 
ATOM   4778 O  O   . ASN B 1 134 ? -21.882 -11.513 39.817  1.00 38.86  ? 134  ASN B O   1 
ATOM   4779 C  CB  . ASN B 1 134 ? -21.094 -11.954 36.586  1.00 32.22  ? 134  ASN B CB  1 
ATOM   4780 C  CG  . ASN B 1 134 ? -20.054 -11.776 35.523  1.00 33.16  ? 134  ASN B CG  1 
ATOM   4781 O  OD1 . ASN B 1 134 ? -20.059 -10.780 34.791  1.00 34.46  ? 134  ASN B OD1 1 
ATOM   4782 N  ND2 . ASN B 1 134 ? -19.159 -12.739 35.418  1.00 32.75  ? 134  ASN B ND2 1 
ATOM   4783 N  N   . ALA B 1 135 ? -23.334 -10.837 38.235  1.00 41.39  ? 135  ALA B N   1 
ATOM   4784 C  CA  . ALA B 1 135 ? -24.526 -11.030 39.045  1.00 47.28  ? 135  ALA B CA  1 
ATOM   4785 C  C   . ALA B 1 135 ? -24.468 -12.341 39.804  1.00 39.66  ? 135  ALA B C   1 
ATOM   4786 O  O   . ALA B 1 135 ? -24.239 -13.407 39.220  1.00 40.26  ? 135  ALA B O   1 
ATOM   4787 C  CB  . ALA B 1 135 ? -25.768 -10.999 38.148  1.00 45.75  ? 135  ALA B CB  1 
ATOM   4788 N  N   . ASP B 1 136 ? -24.635 -12.249 41.116  1.00 46.38  ? 136  ASP B N   1 
ATOM   4789 C  CA  . ASP B 1 136 ? -24.822 -13.378 42.016  1.00 45.12  ? 136  ASP B CA  1 
ATOM   4790 C  C   . ASP B 1 136 ? -23.627 -14.320 42.077  1.00 45.19  ? 136  ASP B C   1 
ATOM   4791 O  O   . ASP B 1 136 ? -23.741 -15.427 42.618  1.00 46.80  ? 136  ASP B O   1 
ATOM   4792 C  CB  . ASP B 1 136 ? -26.096 -14.137 41.654  1.00 53.49  ? 136  ASP B CB  1 
ATOM   4793 C  CG  . ASP B 1 136 ? -27.333 -13.424 42.160  1.00 57.50  ? 136  ASP B CG  1 
ATOM   4794 O  OD1 . ASP B 1 136 ? -27.276 -12.865 43.287  1.00 57.12  ? 136  ASP B OD1 1 
ATOM   4795 O  OD2 . ASP B 1 136 ? -28.335 -13.377 41.416  1.00 60.77  ? 136  ASP B OD2 1 
ATOM   4796 N  N   . GLU B 1 137 ? -22.478 -13.917 41.548  1.00 38.61  ? 137  GLU B N   1 
ATOM   4797 C  CA  . GLU B 1 137 ? -21.257 -14.611 41.915  1.00 35.95  ? 137  GLU B CA  1 
ATOM   4798 C  C   . GLU B 1 137 ? -20.904 -14.270 43.357  1.00 39.13  ? 137  GLU B C   1 
ATOM   4799 O  O   . GLU B 1 137 ? -21.375 -13.279 43.921  1.00 40.81  ? 137  GLU B O   1 
ATOM   4800 C  CB  . GLU B 1 137 ? -20.118 -14.235 40.964  1.00 34.81  ? 137  GLU B CB  1 
ATOM   4801 C  CG  . GLU B 1 137 ? -20.464 -14.619 39.530  1.00 37.92  ? 137  GLU B CG  1 
ATOM   4802 C  CD  . GLU B 1 137 ? -19.364 -14.336 38.524  1.00 38.51  ? 137  GLU B CD  1 
ATOM   4803 O  OE1 . GLU B 1 137 ? -18.458 -13.527 38.801  1.00 36.96  ? 137  GLU B OE1 1 
ATOM   4804 O  OE2 . GLU B 1 137 ? -19.434 -14.925 37.433  1.00 38.35  ? 137  GLU B OE2 1 
ATOM   4805 N  N   . HIS B 1 138 ? -20.089 -15.114 43.967  1.00 37.86  ? 138  HIS B N   1 
ATOM   4806 C  CA  . HIS B 1 138 ? -19.735 -14.892 45.360  1.00 35.27  ? 138  HIS B CA  1 
ATOM   4807 C  C   . HIS B 1 138 ? -18.224 -14.803 45.495  1.00 35.55  ? 138  HIS B C   1 
ATOM   4808 O  O   . HIS B 1 138 ? -17.473 -14.967 44.526  1.00 31.67  ? 138  HIS B O   1 
ATOM   4809 C  CB  . HIS B 1 138 ? -20.306 -15.997 46.254  1.00 36.34  ? 138  HIS B CB  1 
ATOM   4810 C  CG  . HIS B 1 138 ? -19.748 -17.356 45.976  1.00 37.12  ? 138  HIS B CG  1 
ATOM   4811 N  ND1 . HIS B 1 138 ? -20.367 -18.258 45.135  1.00 40.93  ? 138  HIS B ND1 1 
ATOM   4812 C  CD2 . HIS B 1 138 ? -18.643 -17.980 46.450  1.00 39.76  ? 138  HIS B CD2 1 
ATOM   4813 C  CE1 . HIS B 1 138 ? -19.661 -19.372 45.095  1.00 43.90  ? 138  HIS B CE1 1 
ATOM   4814 N  NE2 . HIS B 1 138 ? -18.605 -19.227 45.878  1.00 40.77  ? 138  HIS B NE2 1 
ATOM   4815 N  N   . ILE B 1 139 ? -17.806 -14.492 46.715  1.00 36.12  ? 139  ILE B N   1 
ATOM   4816 C  CA  . ILE B 1 139 ? -16.405 -14.296 47.072  1.00 33.47  ? 139  ILE B CA  1 
ATOM   4817 C  C   . ILE B 1 139 ? -15.990 -15.434 47.994  1.00 32.53  ? 139  ILE B C   1 
ATOM   4818 O  O   . ILE B 1 139 ? -16.695 -15.736 48.963  1.00 33.38  ? 139  ILE B O   1 
ATOM   4819 C  CB  . ILE B 1 139 ? -16.192 -12.946 47.776  1.00 35.74  ? 139  ILE B CB  1 
ATOM   4820 C  CG1 . ILE B 1 139 ? -16.402 -11.758 46.824  1.00 31.81  ? 139  ILE B CG1 1 
ATOM   4821 C  CG2 . ILE B 1 139 ? -14.838 -12.947 48.535  1.00 32.37  ? 139  ILE B CG2 1 
ATOM   4822 C  CD1 . ILE B 1 139 ? -16.800 -10.482 47.557  1.00 36.96  ? 139  ILE B CD1 1 
ATOM   4823 N  N   . GLU B 1 140 ? -14.838 -16.048 47.709  1.00 32.13  ? 140  GLU B N   1 
ATOM   4824 C  CA  . GLU B 1 140 ? -14.241 -17.044 48.596  1.00 33.27  ? 140  GLU B CA  1 
ATOM   4825 C  C   . GLU B 1 140 ? -13.294 -16.289 49.522  1.00 33.00  ? 140  GLU B C   1 
ATOM   4826 O  O   . GLU B 1 140 ? -12.227 -15.833 49.097  1.00 31.86  ? 140  GLU B O   1 
ATOM   4827 C  CB  . GLU B 1 140 ? -13.517 -18.135 47.806  1.00 36.83  ? 140  GLU B CB  1 
ATOM   4828 C  CG  . GLU B 1 140 ? -14.448 -18.878 46.835  1.00 37.78  ? 140  GLU B CG  1 
ATOM   4829 C  CD  . GLU B 1 140 ? -13.732 -19.957 46.047  1.00 43.82  ? 140  GLU B CD  1 
ATOM   4830 O  OE1 . GLU B 1 140 ? -12.507 -19.833 45.862  1.00 44.72  ? 140  GLU B OE1 1 
ATOM   4831 O  OE2 . GLU B 1 140 ? -14.391 -20.934 45.629  1.00 46.11  ? 140  GLU B OE2 1 
ATOM   4832 N  N   . VAL B 1 141 ? -13.707 -16.107 50.769  1.00 30.05  ? 141  VAL B N   1 
ATOM   4833 C  CA  . VAL B 1 141 ? -13.101 -15.056 51.585  1.00 29.93  ? 141  VAL B CA  1 
ATOM   4834 C  C   . VAL B 1 141 ? -11.672 -15.420 51.975  1.00 29.01  ? 141  VAL B C   1 
ATOM   4835 O  O   . VAL B 1 141 ? -10.749 -14.653 51.658  1.00 32.18  ? 141  VAL B O   1 
ATOM   4836 C  CB  . VAL B 1 141 ? -13.951 -14.748 52.821  1.00 31.61  ? 141  VAL B CB  1 
ATOM   4837 C  CG1 . VAL B 1 141 ? -13.186 -13.806 53.767  1.00 31.76  ? 141  VAL B CG1 1 
ATOM   4838 C  CG2 . VAL B 1 141 ? -15.283 -14.109 52.373  1.00 31.98  ? 141  VAL B CG2 1 
ATOM   4839 N  N   . PRO B 1 142 ? -11.431 -16.540 52.654  1.00 30.27  ? 142  PRO B N   1 
ATOM   4840 C  CA  . PRO B 1 142 ? -10.038 -16.841 53.044  1.00 30.11  ? 142  PRO B CA  1 
ATOM   4841 C  C   . PRO B 1 142 ? -9.124  -16.966 51.843  1.00 32.89  ? 142  PRO B C   1 
ATOM   4842 O  O   . PRO B 1 142 ? -7.939  -16.604 51.918  1.00 31.65  ? 142  PRO B O   1 
ATOM   4843 C  CB  . PRO B 1 142 ? -10.147 -18.167 53.803  1.00 31.76  ? 142  PRO B CB  1 
ATOM   4844 C  CG  . PRO B 1 142 ? -11.530 -18.722 53.453  1.00 35.11  ? 142  PRO B CG  1 
ATOM   4845 C  CD  . PRO B 1 142 ? -12.388 -17.516 53.209  1.00 34.08  ? 142  PRO B CD  1 
ATOM   4846 N  N   . GLU B 1 143 ? -9.649  -17.471 50.731  1.00 31.25  ? 143  GLU B N   1 
ATOM   4847 C  CA  . GLU B 1 143 ? -8.841  -17.589 49.518  1.00 31.93  ? 143  GLU B CA  1 
ATOM   4848 C  C   . GLU B 1 143 ? -8.390  -16.217 49.023  1.00 31.86  ? 143  GLU B C   1 
ATOM   4849 O  O   . GLU B 1 143 ? -7.215  -16.009 48.700  1.00 32.47  ? 143  GLU B O   1 
ATOM   4850 C  CB  . GLU B 1 143 ? -9.639  -18.321 48.435  1.00 32.22  ? 143  GLU B CB  1 
ATOM   4851 C  CG  . GLU B 1 143 ? -9.817  -19.800 48.713  1.00 38.90  ? 143  GLU B CG  1 
ATOM   4852 C  CD  . GLU B 1 143 ? -10.881 -20.116 49.773  1.00 38.17  ? 143  GLU B CD  1 
ATOM   4853 O  OE1 . GLU B 1 143 ? -11.676 -19.227 50.157  1.00 34.70  ? 143  GLU B OE1 1 
ATOM   4854 O  OE2 . GLU B 1 143 ? -10.920 -21.276 50.226  1.00 42.64  ? 143  GLU B OE2 1 
ATOM   4855 N  N   . ASP B 1 144 ? -9.313  -15.261 48.940  1.00 28.73  ? 144  ASP B N   1 
ATOM   4856 C  CA  . ASP B 1 144 ? -8.927  -13.940 48.458  1.00 29.09  ? 144  ASP B CA  1 
ATOM   4857 C  C   . ASP B 1 144 ? -8.113  -13.161 49.503  1.00 30.72  ? 144  ASP B C   1 
ATOM   4858 O  O   . ASP B 1 144 ? -7.272  -12.325 49.132  1.00 31.61  ? 144  ASP B O   1 
ATOM   4859 C  CB  . ASP B 1 144 ? -10.178 -13.157 48.048  1.00 32.22  ? 144  ASP B CB  1 
ATOM   4860 C  CG  . ASP B 1 144 ? -10.555 -13.381 46.601  1.00 32.68  ? 144  ASP B CG  1 
ATOM   4861 O  OD1 . ASP B 1 144 ? -9.721  -13.936 45.844  1.00 33.24  ? 144  ASP B OD1 1 
ATOM   4862 O  OD2 . ASP B 1 144 ? -11.679 -12.978 46.213  1.00 33.15  ? 144  ASP B OD2 1 
ATOM   4863 N  N   . MET B 1 145 ? -8.344  -13.404 50.804  1.00 32.90  ? 145  MET B N   1 
ATOM   4864 C  CA  . MET B 1 145 ? -7.519  -12.733 51.810  1.00 31.01  ? 145  MET B CA  1 
ATOM   4865 C  C   . MET B 1 145 ? -6.084  -13.245 51.755  1.00 31.53  ? 145  MET B C   1 
ATOM   4866 O  O   . MET B 1 145 ? -5.142  -12.471 51.947  1.00 34.28  ? 145  MET B O   1 
ATOM   4867 C  CB  . MET B 1 145 ? -8.105  -12.920 53.224  1.00 27.90  ? 145  MET B CB  1 
ATOM   4868 C  CG  . MET B 1 145 ? -9.498  -12.284 53.433  1.00 30.22  ? 145  MET B CG  1 
ATOM   4869 S  SD  . MET B 1 145 ? -9.511  -10.528 53.033  1.00 32.36  ? 145  MET B SD  1 
ATOM   4870 C  CE  . MET B 1 145 ? -10.221 -10.560 51.379  1.00 33.40  ? 145  MET B CE  1 
ATOM   4871 N  N   . THR B 1 146 ? -5.899  -14.523 51.436  1.00 28.65  ? 146  THR B N   1 
ATOM   4872 C  CA  . THR B 1 146 ? -4.539  -15.050 51.250  1.00 30.27  ? 146  THR B CA  1 
ATOM   4873 C  C   . THR B 1 146 ? -3.906  -14.510 49.970  1.00 32.19  ? 146  THR B C   1 
ATOM   4874 O  O   . THR B 1 146 ? -2.708  -14.210 49.943  1.00 30.56  ? 146  THR B O   1 
ATOM   4875 C  CB  . THR B 1 146 ? -4.567  -16.581 51.242  1.00 33.40  ? 146  THR B CB  1 
ATOM   4876 O  OG1 . THR B 1 146 ? -4.846  -17.071 52.562  1.00 35.10  ? 146  THR B OG1 1 
ATOM   4877 C  CG2 . THR B 1 146 ? -3.237  -17.160 50.758  1.00 33.08  ? 146  THR B CG2 1 
ATOM   4878 N  N   . ARG B 1 147 ? -4.685  -14.371 48.890  1.00 31.11  ? 147  ARG B N   1 
ATOM   4879 C  CA  . ARG B 1 147 ? -4.153  -13.688 47.714  1.00 28.58  ? 147  ARG B CA  1 
ATOM   4880 C  C   . ARG B 1 147 ? -3.629  -12.310 48.100  1.00 32.95  ? 147  ARG B C   1 
ATOM   4881 O  O   . ARG B 1 147 ? -2.511  -11.927 47.739  1.00 33.41  ? 147  ARG B O   1 
ATOM   4882 C  CB  . ARG B 1 147 ? -5.232  -13.552 46.631  1.00 30.58  ? 147  ARG B CB  1 
ATOM   4883 C  CG  . ARG B 1 147 ? -5.579  -14.855 45.926  1.00 31.37  ? 147  ARG B CG  1 
ATOM   4884 C  CD  . ARG B 1 147 ? -6.572  -14.582 44.783  1.00 31.51  ? 147  ARG B CD  1 
ATOM   4885 N  NE  . ARG B 1 147 ? -6.810  -15.787 43.994  1.00 36.16  ? 147  ARG B NE  1 
ATOM   4886 C  CZ  . ARG B 1 147 ? -7.752  -16.693 44.246  1.00 39.59  ? 147  ARG B CZ  1 
ATOM   4887 N  NH1 . ARG B 1 147 ? -8.642  -16.527 45.221  1.00 33.44  ? 147  ARG B NH1 1 
ATOM   4888 N  NH2 . ARG B 1 147 ? -7.804  -17.796 43.497  1.00 39.52  ? 147  ARG B NH2 1 
ATOM   4889 N  N   . LEU B 1 148 ? -4.423  -11.559 48.864  1.00 29.84  ? 148  LEU B N   1 
ATOM   4890 C  CA  . LEU B 1 148 ? -4.025  -10.203 49.216  1.00 31.19  ? 148  LEU B CA  1 
ATOM   4891 C  C   . LEU B 1 148 ? -2.801  -10.209 50.121  1.00 31.55  ? 148  LEU B C   1 
ATOM   4892 O  O   . LEU B 1 148 ? -1.847  -9.454  49.895  1.00 31.85  ? 148  LEU B O   1 
ATOM   4893 C  CB  . LEU B 1 148 ? -5.171  -9.469  49.911  1.00 34.42  ? 148  LEU B CB  1 
ATOM   4894 C  CG  . LEU B 1 148 ? -4.656  -8.105  50.394  1.00 35.52  ? 148  LEU B CG  1 
ATOM   4895 C  CD1 . LEU B 1 148 ? -5.420  -6.984  49.717  1.00 37.14  ? 148  LEU B CD1 1 
ATOM   4896 C  CD2 . LEU B 1 148 ? -4.686  -7.984  51.926  1.00 36.74  ? 148  LEU B CD2 1 
ATOM   4897 N  N   . THR B 1 149 ? -2.808  -11.038 51.164  1.00 31.49  ? 149  THR B N   1 
ATOM   4898 C  CA  . THR B 1 149 ? -1.734  -10.874 52.141  1.00 29.29  ? 149  THR B CA  1 
ATOM   4899 C  C   . THR B 1 149 ? -0.413  -11.431 51.631  1.00 30.96  ? 149  THR B C   1 
ATOM   4900 O  O   . THR B 1 149 ? 0.641   -10.856 51.921  1.00 29.57  ? 149  THR B O   1 
ATOM   4901 C  CB  . THR B 1 149 ? -2.094  -11.512 53.483  1.00 31.36  ? 149  THR B CB  1 
ATOM   4902 O  OG1 . THR B 1 149 ? -2.400  -12.899 53.299  1.00 32.40  ? 149  THR B OG1 1 
ATOM   4903 C  CG2 . THR B 1 149 ? -3.305  -10.783 54.120  1.00 31.16  ? 149  THR B CG2 1 
ATOM   4904 N  N   . LEU B 1 150 ? -0.430  -12.546 50.893  1.00 32.01  ? 150  LEU B N   1 
ATOM   4905 C  CA  . LEU B 1 150 ? 0.810   -13.019 50.273  1.00 31.97  ? 150  LEU B CA  1 
ATOM   4906 C  C   . LEU B 1 150 ? 1.374   -11.970 49.321  1.00 32.84  ? 150  LEU B C   1 
ATOM   4907 O  O   . LEU B 1 150 ? 2.573   -11.664 49.334  1.00 30.62  ? 150  LEU B O   1 
ATOM   4908 C  CB  . LEU B 1 150 ? 0.574   -14.331 49.522  1.00 32.35  ? 150  LEU B CB  1 
ATOM   4909 C  CG  . LEU B 1 150 ? 1.822   -14.871 48.818  1.00 34.05  ? 150  LEU B CG  1 
ATOM   4910 C  CD1 . LEU B 1 150 ? 2.788   -15.421 49.867  1.00 37.79  ? 150  LEU B CD1 1 
ATOM   4911 C  CD2 . LEU B 1 150 ? 1.452   -15.942 47.810  1.00 37.88  ? 150  LEU B CD2 1 
ATOM   4912 N  N   . ASP B 1 151 ? 0.524   -11.408 48.469  1.00 31.09  ? 151  ASP B N   1 
ATOM   4913 C  CA  . ASP B 1 151 ? 1.037   -10.428 47.525  1.00 30.12  ? 151  ASP B CA  1 
ATOM   4914 C  C   . ASP B 1 151 ? 1.574   -9.193  48.232  1.00 30.48  ? 151  ASP B C   1 
ATOM   4915 O  O   . ASP B 1 151 ? 2.557   -8.602  47.774  1.00 31.82  ? 151  ASP B O   1 
ATOM   4916 C  CB  . ASP B 1 151 ? -0.052  -10.063 46.514  1.00 31.84  ? 151  ASP B CB  1 
ATOM   4917 C  CG  . ASP B 1 151 ? -0.151  -11.085 45.406  1.00 31.37  ? 151  ASP B CG  1 
ATOM   4918 O  OD1 . ASP B 1 151 ? 0.223   -12.248 45.648  1.00 34.18  ? 151  ASP B OD1 1 
ATOM   4919 O  OD2 . ASP B 1 151 ? -0.597  -10.722 44.309  1.00 34.60  ? 151  ASP B OD2 1 
ATOM   4920 N  N   . THR B 1 152 ? 0.966   -8.801  49.353  1.00 29.46  ? 152  THR B N   1 
ATOM   4921 C  CA  . THR B 1 152 ? 1.430   -7.613  50.064  1.00 30.01  ? 152  THR B CA  1 
ATOM   4922 C  C   . THR B 1 152 ? 2.813   -7.831  50.677  1.00 32.23  ? 152  THR B C   1 
ATOM   4923 O  O   . THR B 1 152 ? 3.688   -6.966  50.549  1.00 32.26  ? 152  THR B O   1 
ATOM   4924 C  CB  . THR B 1 152 ? 0.407   -7.197  51.123  1.00 32.15  ? 152  THR B CB  1 
ATOM   4925 O  OG1 . THR B 1 152 ? -0.839  -6.910  50.460  1.00 31.29  ? 152  THR B OG1 1 
ATOM   4926 C  CG2 . THR B 1 152 ? 0.873   -5.919  51.857  1.00 30.46  ? 152  THR B CG2 1 
ATOM   4927 N  N   . ILE B 1 153 ? 3.043   -8.972  51.342  1.00 31.08  ? 153  ILE B N   1 
ATOM   4928 C  CA  . ILE B 1 153 ? 4.374   -9.177  51.921  1.00 31.70  ? 153  ILE B CA  1 
ATOM   4929 C  C   . ILE B 1 153 ? 5.403   -9.371  50.809  1.00 33.53  ? 153  ILE B C   1 
ATOM   4930 O  O   . ILE B 1 153 ? 6.538   -8.886  50.902  1.00 31.27  ? 153  ILE B O   1 
ATOM   4931 C  CB  . ILE B 1 153 ? 4.397   -10.331 52.952  1.00 31.05  ? 153  ILE B CB  1 
ATOM   4932 C  CG1 . ILE B 1 153 ? 5.759   -10.370 53.676  1.00 31.35  ? 153  ILE B CG1 1 
ATOM   4933 C  CG2 . ILE B 1 153 ? 4.123   -11.698 52.321  1.00 30.17  ? 153  ILE B CG2 1 
ATOM   4934 C  CD1 . ILE B 1 153 ? 6.044   -9.117  54.502  1.00 33.46  ? 153  ILE B CD1 1 
ATOM   4935 N  N   . GLY B 1 154 ? 5.024   -10.048 49.726  1.00 30.35  ? 154  GLY B N   1 
ATOM   4936 C  CA  . GLY B 1 154 ? 5.947   -10.184 48.606  1.00 31.43  ? 154  GLY B CA  1 
ATOM   4937 C  C   . GLY B 1 154 ? 6.364   -8.841  48.028  1.00 33.05  ? 154  GLY B C   1 
ATOM   4938 O  O   . GLY B 1 154 ? 7.551   -8.587  47.788  1.00 31.80  ? 154  GLY B O   1 
ATOM   4939 N  N   . LEU B 1 155 ? 5.397   -7.946  47.820  1.00 29.86  ? 155  LEU B N   1 
ATOM   4940 C  CA  . LEU B 1 155 ? 5.711   -6.668  47.187  1.00 30.52  ? 155  LEU B CA  1 
ATOM   4941 C  C   . LEU B 1 155 ? 6.388   -5.713  48.167  1.00 33.27  ? 155  LEU B C   1 
ATOM   4942 O  O   . LEU B 1 155 ? 7.462   -5.172  47.870  1.00 33.65  ? 155  LEU B O   1 
ATOM   4943 C  CB  . LEU B 1 155 ? 4.437   -6.041  46.596  1.00 34.75  ? 155  LEU B CB  1 
ATOM   4944 C  CG  . LEU B 1 155 ? 4.598   -4.760  45.763  1.00 33.11  ? 155  LEU B CG  1 
ATOM   4945 C  CD1 . LEU B 1 155 ? 5.516   -4.963  44.570  1.00 35.42  ? 155  LEU B CD1 1 
ATOM   4946 C  CD2 . LEU B 1 155 ? 3.223   -4.198  45.309  1.00 32.00  ? 155  LEU B CD2 1 
ATOM   4947 N  N   . CYS B 1 156 ? 5.789   -5.509  49.347  1.00 32.12  ? 156  CYS B N   1 
ATOM   4948 C  CA  . CYS B 1 156 ? 6.380   -4.615  50.340  1.00 31.69  ? 156  CYS B CA  1 
ATOM   4949 C  C   . CYS B 1 156 ? 7.726   -5.134  50.812  1.00 36.07  ? 156  CYS B C   1 
ATOM   4950 O  O   . CYS B 1 156 ? 8.672   -4.360  50.994  1.00 36.34  ? 156  CYS B O   1 
ATOM   4951 C  CB  . CYS B 1 156 ? 5.447   -4.454  51.544  1.00 34.26  ? 156  CYS B CB  1 
ATOM   4952 S  SG  . CYS B 1 156 ? 3.860   -3.693  51.137  1.00 37.09  ? 156  CYS B SG  1 
ATOM   4953 N  N   . GLY B 1 157 ? 7.825   -6.441  51.051  1.00 33.63  ? 157  GLY B N   1 
ATOM   4954 C  CA  . GLY B 1 157 ? 9.025   -6.960  51.685  1.00 32.65  ? 157  GLY B CA  1 
ATOM   4955 C  C   . GLY B 1 157 ? 10.128  -7.261  50.701  1.00 36.17  ? 157  GLY B C   1 
ATOM   4956 O  O   . GLY B 1 157 ? 11.310  -7.066  51.010  1.00 35.80  ? 157  GLY B O   1 
ATOM   4957 N  N   . PHE B 1 158 ? 9.769   -7.699  49.494  1.00 32.48  ? 158  PHE B N   1 
ATOM   4958 C  CA  . PHE B 1 158 ? 10.768  -8.229  48.587  1.00 30.07  ? 158  PHE B CA  1 
ATOM   4959 C  C   . PHE B 1 158 ? 10.700  -7.641  47.184  1.00 35.03  ? 158  PHE B C   1 
ATOM   4960 O  O   . PHE B 1 158 ? 11.440  -8.095  46.309  1.00 36.44  ? 158  PHE B O   1 
ATOM   4961 C  CB  . PHE B 1 158 ? 10.647  -9.756  48.558  1.00 31.50  ? 158  PHE B CB  1 
ATOM   4962 C  CG  . PHE B 1 158 ? 10.729  -10.368 49.935  1.00 34.74  ? 158  PHE B CG  1 
ATOM   4963 C  CD1 . PHE B 1 158 ? 11.955  -10.714 50.471  1.00 31.77  ? 158  PHE B CD1 1 
ATOM   4964 C  CD2 . PHE B 1 158 ? 9.589   -10.530 50.719  1.00 29.99  ? 158  PHE B CD2 1 
ATOM   4965 C  CE1 . PHE B 1 158 ? 12.057  -11.248 51.757  1.00 35.88  ? 158  PHE B CE1 1 
ATOM   4966 C  CE2 . PHE B 1 158 ? 9.673   -11.069 52.006  1.00 30.96  ? 158  PHE B CE2 1 
ATOM   4967 C  CZ  . PHE B 1 158 ? 10.919  -11.435 52.529  1.00 35.57  ? 158  PHE B CZ  1 
ATOM   4968 N  N   . ASN B 1 159 ? 9.887   -6.612  46.964  1.00 31.56  ? 159  ASN B N   1 
ATOM   4969 C  CA  . ASN B 1 159 ? 9.657   -6.074  45.619  1.00 34.17  ? 159  ASN B CA  1 
ATOM   4970 C  C   . ASN B 1 159 ? 9.435   -7.195  44.605  1.00 37.46  ? 159  ASN B C   1 
ATOM   4971 O  O   . ASN B 1 159 ? 9.929   -7.156  43.469  1.00 37.42  ? 159  ASN B O   1 
ATOM   4972 C  CB  . ASN B 1 159 ? 10.810  -5.159  45.190  1.00 36.06  ? 159  ASN B CB  1 
ATOM   4973 C  CG  . ASN B 1 159 ? 10.390  -4.161  44.132  1.00 46.22  ? 159  ASN B CG  1 
ATOM   4974 O  OD1 . ASN B 1 159 ? 9.196   -3.940  43.918  1.00 38.00  ? 159  ASN B OD1 1 
ATOM   4975 N  ND2 . ASN B 1 159 ? 11.366  -3.558  43.455  1.00 50.70  ? 159  ASN B ND2 1 
ATOM   4976 N  N   . TYR B 1 160 ? 8.672   -8.209  45.010  1.00 35.08  ? 160  TYR B N   1 
ATOM   4977 C  CA  . TYR B 1 160 ? 8.388   -9.358  44.166  1.00 32.60  ? 160  TYR B CA  1 
ATOM   4978 C  C   . TYR B 1 160 ? 6.880   -9.512  44.028  1.00 33.96  ? 160  TYR B C   1 
ATOM   4979 O  O   . TYR B 1 160 ? 6.175   -9.477  45.035  1.00 31.07  ? 160  TYR B O   1 
ATOM   4980 C  CB  . TYR B 1 160 ? 8.972   -10.636 44.758  1.00 34.61  ? 160  TYR B CB  1 
ATOM   4981 C  CG  . TYR B 1 160 ? 8.852   -11.847 43.860  1.00 38.89  ? 160  TYR B CG  1 
ATOM   4982 C  CD1 . TYR B 1 160 ? 9.777   -12.066 42.843  1.00 43.44  ? 160  TYR B CD1 1 
ATOM   4983 C  CD2 . TYR B 1 160 ? 7.831   -12.780 44.039  1.00 40.75  ? 160  TYR B CD2 1 
ATOM   4984 C  CE1 . TYR B 1 160 ? 9.689   -13.173 42.025  1.00 46.05  ? 160  TYR B CE1 1 
ATOM   4985 C  CE2 . TYR B 1 160 ? 7.736   -13.893 43.227  1.00 44.75  ? 160  TYR B CE2 1 
ATOM   4986 C  CZ  . TYR B 1 160 ? 8.665   -14.081 42.215  1.00 46.30  ? 160  TYR B CZ  1 
ATOM   4987 O  OH  . TYR B 1 160 ? 8.578   -15.197 41.402  1.00 52.74  ? 160  TYR B OH  1 
ATOM   4988 N  N   . ARG B 1 161 ? 6.387   -9.708  42.793  1.00 35.78  ? 161  ARG B N   1 
ATOM   4989 C  CA  . ARG B 1 161 ? 4.939   -9.805  42.554  1.00 31.78  ? 161  ARG B CA  1 
ATOM   4990 C  C   . ARG B 1 161 ? 4.528   -11.270 42.394  1.00 34.09  ? 161  ARG B C   1 
ATOM   4991 O  O   . ARG B 1 161 ? 4.845   -11.912 41.390  1.00 33.88  ? 161  ARG B O   1 
ATOM   4992 C  CB  . ARG B 1 161 ? 4.541   -8.957  41.345  1.00 34.86  ? 161  ARG B CB  1 
ATOM   4993 C  CG  . ARG B 1 161 ? 4.573   -7.466  41.675  1.00 35.13  ? 161  ARG B CG  1 
ATOM   4994 C  CD  . ARG B 1 161 ? 3.974   -6.592  40.597  1.00 37.51  ? 161  ARG B CD  1 
ATOM   4995 N  NE  . ARG B 1 161 ? 4.067   -5.181  40.947  1.00 34.56  ? 161  ARG B NE  1 
ATOM   4996 C  CZ  . ARG B 1 161 ? 3.087   -4.464  41.475  1.00 33.91  ? 161  ARG B CZ  1 
ATOM   4997 N  NH1 . ARG B 1 161 ? 1.898   -4.998  41.733  1.00 32.18  ? 161  ARG B NH1 1 
ATOM   4998 N  NH2 . ARG B 1 161 ? 3.296   -3.173  41.737  1.00 33.41  ? 161  ARG B NH2 1 
ATOM   4999 N  N   . PHE B 1 162 ? 3.806   -11.797 43.389  1.00 31.21  ? 162  PHE B N   1 
ATOM   5000 C  CA  . PHE B 1 162 ? 3.260   -13.141 43.265  1.00 33.71  ? 162  PHE B CA  1 
ATOM   5001 C  C   . PHE B 1 162 ? 2.098   -13.180 42.277  1.00 34.16  ? 162  PHE B C   1 
ATOM   5002 O  O   . PHE B 1 162 ? 1.761   -14.256 41.769  1.00 35.11  ? 162  PHE B O   1 
ATOM   5003 C  CB  . PHE B 1 162 ? 2.796   -13.657 44.632  1.00 34.85  ? 162  PHE B CB  1 
ATOM   5004 C  CG  . PHE B 1 162 ? 3.922   -13.989 45.581  1.00 35.49  ? 162  PHE B CG  1 
ATOM   5005 C  CD1 . PHE B 1 162 ? 4.666   -15.143 45.411  1.00 44.24  ? 162  PHE B CD1 1 
ATOM   5006 C  CD2 . PHE B 1 162 ? 4.199   -13.171 46.659  1.00 33.75  ? 162  PHE B CD2 1 
ATOM   5007 C  CE1 . PHE B 1 162 ? 5.705   -15.461 46.291  1.00 46.12  ? 162  PHE B CE1 1 
ATOM   5008 C  CE2 . PHE B 1 162 ? 5.243   -13.471 47.543  1.00 37.11  ? 162  PHE B CE2 1 
ATOM   5009 C  CZ  . PHE B 1 162 ? 5.992   -14.625 47.358  1.00 38.26  ? 162  PHE B CZ  1 
ATOM   5010 N  N   . ASN B 1 163 ? 1.490   -12.028 42.003  1.00 31.55  ? 163  ASN B N   1 
ATOM   5011 C  CA  . ASN B 1 163 ? 0.367   -11.919 41.065  1.00 30.71  ? 163  ASN B CA  1 
ATOM   5012 C  C   . ASN B 1 163 ? -0.731  -12.940 41.366  1.00 32.37  ? 163  ASN B C   1 
ATOM   5013 O  O   . ASN B 1 163 ? -1.274  -13.596 40.476  1.00 33.48  ? 163  ASN B O   1 
ATOM   5014 C  CB  . ASN B 1 163 ? 0.874   -12.016 39.626  1.00 32.27  ? 163  ASN B CB  1 
ATOM   5015 C  CG  . ASN B 1 163 ? 1.637   -10.778 39.238  1.00 31.57  ? 163  ASN B CG  1 
ATOM   5016 O  OD1 . ASN B 1 163 ? 1.170   -9.664  39.484  1.00 36.08  ? 163  ASN B OD1 1 
ATOM   5017 N  ND2 . ASN B 1 163 ? 2.829   -10.949 38.661  1.00 35.32  ? 163  ASN B ND2 1 
ATOM   5018 N  N   . SER B 1 164 ? -1.100  -13.014 42.650  1.00 30.64  ? 164  SER B N   1 
ATOM   5019 C  CA  . SER B 1 164 ? -2.081  -13.996 43.094  1.00 31.07  ? 164  SER B CA  1 
ATOM   5020 C  C   . SER B 1 164 ? -3.461  -13.726 42.514  1.00 35.32  ? 164  SER B C   1 
ATOM   5021 O  O   . SER B 1 164 ? -4.250  -14.663 42.361  1.00 33.67  ? 164  SER B O   1 
ATOM   5022 C  CB  . SER B 1 164 ? -2.165  -14.009 44.619  1.00 33.04  ? 164  SER B CB  1 
ATOM   5023 O  OG  . SER B 1 164 ? -0.946  -14.448 45.184  1.00 34.50  ? 164  SER B OG  1 
ATOM   5024 N  N   . PHE B 1 165 ? -3.781  -12.469 42.223  1.00 33.41  ? 165  PHE B N   1 
ATOM   5025 C  CA  . PHE B 1 165 ? -5.090  -12.172 41.647  1.00 32.79  ? 165  PHE B CA  1 
ATOM   5026 C  C   . PHE B 1 165 ? -5.149  -12.499 40.166  1.00 36.20  ? 165  PHE B C   1 
ATOM   5027 O  O   . PHE B 1 165 ? -6.230  -12.399 39.574  1.00 36.31  ? 165  PHE B O   1 
ATOM   5028 C  CB  . PHE B 1 165 ? -5.470  -10.708 41.901  1.00 31.52  ? 165  PHE B CB  1 
ATOM   5029 C  CG  . PHE B 1 165 ? -5.820  -10.432 43.344  1.00 33.13  ? 165  PHE B CG  1 
ATOM   5030 C  CD1 . PHE B 1 165 ? -6.977  -10.974 43.914  1.00 31.48  ? 165  PHE B CD1 1 
ATOM   5031 C  CD2 . PHE B 1 165 ? -4.969  -9.690  44.144  1.00 28.53  ? 165  PHE B CD2 1 
ATOM   5032 C  CE1 . PHE B 1 165 ? -7.287  -10.746 45.236  1.00 34.99  ? 165  PHE B CE1 1 
ATOM   5033 C  CE2 . PHE B 1 165 ? -5.281  -9.448  45.487  1.00 32.46  ? 165  PHE B CE2 1 
ATOM   5034 C  CZ  . PHE B 1 165 ? -6.435  -9.990  46.030  1.00 32.67  ? 165  PHE B CZ  1 
ATOM   5035 N  N   . TYR B 1 166 ? -4.035  -12.923 39.568  1.00 33.01  ? 166  TYR B N   1 
ATOM   5036 C  CA  . TYR B 1 166 ? -4.030  -13.418 38.193  1.00 34.51  ? 166  TYR B CA  1 
ATOM   5037 C  C   . TYR B 1 166 ? -4.185  -14.934 38.120  1.00 35.85  ? 166  TYR B C   1 
ATOM   5038 O  O   . TYR B 1 166 ? -4.055  -15.509 37.035  1.00 37.66  ? 166  TYR B O   1 
ATOM   5039 C  CB  . TYR B 1 166 ? -2.745  -12.963 37.482  1.00 35.54  ? 166  TYR B CB  1 
ATOM   5040 C  CG  . TYR B 1 166 ? -2.731  -11.472 37.297  1.00 34.33  ? 166  TYR B CG  1 
ATOM   5041 C  CD1 . TYR B 1 166 ? -2.330  -10.624 38.332  1.00 32.70  ? 166  TYR B CD1 1 
ATOM   5042 C  CD2 . TYR B 1 166 ? -3.187  -10.898 36.106  1.00 33.35  ? 166  TYR B CD2 1 
ATOM   5043 C  CE1 . TYR B 1 166 ? -2.341  -9.245  38.170  1.00 33.76  ? 166  TYR B CE1 1 
ATOM   5044 C  CE2 . TYR B 1 166 ? -3.210  -9.525  35.931  1.00 30.14  ? 166  TYR B CE2 1 
ATOM   5045 C  CZ  . TYR B 1 166 ? -2.792  -8.697  36.971  1.00 31.92  ? 166  TYR B CZ  1 
ATOM   5046 O  OH  . TYR B 1 166 ? -2.827  -7.332  36.808  1.00 33.97  ? 166  TYR B OH  1 
ATOM   5047 N  N   . ARG B 1 167 ? -4.475  -15.589 39.250  1.00 35.78  ? 167  ARG B N   1 
ATOM   5048 C  CA  . ARG B 1 167 ? -4.608  -17.037 39.327  1.00 38.38  ? 167  ARG B CA  1 
ATOM   5049 C  C   . ARG B 1 167 ? -5.953  -17.407 39.935  1.00 42.00  ? 167  ARG B C   1 
ATOM   5050 O  O   . ARG B 1 167 ? -6.369  -16.831 40.942  1.00 40.30  ? 167  ARG B O   1 
ATOM   5051 C  CB  . ARG B 1 167 ? -3.490  -17.666 40.174  1.00 40.47  ? 167  ARG B CB  1 
ATOM   5052 C  CG  . ARG B 1 167 ? -2.100  -17.180 39.820  1.00 41.11  ? 167  ARG B CG  1 
ATOM   5053 C  CD  . ARG B 1 167 ? -1.128  -17.457 40.949  1.00 44.21  ? 167  ARG B CD  1 
ATOM   5054 N  NE  . ARG B 1 167 ? 0.138   -16.774 40.722  1.00 49.40  ? 167  ARG B NE  1 
ATOM   5055 C  CZ  . ARG B 1 167 ? 1.160   -17.299 40.061  1.00 51.20  ? 167  ARG B CZ  1 
ATOM   5056 N  NH1 . ARG B 1 167 ? 1.131   -18.550 39.623  1.00 51.47  ? 167  ARG B NH1 1 
ATOM   5057 N  NH2 . ARG B 1 167 ? 2.241   -16.555 39.845  1.00 48.09  ? 167  ARG B NH2 1 
ATOM   5058 N  N   . ASP B 1 168 ? -6.629  -18.375 39.320  1.00 39.73  ? 168  ASP B N   1 
ATOM   5059 C  CA  . ASP B 1 168 ? -7.870  -18.906 39.872  1.00 42.73  ? 168  ASP B CA  1 
ATOM   5060 C  C   . ASP B 1 168 ? -7.631  -20.039 40.862  1.00 46.19  ? 168  ASP B C   1 
ATOM   5061 O  O   . ASP B 1 168 ? -8.518  -20.338 41.667  1.00 47.16  ? 168  ASP B O   1 
ATOM   5062 C  CB  . ASP B 1 168 ? -8.796  -19.369 38.734  1.00 40.45  ? 168  ASP B CB  1 
ATOM   5063 C  CG  . ASP B 1 168 ? -8.150  -20.416 37.844  1.00 46.57  ? 168  ASP B CG  1 
ATOM   5064 O  OD1 . ASP B 1 168 ? -7.335  -20.039 36.975  1.00 50.40  ? 168  ASP B OD1 1 
ATOM   5065 O  OD2 . ASP B 1 168 ? -8.429  -21.621 38.023  1.00 56.15  ? 168  ASP B OD2 1 
ATOM   5066 N  N   . GLN B 1 169 ? -6.459  -20.653 40.826  1.00 43.27  ? 169  GLN B N   1 
ATOM   5067 C  CA  . GLN B 1 169 ? -5.976  -21.650 41.760  1.00 48.89  ? 169  GLN B CA  1 
ATOM   5068 C  C   . GLN B 1 169 ? -5.015  -21.000 42.742  1.00 49.47  ? 169  GLN B C   1 
ATOM   5069 O  O   . GLN B 1 169 ? -4.493  -19.913 42.481  1.00 46.23  ? 169  GLN B O   1 
ATOM   5070 C  CB  . GLN B 1 169 ? -5.273  -22.776 40.997  1.00 55.27  ? 169  GLN B CB  1 
ATOM   5071 C  CG  . GLN B 1 169 ? -5.939  -24.143 41.133  1.00 68.67  ? 169  GLN B CG  1 
ATOM   5072 C  CD  . GLN B 1 169 ? -4.992  -25.290 40.810  1.00 76.35  ? 169  GLN B CD  1 
ATOM   5073 O  OE1 . GLN B 1 169 ? -4.774  -25.617 39.638  1.00 77.23  ? 169  GLN B OE1 1 
ATOM   5074 N  NE2 . GLN B 1 169 ? -4.425  -25.905 41.846  1.00 72.19  ? 169  GLN B NE2 1 
ATOM   5075 N  N   . PRO B 1 170 ? -4.759  -21.621 43.894  1.00 51.66  ? 170  PRO B N   1 
ATOM   5076 C  CA  . PRO B 1 170 ? -3.791  -21.035 44.826  1.00 48.65  ? 170  PRO B CA  1 
ATOM   5077 C  C   . PRO B 1 170 ? -2.415  -20.966 44.188  1.00 46.68  ? 170  PRO B C   1 
ATOM   5078 O  O   . PRO B 1 170 ? -2.045  -21.799 43.353  1.00 45.43  ? 170  PRO B O   1 
ATOM   5079 C  CB  . PRO B 1 170 ? -3.807  -22.000 46.023  1.00 48.83  ? 170  PRO B CB  1 
ATOM   5080 C  CG  . PRO B 1 170 ? -5.058  -22.779 45.881  1.00 50.27  ? 170  PRO B CG  1 
ATOM   5081 C  CD  . PRO B 1 170 ? -5.322  -22.879 44.405  1.00 46.82  ? 170  PRO B CD  1 
ATOM   5082 N  N   . HIS B 1 171 ? -1.662  -19.941 44.568  1.00 44.48  ? 171  HIS B N   1 
ATOM   5083 C  CA  . HIS B 1 171 ? -0.272  -19.869 44.149  1.00 43.97  ? 171  HIS B CA  1 
ATOM   5084 C  C   . HIS B 1 171 ? 0.455   -21.138 44.590  1.00 46.61  ? 171  HIS B C   1 
ATOM   5085 O  O   . HIS B 1 171 ? 0.174   -21.669 45.673  1.00 41.88  ? 171  HIS B O   1 
ATOM   5086 C  CB  . HIS B 1 171 ? 0.409   -18.637 44.750  1.00 44.55  ? 171  HIS B CB  1 
ATOM   5087 C  CG  . HIS B 1 171 ? 1.753   -18.343 44.164  1.00 42.71  ? 171  HIS B CG  1 
ATOM   5088 N  ND1 . HIS B 1 171 ? 2.868   -19.105 44.435  1.00 46.89  ? 171  HIS B ND1 1 
ATOM   5089 C  CD2 . HIS B 1 171 ? 2.163   -17.367 43.319  1.00 45.50  ? 171  HIS B CD2 1 
ATOM   5090 C  CE1 . HIS B 1 171 ? 3.907   -18.615 43.782  1.00 48.48  ? 171  HIS B CE1 1 
ATOM   5091 N  NE2 . HIS B 1 171 ? 3.505   -17.561 43.094  1.00 46.74  ? 171  HIS B NE2 1 
ATOM   5092 N  N   . PRO B 1 172 ? 1.391   -21.650 43.786  1.00 44.91  ? 172  PRO B N   1 
ATOM   5093 C  CA  . PRO B 1 172 ? 2.091   -22.889 44.171  1.00 44.69  ? 172  PRO B CA  1 
ATOM   5094 C  C   . PRO B 1 172 ? 2.798   -22.805 45.516  1.00 44.76  ? 172  PRO B C   1 
ATOM   5095 O  O   . PRO B 1 172 ? 2.904   -23.817 46.232  1.00 41.64  ? 172  PRO B O   1 
ATOM   5096 C  CB  . PRO B 1 172 ? 3.094   -23.085 43.028  1.00 46.29  ? 172  PRO B CB  1 
ATOM   5097 C  CG  . PRO B 1 172 ? 2.489   -22.398 41.871  1.00 46.86  ? 172  PRO B CG  1 
ATOM   5098 C  CD  . PRO B 1 172 ? 1.695   -21.238 42.404  1.00 50.05  ? 172  PRO B CD  1 
ATOM   5099 N  N   . PHE B 1 173 ? 3.312   -21.631 45.878  1.00 43.30  ? 173  PHE B N   1 
ATOM   5100 C  CA  . PHE B 1 173 ? 3.936   -21.508 47.186  1.00 39.33  ? 173  PHE B CA  1 
ATOM   5101 C  C   . PHE B 1 173 ? 2.912   -21.769 48.275  1.00 36.80  ? 173  PHE B C   1 
ATOM   5102 O  O   . PHE B 1 173 ? 3.219   -22.407 49.287  1.00 39.26  ? 173  PHE B O   1 
ATOM   5103 C  CB  . PHE B 1 173 ? 4.558   -20.122 47.350  1.00 40.23  ? 173  PHE B CB  1 
ATOM   5104 C  CG  . PHE B 1 173 ? 5.244   -19.915 48.672  1.00 40.25  ? 173  PHE B CG  1 
ATOM   5105 C  CD1 . PHE B 1 173 ? 4.541   -19.449 49.768  1.00 40.62  ? 173  PHE B CD1 1 
ATOM   5106 C  CD2 . PHE B 1 173 ? 6.594   -20.158 48.807  1.00 38.61  ? 173  PHE B CD2 1 
ATOM   5107 C  CE1 . PHE B 1 173 ? 5.183   -19.252 50.985  1.00 36.56  ? 173  PHE B CE1 1 
ATOM   5108 C  CE2 . PHE B 1 173 ? 7.236   -19.953 50.005  1.00 38.99  ? 173  PHE B CE2 1 
ATOM   5109 C  CZ  . PHE B 1 173 ? 6.523   -19.496 51.098  1.00 40.39  ? 173  PHE B CZ  1 
ATOM   5110 N  N   . ILE B 1 174 ? 1.680   -21.299 48.071  1.00 36.21  ? 174  ILE B N   1 
ATOM   5111 C  CA  . ILE B 1 174 ? 0.632   -21.505 49.060  1.00 38.36  ? 174  ILE B CA  1 
ATOM   5112 C  C   . ILE B 1 174 ? 0.269   -22.977 49.152  1.00 37.41  ? 174  ILE B C   1 
ATOM   5113 O  O   . ILE B 1 174 ? 0.084   -23.510 50.247  1.00 35.94  ? 174  ILE B O   1 
ATOM   5114 C  CB  . ILE B 1 174 ? -0.602  -20.647 48.738  1.00 35.72  ? 174  ILE B CB  1 
ATOM   5115 C  CG1 . ILE B 1 174 ? -0.254  -19.154 48.846  1.00 37.64  ? 174  ILE B CG1 1 
ATOM   5116 C  CG2 . ILE B 1 174 ? -1.753  -21.020 49.664  1.00 38.20  ? 174  ILE B CG2 1 
ATOM   5117 C  CD1 . ILE B 1 174 ? 0.236   -18.720 50.248  1.00 33.99  ? 174  ILE B CD1 1 
ATOM   5118 N  N   . THR B 1 175 ? 0.155   -23.660 48.012  1.00 37.42  ? 175  THR B N   1 
ATOM   5119 C  CA  . THR B 1 175 ? -0.176  -25.081 48.057  1.00 39.00  ? 175  THR B CA  1 
ATOM   5120 C  C   . THR B 1 175 ? 0.846   -25.858 48.878  1.00 38.26  ? 175  THR B C   1 
ATOM   5121 O  O   . THR B 1 175 ? 0.485   -26.666 49.742  1.00 36.64  ? 175  THR B O   1 
ATOM   5122 C  CB  . THR B 1 175 ? -0.270  -25.645 46.642  1.00 40.03  ? 175  THR B CB  1 
ATOM   5123 O  OG1 . THR B 1 175 ? -1.347  -24.997 45.961  1.00 42.02  ? 175  THR B OG1 1 
ATOM   5124 C  CG2 . THR B 1 175 ? -0.542  -27.142 46.696  1.00 38.77  ? 175  THR B CG2 1 
ATOM   5125 N  N   . SER B 1 176 ? 2.135   -25.611 48.640  1.00 36.83  ? 176  SER B N   1 
ATOM   5126 C  CA  . SER B 1 176 ? 3.162   -26.349 49.367  1.00 37.63  ? 176  SER B CA  1 
ATOM   5127 C  C   . SER B 1 176 ? 3.297   -25.874 50.810  1.00 35.68  ? 176  SER B C   1 
ATOM   5128 O  O   . SER B 1 176 ? 3.598   -26.682 51.699  1.00 34.45  ? 176  SER B O   1 
ATOM   5129 C  CB  . SER B 1 176 ? 4.508   -26.229 48.640  1.00 37.79  ? 176  SER B CB  1 
ATOM   5130 O  OG  . SER B 1 176 ? 4.511   -27.013 47.460  1.00 39.93  ? 176  SER B OG  1 
ATOM   5131 N  N   . MET B 1 177 ? 3.086   -24.580 51.069  1.00 34.05  ? 177  MET B N   1 
ATOM   5132 C  CA  . MET B 1 177 ? 3.125   -24.096 52.444  1.00 33.32  ? 177  MET B CA  1 
ATOM   5133 C  C   . MET B 1 177 ? 2.005   -24.708 53.274  1.00 34.26  ? 177  MET B C   1 
ATOM   5134 O  O   . MET B 1 177 ? 2.238   -25.191 54.385  1.00 33.99  ? 177  MET B O   1 
ATOM   5135 C  CB  . MET B 1 177 ? 3.036   -22.571 52.486  1.00 32.25  ? 177  MET B CB  1 
ATOM   5136 C  CG  . MET B 1 177 ? 2.935   -22.059 53.930  1.00 35.51  ? 177  MET B CG  1 
ATOM   5137 S  SD  . MET B 1 177 ? 2.216   -20.415 54.095  1.00 37.52  ? 177  MET B SD  1 
ATOM   5138 C  CE  . MET B 1 177 ? 0.469   -20.759 53.781  1.00 34.25  ? 177  MET B CE  1 
ATOM   5139 N  N   . VAL B 1 178 ? 0.775   -24.702 52.748  1.00 35.09  ? 178  VAL B N   1 
ATOM   5140 C  CA  . VAL B 1 178 ? -0.342  -25.272 53.499  1.00 36.47  ? 178  VAL B CA  1 
ATOM   5141 C  C   . VAL B 1 178 ? -0.101  -26.752 53.767  1.00 37.36  ? 178  VAL B C   1 
ATOM   5142 O  O   . VAL B 1 178 ? -0.294  -27.239 54.891  1.00 37.19  ? 178  VAL B O   1 
ATOM   5143 C  CB  . VAL B 1 178 ? -1.666  -25.035 52.752  1.00 35.63  ? 178  VAL B CB  1 
ATOM   5144 C  CG1 . VAL B 1 178 ? -2.792  -25.843 53.390  1.00 38.93  ? 178  VAL B CG1 1 
ATOM   5145 C  CG2 . VAL B 1 178 ? -2.000  -23.527 52.734  1.00 35.84  ? 178  VAL B CG2 1 
ATOM   5146 N  N   . ARG B 1 179 ? 0.359   -27.484 52.753  1.00 36.92  ? 179  ARG B N   1 
ATOM   5147 C  CA  . ARG B 1 179 ? 0.593   -28.913 52.925  1.00 35.70  ? 179  ARG B CA  1 
ATOM   5148 C  C   . ARG B 1 179 ? 1.698   -29.169 53.937  1.00 36.35  ? 179  ARG B C   1 
ATOM   5149 O  O   . ARG B 1 179 ? 1.644   -30.147 54.692  1.00 36.08  ? 179  ARG B O   1 
ATOM   5150 C  CB  . ARG B 1 179 ? 0.931   -29.549 51.577  1.00 40.72  ? 179  ARG B CB  1 
ATOM   5151 C  CG  . ARG B 1 179 ? 0.665   -31.040 51.516  1.00 42.72  ? 179  ARG B CG  1 
ATOM   5152 C  CD  . ARG B 1 179 ? 0.397   -31.475 50.062  1.00 43.61  ? 179  ARG B CD  1 
ATOM   5153 N  NE  . ARG B 1 179 ? 1.424   -30.972 49.153  1.00 40.76  ? 179  ARG B NE  1 
ATOM   5154 C  CZ  . ARG B 1 179 ? 1.209   -30.656 47.884  1.00 47.04  ? 179  ARG B CZ  1 
ATOM   5155 N  NH1 . ARG B 1 179 ? 0.027   -30.843 47.313  1.00 47.91  ? 179  ARG B NH1 1 
ATOM   5156 N  NH2 . ARG B 1 179 ? 2.204   -30.141 47.166  1.00 42.13  ? 179  ARG B NH2 1 
ATOM   5157 N  N   . ALA B 1 180 ? 2.708   -28.297 53.973  1.00 33.25  ? 180  ALA B N   1 
ATOM   5158 C  CA  . ALA B 1 180 ? 3.784   -28.456 54.944  1.00 35.18  ? 180  ALA B CA  1 
ATOM   5159 C  C   . ALA B 1 180 ? 3.295   -28.159 56.359  1.00 36.78  ? 180  ALA B C   1 
ATOM   5160 O  O   . ALA B 1 180 ? 3.609   -28.898 57.301  1.00 34.17  ? 180  ALA B O   1 
ATOM   5161 C  CB  . ALA B 1 180 ? 4.955   -27.544 54.564  1.00 38.74  ? 180  ALA B CB  1 
ATOM   5162 N  N   . LEU B 1 181 ? 2.522   -27.082 56.525  1.00 33.15  ? 181  LEU B N   1 
ATOM   5163 C  CA  . LEU B 1 181 ? 1.915   -26.803 57.821  1.00 33.09  ? 181  LEU B CA  1 
ATOM   5164 C  C   . LEU B 1 181 ? 0.984   -27.932 58.237  1.00 36.40  ? 181  LEU B C   1 
ATOM   5165 O  O   . LEU B 1 181 ? 0.965   -28.322 59.409  1.00 36.25  ? 181  LEU B O   1 
ATOM   5166 C  CB  . LEU B 1 181 ? 1.148   -25.476 57.777  1.00 31.67  ? 181  LEU B CB  1 
ATOM   5167 C  CG  . LEU B 1 181 ? 2.035   -24.247 57.557  1.00 30.57  ? 181  LEU B CG  1 
ATOM   5168 C  CD1 . LEU B 1 181 ? 1.160   -23.007 57.358  1.00 35.18  ? 181  LEU B CD1 1 
ATOM   5169 C  CD2 . LEU B 1 181 ? 3.006   -24.079 58.740  1.00 35.28  ? 181  LEU B CD2 1 
ATOM   5170 N  N   . ASP B 1 182 ? 0.182   -28.452 57.292  1.00 35.40  ? 182  ASP B N   1 
ATOM   5171 C  CA  . ASP B 1 182 ? -0.667  -29.607 57.592  1.00 41.00  ? 182  ASP B CA  1 
ATOM   5172 C  C   . ASP B 1 182 ? 0.161   -30.766 58.114  1.00 34.95  ? 182  ASP B C   1 
ATOM   5173 O  O   . ASP B 1 182 ? -0.207  -31.428 59.091  1.00 36.55  ? 182  ASP B O   1 
ATOM   5174 C  CB  . ASP B 1 182 ? -1.419  -30.078 56.350  1.00 41.08  ? 182  ASP B CB  1 
ATOM   5175 C  CG  . ASP B 1 182 ? -2.619  -29.246 56.036  1.00 50.17  ? 182  ASP B CG  1 
ATOM   5176 O  OD1 . ASP B 1 182 ? -3.306  -28.797 56.979  1.00 59.47  ? 182  ASP B OD1 1 
ATOM   5177 O  OD2 . ASP B 1 182 ? -2.914  -29.112 54.827  1.00 53.03  ? 182  ASP B OD2 1 
ATOM   5178 N  N   . GLU B 1 183 ? 1.259   -31.059 57.435  1.00 35.21  ? 183  GLU B N   1 
ATOM   5179 C  CA  . GLU B 1 183 ? 2.081   -32.191 57.831  1.00 35.53  ? 183  GLU B CA  1 
ATOM   5180 C  C   . GLU B 1 183 ? 2.645   -31.975 59.232  1.00 37.55  ? 183  GLU B C   1 
ATOM   5181 O  O   . GLU B 1 183 ? 2.604   -32.875 60.077  1.00 36.83  ? 183  GLU B O   1 
ATOM   5182 C  CB  . GLU B 1 183 ? 3.185   -32.398 56.793  1.00 37.48  ? 183  GLU B CB  1 
ATOM   5183 C  CG  . GLU B 1 183 ? 4.288   -33.347 57.236  1.00 40.82  ? 183  GLU B CG  1 
ATOM   5184 C  CD  . GLU B 1 183 ? 3.841   -34.804 57.313  1.00 43.22  ? 183  GLU B CD  1 
ATOM   5185 O  OE1 . GLU B 1 183 ? 2.661   -35.101 57.006  1.00 41.22  ? 183  GLU B OE1 1 
ATOM   5186 O  OE2 . GLU B 1 183 ? 4.683   -35.643 57.710  1.00 42.72  ? 183  GLU B OE2 1 
ATOM   5187 N  N   . ALA B 1 184 ? 3.160   -30.769 59.504  1.00 37.10  ? 184  ALA B N   1 
ATOM   5188 C  CA  . ALA B 1 184 ? 3.677   -30.484 60.840  1.00 33.74  ? 184  ALA B CA  1 
ATOM   5189 C  C   . ALA B 1 184 ? 2.602   -30.677 61.898  1.00 36.64  ? 184  ALA B C   1 
ATOM   5190 O  O   . ALA B 1 184 ? 2.887   -31.153 63.000  1.00 37.62  ? 184  ALA B O   1 
ATOM   5191 C  CB  . ALA B 1 184 ? 4.243   -29.063 60.911  1.00 37.63  ? 184  ALA B CB  1 
ATOM   5192 N  N   . MET B 1 185 ? 1.352   -30.332 61.582  1.00 33.05  ? 185  MET B N   1 
ATOM   5193 C  CA  . MET B 1 185 ? 0.348   -30.436 62.628  1.00 31.16  ? 185  MET B CA  1 
ATOM   5194 C  C   . MET B 1 185 ? -0.074  -31.895 62.801  1.00 33.09  ? 185  MET B C   1 
ATOM   5195 O  O   . MET B 1 185 ? -0.245  -32.361 63.931  1.00 35.56  ? 185  MET B O   1 
ATOM   5196 C  CB  . MET B 1 185 ? -0.845  -29.532 62.301  1.00 33.87  ? 185  MET B CB  1 
ATOM   5197 C  CG  . MET B 1 185 ? -1.978  -29.575 63.329  1.00 32.29  ? 185  MET B CG  1 
ATOM   5198 S  SD  . MET B 1 185 ? -3.482  -28.736 62.783  1.00 35.35  ? 185  MET B SD  1 
ATOM   5199 C  CE  . MET B 1 185 ? -4.157  -30.002 61.707  1.00 37.90  ? 185  MET B CE  1 
ATOM   5200 N  N   . ASN B 1 186 ? -0.230  -32.632 61.689  1.00 36.74  ? 186  ASN B N   1 
ATOM   5201 C  CA  . ASN B 1 186 ? -0.504  -34.069 61.765  1.00 36.14  ? 186  ASN B CA  1 
ATOM   5202 C  C   . ASN B 1 186 ? 0.629   -34.837 62.427  1.00 39.51  ? 186  ASN B C   1 
ATOM   5203 O  O   . ASN B 1 186 ? 0.385   -35.846 63.105  1.00 38.19  ? 186  ASN B O   1 
ATOM   5204 C  CB  . ASN B 1 186 ? -0.779  -34.645 60.362  1.00 38.66  ? 186  ASN B CB  1 
ATOM   5205 C  CG  . ASN B 1 186 ? -1.411  -36.051 60.411  1.00 47.01  ? 186  ASN B CG  1 
ATOM   5206 O  OD1 . ASN B 1 186 ? -0.697  -37.061 60.373  1.00 48.38  ? 186  ASN B OD1 1 
ATOM   5207 N  ND2 . ASN B 1 186 ? -2.734  -36.116 60.540  1.00 49.96  ? 186  ASN B ND2 1 
ATOM   5208 N  N   . LYS B 1 187 ? 1.870   -34.392 62.236  1.00 33.99  ? 187  LYS B N   1 
ATOM   5209 C  CA  . LYS B 1 187 ? 2.993   -35.092 62.836  1.00 39.71  ? 187  LYS B CA  1 
ATOM   5210 C  C   . LYS B 1 187 ? 2.960   -35.021 64.362  1.00 37.79  ? 187  LYS B C   1 
ATOM   5211 O  O   . LYS B 1 187 ? 3.508   -35.909 65.024  1.00 37.71  ? 187  LYS B O   1 
ATOM   5212 C  CB  . LYS B 1 187 ? 4.294   -34.522 62.268  1.00 38.86  ? 187  LYS B CB  1 
ATOM   5213 C  CG  . LYS B 1 187 ? 5.446   -35.492 62.264  1.00 50.00  ? 187  LYS B CG  1 
ATOM   5214 C  CD  . LYS B 1 187 ? 6.771   -34.805 61.910  1.00 49.14  ? 187  LYS B CD  1 
ATOM   5215 C  CE  . LYS B 1 187 ? 6.645   -34.000 60.626  1.00 46.35  ? 187  LYS B CE  1 
ATOM   5216 N  NZ  . LYS B 1 187 ? 7.984   -33.811 59.969  1.00 56.73  ? 187  LYS B NZ  1 
ATOM   5217 N  N   . LEU B 1 188 ? 2.280   -34.018 64.933  1.00 36.95  ? 188  LEU B N   1 
ATOM   5218 C  CA  . LEU B 1 188 ? 2.269   -33.852 66.384  1.00 40.47  ? 188  LEU B CA  1 
ATOM   5219 C  C   . LEU B 1 188 ? 1.702   -35.067 67.091  1.00 36.20  ? 188  LEU B C   1 
ATOM   5220 O  O   . LEU B 1 188 ? 2.114   -35.372 68.215  1.00 39.91  ? 188  LEU B O   1 
ATOM   5221 C  CB  . LEU B 1 188 ? 1.445   -32.624 66.788  1.00 38.30  ? 188  LEU B CB  1 
ATOM   5222 C  CG  . LEU B 1 188 ? 1.967   -31.287 66.278  1.00 36.45  ? 188  LEU B CG  1 
ATOM   5223 C  CD1 . LEU B 1 188 ? 0.917   -30.185 66.496  1.00 37.89  ? 188  LEU B CD1 1 
ATOM   5224 C  CD2 . LEU B 1 188 ? 3.272   -30.954 66.978  1.00 40.64  ? 188  LEU B CD2 1 
ATOM   5225 N  N   . GLN B 1 189 ? 0.741   -35.749 66.477  1.00 38.60  ? 189  GLN B N   1 
ATOM   5226 C  CA  . GLN B 1 189 ? 0.030   -36.825 67.150  1.00 42.04  ? 189  GLN B CA  1 
ATOM   5227 C  C   . GLN B 1 189 ? 0.549   -38.211 66.792  1.00 42.74  ? 189  GLN B C   1 
ATOM   5228 O  O   . GLN B 1 189 ? 0.018   -39.204 67.301  1.00 42.33  ? 189  GLN B O   1 
ATOM   5229 C  CB  . GLN B 1 189 ? -1.477  -36.741 66.845  1.00 43.84  ? 189  GLN B CB  1 
ATOM   5230 C  CG  . GLN B 1 189 ? -1.835  -36.610 65.361  1.00 42.16  ? 189  GLN B CG  1 
ATOM   5231 C  CD  . GLN B 1 189 ? -2.029  -37.955 64.673  1.00 47.82  ? 189  GLN B CD  1 
ATOM   5232 O  OE1 . GLN B 1 189 ? -2.909  -38.737 65.048  1.00 50.80  ? 189  GLN B OE1 1 
ATOM   5233 N  NE2 . GLN B 1 189 ? -1.221  -38.223 63.646  1.00 47.41  ? 189  GLN B NE2 1 
ATOM   5234 N  N   . ARG B 1 190 ? 1.560   -38.319 65.927  1.00 40.40  ? 190  ARG B N   1 
ATOM   5235 C  CA  . ARG B 1 190 ? 2.037   -39.640 65.516  1.00 41.77  ? 190  ARG B CA  1 
ATOM   5236 C  C   . ARG B 1 190 ? 2.850   -40.270 66.646  1.00 44.17  ? 190  ARG B C   1 
ATOM   5237 O  O   . ARG B 1 190 ? 3.920   -39.772 67.005  1.00 44.14  ? 190  ARG B O   1 
ATOM   5238 C  CB  . ARG B 1 190 ? 2.871   -39.536 64.242  1.00 41.01  ? 190  ARG B CB  1 
ATOM   5239 C  CG  . ARG B 1 190 ? 2.083   -39.081 63.039  1.00 40.37  ? 190  ARG B CG  1 
ATOM   5240 C  CD  . ARG B 1 190 ? 2.958   -38.896 61.809  1.00 41.17  ? 190  ARG B CD  1 
ATOM   5241 N  NE  . ARG B 1 190 ? 2.151   -38.276 60.773  1.00 39.35  ? 190  ARG B NE  1 
ATOM   5242 C  CZ  . ARG B 1 190 ? 2.625   -37.640 59.714  1.00 41.34  ? 190  ARG B CZ  1 
ATOM   5243 N  NH1 . ARG B 1 190 ? 3.926   -37.591 59.455  1.00 38.84  ? 190  ARG B NH1 1 
ATOM   5244 N  NH2 . ARG B 1 190 ? 1.774   -37.024 58.903  1.00 40.52  ? 190  ARG B NH2 1 
ATOM   5245 N  N   . ALA B 1 191 ? 2.343   -41.369 67.208  1.00 45.20  ? 191  ALA B N   1 
ATOM   5246 C  CA  . ALA B 1 191 ? 3.092   -42.090 68.234  1.00 46.81  ? 191  ALA B CA  1 
ATOM   5247 C  C   . ALA B 1 191 ? 4.378   -42.686 67.669  1.00 50.64  ? 191  ALA B C   1 
ATOM   5248 O  O   . ALA B 1 191 ? 5.426   -42.665 68.331  1.00 48.23  ? 191  ALA B O   1 
ATOM   5249 C  CB  . ALA B 1 191 ? 2.219   -43.183 68.847  1.00 49.20  ? 191  ALA B CB  1 
ATOM   5250 N  N   A ASN B 1 192 ? 4.319   -43.251 66.461  0.43 48.39  ? 192  ASN B N   1 
ATOM   5251 N  N   B ASN B 1 192 ? 4.323   -43.194 66.435  0.57 48.39  ? 192  ASN B N   1 
ATOM   5252 C  CA  A ASN B 1 192 ? 5.503   -43.778 65.782  0.43 47.03  ? 192  ASN B CA  1 
ATOM   5253 C  CA  B ASN B 1 192 ? 5.465   -43.797 65.750  0.57 47.02  ? 192  ASN B CA  1 
ATOM   5254 C  C   A ASN B 1 192 ? 5.696   -43.012 64.481  0.43 46.85  ? 192  ASN B C   1 
ATOM   5255 C  C   B ASN B 1 192 ? 5.708   -43.024 64.461  0.57 46.82  ? 192  ASN B C   1 
ATOM   5256 O  O   A ASN B 1 192 ? 5.154   -43.393 63.431  0.43 47.14  ? 192  ASN B O   1 
ATOM   5257 O  O   B ASN B 1 192 ? 5.207   -43.412 63.392  0.57 47.13  ? 192  ASN B O   1 
ATOM   5258 C  CB  A ASN B 1 192 ? 5.395   -45.279 65.524  0.43 47.97  ? 192  ASN B CB  1 
ATOM   5259 C  CB  B ASN B 1 192 ? 5.211   -45.276 65.461  0.57 48.01  ? 192  ASN B CB  1 
ATOM   5260 C  CG  A ASN B 1 192 ? 6.675   -45.857 64.942  0.43 48.10  ? 192  ASN B CG  1 
ATOM   5261 C  CG  B ASN B 1 192 ? 4.467   -45.971 66.584  0.57 46.26  ? 192  ASN B CG  1 
ATOM   5262 O  OD1 A ASN B 1 192 ? 7.697   -45.168 64.847  0.43 49.58  ? 192  ASN B OD1 1 
ATOM   5263 O  OD1 B ASN B 1 192 ? 4.927   -45.989 67.718  0.57 47.75  ? 192  ASN B OD1 1 
ATOM   5264 N  ND2 A ASN B 1 192 ? 6.627   -47.126 64.548  0.43 50.96  ? 192  ASN B ND2 1 
ATOM   5265 N  ND2 B ASN B 1 192 ? 3.301   -46.526 66.275  0.57 49.62  ? 192  ASN B ND2 1 
ATOM   5266 N  N   . PRO B 1 193 ? 6.470   -41.929 64.508  1.00 47.30  ? 193  PRO B N   1 
ATOM   5267 C  CA  . PRO B 1 193 ? 6.676   -41.134 63.287  1.00 47.18  ? 193  PRO B CA  1 
ATOM   5268 C  C   . PRO B 1 193 ? 7.303   -41.919 62.149  1.00 50.66  ? 193  PRO B C   1 
ATOM   5269 O  O   . PRO B 1 193 ? 7.184   -41.499 60.989  1.00 47.54  ? 193  PRO B O   1 
ATOM   5270 C  CB  . PRO B 1 193 ? 7.602   -39.999 63.753  1.00 47.25  ? 193  PRO B CB  1 
ATOM   5271 C  CG  . PRO B 1 193 ? 7.557   -40.012 65.245  1.00 51.36  ? 193  PRO B CG  1 
ATOM   5272 C  CD  . PRO B 1 193 ? 7.194   -41.397 65.674  1.00 49.73  ? 193  PRO B CD  1 
ATOM   5273 N  N   . ASP B 1 194 ? 7.972   -43.037 62.442  1.00 51.19  ? 194  ASP B N   1 
ATOM   5274 C  CA  . ASP B 1 194 ? 8.709   -43.800 61.444  1.00 54.89  ? 194  ASP B CA  1 
ATOM   5275 C  C   . ASP B 1 194 ? 7.944   -44.999 60.902  1.00 52.42  ? 194  ASP B C   1 
ATOM   5276 O  O   . ASP B 1 194 ? 8.491   -45.748 60.085  1.00 56.08  ? 194  ASP B O   1 
ATOM   5277 C  CB  . ASP B 1 194 ? 10.046  -44.250 62.027  1.00 56.42  ? 194  ASP B CB  1 
ATOM   5278 C  CG  . ASP B 1 194 ? 11.072  -43.148 61.992  1.00 60.60  ? 194  ASP B CG  1 
ATOM   5279 O  OD1 . ASP B 1 194 ? 10.694  -42.012 61.629  1.00 59.35  ? 194  ASP B OD1 1 
ATOM   5280 O  OD2 . ASP B 1 194 ? 12.238  -43.404 62.347  1.00 70.31  ? 194  ASP B OD2 1 
ATOM   5281 N  N   . ASP B 1 195 ? 6.705   -45.197 61.328  1.00 49.76  ? 195  ASP B N   1 
ATOM   5282 C  CA  . ASP B 1 195 ? 5.786   -46.111 60.664  1.00 50.41  ? 195  ASP B CA  1 
ATOM   5283 C  C   . ASP B 1 195 ? 5.882   -45.885 59.157  1.00 54.52  ? 195  ASP B C   1 
ATOM   5284 O  O   . ASP B 1 195 ? 5.901   -44.729 58.708  1.00 50.99  ? 195  ASP B O   1 
ATOM   5285 C  CB  . ASP B 1 195 ? 4.360   -45.873 61.169  1.00 50.69  ? 195  ASP B CB  1 
ATOM   5286 C  CG  . ASP B 1 195 ? 3.373   -46.944 60.720  1.00 53.14  ? 195  ASP B CG  1 
ATOM   5287 O  OD1 . ASP B 1 195 ? 3.271   -47.219 59.506  1.00 53.18  ? 195  ASP B OD1 1 
ATOM   5288 O  OD2 . ASP B 1 195 ? 2.663   -47.486 61.595  1.00 61.95  ? 195  ASP B OD2 1 
ATOM   5289 N  N   . PRO B 1 196 ? 5.982   -46.948 58.351  1.00 53.27  ? 196  PRO B N   1 
ATOM   5290 C  CA  . PRO B 1 196 ? 6.010   -46.765 56.887  1.00 49.71  ? 196  PRO B CA  1 
ATOM   5291 C  C   . PRO B 1 196 ? 4.786   -46.057 56.350  1.00 48.29  ? 196  PRO B C   1 
ATOM   5292 O  O   . PRO B 1 196 ? 4.841   -45.494 55.251  1.00 50.24  ? 196  PRO B O   1 
ATOM   5293 C  CB  . PRO B 1 196 ? 6.090   -48.200 56.347  1.00 54.41  ? 196  PRO B CB  1 
ATOM   5294 C  CG  . PRO B 1 196 ? 6.602   -49.024 57.469  1.00 55.13  ? 196  PRO B CG  1 
ATOM   5295 C  CD  . PRO B 1 196 ? 6.258   -48.336 58.760  1.00 55.94  ? 196  PRO B CD  1 
ATOM   5296 N  N   . ALA B 1 197 ? 3.677   -46.071 57.088  1.00 50.16  ? 197  ALA B N   1 
ATOM   5297 C  CA  . ALA B 1 197 ? 2.483   -45.367 56.642  1.00 46.83  ? 197  ALA B CA  1 
ATOM   5298 C  C   . ALA B 1 197 ? 2.745   -43.885 56.389  1.00 45.06  ? 197  ALA B C   1 
ATOM   5299 O  O   . ALA B 1 197 ? 1.957   -43.244 55.688  1.00 45.36  ? 197  ALA B O   1 
ATOM   5300 C  CB  . ALA B 1 197 ? 1.366   -45.541 57.674  1.00 49.50  ? 197  ALA B CB  1 
ATOM   5301 N  N   . TYR B 1 198 ? 3.827   -43.330 56.941  1.00 46.04  ? 198  TYR B N   1 
ATOM   5302 C  CA  . TYR B 1 198 ? 4.171   -41.917 56.789  1.00 46.90  ? 198  TYR B CA  1 
ATOM   5303 C  C   . TYR B 1 198 ? 5.274   -41.666 55.765  1.00 47.58  ? 198  TYR B C   1 
ATOM   5304 O  O   . TYR B 1 198 ? 5.667   -40.507 55.573  1.00 42.34  ? 198  TYR B O   1 
ATOM   5305 C  CB  . TYR B 1 198 ? 4.584   -41.334 58.148  1.00 41.06  ? 198  TYR B CB  1 
ATOM   5306 C  CG  . TYR B 1 198 ? 3.561   -41.581 59.232  1.00 40.88  ? 198  TYR B CG  1 
ATOM   5307 C  CD1 . TYR B 1 198 ? 2.246   -41.162 59.074  1.00 43.38  ? 198  TYR B CD1 1 
ATOM   5308 C  CD2 . TYR B 1 198 ? 3.893   -42.278 60.376  1.00 42.87  ? 198  TYR B CD2 1 
ATOM   5309 C  CE1 . TYR B 1 198 ? 1.297   -41.394 60.045  1.00 47.60  ? 198  TYR B CE1 1 
ATOM   5310 C  CE2 . TYR B 1 198 ? 2.947   -42.522 61.363  1.00 44.10  ? 198  TYR B CE2 1 
ATOM   5311 C  CZ  . TYR B 1 198 ? 1.648   -42.077 61.187  1.00 45.68  ? 198  TYR B CZ  1 
ATOM   5312 O  OH  . TYR B 1 198 ? 0.701   -42.312 62.162  1.00 52.12  ? 198  TYR B OH  1 
ATOM   5313 N  N   . ASP B 1 199 ? 5.792   -42.715 55.109  1.00 43.51  ? 199  ASP B N   1 
ATOM   5314 C  CA  . ASP B 1 199 ? 6.854   -42.516 54.122  1.00 46.97  ? 199  ASP B CA  1 
ATOM   5315 C  C   . ASP B 1 199 ? 6.438   -41.497 53.070  1.00 44.35  ? 199  ASP B C   1 
ATOM   5316 O  O   . ASP B 1 199 ? 7.199   -40.590 52.729  1.00 43.94  ? 199  ASP B O   1 
ATOM   5317 C  CB  . ASP B 1 199 ? 7.230   -43.843 53.445  1.00 48.83  ? 199  ASP B CB  1 
ATOM   5318 C  CG  . ASP B 1 199 ? 7.983   -44.786 54.369  1.00 52.02  ? 199  ASP B CG  1 
ATOM   5319 O  OD1 . ASP B 1 199 ? 8.500   -44.319 55.407  1.00 54.92  ? 199  ASP B OD1 1 
ATOM   5320 O  OD2 . ASP B 1 199 ? 8.077   -45.997 54.050  1.00 55.50  ? 199  ASP B OD2 1 
ATOM   5321 N  N   . GLU B 1 200 ? 5.224   -41.639 52.537  1.00 45.55  ? 200  GLU B N   1 
ATOM   5322 C  CA  . GLU B 1 200 ? 4.768   -40.709 51.512  1.00 49.02  ? 200  GLU B CA  1 
ATOM   5323 C  C   . GLU B 1 200 ? 4.624   -39.299 52.073  1.00 46.08  ? 200  GLU B C   1 
ATOM   5324 O  O   . GLU B 1 200 ? 4.987   -38.324 51.404  1.00 43.70  ? 200  GLU B O   1 
ATOM   5325 C  CB  . GLU B 1 200 ? 3.454   -41.198 50.908  1.00 47.04  ? 200  GLU B CB  1 
ATOM   5326 C  CG  . GLU B 1 200 ? 2.867   -40.279 49.860  1.00 51.64  ? 200  GLU B CG  1 
ATOM   5327 C  CD  . GLU B 1 200 ? 3.833   -39.974 48.720  1.00 56.42  ? 200  GLU B CD  1 
ATOM   5328 O  OE1 . GLU B 1 200 ? 4.825   -40.717 48.545  1.00 62.55  ? 200  GLU B OE1 1 
ATOM   5329 O  OE2 . GLU B 1 200 ? 3.591   -38.990 47.989  1.00 61.39  ? 200  GLU B OE2 1 
ATOM   5330 N  N   . ASN B 1 201 ? 4.110   -39.168 53.301  1.00 43.90  ? 201  ASN B N   1 
ATOM   5331 C  CA  . ASN B 1 201 ? 4.047   -37.850 53.932  1.00 42.11  ? 201  ASN B CA  1 
ATOM   5332 C  C   . ASN B 1 201 ? 5.425   -37.203 53.953  1.00 42.24  ? 201  ASN B C   1 
ATOM   5333 O  O   . ASN B 1 201 ? 5.579   -36.018 53.634  1.00 43.00  ? 201  ASN B O   1 
ATOM   5334 C  CB  . ASN B 1 201 ? 3.495   -37.955 55.355  1.00 46.05  ? 201  ASN B CB  1 
ATOM   5335 C  CG  . ASN B 1 201 ? 2.117   -38.560 55.397  1.00 48.21  ? 201  ASN B CG  1 
ATOM   5336 O  OD1 . ASN B 1 201 ? 1.941   -39.681 55.867  1.00 52.08  ? 201  ASN B OD1 1 
ATOM   5337 N  ND2 . ASN B 1 201 ? 1.132   -37.833 54.884  1.00 49.20  ? 201  ASN B ND2 1 
ATOM   5338 N  N   . LYS B 1 202 ? 6.447   -37.977 54.323  1.00 43.33  ? 202  LYS B N   1 
ATOM   5339 C  CA  . LYS B 1 202 ? 7.796   -37.425 54.375  1.00 43.64  ? 202  LYS B CA  1 
ATOM   5340 C  C   . LYS B 1 202 ? 8.282   -37.020 52.988  1.00 44.17  ? 202  LYS B C   1 
ATOM   5341 O  O   . LYS B 1 202 ? 8.886   -35.952 52.822  1.00 42.68  ? 202  LYS B O   1 
ATOM   5342 C  CB  . LYS B 1 202 ? 8.747   -38.430 55.022  1.00 45.98  ? 202  LYS B CB  1 
ATOM   5343 C  CG  . LYS B 1 202 ? 8.386   -38.749 56.477  1.00 45.76  ? 202  LYS B CG  1 
ATOM   5344 C  CD  . LYS B 1 202 ? 9.223   -39.893 57.046  1.00 47.48  ? 202  LYS B CD  1 
ATOM   5345 C  CE  . LYS B 1 202 ? 8.870   -40.139 58.509  1.00 44.83  ? 202  LYS B CE  1 
ATOM   5346 N  NZ  . LYS B 1 202 ? 9.513   -41.366 59.030  1.00 51.10  ? 202  LYS B NZ  1 
ATOM   5347 N  N   . ARG B 1 203 ? 8.033   -37.858 51.980  1.00 43.89  ? 203  ARG B N   1 
ATOM   5348 C  CA  . ARG B 1 203 ? 8.406   -37.499 50.616  1.00 44.51  ? 203  ARG B CA  1 
ATOM   5349 C  C   . ARG B 1 203 ? 7.734   -36.198 50.195  1.00 42.92  ? 203  ARG B C   1 
ATOM   5350 O  O   . ARG B 1 203 ? 8.386   -35.279 49.684  1.00 43.00  ? 203  ARG B O   1 
ATOM   5351 C  CB  . ARG B 1 203 ? 8.034   -38.622 49.649  1.00 45.79  ? 203  ARG B CB  1 
ATOM   5352 C  CG  . ARG B 1 203 ? 8.790   -38.548 48.327  1.00 55.66  ? 203  ARG B CG  1 
ATOM   5353 C  CD  . ARG B 1 203 ? 7.960   -39.072 47.145  1.00 58.38  ? 203  ARG B CD  1 
ATOM   5354 N  NE  . ARG B 1 203 ? 6.604   -38.529 47.135  1.00 61.43  ? 203  ARG B NE  1 
ATOM   5355 C  CZ  . ARG B 1 203 ? 6.248   -37.401 46.531  1.00 59.56  ? 203  ARG B CZ  1 
ATOM   5356 N  NH1 . ARG B 1 203 ? 7.128   -36.655 45.878  1.00 60.31  ? 203  ARG B NH1 1 
ATOM   5357 N  NH2 . ARG B 1 203 ? 4.979   -37.006 46.594  1.00 56.36  ? 203  ARG B NH2 1 
ATOM   5358 N  N   . GLN B 1 204 ? 6.422   -36.102 50.411  1.00 40.35  ? 204  GLN B N   1 
ATOM   5359 C  CA  . GLN B 1 204 ? 5.704   -34.891 50.035  1.00 40.84  ? 204  GLN B CA  1 
ATOM   5360 C  C   . GLN B 1 204 ? 6.220   -33.683 50.809  1.00 39.72  ? 204  GLN B C   1 
ATOM   5361 O  O   . GLN B 1 204 ? 6.306   -32.576 50.262  1.00 38.84  ? 204  GLN B O   1 
ATOM   5362 C  CB  . GLN B 1 204 ? 4.211   -35.081 50.273  1.00 42.56  ? 204  GLN B CB  1 
ATOM   5363 C  CG  . GLN B 1 204 ? 3.408   -33.851 49.934  1.00 42.96  ? 204  GLN B CG  1 
ATOM   5364 C  CD  . GLN B 1 204 ? 3.414   -33.563 48.449  1.00 44.91  ? 204  GLN B CD  1 
ATOM   5365 O  OE1 . GLN B 1 204 ? 4.113   -32.663 47.972  1.00 43.07  ? 204  GLN B OE1 1 
ATOM   5366 N  NE2 . GLN B 1 204 ? 2.638   -34.332 47.705  1.00 46.55  ? 204  GLN B NE2 1 
ATOM   5367 N  N   . PHE B 1 205 ? 6.554   -33.877 52.088  1.00 37.44  ? 205  PHE B N   1 
ATOM   5368 C  CA  . PHE B 1 205 ? 7.091   -32.791 52.905  1.00 37.76  ? 205  PHE B CA  1 
ATOM   5369 C  C   . PHE B 1 205 ? 8.381   -32.244 52.304  1.00 39.01  ? 205  PHE B C   1 
ATOM   5370 O  O   . PHE B 1 205 ? 8.547   -31.026 52.151  1.00 38.60  ? 205  PHE B O   1 
ATOM   5371 C  CB  . PHE B 1 205 ? 7.309   -33.296 54.335  1.00 38.44  ? 205  PHE B CB  1 
ATOM   5372 C  CG  . PHE B 1 205 ? 7.612   -32.208 55.348  1.00 38.48  ? 205  PHE B CG  1 
ATOM   5373 C  CD1 . PHE B 1 205 ? 6.694   -31.205 55.620  1.00 35.25  ? 205  PHE B CD1 1 
ATOM   5374 C  CD2 . PHE B 1 205 ? 8.807   -32.222 56.055  1.00 41.21  ? 205  PHE B CD2 1 
ATOM   5375 C  CE1 . PHE B 1 205 ? 6.973   -30.221 56.568  1.00 31.39  ? 205  PHE B CE1 1 
ATOM   5376 C  CE2 . PHE B 1 205 ? 9.090   -31.251 56.996  1.00 35.95  ? 205  PHE B CE2 1 
ATOM   5377 C  CZ  . PHE B 1 205 ? 8.178   -30.245 57.253  1.00 39.45  ? 205  PHE B CZ  1 
ATOM   5378 N  N   . GLN B 1 206 ? 9.303   -33.132 51.933  1.00 38.89  ? 206  GLN B N   1 
ATOM   5379 C  CA  . GLN B 1 206 ? 10.550  -32.676 51.328  1.00 40.97  ? 206  GLN B CA  1 
ATOM   5380 C  C   . GLN B 1 206 ? 10.278  -31.949 50.020  1.00 41.99  ? 206  GLN B C   1 
ATOM   5381 O  O   . GLN B 1 206 ? 10.929  -30.946 49.706  1.00 42.97  ? 206  GLN B O   1 
ATOM   5382 C  CB  . GLN B 1 206 ? 11.487  -33.867 51.108  1.00 40.61  ? 206  GLN B CB  1 
ATOM   5383 C  CG  . GLN B 1 206 ? 12.073  -34.444 52.397  1.00 46.58  ? 206  GLN B CG  1 
ATOM   5384 C  CD  . GLN B 1 206 ? 12.694  -33.389 53.305  1.00 50.26  ? 206  GLN B CD  1 
ATOM   5385 O  OE1 . GLN B 1 206 ? 13.548  -32.605 52.880  1.00 53.83  ? 206  GLN B OE1 1 
ATOM   5386 N  NE2 . GLN B 1 206 ? 12.256  -33.358 54.565  1.00 45.12  ? 206  GLN B NE2 1 
ATOM   5387 N  N   . GLU B 1 207 ? 9.315   -32.446 49.246  1.00 39.94  ? 207  GLU B N   1 
ATOM   5388 C  CA  . GLU B 1 207 ? 8.981   -31.811 47.980  1.00 41.24  ? 207  GLU B CA  1 
ATOM   5389 C  C   . GLU B 1 207 ? 8.413   -30.416 48.210  1.00 41.86  ? 207  GLU B C   1 
ATOM   5390 O  O   . GLU B 1 207 ? 8.745   -29.470 47.484  1.00 37.75  ? 207  GLU B O   1 
ATOM   5391 C  CB  . GLU B 1 207 ? 7.988   -32.694 47.221  1.00 43.16  ? 207  GLU B CB  1 
ATOM   5392 C  CG  . GLU B 1 207 ? 7.364   -32.074 45.986  1.00 50.77  ? 207  GLU B CG  1 
ATOM   5393 C  CD  . GLU B 1 207 ? 6.244   -32.944 45.429  1.00 57.41  ? 207  GLU B CD  1 
ATOM   5394 O  OE1 . GLU B 1 207 ? 6.488   -34.153 45.204  1.00 63.27  ? 207  GLU B OE1 1 
ATOM   5395 O  OE2 . GLU B 1 207 ? 5.120   -32.426 45.232  1.00 56.48  ? 207  GLU B OE2 1 
ATOM   5396 N  N   . ASP B 1 208 ? 7.552   -30.270 49.220  1.00 38.88  ? 208  ASP B N   1 
ATOM   5397 C  CA  . ASP B 1 208 ? 6.979   -28.966 49.516  1.00 37.91  ? 208  ASP B CA  1 
ATOM   5398 C  C   . ASP B 1 208 ? 8.045   -27.995 50.006  1.00 38.76  ? 208  ASP B C   1 
ATOM   5399 O  O   . ASP B 1 208 ? 7.991   -26.805 49.677  1.00 39.06  ? 208  ASP B O   1 
ATOM   5400 C  CB  . ASP B 1 208 ? 5.852   -29.122 50.540  1.00 36.71  ? 208  ASP B CB  1 
ATOM   5401 C  CG  . ASP B 1 208 ? 4.597   -29.696 49.925  1.00 40.46  ? 208  ASP B CG  1 
ATOM   5402 O  OD1 . ASP B 1 208 ? 4.344   -29.396 48.736  1.00 40.78  ? 208  ASP B OD1 1 
ATOM   5403 O  OD2 . ASP B 1 208 ? 3.863   -30.443 50.617  1.00 38.14  ? 208  ASP B OD2 1 
ATOM   5404 N  N   . ILE B 1 209 ? 9.033   -28.478 50.769  1.00 35.94  ? 209  ILE B N   1 
ATOM   5405 C  CA  . ILE B 1 209 ? 10.117  -27.603 51.194  1.00 36.68  ? 209  ILE B CA  1 
ATOM   5406 C  C   . ILE B 1 209 ? 10.915  -27.130 49.985  1.00 39.87  ? 209  ILE B C   1 
ATOM   5407 O  O   . ILE B 1 209 ? 11.327  -25.963 49.914  1.00 39.21  ? 209  ILE B O   1 
ATOM   5408 C  CB  . ILE B 1 209 ? 11.006  -28.313 52.231  1.00 38.77  ? 209  ILE B CB  1 
ATOM   5409 C  CG1 . ILE B 1 209 ? 10.235  -28.516 53.541  1.00 37.29  ? 209  ILE B CG1 1 
ATOM   5410 C  CG2 . ILE B 1 209 ? 12.288  -27.516 52.491  1.00 40.69  ? 209  ILE B CG2 1 
ATOM   5411 C  CD1 . ILE B 1 209 ? 10.981  -29.375 54.552  1.00 36.97  ? 209  ILE B CD1 1 
ATOM   5412 N  N   . LYS B 1 210 ? 11.131  -28.019 49.008  1.00 38.62  ? 210  LYS B N   1 
ATOM   5413 C  CA  . LYS B 1 210 ? 11.863  -27.629 47.806  1.00 39.94  ? 210  LYS B CA  1 
ATOM   5414 C  C   . LYS B 1 210 ? 11.107  -26.570 47.020  1.00 38.56  ? 210  LYS B C   1 
ATOM   5415 O  O   . LYS B 1 210 ? 11.711  -25.627 46.499  1.00 42.51  ? 210  LYS B O   1 
ATOM   5416 C  CB  . LYS B 1 210 ? 12.139  -28.845 46.920  1.00 43.00  ? 210  LYS B CB  1 
ATOM   5417 C  CG  . LYS B 1 210 ? 13.255  -28.591 45.872  1.00 52.45  ? 210  LYS B CG  1 
ATOM   5418 C  CD  . LYS B 1 210 ? 13.238  -29.596 44.719  1.00 56.70  ? 210  LYS B CD  1 
ATOM   5419 C  CE  . LYS B 1 210 ? 13.655  -28.942 43.387  1.00 53.40  ? 210  LYS B CE  1 
ATOM   5420 N  NZ  . LYS B 1 210 ? 12.495  -28.526 42.541  1.00 58.84  ? 210  LYS B NZ  1 
ATOM   5421 N  N   . VAL B 1 211 ? 9.785   -26.708 46.920  1.00 36.43  ? 211  VAL B N   1 
ATOM   5422 C  CA  . VAL B 1 211 ? 8.995   -25.699 46.223  1.00 39.76  ? 211  VAL B CA  1 
ATOM   5423 C  C   . VAL B 1 211 ? 9.164   -24.339 46.892  1.00 40.07  ? 211  VAL B C   1 
ATOM   5424 O  O   . VAL B 1 211 ? 9.303   -23.307 46.220  1.00 39.41  ? 211  VAL B O   1 
ATOM   5425 C  CB  . VAL B 1 211 ? 7.515   -26.130 46.167  1.00 40.05  ? 211  VAL B CB  1 
ATOM   5426 C  CG1 . VAL B 1 211 ? 6.621   -24.957 45.786  1.00 42.87  ? 211  VAL B CG1 1 
ATOM   5427 C  CG2 . VAL B 1 211 ? 7.335   -27.283 45.186  1.00 41.03  ? 211  VAL B CG2 1 
ATOM   5428 N  N   . MET B 1 212 ? 9.131   -24.306 48.228  1.00 36.58  ? 212  MET B N   1 
ATOM   5429 C  CA  . MET B 1 212 ? 9.273   -23.021 48.900  1.00 38.55  ? 212  MET B CA  1 
ATOM   5430 C  C   . MET B 1 212 ? 10.660  -22.442 48.667  1.00 38.07  ? 212  MET B C   1 
ATOM   5431 O  O   . MET B 1 212 ? 10.802  -21.245 48.394  1.00 39.96  ? 212  MET B O   1 
ATOM   5432 C  CB  . MET B 1 212 ? 8.968   -23.177 50.394  1.00 37.77  ? 212  MET B CB  1 
ATOM   5433 C  CG  . MET B 1 212 ? 7.519   -23.583 50.629  1.00 35.56  ? 212  MET B CG  1 
ATOM   5434 S  SD  . MET B 1 212 ? 6.933   -23.393 52.344  1.00 40.52  ? 212  MET B SD  1 
ATOM   5435 C  CE  . MET B 1 212 ? 7.675   -24.854 53.069  1.00 39.87  ? 212  MET B CE  1 
ATOM   5436 N  N   . ASN B 1 213 ? 11.695  -23.277 48.761  1.00 38.43  ? 213  ASN B N   1 
ATOM   5437 C  CA  . ASN B 1 213 ? 13.054  -22.798 48.535  1.00 39.38  ? 213  ASN B CA  1 
ATOM   5438 C  C   . ASN B 1 213 ? 13.290  -22.386 47.088  1.00 42.23  ? 213  ASN B C   1 
ATOM   5439 O  O   . ASN B 1 213 ? 14.097  -21.485 46.834  1.00 44.11  ? 213  ASN B O   1 
ATOM   5440 C  CB  . ASN B 1 213 ? 14.067  -23.854 48.950  1.00 44.24  ? 213  ASN B CB  1 
ATOM   5441 C  CG  . ASN B 1 213 ? 14.438  -23.745 50.407  1.00 46.42  ? 213  ASN B CG  1 
ATOM   5442 O  OD1 . ASN B 1 213 ? 15.280  -22.929 50.772  1.00 53.39  ? 213  ASN B OD1 1 
ATOM   5443 N  ND2 . ASN B 1 213 ? 13.789  -24.535 51.254  1.00 42.74  ? 213  ASN B ND2 1 
ATOM   5444 N  N   . ASP B 1 214 ? 12.624  -23.033 46.128  1.00 41.03  ? 214  ASP B N   1 
ATOM   5445 C  CA  . ASP B 1 214 ? 12.767  -22.591 44.744  1.00 44.91  ? 214  ASP B CA  1 
ATOM   5446 C  C   . ASP B 1 214 ? 12.293  -21.151 44.588  1.00 43.35  ? 214  ASP B C   1 
ATOM   5447 O  O   . ASP B 1 214 ? 12.943  -20.337 43.918  1.00 41.43  ? 214  ASP B O   1 
ATOM   5448 C  CB  . ASP B 1 214 ? 11.995  -23.518 43.802  1.00 44.41  ? 214  ASP B CB  1 
ATOM   5449 C  CG  . ASP B 1 214 ? 12.696  -24.863 43.586  1.00 46.55  ? 214  ASP B CG  1 
ATOM   5450 O  OD1 . ASP B 1 214 ? 13.876  -25.006 43.968  1.00 46.55  ? 214  ASP B OD1 1 
ATOM   5451 O  OD2 . ASP B 1 214 ? 12.065  -25.774 43.015  1.00 51.95  ? 214  ASP B OD2 1 
ATOM   5452 N  N   . LEU B 1 215 ? 11.175  -20.808 45.226  1.00 39.39  ? 215  LEU B N   1 
ATOM   5453 C  CA  . LEU B 1 215 ? 10.685  -19.435 45.162  1.00 38.03  ? 215  LEU B CA  1 
ATOM   5454 C  C   . LEU B 1 215 ? 11.644  -18.469 45.844  1.00 39.50  ? 215  LEU B C   1 
ATOM   5455 O  O   . LEU B 1 215 ? 11.870  -17.353 45.354  1.00 38.76  ? 215  LEU B O   1 
ATOM   5456 C  CB  . LEU B 1 215 ? 9.297   -19.349 45.788  1.00 41.50  ? 215  LEU B CB  1 
ATOM   5457 C  CG  . LEU B 1 215 ? 8.834   -17.902 45.855  1.00 42.21  ? 215  LEU B CG  1 
ATOM   5458 C  CD1 . LEU B 1 215 ? 8.419   -17.470 44.457  1.00 47.72  ? 215  LEU B CD1 1 
ATOM   5459 C  CD2 . LEU B 1 215 ? 7.691   -17.789 46.805  1.00 45.35  ? 215  LEU B CD2 1 
ATOM   5460 N  N   . VAL B 1 216 ? 12.214  -18.876 46.980  1.00 40.02  ? 216  VAL B N   1 
ATOM   5461 C  CA  . VAL B 1 216 ? 13.234  -18.069 47.645  1.00 36.37  ? 216  VAL B CA  1 
ATOM   5462 C  C   . VAL B 1 216 ? 14.404  -17.793 46.703  1.00 42.27  ? 216  VAL B C   1 
ATOM   5463 O  O   . VAL B 1 216 ? 14.941  -16.678 46.668  1.00 42.92  ? 216  VAL B O   1 
ATOM   5464 C  CB  . VAL B 1 216 ? 13.694  -18.773 48.935  1.00 38.30  ? 216  VAL B CB  1 
ATOM   5465 C  CG1 . VAL B 1 216 ? 14.907  -18.072 49.518  1.00 42.41  ? 216  VAL B CG1 1 
ATOM   5466 C  CG2 . VAL B 1 216 ? 12.547  -18.818 49.932  1.00 39.19  ? 216  VAL B CG2 1 
ATOM   5467 N  N   . ASP B 1 217 ? 14.832  -18.809 45.945  1.00 43.68  ? 217  ASP B N   1 
ATOM   5468 C  CA  . ASP B 1 217 ? 15.882  -18.614 44.942  1.00 44.33  ? 217  ASP B CA  1 
ATOM   5469 C  C   . ASP B 1 217 ? 15.503  -17.518 43.950  1.00 46.59  ? 217  ASP B C   1 
ATOM   5470 O  O   . ASP B 1 217 ? 16.323  -16.654 43.610  1.00 47.72  ? 217  ASP B O   1 
ATOM   5471 C  CB  . ASP B 1 217 ? 16.144  -19.917 44.180  1.00 47.26  ? 217  ASP B CB  1 
ATOM   5472 C  CG  . ASP B 1 217 ? 16.802  -20.991 45.021  1.00 51.12  ? 217  ASP B CG  1 
ATOM   5473 O  OD1 . ASP B 1 217 ? 17.357  -20.689 46.098  1.00 51.57  ? 217  ASP B OD1 1 
ATOM   5474 O  OD2 . ASP B 1 217 ? 16.763  -22.161 44.577  1.00 56.33  ? 217  ASP B OD2 1 
ATOM   5475 N  N   . LYS B 1 218 ? 14.268  -17.558 43.448  1.00 43.53  ? 218  LYS B N   1 
ATOM   5476 C  CA  . LYS B 1 218 ? 13.837  -16.575 42.462  1.00 43.52  ? 218  LYS B CA  1 
ATOM   5477 C  C   . LYS B 1 218 ? 13.878  -15.163 43.033  1.00 46.36  ? 218  LYS B C   1 
ATOM   5478 O  O   . LYS B 1 218 ? 14.276  -14.215 42.343  1.00 45.16  ? 218  LYS B O   1 
ATOM   5479 C  CB  . LYS B 1 218 ? 12.432  -16.927 41.962  1.00 46.04  ? 218  LYS B CB  1 
ATOM   5480 C  CG  . LYS B 1 218 ? 12.436  -17.921 40.808  1.00 50.95  ? 218  LYS B CG  1 
ATOM   5481 C  CD  . LYS B 1 218 ? 11.124  -17.928 40.040  1.00 59.69  ? 218  LYS B CD  1 
ATOM   5482 C  CE  . LYS B 1 218 ? 10.553  -19.336 39.949  1.00 60.88  ? 218  LYS B CE  1 
ATOM   5483 N  NZ  . LYS B 1 218 ? 9.305   -19.384 39.129  1.00 66.04  ? 218  LYS B NZ  1 
ATOM   5484 N  N   . ILE B 1 219 ? 13.465  -15.002 44.293  1.00 39.77  ? 219  ILE B N   1 
ATOM   5485 C  CA  . ILE B 1 219 ? 13.450  -13.680 44.910  1.00 36.96  ? 219  ILE B CA  1 
ATOM   5486 C  C   . ILE B 1 219 ? 14.866  -13.139 45.045  1.00 41.06  ? 219  ILE B C   1 
ATOM   5487 O  O   . ILE B 1 219 ? 15.131  -11.964 44.755  1.00 39.69  ? 219  ILE B O   1 
ATOM   5488 C  CB  . ILE B 1 219 ? 12.730  -13.743 46.273  1.00 35.78  ? 219  ILE B CB  1 
ATOM   5489 C  CG1 . ILE B 1 219 ? 11.241  -14.046 46.063  1.00 36.98  ? 219  ILE B CG1 1 
ATOM   5490 C  CG2 . ILE B 1 219 ? 12.950  -12.461 47.072  1.00 36.81  ? 219  ILE B CG2 1 
ATOM   5491 C  CD1 . ILE B 1 219 ? 10.462  -14.255 47.359  1.00 36.85  ? 219  ILE B CD1 1 
ATOM   5492 N  N   . ILE B 1 220 ? 15.790  -13.982 45.503  1.00 39.01  ? 220  ILE B N   1 
ATOM   5493 C  CA  . ILE B 1 220 ? 17.179  -13.563 45.663  1.00 40.89  ? 220  ILE B CA  1 
ATOM   5494 C  C   . ILE B 1 220 ? 17.786  -13.188 44.317  1.00 45.71  ? 220  ILE B C   1 
ATOM   5495 O  O   . ILE B 1 220 ? 18.467  -12.162 44.190  1.00 47.04  ? 220  ILE B O   1 
ATOM   5496 C  CB  . ILE B 1 220 ? 17.986  -14.671 46.360  1.00 44.77  ? 220  ILE B CB  1 
ATOM   5497 C  CG1 . ILE B 1 220 ? 17.526  -14.817 47.812  1.00 46.87  ? 220  ILE B CG1 1 
ATOM   5498 C  CG2 . ILE B 1 220 ? 19.483  -14.374 46.272  1.00 43.36  ? 220  ILE B CG2 1 
ATOM   5499 C  CD1 . ILE B 1 220 ? 18.102  -16.034 48.525  1.00 50.93  ? 220  ILE B CD1 1 
ATOM   5500 N  N   . ALA B 1 221 ? 17.544  -14.010 43.294  1.00 48.86  ? 221  ALA B N   1 
ATOM   5501 C  CA  . ALA B 1 221 ? 18.069  -13.723 41.959  1.00 49.49  ? 221  ALA B CA  1 
ATOM   5502 C  C   . ALA B 1 221 ? 17.474  -12.439 41.392  1.00 51.27  ? 221  ALA B C   1 
ATOM   5503 O  O   . ALA B 1 221 ? 18.193  -11.599 40.838  1.00 56.87  ? 221  ALA B O   1 
ATOM   5504 C  CB  . ALA B 1 221 ? 17.790  -14.902 41.026  1.00 47.38  ? 221  ALA B CB  1 
ATOM   5505 N  N   . ASP B 1 222 ? 16.151  -12.287 41.499  1.00 48.07  ? 222  ASP B N   1 
ATOM   5506 C  CA  . ASP B 1 222 ? 15.481  -11.068 41.050  1.00 47.86  ? 222  ASP B CA  1 
ATOM   5507 C  C   . ASP B 1 222 ? 16.142  -9.833  41.655  1.00 53.24  ? 222  ASP B C   1 
ATOM   5508 O  O   . ASP B 1 222 ? 16.437  -8.859  40.952  1.00 54.76  ? 222  ASP B O   1 
ATOM   5509 C  CB  . ASP B 1 222 ? 13.991  -11.152 41.418  1.00 47.96  ? 222  ASP B CB  1 
ATOM   5510 C  CG  . ASP B 1 222 ? 13.188  -9.927  40.987  1.00 53.91  ? 222  ASP B CG  1 
ATOM   5511 O  OD1 . ASP B 1 222 ? 13.222  -8.902  41.705  1.00 54.77  ? 222  ASP B OD1 1 
ATOM   5512 O  OD2 . ASP B 1 222 ? 12.486  -10.003 39.951  1.00 51.77  ? 222  ASP B OD2 1 
ATOM   5513 N  N   . ARG B 1 223 ? 16.414  -9.869  42.963  1.00 47.66  ? 223  ARG B N   1 
ATOM   5514 C  CA  . ARG B 1 223 ? 17.037  -8.724  43.621  1.00 44.88  ? 223  ARG B CA  1 
ATOM   5515 C  C   . ARG B 1 223 ? 18.478  -8.540  43.170  1.00 54.01  ? 223  ARG B C   1 
ATOM   5516 O  O   . ARG B 1 223 ? 18.920  -7.410  42.941  1.00 53.23  ? 223  ARG B O   1 
ATOM   5517 C  CB  . ARG B 1 223 ? 16.988  -8.894  45.139  1.00 41.54  ? 223  ARG B CB  1 
ATOM   5518 C  CG  . ARG B 1 223 ? 17.660  -7.771  45.922  1.00 39.33  ? 223  ARG B CG  1 
ATOM   5519 C  CD  . ARG B 1 223 ? 17.051  -6.418  45.598  1.00 41.64  ? 223  ARG B CD  1 
ATOM   5520 N  NE  . ARG B 1 223 ? 15.610  -6.425  45.830  1.00 42.69  ? 223  ARG B NE  1 
ATOM   5521 C  CZ  . ARG B 1 223 ? 15.017  -5.927  46.910  1.00 40.62  ? 223  ARG B CZ  1 
ATOM   5522 N  NH1 . ARG B 1 223 ? 15.708  -5.350  47.875  1.00 37.63  ? 223  ARG B NH1 1 
ATOM   5523 N  NH2 . ARG B 1 223 ? 13.693  -6.012  47.026  1.00 38.30  ? 223  ARG B NH2 1 
ATOM   5524 N  N   . LYS B 1 224 ? 19.238  -9.633  43.073  1.00 52.16  ? 224  LYS B N   1 
ATOM   5525 C  CA  . LYS B 1 224 ? 20.631  -9.516  42.651  1.00 61.01  ? 224  LYS B CA  1 
ATOM   5526 C  C   . LYS B 1 224 ? 20.735  -8.979  41.228  1.00 63.77  ? 224  LYS B C   1 
ATOM   5527 O  O   . LYS B 1 224 ? 21.667  -8.232  40.911  1.00 66.91  ? 224  LYS B O   1 
ATOM   5528 C  CB  . LYS B 1 224 ? 21.334  -10.869 42.770  1.00 59.21  ? 224  LYS B CB  1 
ATOM   5529 C  CG  . LYS B 1 224 ? 22.855  -10.787 42.699  1.00 76.05  ? 224  LYS B CG  1 
ATOM   5530 C  CD  . LYS B 1 224 ? 23.511  -12.051 43.247  1.00 82.85  ? 224  LYS B CD  1 
ATOM   5531 C  CE  . LYS B 1 224 ? 23.814  -13.054 42.142  1.00 89.26  ? 224  LYS B CE  1 
ATOM   5532 N  NZ  . LYS B 1 224 ? 22.576  -13.520 41.457  1.00 86.69  ? 224  LYS B NZ  1 
ATOM   5533 N  N   . ALA B 1 225 ? 19.787  -9.336  40.366  1.00 62.28  ? 225  ALA B N   1 
ATOM   5534 C  CA  . ALA B 1 225 ? 19.773  -8.854  38.992  1.00 65.81  ? 225  ALA B CA  1 
ATOM   5535 C  C   . ALA B 1 225 ? 19.173  -7.464  38.859  1.00 69.69  ? 225  ALA B C   1 
ATOM   5536 O  O   . ALA B 1 225 ? 19.127  -6.934  37.744  1.00 74.17  ? 225  ALA B O   1 
ATOM   5537 C  CB  . ALA B 1 225 ? 18.994  -9.827  38.106  1.00 62.98  ? 225  ALA B CB  1 
ATOM   5538 N  N   . SER B 1 226 ? 18.724  -6.864  39.959  1.00 67.02  ? 226  SER B N   1 
ATOM   5539 C  CA  . SER B 1 226 ? 17.888  -5.670  39.903  1.00 70.62  ? 226  SER B CA  1 
ATOM   5540 C  C   . SER B 1 226 ? 18.761  -4.430  39.768  1.00 79.47  ? 226  SER B C   1 
ATOM   5541 O  O   . SER B 1 226 ? 19.530  -4.101  40.678  1.00 77.15  ? 226  SER B O   1 
ATOM   5542 C  CB  . SER B 1 226 ? 17.008  -5.583  41.146  1.00 71.93  ? 226  SER B CB  1 
ATOM   5543 O  OG  . SER B 1 226 ? 16.317  -4.348  41.192  1.00 79.64  ? 226  SER B OG  1 
ATOM   5544 N  N   . GLY B 1 227 ? 18.642  -3.742  38.626  1.00 86.43  ? 227  GLY B N   1 
ATOM   5545 C  CA  . GLY B 1 227 ? 19.252  -2.432  38.468  1.00 86.94  ? 227  GLY B CA  1 
ATOM   5546 C  C   . GLY B 1 227 ? 18.500  -1.321  39.165  1.00 87.77  ? 227  GLY B C   1 
ATOM   5547 O  O   . GLY B 1 227 ? 19.092  -0.281  39.471  1.00 88.77  ? 227  GLY B O   1 
ATOM   5548 N  N   . GLU B 1 228 ? 17.206  -1.520  39.411  1.00 86.71  ? 228  GLU B N   1 
ATOM   5549 C  CA  . GLU B 1 228 ? 16.438  -0.621  40.261  1.00 86.78  ? 228  GLU B CA  1 
ATOM   5550 C  C   . GLU B 1 228 ? 16.839  -0.824  41.718  1.00 88.35  ? 228  GLU B C   1 
ATOM   5551 O  O   . GLU B 1 228 ? 16.954  -1.961  42.187  1.00 87.57  ? 228  GLU B O   1 
ATOM   5552 C  CB  . GLU B 1 228 ? 14.943  -0.886  40.078  1.00 86.18  ? 228  GLU B CB  1 
ATOM   5553 C  CG  . GLU B 1 228 ? 14.135  -0.867  41.370  1.00 85.38  ? 228  GLU B CG  1 
ATOM   5554 C  CD  . GLU B 1 228 ? 12.671  -1.233  41.156  1.00 85.13  ? 228  GLU B CD  1 
ATOM   5555 O  OE1 . GLU B 1 228 ? 12.384  -2.044  40.249  1.00 82.10  ? 228  GLU B OE1 1 
ATOM   5556 O  OE2 . GLU B 1 228 ? 11.806  -0.704  41.891  1.00 84.38  ? 228  GLU B OE2 1 
ATOM   5557 N  N   . GLN B 1 229 ? 17.058  0.275   42.438  1.00 87.83  ? 229  GLN B N   1 
ATOM   5558 C  CA  . GLN B 1 229 ? 17.438  0.190   43.842  1.00 85.54  ? 229  GLN B CA  1 
ATOM   5559 C  C   . GLN B 1 229 ? 16.201  0.183   44.735  1.00 80.61  ? 229  GLN B C   1 
ATOM   5560 O  O   . GLN B 1 229 ? 15.210  0.866   44.456  1.00 80.99  ? 229  GLN B O   1 
ATOM   5561 C  CB  . GLN B 1 229 ? 18.367  1.343   44.233  1.00 87.37  ? 229  GLN B CB  1 
ATOM   5562 C  CG  . GLN B 1 229 ? 17.858  2.735   43.891  1.00 93.90  ? 229  GLN B CG  1 
ATOM   5563 C  CD  . GLN B 1 229 ? 18.859  3.821   44.255  1.00 102.72 ? 229  GLN B CD  1 
ATOM   5564 O  OE1 . GLN B 1 229 ? 19.970  3.862   43.722  1.00 103.93 ? 229  GLN B OE1 1 
ATOM   5565 N  NE2 . GLN B 1 229 ? 18.469  4.706   45.170  1.00 102.38 ? 229  GLN B NE2 1 
ATOM   5566 N  N   . SER B 1 230 ? 16.267  -0.602  45.809  1.00 74.13  ? 230  SER B N   1 
ATOM   5567 C  CA  . SER B 1 230 ? 15.176  -0.753  46.761  1.00 66.05  ? 230  SER B CA  1 
ATOM   5568 C  C   . SER B 1 230 ? 15.678  -0.442  48.170  1.00 64.00  ? 230  SER B C   1 
ATOM   5569 O  O   . SER B 1 230 ? 16.885  -0.328  48.421  1.00 59.20  ? 230  SER B O   1 
ATOM   5570 C  CB  . SER B 1 230 ? 14.579  -2.171  46.707  1.00 62.02  ? 230  SER B CB  1 
ATOM   5571 O  OG  . SER B 1 230 ? 13.857  -2.410  45.506  1.00 62.33  ? 230  SER B OG  1 
ATOM   5572 N  N   . ASP B 1 231 ? 14.734  -0.302  49.097  1.00 55.52  ? 231  ASP B N   1 
ATOM   5573 C  CA  . ASP B 1 231 ? 15.076  -0.067  50.497  1.00 55.58  ? 231  ASP B CA  1 
ATOM   5574 C  C   . ASP B 1 231 ? 14.052  -0.753  51.405  1.00 57.02  ? 231  ASP B C   1 
ATOM   5575 O  O   . ASP B 1 231 ? 13.493  -0.148  52.322  1.00 59.08  ? 231  ASP B O   1 
ATOM   5576 C  CB  . ASP B 1 231 ? 15.168  1.429   50.792  1.00 60.70  ? 231  ASP B CB  1 
ATOM   5577 C  CG  . ASP B 1 231 ? 15.635  1.707   52.204  1.00 70.43  ? 231  ASP B CG  1 
ATOM   5578 O  OD1 . ASP B 1 231 ? 16.217  0.781   52.812  1.00 67.91  ? 231  ASP B OD1 1 
ATOM   5579 O  OD2 . ASP B 1 231 ? 15.430  2.838   52.703  1.00 73.15  ? 231  ASP B OD2 1 
ATOM   5580 N  N   . ASP B 1 232 ? 13.823  -2.044  51.184  1.00 46.28  ? 232  ASP B N   1 
ATOM   5581 C  CA  . ASP B 1 232 ? 12.772  -2.784  51.863  1.00 43.77  ? 232  ASP B CA  1 
ATOM   5582 C  C   . ASP B 1 232 ? 13.359  -3.829  52.819  1.00 42.11  ? 232  ASP B C   1 
ATOM   5583 O  O   . ASP B 1 232 ? 14.545  -3.790  53.182  1.00 40.66  ? 232  ASP B O   1 
ATOM   5584 C  CB  . ASP B 1 232 ? 11.874  -3.422  50.804  1.00 40.89  ? 232  ASP B CB  1 
ATOM   5585 C  CG  . ASP B 1 232 ? 12.667  -4.219  49.792  1.00 38.79  ? 232  ASP B CG  1 
ATOM   5586 O  OD1 . ASP B 1 232 ? 13.853  -4.508  50.071  1.00 42.11  ? 232  ASP B OD1 1 
ATOM   5587 O  OD2 . ASP B 1 232 ? 12.132  -4.557  48.717  1.00 37.74  ? 232  ASP B OD2 1 
ATOM   5588 N  N   . LEU B 1 233 ? 12.507  -4.766  53.248  1.00 37.38  ? 233  LEU B N   1 
ATOM   5589 C  CA  . LEU B 1 233 ? 12.943  -5.831  54.153  1.00 37.12  ? 233  LEU B CA  1 
ATOM   5590 C  C   . LEU B 1 233 ? 14.110  -6.617  53.556  1.00 38.02  ? 233  LEU B C   1 
ATOM   5591 O  O   . LEU B 1 233 ? 15.103  -6.901  54.236  1.00 37.79  ? 233  LEU B O   1 
ATOM   5592 C  CB  . LEU B 1 233 ? 11.755  -6.745  54.470  1.00 37.81  ? 233  LEU B CB  1 
ATOM   5593 C  CG  . LEU B 1 233 ? 11.926  -7.925  55.416  1.00 35.37  ? 233  LEU B CG  1 
ATOM   5594 C  CD1 . LEU B 1 233 ? 12.244  -7.426  56.833  1.00 37.77  ? 233  LEU B CD1 1 
ATOM   5595 C  CD2 . LEU B 1 233 ? 10.646  -8.783  55.423  1.00 35.02  ? 233  LEU B CD2 1 
ATOM   5596 N  N   . LEU B 1 234 ? 14.022  -6.963  52.272  1.00 35.29  ? 234  LEU B N   1 
ATOM   5597 C  CA  . LEU B 1 234 ? 15.109  -7.719  51.652  1.00 34.05  ? 234  LEU B CA  1 
ATOM   5598 C  C   . LEU B 1 234 ? 16.398  -6.902  51.616  1.00 35.45  ? 234  LEU B C   1 
ATOM   5599 O  O   . LEU B 1 234 ? 17.489  -7.458  51.785  1.00 38.56  ? 234  LEU B O   1 
ATOM   5600 C  CB  . LEU B 1 234 ? 14.708  -8.164  50.243  1.00 36.24  ? 234  LEU B CB  1 
ATOM   5601 C  CG  . LEU B 1 234 ? 15.709  -9.040  49.476  1.00 36.31  ? 234  LEU B CG  1 
ATOM   5602 C  CD1 . LEU B 1 234 ? 16.112  -10.269 50.277  1.00 34.72  ? 234  LEU B CD1 1 
ATOM   5603 C  CD2 . LEU B 1 234 ? 15.104  -9.466  48.136  1.00 35.58  ? 234  LEU B CD2 1 
ATOM   5604 N  N   . THR B 1 235 ? 16.292  -5.583  51.437  1.00 35.14  ? 235  THR B N   1 
ATOM   5605 C  CA  . THR B 1 235 ? 17.492  -4.747  51.451  1.00 36.56  ? 235  THR B CA  1 
ATOM   5606 C  C   . THR B 1 235 ? 18.233  -4.885  52.778  1.00 38.35  ? 235  THR B C   1 
ATOM   5607 O  O   . THR B 1 235 ? 19.459  -5.043  52.800  1.00 40.07  ? 235  THR B O   1 
ATOM   5608 C  CB  . THR B 1 235 ? 17.135  -3.281  51.201  1.00 39.29  ? 235  THR B CB  1 
ATOM   5609 O  OG1 . THR B 1 235 ? 16.450  -3.145  49.953  1.00 39.15  ? 235  THR B OG1 1 
ATOM   5610 C  CG2 . THR B 1 235 ? 18.404  -2.442  51.151  1.00 43.09  ? 235  THR B CG2 1 
ATOM   5611 N  N   . HIS B 1 236 ? 17.498  -4.823  53.897  1.00 35.11  ? 236  HIS B N   1 
ATOM   5612 C  CA  . HIS B 1 236 ? 18.127  -4.928  55.217  1.00 38.07  ? 236  HIS B CA  1 
ATOM   5613 C  C   . HIS B 1 236 ? 18.696  -6.320  55.440  1.00 40.35  ? 236  HIS B C   1 
ATOM   5614 O  O   . HIS B 1 236 ? 19.786  -6.484  55.999  1.00 39.36  ? 236  HIS B O   1 
ATOM   5615 C  CB  . HIS B 1 236 ? 17.114  -4.600  56.319  1.00 42.93  ? 236  HIS B CB  1 
ATOM   5616 C  CG  . HIS B 1 236 ? 16.702  -3.159  56.376  1.00 44.37  ? 236  HIS B CG  1 
ATOM   5617 N  ND1 . HIS B 1 236 ? 15.826  -2.589  55.478  1.00 45.19  ? 236  HIS B ND1 1 
ATOM   5618 C  CD2 . HIS B 1 236 ? 17.038  -2.176  57.246  1.00 49.70  ? 236  HIS B CD2 1 
ATOM   5619 C  CE1 . HIS B 1 236 ? 15.650  -1.315  55.782  1.00 50.49  ? 236  HIS B CE1 1 
ATOM   5620 N  NE2 . HIS B 1 236 ? 16.370  -1.042  56.857  1.00 53.60  ? 236  HIS B NE2 1 
ATOM   5621 N  N   . MET B 1 237 ? 17.927  -7.330  55.057  1.00 37.77  ? 237  MET B N   1 
ATOM   5622 C  CA  . MET B 1 237 ? 18.356  -8.720  54.976  1.00 37.42  ? 237  MET B CA  1 
ATOM   5623 C  C   . MET B 1 237 ? 19.750  -8.823  54.378  1.00 43.90  ? 237  MET B C   1 
ATOM   5624 O  O   . MET B 1 237 ? 20.673  -9.396  54.974  1.00 42.04  ? 237  MET B O   1 
ATOM   5625 C  CB  . MET B 1 237 ? 17.305  -9.377  54.086  1.00 42.61  ? 237  MET B CB  1 
ATOM   5626 C  CG  . MET B 1 237 ? 16.027  -9.764  54.795  1.00 44.63  ? 237  MET B CG  1 
ATOM   5627 S  SD  . MET B 1 237 ? 15.348  -11.373 54.414  1.00 37.72  ? 237  MET B SD  1 
ATOM   5628 C  CE  . MET B 1 237 ? 13.769  -11.214 55.281  1.00 34.48  ? 237  MET B CE  1 
ATOM   5629 N  N   . LEU B 1 238 ? 19.910  -8.245  53.190  1.00 40.16  ? 238  LEU B N   1 
ATOM   5630 C  CA  . LEU B 1 238 ? 21.118  -8.418  52.395  1.00 41.50  ? 238  LEU B CA  1 
ATOM   5631 C  C   . LEU B 1 238 ? 22.228  -7.447  52.772  1.00 43.08  ? 238  LEU B C   1 
ATOM   5632 O  O   . LEU B 1 238 ? 23.400  -7.745  52.528  1.00 50.53  ? 238  LEU B O   1 
ATOM   5633 C  CB  . LEU B 1 238 ? 20.794  -8.252  50.905  1.00 42.73  ? 238  LEU B CB  1 
ATOM   5634 C  CG  . LEU B 1 238 ? 19.855  -9.284  50.278  1.00 42.33  ? 238  LEU B CG  1 
ATOM   5635 C  CD1 . LEU B 1 238 ? 19.443  -8.865  48.861  1.00 41.53  ? 238  LEU B CD1 1 
ATOM   5636 C  CD2 . LEU B 1 238 ? 20.472  -10.688 50.275  1.00 43.36  ? 238  LEU B CD2 1 
ATOM   5637 N  N   . ASN B 1 239 ? 21.906  -6.305  53.362  1.00 42.89  ? 239  ASN B N   1 
ATOM   5638 C  CA  . ASN B 1 239 ? 22.918  -5.282  53.582  1.00 45.35  ? 239  ASN B CA  1 
ATOM   5639 C  C   . ASN B 1 239 ? 23.061  -4.817  55.014  1.00 44.85  ? 239  ASN B C   1 
ATOM   5640 O  O   . ASN B 1 239 ? 24.106  -4.244  55.340  1.00 44.98  ? 239  ASN B O   1 
ATOM   5641 C  CB  . ASN B 1 239 ? 22.632  -4.056  52.701  1.00 44.93  ? 239  ASN B CB  1 
ATOM   5642 C  CG  . ASN B 1 239 ? 22.569  -4.415  51.233  1.00 51.39  ? 239  ASN B CG  1 
ATOM   5643 O  OD1 . ASN B 1 239 ? 23.597  -4.597  50.587  1.00 53.25  ? 239  ASN B OD1 1 
ATOM   5644 N  ND2 . ASN B 1 239 ? 21.359  -4.550  50.704  1.00 47.53  ? 239  ASN B ND2 1 
ATOM   5645 N  N   . GLY B 1 240 ? 22.067  -5.022  55.876  1.00 39.36  ? 240  GLY B N   1 
ATOM   5646 C  CA  . GLY B 1 240 ? 22.129  -4.443  57.201  1.00 37.76  ? 240  GLY B CA  1 
ATOM   5647 C  C   . GLY B 1 240 ? 23.167  -5.122  58.076  1.00 37.61  ? 240  GLY B C   1 
ATOM   5648 O  O   . GLY B 1 240 ? 23.421  -6.321  57.962  1.00 39.71  ? 240  GLY B O   1 
ATOM   5649 N  N   . LYS B 1 241 ? 23.782  -4.331  58.955  1.00 41.01  ? 241  LYS B N   1 
ATOM   5650 C  CA  . LYS B 1 241 ? 24.774  -4.826  59.908  1.00 39.71  ? 241  LYS B CA  1 
ATOM   5651 C  C   . LYS B 1 241 ? 24.210  -4.751  61.316  1.00 35.29  ? 241  LYS B C   1 
ATOM   5652 O  O   . LYS B 1 241 ? 23.664  -3.717  61.721  1.00 37.19  ? 241  LYS B O   1 
ATOM   5653 C  CB  . LYS B 1 241 ? 26.080  -4.020  59.842  1.00 40.91  ? 241  LYS B CB  1 
ATOM   5654 C  CG  . LYS B 1 241 ? 26.633  -3.873  58.449  1.00 45.93  ? 241  LYS B CG  1 
ATOM   5655 C  CD  . LYS B 1 241 ? 27.249  -5.158  57.962  1.00 48.90  ? 241  LYS B CD  1 
ATOM   5656 C  CE  . LYS B 1 241 ? 28.178  -4.894  56.775  1.00 52.47  ? 241  LYS B CE  1 
ATOM   5657 N  NZ  . LYS B 1 241 ? 28.971  -3.652  56.980  1.00 58.02  ? 241  LYS B NZ  1 
ATOM   5658 N  N   . ASP B 1 242 ? 24.368  -5.833  62.063  1.00 35.91  ? 242  ASP B N   1 
ATOM   5659 C  CA  . ASP B 1 242 ? 24.023  -5.845  63.473  1.00 35.78  ? 242  ASP B CA  1 
ATOM   5660 C  C   . ASP B 1 242 ? 24.981  -4.960  64.253  1.00 37.18  ? 242  ASP B C   1 
ATOM   5661 O  O   . ASP B 1 242 ? 26.191  -5.227  64.251  1.00 35.33  ? 242  ASP B O   1 
ATOM   5662 C  CB  . ASP B 1 242 ? 24.075  -7.280  63.990  1.00 33.61  ? 242  ASP B CB  1 
ATOM   5663 C  CG  . ASP B 1 242 ? 24.055  -7.371  65.494  1.00 34.97  ? 242  ASP B CG  1 
ATOM   5664 O  OD1 . ASP B 1 242 ? 23.472  -6.487  66.155  1.00 35.34  ? 242  ASP B OD1 1 
ATOM   5665 O  OD2 . ASP B 1 242 ? 24.610  -8.361  66.019  1.00 35.81  ? 242  ASP B OD2 1 
ATOM   5666 N  N   . PRO B 1 243 ? 24.498  -3.933  64.952  1.00 36.15  ? 243  PRO B N   1 
ATOM   5667 C  CA  . PRO B 1 243 ? 25.411  -3.062  65.712  1.00 38.07  ? 243  PRO B CA  1 
ATOM   5668 C  C   . PRO B 1 243 ? 26.194  -3.780  66.784  1.00 38.96  ? 243  PRO B C   1 
ATOM   5669 O  O   . PRO B 1 243 ? 27.287  -3.320  67.147  1.00 40.10  ? 243  PRO B O   1 
ATOM   5670 C  CB  . PRO B 1 243 ? 24.470  -2.023  66.341  1.00 41.16  ? 243  PRO B CB  1 
ATOM   5671 C  CG  . PRO B 1 243 ? 23.224  -2.088  65.523  1.00 44.66  ? 243  PRO B CG  1 
ATOM   5672 C  CD  . PRO B 1 243 ? 23.093  -3.496  65.059  1.00 40.12  ? 243  PRO B CD  1 
ATOM   5673 N  N   . GLU B 1 244 ? 25.660  -4.868  67.341  1.00 35.45  ? 244  GLU B N   1 
ATOM   5674 C  CA  . GLU B 1 244 ? 26.364  -5.523  68.432  1.00 37.02  ? 244  GLU B CA  1 
ATOM   5675 C  C   . GLU B 1 244 ? 27.541  -6.326  67.885  1.00 37.53  ? 244  GLU B C   1 
ATOM   5676 O  O   . GLU B 1 244 ? 28.698  -6.006  68.170  1.00 38.29  ? 244  GLU B O   1 
ATOM   5677 C  CB  . GLU B 1 244 ? 25.406  -6.391  69.258  1.00 39.70  ? 244  GLU B CB  1 
ATOM   5678 C  CG  . GLU B 1 244 ? 26.123  -7.287  70.256  1.00 45.80  ? 244  GLU B CG  1 
ATOM   5679 C  CD  . GLU B 1 244 ? 25.203  -8.245  71.008  1.00 50.37  ? 244  GLU B CD  1 
ATOM   5680 O  OE1 . GLU B 1 244 ? 24.016  -8.408  70.639  1.00 41.72  ? 244  GLU B OE1 1 
ATOM   5681 O  OE2 . GLU B 1 244 ? 25.679  -8.819  72.005  1.00 56.03  ? 244  GLU B OE2 1 
ATOM   5682 N  N   . THR B 1 245 ? 27.271  -7.334  67.041  1.00 35.74  ? 245  THR B N   1 
ATOM   5683 C  CA  . THR B 1 245 ? 28.363  -8.099  66.439  1.00 38.42  ? 245  THR B CA  1 
ATOM   5684 C  C   . THR B 1 245 ? 29.059  -7.340  65.324  1.00 42.19  ? 245  THR B C   1 
ATOM   5685 O  O   . THR B 1 245 ? 30.213  -7.662  65.002  1.00 42.09  ? 245  THR B O   1 
ATOM   5686 C  CB  . THR B 1 245 ? 27.865  -9.432  65.871  1.00 38.77  ? 245  THR B CB  1 
ATOM   5687 O  OG1 . THR B 1 245 ? 26.936  -9.193  64.797  1.00 37.16  ? 245  THR B OG1 1 
ATOM   5688 C  CG2 . THR B 1 245 ? 27.213  -10.267 66.959  1.00 36.73  ? 245  THR B CG2 1 
ATOM   5689 N  N   . GLY B 1 246 ? 28.379  -6.365  64.712  1.00 37.13  ? 246  GLY B N   1 
ATOM   5690 C  CA  . GLY B 1 246 ? 28.878  -5.659  63.556  1.00 37.17  ? 246  GLY B CA  1 
ATOM   5691 C  C   . GLY B 1 246 ? 28.769  -6.416  62.255  1.00 35.70  ? 246  GLY B C   1 
ATOM   5692 O  O   . GLY B 1 246 ? 29.227  -5.912  61.219  1.00 38.59  ? 246  GLY B O   1 
ATOM   5693 N  N   . GLU B 1 247 ? 28.177  -7.610  62.267  1.00 37.23  ? 247  GLU B N   1 
ATOM   5694 C  CA  . GLU B 1 247 ? 28.080  -8.519  61.138  1.00 34.87  ? 247  GLU B CA  1 
ATOM   5695 C  C   . GLU B 1 247 ? 26.733  -8.397  60.434  1.00 36.49  ? 247  GLU B C   1 
ATOM   5696 O  O   . GLU B 1 247 ? 25.719  -8.123  61.076  1.00 33.92  ? 247  GLU B O   1 
ATOM   5697 C  CB  . GLU B 1 247 ? 28.228  -9.967  61.600  1.00 33.98  ? 247  GLU B CB  1 
ATOM   5698 C  CG  . GLU B 1 247 ? 29.485  -10.284 62.385  1.00 36.18  ? 247  GLU B CG  1 
ATOM   5699 C  CD  . GLU B 1 247 ? 29.341  -11.594 63.144  1.00 42.04  ? 247  GLU B CD  1 
ATOM   5700 O  OE1 . GLU B 1 247 ? 28.349  -12.325 62.904  1.00 38.03  ? 247  GLU B OE1 1 
ATOM   5701 O  OE2 . GLU B 1 247 ? 30.194  -11.874 64.005  1.00 37.88  ? 247  GLU B OE2 1 
ATOM   5702 N  N   . PRO B 1 248 ? 26.709  -8.653  59.132  1.00 36.09  ? 248  PRO B N   1 
ATOM   5703 C  CA  . PRO B 1 248 ? 25.451  -8.876  58.416  1.00 38.03  ? 248  PRO B CA  1 
ATOM   5704 C  C   . PRO B 1 248 ? 25.042  -10.339 58.535  1.00 36.29  ? 248  PRO B C   1 
ATOM   5705 O  O   . PRO B 1 248 ? 25.820  -11.195 58.944  1.00 36.26  ? 248  PRO B O   1 
ATOM   5706 C  CB  . PRO B 1 248 ? 25.826  -8.547  56.965  1.00 40.08  ? 248  PRO B CB  1 
ATOM   5707 C  CG  . PRO B 1 248 ? 27.230  -9.079  56.865  1.00 39.87  ? 248  PRO B CG  1 
ATOM   5708 C  CD  . PRO B 1 248 ? 27.876  -8.817  58.240  1.00 37.03  ? 248  PRO B CD  1 
ATOM   5709 N  N   . LEU B 1 249 ? 23.801  -10.625 58.139  1.00 36.46  ? 249  LEU B N   1 
ATOM   5710 C  CA  . LEU B 1 249 ? 23.405  -12.025 58.075  1.00 36.14  ? 249  LEU B CA  1 
ATOM   5711 C  C   . LEU B 1 249 ? 24.198  -12.761 56.998  1.00 36.56  ? 249  LEU B C   1 
ATOM   5712 O  O   . LEU B 1 249 ? 24.572  -12.188 55.968  1.00 37.76  ? 249  LEU B O   1 
ATOM   5713 C  CB  . LEU B 1 249 ? 21.914  -12.155 57.769  1.00 39.45  ? 249  LEU B CB  1 
ATOM   5714 C  CG  . LEU B 1 249 ? 20.974  -11.405 58.703  1.00 38.01  ? 249  LEU B CG  1 
ATOM   5715 C  CD1 . LEU B 1 249 ? 19.548  -11.590 58.182  1.00 35.38  ? 249  LEU B CD1 1 
ATOM   5716 C  CD2 . LEU B 1 249 ? 21.107  -11.875 60.127  1.00 32.80  ? 249  LEU B CD2 1 
ATOM   5717 N  N   . ASP B 1 250 ? 24.435  -14.048 57.226  1.00 35.98  ? 250  ASP B N   1 
ATOM   5718 C  CA  . ASP B 1 250 ? 25.021  -14.884 56.189  1.00 38.98  ? 250  ASP B CA  1 
ATOM   5719 C  C   . ASP B 1 250 ? 23.930  -15.451 55.276  1.00 40.38  ? 250  ASP B C   1 
ATOM   5720 O  O   . ASP B 1 250 ? 22.727  -15.333 55.541  1.00 37.76  ? 250  ASP B O   1 
ATOM   5721 C  CB  . ASP B 1 250 ? 25.908  -15.982 56.802  1.00 41.37  ? 250  ASP B CB  1 
ATOM   5722 C  CG  . ASP B 1 250 ? 25.137  -17.004 57.644  1.00 45.83  ? 250  ASP B CG  1 
ATOM   5723 O  OD1 . ASP B 1 250 ? 24.037  -17.454 57.260  1.00 39.15  ? 250  ASP B OD1 1 
ATOM   5724 O  OD2 . ASP B 1 250 ? 25.642  -17.338 58.739  1.00 54.43  ? 250  ASP B OD2 1 
ATOM   5725 N  N   . ASP B 1 251 ? 24.375  -16.027 54.153  1.00 40.84  ? 251  ASP B N   1 
ATOM   5726 C  CA  . ASP B 1 251 ? 23.456  -16.448 53.097  1.00 41.37  ? 251  ASP B CA  1 
ATOM   5727 C  C   . ASP B 1 251 ? 22.468  -17.496 53.592  1.00 38.07  ? 251  ASP B C   1 
ATOM   5728 O  O   . ASP B 1 251 ? 21.289  -17.483 53.210  1.00 37.11  ? 251  ASP B O   1 
ATOM   5729 C  CB  . ASP B 1 251 ? 24.249  -16.999 51.910  1.00 42.72  ? 251  ASP B CB  1 
ATOM   5730 C  CG  . ASP B 1 251 ? 24.839  -15.900 51.036  1.00 51.79  ? 251  ASP B CG  1 
ATOM   5731 O  OD1 . ASP B 1 251 ? 24.503  -14.715 51.243  1.00 50.77  ? 251  ASP B OD1 1 
ATOM   5732 O  OD2 . ASP B 1 251 ? 25.638  -16.226 50.133  1.00 54.56  ? 251  ASP B OD2 1 
ATOM   5733 N  N   . GLU B 1 252 ? 22.937  -18.437 54.413  1.00 37.12  ? 252  GLU B N   1 
ATOM   5734 C  CA  . GLU B 1 252 ? 22.059  -19.497 54.900  1.00 37.39  ? 252  GLU B CA  1 
ATOM   5735 C  C   . GLU B 1 252 ? 20.935  -18.922 55.749  1.00 37.32  ? 252  GLU B C   1 
ATOM   5736 O  O   . GLU B 1 252 ? 19.766  -19.296 55.594  1.00 36.47  ? 252  GLU B O   1 
ATOM   5737 C  CB  . GLU B 1 252 ? 22.862  -20.520 55.712  1.00 40.18  ? 252  GLU B CB  1 
ATOM   5738 C  CG  . GLU B 1 252 ? 22.055  -21.750 56.108  1.00 45.21  ? 252  GLU B CG  1 
ATOM   5739 C  CD  . GLU B 1 252 ? 22.774  -22.627 57.118  1.00 54.12  ? 252  GLU B CD  1 
ATOM   5740 O  OE1 . GLU B 1 252 ? 23.894  -23.082 56.802  1.00 64.65  ? 252  GLU B OE1 1 
ATOM   5741 O  OE2 . GLU B 1 252 ? 22.230  -22.856 58.226  1.00 53.42  ? 252  GLU B OE2 1 
ATOM   5742 N  N   . ASN B 1 253 ? 21.276  -18.031 56.677  1.00 34.60  ? 253  ASN B N   1 
ATOM   5743 C  CA  . ASN B 1 253 ? 20.235  -17.447 57.518  1.00 32.07  ? 253  ASN B CA  1 
ATOM   5744 C  C   . ASN B 1 253 ? 19.296  -16.561 56.707  1.00 32.65  ? 253  ASN B C   1 
ATOM   5745 O  O   . ASN B 1 253 ? 18.093  -16.501 56.992  1.00 31.41  ? 253  ASN B O   1 
ATOM   5746 C  CB  . ASN B 1 253 ? 20.849  -16.652 58.667  1.00 35.57  ? 253  ASN B CB  1 
ATOM   5747 C  CG  . ASN B 1 253 ? 19.804  -16.192 59.660  1.00 31.53  ? 253  ASN B CG  1 
ATOM   5748 O  OD1 . ASN B 1 253 ? 19.483  -15.011 59.738  1.00 31.98  ? 253  ASN B OD1 1 
ATOM   5749 N  ND2 . ASN B 1 253 ? 19.242  -17.137 60.405  1.00 32.04  ? 253  ASN B ND2 1 
ATOM   5750 N  N   . ILE B 1 254 ? 19.818  -15.860 55.702  1.00 32.55  ? 254  ILE B N   1 
ATOM   5751 C  CA  . ILE B 1 254 ? 18.951  -15.038 54.856  1.00 33.93  ? 254  ILE B CA  1 
ATOM   5752 C  C   . ILE B 1 254 ? 17.844  -15.889 54.234  1.00 34.84  ? 254  ILE B C   1 
ATOM   5753 O  O   . ILE B 1 254 ? 16.663  -15.497 54.223  1.00 33.17  ? 254  ILE B O   1 
ATOM   5754 C  CB  . ILE B 1 254 ? 19.784  -14.308 53.786  1.00 33.22  ? 254  ILE B CB  1 
ATOM   5755 C  CG1 . ILE B 1 254 ? 20.575  -13.160 54.421  1.00 35.47  ? 254  ILE B CG1 1 
ATOM   5756 C  CG2 . ILE B 1 254 ? 18.880  -13.794 52.656  1.00 36.21  ? 254  ILE B CG2 1 
ATOM   5757 C  CD1 . ILE B 1 254 ? 21.688  -12.653 53.514  1.00 40.36  ? 254  ILE B CD1 1 
ATOM   5758 N  N   . ARG B 1 255 ? 18.197  -17.077 53.727  1.00 32.64  ? 255  ARG B N   1 
ATOM   5759 C  CA  . ARG B 1 255 ? 17.185  -17.929 53.098  1.00 33.97  ? 255  ARG B CA  1 
ATOM   5760 C  C   . ARG B 1 255 ? 16.106  -18.323 54.101  1.00 33.18  ? 255  ARG B C   1 
ATOM   5761 O  O   . ARG B 1 255 ? 14.914  -18.367 53.762  1.00 34.40  ? 255  ARG B O   1 
ATOM   5762 C  CB  . ARG B 1 255 ? 17.829  -19.176 52.481  1.00 37.68  ? 255  ARG B CB  1 
ATOM   5763 C  CG  . ARG B 1 255 ? 18.907  -18.897 51.428  1.00 44.80  ? 255  ARG B CG  1 
ATOM   5764 C  CD  . ARG B 1 255 ? 19.421  -20.197 50.797  1.00 47.71  ? 255  ARG B CD  1 
ATOM   5765 N  NE  . ARG B 1 255 ? 18.307  -20.974 50.263  1.00 51.00  ? 255  ARG B NE  1 
ATOM   5766 C  CZ  . ARG B 1 255 ? 17.840  -20.865 49.026  1.00 51.51  ? 255  ARG B CZ  1 
ATOM   5767 N  NH1 . ARG B 1 255 ? 18.424  -20.082 48.130  1.00 53.18  ? 255  ARG B NH1 1 
ATOM   5768 N  NH2 . ARG B 1 255 ? 16.748  -21.540 48.685  1.00 47.77  ? 255  ARG B NH2 1 
ATOM   5769 N  N   . TYR B 1 256 ? 16.504  -18.617 55.340  1.00 31.82  ? 256  TYR B N   1 
ATOM   5770 C  CA  . TYR B 1 256 ? 15.523  -18.934 56.378  1.00 32.88  ? 256  TYR B CA  1 
ATOM   5771 C  C   . TYR B 1 256 ? 14.651  -17.732 56.714  1.00 33.36  ? 256  TYR B C   1 
ATOM   5772 O  O   . TYR B 1 256 ? 13.451  -17.891 56.989  1.00 32.85  ? 256  TYR B O   1 
ATOM   5773 C  CB  . TYR B 1 256 ? 16.214  -19.415 57.657  1.00 31.45  ? 256  TYR B CB  1 
ATOM   5774 C  CG  . TYR B 1 256 ? 16.797  -20.802 57.579  1.00 32.49  ? 256  TYR B CG  1 
ATOM   5775 C  CD1 . TYR B 1 256 ? 16.090  -21.848 56.984  1.00 32.69  ? 256  TYR B CD1 1 
ATOM   5776 C  CD2 . TYR B 1 256 ? 18.058  -21.072 58.100  1.00 35.31  ? 256  TYR B CD2 1 
ATOM   5777 C  CE1 . TYR B 1 256 ? 16.628  -23.128 56.918  1.00 39.45  ? 256  TYR B CE1 1 
ATOM   5778 C  CE2 . TYR B 1 256 ? 18.601  -22.351 58.040  1.00 36.61  ? 256  TYR B CE2 1 
ATOM   5779 C  CZ  . TYR B 1 256 ? 17.892  -23.365 57.446  1.00 41.28  ? 256  TYR B CZ  1 
ATOM   5780 O  OH  . TYR B 1 256 ? 18.447  -24.625 57.382  1.00 42.16  ? 256  TYR B OH  1 
ATOM   5781 N  N   . GLN B 1 257 ? 15.239  -16.532 56.759  1.00 32.46  ? 257  GLN B N   1 
ATOM   5782 C  CA  . GLN B 1 257 ? 14.423  -15.355 57.043  1.00 30.95  ? 257  GLN B CA  1 
ATOM   5783 C  C   . GLN B 1 257 ? 13.424  -15.114 55.922  1.00 32.16  ? 257  GLN B C   1 
ATOM   5784 O  O   . GLN B 1 257 ? 12.280  -14.734 56.182  1.00 33.49  ? 257  GLN B O   1 
ATOM   5785 C  CB  . GLN B 1 257 ? 15.285  -14.107 57.257  1.00 35.03  ? 257  GLN B CB  1 
ATOM   5786 C  CG  . GLN B 1 257 ? 16.368  -14.204 58.353  1.00 31.27  ? 257  GLN B CG  1 
ATOM   5787 C  CD  . GLN B 1 257 ? 15.838  -14.432 59.757  1.00 32.37  ? 257  GLN B CD  1 
ATOM   5788 O  OE1 . GLN B 1 257 ? 14.625  -14.418 60.000  1.00 29.86  ? 257  GLN B OE1 1 
ATOM   5789 N  NE2 . GLN B 1 257 ? 16.760  -14.615 60.715  1.00 32.24  ? 257  GLN B NE2 1 
ATOM   5790 N  N   . ILE B 1 258 ? 13.827  -15.332 54.669  1.00 32.90  ? 258  ILE B N   1 
ATOM   5791 C  CA  . ILE B 1 258 ? 12.882  -15.109 53.573  1.00 32.31  ? 258  ILE B CA  1 
ATOM   5792 C  C   . ILE B 1 258 ? 11.696  -16.064 53.683  1.00 32.35  ? 258  ILE B C   1 
ATOM   5793 O  O   . ILE B 1 258 ? 10.530  -15.649 53.584  1.00 32.58  ? 258  ILE B O   1 
ATOM   5794 C  CB  . ILE B 1 258 ? 13.582  -15.225 52.209  1.00 32.46  ? 258  ILE B CB  1 
ATOM   5795 C  CG1 . ILE B 1 258 ? 14.619  -14.100 52.080  1.00 36.19  ? 258  ILE B CG1 1 
ATOM   5796 C  CG2 . ILE B 1 258 ? 12.532  -15.107 51.085  1.00 30.55  ? 258  ILE B CG2 1 
ATOM   5797 C  CD1 . ILE B 1 258 ? 15.559  -14.266 50.868  1.00 35.90  ? 258  ILE B CD1 1 
ATOM   5798 N  N   . ILE B 1 259 ? 11.967  -17.359 53.865  1.00 33.81  ? 259  ILE B N   1 
ATOM   5799 C  CA  . ILE B 1 259 ? 10.880  -18.317 54.110  1.00 33.43  ? 259  ILE B CA  1 
ATOM   5800 C  C   . ILE B 1 259 ? 10.037  -17.874 55.301  1.00 34.19  ? 259  ILE B C   1 
ATOM   5801 O  O   . ILE B 1 259 ? 8.793   -17.867 55.251  1.00 31.43  ? 259  ILE B O   1 
ATOM   5802 C  CB  . ILE B 1 259 ? 11.459  -19.727 54.334  1.00 32.89  ? 259  ILE B CB  1 
ATOM   5803 C  CG1 . ILE B 1 259 ? 12.139  -20.222 53.051  1.00 39.25  ? 259  ILE B CG1 1 
ATOM   5804 C  CG2 . ILE B 1 259 ? 10.382  -20.706 54.820  1.00 37.42  ? 259  ILE B CG2 1 
ATOM   5805 C  CD1 . ILE B 1 259 ? 12.885  -21.530 53.240  1.00 42.58  ? 259  ILE B CD1 1 
ATOM   5806 N  N   . THR B 1 260 ? 10.702  -17.514 56.398  1.00 29.81  ? 260  THR B N   1 
ATOM   5807 C  CA  . THR B 1 260 ? 9.988   -17.118 57.611  1.00 31.93  ? 260  THR B CA  1 
ATOM   5808 C  C   . THR B 1 260 ? 9.067   -15.930 57.345  1.00 33.71  ? 260  THR B C   1 
ATOM   5809 O  O   . THR B 1 260 ? 7.879   -15.954 57.696  1.00 30.63  ? 260  THR B O   1 
ATOM   5810 C  CB  . THR B 1 260 ? 10.997  -16.792 58.718  1.00 30.67  ? 260  THR B CB  1 
ATOM   5811 O  OG1 . THR B 1 260 ? 11.750  -17.976 59.028  1.00 30.86  ? 260  THR B OG1 1 
ATOM   5812 C  CG2 . THR B 1 260 ? 10.302  -16.285 59.978  1.00 30.26  ? 260  THR B CG2 1 
ATOM   5813 N  N   . PHE B 1 261 ? 9.584   -14.888 56.695  1.00 29.18  ? 261  PHE B N   1 
ATOM   5814 C  CA  . PHE B 1 261 ? 8.750   -13.700 56.503  1.00 30.81  ? 261  PHE B CA  1 
ATOM   5815 C  C   . PHE B 1 261 ? 7.678   -13.896 55.427  1.00 33.01  ? 261  PHE B C   1 
ATOM   5816 O  O   . PHE B 1 261 ? 6.599   -13.287 55.520  1.00 32.52  ? 261  PHE B O   1 
ATOM   5817 C  CB  . PHE B 1 261 ? 9.641   -12.483 56.217  1.00 32.51  ? 261  PHE B CB  1 
ATOM   5818 C  CG  . PHE B 1 261 ? 10.168  -11.853 57.478  1.00 30.38  ? 261  PHE B CG  1 
ATOM   5819 C  CD1 . PHE B 1 261 ? 11.364  -12.286 58.034  1.00 32.96  ? 261  PHE B CD1 1 
ATOM   5820 C  CD2 . PHE B 1 261 ? 9.446   -10.881 58.144  1.00 32.35  ? 261  PHE B CD2 1 
ATOM   5821 C  CE1 . PHE B 1 261 ? 11.831  -11.746 59.200  1.00 32.69  ? 261  PHE B CE1 1 
ATOM   5822 C  CE2 . PHE B 1 261 ? 9.902   -10.330 59.343  1.00 30.72  ? 261  PHE B CE2 1 
ATOM   5823 C  CZ  . PHE B 1 261 ? 11.110  -10.758 59.868  1.00 33.37  ? 261  PHE B CZ  1 
ATOM   5824 N  N   . LEU B 1 262 ? 7.918   -14.738 54.420  1.00 30.52  ? 262  LEU B N   1 
ATOM   5825 C  CA  . LEU B 1 262 ? 6.845   -15.000 53.456  1.00 31.79  ? 262  LEU B CA  1 
ATOM   5826 C  C   . LEU B 1 262 ? 5.667   -15.697 54.131  1.00 32.37  ? 262  LEU B C   1 
ATOM   5827 O  O   . LEU B 1 262 ? 4.497   -15.441 53.794  1.00 33.12  ? 262  LEU B O   1 
ATOM   5828 C  CB  . LEU B 1 262 ? 7.356   -15.859 52.296  1.00 31.17  ? 262  LEU B CB  1 
ATOM   5829 C  CG  . LEU B 1 262 ? 8.296   -15.111 51.347  1.00 34.39  ? 262  LEU B CG  1 
ATOM   5830 C  CD1 . LEU B 1 262 ? 8.856   -16.067 50.312  1.00 32.92  ? 262  LEU B CD1 1 
ATOM   5831 C  CD2 . LEU B 1 262 ? 7.590   -13.934 50.689  1.00 31.26  ? 262  LEU B CD2 1 
ATOM   5832 N  N   . ILE B 1 263 ? 5.953   -16.594 55.074  1.00 31.28  ? 263  ILE B N   1 
ATOM   5833 C  CA  . ILE B 1 263 ? 4.892   -17.348 55.743  1.00 30.25  ? 263  ILE B CA  1 
ATOM   5834 C  C   . ILE B 1 263 ? 4.293   -16.543 56.888  1.00 30.87  ? 263  ILE B C   1 
ATOM   5835 O  O   . ILE B 1 263 ? 3.095   -16.229 56.896  1.00 32.03  ? 263  ILE B O   1 
ATOM   5836 C  CB  . ILE B 1 263 ? 5.420   -18.704 56.239  1.00 31.03  ? 263  ILE B CB  1 
ATOM   5837 C  CG1 . ILE B 1 263 ? 5.823   -19.586 55.050  1.00 30.21  ? 263  ILE B CG1 1 
ATOM   5838 C  CG2 . ILE B 1 263 ? 4.361   -19.379 57.127  1.00 34.63  ? 263  ILE B CG2 1 
ATOM   5839 C  CD1 . ILE B 1 263 ? 6.505   -20.853 55.499  1.00 34.97  ? 263  ILE B CD1 1 
ATOM   5840 N  N   . ALA B 1 264 ? 5.121   -16.199 57.884  1.00 30.25  ? 264  ALA B N   1 
ATOM   5841 C  CA  . ALA B 1 264 ? 4.614   -15.427 59.010  1.00 30.95  ? 264  ALA B CA  1 
ATOM   5842 C  C   . ALA B 1 264 ? 4.079   -14.077 58.565  1.00 29.35  ? 264  ALA B C   1 
ATOM   5843 O  O   . ALA B 1 264 ? 3.166   -13.534 59.201  1.00 32.91  ? 264  ALA B O   1 
ATOM   5844 C  CB  . ALA B 1 264 ? 5.710   -15.245 60.075  1.00 30.36  ? 264  ALA B CB  1 
ATOM   5845 N  N   . GLY B 1 265 ? 4.617   -13.525 57.483  1.00 30.73  ? 265  GLY B N   1 
ATOM   5846 C  CA  . GLY B 1 265 ? 4.198   -12.221 57.025  1.00 32.10  ? 265  GLY B CA  1 
ATOM   5847 C  C   . GLY B 1 265 ? 2.899   -12.200 56.249  1.00 31.40  ? 265  GLY B C   1 
ATOM   5848 O  O   . GLY B 1 265 ? 2.488   -11.117 55.834  1.00 32.62  ? 265  GLY B O   1 
ATOM   5849 N  N   . HIS B 1 266 ? 2.242   -13.343 56.036  1.00 31.95  ? 266  HIS B N   1 
ATOM   5850 C  CA  . HIS B 1 266 ? 0.930   -13.297 55.381  1.00 30.97  ? 266  HIS B CA  1 
ATOM   5851 C  C   . HIS B 1 266 ? -0.128  -14.203 56.008  1.00 31.39  ? 266  HIS B C   1 
ATOM   5852 O  O   . HIS B 1 266 ? -1.302  -13.825 56.030  1.00 31.01  ? 266  HIS B O   1 
ATOM   5853 C  CB  . HIS B 1 266 ? 1.062   -13.612 53.882  1.00 29.81  ? 266  HIS B CB  1 
ATOM   5854 C  CG  . HIS B 1 266 ? 0.807   -15.046 53.531  1.00 32.66  ? 266  HIS B CG  1 
ATOM   5855 N  ND1 . HIS B 1 266 ? 1.799   -16.004 53.540  1.00 32.33  ? 266  HIS B ND1 1 
ATOM   5856 C  CD2 . HIS B 1 266 ? -0.332  -15.690 53.173  1.00 31.11  ? 266  HIS B CD2 1 
ATOM   5857 C  CE1 . HIS B 1 266 ? 1.282   -17.179 53.219  1.00 30.95  ? 266  HIS B CE1 1 
ATOM   5858 N  NE2 . HIS B 1 266 ? -0.013  -17.016 52.997  1.00 32.60  ? 266  HIS B NE2 1 
ATOM   5859 N  N   . GLU B 1 267 ? 0.243   -15.395 56.488  1.00 30.86  ? 267  GLU B N   1 
ATOM   5860 C  CA  . GLU B 1 267 ? -0.770  -16.407 56.795  1.00 29.58  ? 267  GLU B CA  1 
ATOM   5861 C  C   . GLU B 1 267 ? -1.693  -15.948 57.919  1.00 29.40  ? 267  GLU B C   1 
ATOM   5862 O  O   . GLU B 1 267 ? -2.926  -15.990 57.790  1.00 29.91  ? 267  GLU B O   1 
ATOM   5863 C  CB  . GLU B 1 267 ? -0.085  -17.733 57.143  1.00 33.51  ? 267  GLU B CB  1 
ATOM   5864 C  CG  . GLU B 1 267 ? -0.914  -18.636 58.035  1.00 34.78  ? 267  GLU B CG  1 
ATOM   5865 C  CD  . GLU B 1 267 ? -2.091  -19.247 57.308  1.00 37.78  ? 267  GLU B CD  1 
ATOM   5866 O  OE1 . GLU B 1 267 ? -2.023  -19.388 56.080  1.00 37.69  ? 267  GLU B OE1 1 
ATOM   5867 O  OE2 . GLU B 1 267 ? -3.088  -19.599 57.978  1.00 42.25  ? 267  GLU B OE2 1 
ATOM   5868 N  N   . THR B 1 268 ? -1.114  -15.486 59.020  1.00 28.80  ? 268  THR B N   1 
ATOM   5869 C  CA  . THR B 1 268 ? -1.920  -15.046 60.162  1.00 29.71  ? 268  THR B CA  1 
ATOM   5870 C  C   . THR B 1 268 ? -2.723  -13.792 59.858  1.00 31.62  ? 268  THR B C   1 
ATOM   5871 O  O   . THR B 1 268 ? -3.777  -13.580 60.466  1.00 30.22  ? 268  THR B O   1 
ATOM   5872 C  CB  . THR B 1 268 ? -1.015  -14.810 61.364  1.00 31.56  ? 268  THR B CB  1 
ATOM   5873 O  OG1 . THR B 1 268 ? 0.157   -14.099 60.943  1.00 32.14  ? 268  THR B OG1 1 
ATOM   5874 C  CG2 . THR B 1 268 ? -0.598  -16.158 61.974  1.00 31.75  ? 268  THR B CG2 1 
ATOM   5875 N  N   . THR B 1 269 ? -2.244  -12.948 58.947  1.00 28.69  ? 269  THR B N   1 
ATOM   5876 C  CA  . THR B 1 269 ? -3.013  -11.761 58.586  1.00 30.46  ? 269  THR B CA  1 
ATOM   5877 C  C   . THR B 1 269 ? -4.180  -12.118 57.676  1.00 32.28  ? 269  THR B C   1 
ATOM   5878 O  O   . THR B 1 269 ? -5.237  -11.473 57.732  1.00 29.77  ? 269  THR B O   1 
ATOM   5879 C  CB  . THR B 1 269 ? -2.105  -10.722 57.912  1.00 29.87  ? 269  THR B CB  1 
ATOM   5880 O  OG1 . THR B 1 269 ? -1.011  -10.384 58.780  1.00 30.17  ? 269  THR B OG1 1 
ATOM   5881 C  CG2 . THR B 1 269 ? -2.868  -9.436  57.576  1.00 29.80  ? 269  THR B CG2 1 
ATOM   5882 N  N   . SER B 1 270 ? -4.009  -13.136 56.831  1.00 29.86  ? 270  SER B N   1 
ATOM   5883 C  CA  . SER B 1 270 ? -5.147  -13.648 56.065  1.00 29.03  ? 270  SER B CA  1 
ATOM   5884 C  C   . SER B 1 270 ? -6.220  -14.188 57.005  1.00 31.48  ? 270  SER B C   1 
ATOM   5885 O  O   . SER B 1 270 ? -7.420  -13.921 56.830  1.00 32.04  ? 270  SER B O   1 
ATOM   5886 C  CB  . SER B 1 270 ? -4.679  -14.749 55.106  1.00 29.68  ? 270  SER B CB  1 
ATOM   5887 O  OG  . SER B 1 270 ? -5.800  -15.426 54.553  1.00 37.46  ? 270  SER B OG  1 
ATOM   5888 N  N   . GLY B 1 271 ? -5.799  -14.968 58.008  1.00 31.75  ? 271  GLY B N   1 
ATOM   5889 C  CA  . GLY B 1 271 ? -6.738  -15.426 59.012  1.00 29.89  ? 271  GLY B CA  1 
ATOM   5890 C  C   . GLY B 1 271 ? -7.462  -14.283 59.697  1.00 30.01  ? 271  GLY B C   1 
ATOM   5891 O  O   . GLY B 1 271 ? -8.684  -14.327 59.864  1.00 30.41  ? 271  GLY B O   1 
ATOM   5892 N  N   . LEU B 1 272 ? -6.728  -13.237 60.091  1.00 30.52  ? 272  LEU B N   1 
ATOM   5893 C  CA  . LEU B 1 272 ? -7.367  -12.119 60.793  1.00 30.90  ? 272  LEU B CA  1 
ATOM   5894 C  C   . LEU B 1 272 ? -8.462  -11.484 59.941  1.00 31.50  ? 272  LEU B C   1 
ATOM   5895 O  O   . LEU B 1 272 ? -9.598  -11.286 60.399  1.00 32.00  ? 272  LEU B O   1 
ATOM   5896 C  CB  . LEU B 1 272 ? -6.319  -11.072 61.161  1.00 31.42  ? 272  LEU B CB  1 
ATOM   5897 C  CG  . LEU B 1 272 ? -6.839  -9.740  61.709  1.00 29.19  ? 272  LEU B CG  1 
ATOM   5898 C  CD1 . LEU B 1 272 ? -7.780  -9.924  62.926  1.00 27.83  ? 272  LEU B CD1 1 
ATOM   5899 C  CD2 . LEU B 1 272 ? -5.655  -8.853  62.072  1.00 32.67  ? 272  LEU B CD2 1 
ATOM   5900 N  N   . LEU B 1 273 ? -8.131  -11.135 58.700  1.00 28.16  ? 273  LEU B N   1 
ATOM   5901 C  CA  . LEU B 1 273 ? -9.112  -10.493 57.833  1.00 27.81  ? 273  LEU B CA  1 
ATOM   5902 C  C   . LEU B 1 273 ? -10.320 -11.393 57.639  1.00 30.95  ? 273  LEU B C   1 
ATOM   5903 O  O   . LEU B 1 273 ? -11.461 -10.916 57.625  1.00 31.13  ? 273  LEU B O   1 
ATOM   5904 C  CB  . LEU B 1 273 ? -8.478  -10.138 56.481  1.00 29.73  ? 273  LEU B CB  1 
ATOM   5905 C  CG  . LEU B 1 273 ? -7.577  -8.895  56.537  1.00 31.23  ? 273  LEU B CG  1 
ATOM   5906 C  CD1 . LEU B 1 273 ? -6.643  -8.794  55.317  1.00 32.52  ? 273  LEU B CD1 1 
ATOM   5907 C  CD2 . LEU B 1 273 ? -8.462  -7.655  56.631  1.00 33.99  ? 273  LEU B CD2 1 
ATOM   5908 N  N   . SER B 1 274 ? -10.084 -12.700 57.469  1.00 30.13  ? 274  SER B N   1 
ATOM   5909 C  CA  . SER B 1 274 ? -11.195 -13.622 57.272  1.00 30.98  ? 274  SER B CA  1 
ATOM   5910 C  C   . SER B 1 274 ? -12.092 -13.649 58.501  1.00 30.41  ? 274  SER B C   1 
ATOM   5911 O  O   . SER B 1 274 ? -13.316 -13.559 58.381  1.00 31.56  ? 274  SER B O   1 
ATOM   5912 C  CB  . SER B 1 274 ? -10.680 -15.035 56.942  1.00 31.49  ? 274  SER B CB  1 
ATOM   5913 O  OG  . SER B 1 274 ? -9.854  -15.036 55.775  1.00 30.29  ? 274  SER B OG  1 
ATOM   5914 N  N   . PHE B 1 275 ? -11.502 -13.788 59.698  1.00 28.82  ? 275  PHE B N   1 
ATOM   5915 C  CA  . PHE B 1 275 ? -12.317 -13.768 60.918  1.00 30.51  ? 275  PHE B CA  1 
ATOM   5916 C  C   . PHE B 1 275 ? -13.029 -12.429 61.081  1.00 32.75  ? 275  PHE B C   1 
ATOM   5917 O  O   . PHE B 1 275 ? -14.198 -12.380 61.493  1.00 33.30  ? 275  PHE B O   1 
ATOM   5918 C  CB  . PHE B 1 275 ? -11.460 -14.053 62.154  1.00 28.94  ? 275  PHE B CB  1 
ATOM   5919 C  CG  . PHE B 1 275 ? -11.206 -15.520 62.410  1.00 30.57  ? 275  PHE B CG  1 
ATOM   5920 C  CD1 . PHE B 1 275 ? -12.244 -16.374 62.822  1.00 31.91  ? 275  PHE B CD1 1 
ATOM   5921 C  CD2 . PHE B 1 275 ? -9.923  -16.040 62.271  1.00 30.75  ? 275  PHE B CD2 1 
ATOM   5922 C  CE1 . PHE B 1 275 ? -12.010 -17.720 63.080  1.00 31.76  ? 275  PHE B CE1 1 
ATOM   5923 C  CE2 . PHE B 1 275 ? -9.671  -17.384 62.525  1.00 33.17  ? 275  PHE B CE2 1 
ATOM   5924 C  CZ  . PHE B 1 275 ? -10.710 -18.235 62.921  1.00 34.67  ? 275  PHE B CZ  1 
ATOM   5925 N  N   . ALA B 1 276 ? -12.344 -11.328 60.761  1.00 29.38  ? 276  ALA B N   1 
ATOM   5926 C  CA  . ALA B 1 276 ? -12.963 -10.014 60.919  1.00 31.13  ? 276  ALA B CA  1 
ATOM   5927 C  C   . ALA B 1 276 ? -14.208 -9.888  60.043  1.00 32.05  ? 276  ALA B C   1 
ATOM   5928 O  O   . ALA B 1 276 ? -15.269 -9.437  60.503  1.00 31.62  ? 276  ALA B O   1 
ATOM   5929 C  CB  . ALA B 1 276 ? -11.951 -8.911  60.592  1.00 31.15  ? 276  ALA B CB  1 
ATOM   5930 N  N   . LEU B 1 277 ? -14.106 -10.299 58.774  1.00 30.02  ? 277  LEU B N   1 
ATOM   5931 C  CA  . LEU B 1 277 ? -15.281 -10.192 57.908  1.00 29.25  ? 277  LEU B CA  1 
ATOM   5932 C  C   . LEU B 1 277 ? -16.382 -11.133 58.370  1.00 32.40  ? 277  LEU B C   1 
ATOM   5933 O  O   . LEU B 1 277 ? -17.576 -10.790 58.297  1.00 31.05  ? 277  LEU B O   1 
ATOM   5934 C  CB  . LEU B 1 277 ? -14.902 -10.463 56.447  1.00 30.32  ? 277  LEU B CB  1 
ATOM   5935 C  CG  . LEU B 1 277 ? -16.043 -10.186 55.462  1.00 34.94  ? 277  LEU B CG  1 
ATOM   5936 C  CD1 . LEU B 1 277 ? -16.487 -8.731  55.526  1.00 34.88  ? 277  LEU B CD1 1 
ATOM   5937 C  CD2 . LEU B 1 277 ? -15.606 -10.565 54.043  1.00 35.79  ? 277  LEU B CD2 1 
ATOM   5938 N  N   . TYR B 1 278 ? -16.008 -12.326 58.839  1.00 30.39  ? 278  TYR B N   1 
ATOM   5939 C  CA  . TYR B 1 278 ? -16.998 -13.226 59.427  1.00 30.16  ? 278  TYR B CA  1 
ATOM   5940 C  C   . TYR B 1 278 ? -17.745 -12.543 60.563  1.00 33.60  ? 278  TYR B C   1 
ATOM   5941 O  O   . TYR B 1 278 ? -18.983 -12.526 60.593  1.00 31.31  ? 278  TYR B O   1 
ATOM   5942 C  CB  . TYR B 1 278 ? -16.332 -14.512 59.929  1.00 30.99  ? 278  TYR B CB  1 
ATOM   5943 C  CG  . TYR B 1 278 ? -17.238 -15.316 60.827  1.00 32.97  ? 278  TYR B CG  1 
ATOM   5944 C  CD1 . TYR B 1 278 ? -18.184 -16.193 60.288  1.00 32.63  ? 278  TYR B CD1 1 
ATOM   5945 C  CD2 . TYR B 1 278 ? -17.178 -15.174 62.216  1.00 32.66  ? 278  TYR B CD2 1 
ATOM   5946 C  CE1 . TYR B 1 278 ? -19.042 -16.908 61.121  1.00 35.82  ? 278  TYR B CE1 1 
ATOM   5947 C  CE2 . TYR B 1 278 ? -18.026 -15.895 63.055  1.00 34.33  ? 278  TYR B CE2 1 
ATOM   5948 C  CZ  . TYR B 1 278 ? -18.962 -16.753 62.498  1.00 36.19  ? 278  TYR B CZ  1 
ATOM   5949 O  OH  . TYR B 1 278 ? -19.813 -17.453 63.337  1.00 33.69  ? 278  TYR B OH  1 
ATOM   5950 N  N   . PHE B 1 279 ? -17.013 -11.992 61.532  1.00 31.07  ? 279  PHE B N   1 
ATOM   5951 C  CA  . PHE B 1 279 ? -17.707 -11.365 62.659  1.00 30.57  ? 279  PHE B CA  1 
ATOM   5952 C  C   . PHE B 1 279 ? -18.533 -10.161 62.217  1.00 31.47  ? 279  PHE B C   1 
ATOM   5953 O  O   . PHE B 1 279 ? -19.615 -9.921  62.759  1.00 31.96  ? 279  PHE B O   1 
ATOM   5954 C  CB  . PHE B 1 279 ? -16.706 -10.979 63.744  1.00 30.32  ? 279  PHE B CB  1 
ATOM   5955 C  CG  . PHE B 1 279 ? -16.270 -12.143 64.572  1.00 32.77  ? 279  PHE B CG  1 
ATOM   5956 C  CD1 . PHE B 1 279 ? -17.198 -12.871 65.315  1.00 32.61  ? 279  PHE B CD1 1 
ATOM   5957 C  CD2 . PHE B 1 279 ? -14.936 -12.549 64.587  1.00 31.76  ? 279  PHE B CD2 1 
ATOM   5958 C  CE1 . PHE B 1 279 ? -16.801 -13.960 66.094  1.00 35.82  ? 279  PHE B CE1 1 
ATOM   5959 C  CE2 . PHE B 1 279 ? -14.542 -13.647 65.351  1.00 33.60  ? 279  PHE B CE2 1 
ATOM   5960 C  CZ  . PHE B 1 279 ? -15.478 -14.349 66.108  1.00 34.69  ? 279  PHE B CZ  1 
ATOM   5961 N  N   . LEU B 1 280 ? -18.084 -9.428  61.210  1.00 32.04  ? 280  LEU B N   1 
ATOM   5962 C  CA  . LEU B 1 280 ? -18.861 -8.275  60.762  1.00 31.10  ? 280  LEU B CA  1 
ATOM   5963 C  C   . LEU B 1 280 ? -20.199 -8.703  60.160  1.00 33.19  ? 280  LEU B C   1 
ATOM   5964 O  O   . LEU B 1 280 ? -21.247 -8.130  60.485  1.00 33.98  ? 280  LEU B O   1 
ATOM   5965 C  CB  . LEU B 1 280 ? -18.045 -7.467  59.754  1.00 32.13  ? 280  LEU B CB  1 
ATOM   5966 C  CG  . LEU B 1 280 ? -16.920 -6.672  60.407  1.00 31.70  ? 280  LEU B CG  1 
ATOM   5967 C  CD1 . LEU B 1 280 ? -16.035 -6.057  59.322  1.00 34.36  ? 280  LEU B CD1 1 
ATOM   5968 C  CD2 . LEU B 1 280 ? -17.462 -5.586  61.319  1.00 38.66  ? 280  LEU B CD2 1 
ATOM   5969 N  N   . VAL B 1 281 ? -20.192 -9.705  59.278  1.00 31.80  ? 281  VAL B N   1 
ATOM   5970 C  CA  . VAL B 1 281 ? -21.471 -10.094 58.666  1.00 31.20  ? 281  VAL B CA  1 
ATOM   5971 C  C   . VAL B 1 281 ? -22.379 -10.781 59.678  1.00 35.05  ? 281  VAL B C   1 
ATOM   5972 O  O   . VAL B 1 281 ? -23.607 -10.801 59.489  1.00 34.25  ? 281  VAL B O   1 
ATOM   5973 C  CB  . VAL B 1 281 ? -21.294 -10.972 57.405  1.00 33.15  ? 281  VAL B CB  1 
ATOM   5974 C  CG1 . VAL B 1 281 ? -20.431 -10.270 56.374  1.00 36.34  ? 281  VAL B CG1 1 
ATOM   5975 C  CG2 . VAL B 1 281 ? -20.747 -12.375 57.741  1.00 33.46  ? 281  VAL B CG2 1 
ATOM   5976 N  N   . LYS B 1 282 ? -21.832 -11.328 60.762  1.00 30.56  ? 282  LYS B N   1 
ATOM   5977 C  CA  . LYS B 1 282 ? -22.672 -11.891 61.814  1.00 33.30  ? 282  LYS B CA  1 
ATOM   5978 C  C   . LYS B 1 282 ? -23.125 -10.852 62.837  1.00 33.36  ? 282  LYS B C   1 
ATOM   5979 O  O   . LYS B 1 282 ? -23.928 -11.185 63.717  1.00 34.04  ? 282  LYS B O   1 
ATOM   5980 C  CB  . LYS B 1 282 ? -21.932 -13.024 62.542  1.00 33.24  ? 282  LYS B CB  1 
ATOM   5981 C  CG  . LYS B 1 282 ? -21.533 -14.235 61.655  1.00 33.33  ? 282  LYS B CG  1 
ATOM   5982 C  CD  . LYS B 1 282 ? -22.776 -14.911 61.023  1.00 35.25  ? 282  LYS B CD  1 
ATOM   5983 C  CE  . LYS B 1 282 ? -22.429 -16.303 60.459  1.00 34.73  ? 282  LYS B CE  1 
ATOM   5984 N  NZ  . LYS B 1 282 ? -23.641 -16.923 59.815  1.00 33.03  ? 282  LYS B NZ  1 
ATOM   5985 N  N   . ASN B 1 283 ? -22.645 -9.610  62.753  1.00 34.20  ? 283  ASN B N   1 
ATOM   5986 C  CA  . ASN B 1 283 ? -22.965 -8.581  63.750  1.00 34.41  ? 283  ASN B CA  1 
ATOM   5987 C  C   . ASN B 1 283 ? -23.270 -7.276  63.033  1.00 33.71  ? 283  ASN B C   1 
ATOM   5988 O  O   . ASN B 1 283 ? -22.458 -6.343  63.003  1.00 32.42  ? 283  ASN B O   1 
ATOM   5989 C  CB  . ASN B 1 283 ? -21.836 -8.432  64.779  1.00 32.49  ? 283  ASN B CB  1 
ATOM   5990 C  CG  . ASN B 1 283 ? -21.701 -9.655  65.653  1.00 36.69  ? 283  ASN B CG  1 
ATOM   5991 O  OD1 . ASN B 1 283 ? -22.391 -9.779  66.673  1.00 33.25  ? 283  ASN B OD1 1 
ATOM   5992 N  ND2 . ASN B 1 283 ? -20.824 -10.597 65.244  1.00 31.09  ? 283  ASN B ND2 1 
ATOM   5993 N  N   . PRO B 1 284 ? -24.463 -7.174  62.452  1.00 31.82  ? 284  PRO B N   1 
ATOM   5994 C  CA  . PRO B 1 284 ? -24.797 -6.023  61.602  1.00 33.45  ? 284  PRO B CA  1 
ATOM   5995 C  C   . PRO B 1 284 ? -24.625 -4.670  62.270  1.00 33.42  ? 284  PRO B C   1 
ATOM   5996 O  O   . PRO B 1 284 ? -24.262 -3.703  61.590  1.00 33.24  ? 284  PRO B O   1 
ATOM   5997 C  CB  . PRO B 1 284 ? -26.275 -6.265  61.263  1.00 37.69  ? 284  PRO B CB  1 
ATOM   5998 C  CG  . PRO B 1 284 ? -26.516 -7.701  61.493  1.00 39.99  ? 284  PRO B CG  1 
ATOM   5999 C  CD  . PRO B 1 284 ? -25.515 -8.202  62.477  1.00 34.95  ? 284  PRO B CD  1 
ATOM   6000 N  N   . HIS B 1 285 ? -24.936 -4.551  63.562  1.00 32.00  ? 285  HIS B N   1 
ATOM   6001 C  CA  . HIS B 1 285 ? -24.728 -3.275  64.242  1.00 33.65  ? 285  HIS B CA  1 
ATOM   6002 C  C   . HIS B 1 285 ? -23.268 -2.868  64.161  1.00 34.11  ? 285  HIS B C   1 
ATOM   6003 O  O   . HIS B 1 285 ? -22.951 -1.694  63.948  1.00 35.15  ? 285  HIS B O   1 
ATOM   6004 C  CB  . HIS B 1 285 ? -25.142 -3.373  65.713  1.00 34.25  ? 285  HIS B CB  1 
ATOM   6005 C  CG  . HIS B 1 285 ? -26.624 -3.422  65.927  1.00 32.35  ? 285  HIS B CG  1 
ATOM   6006 N  ND1 . HIS B 1 285 ? -27.478 -2.472  65.414  1.00 38.97  ? 285  HIS B ND1 1 
ATOM   6007 C  CD2 . HIS B 1 285 ? -27.400 -4.315  66.584  1.00 35.17  ? 285  HIS B CD2 1 
ATOM   6008 C  CE1 . HIS B 1 285 ? -28.719 -2.765  65.766  1.00 36.18  ? 285  HIS B CE1 1 
ATOM   6009 N  NE2 . HIS B 1 285 ? -28.700 -3.880  66.470  1.00 34.11  ? 285  HIS B NE2 1 
ATOM   6010 N  N   . VAL B 1 286 ? -22.369 -3.831  64.372  1.00 32.12  ? 286  VAL B N   1 
ATOM   6011 C  CA  . VAL B 1 286 ? -20.934 -3.543  64.326  1.00 32.34  ? 286  VAL B CA  1 
ATOM   6012 C  C   . VAL B 1 286 ? -20.494 -3.235  62.898  1.00 32.39  ? 286  VAL B C   1 
ATOM   6013 O  O   . VAL B 1 286 ? -19.704 -2.312  62.652  1.00 31.21  ? 286  VAL B O   1 
ATOM   6014 C  CB  . VAL B 1 286 ? -20.147 -4.728  64.915  1.00 34.04  ? 286  VAL B CB  1 
ATOM   6015 C  CG1 . VAL B 1 286 ? -18.627 -4.500  64.754  1.00 30.34  ? 286  VAL B CG1 1 
ATOM   6016 C  CG2 . VAL B 1 286 ? -20.526 -4.967  66.371  1.00 31.92  ? 286  VAL B CG2 1 
ATOM   6017 N  N   . LEU B 1 287 ? -20.987 -4.006  61.932  1.00 32.15  ? 287  LEU B N   1 
ATOM   6018 C  CA  . LEU B 1 287 ? -20.682 -3.706  60.543  1.00 32.05  ? 287  LEU B CA  1 
ATOM   6019 C  C   . LEU B 1 287 ? -21.085 -2.277  60.189  1.00 33.41  ? 287  LEU B C   1 
ATOM   6020 O  O   . LEU B 1 287 ? -20.327 -1.548  59.540  1.00 34.47  ? 287  LEU B O   1 
ATOM   6021 C  CB  . LEU B 1 287 ? -21.379 -4.726  59.645  1.00 32.09  ? 287  LEU B CB  1 
ATOM   6022 C  CG  . LEU B 1 287 ? -21.255 -4.567  58.137  1.00 36.04  ? 287  LEU B CG  1 
ATOM   6023 C  CD1 . LEU B 1 287 ? -19.839 -4.280  57.755  1.00 39.62  ? 287  LEU B CD1 1 
ATOM   6024 C  CD2 . LEU B 1 287 ? -21.727 -5.859  57.468  1.00 42.03  ? 287  LEU B CD2 1 
ATOM   6025 N  N   . GLN B 1 288 ? -22.267 -1.844  60.631  1.00 35.35  ? 288  GLN B N   1 
ATOM   6026 C  CA  . GLN B 1 288 ? -22.713 -0.486  60.321  1.00 35.33  ? 288  GLN B CA  1 
ATOM   6027 C  C   . GLN B 1 288 ? -21.752 0.555   60.879  1.00 33.76  ? 288  GLN B C   1 
ATOM   6028 O  O   . GLN B 1 288 ? -21.405 1.521   60.189  1.00 32.12  ? 288  GLN B O   1 
ATOM   6029 C  CB  . GLN B 1 288 ? -24.117 -0.255  60.878  1.00 38.98  ? 288  GLN B CB  1 
ATOM   6030 C  CG  . GLN B 1 288 ? -24.712 1.117   60.544  1.00 45.07  ? 288  GLN B CG  1 
ATOM   6031 C  CD  . GLN B 1 288 ? -26.168 1.244   60.986  1.00 57.35  ? 288  GLN B CD  1 
ATOM   6032 O  OE1 . GLN B 1 288 ? -26.458 1.447   62.166  1.00 61.06  ? 288  GLN B OE1 1 
ATOM   6033 N  NE2 . GLN B 1 288 ? -27.088 1.100   60.039  1.00 60.43  ? 288  GLN B NE2 1 
ATOM   6034 N  N   . LYS B 1 289 ? -21.311 0.374   62.129  1.00 32.94  ? 289  LYS B N   1 
ATOM   6035 C  CA  . LYS B 1 289 ? -20.409 1.353   62.734  1.00 32.18  ? 289  LYS B CA  1 
ATOM   6036 C  C   . LYS B 1 289 ? -19.075 1.377   62.013  1.00 32.86  ? 289  LYS B C   1 
ATOM   6037 O  O   . LYS B 1 289 ? -18.504 2.448   61.788  1.00 32.30  ? 289  LYS B O   1 
ATOM   6038 C  CB  . LYS B 1 289 ? -20.196 1.052   64.222  1.00 34.05  ? 289  LYS B CB  1 
ATOM   6039 C  CG  . LYS B 1 289 ? -21.344 1.552   65.112  1.00 40.86  ? 289  LYS B CG  1 
ATOM   6040 C  CD  . LYS B 1 289 ? -21.167 1.124   66.580  1.00 37.97  ? 289  LYS B CD  1 
ATOM   6041 C  CE  . LYS B 1 289 ? -20.088 1.917   67.323  1.00 37.16  ? 289  LYS B CE  1 
ATOM   6042 N  NZ  . LYS B 1 289 ? -20.255 1.784   68.829  1.00 34.56  ? 289  LYS B NZ  1 
ATOM   6043 N  N   . ALA B 1 290 ? -18.558 0.202   61.642  1.00 32.28  ? 290  ALA B N   1 
ATOM   6044 C  CA  . ALA B 1 290 ? -17.287 0.174   60.929  1.00 30.39  ? 290  ALA B CA  1 
ATOM   6045 C  C   . ALA B 1 290 ? -17.429 0.777   59.539  1.00 31.80  ? 290  ALA B C   1 
ATOM   6046 O  O   . ALA B 1 290 ? -16.549 1.518   59.075  1.00 32.20  ? 290  ALA B O   1 
ATOM   6047 C  CB  . ALA B 1 290 ? -16.771 -1.266  60.845  1.00 33.58  ? 290  ALA B CB  1 
ATOM   6048 N  N   . ALA B 1 291 ? -18.527 0.471   58.850  1.00 30.47  ? 291  ALA B N   1 
ATOM   6049 C  CA  . ALA B 1 291 ? -18.718 1.014   57.511  1.00 33.55  ? 291  ALA B CA  1 
ATOM   6050 C  C   . ALA B 1 291 ? -18.894 2.533   57.542  1.00 32.39  ? 291  ALA B C   1 
ATOM   6051 O  O   . ALA B 1 291 ? -18.420 3.235   56.645  1.00 32.33  ? 291  ALA B O   1 
ATOM   6052 C  CB  . ALA B 1 291 ? -19.909 0.322   56.835  1.00 34.67  ? 291  ALA B CB  1 
ATOM   6053 N  N   . GLU B 1 292 ? -19.601 3.061   58.540  1.00 33.10  ? 292  GLU B N   1 
ATOM   6054 C  CA  . GLU B 1 292 ? -19.688 4.514   58.694  1.00 34.88  ? 292  GLU B CA  1 
ATOM   6055 C  C   . GLU B 1 292 ? -18.311 5.150   58.752  1.00 32.26  ? 292  GLU B C   1 
ATOM   6056 O  O   . GLU B 1 292 ? -18.040 6.150   58.080  1.00 34.27  ? 292  GLU B O   1 
ATOM   6057 C  CB  . GLU B 1 292 ? -20.465 4.867   59.962  1.00 35.61  ? 292  GLU B CB  1 
ATOM   6058 C  CG  . GLU B 1 292 ? -20.864 6.345   60.025  1.00 36.40  ? 292  GLU B CG  1 
ATOM   6059 C  CD  . GLU B 1 292 ? -19.740 7.267   60.541  1.00 38.77  ? 292  GLU B CD  1 
ATOM   6060 O  OE1 . GLU B 1 292 ? -18.835 6.812   61.292  1.00 36.59  ? 292  GLU B OE1 1 
ATOM   6061 O  OE2 . GLU B 1 292 ? -19.760 8.459   60.166  1.00 39.58  ? 292  GLU B OE2 1 
ATOM   6062 N  N   . GLU B 1 293 ? -17.431 4.585   59.572  1.00 31.45  ? 293  GLU B N   1 
ATOM   6063 C  CA  . GLU B 1 293 ? -16.103 5.172   59.726  1.00 31.33  ? 293  GLU B CA  1 
ATOM   6064 C  C   . GLU B 1 293 ? -15.323 5.115   58.423  1.00 34.24  ? 293  GLU B C   1 
ATOM   6065 O  O   . GLU B 1 293 ? -14.693 6.102   58.012  1.00 33.52  ? 293  GLU B O   1 
ATOM   6066 C  CB  . GLU B 1 293 ? -15.347 4.452   60.836  1.00 32.75  ? 293  GLU B CB  1 
ATOM   6067 C  CG  . GLU B 1 293 ? -13.997 5.069   61.113  1.00 32.56  ? 293  GLU B CG  1 
ATOM   6068 C  CD  . GLU B 1 293 ? -13.282 4.333   62.218  1.00 34.28  ? 293  GLU B CD  1 
ATOM   6069 O  OE1 . GLU B 1 293 ? -12.729 3.248   61.929  1.00 32.12  ? 293  GLU B OE1 1 
ATOM   6070 O  OE2 . GLU B 1 293 ? -13.287 4.832   63.362  1.00 35.76  ? 293  GLU B OE2 1 
ATOM   6071 N  N   . ALA B 1 294 ? -15.332 3.953   57.768  1.00 31.76  ? 294  ALA B N   1 
ATOM   6072 C  CA  . ALA B 1 294 ? -14.597 3.827   56.518  1.00 32.91  ? 294  ALA B CA  1 
ATOM   6073 C  C   . ALA B 1 294 ? -15.096 4.837   55.496  1.00 35.63  ? 294  ALA B C   1 
ATOM   6074 O  O   . ALA B 1 294 ? -14.297 5.466   54.801  1.00 34.68  ? 294  ALA B O   1 
ATOM   6075 C  CB  . ALA B 1 294 ? -14.706 2.397   55.980  1.00 33.74  ? 294  ALA B CB  1 
ATOM   6076 N  N   . ALA B 1 295 ? -16.419 4.999   55.383  1.00 34.27  ? 295  ALA B N   1 
ATOM   6077 C  CA  . ALA B 1 295 ? -16.964 5.935   54.400  1.00 36.92  ? 295  ALA B CA  1 
ATOM   6078 C  C   . ALA B 1 295 ? -16.562 7.368   54.725  1.00 38.00  ? 295  ALA B C   1 
ATOM   6079 O  O   . ALA B 1 295 ? -16.240 8.158   53.828  1.00 38.76  ? 295  ALA B O   1 
ATOM   6080 C  CB  . ALA B 1 295 ? -18.490 5.808   54.349  1.00 35.05  ? 295  ALA B CB  1 
ATOM   6081 N  N   . ARG B 1 296 ? -16.564 7.717   56.009  1.00 36.36  ? 296  ARG B N   1 
ATOM   6082 C  CA  . ARG B 1 296 ? -16.296 9.089   56.417  1.00 35.43  ? 296  ARG B CA  1 
ATOM   6083 C  C   . ARG B 1 296 ? -14.815 9.438   56.307  1.00 36.60  ? 296  ARG B C   1 
ATOM   6084 O  O   . ARG B 1 296 ? -14.464 10.559  55.923  1.00 36.58  ? 296  ARG B O   1 
ATOM   6085 C  CB  . ARG B 1 296 ? -16.786 9.289   57.847  1.00 36.51  ? 296  ARG B CB  1 
ATOM   6086 C  CG  . ARG B 1 296 ? -16.259 10.534  58.508  1.00 37.86  ? 296  ARG B CG  1 
ATOM   6087 C  CD  . ARG B 1 296 ? -17.118 10.834  59.731  1.00 39.37  ? 296  ARG B CD  1 
ATOM   6088 N  NE  . ARG B 1 296 ? -17.235 9.686   60.626  1.00 38.58  ? 296  ARG B NE  1 
ATOM   6089 C  CZ  . ARG B 1 296 ? -16.370 9.409   61.596  1.00 40.58  ? 296  ARG B CZ  1 
ATOM   6090 N  NH1 . ARG B 1 296 ? -15.298 10.159  61.796  1.00 40.46  ? 296  ARG B NH1 1 
ATOM   6091 N  NH2 . ARG B 1 296 ? -16.585 8.355   62.384  1.00 40.81  ? 296  ARG B NH2 1 
ATOM   6092 N  N   . VAL B 1 297 ? -13.939 8.498   56.648  1.00 34.63  ? 297  VAL B N   1 
ATOM   6093 C  CA  . VAL B 1 297 ? -12.504 8.770   56.733  1.00 35.48  ? 297  VAL B CA  1 
ATOM   6094 C  C   . VAL B 1 297 ? -11.817 8.627   55.378  1.00 36.03  ? 297  VAL B C   1 
ATOM   6095 O  O   . VAL B 1 297 ? -10.975 9.456   55.005  1.00 34.95  ? 297  VAL B O   1 
ATOM   6096 C  CB  . VAL B 1 297 ? -11.894 7.822   57.786  1.00 34.80  ? 297  VAL B CB  1 
ATOM   6097 C  CG1 . VAL B 1 297 ? -10.343 7.786   57.696  1.00 37.66  ? 297  VAL B CG1 1 
ATOM   6098 C  CG2 . VAL B 1 297 ? -12.346 8.250   59.171  1.00 37.13  ? 297  VAL B CG2 1 
ATOM   6099 N  N   . LEU B 1 298 ? -12.142 7.569   54.629  1.00 34.38  ? 298  LEU B N   1 
ATOM   6100 C  CA  . LEU B 1 298 ? -11.466 7.285   53.358  1.00 37.18  ? 298  LEU B CA  1 
ATOM   6101 C  C   . LEU B 1 298 ? -12.122 8.087   52.230  1.00 36.92  ? 298  LEU B C   1 
ATOM   6102 O  O   . LEU B 1 298 ? -12.784 7.556   51.333  1.00 37.50  ? 298  LEU B O   1 
ATOM   6103 C  CB  . LEU B 1 298 ? -11.498 5.791   53.070  1.00 34.06  ? 298  LEU B CB  1 
ATOM   6104 C  CG  . LEU B 1 298 ? -10.855 4.934   54.147  1.00 33.11  ? 298  LEU B CG  1 
ATOM   6105 C  CD1 . LEU B 1 298 ? -10.897 3.474   53.710  1.00 36.78  ? 298  LEU B CD1 1 
ATOM   6106 C  CD2 . LEU B 1 298 ? -9.421  5.377   54.367  1.00 32.57  ? 298  LEU B CD2 1 
ATOM   6107 N  N   . VAL B 1 299 ? -11.911 9.406   52.279  1.00 36.71  ? 299  VAL B N   1 
ATOM   6108 C  CA  . VAL B 1 299 ? -12.588 10.303  51.341  1.00 38.26  ? 299  VAL B CA  1 
ATOM   6109 C  C   . VAL B 1 299 ? -11.929 10.372  49.977  1.00 39.48  ? 299  VAL B C   1 
ATOM   6110 O  O   . VAL B 1 299 ? -12.500 10.974  49.065  1.00 40.56  ? 299  VAL B O   1 
ATOM   6111 C  CB  . VAL B 1 299 ? -12.664 11.736  51.897  1.00 39.99  ? 299  VAL B CB  1 
ATOM   6112 C  CG1 . VAL B 1 299 ? -13.507 11.739  53.150  1.00 41.83  ? 299  VAL B CG1 1 
ATOM   6113 C  CG2 . VAL B 1 299 ? -11.268 12.260  52.188  1.00 40.66  ? 299  VAL B CG2 1 
ATOM   6114 N  N   . ASP B 1 300 ? -10.748 9.801   49.816  1.00 37.85  ? 300  ASP B N   1 
ATOM   6115 C  CA  . ASP B 1 300 ? -10.032 9.835   48.555  1.00 41.49  ? 300  ASP B CA  1 
ATOM   6116 C  C   . ASP B 1 300 ? -10.014 8.454   47.904  1.00 40.49  ? 300  ASP B C   1 
ATOM   6117 O  O   . ASP B 1 300 ? -10.059 7.428   48.595  1.00 38.16  ? 300  ASP B O   1 
ATOM   6118 C  CB  . ASP B 1 300 ? -8.589  10.318  48.757  1.00 38.98  ? 300  ASP B CB  1 
ATOM   6119 C  CG  . ASP B 1 300 ? -8.514  11.725  49.354  1.00 42.24  ? 300  ASP B CG  1 
ATOM   6120 O  OD1 . ASP B 1 300 ? -9.247  12.603  48.871  1.00 45.68  ? 300  ASP B OD1 1 
ATOM   6121 O  OD2 . ASP B 1 300 ? -7.722  11.957  50.293  1.00 41.34  ? 300  ASP B OD2 1 
ATOM   6122 N  N   . PRO B 1 301 ? -9.912  8.397   46.576  1.00 39.17  ? 301  PRO B N   1 
ATOM   6123 C  CA  . PRO B 1 301 ? -9.871  7.086   45.905  1.00 41.69  ? 301  PRO B CA  1 
ATOM   6124 C  C   . PRO B 1 301 ? -8.677  6.248   46.318  1.00 39.54  ? 301  PRO B C   1 
ATOM   6125 O  O   . PRO B 1 301 ? -8.769  5.016   46.321  1.00 42.83  ? 301  PRO B O   1 
ATOM   6126 C  CB  . PRO B 1 301 ? -9.811  7.434   44.410  1.00 44.56  ? 301  PRO B CB  1 
ATOM   6127 C  CG  . PRO B 1 301 ? -9.901  8.914   44.298  1.00 48.04  ? 301  PRO B CG  1 
ATOM   6128 C  CD  . PRO B 1 301 ? -9.870  9.541   45.651  1.00 46.35  ? 301  PRO B CD  1 
ATOM   6129 N  N   . VAL B 1 302 ? -7.553  6.878   46.643  1.00 37.66  ? 302  VAL B N   1 
ATOM   6130 C  CA  . VAL B 1 302 ? -6.363  6.202   47.148  1.00 42.89  ? 302  VAL B CA  1 
ATOM   6131 C  C   . VAL B 1 302 ? -6.234  6.554   48.630  1.00 41.60  ? 302  VAL B C   1 
ATOM   6132 O  O   . VAL B 1 302 ? -5.974  7.719   48.959  1.00 43.60  ? 302  VAL B O   1 
ATOM   6133 C  CB  . VAL B 1 302 ? -5.107  6.620   46.366  1.00 41.88  ? 302  VAL B CB  1 
ATOM   6134 C  CG1 . VAL B 1 302 ? -3.913  5.784   46.773  1.00 44.48  ? 302  VAL B CG1 1 
ATOM   6135 C  CG2 . VAL B 1 302 ? -5.345  6.527   44.851  1.00 45.94  ? 302  VAL B CG2 1 
ATOM   6136 N  N   . PRO B 1 303 ? -6.429  5.606   49.554  1.00 38.17  ? 303  PRO B N   1 
ATOM   6137 C  CA  . PRO B 1 303 ? -6.262  5.928   50.979  1.00 41.32  ? 303  PRO B CA  1 
ATOM   6138 C  C   . PRO B 1 303 ? -4.825  6.306   51.283  1.00 35.75  ? 303  PRO B C   1 
ATOM   6139 O  O   . PRO B 1 303 ? -3.886  5.742   50.723  1.00 37.19  ? 303  PRO B O   1 
ATOM   6140 C  CB  . PRO B 1 303 ? -6.655  4.629   51.693  1.00 41.75  ? 303  PRO B CB  1 
ATOM   6141 C  CG  . PRO B 1 303 ? -7.482  3.866   50.671  1.00 43.21  ? 303  PRO B CG  1 
ATOM   6142 C  CD  . PRO B 1 303 ? -6.883  4.221   49.347  1.00 40.33  ? 303  PRO B CD  1 
ATOM   6143 N  N   . SER B 1 304 ? -4.660  7.280   52.162  1.00 33.63  ? 304  SER B N   1 
ATOM   6144 C  CA  . SER B 1 304 ? -3.337  7.689   52.607  1.00 36.12  ? 304  SER B CA  1 
ATOM   6145 C  C   . SER B 1 304 ? -2.972  7.002   53.920  1.00 34.19  ? 304  SER B C   1 
ATOM   6146 O  O   . SER B 1 304 ? -3.814  6.472   54.645  1.00 32.87  ? 304  SER B O   1 
ATOM   6147 C  CB  . SER B 1 304 ? -3.268  9.210   52.796  1.00 36.51  ? 304  SER B CB  1 
ATOM   6148 O  OG  . SER B 1 304 ? -4.092  9.594   53.890  1.00 37.56  ? 304  SER B OG  1 
ATOM   6149 N  N   . TYR B 1 305 ? -1.681  7.050   54.234  1.00 33.89  ? 305  TYR B N   1 
ATOM   6150 C  CA  . TYR B 1 305 ? -1.209  6.516   55.504  1.00 36.89  ? 305  TYR B CA  1 
ATOM   6151 C  C   . TYR B 1 305 ? -1.938  7.154   56.681  1.00 34.94  ? 305  TYR B C   1 
ATOM   6152 O  O   . TYR B 1 305 ? -2.427  6.455   57.579  1.00 35.75  ? 305  TYR B O   1 
ATOM   6153 C  CB  . TYR B 1 305 ? 0.296   6.744   55.593  1.00 38.66  ? 305  TYR B CB  1 
ATOM   6154 C  CG  . TYR B 1 305 ? 0.921   6.258   56.861  1.00 40.05  ? 305  TYR B CG  1 
ATOM   6155 C  CD1 . TYR B 1 305 ? 1.375   4.953   56.976  1.00 39.82  ? 305  TYR B CD1 1 
ATOM   6156 C  CD2 . TYR B 1 305 ? 1.085   7.116   57.937  1.00 44.59  ? 305  TYR B CD2 1 
ATOM   6157 C  CE1 . TYR B 1 305 ? 1.958   4.509   58.140  1.00 42.30  ? 305  TYR B CE1 1 
ATOM   6158 C  CE2 . TYR B 1 305 ? 1.663   6.681   59.098  1.00 47.08  ? 305  TYR B CE2 1 
ATOM   6159 C  CZ  . TYR B 1 305 ? 2.102   5.379   59.190  1.00 47.00  ? 305  TYR B CZ  1 
ATOM   6160 O  OH  . TYR B 1 305 ? 2.685   4.948   60.355  1.00 56.15  ? 305  TYR B OH  1 
ATOM   6161 N  N   . LYS B 1 306 ? -2.023  8.493   56.693  1.00 34.22  ? 306  LYS B N   1 
ATOM   6162 C  CA  . LYS B 1 306 ? -2.706  9.191   57.779  1.00 36.27  ? 306  LYS B CA  1 
ATOM   6163 C  C   . LYS B 1 306 ? -4.167  8.774   57.888  1.00 32.69  ? 306  LYS B C   1 
ATOM   6164 O  O   . LYS B 1 306 ? -4.697  8.638   58.994  1.00 35.23  ? 306  LYS B O   1 
ATOM   6165 C  CB  . LYS B 1 306 ? -2.616  10.710  57.575  1.00 42.58  ? 306  LYS B CB  1 
ATOM   6166 C  CG  . LYS B 1 306 ? -1.437  11.366  58.278  1.00 47.43  ? 306  LYS B CG  1 
ATOM   6167 C  CD  . LYS B 1 306 ? -1.088  12.709  57.646  1.00 56.88  ? 306  LYS B CD  1 
ATOM   6168 C  CE  . LYS B 1 306 ? 0.234   13.251  58.182  1.00 59.81  ? 306  LYS B CE  1 
ATOM   6169 N  NZ  . LYS B 1 306 ? 1.394   12.651  57.461  1.00 63.11  ? 306  LYS B NZ  1 
ATOM   6170 N  N   . GLN B 1 307 ? -4.847  8.592   56.752  1.00 34.74  ? 307  GLN B N   1 
ATOM   6171 C  CA  . GLN B 1 307 ? -6.254  8.196   56.813  1.00 36.69  ? 307  GLN B CA  1 
ATOM   6172 C  C   . GLN B 1 307 ? -6.415  6.806   57.422  1.00 36.06  ? 307  GLN B C   1 
ATOM   6173 O  O   . GLN B 1 307 ? -7.341  6.566   58.208  1.00 33.77  ? 307  GLN B O   1 
ATOM   6174 C  CB  . GLN B 1 307 ? -6.890  8.250   55.417  1.00 35.92  ? 307  GLN B CB  1 
ATOM   6175 C  CG  . GLN B 1 307 ? -7.171  9.666   54.922  1.00 36.33  ? 307  GLN B CG  1 
ATOM   6176 C  CD  . GLN B 1 307 ? -7.433  9.710   53.421  1.00 39.92  ? 307  GLN B CD  1 
ATOM   6177 O  OE1 . GLN B 1 307 ? -7.154  8.748   52.701  1.00 39.06  ? 307  GLN B OE1 1 
ATOM   6178 N  NE2 . GLN B 1 307 ? -7.964  10.828  52.944  1.00 39.27  ? 307  GLN B NE2 1 
ATOM   6179 N  N   . VAL B 1 308 ? -5.526  5.868   57.085  1.00 32.87  ? 308  VAL B N   1 
ATOM   6180 C  CA  . VAL B 1 308 ? -5.633  4.542   57.694  1.00 33.27  ? 308  VAL B CA  1 
ATOM   6181 C  C   . VAL B 1 308 ? -5.472  4.649   59.206  1.00 34.89  ? 308  VAL B C   1 
ATOM   6182 O  O   . VAL B 1 308 ? -6.175  3.980   59.976  1.00 34.71  ? 308  VAL B O   1 
ATOM   6183 C  CB  . VAL B 1 308 ? -4.609  3.570   57.078  1.00 33.65  ? 308  VAL B CB  1 
ATOM   6184 C  CG1 . VAL B 1 308 ? -4.603  2.236   57.860  1.00 32.58  ? 308  VAL B CG1 1 
ATOM   6185 C  CG2 . VAL B 1 308 ? -4.922  3.323   55.594  1.00 34.12  ? 308  VAL B CG2 1 
ATOM   6186 N  N   . LYS B 1 309 ? -4.572  5.523   59.659  1.00 32.54  ? 309  LYS B N   1 
ATOM   6187 C  CA  . LYS B 1 309 ? -4.381  5.705   61.091  1.00 36.25  ? 309  LYS B CA  1 
ATOM   6188 C  C   . LYS B 1 309 ? -5.627  6.247   61.777  1.00 36.73  ? 309  LYS B C   1 
ATOM   6189 O  O   . LYS B 1 309 ? -5.767  6.089   62.995  1.00 36.11  ? 309  LYS B O   1 
ATOM   6190 C  CB  . LYS B 1 309 ? -3.192  6.637   61.351  1.00 37.90  ? 309  LYS B CB  1 
ATOM   6191 C  CG  . LYS B 1 309 ? -1.865  6.072   60.865  1.00 42.01  ? 309  LYS B CG  1 
ATOM   6192 C  CD  . LYS B 1 309 ? -1.638  4.709   61.486  1.00 46.79  ? 309  LYS B CD  1 
ATOM   6193 C  CE  . LYS B 1 309 ? -0.185  4.289   61.420  1.00 55.39  ? 309  LYS B CE  1 
ATOM   6194 N  NZ  . LYS B 1 309 ? 0.018   3.040   62.210  1.00 60.15  ? 309  LYS B NZ  1 
ATOM   6195 N  N   . GLN B 1 310 ? -6.539  6.868   61.036  1.00 32.31  ? 310  GLN B N   1 
ATOM   6196 C  CA  . GLN B 1 310 ? -7.769  7.389   61.634  1.00 32.72  ? 310  GLN B CA  1 
ATOM   6197 C  C   . GLN B 1 310 ? -8.886  6.360   61.736  1.00 35.88  ? 310  GLN B C   1 
ATOM   6198 O  O   . GLN B 1 310 ? -9.954  6.680   62.282  1.00 35.09  ? 310  GLN B O   1 
ATOM   6199 C  CB  . GLN B 1 310 ? -8.302  8.578   60.827  1.00 37.54  ? 310  GLN B CB  1 
ATOM   6200 C  CG  . GLN B 1 310 ? -7.475  9.845   60.869  1.00 37.41  ? 310  GLN B CG  1 
ATOM   6201 C  CD  . GLN B 1 310 ? -8.038  10.876  59.898  1.00 41.15  ? 310  GLN B CD  1 
ATOM   6202 O  OE1 . GLN B 1 310 ? -7.982  10.689  58.687  1.00 43.20  ? 310  GLN B OE1 1 
ATOM   6203 N  NE2 . GLN B 1 310 ? -8.603  11.952  60.429  1.00 46.80  ? 310  GLN B NE2 1 
ATOM   6204 N  N   . LEU B 1 311 ? -8.703  5.158   61.195  1.00 31.72  ? 311  LEU B N   1 
ATOM   6205 C  CA  . LEU B 1 311 ? -9.756  4.139   61.232  1.00 31.41  ? 311  LEU B CA  1 
ATOM   6206 C  C   . LEU B 1 311 ? -9.708  3.427   62.586  1.00 34.78  ? 311  LEU B C   1 
ATOM   6207 O  O   . LEU B 1 311 ? -9.380  2.244   62.703  1.00 33.26  ? 311  LEU B O   1 
ATOM   6208 C  CB  . LEU B 1 311 ? -9.602  3.169   60.066  1.00 30.31  ? 311  LEU B CB  1 
ATOM   6209 C  CG  . LEU B 1 311 ? -9.740  3.782   58.671  1.00 31.69  ? 311  LEU B CG  1 
ATOM   6210 C  CD1 . LEU B 1 311 ? -9.329  2.742   57.625  1.00 32.68  ? 311  LEU B CD1 1 
ATOM   6211 C  CD2 . LEU B 1 311 ? -11.200 4.273   58.459  1.00 32.99  ? 311  LEU B CD2 1 
ATOM   6212 N  N   . LYS B 1 312 ? -10.079 4.183   63.628  1.00 31.81  ? 312  LYS B N   1 
ATOM   6213 C  CA  . LYS B 1 312 ? -9.966  3.689   65.001  1.00 33.26  ? 312  LYS B CA  1 
ATOM   6214 C  C   . LYS B 1 312 ? -10.894 2.498   65.242  1.00 34.97  ? 312  LYS B C   1 
ATOM   6215 O  O   . LYS B 1 312 ? -10.490 1.485   65.836  1.00 31.59  ? 312  LYS B O   1 
ATOM   6216 C  CB  . LYS B 1 312 ? -10.263 4.837   65.975  1.00 39.10  ? 312  LYS B CB  1 
ATOM   6217 C  CG  . LYS B 1 312 ? -10.322 4.439   67.452  1.00 45.02  ? 312  LYS B CG  1 
ATOM   6218 C  CD  . LYS B 1 312 ? -10.679 5.655   68.329  1.00 53.58  ? 312  LYS B CD  1 
ATOM   6219 C  CE  . LYS B 1 312 ? -10.444 5.411   69.828  1.00 58.02  ? 312  LYS B CE  1 
ATOM   6220 N  NZ  . LYS B 1 312 ? -9.947  4.050   70.148  1.00 57.03  ? 312  LYS B NZ  1 
ATOM   6221 N  N   . TYR B 1 313 ? -12.156 2.612   64.809  1.00 31.14  ? 313  TYR B N   1 
ATOM   6222 C  CA  . TYR B 1 313 ? -13.115 1.538   65.065  1.00 32.42  ? 313  TYR B CA  1 
ATOM   6223 C  C   . TYR B 1 313 ? -12.817 0.317   64.207  1.00 30.71  ? 313  TYR B C   1 
ATOM   6224 O  O   . TYR B 1 313 ? -12.995 -0.823  64.661  1.00 32.33  ? 313  TYR B O   1 
ATOM   6225 C  CB  . TYR B 1 313 ? -14.552 2.024   64.828  1.00 30.83  ? 313  TYR B CB  1 
ATOM   6226 C  CG  . TYR B 1 313 ? -15.601 1.045   65.347  1.00 33.42  ? 313  TYR B CG  1 
ATOM   6227 C  CD1 . TYR B 1 313 ? -16.032 1.086   66.668  1.00 34.37  ? 313  TYR B CD1 1 
ATOM   6228 C  CD2 . TYR B 1 313 ? -16.159 0.083   64.503  1.00 30.42  ? 313  TYR B CD2 1 
ATOM   6229 C  CE1 . TYR B 1 313 ? -16.979 0.193   67.152  1.00 35.51  ? 313  TYR B CE1 1 
ATOM   6230 C  CE2 . TYR B 1 313 ? -17.116 -0.832  64.979  1.00 31.10  ? 313  TYR B CE2 1 
ATOM   6231 C  CZ  . TYR B 1 313 ? -17.529 -0.759  66.300  1.00 32.63  ? 313  TYR B CZ  1 
ATOM   6232 O  OH  . TYR B 1 313 ? -18.475 -1.648  66.789  1.00 32.47  ? 313  TYR B OH  1 
ATOM   6233 N  N   . VAL B 1 314 ? -12.353 0.524   62.966  1.00 30.62  ? 314  VAL B N   1 
ATOM   6234 C  CA  . VAL B 1 314 ? -11.882 -0.614  62.184  1.00 30.91  ? 314  VAL B CA  1 
ATOM   6235 C  C   . VAL B 1 314 ? -10.777 -1.327  62.942  1.00 33.07  ? 314  VAL B C   1 
ATOM   6236 O  O   . VAL B 1 314 ? -10.762 -2.558  63.040  1.00 29.62  ? 314  VAL B O   1 
ATOM   6237 C  CB  . VAL B 1 314 ? -11.427 -0.159  60.783  1.00 32.58  ? 314  VAL B CB  1 
ATOM   6238 C  CG1 . VAL B 1 314 ? -10.802 -1.317  60.012  1.00 30.80  ? 314  VAL B CG1 1 
ATOM   6239 C  CG2 . VAL B 1 314 ? -12.615 0.454   59.995  1.00 30.23  ? 314  VAL B CG2 1 
ATOM   6240 N  N   . GLY B 1 315 ? -9.861  -0.560  63.539  1.00 32.75  ? 315  GLY B N   1 
ATOM   6241 C  CA  . GLY B 1 315 ? -8.822  -1.166  64.360  1.00 35.39  ? 315  GLY B CA  1 
ATOM   6242 C  C   . GLY B 1 315 ? -9.380  -1.927  65.548  1.00 32.62  ? 315  GLY B C   1 
ATOM   6243 O  O   . GLY B 1 315 ? -8.858  -2.981  65.923  1.00 33.43  ? 315  GLY B O   1 
ATOM   6244 N  N   . MET B 1 316 ? -10.447 -1.404  66.162  1.00 31.25  ? 316  MET B N   1 
ATOM   6245 C  CA  . MET B 1 316 ? -11.066 -2.118  67.276  1.00 32.29  ? 316  MET B CA  1 
ATOM   6246 C  C   . MET B 1 316 ? -11.712 -3.426  66.812  1.00 29.09  ? 316  MET B C   1 
ATOM   6247 O  O   . MET B 1 316 ? -11.669 -4.439  67.518  1.00 31.19  ? 316  MET B O   1 
ATOM   6248 C  CB  . MET B 1 316 ? -12.114 -1.238  67.962  1.00 32.06  ? 316  MET B CB  1 
ATOM   6249 C  CG  . MET B 1 316 ? -11.563 -0.110  68.862  1.00 33.60  ? 316  MET B CG  1 
ATOM   6250 S  SD  . MET B 1 316 ? -12.634 1.360   68.916  1.00 40.56  ? 316  MET B SD  1 
ATOM   6251 C  CE  . MET B 1 316 ? -13.962 0.675   69.879  1.00 40.95  ? 316  MET B CE  1 
ATOM   6252 N  N   . VAL B 1 317 ? -12.331 -3.417  65.632  1.00 29.42  ? 317  VAL B N   1 
ATOM   6253 C  CA  . VAL B 1 317 ? -12.876 -4.646  65.058  1.00 29.82  ? 317  VAL B CA  1 
ATOM   6254 C  C   . VAL B 1 317 ? -11.785 -5.702  64.935  1.00 30.78  ? 317  VAL B C   1 
ATOM   6255 O  O   . VAL B 1 317 ? -11.976 -6.867  65.294  1.00 29.96  ? 317  VAL B O   1 
ATOM   6256 C  CB  . VAL B 1 317 ? -13.506 -4.348  63.683  1.00 29.16  ? 317  VAL B CB  1 
ATOM   6257 C  CG1 . VAL B 1 317 ? -13.764 -5.652  62.912  1.00 28.69  ? 317  VAL B CG1 1 
ATOM   6258 C  CG2 . VAL B 1 317 ? -14.804 -3.520  63.836  1.00 30.62  ? 317  VAL B CG2 1 
ATOM   6259 N  N   . LEU B 1 318 ? -10.629 -5.308  64.387  1.00 30.90  ? 318  LEU B N   1 
ATOM   6260 C  CA  . LEU B 1 318 ? -9.534  -6.258  64.210  1.00 32.28  ? 318  LEU B CA  1 
ATOM   6261 C  C   . LEU B 1 318 ? -9.021  -6.793  65.548  1.00 30.75  ? 318  LEU B C   1 
ATOM   6262 O  O   . LEU B 1 318 ? -8.791  -8.001  65.697  1.00 31.31  ? 318  LEU B O   1 
ATOM   6263 C  CB  . LEU B 1 318 ? -8.413  -5.587  63.416  1.00 31.77  ? 318  LEU B CB  1 
ATOM   6264 C  CG  . LEU B 1 318 ? -8.841  -5.317  61.964  1.00 32.74  ? 318  LEU B CG  1 
ATOM   6265 C  CD1 . LEU B 1 318 ? -7.844  -4.364  61.285  1.00 33.58  ? 318  LEU B CD1 1 
ATOM   6266 C  CD2 . LEU B 1 318 ? -8.936  -6.601  61.149  1.00 32.99  ? 318  LEU B CD2 1 
ATOM   6267 N  N   . ASN B 1 319 ? -8.873  -5.926  66.544  1.00 29.03  ? 319  ASN B N   1 
ATOM   6268 C  CA  . ASN B 1 319 ? -8.427  -6.412  67.844  1.00 30.33  ? 319  ASN B CA  1 
ATOM   6269 C  C   . ASN B 1 319 ? -9.456  -7.346  68.471  1.00 29.53  ? 319  ASN B C   1 
ATOM   6270 O  O   . ASN B 1 319 ? -9.090  -8.349  69.092  1.00 29.93  ? 319  ASN B O   1 
ATOM   6271 C  CB  . ASN B 1 319 ? -8.096  -5.236  68.765  1.00 32.58  ? 319  ASN B CB  1 
ATOM   6272 C  CG  . ASN B 1 319 ? -6.710  -4.682  68.486  1.00 37.99  ? 319  ASN B CG  1 
ATOM   6273 O  OD1 . ASN B 1 319 ? -5.807  -5.436  68.144  1.00 36.47  ? 319  ASN B OD1 1 
ATOM   6274 N  ND2 . ASN B 1 319 ? -6.551  -3.372  68.590  1.00 42.44  ? 319  ASN B ND2 1 
ATOM   6275 N  N   . GLU B 1 320 ? -10.753 -7.068  68.282  1.00 30.01  ? 320  GLU B N   1 
ATOM   6276 C  CA  . GLU B 1 320 ? -11.765 -7.967  68.834  1.00 31.80  ? 320  GLU B CA  1 
ATOM   6277 C  C   . GLU B 1 320 ? -11.764 -9.309  68.106  1.00 29.10  ? 320  GLU B C   1 
ATOM   6278 O  O   . GLU B 1 320 ? -11.999 -10.360 68.725  1.00 30.10  ? 320  GLU B O   1 
ATOM   6279 C  CB  . GLU B 1 320 ? -13.151 -7.299  68.777  1.00 30.47  ? 320  GLU B CB  1 
ATOM   6280 C  CG  . GLU B 1 320 ? -14.313 -8.131  69.320  1.00 31.54  ? 320  GLU B CG  1 
ATOM   6281 C  CD  . GLU B 1 320 ? -14.302 -8.284  70.850  1.00 33.25  ? 320  GLU B CD  1 
ATOM   6282 O  OE1 . GLU B 1 320 ? -13.241 -8.098  71.483  1.00 31.80  ? 320  GLU B OE1 1 
ATOM   6283 O  OE2 . GLU B 1 320 ? -15.370 -8.597  71.424  1.00 33.43  ? 320  GLU B OE2 1 
ATOM   6284 N  N   . ALA B 1 321 ? -11.493 -9.302  66.799  1.00 31.17  ? 321  ALA B N   1 
ATOM   6285 C  CA  . ALA B 1 321 ? -11.329 -10.564 66.077  1.00 30.30  ? 321  ALA B CA  1 
ATOM   6286 C  C   . ALA B 1 321 ? -10.068 -11.291 66.534  1.00 29.76  ? 321  ALA B C   1 
ATOM   6287 O  O   . ALA B 1 321 ? -10.068 -12.521 66.673  1.00 30.50  ? 321  ALA B O   1 
ATOM   6288 C  CB  . ALA B 1 321 ? -11.305 -10.318 64.560  1.00 29.65  ? 321  ALA B CB  1 
ATOM   6289 N  N   . LEU B 1 322 ? -9.000  -10.548 66.820  1.00 30.54  ? 322  LEU B N   1 
ATOM   6290 C  CA  . LEU B 1 322 ? -7.819  -11.169 67.415  1.00 30.98  ? 322  LEU B CA  1 
ATOM   6291 C  C   . LEU B 1 322 ? -8.091  -11.666 68.836  1.00 31.79  ? 322  LEU B C   1 
ATOM   6292 O  O   . LEU B 1 322 ? -7.463  -12.630 69.279  1.00 31.63  ? 322  LEU B O   1 
ATOM   6293 C  CB  . LEU B 1 322 ? -6.656  -10.182 67.437  1.00 32.99  ? 322  LEU B CB  1 
ATOM   6294 C  CG  . LEU B 1 322 ? -6.014  -9.932  66.070  1.00 30.44  ? 322  LEU B CG  1 
ATOM   6295 C  CD1 . LEU B 1 322 ? -4.887  -8.919  66.262  1.00 34.66  ? 322  LEU B CD1 1 
ATOM   6296 C  CD2 . LEU B 1 322 ? -5.478  -11.239 65.469  1.00 29.58  ? 322  LEU B CD2 1 
ATOM   6297 N  N   . ARG B 1 323 ? -9.000  -11.020 69.577  1.00 29.80  ? 323  ARG B N   1 
ATOM   6298 C  CA  . ARG B 1 323 ? -9.335  -11.540 70.899  1.00 29.49  ? 323  ARG B CA  1 
ATOM   6299 C  C   . ARG B 1 323 ? -9.960  -12.922 70.779  1.00 31.72  ? 323  ARG B C   1 
ATOM   6300 O  O   . ARG B 1 323 ? -9.519  -13.877 71.424  1.00 31.53  ? 323  ARG B O   1 
ATOM   6301 C  CB  . ARG B 1 323 ? -10.280 -10.575 71.645  1.00 31.17  ? 323  ARG B CB  1 
ATOM   6302 C  CG  . ARG B 1 323 ? -10.466 -10.959 73.145  1.00 30.47  ? 323  ARG B CG  1 
ATOM   6303 C  CD  . ARG B 1 323 ? -11.467 -10.051 73.878  1.00 31.91  ? 323  ARG B CD  1 
ATOM   6304 N  NE  . ARG B 1 323 ? -12.810 -10.147 73.301  1.00 30.22  ? 323  ARG B NE  1 
ATOM   6305 C  CZ  . ARG B 1 323 ? -13.670 -11.135 73.532  1.00 32.06  ? 323  ARG B CZ  1 
ATOM   6306 N  NH1 . ARG B 1 323 ? -13.381 -12.135 74.348  1.00 32.41  ? 323  ARG B NH1 1 
ATOM   6307 N  NH2 . ARG B 1 323 ? -14.853 -11.120 72.922  1.00 31.34  ? 323  ARG B NH2 1 
ATOM   6308 N  N   . LEU B 1 324 ? -11.000 -13.051 69.954  1.00 32.75  ? 324  LEU B N   1 
ATOM   6309 C  CA  . LEU B 1 324 ? -11.736 -14.309 69.928  1.00 30.32  ? 324  LEU B CA  1 
ATOM   6310 C  C   . LEU B 1 324 ? -10.960 -15.410 69.214  1.00 31.51  ? 324  LEU B C   1 
ATOM   6311 O  O   . LEU B 1 324 ? -10.971 -16.563 69.656  1.00 32.47  ? 324  LEU B O   1 
ATOM   6312 C  CB  . LEU B 1 324 ? -13.107 -14.096 69.286  1.00 31.01  ? 324  LEU B CB  1 
ATOM   6313 C  CG  . LEU B 1 324 ? -14.091 -13.473 70.285  1.00 30.30  ? 324  LEU B CG  1 
ATOM   6314 C  CD1 . LEU B 1 324 ? -15.334 -12.945 69.545  1.00 37.12  ? 324  LEU B CD1 1 
ATOM   6315 C  CD2 . LEU B 1 324 ? -14.509 -14.472 71.392  1.00 33.22  ? 324  LEU B CD2 1 
ATOM   6316 N  N   . TRP B 1 325 ? -10.280 -15.097 68.118  1.00 30.90  ? 325  TRP B N   1 
ATOM   6317 C  CA  . TRP B 1 325 ? -9.601  -16.125 67.322  1.00 28.28  ? 325  TRP B CA  1 
ATOM   6318 C  C   . TRP B 1 325 ? -8.212  -15.653 66.931  1.00 29.97  ? 325  TRP B C   1 
ATOM   6319 O  O   . TRP B 1 325 ? -7.921  -15.426 65.754  1.00 32.30  ? 325  TRP B O   1 
ATOM   6320 C  CB  . TRP B 1 325 ? -10.438 -16.502 66.094  1.00 30.41  ? 325  TRP B CB  1 
ATOM   6321 C  CG  . TRP B 1 325 ? -11.628 -17.277 66.562  1.00 31.33  ? 325  TRP B CG  1 
ATOM   6322 C  CD1 . TRP B 1 325 ? -12.934 -16.884 66.530  1.00 31.86  ? 325  TRP B CD1 1 
ATOM   6323 C  CD2 . TRP B 1 325 ? -11.604 -18.561 67.204  1.00 31.22  ? 325  TRP B CD2 1 
ATOM   6324 N  NE1 . TRP B 1 325 ? -13.729 -17.859 67.103  1.00 31.36  ? 325  TRP B NE1 1 
ATOM   6325 C  CE2 . TRP B 1 325 ? -12.934 -18.896 67.521  1.00 35.01  ? 325  TRP B CE2 1 
ATOM   6326 C  CE3 . TRP B 1 325 ? -10.584 -19.459 67.540  1.00 30.54  ? 325  TRP B CE3 1 
ATOM   6327 C  CZ2 . TRP B 1 325 ? -13.269 -20.096 68.148  1.00 36.18  ? 325  TRP B CZ2 1 
ATOM   6328 C  CZ3 . TRP B 1 325 ? -10.913 -20.646 68.165  1.00 34.70  ? 325  TRP B CZ3 1 
ATOM   6329 C  CH2 . TRP B 1 325 ? -12.248 -20.962 68.457  1.00 35.17  ? 325  TRP B CH2 1 
ATOM   6330 N  N   . PRO B 1 326 ? -7.305  -15.558 67.898  1.00 30.58  ? 326  PRO B N   1 
ATOM   6331 C  CA  . PRO B 1 326 ? -5.918  -15.199 67.559  1.00 29.36  ? 326  PRO B CA  1 
ATOM   6332 C  C   . PRO B 1 326 ? -5.335  -16.259 66.632  1.00 30.01  ? 326  PRO B C   1 
ATOM   6333 O  O   . PRO B 1 326 ? -5.388  -17.453 66.929  1.00 29.81  ? 326  PRO B O   1 
ATOM   6334 C  CB  . PRO B 1 326 ? -5.216  -15.180 68.921  1.00 29.51  ? 326  PRO B CB  1 
ATOM   6335 C  CG  . PRO B 1 326 ? -6.057  -16.113 69.803  1.00 31.80  ? 326  PRO B CG  1 
ATOM   6336 C  CD  . PRO B 1 326 ? -7.474  -15.907 69.323  1.00 32.37  ? 326  PRO B CD  1 
ATOM   6337 N  N   . THR B 1 327 ? -4.793  -15.822 65.491  1.00 29.39  ? 327  THR B N   1 
ATOM   6338 C  CA  . THR B 1 327 ? -4.566  -16.746 64.387  1.00 31.31  ? 327  THR B CA  1 
ATOM   6339 C  C   . THR B 1 327 ? -3.255  -17.511 64.489  1.00 30.48  ? 327  THR B C   1 
ATOM   6340 O  O   . THR B 1 327 ? -3.086  -18.501 63.769  1.00 30.09  ? 327  THR B O   1 
ATOM   6341 C  CB  . THR B 1 327 ? -4.649  -16.016 63.045  1.00 30.81  ? 327  THR B CB  1 
ATOM   6342 O  OG1 . THR B 1 327 ? -3.862  -14.819 63.090  1.00 31.51  ? 327  THR B OG1 1 
ATOM   6343 C  CG2 . THR B 1 327 ? -6.111  -15.638 62.741  1.00 29.57  ? 327  THR B CG2 1 
ATOM   6344 N  N   . ALA B 1 328 ? -2.339  -17.092 65.368  1.00 29.30  ? 328  ALA B N   1 
ATOM   6345 C  CA  . ALA B 1 328 ? -1.253  -17.956 65.833  1.00 30.74  ? 328  ALA B CA  1 
ATOM   6346 C  C   . ALA B 1 328 ? -1.580  -18.291 67.285  1.00 29.78  ? 328  ALA B C   1 
ATOM   6347 O  O   . ALA B 1 328 ? -1.207  -17.548 68.204  1.00 32.03  ? 328  ALA B O   1 
ATOM   6348 C  CB  . ALA B 1 328 ? 0.117   -17.276 65.703  1.00 31.24  ? 328  ALA B CB  1 
ATOM   6349 N  N   . PRO B 1 329 ? -2.316  -19.377 67.542  1.00 30.87  ? 329  PRO B N   1 
ATOM   6350 C  CA  . PRO B 1 329 ? -3.140  -19.451 68.761  1.00 33.25  ? 329  PRO B CA  1 
ATOM   6351 C  C   . PRO B 1 329 ? -2.422  -19.925 70.014  1.00 31.58  ? 329  PRO B C   1 
ATOM   6352 O  O   . PRO B 1 329 ? -3.057  -20.062 71.072  1.00 31.68  ? 329  PRO B O   1 
ATOM   6353 C  CB  . PRO B 1 329 ? -4.243  -20.440 68.360  1.00 34.79  ? 329  PRO B CB  1 
ATOM   6354 C  CG  . PRO B 1 329 ? -3.597  -21.338 67.354  1.00 33.23  ? 329  PRO B CG  1 
ATOM   6355 C  CD  . PRO B 1 329 ? -2.643  -20.438 66.568  1.00 31.38  ? 329  PRO B CD  1 
ATOM   6356 N  N   . ALA B 1 330 ? -1.116  -20.137 69.966  1.00 29.94  ? 330  ALA B N   1 
ATOM   6357 C  CA  . ALA B 1 330 ? -0.426  -20.514 71.192  1.00 29.83  ? 330  ALA B CA  1 
ATOM   6358 C  C   . ALA B 1 330 ? 1.032   -20.146 71.032  1.00 31.03  ? 330  ALA B C   1 
ATOM   6359 O  O   . ALA B 1 330 ? 1.534   -19.994 69.912  1.00 31.31  ? 330  ALA B O   1 
ATOM   6360 C  CB  . ALA B 1 330 ? -0.566  -22.013 71.487  1.00 30.40  ? 330  ALA B CB  1 
ATOM   6361 N  N   . PHE B 1 331 ? 1.697   -19.990 72.167  1.00 30.98  ? 331  PHE B N   1 
ATOM   6362 C  CA  . PHE B 1 331 ? 3.151   -19.933 72.196  1.00 31.10  ? 331  PHE B CA  1 
ATOM   6363 C  C   . PHE B 1 331 ? 3.612   -20.685 73.429  1.00 33.32  ? 331  PHE B C   1 
ATOM   6364 O  O   . PHE B 1 331 ? 2.837   -20.944 74.357  1.00 33.23  ? 331  PHE B O   1 
ATOM   6365 C  CB  . PHE B 1 331 ? 3.709   -18.490 72.152  1.00 30.79  ? 331  PHE B CB  1 
ATOM   6366 C  CG  . PHE B 1 331 ? 3.199   -17.547 73.239  1.00 31.71  ? 331  PHE B CG  1 
ATOM   6367 C  CD1 . PHE B 1 331 ? 2.019   -16.827 73.066  1.00 30.11  ? 331  PHE B CD1 1 
ATOM   6368 C  CD2 . PHE B 1 331 ? 3.956   -17.305 74.375  1.00 32.00  ? 331  PHE B CD2 1 
ATOM   6369 C  CE1 . PHE B 1 331 ? 1.568   -15.929 74.041  1.00 32.49  ? 331  PHE B CE1 1 
ATOM   6370 C  CE2 . PHE B 1 331 ? 3.515   -16.416 75.361  1.00 34.87  ? 331  PHE B CE2 1 
ATOM   6371 C  CZ  . PHE B 1 331 ? 2.316   -15.725 75.192  1.00 33.24  ? 331  PHE B CZ  1 
ATOM   6372 N  N   . SER B 1 332 ? 4.893   -21.040 73.424  1.00 33.63  ? 332  SER B N   1 
ATOM   6373 C  CA  . SER B 1 332 ? 5.472   -21.945 74.399  1.00 32.06  ? 332  SER B CA  1 
ATOM   6374 C  C   . SER B 1 332 ? 6.604   -21.242 75.136  1.00 31.24  ? 332  SER B C   1 
ATOM   6375 O  O   . SER B 1 332 ? 7.317   -20.413 74.558  1.00 31.28  ? 332  SER B O   1 
ATOM   6376 C  CB  . SER B 1 332 ? 5.985   -23.220 73.699  1.00 30.08  ? 332  SER B CB  1 
ATOM   6377 O  OG  . SER B 1 332 ? 6.351   -24.203 74.649  1.00 34.00  ? 332  SER B OG  1 
ATOM   6378 N  N   . LEU B 1 333 ? 6.768   -21.597 76.412  1.00 31.03  ? 333  LEU B N   1 
ATOM   6379 C  CA  . LEU B 1 333 ? 7.796   -21.047 77.286  1.00 34.30  ? 333  LEU B CA  1 
ATOM   6380 C  C   . LEU B 1 333 ? 8.479   -22.175 78.048  1.00 32.94  ? 333  LEU B C   1 
ATOM   6381 O  O   . LEU B 1 333 ? 7.920   -23.265 78.223  1.00 35.32  ? 333  LEU B O   1 
ATOM   6382 C  CB  . LEU B 1 333 ? 7.187   -20.046 78.283  1.00 35.22  ? 333  LEU B CB  1 
ATOM   6383 C  CG  . LEU B 1 333 ? 6.398   -18.937 77.577  1.00 35.74  ? 333  LEU B CG  1 
ATOM   6384 C  CD1 . LEU B 1 333 ? 5.319   -18.346 78.469  1.00 40.22  ? 333  LEU B CD1 1 
ATOM   6385 C  CD2 . LEU B 1 333 ? 7.346   -17.878 77.039  1.00 31.49  ? 333  LEU B CD2 1 
ATOM   6386 N  N   . TYR B 1 334 ? 9.707   -21.915 78.510  1.00 33.27  ? 334  TYR B N   1 
ATOM   6387 C  CA  . TYR B 1 334 ? 10.365  -22.826 79.439  1.00 34.81  ? 334  TYR B CA  1 
ATOM   6388 C  C   . TYR B 1 334 ? 10.888  -22.028 80.627  1.00 33.20  ? 334  TYR B C   1 
ATOM   6389 O  O   . TYR B 1 334 ? 11.236  -20.854 80.502  1.00 31.64  ? 334  TYR B O   1 
ATOM   6390 C  CB  . TYR B 1 334 ? 11.518  -23.628 78.788  1.00 36.41  ? 334  TYR B CB  1 
ATOM   6391 C  CG  . TYR B 1 334 ? 12.713  -22.787 78.436  1.00 35.23  ? 334  TYR B CG  1 
ATOM   6392 C  CD1 . TYR B 1 334 ? 12.801  -22.168 77.194  1.00 33.78  ? 334  TYR B CD1 1 
ATOM   6393 C  CD2 . TYR B 1 334 ? 13.758  -22.596 79.348  1.00 36.62  ? 334  TYR B CD2 1 
ATOM   6394 C  CE1 . TYR B 1 334 ? 13.892  -21.377 76.855  1.00 34.37  ? 334  TYR B CE1 1 
ATOM   6395 C  CE2 . TYR B 1 334 ? 14.849  -21.805 79.020  1.00 36.58  ? 334  TYR B CE2 1 
ATOM   6396 C  CZ  . TYR B 1 334 ? 14.907  -21.197 77.769  1.00 37.46  ? 334  TYR B CZ  1 
ATOM   6397 O  OH  . TYR B 1 334 ? 15.985  -20.406 77.418  1.00 37.27  ? 334  TYR B OH  1 
ATOM   6398 N  N   . ALA B 1 335 ? 10.914  -22.669 81.788  1.00 32.84  ? 335  ALA B N   1 
ATOM   6399 C  CA  . ALA B 1 335 ? 11.374  -22.006 83.007  1.00 33.56  ? 335  ALA B CA  1 
ATOM   6400 C  C   . ALA B 1 335 ? 12.895  -21.879 83.000  1.00 34.83  ? 335  ALA B C   1 
ATOM   6401 O  O   . ALA B 1 335 ? 13.605  -22.879 82.857  1.00 36.48  ? 335  ALA B O   1 
ATOM   6402 C  CB  . ALA B 1 335 ? 10.909  -22.790 84.228  1.00 36.34  ? 335  ALA B CB  1 
ATOM   6403 N  N   . LYS B 1 336 ? 13.389  -20.651 83.170  1.00 35.80  ? 336  LYS B N   1 
ATOM   6404 C  CA  . LYS B 1 336 ? 14.834  -20.416 83.179  1.00 36.55  ? 336  LYS B CA  1 
ATOM   6405 C  C   . LYS B 1 336 ? 15.502  -21.002 84.421  1.00 41.77  ? 336  LYS B C   1 
ATOM   6406 O  O   . LYS B 1 336 ? 16.670  -21.424 84.369  1.00 39.59  ? 336  LYS B O   1 
ATOM   6407 C  CB  . LYS B 1 336 ? 15.111  -18.914 83.092  1.00 35.87  ? 336  LYS B CB  1 
ATOM   6408 C  CG  . LYS B 1 336 ? 14.773  -18.298 81.723  1.00 39.10  ? 336  LYS B CG  1 
ATOM   6409 C  CD  . LYS B 1 336 ? 14.631  -16.784 81.803  1.00 37.97  ? 336  LYS B CD  1 
ATOM   6410 C  CE  . LYS B 1 336 ? 15.949  -16.084 82.185  1.00 39.89  ? 336  LYS B CE  1 
ATOM   6411 N  NZ  . LYS B 1 336 ? 16.988  -16.191 81.107  1.00 44.30  ? 336  LYS B NZ  1 
ATOM   6412 N  N   . GLU B 1 337 ? 14.788  -21.015 85.536  1.00 37.36  ? 337  GLU B N   1 
ATOM   6413 C  CA  . GLU B 1 337 ? 15.267  -21.584 86.787  1.00 41.95  ? 337  GLU B CA  1 
ATOM   6414 C  C   . GLU B 1 337 ? 14.075  -22.211 87.489  1.00 42.73  ? 337  GLU B C   1 
ATOM   6415 O  O   . GLU B 1 337 ? 12.926  -21.961 87.126  1.00 38.89  ? 337  GLU B O   1 
ATOM   6416 C  CB  . GLU B 1 337 ? 15.915  -20.521 87.682  1.00 41.80  ? 337  GLU B CB  1 
ATOM   6417 C  CG  . GLU B 1 337 ? 17.146  -19.805 87.091  1.00 42.41  ? 337  GLU B CG  1 
ATOM   6418 C  CD  . GLU B 1 337 ? 18.353  -20.714 86.825  1.00 45.60  ? 337  GLU B CD  1 
ATOM   6419 O  OE1 . GLU B 1 337 ? 18.430  -21.835 87.372  1.00 44.40  ? 337  GLU B OE1 1 
ATOM   6420 O  OE2 . GLU B 1 337 ? 19.244  -20.292 86.057  1.00 48.79  ? 337  GLU B OE2 1 
ATOM   6421 N  N   . ASP B 1 338 ? 14.350  -23.029 88.506  1.00 39.78  ? 338  ASP B N   1 
ATOM   6422 C  CA  . ASP B 1 338 ? 13.282  -23.448 89.407  1.00 42.47  ? 338  ASP B CA  1 
ATOM   6423 C  C   . ASP B 1 338 ? 12.486  -22.228 89.844  1.00 40.48  ? 338  ASP B C   1 
ATOM   6424 O  O   . ASP B 1 338 ? 13.056  -21.178 90.158  1.00 42.64  ? 338  ASP B O   1 
ATOM   6425 C  CB  . ASP B 1 338 ? 13.848  -24.144 90.645  1.00 40.46  ? 338  ASP B CB  1 
ATOM   6426 C  CG  . ASP B 1 338 ? 14.557  -25.445 90.335  1.00 41.61  ? 338  ASP B CG  1 
ATOM   6427 O  OD1 . ASP B 1 338 ? 14.489  -25.960 89.204  1.00 42.44  ? 338  ASP B OD1 1 
ATOM   6428 O  OD2 . ASP B 1 338 ? 15.211  -25.964 91.263  1.00 51.05  ? 338  ASP B OD2 1 
ATOM   6429 N  N   . THR B 1 339 ? 11.161  -22.368 89.877  1.00 40.71  ? 339  THR B N   1 
ATOM   6430 C  CA  . THR B 1 339 ? 10.291  -21.262 90.254  1.00 39.78  ? 339  THR B CA  1 
ATOM   6431 C  C   . THR B 1 339 ? 8.909   -21.835 90.552  1.00 40.30  ? 339  THR B C   1 
ATOM   6432 O  O   . THR B 1 339 ? 8.582   -22.944 90.125  1.00 43.48  ? 339  THR B O   1 
ATOM   6433 C  CB  . THR B 1 339 ? 10.222  -20.204 89.143  1.00 39.16  ? 339  THR B CB  1 
ATOM   6434 O  OG1 . THR B 1 339 ? 9.693   -18.980 89.663  1.00 43.01  ? 339  THR B OG1 1 
ATOM   6435 C  CG2 . THR B 1 339 ? 9.349   -20.692 87.967  1.00 38.59  ? 339  THR B CG2 1 
ATOM   6436 N  N   . VAL B 1 340 ? 8.098   -21.073 91.283  1.00 38.66  ? 340  VAL B N   1 
ATOM   6437 C  CA  . VAL B 1 340 ? 6.745   -21.506 91.633  1.00 40.04  ? 340  VAL B CA  1 
ATOM   6438 C  C   . VAL B 1 340 ? 5.742   -20.646 90.880  1.00 37.53  ? 340  VAL B C   1 
ATOM   6439 O  O   . VAL B 1 340 ? 5.715   -19.418 91.042  1.00 41.63  ? 340  VAL B O   1 
ATOM   6440 C  CB  . VAL B 1 340 ? 6.488   -21.442 93.145  1.00 44.05  ? 340  VAL B CB  1 
ATOM   6441 C  CG1 . VAL B 1 340 ? 5.050   -21.879 93.436  1.00 39.82  ? 340  VAL B CG1 1 
ATOM   6442 C  CG2 . VAL B 1 340 ? 7.477   -22.335 93.870  1.00 40.50  ? 340  VAL B CG2 1 
ATOM   6443 N  N   . LEU B 1 341 ? 4.886   -21.298 90.096  1.00 40.60  ? 341  LEU B N   1 
ATOM   6444 C  CA  . LEU B 1 341 ? 3.884   -20.613 89.292  1.00 40.78  ? 341  LEU B CA  1 
ATOM   6445 C  C   . LEU B 1 341 ? 2.629   -20.363 90.124  1.00 39.21  ? 341  LEU B C   1 
ATOM   6446 O  O   . LEU B 1 341 ? 2.026   -21.306 90.652  1.00 40.22  ? 341  LEU B O   1 
ATOM   6447 C  CB  . LEU B 1 341 ? 3.550   -21.441 88.051  1.00 36.78  ? 341  LEU B CB  1 
ATOM   6448 C  CG  . LEU B 1 341 ? 2.717   -20.738 86.992  1.00 40.33  ? 341  LEU B CG  1 
ATOM   6449 C  CD1 . LEU B 1 341 ? 3.530   -19.592 86.375  1.00 38.92  ? 341  LEU B CD1 1 
ATOM   6450 C  CD2 . LEU B 1 341 ? 2.311   -21.757 85.942  1.00 39.69  ? 341  LEU B CD2 1 
ATOM   6451 N  N   . GLY B 1 342 ? 2.248   -19.096 90.245  1.00 38.51  ? 342  GLY B N   1 
ATOM   6452 C  CA  . GLY B 1 342 ? 1.005   -18.731 90.910  1.00 44.15  ? 342  GLY B CA  1 
ATOM   6453 C  C   . GLY B 1 342 ? 0.925   -19.121 92.370  1.00 46.86  ? 342  GLY B C   1 
ATOM   6454 O  O   . GLY B 1 342 ? -0.176  -19.356 92.882  1.00 42.07  ? 342  GLY B O   1 
ATOM   6455 N  N   . GLY B 1 343 ? 2.061   -19.201 93.059  1.00 43.68  ? 343  GLY B N   1 
ATOM   6456 C  CA  . GLY B 1 343 ? 2.060   -19.641 94.442  1.00 45.45  ? 343  GLY B CA  1 
ATOM   6457 C  C   . GLY B 1 343 ? 1.603   -21.063 94.668  1.00 46.04  ? 343  GLY B C   1 
ATOM   6458 O  O   . GLY B 1 343 ? 1.456   -21.472 95.825  1.00 48.40  ? 343  GLY B O   1 
ATOM   6459 N  N   . GLU B 1 344 ? 1.387   -21.844 93.611  1.00 44.73  ? 344  GLU B N   1 
ATOM   6460 C  CA  . GLU B 1 344 ? 0.761   -23.155 93.769  1.00 42.84  ? 344  GLU B CA  1 
ATOM   6461 C  C   . GLU B 1 344 ? 1.417   -24.285 92.987  1.00 45.67  ? 344  GLU B C   1 
ATOM   6462 O  O   . GLU B 1 344 ? 1.256   -25.442 93.386  1.00 44.33  ? 344  GLU B O   1 
ATOM   6463 C  CB  . GLU B 1 344 ? -0.722  -23.076 93.374  1.00 46.91  ? 344  GLU B CB  1 
ATOM   6464 C  CG  . GLU B 1 344 ? -1.535  -22.175 94.290  1.00 52.28  ? 344  GLU B CG  1 
ATOM   6465 C  CD  . GLU B 1 344 ? -2.927  -21.866 93.766  1.00 55.13  ? 344  GLU B CD  1 
ATOM   6466 O  OE1 . GLU B 1 344 ? -3.193  -22.091 92.567  1.00 51.91  ? 344  GLU B OE1 1 
ATOM   6467 O  OE2 . GLU B 1 344 ? -3.762  -21.397 94.566  1.00 61.45  ? 344  GLU B OE2 1 
ATOM   6468 N  N   . TYR B 1 345 ? 2.123   -24.014 91.889  1.00 40.53  ? 345  TYR B N   1 
ATOM   6469 C  CA  . TYR B 1 345 ? 2.620   -25.062 90.998  1.00 41.25  ? 345  TYR B CA  1 
ATOM   6470 C  C   . TYR B 1 345 ? 4.131   -24.966 90.861  1.00 43.75  ? 345  TYR B C   1 
ATOM   6471 O  O   . TYR B 1 345 ? 4.637   -24.152 90.068  1.00 40.38  ? 345  TYR B O   1 
ATOM   6472 C  CB  . TYR B 1 345 ? 1.945   -24.960 89.632  1.00 41.17  ? 345  TYR B CB  1 
ATOM   6473 C  CG  . TYR B 1 345 ? 0.439   -25.017 89.746  1.00 38.09  ? 345  TYR B CG  1 
ATOM   6474 C  CD1 . TYR B 1 345 ? -0.209  -26.222 89.971  1.00 42.44  ? 345  TYR B CD1 1 
ATOM   6475 C  CD2 . TYR B 1 345 ? -0.325  -23.870 89.654  1.00 36.86  ? 345  TYR B CD2 1 
ATOM   6476 C  CE1 . TYR B 1 345 ? -1.583  -26.283 90.091  1.00 41.28  ? 345  TYR B CE1 1 
ATOM   6477 C  CE2 . TYR B 1 345 ? -1.692  -23.915 89.777  1.00 40.21  ? 345  TYR B CE2 1 
ATOM   6478 C  CZ  . TYR B 1 345 ? -2.318  -25.125 90.002  1.00 43.22  ? 345  TYR B CZ  1 
ATOM   6479 O  OH  . TYR B 1 345 ? -3.687  -25.169 90.123  1.00 47.42  ? 345  TYR B OH  1 
ATOM   6480 N  N   . PRO B 1 346 ? 4.887   -25.770 91.606  1.00 45.57  ? 346  PRO B N   1 
ATOM   6481 C  CA  . PRO B 1 346 ? 6.348   -25.714 91.497  1.00 44.76  ? 346  PRO B CA  1 
ATOM   6482 C  C   . PRO B 1 346 ? 6.801   -26.218 90.140  1.00 43.05  ? 346  PRO B C   1 
ATOM   6483 O  O   . PRO B 1 346 ? 6.306   -27.228 89.632  1.00 41.22  ? 346  PRO B O   1 
ATOM   6484 C  CB  . PRO B 1 346 ? 6.833   -26.636 92.629  1.00 46.76  ? 346  PRO B CB  1 
ATOM   6485 C  CG  . PRO B 1 346 ? 5.621   -26.866 93.504  1.00 48.72  ? 346  PRO B CG  1 
ATOM   6486 C  CD  . PRO B 1 346 ? 4.449   -26.793 92.570  1.00 46.32  ? 346  PRO B CD  1 
ATOM   6487 N  N   . LEU B 1 347 ? 7.749   -25.499 89.552  1.00 39.12  ? 347  LEU B N   1 
ATOM   6488 C  CA  . LEU B 1 347 ? 8.348   -25.876 88.283  1.00 39.37  ? 347  LEU B CA  1 
ATOM   6489 C  C   . LEU B 1 347 ? 9.854   -25.988 88.461  1.00 40.47  ? 347  LEU B C   1 
ATOM   6490 O  O   . LEU B 1 347 ? 10.461  -25.218 89.215  1.00 41.27  ? 347  LEU B O   1 
ATOM   6491 C  CB  . LEU B 1 347 ? 8.033   -24.850 87.174  1.00 40.91  ? 347  LEU B CB  1 
ATOM   6492 C  CG  . LEU B 1 347 ? 6.558   -24.635 86.819  1.00 38.13  ? 347  LEU B CG  1 
ATOM   6493 C  CD1 . LEU B 1 347 ? 6.418   -23.514 85.789  1.00 36.49  ? 347  LEU B CD1 1 
ATOM   6494 C  CD2 . LEU B 1 347 ? 5.916   -25.926 86.310  1.00 39.42  ? 347  LEU B CD2 1 
ATOM   6495 N  N   . GLU B 1 348 ? 10.442  -26.942 87.760  1.00 39.91  ? 348  GLU B N   1 
ATOM   6496 C  CA  . GLU B 1 348 ? 11.885  -27.097 87.699  1.00 41.65  ? 348  GLU B CA  1 
ATOM   6497 C  C   . GLU B 1 348 ? 12.428  -26.419 86.453  1.00 41.20  ? 348  GLU B C   1 
ATOM   6498 O  O   . GLU B 1 348 ? 11.743  -26.306 85.434  1.00 37.59  ? 348  GLU B O   1 
ATOM   6499 C  CB  . GLU B 1 348 ? 12.289  -28.571 87.688  1.00 43.29  ? 348  GLU B CB  1 
ATOM   6500 C  CG  . GLU B 1 348 ? 11.819  -29.356 88.895  1.00 49.28  ? 348  GLU B CG  1 
ATOM   6501 C  CD  . GLU B 1 348 ? 12.161  -30.827 88.770  1.00 57.20  ? 348  GLU B CD  1 
ATOM   6502 O  OE1 . GLU B 1 348 ? 13.218  -31.237 89.293  1.00 66.87  ? 348  GLU B OE1 1 
ATOM   6503 O  OE2 . GLU B 1 348 ? 11.380  -31.568 88.137  1.00 60.93  ? 348  GLU B OE2 1 
ATOM   6504 N  N   . LYS B 1 349 ? 13.677  -25.976 86.548  1.00 39.01  ? 349  LYS B N   1 
ATOM   6505 C  CA  . LYS B 1 349 ? 14.386  -25.426 85.408  1.00 38.20  ? 349  LYS B CA  1 
ATOM   6506 C  C   . LYS B 1 349 ? 14.166  -26.308 84.195  1.00 36.62  ? 349  LYS B C   1 
ATOM   6507 O  O   . LYS B 1 349 ? 14.332  -27.531 84.260  1.00 38.95  ? 349  LYS B O   1 
ATOM   6508 C  CB  . LYS B 1 349 ? 15.880  -25.335 85.729  1.00 42.54  ? 349  LYS B CB  1 
ATOM   6509 C  CG  . LYS B 1 349 ? 16.753  -25.015 84.527  1.00 41.63  ? 349  LYS B CG  1 
ATOM   6510 C  CD  . LYS B 1 349 ? 18.173  -24.683 84.984  1.00 46.57  ? 349  LYS B CD  1 
ATOM   6511 C  CE  . LYS B 1 349 ? 19.036  -24.293 83.808  1.00 48.94  ? 349  LYS B CE  1 
ATOM   6512 N  NZ  . LYS B 1 349 ? 20.423  -23.965 84.245  1.00 55.62  ? 349  LYS B NZ  1 
ATOM   6513 N  N   . GLY B 1 350 ? 13.773  -25.682 83.087  1.00 38.03  ? 350  GLY B N   1 
ATOM   6514 C  CA  . GLY B 1 350 ? 13.533  -26.396 81.858  1.00 35.21  ? 350  GLY B CA  1 
ATOM   6515 C  C   . GLY B 1 350 ? 12.103  -26.849 81.627  1.00 37.77  ? 350  GLY B C   1 
ATOM   6516 O  O   . GLY B 1 350 ? 11.784  -27.250 80.498  1.00 36.82  ? 350  GLY B O   1 
ATOM   6517 N  N   . ASP B 1 351 ? 11.247  -26.819 82.656  1.00 35.66  ? 351  ASP B N   1 
ATOM   6518 C  CA  . ASP B 1 351 ? 9.854   -27.222 82.491  1.00 36.29  ? 351  ASP B CA  1 
ATOM   6519 C  C   . ASP B 1 351 ? 9.157   -26.290 81.508  1.00 36.45  ? 351  ASP B C   1 
ATOM   6520 O  O   . ASP B 1 351 ? 9.371   -25.077 81.526  1.00 35.14  ? 351  ASP B O   1 
ATOM   6521 C  CB  . ASP B 1 351 ? 9.103   -27.177 83.830  1.00 37.24  ? 351  ASP B CB  1 
ATOM   6522 C  CG  . ASP B 1 351 ? 9.387   -28.379 84.734  1.00 35.92  ? 351  ASP B CG  1 
ATOM   6523 O  OD1 . ASP B 1 351 ? 10.057  -29.334 84.300  1.00 35.42  ? 351  ASP B OD1 1 
ATOM   6524 O  OD2 . ASP B 1 351 ? 8.921   -28.348 85.900  1.00 40.35  ? 351  ASP B OD2 1 
ATOM   6525 N  N   . GLU B 1 352 ? 8.261   -26.862 80.710  1.00 35.20  ? 352  GLU B N   1 
ATOM   6526 C  CA  . GLU B 1 352 ? 7.615   -26.221 79.580  1.00 36.97  ? 352  GLU B CA  1 
ATOM   6527 C  C   . GLU B 1 352 ? 6.185   -25.794 79.929  1.00 37.71  ? 352  GLU B C   1 
ATOM   6528 O  O   . GLU B 1 352 ? 5.510   -26.418 80.759  1.00 35.89  ? 352  GLU B O   1 
ATOM   6529 C  CB  . GLU B 1 352 ? 7.611   -27.225 78.435  1.00 38.62  ? 352  GLU B CB  1 
ATOM   6530 C  CG  . GLU B 1 352 ? 8.917   -27.252 77.701  1.00 42.65  ? 352  GLU B CG  1 
ATOM   6531 C  CD  . GLU B 1 352 ? 8.913   -28.235 76.558  1.00 51.66  ? 352  GLU B CD  1 
ATOM   6532 O  OE1 . GLU B 1 352 ? 7.824   -28.543 76.014  1.00 46.00  ? 352  GLU B OE1 1 
ATOM   6533 O  OE2 . GLU B 1 352 ? 10.015  -28.728 76.241  1.00 55.74  ? 352  GLU B OE2 1 
ATOM   6534 N  N   . LEU B 1 353 ? 5.742   -24.703 79.299  1.00 33.25  ? 353  LEU B N   1 
ATOM   6535 C  CA  . LEU B 1 353 ? 4.381   -24.197 79.402  1.00 34.23  ? 353  LEU B CA  1 
ATOM   6536 C  C   . LEU B 1 353 ? 3.858   -23.924 78.002  1.00 34.41  ? 353  LEU B C   1 
ATOM   6537 O  O   . LEU B 1 353 ? 4.620   -23.570 77.097  1.00 34.02  ? 353  LEU B O   1 
ATOM   6538 C  CB  . LEU B 1 353 ? 4.310   -22.892 80.206  1.00 32.41  ? 353  LEU B CB  1 
ATOM   6539 C  CG  . LEU B 1 353 ? 4.873   -22.914 81.627  1.00 31.58  ? 353  LEU B CG  1 
ATOM   6540 C  CD1 . LEU B 1 353 ? 5.059   -21.502 82.104  1.00 34.45  ? 353  LEU B CD1 1 
ATOM   6541 C  CD2 . LEU B 1 353 ? 3.929   -23.697 82.576  1.00 34.96  ? 353  LEU B CD2 1 
ATOM   6542 N  N   . MET B 1 354 ? 2.550   -24.066 77.830  1.00 33.24  ? 354  MET B N   1 
ATOM   6543 C  CA  . MET B 1 354 ? 1.905   -23.662 76.592  1.00 32.25  ? 354  MET B CA  1 
ATOM   6544 C  C   . MET B 1 354 ? 0.877   -22.610 76.959  1.00 29.92  ? 354  MET B C   1 
ATOM   6545 O  O   . MET B 1 354 ? 0.061   -22.836 77.858  1.00 32.14  ? 354  MET B O   1 
ATOM   6546 C  CB  . MET B 1 354 ? 1.193   -24.818 75.903  1.00 32.07  ? 354  MET B CB  1 
ATOM   6547 C  CG  . MET B 1 354 ? 2.094   -25.905 75.395  1.00 33.09  ? 354  MET B CG  1 
ATOM   6548 S  SD  . MET B 1 354 ? 3.147   -25.415 74.015  1.00 36.42  ? 354  MET B SD  1 
ATOM   6549 C  CE  . MET B 1 354 ? 1.923   -24.950 72.794  1.00 32.98  ? 354  MET B CE  1 
ATOM   6550 N  N   . VAL B 1 355 ? 0.912   -21.472 76.283  1.00 33.32  ? 355  VAL B N   1 
ATOM   6551 C  CA  . VAL B 1 355 ? -0.068  -20.419 76.515  1.00 31.47  ? 355  VAL B CA  1 
ATOM   6552 C  C   . VAL B 1 355 ? -1.173  -20.580 75.483  1.00 28.32  ? 355  VAL B C   1 
ATOM   6553 O  O   . VAL B 1 355 ? -0.931  -20.447 74.281  1.00 29.88  ? 355  VAL B O   1 
ATOM   6554 C  CB  . VAL B 1 355 ? 0.569   -19.028 76.415  1.00 33.45  ? 355  VAL B CB  1 
ATOM   6555 C  CG1 . VAL B 1 355 ? -0.507  -17.953 76.495  1.00 33.94  ? 355  VAL B CG1 1 
ATOM   6556 C  CG2 . VAL B 1 355 ? 1.594   -18.843 77.525  1.00 32.87  ? 355  VAL B CG2 1 
ATOM   6557 N  N   . LEU B 1 356 ? -2.391  -20.841 75.952  1.00 30.54  ? 356  LEU B N   1 
ATOM   6558 C  CA  . LEU B 1 356 ? -3.529  -21.058 75.059  1.00 33.69  ? 356  LEU B CA  1 
ATOM   6559 C  C   . LEU B 1 356 ? -4.221  -19.715 74.859  1.00 32.79  ? 356  LEU B C   1 
ATOM   6560 O  O   . LEU B 1 356 ? -5.088  -19.330 75.641  1.00 32.42  ? 356  LEU B O   1 
ATOM   6561 C  CB  . LEU B 1 356 ? -4.464  -22.103 75.656  1.00 34.06  ? 356  LEU B CB  1 
ATOM   6562 C  CG  . LEU B 1 356 ? -5.422  -22.920 74.791  1.00 40.37  ? 356  LEU B CG  1 
ATOM   6563 C  CD1 . LEU B 1 356 ? -4.739  -23.508 73.535  1.00 43.51  ? 356  LEU B CD1 1 
ATOM   6564 C  CD2 . LEU B 1 356 ? -5.974  -24.050 75.664  1.00 39.32  ? 356  LEU B CD2 1 
ATOM   6565 N  N   . ILE B 1 357 ? -3.845  -18.991 73.789  1.00 30.54  ? 357  ILE B N   1 
ATOM   6566 C  CA  . ILE B 1 357 ? -4.255  -17.586 73.672  1.00 30.21  ? 357  ILE B CA  1 
ATOM   6567 C  C   . ILE B 1 357 ? -5.768  -17.454 73.588  1.00 30.78  ? 357  ILE B C   1 
ATOM   6568 O  O   . ILE B 1 357 ? -6.326  -16.543 74.227  1.00 30.87  ? 357  ILE B O   1 
ATOM   6569 C  CB  . ILE B 1 357 ? -3.533  -16.908 72.497  1.00 31.54  ? 357  ILE B CB  1 
ATOM   6570 C  CG1 . ILE B 1 357 ? -2.022  -17.136 72.552  1.00 30.91  ? 357  ILE B CG1 1 
ATOM   6571 C  CG2 . ILE B 1 357 ? -3.796  -15.396 72.534  1.00 31.71  ? 357  ILE B CG2 1 
ATOM   6572 C  CD1 . ILE B 1 357 ? -1.339  -16.580 71.317  1.00 30.27  ? 357  ILE B CD1 1 
ATOM   6573 N  N   . PRO B 1 358 ? -6.492  -18.288 72.834  1.00 32.81  ? 358  PRO B N   1 
ATOM   6574 C  CA  . PRO B 1 358 ? -7.956  -18.131 72.794  1.00 30.46  ? 358  PRO B CA  1 
ATOM   6575 C  C   . PRO B 1 358 ? -8.588  -18.265 74.161  1.00 33.94  ? 358  PRO B C   1 
ATOM   6576 O  O   . PRO B 1 358 ? -9.602  -17.605 74.434  1.00 33.47  ? 358  PRO B O   1 
ATOM   6577 C  CB  . PRO B 1 358 ? -8.410  -19.256 71.850  1.00 33.16  ? 358  PRO B CB  1 
ATOM   6578 C  CG  . PRO B 1 358 ? -7.200  -19.522 70.983  1.00 30.03  ? 358  PRO B CG  1 
ATOM   6579 C  CD  . PRO B 1 358 ? -6.041  -19.376 71.950  1.00 30.71  ? 358  PRO B CD  1 
ATOM   6580 N  N   . GLN B 1 359 ? -8.011  -19.091 75.042  1.00 33.02  ? 359  GLN B N   1 
ATOM   6581 C  CA  . GLN B 1 359 ? -8.590  -19.227 76.377  1.00 36.57  ? 359  GLN B CA  1 
ATOM   6582 C  C   . GLN B 1 359 ? -8.250  -18.030 77.247  1.00 32.81  ? 359  GLN B C   1 
ATOM   6583 O  O   . GLN B 1 359 ? -9.089  -17.561 78.015  1.00 33.41  ? 359  GLN B O   1 
ATOM   6584 C  CB  . GLN B 1 359 ? -8.118  -20.520 77.048  1.00 36.65  ? 359  GLN B CB  1 
ATOM   6585 C  CG  . GLN B 1 359 ? -8.701  -21.777 76.408  1.00 37.75  ? 359  GLN B CG  1 
ATOM   6586 C  CD  . GLN B 1 359 ? -10.230 -21.770 76.371  1.00 37.99  ? 359  GLN B CD  1 
ATOM   6587 O  OE1 . GLN B 1 359 ? -10.827 -21.639 75.315  1.00 39.21  ? 359  GLN B OE1 1 
ATOM   6588 N  NE2 . GLN B 1 359 ? -10.853 -21.909 77.525  1.00 41.70  ? 359  GLN B NE2 1 
ATOM   6589 N  N   . LEU B 1 360 ? -7.015  -17.531 77.154  1.00 31.20  ? 360  LEU B N   1 
ATOM   6590 C  CA  . LEU B 1 360 ? -6.665  -16.290 77.832  1.00 31.22  ? 360  LEU B CA  1 
ATOM   6591 C  C   . LEU B 1 360 ? -7.676  -15.197 77.508  1.00 33.01  ? 360  LEU B C   1 
ATOM   6592 O  O   . LEU B 1 360 ? -8.152  -14.484 78.399  1.00 32.71  ? 360  LEU B O   1 
ATOM   6593 C  CB  . LEU B 1 360 ? -5.249  -15.853 77.415  1.00 28.72  ? 360  LEU B CB  1 
ATOM   6594 C  CG  . LEU B 1 360 ? -4.858  -14.445 77.889  1.00 30.88  ? 360  LEU B CG  1 
ATOM   6595 C  CD1 . LEU B 1 360 ? -4.626  -14.412 79.393  1.00 32.69  ? 360  LEU B CD1 1 
ATOM   6596 C  CD2 . LEU B 1 360 ? -3.601  -13.968 77.171  1.00 30.86  ? 360  LEU B CD2 1 
ATOM   6597 N  N   . HIS B 1 361 ? -8.025  -15.066 76.223  1.00 29.93  ? 361  HIS B N   1 
ATOM   6598 C  CA  . HIS B 1 361 ? -8.892  -14.013 75.720  1.00 31.20  ? 361  HIS B CA  1 
ATOM   6599 C  C   . HIS B 1 361 ? -10.356 -14.228 76.090  1.00 35.19  ? 361  HIS B C   1 
ATOM   6600 O  O   . HIS B 1 361 ? -11.197 -13.368 75.781  1.00 32.65  ? 361  HIS B O   1 
ATOM   6601 C  CB  . HIS B 1 361 ? -8.715  -13.911 74.202  1.00 28.96  ? 361  HIS B CB  1 
ATOM   6602 C  CG  . HIS B 1 361 ? -7.372  -13.364 73.792  1.00 31.30  ? 361  HIS B CG  1 
ATOM   6603 N  ND1 . HIS B 1 361 ? -6.945  -13.355 72.485  1.00 31.77  ? 361  HIS B ND1 1 
ATOM   6604 C  CD2 . HIS B 1 361 ? -6.367  -12.810 74.520  1.00 35.38  ? 361  HIS B CD2 1 
ATOM   6605 C  CE1 . HIS B 1 361 ? -5.738  -12.811 72.417  1.00 30.29  ? 361  HIS B CE1 1 
ATOM   6606 N  NE2 . HIS B 1 361 ? -5.361  -12.478 73.640  1.00 30.62  ? 361  HIS B NE2 1 
ATOM   6607 N  N   . ARG B 1 362 ? -10.661 -15.350 76.746  1.00 33.02  ? 362  ARG B N   1 
ATOM   6608 C  CA  . ARG B 1 362 ? -11.997 -15.652 77.250  1.00 31.99  ? 362  ARG B CA  1 
ATOM   6609 C  C   . ARG B 1 362 ? -12.030 -15.712 78.778  1.00 34.52  ? 362  ARG B C   1 
ATOM   6610 O  O   . ARG B 1 362 ? -12.968 -16.275 79.363  1.00 33.69  ? 362  ARG B O   1 
ATOM   6611 C  CB  . ARG B 1 362 ? -12.488 -16.968 76.648  1.00 32.35  ? 362  ARG B CB  1 
ATOM   6612 C  CG  . ARG B 1 362 ? -12.891 -16.862 75.163  1.00 31.42  ? 362  ARG B CG  1 
ATOM   6613 C  CD  . ARG B 1 362 ? -12.959 -18.263 74.526  1.00 33.31  ? 362  ARG B CD  1 
ATOM   6614 N  NE  . ARG B 1 362 ? -13.483 -18.232 73.164  1.00 33.25  ? 362  ARG B NE  1 
ATOM   6615 C  CZ  . ARG B 1 362 ? -12.794 -17.854 72.094  1.00 34.78  ? 362  ARG B CZ  1 
ATOM   6616 N  NH1 . ARG B 1 362 ? -11.538 -17.449 72.188  1.00 32.06  ? 362  ARG B NH1 1 
ATOM   6617 N  NH2 . ARG B 1 362 ? -13.381 -17.877 70.902  1.00 33.85  ? 362  ARG B NH2 1 
ATOM   6618 N  N   . ASP B 1 363 ? -10.997 -15.190 79.433  1.00 33.16  ? 363  ASP B N   1 
ATOM   6619 C  CA  . ASP B 1 363 ? -10.950 -15.130 80.896  1.00 34.58  ? 363  ASP B CA  1 
ATOM   6620 C  C   . ASP B 1 363 ? -12.011 -14.154 81.396  1.00 33.70  ? 363  ASP B C   1 
ATOM   6621 O  O   . ASP B 1 363 ? -11.879 -12.938 81.234  1.00 33.48  ? 363  ASP B O   1 
ATOM   6622 C  CB  . ASP B 1 363 ? -9.553  -14.711 81.352  1.00 32.83  ? 363  ASP B CB  1 
ATOM   6623 C  CG  . ASP B 1 363 ? -9.355  -14.825 82.861  1.00 35.09  ? 363  ASP B CG  1 
ATOM   6624 O  OD1 . ASP B 1 363 ? -10.355 -14.798 83.605  1.00 35.57  ? 363  ASP B OD1 1 
ATOM   6625 O  OD2 . ASP B 1 363 ? -8.189  -14.911 83.300  1.00 33.90  ? 363  ASP B OD2 1 
ATOM   6626 N  N   . LYS B 1 364 ? -13.071 -14.688 82.000  1.00 33.81  ? 364  LYS B N   1 
ATOM   6627 C  CA  . LYS B 1 364 ? -14.178 -13.844 82.431  1.00 37.26  ? 364  LYS B CA  1 
ATOM   6628 C  C   . LYS B 1 364 ? -13.794 -12.909 83.571  1.00 37.12  ? 364  LYS B C   1 
ATOM   6629 O  O   . LYS B 1 364 ? -14.434 -11.858 83.745  1.00 34.56  ? 364  LYS B O   1 
ATOM   6630 C  CB  . LYS B 1 364 ? -15.359 -14.729 82.836  1.00 37.58  ? 364  LYS B CB  1 
ATOM   6631 C  CG  . LYS B 1 364 ? -15.939 -15.491 81.665  1.00 38.68  ? 364  LYS B CG  1 
ATOM   6632 C  CD  . LYS B 1 364 ? -17.217 -16.209 82.035  1.00 45.77  ? 364  LYS B CD  1 
ATOM   6633 C  CE  . LYS B 1 364 ? -17.865 -16.794 80.778  1.00 53.83  ? 364  LYS B CE  1 
ATOM   6634 N  NZ  . LYS B 1 364 ? -18.988 -17.714 81.098  1.00 58.69  ? 364  LYS B NZ  1 
ATOM   6635 N  N   . THR B 1 365 ? -12.771 -13.253 84.354  1.00 36.20  ? 365  THR B N   1 
ATOM   6636 C  CA  . THR B 1 365 ? -12.352 -12.348 85.418  1.00 34.53  ? 365  THR B CA  1 
ATOM   6637 C  C   . THR B 1 365 ? -11.700 -11.085 84.860  1.00 38.60  ? 365  THR B C   1 
ATOM   6638 O  O   . THR B 1 365 ? -11.611 -10.075 85.569  1.00 37.60  ? 365  THR B O   1 
ATOM   6639 C  CB  . THR B 1 365 ? -11.401 -13.060 86.380  1.00 39.70  ? 365  THR B CB  1 
ATOM   6640 O  OG1 . THR B 1 365 ? -10.148 -13.271 85.722  1.00 38.96  ? 365  THR B OG1 1 
ATOM   6641 C  CG2 . THR B 1 365 ? -11.979 -14.407 86.816  1.00 40.15  ? 365  THR B CG2 1 
ATOM   6642 N  N   . ILE B 1 366 ? -11.268 -11.118 83.604  1.00 34.45  ? 366  ILE B N   1 
ATOM   6643 C  CA  . ILE B 1 366 ? -10.709 -9.961  82.920  1.00 36.53  ? 366  ILE B CA  1 
ATOM   6644 C  C   . ILE B 1 366 ? -11.763 -9.239  82.101  1.00 35.87  ? 366  ILE B C   1 
ATOM   6645 O  O   . ILE B 1 366 ? -11.932 -8.026  82.216  1.00 40.62  ? 366  ILE B O   1 
ATOM   6646 C  CB  . ILE B 1 366 ? -9.534  -10.398 82.013  1.00 33.20  ? 366  ILE B CB  1 
ATOM   6647 C  CG1 . ILE B 1 366 ? -8.411  -10.996 82.855  1.00 36.55  ? 366  ILE B CG1 1 
ATOM   6648 C  CG2 . ILE B 1 366 ? -9.040  -9.216  81.185  1.00 39.77  ? 366  ILE B CG2 1 
ATOM   6649 C  CD1 . ILE B 1 366 ? -7.719  -9.992  83.765  1.00 43.29  ? 366  ILE B CD1 1 
ATOM   6650 N  N   . TRP B 1 367 ? -12.466 -9.980  81.252  1.00 37.52  ? 367  TRP B N   1 
ATOM   6651 C  CA  . TRP B 1 367 ? -13.279 -9.402  80.200  1.00 33.24  ? 367  TRP B CA  1 
ATOM   6652 C  C   . TRP B 1 367 ? -14.753 -9.283  80.572  1.00 38.51  ? 367  TRP B C   1 
ATOM   6653 O  O   . TRP B 1 367 ? -15.495 -8.581  79.882  1.00 41.48  ? 367  TRP B O   1 
ATOM   6654 C  CB  . TRP B 1 367 ? -13.124 -10.237 78.926  1.00 36.69  ? 367  TRP B CB  1 
ATOM   6655 C  CG  . TRP B 1 367 ? -11.690 -10.306 78.444  1.00 33.06  ? 367  TRP B CG  1 
ATOM   6656 C  CD1 . TRP B 1 367 ? -10.778 -11.276 78.706  1.00 34.93  ? 367  TRP B CD1 1 
ATOM   6657 C  CD2 . TRP B 1 367 ? -11.030 -9.339  77.609  1.00 32.71  ? 367  TRP B CD2 1 
ATOM   6658 N  NE1 . TRP B 1 367 ? -9.572  -10.972 78.093  1.00 32.81  ? 367  TRP B NE1 1 
ATOM   6659 C  CE2 . TRP B 1 367 ? -9.707  -9.787  77.414  1.00 34.21  ? 367  TRP B CE2 1 
ATOM   6660 C  CE3 . TRP B 1 367 ? -11.430 -8.133  77.020  1.00 36.88  ? 367  TRP B CE3 1 
ATOM   6661 C  CZ2 . TRP B 1 367 ? -8.779  -9.076  76.637  1.00 33.89  ? 367  TRP B CZ2 1 
ATOM   6662 C  CZ3 . TRP B 1 367 ? -10.507 -7.421  76.251  1.00 33.39  ? 367  TRP B CZ3 1 
ATOM   6663 C  CH2 . TRP B 1 367 ? -9.195  -7.901  76.067  1.00 32.11  ? 367  TRP B CH2 1 
ATOM   6664 N  N   . GLY B 1 368 ? -15.187 -9.933  81.638  1.00 36.29  ? 368  GLY B N   1 
ATOM   6665 C  CA  . GLY B 1 368 ? -16.592 -9.939  82.000  1.00 37.69  ? 368  GLY B CA  1 
ATOM   6666 C  C   . GLY B 1 368 ? -17.287 -11.171 81.466  1.00 42.16  ? 368  GLY B C   1 
ATOM   6667 O  O   . GLY B 1 368 ? -16.691 -12.033 80.812  1.00 39.93  ? 368  GLY B O   1 
ATOM   6668 N  N   . ASP B 1 369 ? -18.594 -11.227 81.734  1.00 42.19  ? 369  ASP B N   1 
ATOM   6669 C  CA  . ASP B 1 369 ? -19.371 -12.422 81.429  1.00 43.49  ? 369  ASP B CA  1 
ATOM   6670 C  C   . ASP B 1 369 ? -19.599 -12.607 79.932  1.00 42.14  ? 369  ASP B C   1 
ATOM   6671 O  O   . ASP B 1 369 ? -19.821 -13.731 79.484  1.00 48.28  ? 369  ASP B O   1 
ATOM   6672 C  CB  . ASP B 1 369 ? -20.719 -12.356 82.143  1.00 50.32  ? 369  ASP B CB  1 
ATOM   6673 C  CG  . ASP B 1 369 ? -20.577 -12.356 83.640  1.00 53.98  ? 369  ASP B CG  1 
ATOM   6674 O  OD1 . ASP B 1 369 ? -19.834 -13.214 84.157  1.00 56.45  ? 369  ASP B OD1 1 
ATOM   6675 O  OD2 . ASP B 1 369 ? -21.183 -11.477 84.287  1.00 59.10  ? 369  ASP B OD2 1 
ATOM   6676 N  N   . ASP B 1 370 ? -19.566 -11.532 79.152  1.00 38.07  ? 370  ASP B N   1 
ATOM   6677 C  CA  . ASP B 1 370 ? -19.968 -11.601 77.747  1.00 41.34  ? 370  ASP B CA  1 
ATOM   6678 C  C   . ASP B 1 370 ? -18.812 -11.949 76.807  1.00 39.56  ? 370  ASP B C   1 
ATOM   6679 O  O   . ASP B 1 370 ? -18.773 -11.439 75.684  1.00 38.39  ? 370  ASP B O   1 
ATOM   6680 C  CB  . ASP B 1 370 ? -20.608 -10.271 77.355  1.00 43.43  ? 370  ASP B CB  1 
ATOM   6681 C  CG  . ASP B 1 370 ? -19.634 -9.097  77.443  1.00 44.41  ? 370  ASP B CG  1 
ATOM   6682 O  OD1 . ASP B 1 370 ? -18.493 -9.276  77.931  1.00 44.76  ? 370  ASP B OD1 1 
ATOM   6683 O  OD2 . ASP B 1 370 ? -20.017 -7.979  77.031  1.00 49.17  ? 370  ASP B OD2 1 
ATOM   6684 N  N   . VAL B 1 371 ? -17.882 -12.826 77.207  1.00 39.33  ? 371  VAL B N   1 
ATOM   6685 C  CA  . VAL B 1 371 ? -16.643 -12.996 76.446  1.00 35.67  ? 371  VAL B CA  1 
ATOM   6686 C  C   . VAL B 1 371 ? -16.848 -13.594 75.064  1.00 35.63  ? 371  VAL B C   1 
ATOM   6687 O  O   . VAL B 1 371 ? -15.985 -13.416 74.193  1.00 36.78  ? 371  VAL B O   1 
ATOM   6688 C  CB  . VAL B 1 371 ? -15.617 -13.867 77.203  1.00 39.88  ? 371  VAL B CB  1 
ATOM   6689 C  CG1 . VAL B 1 371 ? -15.140 -13.159 78.461  1.00 44.17  ? 371  VAL B CG1 1 
ATOM   6690 C  CG2 . VAL B 1 371 ? -16.206 -15.246 77.542  1.00 42.26  ? 371  VAL B CG2 1 
ATOM   6691 N  N   . GLU B 1 372 ? -17.939 -14.321 74.825  1.00 34.44  ? 372  GLU B N   1 
ATOM   6692 C  CA  . GLU B 1 372 ? -18.144 -14.894 73.498  1.00 37.14  ? 372  GLU B CA  1 
ATOM   6693 C  C   . GLU B 1 372 ? -18.753 -13.906 72.508  1.00 36.04  ? 372  GLU B C   1 
ATOM   6694 O  O   . GLU B 1 372 ? -18.773 -14.190 71.304  1.00 37.57  ? 372  GLU B O   1 
ATOM   6695 C  CB  . GLU B 1 372 ? -19.034 -16.138 73.594  1.00 36.99  ? 372  GLU B CB  1 
ATOM   6696 C  CG  . GLU B 1 372 ? -18.391 -17.315 74.337  1.00 40.73  ? 372  GLU B CG  1 
ATOM   6697 C  CD  . GLU B 1 372 ? -17.262 -17.954 73.539  1.00 41.67  ? 372  GLU B CD  1 
ATOM   6698 O  OE1 . GLU B 1 372 ? -17.360 -18.006 72.289  1.00 45.06  ? 372  GLU B OE1 1 
ATOM   6699 O  OE2 . GLU B 1 372 ? -16.287 -18.406 74.168  1.00 49.33  ? 372  GLU B OE2 1 
ATOM   6700 N  N   . GLU B 1 373 ? -19.237 -12.759 72.972  1.00 34.29  ? 373  GLU B N   1 
ATOM   6701 C  CA  . GLU B 1 373 ? -19.838 -11.779 72.080  1.00 33.26  ? 373  GLU B CA  1 
ATOM   6702 C  C   . GLU B 1 373 ? -18.763 -10.944 71.395  1.00 32.87  ? 373  GLU B C   1 
ATOM   6703 O  O   . GLU B 1 373 ? -17.685 -10.694 71.947  1.00 33.50  ? 373  GLU B O   1 
ATOM   6704 C  CB  . GLU B 1 373 ? -20.823 -10.894 72.850  1.00 39.45  ? 373  GLU B CB  1 
ATOM   6705 C  CG  . GLU B 1 373 ? -22.046 -11.698 73.293  1.00 38.39  ? 373  GLU B CG  1 
ATOM   6706 C  CD  . GLU B 1 373 ? -23.006 -10.942 74.206  1.00 47.54  ? 373  GLU B CD  1 
ATOM   6707 O  OE1 . GLU B 1 373 ? -22.727 -9.778  74.574  1.00 45.08  ? 373  GLU B OE1 1 
ATOM   6708 O  OE2 . GLU B 1 373 ? -24.048 -11.536 74.565  1.00 52.59  ? 373  GLU B OE2 1 
ATOM   6709 N  N   . PHE B 1 374 ? -19.068 -10.530 70.165  1.00 32.75  ? 374  PHE B N   1 
ATOM   6710 C  CA  . PHE B 1 374 ? -18.163 -9.725  69.350  1.00 33.35  ? 374  PHE B CA  1 
ATOM   6711 C  C   . PHE B 1 374 ? -18.483 -8.262  69.617  1.00 33.23  ? 374  PHE B C   1 
ATOM   6712 O  O   . PHE B 1 374 ? -19.470 -7.721  69.102  1.00 31.88  ? 374  PHE B O   1 
ATOM   6713 C  CB  . PHE B 1 374 ? -18.311 -10.057 67.870  1.00 31.83  ? 374  PHE B CB  1 
ATOM   6714 C  CG  . PHE B 1 374 ? -17.266 -9.419  67.028  1.00 30.98  ? 374  PHE B CG  1 
ATOM   6715 C  CD1 . PHE B 1 374 ? -15.990 -9.955  66.995  1.00 32.89  ? 374  PHE B CD1 1 
ATOM   6716 C  CD2 . PHE B 1 374 ? -17.538 -8.267  66.284  1.00 31.64  ? 374  PHE B CD2 1 
ATOM   6717 C  CE1 . PHE B 1 374 ? -14.997 -9.361  66.236  1.00 28.39  ? 374  PHE B CE1 1 
ATOM   6718 C  CE2 . PHE B 1 374 ? -16.545 -7.675  65.519  1.00 33.72  ? 374  PHE B CE2 1 
ATOM   6719 C  CZ  . PHE B 1 374 ? -15.269 -8.215  65.514  1.00 34.38  ? 374  PHE B CZ  1 
ATOM   6720 N  N   . ARG B 1 375 ? -17.656 -7.616  70.433  1.00 30.78  ? 375  ARG B N   1 
ATOM   6721 C  CA  . ARG B 1 375 ? -17.930 -6.252  70.884  1.00 32.20  ? 375  ARG B CA  1 
ATOM   6722 C  C   . ARG B 1 375 ? -16.656 -5.435  70.772  1.00 33.04  ? 375  ARG B C   1 
ATOM   6723 O  O   . ARG B 1 375 ? -15.883 -5.326  71.736  1.00 33.64  ? 375  ARG B O   1 
ATOM   6724 C  CB  . ARG B 1 375 ? -18.479 -6.242  72.315  1.00 30.90  ? 375  ARG B CB  1 
ATOM   6725 C  CG  . ARG B 1 375 ? -19.873 -6.828  72.440  1.00 35.46  ? 375  ARG B CG  1 
ATOM   6726 C  CD  . ARG B 1 375 ? -20.372 -6.829  73.897  1.00 38.64  ? 375  ARG B CD  1 
ATOM   6727 N  NE  . ARG B 1 375 ? -21.721 -7.386  73.950  1.00 41.60  ? 375  ARG B NE  1 
ATOM   6728 C  CZ  . ARG B 1 375 ? -22.792 -6.772  73.458  1.00 45.76  ? 375  ARG B CZ  1 
ATOM   6729 N  NH1 . ARG B 1 375 ? -22.729 -5.526  73.007  1.00 41.05  ? 375  ARG B NH1 1 
ATOM   6730 N  NH2 . ARG B 1 375 ? -23.957 -7.415  73.433  1.00 44.29  ? 375  ARG B NH2 1 
ATOM   6731 N  N   . PRO B 1 376 ? -16.400 -4.844  69.598  1.00 31.57  ? 376  PRO B N   1 
ATOM   6732 C  CA  . PRO B 1 376 ? -15.191 -4.018  69.443  1.00 32.02  ? 376  PRO B CA  1 
ATOM   6733 C  C   . PRO B 1 376 ? -15.098 -2.895  70.462  1.00 34.84  ? 376  PRO B C   1 
ATOM   6734 O  O   . PRO B 1 376 ? -13.986 -2.448  70.776  1.00 32.52  ? 376  PRO B O   1 
ATOM   6735 C  CB  . PRO B 1 376 ? -15.319 -3.475  68.017  1.00 29.66  ? 376  PRO B CB  1 
ATOM   6736 C  CG  . PRO B 1 376 ? -16.153 -4.500  67.297  1.00 33.87  ? 376  PRO B CG  1 
ATOM   6737 C  CD  . PRO B 1 376 ? -17.166 -4.941  68.335  1.00 29.48  ? 376  PRO B CD  1 
ATOM   6738 N  N   . GLU B 1 377 ? -16.232 -2.442  71.001  1.00 34.86  ? 377  GLU B N   1 
ATOM   6739 C  CA  . GLU B 1 377 ? -16.234 -1.404  72.024  1.00 36.76  ? 377  GLU B CA  1 
ATOM   6740 C  C   . GLU B 1 377 ? -15.351 -1.744  73.226  1.00 37.70  ? 377  GLU B C   1 
ATOM   6741 O  O   . GLU B 1 377 ? -14.939 -0.828  73.948  1.00 38.59  ? 377  GLU B O   1 
ATOM   6742 C  CB  . GLU B 1 377 ? -17.676 -1.157  72.471  1.00 37.39  ? 377  GLU B CB  1 
ATOM   6743 C  CG  . GLU B 1 377 ? -18.512 -0.436  71.411  1.00 36.81  ? 377  GLU B CG  1 
ATOM   6744 C  CD  . GLU B 1 377 ? -18.968 -1.345  70.286  1.00 35.54  ? 377  GLU B CD  1 
ATOM   6745 O  OE1 . GLU B 1 377 ? -18.957 -2.577  70.469  1.00 34.47  ? 377  GLU B OE1 1 
ATOM   6746 O  OE2 . GLU B 1 377 ? -19.367 -0.823  69.219  1.00 35.83  ? 377  GLU B OE2 1 
ATOM   6747 N  N   . ARG B 1 378 ? -15.057 -3.030  73.463  1.00 36.08  ? 378  ARG B N   1 
ATOM   6748 C  CA  . ARG B 1 378 ? -14.125 -3.402  74.533  1.00 38.58  ? 378  ARG B CA  1 
ATOM   6749 C  C   . ARG B 1 378 ? -12.795 -2.700  74.410  1.00 38.56  ? 378  ARG B C   1 
ATOM   6750 O  O   . ARG B 1 378 ? -12.078 -2.562  75.409  1.00 38.69  ? 378  ARG B O   1 
ATOM   6751 C  CB  . ARG B 1 378 ? -13.801 -4.893  74.520  1.00 38.12  ? 378  ARG B CB  1 
ATOM   6752 C  CG  . ARG B 1 378 ? -14.916 -5.799  74.754  1.00 41.86  ? 378  ARG B CG  1 
ATOM   6753 C  CD  . ARG B 1 378 ? -14.384 -7.182  74.503  1.00 35.00  ? 378  ARG B CD  1 
ATOM   6754 N  NE  . ARG B 1 378 ? -15.477 -8.028  74.093  1.00 34.95  ? 378  ARG B NE  1 
ATOM   6755 C  CZ  . ARG B 1 378 ? -16.340 -8.564  74.936  1.00 36.60  ? 378  ARG B CZ  1 
ATOM   6756 N  NH1 . ARG B 1 378 ? -16.246 -8.359  76.246  1.00 38.39  ? 378  ARG B NH1 1 
ATOM   6757 N  NH2 . ARG B 1 378 ? -17.312 -9.328  74.458  1.00 35.12  ? 378  ARG B NH2 1 
ATOM   6758 N  N   . PHE B 1 379 ? -12.402 -2.343  73.191  1.00 35.22  ? 379  PHE B N   1 
ATOM   6759 C  CA  . PHE B 1 379 ? -11.090 -1.773  72.932  1.00 35.26  ? 379  PHE B CA  1 
ATOM   6760 C  C   . PHE B 1 379 ? -11.135 -0.259  72.777  1.00 38.70  ? 379  PHE B C   1 
ATOM   6761 O  O   . PHE B 1 379 ? -10.137 0.344   72.360  1.00 39.44  ? 379  PHE B O   1 
ATOM   6762 C  CB  . PHE B 1 379 ? -10.470 -2.434  71.689  1.00 37.45  ? 379  PHE B CB  1 
ATOM   6763 C  CG  . PHE B 1 379 ? -10.058 -3.866  71.920  1.00 35.15  ? 379  PHE B CG  1 
ATOM   6764 C  CD1 . PHE B 1 379 ? -8.793  -4.164  72.411  1.00 35.26  ? 379  PHE B CD1 1 
ATOM   6765 C  CD2 . PHE B 1 379 ? -10.937 -4.919  71.672  1.00 32.78  ? 379  PHE B CD2 1 
ATOM   6766 C  CE1 . PHE B 1 379 ? -8.406  -5.481  72.649  1.00 34.99  ? 379  PHE B CE1 1 
ATOM   6767 C  CE2 . PHE B 1 379 ? -10.561 -6.246  71.922  1.00 33.66  ? 379  PHE B CE2 1 
ATOM   6768 C  CZ  . PHE B 1 379 ? -9.284  -6.532  72.403  1.00 33.93  ? 379  PHE B CZ  1 
ATOM   6769 N  N   . GLU B 1 380 ? -12.269 0.369   73.106  1.00 40.06  ? 380  GLU B N   1 
ATOM   6770 C  CA  . GLU B 1 380 ? -12.380 1.819   72.965  1.00 39.79  ? 380  GLU B CA  1 
ATOM   6771 C  C   . GLU B 1 380 ? -11.280 2.525   73.737  1.00 47.10  ? 380  GLU B C   1 
ATOM   6772 O  O   . GLU B 1 380 ? -10.643 3.458   73.233  1.00 48.55  ? 380  GLU B O   1 
ATOM   6773 C  CB  . GLU B 1 380 ? -13.745 2.306   73.456  1.00 45.37  ? 380  GLU B CB  1 
ATOM   6774 C  CG  . GLU B 1 380 ? -14.890 2.161   72.485  1.00 48.19  ? 380  GLU B CG  1 
ATOM   6775 C  CD  . GLU B 1 380 ? -16.220 2.529   73.123  1.00 49.21  ? 380  GLU B CD  1 
ATOM   6776 O  OE1 . GLU B 1 380 ? -17.246 2.520   72.417  1.00 55.83  ? 380  GLU B OE1 1 
ATOM   6777 O  OE2 . GLU B 1 380 ? -16.230 2.812   74.341  1.00 60.31  ? 380  GLU B OE2 1 
ATOM   6778 N  N   . ASN B 1 381 ? -11.054 2.084   74.973  1.00 45.67  ? 381  ASN B N   1 
ATOM   6779 C  CA  . ASN B 1 381 ? -10.099 2.666   75.908  1.00 47.40  ? 381  ASN B CA  1 
ATOM   6780 C  C   . ASN B 1 381 ? -8.967  1.673   76.137  1.00 43.77  ? 381  ASN B C   1 
ATOM   6781 O  O   . ASN B 1 381 ? -9.073  0.787   76.998  1.00 48.49  ? 381  ASN B O   1 
ATOM   6782 C  CB  . ASN B 1 381 ? -10.805 3.008   77.222  1.00 49.61  ? 381  ASN B CB  1 
ATOM   6783 C  CG  . ASN B 1 381 ? -9.917  3.765   78.185  1.00 54.50  ? 381  ASN B CG  1 
ATOM   6784 O  OD1 . ASN B 1 381 ? -8.708  3.906   77.967  1.00 51.25  ? 381  ASN B OD1 1 
ATOM   6785 N  ND2 . ASN B 1 381 ? -10.513 4.247   79.271  1.00 53.49  ? 381  ASN B ND2 1 
ATOM   6786 N  N   . PRO B 1 382 ? -7.866  1.772   75.392  1.00 50.10  ? 382  PRO B N   1 
ATOM   6787 C  CA  . PRO B 1 382 ? -6.787  0.783   75.551  1.00 51.69  ? 382  PRO B CA  1 
ATOM   6788 C  C   . PRO B 1 382 ? -6.215  0.743   76.954  1.00 52.55  ? 382  PRO B C   1 
ATOM   6789 O  O   . PRO B 1 382 ? -5.695  -0.301  77.370  1.00 49.33  ? 382  PRO B O   1 
ATOM   6790 C  CB  . PRO B 1 382 ? -5.724  1.223   74.533  1.00 53.04  ? 382  PRO B CB  1 
ATOM   6791 C  CG  . PRO B 1 382 ? -6.192  2.500   73.940  1.00 55.33  ? 382  PRO B CG  1 
ATOM   6792 C  CD  . PRO B 1 382 ? -7.564  2.827   74.410  1.00 54.84  ? 382  PRO B CD  1 
ATOM   6793 N  N   . SER B 1 383 ? -6.297  1.853   77.698  1.00 51.40  ? 383  SER B N   1 
ATOM   6794 C  CA  . SER B 1 383 ? -5.762  1.877   79.057  1.00 55.14  ? 383  SER B CA  1 
ATOM   6795 C  C   . SER B 1 383 ? -6.490  0.905   79.967  1.00 51.80  ? 383  SER B C   1 
ATOM   6796 O  O   . SER B 1 383 ? -5.922  0.431   80.955  1.00 53.21  ? 383  SER B O   1 
ATOM   6797 C  CB  . SER B 1 383 ? -5.844  3.291   79.637  1.00 51.37  ? 383  SER B CB  1 
ATOM   6798 O  OG  . SER B 1 383 ? -4.908  4.142   79.009  1.00 58.29  ? 383  SER B OG  1 
ATOM   6799 N  N   . ALA B 1 384 ? -7.742  0.593   79.652  1.00 52.79  ? 384  ALA B N   1 
ATOM   6800 C  CA  . ALA B 1 384 ? -8.540  -0.256  80.517  1.00 53.13  ? 384  ALA B CA  1 
ATOM   6801 C  C   . ALA B 1 384 ? -8.162  -1.732  80.431  1.00 54.18  ? 384  ALA B C   1 
ATOM   6802 O  O   . ALA B 1 384 ? -8.661  -2.521  81.240  1.00 51.56  ? 384  ALA B O   1 
ATOM   6803 C  CB  . ALA B 1 384 ? -10.021 -0.066  80.178  1.00 54.99  ? 384  ALA B CB  1 
ATOM   6804 N  N   . ILE B 1 385 ? -7.307  -2.124  79.492  1.00 48.90  ? 385  ILE B N   1 
ATOM   6805 C  CA  . ILE B 1 385 ? -6.951  -3.527  79.290  1.00 50.19  ? 385  ILE B CA  1 
ATOM   6806 C  C   . ILE B 1 385 ? -5.778  -3.860  80.206  1.00 47.07  ? 385  ILE B C   1 
ATOM   6807 O  O   . ILE B 1 385 ? -4.684  -3.300  80.017  1.00 49.61  ? 385  ILE B O   1 
ATOM   6808 C  CB  . ILE B 1 385 ? -6.584  -3.810  77.828  1.00 48.02  ? 385  ILE B CB  1 
ATOM   6809 C  CG1 . ILE B 1 385 ? -7.672  -3.302  76.875  1.00 51.38  ? 385  ILE B CG1 1 
ATOM   6810 C  CG2 . ILE B 1 385 ? -6.307  -5.292  77.636  1.00 47.61  ? 385  ILE B CG2 1 
ATOM   6811 C  CD1 . ILE B 1 385 ? -8.879  -4.196  76.793  1.00 51.65  ? 385  ILE B CD1 1 
ATOM   6812 N  N   . PRO B 1 386 ? -5.940  -4.773  81.168  1.00 46.41  ? 386  PRO B N   1 
ATOM   6813 C  CA  . PRO B 1 386 ? -4.824  -5.121  82.060  1.00 45.56  ? 386  PRO B CA  1 
ATOM   6814 C  C   . PRO B 1 386 ? -3.640  -5.678  81.285  1.00 51.18  ? 386  PRO B C   1 
ATOM   6815 O  O   . PRO B 1 386 ? -3.796  -6.250  80.206  1.00 42.43  ? 386  PRO B O   1 
ATOM   6816 C  CB  . PRO B 1 386 ? -5.432  -6.183  82.991  1.00 47.38  ? 386  PRO B CB  1 
ATOM   6817 C  CG  . PRO B 1 386 ? -6.917  -6.003  82.874  1.00 48.87  ? 386  PRO B CG  1 
ATOM   6818 C  CD  . PRO B 1 386 ? -7.166  -5.525  81.478  1.00 47.77  ? 386  PRO B CD  1 
ATOM   6819 N  N   . GLN B 1 387 ? -2.441  -5.503  81.849  1.00 45.57  ? 387  GLN B N   1 
ATOM   6820 C  CA  . GLN B 1 387 ? -1.236  -6.061  81.248  1.00 48.09  ? 387  GLN B CA  1 
ATOM   6821 C  C   . GLN B 1 387 ? -1.349  -7.577  81.121  1.00 42.32  ? 387  GLN B C   1 
ATOM   6822 O  O   . GLN B 1 387 ? -1.819  -8.259  82.037  1.00 44.76  ? 387  GLN B O   1 
ATOM   6823 C  CB  . GLN B 1 387 ? -0.006  -5.714  82.096  1.00 51.89  ? 387  GLN B CB  1 
ATOM   6824 C  CG  . GLN B 1 387 ? 1.332   -6.064  81.443  1.00 54.09  ? 387  GLN B CG  1 
ATOM   6825 C  CD  . GLN B 1 387 ? 2.521   -5.700  82.323  1.00 61.34  ? 387  GLN B CD  1 
ATOM   6826 O  OE1 . GLN B 1 387 ? 3.665   -5.692  81.868  1.00 63.36  ? 387  GLN B OE1 1 
ATOM   6827 N  NE2 . GLN B 1 387 ? 2.254   -5.425  83.600  1.00 62.03  ? 387  GLN B NE2 1 
ATOM   6828 N  N   . HIS B 1 388 ? -0.881  -8.107  79.989  1.00 41.74  ? 388  HIS B N   1 
ATOM   6829 C  CA  . HIS B 1 388 ? -0.839  -9.535  79.679  1.00 40.98  ? 388  HIS B CA  1 
ATOM   6830 C  C   . HIS B 1 388 ? -2.223  -10.164 79.563  1.00 37.15  ? 388  HIS B C   1 
ATOM   6831 O  O   . HIS B 1 388 ? -2.335  -11.391 79.546  1.00 39.86  ? 388  HIS B O   1 
ATOM   6832 C  CB  . HIS B 1 388 ? -0.005  -10.303 80.709  1.00 41.94  ? 388  HIS B CB  1 
ATOM   6833 C  CG  . HIS B 1 388 ? 1.412   -9.820  80.798  1.00 42.53  ? 388  HIS B CG  1 
ATOM   6834 N  ND1 . HIS B 1 388 ? 2.206   -9.647  79.684  1.00 49.06  ? 388  HIS B ND1 1 
ATOM   6835 C  CD2 . HIS B 1 388 ? 2.166   -9.444  81.860  1.00 45.54  ? 388  HIS B CD2 1 
ATOM   6836 C  CE1 . HIS B 1 388 ? 3.394   -9.203  80.057  1.00 46.80  ? 388  HIS B CE1 1 
ATOM   6837 N  NE2 . HIS B 1 388 ? 3.395   -9.067  81.371  1.00 46.22  ? 388  HIS B NE2 1 
ATOM   6838 N  N   . ALA B 1 389 ? -3.280  -9.363  79.470  1.00 35.23  ? 389  ALA B N   1 
ATOM   6839 C  CA  . ALA B 1 389 ? -4.614  -9.918  79.237  1.00 35.38  ? 389  ALA B CA  1 
ATOM   6840 C  C   . ALA B 1 389 ? -4.896  -10.169 77.759  1.00 34.43  ? 389  ALA B C   1 
ATOM   6841 O  O   . ALA B 1 389 ? -5.739  -11.007 77.430  1.00 32.77  ? 389  ALA B O   1 
ATOM   6842 C  CB  . ALA B 1 389 ? -5.678  -8.984  79.802  1.00 39.51  ? 389  ALA B CB  1 
ATOM   6843 N  N   . PHE B 1 390 ? -4.188  -9.490  76.865  1.00 33.16  ? 390  PHE B N   1 
ATOM   6844 C  CA  . PHE B 1 390 ? -4.460  -9.544  75.430  1.00 30.46  ? 390  PHE B CA  1 
ATOM   6845 C  C   . PHE B 1 390 ? -3.126  -9.772  74.728  1.00 34.33  ? 390  PHE B C   1 
ATOM   6846 O  O   . PHE B 1 390 ? -2.281  -8.876  74.706  1.00 34.88  ? 390  PHE B O   1 
ATOM   6847 C  CB  . PHE B 1 390 ? -5.125  -8.243  74.985  1.00 30.74  ? 390  PHE B CB  1 
ATOM   6848 C  CG  . PHE B 1 390 ? -5.453  -8.179  73.508  1.00 30.72  ? 390  PHE B CG  1 
ATOM   6849 C  CD1 . PHE B 1 390 ? -6.373  -9.046  72.947  1.00 31.81  ? 390  PHE B CD1 1 
ATOM   6850 C  CD2 . PHE B 1 390 ? -4.855  -7.229  72.694  1.00 29.79  ? 390  PHE B CD2 1 
ATOM   6851 C  CE1 . PHE B 1 390 ? -6.688  -8.961  71.591  1.00 29.68  ? 390  PHE B CE1 1 
ATOM   6852 C  CE2 . PHE B 1 390 ? -5.151  -7.142  71.334  1.00 32.74  ? 390  PHE B CE2 1 
ATOM   6853 C  CZ  . PHE B 1 390 ? -6.067  -8.008  70.783  1.00 32.09  ? 390  PHE B CZ  1 
ATOM   6854 N  N   . LYS B 1 391 ? -2.915  -10.985 74.208  1.00 33.92  ? 391  LYS B N   1 
ATOM   6855 C  CA  . LYS B 1 391 ? -1.582  -11.365 73.740  1.00 34.10  ? 391  LYS B CA  1 
ATOM   6856 C  C   . LYS B 1 391 ? -1.598  -12.040 72.376  1.00 32.18  ? 391  LYS B C   1 
ATOM   6857 O  O   . LYS B 1 391 ? -0.900  -13.043 72.183  1.00 32.06  ? 391  LYS B O   1 
ATOM   6858 C  CB  . LYS B 1 391 ? -0.917  -12.310 74.747  1.00 32.92  ? 391  LYS B CB  1 
ATOM   6859 C  CG  . LYS B 1 391 ? -0.928  -11.790 76.180  1.00 36.66  ? 391  LYS B CG  1 
ATOM   6860 C  CD  . LYS B 1 391 ? 0.041   -10.641 76.323  1.00 40.14  ? 391  LYS B CD  1 
ATOM   6861 C  CE  . LYS B 1 391 ? 1.485   -11.129 76.263  1.00 37.91  ? 391  LYS B CE  1 
ATOM   6862 N  NZ  . LYS B 1 391 ? 2.427   -10.006 76.621  1.00 42.08  ? 391  LYS B NZ  1 
ATOM   6863 N  N   . PRO B 1 392 ? -2.359  -11.533 71.405  1.00 32.50  ? 392  PRO B N   1 
ATOM   6864 C  CA  . PRO B 1 392 ? -2.375  -12.179 70.087  1.00 30.38  ? 392  PRO B CA  1 
ATOM   6865 C  C   . PRO B 1 392 ? -1.036  -12.100 69.386  1.00 32.35  ? 392  PRO B C   1 
ATOM   6866 O  O   . PRO B 1 392 ? -0.839  -12.799 68.386  1.00 31.52  ? 392  PRO B O   1 
ATOM   6867 C  CB  . PRO B 1 392 ? -3.438  -11.389 69.315  1.00 32.05  ? 392  PRO B CB  1 
ATOM   6868 C  CG  . PRO B 1 392 ? -3.316  -10.004 69.898  1.00 32.77  ? 392  PRO B CG  1 
ATOM   6869 C  CD  . PRO B 1 392 ? -3.053  -10.239 71.391  1.00 32.00  ? 392  PRO B CD  1 
ATOM   6870 N  N   . HIS B 1 393 ? -0.119  -11.261 69.859  1.00 30.71  ? 393  HIS B N   1 
ATOM   6871 C  CA  . HIS B 1 393 ? 1.171   -11.135 69.182  1.00 31.74  ? 393  HIS B CA  1 
ATOM   6872 C  C   . HIS B 1 393 ? 2.327   -11.620 70.048  1.00 32.92  ? 393  HIS B C   1 
ATOM   6873 O  O   . HIS B 1 393 ? 3.475   -11.205 69.841  1.00 32.55  ? 393  HIS B O   1 
ATOM   6874 C  CB  . HIS B 1 393 ? 1.383   -9.699  68.702  1.00 33.82  ? 393  HIS B CB  1 
ATOM   6875 C  CG  . HIS B 1 393 ? 0.565   -9.357  67.485  1.00 38.03  ? 393  HIS B CG  1 
ATOM   6876 N  ND1 . HIS B 1 393 ? -0.576  -8.589  67.546  1.00 38.31  ? 393  HIS B ND1 1 
ATOM   6877 C  CD2 . HIS B 1 393 ? 0.712   -9.706  66.181  1.00 38.77  ? 393  HIS B CD2 1 
ATOM   6878 C  CE1 . HIS B 1 393 ? -1.091  -8.463  66.336  1.00 38.78  ? 393  HIS B CE1 1 
ATOM   6879 N  NE2 . HIS B 1 393 ? -0.328  -9.135  65.486  1.00 39.57  ? 393  HIS B NE2 1 
ATOM   6880 N  N   . GLY B 1 394 ? 2.062   -12.504 71.010  1.00 31.31  ? 394  GLY B N   1 
ATOM   6881 C  CA  . GLY B 1 394 ? 3.178   -13.056 71.759  1.00 32.68  ? 394  GLY B CA  1 
ATOM   6882 C  C   . GLY B 1 394 ? 3.618   -12.125 72.875  1.00 35.82  ? 394  GLY B C   1 
ATOM   6883 O  O   . GLY B 1 394 ? 2.865   -11.252 73.330  1.00 31.54  ? 394  GLY B O   1 
ATOM   6884 N  N   . ASN B 1 395 ? 4.865   -12.317 73.328  1.00 32.29  ? 395  ASN B N   1 
ATOM   6885 C  CA  . ASN B 1 395 ? 5.301   -11.650 74.540  1.00 34.04  ? 395  ASN B CA  1 
ATOM   6886 C  C   . ASN B 1 395 ? 6.750   -11.193 74.463  1.00 32.68  ? 395  ASN B C   1 
ATOM   6887 O  O   . ASN B 1 395 ? 7.617   -11.929 73.987  1.00 33.50  ? 395  ASN B O   1 
ATOM   6888 C  CB  . ASN B 1 395 ? 5.167   -12.560 75.756  1.00 33.35  ? 395  ASN B CB  1 
ATOM   6889 C  CG  . ASN B 1 395 ? 5.550   -11.852 77.024  1.00 35.33  ? 395  ASN B CG  1 
ATOM   6890 O  OD1 . ASN B 1 395 ? 4.877   -10.905 77.440  1.00 37.50  ? 395  ASN B OD1 1 
ATOM   6891 N  ND2 . ASN B 1 395 ? 6.645   -12.285 77.646  1.00 34.31  ? 395  ASN B ND2 1 
ATOM   6892 N  N   . GLY B 1 396 ? 6.998   -9.988  74.978  1.00 32.86  ? 396  GLY B N   1 
ATOM   6893 C  CA  . GLY B 1 396 ? 8.339   -9.518  75.318  1.00 32.68  ? 396  GLY B CA  1 
ATOM   6894 C  C   . GLY B 1 396 ? 9.238   -9.357  74.107  1.00 31.01  ? 396  GLY B C   1 
ATOM   6895 O  O   . GLY B 1 396 ? 8.808   -8.986  73.014  1.00 33.24  ? 396  GLY B O   1 
ATOM   6896 N  N   . GLN B 1 397 ? 10.527  -9.629  74.308  1.00 31.91  ? 397  GLN B N   1 
ATOM   6897 C  CA  . GLN B 1 397 ? 11.455  -9.486  73.194  1.00 32.47  ? 397  GLN B CA  1 
ATOM   6898 C  C   . GLN B 1 397 ? 11.186  -10.502 72.091  1.00 33.84  ? 397  GLN B C   1 
ATOM   6899 O  O   . GLN B 1 397 ? 11.655  -10.304 70.968  1.00 34.12  ? 397  GLN B O   1 
ATOM   6900 C  CB  . GLN B 1 397 ? 12.905  -9.602  73.690  1.00 34.20  ? 397  GLN B CB  1 
ATOM   6901 C  CG  . GLN B 1 397 ? 13.311  -10.984 74.171  1.00 31.75  ? 397  GLN B CG  1 
ATOM   6902 C  CD  . GLN B 1 397 ? 14.742  -11.011 74.699  1.00 36.11  ? 397  GLN B CD  1 
ATOM   6903 O  OE1 . GLN B 1 397 ? 15.542  -10.130 74.389  1.00 36.51  ? 397  GLN B OE1 1 
ATOM   6904 N  NE2 . GLN B 1 397 ? 15.065  -12.030 75.489  1.00 36.86  ? 397  GLN B NE2 1 
ATOM   6905 N  N   . ARG B 1 398 ? 10.443  -11.576 72.379  1.00 30.25  ? 398  ARG B N   1 
ATOM   6906 C  CA  . ARG B 1 398 ? 10.065  -12.552 71.366  1.00 30.81  ? 398  ARG B CA  1 
ATOM   6907 C  C   . ARG B 1 398 ? 8.661   -12.288 70.818  1.00 28.44  ? 398  ARG B C   1 
ATOM   6908 O  O   . ARG B 1 398 ? 8.056   -13.176 70.203  1.00 32.37  ? 398  ARG B O   1 
ATOM   6909 C  CB  . ARG B 1 398 ? 10.166  -13.971 71.932  1.00 30.79  ? 398  ARG B CB  1 
ATOM   6910 C  CG  . ARG B 1 398 ? 11.606  -14.389 72.360  1.00 30.18  ? 398  ARG B CG  1 
ATOM   6911 C  CD  . ARG B 1 398 ? 12.649  -14.160 71.246  1.00 30.57  ? 398  ARG B CD  1 
ATOM   6912 N  NE  . ARG B 1 398 ? 12.373  -14.870 69.999  1.00 28.73  ? 398  ARG B NE  1 
ATOM   6913 C  CZ  . ARG B 1 398 ? 12.790  -16.096 69.718  1.00 30.84  ? 398  ARG B CZ  1 
ATOM   6914 N  NH1 . ARG B 1 398 ? 13.474  -16.821 70.602  1.00 30.67  ? 398  ARG B NH1 1 
ATOM   6915 N  NH2 . ARG B 1 398 ? 12.539  -16.604 68.510  1.00 29.34  ? 398  ARG B NH2 1 
ATOM   6916 N  N   . ALA B 1 399 ? 8.126   -11.100 71.062  1.00 31.45  ? 399  ALA B N   1 
ATOM   6917 C  CA  . ALA B 1 399 ? 6.826   -10.753 70.509  1.00 31.95  ? 399  ALA B CA  1 
ATOM   6918 C  C   . ALA B 1 399 ? 6.923   -10.609 68.992  1.00 30.62  ? 399  ALA B C   1 
ATOM   6919 O  O   . ALA B 1 399 ? 8.005   -10.521 68.409  1.00 32.39  ? 399  ALA B O   1 
ATOM   6920 C  CB  . ALA B 1 399 ? 6.298   -9.463  71.142  1.00 32.15  ? 399  ALA B CB  1 
ATOM   6921 N  N   . CYS B 1 400 ? 5.767   -10.588 68.346  1.00 30.78  ? 400  CYS B N   1 
ATOM   6922 C  CA  . CYS B 1 400 ? 5.699   -10.505 66.890  1.00 29.97  ? 400  CYS B CA  1 
ATOM   6923 C  C   . CYS B 1 400 ? 6.374   -9.240  66.364  1.00 29.66  ? 400  CYS B C   1 
ATOM   6924 O  O   . CYS B 1 400 ? 5.978   -8.121  66.697  1.00 32.96  ? 400  CYS B O   1 
ATOM   6925 C  CB  . CYS B 1 400 ? 4.226   -10.532 66.475  1.00 30.25  ? 400  CYS B CB  1 
ATOM   6926 S  SG  . CYS B 1 400 ? 3.998   -10.342 64.700  1.00 31.58  ? 400  CYS B SG  1 
ATOM   6927 N  N   . ILE B 1 401 ? 7.385   -9.409  65.510  1.00 29.06  ? 401  ILE B N   1 
ATOM   6928 C  CA  . ILE B 1 401 ? 8.048   -8.241  64.941  1.00 30.63  ? 401  ILE B CA  1 
ATOM   6929 C  C   . ILE B 1 401 ? 7.179   -7.529  63.904  1.00 35.51  ? 401  ILE B C   1 
ATOM   6930 O  O   . ILE B 1 401 ? 7.376   -6.336  63.655  1.00 35.00  ? 401  ILE B O   1 
ATOM   6931 C  CB  . ILE B 1 401 ? 9.402   -8.654  64.327  1.00 29.97  ? 401  ILE B CB  1 
ATOM   6932 C  CG1 . ILE B 1 401 ? 10.336  -7.448  64.199  1.00 32.80  ? 401  ILE B CG1 1 
ATOM   6933 C  CG2 . ILE B 1 401 ? 9.201   -9.312  62.960  1.00 33.85  ? 401  ILE B CG2 1 
ATOM   6934 C  CD1 . ILE B 1 401 ? 11.699  -7.818  63.601  1.00 37.63  ? 401  ILE B CD1 1 
ATOM   6935 N  N   . GLY B 1 402 ? 6.220   -8.220  63.290  1.00 34.74  ? 402  GLY B N   1 
ATOM   6936 C  CA  . GLY B 1 402 ? 5.429   -7.670  62.201  1.00 31.93  ? 402  GLY B CA  1 
ATOM   6937 C  C   . GLY B 1 402 ? 4.065   -7.147  62.595  1.00 33.14  ? 402  GLY B C   1 
ATOM   6938 O  O   . GLY B 1 402 ? 3.226   -6.908  61.717  1.00 34.35  ? 402  GLY B O   1 
ATOM   6939 N  N   . GLN B 1 403 ? 3.815   -6.957  63.890  1.00 28.54  ? 403  GLN B N   1 
ATOM   6940 C  CA  . GLN B 1 403 ? 2.460   -6.673  64.345  1.00 31.30  ? 403  GLN B CA  1 
ATOM   6941 C  C   . GLN B 1 403 ? 1.941   -5.337  63.816  1.00 36.58  ? 403  GLN B C   1 
ATOM   6942 O  O   . GLN B 1 403 ? 0.770   -5.242  63.420  1.00 35.08  ? 403  GLN B O   1 
ATOM   6943 C  CB  . GLN B 1 403 ? 2.454   -6.818  65.867  1.00 36.97  ? 403  GLN B CB  1 
ATOM   6944 C  CG  . GLN B 1 403 ? 3.322   -5.881  66.625  1.00 37.39  ? 403  GLN B CG  1 
ATOM   6945 C  CD  . GLN B 1 403 ? 3.228   -6.149  68.137  1.00 46.87  ? 403  GLN B CD  1 
ATOM   6946 O  OE1 . GLN B 1 403 ? 2.257   -5.747  68.782  1.00 41.31  ? 403  GLN B OE1 1 
ATOM   6947 N  NE2 . GLN B 1 403 ? 4.252   -6.857  68.700  1.00 36.10  ? 403  GLN B NE2 1 
ATOM   6948 N  N   . GLN B 1 404 ? 2.802   -4.318  63.714  1.00 34.84  ? 404  GLN B N   1 
ATOM   6949 C  CA  . GLN B 1 404 ? 2.349   -3.053  63.136  1.00 38.07  ? 404  GLN B CA  1 
ATOM   6950 C  C   . GLN B 1 404 ? 2.089   -3.188  61.636  1.00 34.77  ? 404  GLN B C   1 
ATOM   6951 O  O   . GLN B 1 404 ? 1.137   -2.596  61.107  1.00 35.48  ? 404  GLN B O   1 
ATOM   6952 C  CB  . GLN B 1 404 ? 3.371   -1.950  63.407  1.00 42.26  ? 404  GLN B CB  1 
ATOM   6953 C  CG  . GLN B 1 404 ? 3.498   -1.609  64.884  1.00 49.29  ? 404  GLN B CG  1 
ATOM   6954 C  CD  . GLN B 1 404 ? 2.206   -1.057  65.452  1.00 59.46  ? 404  GLN B CD  1 
ATOM   6955 O  OE1 . GLN B 1 404 ? 1.380   -1.805  65.990  1.00 66.78  ? 404  GLN B OE1 1 
ATOM   6956 N  NE2 . GLN B 1 404 ? 2.014   0.257   65.327  1.00 66.29  ? 404  GLN B NE2 1 
ATOM   6957 N  N   . PHE B 1 405 ? 2.923   -3.966  60.942  1.00 32.24  ? 405  PHE B N   1 
ATOM   6958 C  CA  . PHE B 1 405 ? 2.712   -4.236  59.519  1.00 32.83  ? 405  PHE B CA  1 
ATOM   6959 C  C   . PHE B 1 405 ? 1.358   -4.889  59.291  1.00 33.22  ? 405  PHE B C   1 
ATOM   6960 O  O   . PHE B 1 405 ? 0.580   -4.462  58.424  1.00 32.33  ? 405  PHE B O   1 
ATOM   6961 C  CB  . PHE B 1 405 ? 3.843   -5.139  59.008  1.00 33.25  ? 405  PHE B CB  1 
ATOM   6962 C  CG  . PHE B 1 405 ? 3.855   -5.346  57.517  1.00 35.69  ? 405  PHE B CG  1 
ATOM   6963 C  CD1 . PHE B 1 405 ? 3.048   -6.312  56.928  1.00 33.77  ? 405  PHE B CD1 1 
ATOM   6964 C  CD2 . PHE B 1 405 ? 4.705   -4.600  56.703  1.00 36.36  ? 405  PHE B CD2 1 
ATOM   6965 C  CE1 . PHE B 1 405 ? 3.078   -6.522  55.539  1.00 35.55  ? 405  PHE B CE1 1 
ATOM   6966 C  CE2 . PHE B 1 405 ? 4.736   -4.798  55.313  1.00 36.92  ? 405  PHE B CE2 1 
ATOM   6967 C  CZ  . PHE B 1 405 ? 3.921   -5.757  54.731  1.00 35.90  ? 405  PHE B CZ  1 
ATOM   6968 N  N   . ALA B 1 406 ? 1.086   -5.960  60.038  1.00 31.91  ? 406  ALA B N   1 
ATOM   6969 C  CA  . ALA B 1 406 ? -0.169  -6.692  59.895  1.00 30.64  ? 406  ALA B CA  1 
ATOM   6970 C  C   . ALA B 1 406 ? -1.368  -5.790  60.159  1.00 34.33  ? 406  ALA B C   1 
ATOM   6971 O  O   . ALA B 1 406 ? -2.360  -5.826  59.418  1.00 31.35  ? 406  ALA B O   1 
ATOM   6972 C  CB  . ALA B 1 406 ? -0.183  -7.883  60.858  1.00 31.31  ? 406  ALA B CB  1 
ATOM   6973 N  N   . LEU B 1 407 ? -1.312  -4.983  61.222  1.00 32.97  ? 407  LEU B N   1 
ATOM   6974 C  CA  . LEU B 1 407 ? -2.494  -4.187  61.557  1.00 35.94  ? 407  LEU B CA  1 
ATOM   6975 C  C   . LEU B 1 407 ? -2.686  -3.027  60.585  1.00 32.63  ? 407  LEU B C   1 
ATOM   6976 O  O   . LEU B 1 407 ? -3.830  -2.663  60.271  1.00 33.88  ? 407  LEU B O   1 
ATOM   6977 C  CB  . LEU B 1 407 ? -2.409  -3.687  63.002  1.00 37.26  ? 407  LEU B CB  1 
ATOM   6978 C  CG  . LEU B 1 407 ? -2.651  -4.802  64.032  1.00 39.79  ? 407  LEU B CG  1 
ATOM   6979 C  CD1 . LEU B 1 407 ? -2.439  -4.286  65.463  1.00 45.75  ? 407  LEU B CD1 1 
ATOM   6980 C  CD2 . LEU B 1 407 ? -4.024  -5.424  63.860  1.00 41.58  ? 407  LEU B CD2 1 
ATOM   6981 N  N   . HIS B 1 408 ? -1.599  -2.451  60.063  1.00 34.91  ? 408  HIS B N   1 
ATOM   6982 C  CA  . HIS B 1 408 ? -1.774  -1.400  59.064  1.00 32.56  ? 408  HIS B CA  1 
ATOM   6983 C  C   . HIS B 1 408 ? -2.378  -1.972  57.789  1.00 31.96  ? 408  HIS B C   1 
ATOM   6984 O  O   . HIS B 1 408 ? -3.323  -1.409  57.232  1.00 31.97  ? 408  HIS B O   1 
ATOM   6985 C  CB  . HIS B 1 408 ? -0.442  -0.703  58.774  1.00 33.28  ? 408  HIS B CB  1 
ATOM   6986 C  CG  . HIS B 1 408 ? -0.590  0.548   57.964  1.00 32.42  ? 408  HIS B CG  1 
ATOM   6987 N  ND1 . HIS B 1 408 ? -0.964  1.752   58.519  1.00 33.61  ? 408  HIS B ND1 1 
ATOM   6988 C  CD2 . HIS B 1 408 ? -0.461  0.770   56.634  1.00 33.43  ? 408  HIS B CD2 1 
ATOM   6989 C  CE1 . HIS B 1 408 ? -1.035  2.670   57.569  1.00 36.04  ? 408  HIS B CE1 1 
ATOM   6990 N  NE2 . HIS B 1 408 ? -0.735  2.101   56.415  1.00 34.57  ? 408  HIS B NE2 1 
ATOM   6991 N  N   . GLU B 1 409 ? -1.864  -3.113  57.329  1.00 28.49  ? 409  GLU B N   1 
ATOM   6992 C  CA  . GLU B 1 409 ? -2.420  -3.755  56.140  1.00 30.32  ? 409  GLU B CA  1 
ATOM   6993 C  C   . GLU B 1 409 ? -3.888  -4.103  56.347  1.00 28.81  ? 409  GLU B C   1 
ATOM   6994 O  O   . GLU B 1 409 ? -4.743  -3.800  55.498  1.00 31.65  ? 409  GLU B O   1 
ATOM   6995 C  CB  . GLU B 1 409 ? -1.616  -5.016  55.816  1.00 33.29  ? 409  GLU B CB  1 
ATOM   6996 C  CG  . GLU B 1 409 ? -2.167  -5.809  54.640  1.00 31.63  ? 409  GLU B CG  1 
ATOM   6997 C  CD  . GLU B 1 409 ? -1.387  -7.092  54.391  1.00 34.23  ? 409  GLU B CD  1 
ATOM   6998 O  OE1 . GLU B 1 409 ? -0.417  -7.360  55.145  1.00 31.87  ? 409  GLU B OE1 1 
ATOM   6999 O  OE2 . GLU B 1 409 ? -1.714  -7.811  53.424  1.00 32.69  ? 409  GLU B OE2 1 
ATOM   7000 N  N   . ALA B 1 410 ? -4.191  -4.769  57.463  1.00 30.59  ? 410  ALA B N   1 
ATOM   7001 C  CA  . ALA B 1 410 ? -5.560  -5.228  57.698  1.00 33.13  ? 410  ALA B CA  1 
ATOM   7002 C  C   . ALA B 1 410 ? -6.521  -4.055  57.843  1.00 31.82  ? 410  ALA B C   1 
ATOM   7003 O  O   . ALA B 1 410 ? -7.674  -4.131  57.397  1.00 32.06  ? 410  ALA B O   1 
ATOM   7004 C  CB  . ALA B 1 410 ? -5.600  -6.123  58.943  1.00 32.15  ? 410  ALA B CB  1 
ATOM   7005 N  N   . THR B 1 411 ? -6.090  -2.984  58.510  1.00 31.19  ? 411  THR B N   1 
ATOM   7006 C  CA  . THR B 1 411 ? -6.960  -1.817  58.664  1.00 31.05  ? 411  THR B CA  1 
ATOM   7007 C  C   . THR B 1 411 ? -7.222  -1.153  57.316  1.00 31.66  ? 411  THR B C   1 
ATOM   7008 O  O   . THR B 1 411 ? -8.369  -0.831  56.977  1.00 33.89  ? 411  THR B O   1 
ATOM   7009 C  CB  . THR B 1 411 ? -6.346  -0.821  59.651  1.00 33.29  ? 411  THR B CB  1 
ATOM   7010 O  OG1 . THR B 1 411 ? -6.084  -1.485  60.898  1.00 31.67  ? 411  THR B OG1 1 
ATOM   7011 C  CG2 . THR B 1 411 ? -7.314  0.337   59.913  1.00 32.02  ? 411  THR B CG2 1 
ATOM   7012 N  N   . LEU B 1 412 ? -6.162  -0.946  56.532  1.00 31.52  ? 412  LEU B N   1 
ATOM   7013 C  CA  . LEU B 1 412 ? -6.308  -0.412  55.183  1.00 30.53  ? 412  LEU B CA  1 
ATOM   7014 C  C   . LEU B 1 412 ? -7.293  -1.239  54.382  1.00 32.53  ? 412  LEU B C   1 
ATOM   7015 O  O   . LEU B 1 412 ? -8.248  -0.711  53.794  1.00 31.96  ? 412  LEU B O   1 
ATOM   7016 C  CB  . LEU B 1 412 ? -4.942  -0.413  54.482  1.00 28.55  ? 412  LEU B CB  1 
ATOM   7017 C  CG  . LEU B 1 412 ? -5.000  -0.218  52.966  1.00 36.34  ? 412  LEU B CG  1 
ATOM   7018 C  CD1 . LEU B 1 412 ? -5.541  1.172   52.605  1.00 34.29  ? 412  LEU B CD1 1 
ATOM   7019 C  CD2 . LEU B 1 412 ? -3.622  -0.435  52.369  1.00 36.05  ? 412  LEU B CD2 1 
ATOM   7020 N  N   . VAL B 1 413 ? -7.068  -2.552  54.353  1.00 30.20  ? 413  VAL B N   1 
ATOM   7021 C  CA  . VAL B 1 413 ? -7.815  -3.419  53.448  1.00 33.09  ? 413  VAL B CA  1 
ATOM   7022 C  C   . VAL B 1 413 ? -9.264  -3.533  53.902  1.00 33.67  ? 413  VAL B C   1 
ATOM   7023 O  O   . VAL B 1 413 ? -10.192 -3.420  53.095  1.00 32.68  ? 413  VAL B O   1 
ATOM   7024 C  CB  . VAL B 1 413 ? -7.127  -4.795  53.363  1.00 34.93  ? 413  VAL B CB  1 
ATOM   7025 C  CG1 . VAL B 1 413 ? -8.024  -5.832  52.717  1.00 37.11  ? 413  VAL B CG1 1 
ATOM   7026 C  CG2 . VAL B 1 413 ? -5.786  -4.658  52.605  1.00 36.92  ? 413  VAL B CG2 1 
ATOM   7027 N  N   . LEU B 1 414 ? -9.483  -3.758  55.199  1.00 31.44  ? 414  LEU B N   1 
ATOM   7028 C  CA  . LEU B 1 414 ? -10.853 -3.832  55.701  1.00 31.62  ? 414  LEU B CA  1 
ATOM   7029 C  C   . LEU B 1 414 ? -11.571 -2.493  55.522  1.00 33.22  ? 414  LEU B C   1 
ATOM   7030 O  O   . LEU B 1 414 ? -12.764 -2.457  55.194  1.00 32.44  ? 414  LEU B O   1 
ATOM   7031 C  CB  . LEU B 1 414 ? -10.856 -4.255  57.173  1.00 34.27  ? 414  LEU B CB  1 
ATOM   7032 C  CG  . LEU B 1 414 ? -12.192 -4.626  57.834  1.00 33.57  ? 414  LEU B CG  1 
ATOM   7033 C  CD1 . LEU B 1 414 ? -12.970 -5.613  56.968  1.00 33.59  ? 414  LEU B CD1 1 
ATOM   7034 C  CD2 . LEU B 1 414 ? -11.967 -5.198  59.243  1.00 31.34  ? 414  LEU B CD2 1 
ATOM   7035 N  N   . GLY B 1 415 ? -10.859 -1.384  55.747  1.00 32.14  ? 415  GLY B N   1 
ATOM   7036 C  CA  . GLY B 1 415 ? -11.430 -0.068  55.471  1.00 32.48  ? 415  GLY B CA  1 
ATOM   7037 C  C   . GLY B 1 415 ? -11.896 0.067   54.031  1.00 35.89  ? 415  GLY B C   1 
ATOM   7038 O  O   . GLY B 1 415 ? -13.033 0.464   53.762  1.00 32.94  ? 415  GLY B O   1 
ATOM   7039 N  N   . MET B 1 416 ? -11.031 -0.295  53.083  1.00 31.70  ? 416  MET B N   1 
ATOM   7040 C  CA  . MET B 1 416 ? -11.424 -0.211  51.683  1.00 33.67  ? 416  MET B CA  1 
ATOM   7041 C  C   . MET B 1 416 ? -12.594 -1.143  51.373  1.00 29.80  ? 416  MET B C   1 
ATOM   7042 O  O   . MET B 1 416 ? -13.523 -0.765  50.639  1.00 32.58  ? 416  MET B O   1 
ATOM   7043 C  CB  . MET B 1 416 ? -10.233 -0.518  50.782  1.00 31.77  ? 416  MET B CB  1 
ATOM   7044 C  CG  . MET B 1 416 ? -9.349  0.702   50.618  1.00 35.20  ? 416  MET B CG  1 
ATOM   7045 S  SD  . MET B 1 416 ? -7.839  0.372   49.681  1.00 38.55  ? 416  MET B SD  1 
ATOM   7046 C  CE  . MET B 1 416 ? -8.487  0.725   48.059  1.00 37.86  ? 416  MET B CE  1 
ATOM   7047 N  N   . MET B 1 417 ? -12.573 -2.370  51.915  1.00 31.77  ? 417  MET B N   1 
ATOM   7048 C  CA  . MET B 1 417 ? -13.690 -3.282  51.676  1.00 31.62  ? 417  MET B CA  1 
ATOM   7049 C  C   . MET B 1 417 ? -15.002 -2.697  52.150  1.00 35.49  ? 417  MET B C   1 
ATOM   7050 O  O   . MET B 1 417 ? -16.017 -2.783  51.444  1.00 33.25  ? 417  MET B O   1 
ATOM   7051 C  CB  . MET B 1 417 ? -13.465 -4.648  52.329  1.00 32.88  ? 417  MET B CB  1 
ATOM   7052 C  CG  . MET B 1 417 ? -12.161 -5.334  51.917  1.00 35.31  ? 417  MET B CG  1 
ATOM   7053 S  SD  . MET B 1 417 ? -11.690 -6.772  52.931  1.00 35.45  ? 417  MET B SD  1 
ATOM   7054 C  CE  . MET B 1 417 ? -13.259 -7.472  53.435  1.00 36.66  ? 417  MET B CE  1 
ATOM   7055 N  N   . LEU B 1 418 ? -15.003 -2.101  53.339  1.00 33.80  ? 418  LEU B N   1 
ATOM   7056 C  CA  . LEU B 1 418 ? -16.242 -1.556  53.886  1.00 32.30  ? 418  LEU B CA  1 
ATOM   7057 C  C   . LEU B 1 418 ? -16.659 -0.283  53.173  1.00 34.11  ? 418  LEU B C   1 
ATOM   7058 O  O   . LEU B 1 418 ? -17.852 0.058   53.146  1.00 35.62  ? 418  LEU B O   1 
ATOM   7059 C  CB  . LEU B 1 418 ? -16.063 -1.289  55.377  1.00 32.16  ? 418  LEU B CB  1 
ATOM   7060 C  CG  . LEU B 1 418 ? -15.849 -2.569  56.180  1.00 36.22  ? 418  LEU B CG  1 
ATOM   7061 C  CD1 . LEU B 1 418 ? -15.717 -2.215  57.641  1.00 38.24  ? 418  LEU B CD1 1 
ATOM   7062 C  CD2 . LEU B 1 418 ? -16.999 -3.549  55.971  1.00 38.12  ? 418  LEU B CD2 1 
ATOM   7063 N  N   . LYS B 1 419 ? -15.692 0.455   52.638  1.00 32.84  ? 419  LYS B N   1 
ATOM   7064 C  CA  . LYS B 1 419 ? -16.011 1.634   51.839  1.00 31.71  ? 419  LYS B CA  1 
ATOM   7065 C  C   . LYS B 1 419 ? -16.725 1.252   50.547  1.00 35.86  ? 419  LYS B C   1 
ATOM   7066 O  O   . LYS B 1 419 ? -17.697 1.906   50.150  1.00 34.81  ? 419  LYS B O   1 
ATOM   7067 C  CB  . LYS B 1 419 ? -14.730 2.414   51.519  1.00 32.10  ? 419  LYS B CB  1 
ATOM   7068 C  CG  . LYS B 1 419 ? -14.923 3.597   50.543  1.00 31.79  ? 419  LYS B CG  1 
ATOM   7069 C  CD  . LYS B 1 419 ? -13.586 4.291   50.235  1.00 34.22  ? 419  LYS B CD  1 
ATOM   7070 C  CE  . LYS B 1 419 ? -13.743 5.389   49.180  1.00 35.40  ? 419  LYS B CE  1 
ATOM   7071 N  NZ  . LYS B 1 419 ? -12.459 6.086   48.911  1.00 35.48  ? 419  LYS B NZ  1 
ATOM   7072 N  N   . HIS B 1 420 ? -16.260 0.197   49.874  1.00 32.59  ? 420  HIS B N   1 
ATOM   7073 C  CA  . HIS B 1 420 ? -16.653 -0.038  48.491  1.00 32.88  ? 420  HIS B CA  1 
ATOM   7074 C  C   . HIS B 1 420 ? -17.800 -1.028  48.306  1.00 32.51  ? 420  HIS B C   1 
ATOM   7075 O  O   . HIS B 1 420 ? -18.360 -1.087  47.199  1.00 33.65  ? 420  HIS B O   1 
ATOM   7076 C  CB  . HIS B 1 420 ? -15.433 -0.504  47.694  1.00 34.13  ? 420  HIS B CB  1 
ATOM   7077 C  CG  . HIS B 1 420 ? -14.494 0.614   47.365  1.00 35.88  ? 420  HIS B CG  1 
ATOM   7078 N  ND1 . HIS B 1 420 ? -14.741 1.511   46.344  1.00 36.37  ? 420  HIS B ND1 1 
ATOM   7079 C  CD2 . HIS B 1 420 ? -13.338 1.013   47.947  1.00 34.78  ? 420  HIS B CD2 1 
ATOM   7080 C  CE1 . HIS B 1 420 ? -13.762 2.399   46.295  1.00 36.93  ? 420  HIS B CE1 1 
ATOM   7081 N  NE2 . HIS B 1 420 ? -12.902 2.126   47.263  1.00 35.81  ? 420  HIS B NE2 1 
ATOM   7082 N  N   . PHE B 1 421 ? -18.160 -1.803  49.328  1.00 32.39  ? 421  PHE B N   1 
ATOM   7083 C  CA  . PHE B 1 421 ? -19.155 -2.861  49.171  1.00 34.86  ? 421  PHE B CA  1 
ATOM   7084 C  C   . PHE B 1 421 ? -20.046 -2.963  50.400  1.00 36.07  ? 421  PHE B C   1 
ATOM   7085 O  O   . PHE B 1 421 ? -19.610 -2.715  51.524  1.00 34.37  ? 421  PHE B O   1 
ATOM   7086 C  CB  . PHE B 1 421 ? -18.501 -4.239  48.944  1.00 34.21  ? 421  PHE B CB  1 
ATOM   7087 C  CG  . PHE B 1 421 ? -17.515 -4.262  47.811  1.00 36.22  ? 421  PHE B CG  1 
ATOM   7088 C  CD1 . PHE B 1 421 ? -17.944 -4.453  46.510  1.00 34.91  ? 421  PHE B CD1 1 
ATOM   7089 C  CD2 . PHE B 1 421 ? -16.163 -4.074  48.051  1.00 32.36  ? 421  PHE B CD2 1 
ATOM   7090 C  CE1 . PHE B 1 421 ? -17.038 -4.459  45.451  1.00 34.92  ? 421  PHE B CE1 1 
ATOM   7091 C  CE2 . PHE B 1 421 ? -15.233 -4.076  46.999  1.00 30.53  ? 421  PHE B CE2 1 
ATOM   7092 C  CZ  . PHE B 1 421 ? -15.673 -4.272  45.697  1.00 33.68  ? 421  PHE B CZ  1 
ATOM   7093 N  N   . ASP B 1 422 ? -21.301 -3.359  50.169  1.00 34.53  ? 422  ASP B N   1 
ATOM   7094 C  CA  . ASP B 1 422 ? -22.113 -3.976  51.213  1.00 34.51  ? 422  ASP B CA  1 
ATOM   7095 C  C   . ASP B 1 422 ? -21.927 -5.489  51.125  1.00 38.08  ? 422  ASP B C   1 
ATOM   7096 O  O   . ASP B 1 422 ? -21.761 -6.041  50.035  1.00 40.25  ? 422  ASP B O   1 
ATOM   7097 C  CB  . ASP B 1 422 ? -23.592 -3.608  51.057  1.00 40.18  ? 422  ASP B CB  1 
ATOM   7098 C  CG  . ASP B 1 422 ? -23.863 -2.148  51.353  1.00 41.08  ? 422  ASP B CG  1 
ATOM   7099 O  OD1 . ASP B 1 422 ? -23.662 -1.734  52.510  1.00 42.36  ? 422  ASP B OD1 1 
ATOM   7100 O  OD2 . ASP B 1 422 ? -24.253 -1.412  50.427  1.00 47.70  ? 422  ASP B OD2 1 
ATOM   7101 N  N   . PHE B 1 423 ? -21.950 -6.165  52.265  1.00 36.24  ? 423  PHE B N   1 
ATOM   7102 C  CA  . PHE B 1 423 ? -21.673 -7.592  52.293  1.00 33.29  ? 423  PHE B CA  1 
ATOM   7103 C  C   . PHE B 1 423 ? -22.881 -8.361  52.788  1.00 37.89  ? 423  PHE B C   1 
ATOM   7104 O  O   . PHE B 1 423 ? -23.588 -7.905  53.697  1.00 37.45  ? 423  PHE B O   1 
ATOM   7105 C  CB  . PHE B 1 423 ? -20.449 -7.895  53.166  1.00 35.70  ? 423  PHE B CB  1 
ATOM   7106 C  CG  . PHE B 1 423 ? -19.173 -7.355  52.596  1.00 36.06  ? 423  PHE B CG  1 
ATOM   7107 C  CD1 . PHE B 1 423 ? -18.471 -8.081  51.644  1.00 35.46  ? 423  PHE B CD1 1 
ATOM   7108 C  CD2 . PHE B 1 423 ? -18.698 -6.108  52.977  1.00 35.58  ? 423  PHE B CD2 1 
ATOM   7109 C  CE1 . PHE B 1 423 ? -17.298 -7.569  51.090  1.00 36.16  ? 423  PHE B CE1 1 
ATOM   7110 C  CE2 . PHE B 1 423 ? -17.532 -5.598  52.437  1.00 37.23  ? 423  PHE B CE2 1 
ATOM   7111 C  CZ  . PHE B 1 423 ? -16.834 -6.323  51.487  1.00 36.71  ? 423  PHE B CZ  1 
ATOM   7112 N  N   . GLU B 1 424 ? -23.109 -9.522  52.174  1.00 36.24  ? 424  GLU B N   1 
ATOM   7113 C  CA  . GLU B 1 424 ? -24.228 -10.399 52.495  1.00 35.13  ? 424  GLU B CA  1 
ATOM   7114 C  C   . GLU B 1 424 ? -23.719 -11.797 52.829  1.00 37.08  ? 424  GLU B C   1 
ATOM   7115 O  O   . GLU B 1 424 ? -22.993 -12.407 52.037  1.00 37.67  ? 424  GLU B O   1 
ATOM   7116 C  CB  . GLU B 1 424 ? -25.228 -10.477 51.331  1.00 35.72  ? 424  GLU B CB  1 
ATOM   7117 C  CG  . GLU B 1 424 ? -26.389 -11.424 51.624  1.00 43.88  ? 424  GLU B CG  1 
ATOM   7118 C  CD  . GLU B 1 424 ? -27.245 -11.718 50.404  1.00 47.41  ? 424  GLU B CD  1 
ATOM   7119 O  OE1 . GLU B 1 424 ? -26.909 -11.241 49.298  1.00 48.17  ? 424  GLU B OE1 1 
ATOM   7120 O  OE2 . GLU B 1 424 ? -28.263 -12.420 50.561  1.00 49.85  ? 424  GLU B OE2 1 
ATOM   7121 N  N   . ASP B 1 425 ? -24.113 -12.297 54.002  1.00 33.88  ? 425  ASP B N   1 
ATOM   7122 C  CA  . ASP B 1 425 ? -23.867 -13.679 54.417  1.00 36.01  ? 425  ASP B CA  1 
ATOM   7123 C  C   . ASP B 1 425 ? -24.964 -14.552 53.800  1.00 34.86  ? 425  ASP B C   1 
ATOM   7124 O  O   . ASP B 1 425 ? -25.887 -15.037 54.460  1.00 34.59  ? 425  ASP B O   1 
ATOM   7125 C  CB  . ASP B 1 425 ? -23.825 -13.744 55.941  1.00 36.03  ? 425  ASP B CB  1 
ATOM   7126 C  CG  . ASP B 1 425 ? -23.718 -15.155 56.494  1.00 33.59  ? 425  ASP B CG  1 
ATOM   7127 O  OD1 . ASP B 1 425 ? -23.189 -16.071 55.822  1.00 33.23  ? 425  ASP B OD1 1 
ATOM   7128 O  OD2 . ASP B 1 425 ? -24.171 -15.335 57.642  1.00 37.03  ? 425  ASP B OD2 1 
ATOM   7129 N  N   . HIS B 1 426 ? -24.858 -14.740 52.484  1.00 35.66  ? 426  HIS B N   1 
ATOM   7130 C  CA  . HIS B 1 426 ? -25.982 -15.297 51.734  1.00 37.45  ? 426  HIS B CA  1 
ATOM   7131 C  C   . HIS B 1 426 ? -26.220 -16.777 52.028  1.00 40.08  ? 426  HIS B C   1 
ATOM   7132 O  O   . HIS B 1 426 ? -27.330 -17.263 51.795  1.00 38.03  ? 426  HIS B O   1 
ATOM   7133 C  CB  . HIS B 1 426 ? -25.777 -15.083 50.229  1.00 38.75  ? 426  HIS B CB  1 
ATOM   7134 C  CG  . HIS B 1 426 ? -24.594 -15.808 49.677  1.00 36.03  ? 426  HIS B CG  1 
ATOM   7135 N  ND1 . HIS B 1 426 ? -23.299 -15.532 50.072  1.00 37.08  ? 426  HIS B ND1 1 
ATOM   7136 C  CD2 . HIS B 1 426 ? -24.510 -16.825 48.790  1.00 39.48  ? 426  HIS B CD2 1 
ATOM   7137 C  CE1 . HIS B 1 426 ? -22.470 -16.341 49.438  1.00 41.11  ? 426  HIS B CE1 1 
ATOM   7138 N  NE2 . HIS B 1 426 ? -23.178 -17.129 48.648  1.00 39.76  ? 426  HIS B NE2 1 
ATOM   7139 N  N   . THR B 1 427 ? -25.224 -17.506 52.541  1.00 36.13  ? 427  THR B N   1 
ATOM   7140 C  CA  . THR B 1 427 ? -25.412 -18.911 52.896  1.00 35.58  ? 427  THR B CA  1 
ATOM   7141 C  C   . THR B 1 427 ? -25.709 -19.130 54.377  1.00 33.58  ? 427  THR B C   1 
ATOM   7142 O  O   . THR B 1 427 ? -25.903 -20.273 54.790  1.00 36.90  ? 427  THR B O   1 
ATOM   7143 C  CB  . THR B 1 427 ? -24.183 -19.745 52.498  1.00 38.43  ? 427  THR B CB  1 
ATOM   7144 O  OG1 . THR B 1 427 ? -23.076 -19.460 53.378  1.00 37.50  ? 427  THR B OG1 1 
ATOM   7145 C  CG2 . THR B 1 427 ? -23.796 -19.475 51.036  1.00 35.45  ? 427  THR B CG2 1 
ATOM   7146 N  N   . ASN B 1 428 ? -25.795 -18.072 55.170  1.00 34.15  ? 428  ASN B N   1 
ATOM   7147 C  CA  . ASN B 1 428 ? -25.823 -18.189 56.621  1.00 35.10  ? 428  ASN B CA  1 
ATOM   7148 C  C   . ASN B 1 428 ? -24.716 -19.133 57.083  1.00 36.86  ? 428  ASN B C   1 
ATOM   7149 O  O   . ASN B 1 428 ? -24.936 -20.181 57.698  1.00 36.90  ? 428  ASN B O   1 
ATOM   7150 C  CB  . ASN B 1 428 ? -27.201 -18.640 57.127  1.00 38.88  ? 428  ASN B CB  1 
ATOM   7151 C  CG  . ASN B 1 428 ? -27.266 -18.649 58.624  1.00 46.43  ? 428  ASN B CG  1 
ATOM   7152 O  OD1 . ASN B 1 428 ? -26.610 -17.836 59.276  1.00 46.72  ? 428  ASN B OD1 1 
ATOM   7153 N  ND2 . ASN B 1 428 ? -28.075 -19.542 59.189  1.00 55.96  ? 428  ASN B ND2 1 
ATOM   7154 N  N   . TYR B 1 429 ? -23.497 -18.725 56.757  1.00 32.55  ? 429  TYR B N   1 
ATOM   7155 C  CA  . TYR B 1 429 ? -22.333 -19.582 56.924  1.00 34.17  ? 429  TYR B CA  1 
ATOM   7156 C  C   . TYR B 1 429 ? -22.142 -20.026 58.374  1.00 34.34  ? 429  TYR B C   1 
ATOM   7157 O  O   . TYR B 1 429 ? -22.211 -19.220 59.308  1.00 34.34  ? 429  TYR B O   1 
ATOM   7158 C  CB  . TYR B 1 429 ? -21.107 -18.821 56.420  1.00 32.54  ? 429  TYR B CB  1 
ATOM   7159 C  CG  . TYR B 1 429 ? -19.767 -19.413 56.829  1.00 32.11  ? 429  TYR B CG  1 
ATOM   7160 C  CD1 . TYR B 1 429 ? -19.289 -20.570 56.232  1.00 34.18  ? 429  TYR B CD1 1 
ATOM   7161 C  CD2 . TYR B 1 429 ? -18.989 -18.806 57.821  1.00 33.03  ? 429  TYR B CD2 1 
ATOM   7162 C  CE1 . TYR B 1 429 ? -18.050 -21.116 56.605  1.00 31.31  ? 429  TYR B CE1 1 
ATOM   7163 C  CE2 . TYR B 1 429 ? -17.773 -19.340 58.200  1.00 34.74  ? 429  TYR B CE2 1 
ATOM   7164 C  CZ  . TYR B 1 429 ? -17.306 -20.491 57.580  1.00 32.91  ? 429  TYR B CZ  1 
ATOM   7165 O  OH  . TYR B 1 429 ? -16.082 -21.027 57.960  1.00 32.88  ? 429  TYR B OH  1 
ATOM   7166 N  N   . GLU B 1 430 ? -21.877 -21.317 58.567  1.00 31.63  ? 430  GLU B N   1 
ATOM   7167 C  CA  . GLU B 1 430 ? -21.579 -21.848 59.890  1.00 35.27  ? 430  GLU B CA  1 
ATOM   7168 C  C   . GLU B 1 430 ? -20.069 -21.884 60.071  1.00 35.23  ? 430  GLU B C   1 
ATOM   7169 O  O   . GLU B 1 430 ? -19.368 -22.546 59.302  1.00 34.38  ? 430  GLU B O   1 
ATOM   7170 C  CB  . GLU B 1 430 ? -22.163 -23.247 60.067  1.00 42.18  ? 430  GLU B CB  1 
ATOM   7171 C  CG  . GLU B 1 430 ? -22.050 -23.757 61.484  1.00 45.76  ? 430  GLU B CG  1 
ATOM   7172 C  CD  . GLU B 1 430 ? -22.420 -25.220 61.581  1.00 62.24  ? 430  GLU B CD  1 
ATOM   7173 O  OE1 . GLU B 1 430 ? -23.382 -25.626 60.891  1.00 65.79  ? 430  GLU B OE1 1 
ATOM   7174 O  OE2 . GLU B 1 430 ? -21.762 -25.955 62.351  1.00 70.03  ? 430  GLU B OE2 1 
ATOM   7175 N  N   . LEU B 1 431 ? -19.576 -21.195 61.093  1.00 33.42  ? 431  LEU B N   1 
ATOM   7176 C  CA  . LEU B 1 431 ? -18.137 -21.091 61.274  1.00 34.05  ? 431  LEU B CA  1 
ATOM   7177 C  C   . LEU B 1 431 ? -17.507 -22.477 61.333  1.00 35.76  ? 431  LEU B C   1 
ATOM   7178 O  O   . LEU B 1 431 ? -17.952 -23.353 62.083  1.00 36.75  ? 431  LEU B O   1 
ATOM   7179 C  CB  . LEU B 1 431 ? -17.820 -20.290 62.541  1.00 36.66  ? 431  LEU B CB  1 
ATOM   7180 C  CG  . LEU B 1 431 ? -16.341 -20.012 62.844  1.00 37.72  ? 431  LEU B CG  1 
ATOM   7181 C  CD1 . LEU B 1 431 ? -15.697 -19.340 61.645  1.00 35.56  ? 431  LEU B CD1 1 
ATOM   7182 C  CD2 . LEU B 1 431 ? -16.199 -19.149 64.104  1.00 37.07  ? 431  LEU B CD2 1 
ATOM   7183 N  N   . ASP B 1 432 ? -16.464 -22.663 60.527  1.00 34.46  ? 432  ASP B N   1 
ATOM   7184 C  CA  . ASP B 1 432 ? -15.697 -23.901 60.448  1.00 34.51  ? 432  ASP B CA  1 
ATOM   7185 C  C   . ASP B 1 432 ? -14.236 -23.469 60.422  1.00 32.31  ? 432  ASP B C   1 
ATOM   7186 O  O   . ASP B 1 432 ? -13.782 -22.875 59.436  1.00 32.44  ? 432  ASP B O   1 
ATOM   7187 C  CB  . ASP B 1 432 ? -16.094 -24.690 59.195  1.00 34.60  ? 432  ASP B CB  1 
ATOM   7188 C  CG  . ASP B 1 432 ? -15.365 -26.001 59.048  1.00 40.99  ? 432  ASP B CG  1 
ATOM   7189 O  OD1 . ASP B 1 432 ? -14.574 -26.375 59.934  1.00 39.30  ? 432  ASP B OD1 1 
ATOM   7190 O  OD2 . ASP B 1 432 ? -15.597 -26.672 58.018  1.00 40.76  ? 432  ASP B OD2 1 
ATOM   7191 N  N   . ILE B 1 433 ? -13.523 -23.705 61.514  1.00 32.73  ? 433  ILE B N   1 
ATOM   7192 C  CA  . ILE B 1 433 ? -12.175 -23.163 61.673  1.00 31.43  ? 433  ILE B CA  1 
ATOM   7193 C  C   . ILE B 1 433 ? -11.179 -24.245 61.289  1.00 35.18  ? 433  ILE B C   1 
ATOM   7194 O  O   . ILE B 1 433 ? -11.022 -25.236 62.011  1.00 34.61  ? 433  ILE B O   1 
ATOM   7195 C  CB  . ILE B 1 433 ? -11.933 -22.657 63.100  1.00 32.82  ? 433  ILE B CB  1 
ATOM   7196 C  CG1 . ILE B 1 433 ? -12.873 -21.491 63.410  1.00 32.33  ? 433  ILE B CG1 1 
ATOM   7197 C  CG2 . ILE B 1 433 ? -10.478 -22.179 63.219  1.00 31.68  ? 433  ILE B CG2 1 
ATOM   7198 C  CD1 . ILE B 1 433 ? -12.852 -21.055 64.864  1.00 33.37  ? 433  ILE B CD1 1 
ATOM   7199 N  N   . LYS B 1 434 ? -10.505 -24.054 60.145  1.00 30.90  ? 434  LYS B N   1 
ATOM   7200 C  CA  . LYS B 1 434 ? -9.472  -24.978 59.692  1.00 34.48  ? 434  LYS B CA  1 
ATOM   7201 C  C   . LYS B 1 434 ? -8.186  -24.720 60.459  1.00 33.40  ? 434  LYS B C   1 
ATOM   7202 O  O   . LYS B 1 434 ? -7.808  -23.568 60.683  1.00 33.90  ? 434  LYS B O   1 
ATOM   7203 C  CB  . LYS B 1 434 ? -9.214  -24.812 58.194  1.00 34.35  ? 434  LYS B CB  1 
ATOM   7204 C  CG  . LYS B 1 434 ? -8.201  -25.785 57.613  1.00 36.03  ? 434  LYS B CG  1 
ATOM   7205 C  CD  . LYS B 1 434 ? -8.068  -25.557 56.104  1.00 41.70  ? 434  LYS B CD  1 
ATOM   7206 C  CE  . LYS B 1 434 ? -6.964  -26.422 55.488  1.00 49.44  ? 434  LYS B CE  1 
ATOM   7207 N  NZ  . LYS B 1 434 ? -7.182  -27.874 55.780  1.00 50.09  ? 434  LYS B NZ  1 
ATOM   7208 N  N   . GLU B 1 435 ? -7.512  -25.795 60.856  1.00 31.58  ? 435  GLU B N   1 
ATOM   7209 C  CA  . GLU B 1 435 ? -6.287  -25.684 61.635  1.00 32.62  ? 435  GLU B CA  1 
ATOM   7210 C  C   . GLU B 1 435 ? -5.112  -26.152 60.797  1.00 33.70  ? 435  GLU B C   1 
ATOM   7211 O  O   . GLU B 1 435 ? -5.157  -27.249 60.228  1.00 33.18  ? 435  GLU B O   1 
ATOM   7212 C  CB  . GLU B 1 435 ? -6.385  -26.498 62.925  1.00 31.75  ? 435  GLU B CB  1 
ATOM   7213 C  CG  . GLU B 1 435 ? -7.501  -25.975 63.836  1.00 30.82  ? 435  GLU B CG  1 
ATOM   7214 C  CD  . GLU B 1 435 ? -7.293  -26.311 65.298  1.00 35.50  ? 435  GLU B CD  1 
ATOM   7215 O  OE1 . GLU B 1 435 ? -6.140  -26.609 65.697  1.00 32.40  ? 435  GLU B OE1 1 
ATOM   7216 O  OE2 . GLU B 1 435 ? -8.295  -26.267 66.049  1.00 30.82  ? 435  GLU B OE2 1 
ATOM   7217 N  N   . THR B 1 436 ? -4.081  -25.303 60.714  1.00 31.33  ? 436  THR B N   1 
ATOM   7218 C  CA  . THR B 1 436 ? -2.802  -25.590 60.053  1.00 32.30  ? 436  THR B CA  1 
ATOM   7219 C  C   . THR B 1 436 ? -1.680  -25.059 60.941  1.00 31.41  ? 436  THR B C   1 
ATOM   7220 O  O   . THR B 1 436 ? -0.792  -24.323 60.500  1.00 34.46  ? 436  THR B O   1 
ATOM   7221 C  CB  . THR B 1 436 ? -2.729  -24.972 58.654  1.00 31.91  ? 436  THR B CB  1 
ATOM   7222 O  OG1 . THR B 1 436 ? -2.964  -23.561 58.737  1.00 33.12  ? 436  THR B OG1 1 
ATOM   7223 C  CG2 . THR B 1 436 ? -3.781  -25.609 57.711  1.00 29.14  ? 436  THR B CG2 1 
ATOM   7224 N  N   . LEU B 1 437 ? -1.754  -25.421 62.222  1.00 32.19  ? 437  LEU B N   1 
ATOM   7225 C  CA  . LEU B 1 437 ? -1.092  -24.749 63.334  1.00 32.79  ? 437  LEU B CA  1 
ATOM   7226 C  C   . LEU B 1 437 ? -1.766  -23.396 63.557  1.00 33.19  ? 437  LEU B C   1 
ATOM   7227 O  O   . LEU B 1 437 ? -2.289  -23.122 64.646  1.00 32.07  ? 437  LEU B O   1 
ATOM   7228 C  CB  . LEU B 1 437 ? 0.418   -24.603 63.084  1.00 32.45  ? 437  LEU B CB  1 
ATOM   7229 C  CG  . LEU B 1 437 ? 1.204   -25.894 62.784  1.00 32.18  ? 437  LEU B CG  1 
ATOM   7230 C  CD1 . LEU B 1 437 ? 2.680   -25.543 62.609  1.00 31.53  ? 437  LEU B CD1 1 
ATOM   7231 C  CD2 . LEU B 1 437 ? 1.010   -26.976 63.872  1.00 31.05  ? 437  LEU B CD2 1 
ATOM   7232 N  N   . THR B 1 438 ? -1.794  -22.568 62.517  1.00 31.98  ? 438  THR B N   1 
ATOM   7233 C  CA  . THR B 1 438 ? -2.588  -21.344 62.509  1.00 31.46  ? 438  THR B CA  1 
ATOM   7234 C  C   . THR B 1 438 ? -4.070  -21.672 62.296  1.00 28.74  ? 438  THR B C   1 
ATOM   7235 O  O   . THR B 1 438 ? -4.436  -22.796 61.962  1.00 32.64  ? 438  THR B O   1 
ATOM   7236 C  CB  . THR B 1 438 ? -2.109  -20.417 61.401  1.00 34.22  ? 438  THR B CB  1 
ATOM   7237 O  OG1 . THR B 1 438 ? -2.134  -21.133 60.165  1.00 32.08  ? 438  THR B OG1 1 
ATOM   7238 C  CG2 . THR B 1 438 ? -0.676  -19.961 61.676  1.00 31.36  ? 438  THR B CG2 1 
ATOM   7239 N  N   . LEU B 1 439 ? -4.925  -20.664 62.490  1.00 32.46  ? 439  LEU B N   1 
ATOM   7240 C  CA  . LEU B 1 439 ? -6.376  -20.821 62.424  1.00 30.92  ? 439  LEU B CA  1 
ATOM   7241 C  C   . LEU B 1 439 ? -6.948  -19.928 61.340  1.00 31.51  ? 439  LEU B C   1 
ATOM   7242 O  O   . LEU B 1 439 ? -6.530  -18.769 61.191  1.00 32.32  ? 439  LEU B O   1 
ATOM   7243 C  CB  . LEU B 1 439 ? -7.031  -20.447 63.745  1.00 31.17  ? 439  LEU B CB  1 
ATOM   7244 C  CG  . LEU B 1 439 ? -6.492  -21.076 65.033  1.00 31.73  ? 439  LEU B CG  1 
ATOM   7245 C  CD1 . LEU B 1 439 ? -7.280  -20.567 66.216  1.00 31.49  ? 439  LEU B CD1 1 
ATOM   7246 C  CD2 . LEU B 1 439 ? -6.582  -22.584 64.936  1.00 32.28  ? 439  LEU B CD2 1 
ATOM   7247 N  N   . LYS B 1 440 ? -7.951  -20.449 60.619  1.00 31.22  ? 440  LYS B N   1 
ATOM   7248 C  CA  . LYS B 1 440 ? -8.592  -19.647 59.591  1.00 31.03  ? 440  LYS B CA  1 
ATOM   7249 C  C   . LYS B 1 440 ? -9.960  -20.241 59.278  1.00 31.94  ? 440  LYS B C   1 
ATOM   7250 O  O   . LYS B 1 440 ? -10.078 -21.474 59.234  1.00 31.99  ? 440  LYS B O   1 
ATOM   7251 C  CB  . LYS B 1 440 ? -7.707  -19.604 58.326  1.00 32.19  ? 440  LYS B CB  1 
ATOM   7252 C  CG  . LYS B 1 440 ? -8.105  -18.530 57.325  1.00 33.06  ? 440  LYS B CG  1 
ATOM   7253 C  CD  . LYS B 1 440 ? -7.247  -18.559 56.046  1.00 35.34  ? 440  LYS B CD  1 
ATOM   7254 C  CE  . LYS B 1 440 ? -5.767  -18.460 56.334  1.00 40.77  ? 440  LYS B CE  1 
ATOM   7255 N  NZ  . LYS B 1 440 ? -5.104  -19.810 56.252  1.00 42.98  ? 440  LYS B NZ  1 
ATOM   7256 N  N   . PRO B 1 441 ? -11.002 -19.429 59.054  1.00 33.28  ? 441  PRO B N   1 
ATOM   7257 C  CA  . PRO B 1 441 ? -12.257 -19.999 58.541  1.00 32.15  ? 441  PRO B CA  1 
ATOM   7258 C  C   . PRO B 1 441 ? -12.031 -20.762 57.244  1.00 33.08  ? 441  PRO B C   1 
ATOM   7259 O  O   . PRO B 1 441 ? -11.259 -20.345 56.375  1.00 30.93  ? 441  PRO B O   1 
ATOM   7260 C  CB  . PRO B 1 441 ? -13.145 -18.771 58.309  1.00 32.64  ? 441  PRO B CB  1 
ATOM   7261 C  CG  . PRO B 1 441 ? -12.621 -17.739 59.220  1.00 31.49  ? 441  PRO B CG  1 
ATOM   7262 C  CD  . PRO B 1 441 ? -11.101 -17.970 59.193  1.00 31.35  ? 441  PRO B CD  1 
ATOM   7263 N  N   . GLU B 1 442 ? -12.747 -21.876 57.107  1.00 31.72  ? 442  GLU B N   1 
ATOM   7264 C  CA  . GLU B 1 442 ? -12.836 -22.641 55.871  1.00 31.33  ? 442  GLU B CA  1 
ATOM   7265 C  C   . GLU B 1 442 ? -14.226 -22.519 55.260  1.00 33.10  ? 442  GLU B C   1 
ATOM   7266 O  O   . GLU B 1 442 ? -15.226 -22.587 55.976  1.00 33.83  ? 442  GLU B O   1 
ATOM   7267 C  CB  . GLU B 1 442 ? -12.559 -24.125 56.135  1.00 35.80  ? 442  GLU B CB  1 
ATOM   7268 C  CG  . GLU B 1 442 ? -12.476 -24.931 54.867  1.00 41.51  ? 442  GLU B CG  1 
ATOM   7269 C  CD  . GLU B 1 442 ? -11.767 -26.247 55.064  1.00 45.78  ? 442  GLU B CD  1 
ATOM   7270 O  OE1 . GLU B 1 442 ? -11.764 -26.762 56.197  1.00 42.93  ? 442  GLU B OE1 1 
ATOM   7271 O  OE2 . GLU B 1 442 ? -11.221 -26.765 54.074  1.00 55.87  ? 442  GLU B OE2 1 
ATOM   7272 N  N   . GLY B 1 443 ? -14.290 -22.392 53.935  1.00 33.16  ? 443  GLY B N   1 
ATOM   7273 C  CA  . GLY B 1 443 ? -15.586 -22.432 53.278  1.00 34.57  ? 443  GLY B CA  1 
ATOM   7274 C  C   . GLY B 1 443 ? -16.419 -21.188 53.473  1.00 38.11  ? 443  GLY B C   1 
ATOM   7275 O  O   . GLY B 1 443 ? -17.609 -21.193 53.137  1.00 35.99  ? 443  GLY B O   1 
ATOM   7276 N  N   . PHE B 1 444 ? -15.832 -20.135 54.022  1.00 35.76  ? 444  PHE B N   1 
ATOM   7277 C  CA  . PHE B 1 444 ? -16.537 -18.880 54.246  1.00 36.95  ? 444  PHE B CA  1 
ATOM   7278 C  C   . PHE B 1 444 ? -16.678 -18.143 52.920  1.00 35.33  ? 444  PHE B C   1 
ATOM   7279 O  O   . PHE B 1 444 ? -15.682 -17.859 52.247  1.00 32.78  ? 444  PHE B O   1 
ATOM   7280 C  CB  . PHE B 1 444 ? -15.761 -18.052 55.269  1.00 35.54  ? 444  PHE B CB  1 
ATOM   7281 C  CG  . PHE B 1 444 ? -16.369 -16.717 55.585  1.00 32.45  ? 444  PHE B CG  1 
ATOM   7282 C  CD1 . PHE B 1 444 ? -17.748 -16.535 55.599  1.00 32.60  ? 444  PHE B CD1 1 
ATOM   7283 C  CD2 . PHE B 1 444 ? -15.551 -15.630 55.865  1.00 31.21  ? 444  PHE B CD2 1 
ATOM   7284 C  CE1 . PHE B 1 444 ? -18.288 -15.282 55.895  1.00 34.09  ? 444  PHE B CE1 1 
ATOM   7285 C  CE2 . PHE B 1 444 ? -16.072 -14.394 56.157  1.00 31.84  ? 444  PHE B CE2 1 
ATOM   7286 C  CZ  . PHE B 1 444 ? -17.459 -14.219 56.179  1.00 33.17  ? 444  PHE B CZ  1 
ATOM   7287 N  N   . VAL B 1 445 ? -17.920 -17.887 52.516  1.00 34.34  ? 445  VAL B N   1 
ATOM   7288 C  CA  . VAL B 1 445 ? -18.241 -17.169 51.301  1.00 31.87  ? 445  VAL B CA  1 
ATOM   7289 C  C   . VAL B 1 445 ? -19.249 -16.078 51.637  1.00 34.40  ? 445  VAL B C   1 
ATOM   7290 O  O   . VAL B 1 445 ? -20.056 -16.217 52.562  1.00 34.15  ? 445  VAL B O   1 
ATOM   7291 C  CB  . VAL B 1 445 ? -18.805 -18.110 50.206  1.00 33.77  ? 445  VAL B CB  1 
ATOM   7292 C  CG1 . VAL B 1 445 ? -17.732 -19.069 49.714  1.00 34.65  ? 445  VAL B CG1 1 
ATOM   7293 C  CG2 . VAL B 1 445 ? -19.991 -18.894 50.755  1.00 35.88  ? 445  VAL B CG2 1 
ATOM   7294 N  N   . VAL B 1 446 ? -19.211 -14.996 50.856  1.00 31.84  ? 446  VAL B N   1 
ATOM   7295 C  CA  . VAL B 1 446 ? -20.138 -13.879 50.987  1.00 35.63  ? 446  VAL B CA  1 
ATOM   7296 C  C   . VAL B 1 446 ? -20.443 -13.354 49.591  1.00 36.53  ? 446  VAL B C   1 
ATOM   7297 O  O   . VAL B 1 446 ? -19.747 -13.659 48.617  1.00 35.14  ? 446  VAL B O   1 
ATOM   7298 C  CB  . VAL B 1 446 ? -19.582 -12.732 51.866  1.00 34.10  ? 446  VAL B CB  1 
ATOM   7299 C  CG1 . VAL B 1 446 ? -19.297 -13.215 53.294  1.00 35.81  ? 446  VAL B CG1 1 
ATOM   7300 C  CG2 . VAL B 1 446 ? -18.339 -12.074 51.223  1.00 30.45  ? 446  VAL B CG2 1 
ATOM   7301 N  N   . LYS B 1 447 ? -21.497 -12.548 49.499  1.00 33.35  ? 447  LYS B N   1 
ATOM   7302 C  CA  . LYS B 1 447 ? -21.739 -11.748 48.310  1.00 32.26  ? 447  LYS B CA  1 
ATOM   7303 C  C   . LYS B 1 447 ? -21.476 -10.283 48.627  1.00 35.84  ? 447  LYS B C   1 
ATOM   7304 O  O   . LYS B 1 447 ? -21.808 -9.795  49.719  1.00 36.12  ? 447  LYS B O   1 
ATOM   7305 C  CB  . LYS B 1 447 ? -23.170 -11.935 47.778  1.00 35.40  ? 447  LYS B CB  1 
ATOM   7306 C  CG  . LYS B 1 447 ? -23.423 -13.308 47.192  1.00 38.92  ? 447  LYS B CG  1 
ATOM   7307 C  CD  . LYS B 1 447 ? -24.846 -13.420 46.610  1.00 40.15  ? 447  LYS B CD  1 
ATOM   7308 C  CE  . LYS B 1 447 ? -25.014 -14.716 45.840  1.00 44.76  ? 447  LYS B CE  1 
ATOM   7309 N  NZ  . LYS B 1 447 ? -26.446 -14.880 45.436  1.00 49.12  ? 447  LYS B NZ  1 
ATOM   7310 N  N   . ALA B 1 448 ? -20.858 -9.591  47.681  1.00 34.96  ? 448  ALA B N   1 
ATOM   7311 C  CA  . ALA B 1 448 ? -20.558 -8.178  47.819  1.00 38.14  ? 448  ALA B CA  1 
ATOM   7312 C  C   . ALA B 1 448 ? -21.404 -7.408  46.824  1.00 46.02  ? 448  ALA B C   1 
ATOM   7313 O  O   . ALA B 1 448 ? -21.432 -7.741  45.634  1.00 53.30  ? 448  ALA B O   1 
ATOM   7314 C  CB  . ALA B 1 448 ? -19.066 -7.898  47.597  1.00 39.37  ? 448  ALA B CB  1 
ATOM   7315 N  N   . LYS B 1 449 ? -22.121 -6.415  47.314  1.00 41.53  ? 449  LYS B N   1 
ATOM   7316 C  CA  . LYS B 1 449 ? -22.861 -5.497  46.460  1.00 44.57  ? 449  LYS B CA  1 
ATOM   7317 C  C   . LYS B 1 449 ? -22.080 -4.192  46.412  1.00 37.33  ? 449  LYS B C   1 
ATOM   7318 O  O   . LYS B 1 449 ? -21.935 -3.515  47.432  1.00 38.02  ? 449  LYS B O   1 
ATOM   7319 C  CB  . LYS B 1 449 ? -24.274 -5.283  46.996  1.00 48.22  ? 449  LYS B CB  1 
ATOM   7320 C  CG  . LYS B 1 449 ? -25.318 -5.011  45.922  1.00 55.84  ? 449  LYS B CG  1 
ATOM   7321 C  CD  . LYS B 1 449 ? -26.477 -4.202  46.491  1.00 60.88  ? 449  LYS B CD  1 
ATOM   7322 C  CE  . LYS B 1 449 ? -27.181 -3.389  45.410  1.00 63.03  ? 449  LYS B CE  1 
ATOM   7323 N  NZ  . LYS B 1 449 ? -27.908 -2.222  45.993  1.00 70.52  ? 449  LYS B NZ  1 
ATOM   7324 N  N   . SER B 1 450 ? -21.578 -3.848  45.232  1.00 37.17  ? 450  SER B N   1 
ATOM   7325 C  CA  . SER B 1 450 ? -20.782 -2.639  45.064  1.00 37.11  ? 450  SER B CA  1 
ATOM   7326 C  C   . SER B 1 450 ? -21.577 -1.390  45.412  1.00 40.24  ? 450  SER B C   1 
ATOM   7327 O  O   . SER B 1 450 ? -22.731 -1.234  45.003  1.00 40.12  ? 450  SER B O   1 
ATOM   7328 C  CB  . SER B 1 450 ? -20.294 -2.529  43.621  1.00 38.67  ? 450  SER B CB  1 
ATOM   7329 O  OG  . SER B 1 450 ? -19.596 -1.311  43.429  1.00 37.49  ? 450  SER B OG  1 
ATOM   7330 N  N   . LYS B 1 451 ? -20.949 -0.492  46.162  1.00 36.52  ? 451  LYS B N   1 
ATOM   7331 C  CA  . LYS B 1 451 ? -21.493 0.845   46.370  1.00 38.79  ? 451  LYS B CA  1 
ATOM   7332 C  C   . LYS B 1 451 ? -21.150 1.786   45.221  1.00 43.05  ? 451  LYS B C   1 
ATOM   7333 O  O   . LYS B 1 451 ? -21.475 2.977   45.290  1.00 41.59  ? 451  LYS B O   1 
ATOM   7334 C  CB  . LYS B 1 451 ? -20.986 1.417   47.696  1.00 41.43  ? 451  LYS B CB  1 
ATOM   7335 C  CG  . LYS B 1 451 ? -21.376 0.562   48.893  1.00 37.54  ? 451  LYS B CG  1 
ATOM   7336 C  CD  . LYS B 1 451 ? -20.742 1.072   50.180  1.00 41.68  ? 451  LYS B CD  1 
ATOM   7337 C  CE  . LYS B 1 451 ? -21.514 0.603   51.391  1.00 46.91  ? 451  LYS B CE  1 
ATOM   7338 N  NZ  . LYS B 1 451 ? -22.756 1.387   51.578  1.00 52.93  ? 451  LYS B NZ  1 
ATOM   7339 N  N   . LYS B 1 452 ? -20.488 1.284   44.178  1.00 39.61  ? 452  LYS B N   1 
ATOM   7340 C  CA  . LYS B 1 452 ? -20.196 2.065   42.974  1.00 43.44  ? 452  LYS B CA  1 
ATOM   7341 C  C   . LYS B 1 452 ? -19.440 3.353   43.299  1.00 45.04  ? 452  LYS B C   1 
ATOM   7342 O  O   . LYS B 1 452 ? -19.779 4.444   42.831  1.00 44.52  ? 452  LYS B O   1 
ATOM   7343 C  CB  . LYS B 1 452 ? -21.485 2.358   42.195  1.00 43.71  ? 452  LYS B CB  1 
ATOM   7344 C  CG  . LYS B 1 452 ? -22.220 1.102   41.730  1.00 46.90  ? 452  LYS B CG  1 
ATOM   7345 C  CD  . LYS B 1 452 ? -21.381 0.255   40.767  1.00 50.81  ? 452  LYS B CD  1 
ATOM   7346 C  CE  . LYS B 1 452 ? -22.128 -1.016  40.352  1.00 51.75  ? 452  LYS B CE  1 
ATOM   7347 N  NZ  . LYS B 1 452 ? -21.291 -1.954  39.537  1.00 55.40  ? 452  LYS B NZ  1 
ATOM   7348 N  N   . ILE B 1 453 ? -18.380 3.218   44.085  1.00 40.89  ? 453  ILE B N   1 
ATOM   7349 C  CA  . ILE B 1 453 ? -17.504 4.331   44.431  1.00 40.33  ? 453  ILE B CA  1 
ATOM   7350 C  C   . ILE B 1 453 ? -16.215 4.180   43.631  1.00 42.46  ? 453  ILE B C   1 
ATOM   7351 O  O   . ILE B 1 453 ? -15.524 3.158   43.769  1.00 42.41  ? 453  ILE B O   1 
ATOM   7352 C  CB  . ILE B 1 453 ? -17.210 4.374   45.939  1.00 41.37  ? 453  ILE B CB  1 
ATOM   7353 C  CG1 . ILE B 1 453 ? -18.517 4.502   46.716  1.00 44.19  ? 453  ILE B CG1 1 
ATOM   7354 C  CG2 . ILE B 1 453 ? -16.285 5.546   46.259  1.00 40.26  ? 453  ILE B CG2 1 
ATOM   7355 C  CD1 . ILE B 1 453 ? -18.336 4.390   48.200  1.00 46.21  ? 453  ILE B CD1 1 
ATOM   7356 N  N   . PRO B 1 454 ? -15.851 5.155   42.798  1.00 44.95  ? 454  PRO B N   1 
ATOM   7357 C  CA  . PRO B 1 454 ? -14.699 4.975   41.909  1.00 44.80  ? 454  PRO B CA  1 
ATOM   7358 C  C   . PRO B 1 454 ? -13.392 4.876   42.674  1.00 45.51  ? 454  PRO B C   1 
ATOM   7359 O  O   . PRO B 1 454 ? -13.231 5.444   43.759  1.00 46.43  ? 454  PRO B O   1 
ATOM   7360 C  CB  . PRO B 1 454 ? -14.725 6.236   41.034  1.00 47.60  ? 454  PRO B CB  1 
ATOM   7361 C  CG  . PRO B 1 454 ? -16.123 6.734   41.123  1.00 48.89  ? 454  PRO B CG  1 
ATOM   7362 C  CD  . PRO B 1 454 ? -16.592 6.392   42.500  1.00 49.36  ? 454  PRO B CD  1 
ATOM   7363 N  N   . LEU B 1 455 ? -12.452 4.141   42.081  1.00 41.56  ? 455  LEU B N   1 
ATOM   7364 C  CA  . LEU B 1 455 ? -11.070 4.070   42.557  1.00 43.47  ? 455  LEU B CA  1 
ATOM   7365 C  C   . LEU B 1 455 ? -10.180 5.061   41.819  1.00 46.77  ? 455  LEU B C   1 
ATOM   7366 O  O   . LEU B 1 455 ? -10.628 5.798   40.939  1.00 48.48  ? 455  LEU B O   1 
ATOM   7367 C  CB  . LEU B 1 455 ? -10.502 2.659   42.369  1.00 44.82  ? 455  LEU B CB  1 
ATOM   7368 C  CG  . LEU B 1 455 ? -11.018 1.568   43.296  1.00 42.38  ? 455  LEU B CG  1 
ATOM   7369 C  CD1 . LEU B 1 455 ? -10.671 0.184   42.709  1.00 40.22  ? 455  LEU B CD1 1 
ATOM   7370 C  CD2 . LEU B 1 455 ? -10.424 1.751   44.674  1.00 42.32  ? 455  LEU B CD2 1 
ATOM   7371 O  OXT . LEU B 1 455 ? -8.977  5.122   42.078  1.00 46.17  ? 455  LEU B OXT 1 
HETATM 7372 C  CHA . HEM C 2 .   ? -17.877 -14.011 8.934   1.00 32.81  ? 501  HEM A CHA 1 
HETATM 7373 C  CHB . HEM C 2 .   ? -13.070 -13.415 9.251   1.00 32.64  ? 501  HEM A CHB 1 
HETATM 7374 C  CHC . HEM C 2 .   ? -13.640 -11.063 13.539  1.00 27.48  ? 501  HEM A CHC 1 
HETATM 7375 C  CHD . HEM C 2 .   ? -18.407 -12.004 13.353  1.00 33.01  ? 501  HEM A CHD 1 
HETATM 7376 C  C1A . HEM C 2 .   ? -16.526 -14.025 8.666   1.00 28.89  ? 501  HEM A C1A 1 
HETATM 7377 C  C2A . HEM C 2 .   ? -15.961 -14.574 7.478   1.00 31.34  ? 501  HEM A C2A 1 
HETATM 7378 C  C3A . HEM C 2 .   ? -14.617 -14.421 7.582   1.00 31.03  ? 501  HEM A C3A 1 
HETATM 7379 C  C4A . HEM C 2 .   ? -14.340 -13.756 8.795   1.00 30.32  ? 501  HEM A C4A 1 
HETATM 7380 C  CMA . HEM C 2 .   ? -13.577 -14.834 6.564   1.00 32.33  ? 501  HEM A CMA 1 
HETATM 7381 C  CAA . HEM C 2 .   ? -16.673 -15.212 6.302   1.00 30.37  ? 501  HEM A CAA 1 
HETATM 7382 C  CBA . HEM C 2 .   ? -16.897 -16.716 6.549   1.00 29.07  ? 501  HEM A CBA 1 
HETATM 7383 C  CGA . HEM C 2 .   ? -17.487 -17.448 5.365   1.00 30.40  ? 501  HEM A CGA 1 
HETATM 7384 O  O1A . HEM C 2 .   ? -17.757 -18.661 5.502   1.00 32.17  ? 501  HEM A O1A 1 
HETATM 7385 O  O2A . HEM C 2 .   ? -17.709 -16.892 4.262   1.00 29.67  ? 501  HEM A O2A 1 
HETATM 7386 C  C1B . HEM C 2 .   ? -12.847 -12.711 10.449  1.00 32.37  ? 501  HEM A C1B 1 
HETATM 7387 C  C2B . HEM C 2 .   ? -11.547 -12.338 10.903  1.00 32.08  ? 501  HEM A C2B 1 
HETATM 7388 C  C3B . HEM C 2 .   ? -11.700 -11.675 12.088  1.00 29.62  ? 501  HEM A C3B 1 
HETATM 7389 C  C4B . HEM C 2 .   ? -13.143 -11.655 12.377  1.00 29.91  ? 501  HEM A C4B 1 
HETATM 7390 C  CMB . HEM C 2 .   ? -10.215 -12.600 10.191  1.00 30.04  ? 501  HEM A CMB 1 
HETATM 7391 C  CAB . HEM C 2 .   ? -10.705 -11.070 13.002  1.00 32.93  ? 501  HEM A CAB 1 
HETATM 7392 C  CBB . HEM C 2 .   ? -9.583  -10.495 12.551  1.00 35.40  ? 501  HEM A CBB 1 
HETATM 7393 C  C1C . HEM C 2 .   ? -15.005 -11.097 13.861  1.00 26.69  ? 501  HEM A C1C 1 
HETATM 7394 C  C2C . HEM C 2 .   ? -15.591 -10.524 15.014  1.00 30.57  ? 501  HEM A C2C 1 
HETATM 7395 C  C3C . HEM C 2 .   ? -16.948 -10.818 14.965  1.00 29.32  ? 501  HEM A C3C 1 
HETATM 7396 C  C4C . HEM C 2 .   ? -17.179 -11.530 13.746  1.00 31.26  ? 501  HEM A C4C 1 
HETATM 7397 C  CMC . HEM C 2 .   ? -14.839 -9.796  16.088  1.00 31.23  ? 501  HEM A CMC 1 
HETATM 7398 C  CAC . HEM C 2 .   ? -18.014 -10.436 15.925  1.00 29.10  ? 501  HEM A CAC 1 
HETATM 7399 C  CBC . HEM C 2 .   ? -17.951 -9.320  16.643  1.00 32.47  ? 501  HEM A CBC 1 
HETATM 7400 C  C1D . HEM C 2 .   ? -18.587 -12.644 12.121  1.00 31.74  ? 501  HEM A C1D 1 
HETATM 7401 C  C2D . HEM C 2 .   ? -19.916 -13.107 11.716  1.00 30.21  ? 501  HEM A C2D 1 
HETATM 7402 C  C3D . HEM C 2 .   ? -19.780 -13.650 10.491  1.00 30.31  ? 501  HEM A C3D 1 
HETATM 7403 C  C4D . HEM C 2 .   ? -18.346 -13.524 10.148  1.00 29.68  ? 501  HEM A C4D 1 
HETATM 7404 C  CMD . HEM C 2 .   ? -21.217 -12.965 12.503  1.00 30.84  ? 501  HEM A CMD 1 
HETATM 7405 C  CAD . HEM C 2 .   ? -20.904 -14.201 9.634   1.00 30.96  ? 501  HEM A CAD 1 
HETATM 7406 C  CBD . HEM C 2 .   ? -21.448 -12.998 8.818   1.00 30.45  ? 501  HEM A CBD 1 
HETATM 7407 C  CGD . HEM C 2 .   ? -22.654 -13.287 7.939   1.00 32.42  ? 501  HEM A CGD 1 
HETATM 7408 O  O1D . HEM C 2 .   ? -22.566 -14.151 7.038   1.00 32.39  ? 501  HEM A O1D 1 
HETATM 7409 O  O2D . HEM C 2 .   ? -23.731 -12.645 8.076   1.00 35.53  ? 501  HEM A O2D 1 
HETATM 7410 N  NA  . HEM C 2 .   ? -15.517 -13.522 9.468   1.00 31.88  ? 501  HEM A NA  1 
HETATM 7411 N  NB  . HEM C 2 .   ? -13.746 -12.312 11.372  1.00 28.67  ? 501  HEM A NB  1 
HETATM 7412 N  NC  . HEM C 2 .   ? -15.969 -11.711 13.113  1.00 30.32  ? 501  HEM A NC  1 
HETATM 7413 N  ND  . HEM C 2 .   ? -17.685 -12.934 11.161  1.00 27.19  ? 501  HEM A ND  1 
HETATM 7414 FE FE  . HEM C 2 .   ? -15.801 -12.584 11.223  1.00 32.17  ? 501  HEM A FE  1 
HETATM 7415 C  C1  . D0L D 3 .   ? -13.021 -30.676 1.720   1.00 40.44  ? 502  D0L A C1  1 
HETATM 7416 C  C2  . D0L D 3 .   ? -13.007 -30.831 3.106   1.00 38.19  ? 502  D0L A C2  1 
HETATM 7417 C  C15 . D0L D 3 .   ? -11.599 -24.550 6.293   1.00 36.92  ? 502  D0L A C15 1 
HETATM 7418 C  C14 . D0L D 3 .   ? -10.428 -25.878 7.962   1.00 37.12  ? 502  D0L A C14 1 
HETATM 7419 C  C7  . D0L D 3 .   ? -12.282 -29.845 4.005   1.00 37.59  ? 502  D0L A C7  1 
HETATM 7420 C  C12 . D0L D 3 .   ? -9.303  -27.396 6.462   1.00 37.14  ? 502  D0L A C12 1 
HETATM 7421 C  C10 . D0L D 3 .   ? -10.926 -27.054 4.580   1.00 34.87  ? 502  D0L A C10 1 
HETATM 7422 C  C3  . D0L D 3 .   ? -13.653 -31.933 3.665   1.00 35.38  ? 502  D0L A C3  1 
HETATM 7423 C  C13 . D0L D 3 .   ? -9.675  -27.203 7.932   1.00 34.52  ? 502  D0L A C13 1 
HETATM 7424 C  C11 . D0L D 3 .   ? -10.203 -26.405 5.718   1.00 35.07  ? 502  D0L A C11 1 
HETATM 7425 C  C6  . D0L D 3 .   ? -13.682 -31.597 0.907   1.00 41.45  ? 502  D0L A C6  1 
HETATM 7426 C  C8  . D0L D 3 .   ? -12.867 -28.427 3.948   1.00 36.09  ? 502  D0L A C8  1 
HETATM 7427 C  C5  . D0L D 3 .   ? -14.324 -32.699 1.470   1.00 42.36  ? 502  D0L A C5  1 
HETATM 7428 C  C9  . D0L D 3 .   ? -14.285 -28.436 4.428   1.00 35.66  ? 502  D0L A C9  1 
HETATM 7429 C  C4  . D0L D 3 .   ? -14.307 -32.861 2.855   1.00 43.95  ? 502  D0L A C4  1 
HETATM 7430 O  O2  . D0L D 3 .   ? -14.473 -28.164 5.638   1.00 36.13  ? 502  D0L A O2  1 
HETATM 7431 O  O3  . D0L D 3 .   ? -10.417 -27.068 3.466   1.00 37.84  ? 502  D0L A O3  1 
HETATM 7432 O  O1  . D0L D 3 .   ? -15.212 -28.706 3.640   1.00 34.11  ? 502  D0L A O1  1 
HETATM 7433 N  N2  . D0L D 3 .   ? -11.171 -25.898 6.705   1.00 38.28  ? 502  D0L A N2  1 
HETATM 7434 C  C16 . D0L D 3 .   ? -12.742 -24.040 7.163   1.00 40.56  ? 502  D0L A C16 1 
HETATM 7435 C  C17 . D0L D 3 .   ? -12.301 -22.761 7.865   1.00 39.65  ? 502  D0L A C17 1 
HETATM 7436 C  C18 . D0L D 3 .   ? -13.419 -22.218 8.762   1.00 38.94  ? 502  D0L A C18 1 
HETATM 7437 C  C19 . D0L D 3 .   ? -12.877 -21.091 9.633   1.00 36.15  ? 502  D0L A C19 1 
HETATM 7438 C  C20 . D0L D 3 .   ? -13.965 -20.427 10.487  1.00 36.93  ? 502  D0L A C20 1 
HETATM 7439 C  C21 . D0L D 3 .   ? -14.687 -21.418 11.386  1.00 39.94  ? 502  D0L A C21 1 
HETATM 7440 N  N1  . D0L D 3 .   ? -12.115 -27.585 4.859   1.00 33.33  ? 502  D0L A N1  1 
HETATM 7441 C  CAF . SYN E 4 .   ? -16.305 -20.666 14.841  0.90 38.70  ? 503  SYN A CAF 1 
HETATM 7442 C  CAD . SYN E 4 .   ? -14.930 -20.512 14.892  0.90 42.49  ? 503  SYN A CAD 1 
HETATM 7443 C  CAC . SYN E 4 .   ? -14.337 -19.375 14.387  0.90 39.15  ? 503  SYN A CAC 1 
HETATM 7444 C  CAE . SYN E 4 .   ? -15.112 -18.391 13.821  0.90 34.52  ? 503  SYN A CAE 1 
HETATM 7445 C  CAG . SYN E 4 .   ? -16.487 -18.539 13.771  0.90 35.64  ? 503  SYN A CAG 1 
HETATM 7446 C  CAH . SYN E 4 .   ? -17.112 -19.675 14.282  0.90 36.58  ? 503  SYN A CAH 1 
HETATM 7447 C  CAB . SYN E 4 .   ? -18.578 -19.821 14.232  0.90 41.28  ? 503  SYN A CAB 1 
HETATM 7448 C  CAA . SYN E 4 .   ? -19.313 -20.601 14.969  0.90 41.65  ? 503  SYN A CAA 1 
HETATM 7449 O  O1  . OXY F 5 .   ? -15.274 -14.215 12.204  0.74 35.14  ? 504  OXY A O1  1 
HETATM 7450 O  O2  . OXY F 5 .   ? -14.521 -14.635 13.132  0.74 26.44  ? 504  OXY A O2  1 
HETATM 7451 C  C1  . GOL G 6 .   ? -30.207 -25.694 13.369  1.00 49.36  ? 505  GOL A C1  1 
HETATM 7452 O  O1  . GOL G 6 .   ? -29.150 -26.240 12.642  1.00 51.12  ? 505  GOL A O1  1 
HETATM 7453 C  C2  . GOL G 6 .   ? -31.195 -25.041 12.351  1.00 54.48  ? 505  GOL A C2  1 
HETATM 7454 O  O2  . GOL G 6 .   ? -31.846 -25.932 11.537  1.00 56.83  ? 505  GOL A O2  1 
HETATM 7455 C  C3  . GOL G 6 .   ? -32.146 -24.284 13.295  1.00 54.25  ? 505  GOL A C3  1 
HETATM 7456 O  O3  . GOL G 6 .   ? -33.434 -24.464 12.795  1.00 63.63  ? 505  GOL A O3  1 
HETATM 7457 H  H11 . GOL G 6 .   ? -29.913 -25.021 14.003  1.00 59.26  ? 505  GOL A H11 1 
HETATM 7458 H  H12 . GOL G 6 .   ? -30.682 -26.360 13.890  1.00 59.26  ? 505  GOL A H12 1 
HETATM 7459 H  HO1 . GOL G 6 .   ? -29.437 -26.337 11.854  1.00 61.37  ? 505  GOL A HO1 1 
HETATM 7460 H  H2  . GOL G 6 .   ? -30.730 -24.469 11.720  1.00 65.40  ? 505  GOL A H2  1 
HETATM 7461 H  HO2 . GOL G 6 .   ? -31.781 -26.688 11.888  1.00 68.21  ? 505  GOL A HO2 1 
HETATM 7462 H  H31 . GOL G 6 .   ? -31.875 -23.354 13.335  1.00 65.12  ? 505  GOL A H31 1 
HETATM 7463 H  H32 . GOL G 6 .   ? -32.032 -24.625 14.196  1.00 65.12  ? 505  GOL A H32 1 
HETATM 7464 H  HO3 . GOL G 6 .   ? -33.395 -24.261 11.970  1.00 76.38  ? 505  GOL A HO3 1 
HETATM 7465 C  C1  . GOL H 6 .   ? -6.836  1.413   12.224  1.00 50.42  ? 506  GOL A C1  1 
HETATM 7466 O  O1  . GOL H 6 .   ? -7.072  0.041   12.096  1.00 44.87  ? 506  GOL A O1  1 
HETATM 7467 C  C2  . GOL H 6 .   ? -8.189  2.120   12.552  1.00 56.07  ? 506  GOL A C2  1 
HETATM 7468 O  O2  . GOL H 6 .   ? -7.994  3.325   13.196  1.00 57.27  ? 506  GOL A O2  1 
HETATM 7469 C  C3  . GOL H 6 .   ? -8.833  2.245   11.162  1.00 59.93  ? 506  GOL A C3  1 
HETATM 7470 O  O3  . GOL H 6 .   ? -9.914  3.097   11.300  1.00 67.15  ? 506  GOL A O3  1 
HETATM 7471 H  H11 . GOL H 6 .   ? -6.468  1.800   11.414  1.00 60.53  ? 506  GOL A H11 1 
HETATM 7472 H  H12 . GOL H 6 .   ? -6.199  1.613   12.927  1.00 60.53  ? 506  GOL A H12 1 
HETATM 7473 H  HO1 . GOL H 6 .   ? -6.346  -0.304  11.794  1.00 53.86  ? 506  GOL A HO1 1 
HETATM 7474 H  H2  . GOL H 6 .   ? -8.749  1.614   13.161  1.00 67.30  ? 506  GOL A H2  1 
HETATM 7475 H  HO2 . GOL H 6 .   ? -7.263  3.641   12.926  1.00 68.75  ? 506  GOL A HO2 1 
HETATM 7476 H  H31 . GOL H 6 .   ? -9.077  1.360   10.848  1.00 71.94  ? 506  GOL A H31 1 
HETATM 7477 H  H32 . GOL H 6 .   ? -8.167  2.566   10.534  1.00 71.94  ? 506  GOL A H32 1 
HETATM 7478 H  HO3 . GOL H 6 .   ? -10.254 2.918   12.058  1.00 80.60  ? 506  GOL A HO3 1 
HETATM 7479 C  C1  . GOL I 6 .   ? -28.346 -15.527 -2.882  1.00 47.91  ? 507  GOL A C1  1 
HETATM 7480 O  O1  . GOL I 6 .   ? -27.440 -15.912 -3.905  1.00 44.53  ? 507  GOL A O1  1 
HETATM 7481 C  C2  . GOL I 6 .   ? -29.660 -16.308 -3.152  1.00 54.58  ? 507  GOL A C2  1 
HETATM 7482 O  O2  . GOL I 6 .   ? -29.940 -16.335 -4.503  1.00 56.22  ? 507  GOL A O2  1 
HETATM 7483 C  C3  . GOL I 6 .   ? -29.416 -17.679 -2.534  1.00 52.80  ? 507  GOL A C3  1 
HETATM 7484 O  O3  . GOL I 6 .   ? -30.599 -18.428 -2.732  1.00 58.54  ? 507  GOL A O3  1 
HETATM 7485 H  H11 . GOL I 6 .   ? -28.529 -14.574 -2.880  1.00 57.51  ? 507  GOL A H11 1 
HETATM 7486 H  H12 . GOL I 6 .   ? -28.021 -15.736 -1.993  1.00 57.51  ? 507  GOL A H12 1 
HETATM 7487 H  HO1 . GOL I 6 .   ? -26.756 -15.401 -3.845  1.00 53.46  ? 507  GOL A HO1 1 
HETATM 7488 H  H2  . GOL I 6 .   ? -30.433 -15.895 -2.736  1.00 65.52  ? 507  GOL A H2  1 
HETATM 7489 H  HO2 . GOL I 6 .   ? -29.700 -15.585 -4.824  1.00 67.49  ? 507  GOL A HO2 1 
HETATM 7490 H  H31 . GOL I 6 .   ? -29.183 -17.567 -1.599  1.00 63.38  ? 507  GOL A H31 1 
HETATM 7491 H  H32 . GOL I 6 .   ? -28.634 -18.077 -2.948  1.00 63.38  ? 507  GOL A H32 1 
HETATM 7492 H  HO3 . GOL I 6 .   ? -31.227 -17.986 -2.359  1.00 70.26  ? 507  GOL A HO3 1 
HETATM 7493 C  CHA . HEM J 2 .   ? 6.102   -13.905 66.096  1.00 32.70  ? 501  HEM B CHA 1 
HETATM 7494 C  CHB . HEM J 2 .   ? 1.278   -13.524 65.911  1.00 31.28  ? 501  HEM B CHB 1 
HETATM 7495 C  CHC . HEM J 2 .   ? 1.652   -11.108 61.636  1.00 32.19  ? 501  HEM B CHC 1 
HETATM 7496 C  CHD . HEM J 2 .   ? 6.460   -11.819 61.713  1.00 31.65  ? 501  HEM B CHD 1 
HETATM 7497 C  C1A . HEM J 2 .   ? 4.764   -13.984 66.409  1.00 31.16  ? 501  HEM B C1A 1 
HETATM 7498 C  C2A . HEM J 2 .   ? 4.253   -14.593 67.597  1.00 32.62  ? 501  HEM B C2A 1 
HETATM 7499 C  C3A . HEM J 2 .   ? 2.888   -14.492 67.531  1.00 28.79  ? 501  HEM B C3A 1 
HETATM 7500 C  C4A . HEM J 2 .   ? 2.565   -13.816 66.328  1.00 30.11  ? 501  HEM B C4A 1 
HETATM 7501 C  CMA . HEM J 2 .   ? 1.895   -14.972 68.557  1.00 28.72  ? 501  HEM B CMA 1 
HETATM 7502 C  CAA . HEM J 2 .   ? 5.021   -15.224 68.748  1.00 31.40  ? 501  HEM B CAA 1 
HETATM 7503 C  CBA . HEM J 2 .   ? 5.224   -16.713 68.482  1.00 29.03  ? 501  HEM B CBA 1 
HETATM 7504 C  CGA . HEM J 2 .   ? 5.923   -17.440 69.607  1.00 30.28  ? 501  HEM B CGA 1 
HETATM 7505 O  O1A . HEM J 2 .   ? 6.204   -18.642 69.411  1.00 32.03  ? 501  HEM B O1A 1 
HETATM 7506 O  O2A . HEM J 2 .   ? 6.193   -16.881 70.718  1.00 30.20  ? 501  HEM B O2A 1 
HETATM 7507 C  C1B . HEM J 2 .   ? 1.004   -12.819 64.717  1.00 30.22  ? 501  HEM B C1B 1 
HETATM 7508 C  C2B . HEM J 2 .   ? -0.325  -12.496 64.300  1.00 30.81  ? 501  HEM B C2B 1 
HETATM 7509 C  C3B . HEM J 2 .   ? -0.245  -11.813 63.126  1.00 28.94  ? 501  HEM B C3B 1 
HETATM 7510 C  C4B . HEM J 2 .   ? 1.193   -11.737 62.794  1.00 32.99  ? 501  HEM B C4B 1 
HETATM 7511 C  CMB . HEM J 2 .   ? -1.600  -12.822 65.052  1.00 30.29  ? 501  HEM B CMB 1 
HETATM 7512 C  CAB . HEM J 2 .   ? -1.315  -11.256 62.264  1.00 29.51  ? 501  HEM B CAB 1 
HETATM 7513 C  CBB . HEM J 2 .   ? -2.443  -10.741 62.766  1.00 33.47  ? 501  HEM B CBB 1 
HETATM 7514 C  C1C . HEM J 2 .   ? 3.003   -11.074 61.284  1.00 31.55  ? 501  HEM B C1C 1 
HETATM 7515 C  C2C . HEM J 2 .   ? 3.537   -10.459 60.137  1.00 31.69  ? 501  HEM B C2C 1 
HETATM 7516 C  C3C . HEM J 2 .   ? 4.907   -10.689 60.148  1.00 29.03  ? 501  HEM B C3C 1 
HETATM 7517 C  C4C . HEM J 2 .   ? 5.197   -11.396 61.357  1.00 31.11  ? 501  HEM B C4C 1 
HETATM 7518 C  CMC . HEM J 2 .   ? 2.725   -9.745  59.079  1.00 31.36  ? 501  HEM B CMC 1 
HETATM 7519 C  CAC . HEM J 2 .   ? 5.946   -10.246 59.179  1.00 28.89  ? 501  HEM B CAC 1 
HETATM 7520 C  CBC . HEM J 2 .   ? 5.846   -9.155  58.409  1.00 33.26  ? 501  HEM B CBC 1 
HETATM 7521 C  C1D . HEM J 2 .   ? 6.705   -12.463 62.929  1.00 31.79  ? 501  HEM B C1D 1 
HETATM 7522 C  C2D . HEM J 2 .   ? 8.069   -12.867 63.315  1.00 29.84  ? 501  HEM B C2D 1 
HETATM 7523 C  C3D . HEM J 2 .   ? 7.963   -13.432 64.545  1.00 29.00  ? 501  HEM B C3D 1 
HETATM 7524 C  C4D . HEM J 2 .   ? 6.532   -13.380 64.896  1.00 31.27  ? 501  HEM B C4D 1 
HETATM 7525 C  CMD . HEM J 2 .   ? 9.350   -12.636 62.519  1.00 33.29  ? 501  HEM B CMD 1 
HETATM 7526 C  CAD . HEM J 2 .   ? 9.109   -13.942 65.407  1.00 30.63  ? 501  HEM B CAD 1 
HETATM 7527 C  CBD . HEM J 2 .   ? 9.623   -12.749 66.242  1.00 32.24  ? 501  HEM B CBD 1 
HETATM 7528 C  CGD . HEM J 2 .   ? 10.849  -13.116 67.068  1.00 33.31  ? 501  HEM B CGD 1 
HETATM 7529 O  O1D . HEM J 2 .   ? 10.804  -14.039 67.902  1.00 31.90  ? 501  HEM B O1D 1 
HETATM 7530 O  O2D . HEM J 2 .   ? 11.928  -12.508 66.899  1.00 34.61  ? 501  HEM B O2D 1 
HETATM 7531 N  NA  . HEM J 2 .   ? 3.710   -13.508 65.635  1.00 31.29  ? 501  HEM B NA  1 
HETATM 7532 N  NB  . HEM J 2 .   ? 1.839   -12.366 63.778  1.00 29.18  ? 501  HEM B NB  1 
HETATM 7533 N  NC  . HEM J 2 .   ? 4.007   -11.647 62.011  1.00 32.50  ? 501  HEM B NC  1 
HETATM 7534 N  ND  . HEM J 2 .   ? 5.823   -12.818 63.892  1.00 26.65  ? 501  HEM B ND  1 
HETATM 7535 FE FE  . HEM J 2 .   ? 3.903   -12.565 63.882  1.00 32.12  ? 501  HEM B FE  1 
HETATM 7536 C  C1  . D0L K 3 .   ? 1.987   -31.033 73.206  1.00 37.66  ? 502  D0L B C1  1 
HETATM 7537 C  C2  . D0L K 3 .   ? 1.978   -31.180 71.826  1.00 36.64  ? 502  D0L B C2  1 
HETATM 7538 C  C15 . D0L K 3 .   ? 0.335   -24.745 68.908  1.00 34.25  ? 502  D0L B C15 1 
HETATM 7539 C  C14 . D0L K 3 .   ? -0.743  -26.020 67.167  1.00 34.24  ? 502  D0L B C14 1 
HETATM 7540 C  C7  . D0L K 3 .   ? 1.315   -30.144 70.922  1.00 34.55  ? 502  D0L B C7  1 
HETATM 7541 C  C12 . D0L K 3 .   ? -1.812  -27.704 68.583  1.00 38.85  ? 502  D0L B C12 1 
HETATM 7542 C  C10 . D0L K 3 .   ? -0.201  -27.405 70.490  1.00 31.03  ? 502  D0L B C10 1 
HETATM 7543 C  C3  . D0L K 3 .   ? 2.549   -32.324 71.263  1.00 37.56  ? 502  D0L B C3  1 
HETATM 7544 C  C13 . D0L K 3 .   ? -1.543  -27.323 67.121  1.00 35.36  ? 502  D0L B C13 1 
HETATM 7545 C  C11 . D0L K 3 .   ? -0.972  -26.729 69.395  1.00 33.27  ? 502  D0L B C11 1 
HETATM 7546 C  C6  . D0L K 3 .   ? 2.576   -31.997 74.033  1.00 37.10  ? 502  D0L B C6  1 
HETATM 7547 C  C8  . D0L K 3 .   ? 1.828   -28.707 71.029  1.00 32.20  ? 502  D0L B C8  1 
HETATM 7548 C  C5  . D0L K 3 .   ? 3.151   -33.131 73.473  1.00 36.30  ? 502  D0L B C5  1 
HETATM 7549 C  C9  . D0L K 3 .   ? 3.247   -28.675 70.534  1.00 34.14  ? 502  D0L B C9  1 
HETATM 7550 C  C4  . D0L K 3 .   ? 3.142   -33.292 72.087  1.00 37.23  ? 502  D0L B C4  1 
HETATM 7551 O  O2  . D0L K 3 .   ? 4.182   -28.976 71.315  1.00 33.03  ? 502  D0L B O2  1 
HETATM 7552 O  O3  . D0L K 3 .   ? -0.674  -27.492 71.623  1.00 32.64  ? 502  D0L B O3  1 
HETATM 7553 O  O1  . D0L K 3 .   ? 3.433   -28.364 69.335  1.00 33.06  ? 502  D0L B O1  1 
HETATM 7554 N  N2  . D0L K 3 .   ? -0.041  -26.095 68.438  1.00 34.73  ? 502  D0L B N2  1 
HETATM 7555 C  C16 . D0L K 3 .   ? 1.417   -24.140 68.019  1.00 36.72  ? 502  D0L B C16 1 
HETATM 7556 C  C17 . D0L K 3 .   ? 0.864   -22.940 67.252  1.00 34.92  ? 502  D0L B C17 1 
HETATM 7557 C  C18 . D0L K 3 .   ? 1.948   -22.251 66.425  1.00 35.06  ? 502  D0L B C18 1 
HETATM 7558 C  C19 . D0L K 3 .   ? 1.332   -21.170 65.553  1.00 37.17  ? 502  D0L B C19 1 
HETATM 7559 C  C20 . D0L K 3 .   ? 2.369   -20.447 64.703  1.00 36.23  ? 502  D0L B C20 1 
HETATM 7560 C  C21 . D0L K 3 .   ? 3.020   -21.362 63.680  1.00 41.22  ? 502  D0L B C21 1 
HETATM 7561 N  N1  . D0L K 3 .   ? 1.018   -27.858 70.163  1.00 32.49  ? 502  D0L B N1  1 
HETATM 7562 C  CAF . SYN L 4 .   ? 4.664   -18.332 61.231  0.91 36.05  ? 503  SYN B CAF 1 
HETATM 7563 C  CAD . SYN L 4 .   ? 3.281   -18.420 61.210  0.91 37.13  ? 503  SYN B CAD 1 
HETATM 7564 C  CAC . SYN L 4 .   ? 2.675   -19.552 60.711  0.91 42.70  ? 503  SYN B CAC 1 
HETATM 7565 C  CAE . SYN L 4 .   ? 3.441   -20.591 60.231  0.91 39.89  ? 503  SYN B CAE 1 
HETATM 7566 C  CAG . SYN L 4 .   ? 4.823   -20.508 60.259  0.91 39.02  ? 503  SYN B CAG 1 
HETATM 7567 C  CAH . SYN L 4 .   ? 5.460   -19.369 60.749  0.91 34.05  ? 503  SYN B CAH 1 
HETATM 7568 C  CAB . SYN L 4 .   ? 6.932   -19.269 60.767  0.91 37.55  ? 503  SYN B CAB 1 
HETATM 7569 C  CAA . SYN L 4 .   ? 7.772   -20.042 60.168  0.91 37.64  ? 503  SYN B CAA 1 
HETATM 7570 O  O1  . OXY M 5 .   ? 3.481   -14.221 62.904  0.71 36.12  ? 504  OXY B O1  1 
HETATM 7571 O  O2  . OXY M 5 .   ? 2.721   -14.656 61.993  0.71 27.83  ? 504  OXY B O2  1 
HETATM 7572 C  C1  . GOL N 6 .   ? 18.631  -17.287 76.985  1.00 47.12  ? 505  GOL B C1  1 
HETATM 7573 O  O1  . GOL N 6 .   ? 19.676  -18.124 77.418  1.00 55.06  ? 505  GOL B O1  1 
HETATM 7574 C  C2  . GOL N 6 .   ? 17.982  -16.684 78.250  1.00 52.26  ? 505  GOL B C2  1 
HETATM 7575 O  O2  . GOL N 6 .   ? 18.840  -15.879 78.973  1.00 50.85  ? 505  GOL B O2  1 
HETATM 7576 C  C3  . GOL N 6 .   ? 16.761  -15.934 77.678  1.00 46.54  ? 505  GOL B C3  1 
HETATM 7577 O  O3  . GOL N 6 .   ? 16.073  -15.414 78.771  1.00 42.16  ? 505  GOL B O3  1 
HETATM 7578 H  H11 . GOL N 6 .   ? 17.958  -17.764 76.475  1.00 56.56  ? 505  GOL B H11 1 
HETATM 7579 H  H12 . GOL N 6 .   ? 18.941  -16.570 76.410  1.00 56.56  ? 505  GOL B H12 1 
HETATM 7580 H  HO1 . GOL N 6 .   ? 20.215  -18.190 76.766  1.00 66.09  ? 505  GOL B HO1 1 
HETATM 7581 H  H2  . GOL N 6 .   ? 17.725  -17.369 78.887  1.00 62.73  ? 505  GOL B H2  1 
HETATM 7582 H  HO2 . GOL N 6 .   ? 19.011  -15.202 78.513  1.00 61.05  ? 505  GOL B HO2 1 
HETATM 7583 H  H31 . GOL N 6 .   ? 16.233  -16.549 77.146  1.00 55.88  ? 505  GOL B H31 1 
HETATM 7584 H  H32 . GOL N 6 .   ? 17.069  -15.256 77.056  1.00 55.88  ? 505  GOL B H32 1 
HETATM 7585 H  HO3 . GOL N 6 .   ? 15.627  -16.054 79.102  1.00 50.61  ? 505  GOL B HO3 1 
HETATM 7586 C  C1  . GOL O 6 .   ? -20.650 -6.316  42.141  1.00 51.80  ? 506  GOL B C1  1 
HETATM 7587 O  O1  . GOL O 6 .   ? -21.745 -5.583  42.747  1.00 54.04  ? 506  GOL B O1  1 
HETATM 7588 C  C2  . GOL O 6 .   ? -21.273 -7.607  41.499  1.00 55.39  ? 506  GOL B C2  1 
HETATM 7589 O  O2  . GOL O 6 .   ? -21.595 -8.547  42.459  1.00 63.28  ? 506  GOL B O2  1 
HETATM 7590 C  C3  . GOL O 6 .   ? -22.474 -7.041  40.746  1.00 59.68  ? 506  GOL B C3  1 
HETATM 7591 O  O3  . GOL O 6 .   ? -22.386 -7.496  39.435  1.00 58.97  ? 506  GOL B O3  1 
HETATM 7592 H  H11 . GOL O 6 .   ? -19.970 -6.571  42.783  1.00 62.18  ? 506  GOL B H11 1 
HETATM 7593 H  H12 . GOL O 6 .   ? -20.191 -5.805  41.456  1.00 62.18  ? 506  GOL B H12 1 
HETATM 7594 H  HO1 . GOL O 6 .   ? -21.588 -4.750  42.640  1.00 64.87  ? 506  GOL B HO1 1 
HETATM 7595 H  H2  . GOL O 6 .   ? -20.668 -8.075  40.903  1.00 66.49  ? 506  GOL B H2  1 
HETATM 7596 H  HO2 . GOL O 6 .   ? -20.901 -8.641  42.947  1.00 75.96  ? 506  GOL B HO2 1 
HETATM 7597 H  H31 . GOL O 6 .   ? -22.461 -6.074  40.819  1.00 71.64  ? 506  GOL B H31 1 
HETATM 7598 H  H32 . GOL O 6 .   ? -23.286 -7.321  41.197  1.00 71.64  ? 506  GOL B H32 1 
HETATM 7599 H  HO3 . GOL O 6 .   ? -21.767 -7.047  39.056  1.00 70.79  ? 506  GOL B HO3 1 
HETATM 7600 C  C1  . GOL P 6 .   ? -11.527 -40.086 71.953  1.00 50.14  ? 507  GOL B C1  1 
HETATM 7601 O  O1  . GOL P 6 .   ? -10.990 -38.769 72.197  1.00 55.88  ? 507  GOL B O1  1 
HETATM 7602 C  C2  . GOL P 6 .   ? -12.805 -40.223 72.800  1.00 54.29  ? 507  GOL B C2  1 
HETATM 7603 O  O2  . GOL P 6 .   ? -12.475 -40.524 74.135  1.00 47.78  ? 507  GOL B O2  1 
HETATM 7604 C  C3  . GOL P 6 .   ? -13.513 -38.857 72.598  1.00 47.98  ? 507  GOL B C3  1 
HETATM 7605 O  O3  . GOL P 6 .   ? -14.001 -38.777 71.270  1.00 56.65  ? 507  GOL B O3  1 
HETATM 7606 H  H11 . GOL P 6 .   ? -10.906 -40.791 72.194  1.00 60.19  ? 507  GOL B H11 1 
HETATM 7607 H  H12 . GOL P 6 .   ? -11.745 -40.231 71.019  1.00 60.19  ? 507  GOL B H12 1 
HETATM 7608 H  HO1 . GOL P 6 .   ? -11.013 -38.635 73.050  1.00 67.08  ? 507  GOL B HO1 1 
HETATM 7609 H  H2  . GOL P 6 .   ? -13.388 -40.944 72.516  1.00 65.17  ? 507  GOL B H2  1 
HETATM 7610 H  HO2 . GOL P 6 .   ? -13.201 -40.717 74.530  1.00 57.36  ? 507  GOL B HO2 1 
HETATM 7611 H  H31 . GOL P 6 .   ? -12.880 -38.154 72.810  1.00 57.60  ? 507  GOL B H31 1 
HETATM 7612 H  H32 . GOL P 6 .   ? -14.215 -38.780 73.263  1.00 57.60  ? 507  GOL B H32 1 
HETATM 7613 H  HO3 . GOL P 6 .   ? -13.791 -39.505 70.871  1.00 68.00  ? 507  GOL B HO3 1 
HETATM 7614 C  C1  . GOL Q 6 .   ? 21.081  -24.003 61.072  1.00 56.75  ? 508  GOL B C1  1 
HETATM 7615 O  O1  . GOL Q 6 .   ? 21.874  -23.597 62.165  1.00 63.20  ? 508  GOL B O1  1 
HETATM 7616 C  C2  . GOL Q 6 .   ? 20.173  -25.127 61.613  1.00 58.71  ? 508  GOL B C2  1 
HETATM 7617 O  O2  . GOL Q 6 .   ? 20.064  -25.046 62.995  1.00 59.43  ? 508  GOL B O2  1 
HETATM 7618 C  C3  . GOL Q 6 .   ? 18.843  -24.937 60.863  1.00 52.92  ? 508  GOL B C3  1 
HETATM 7619 O  O3  . GOL Q 6 .   ? 17.875  -25.623 61.609  1.00 50.67  ? 508  GOL B O3  1 
HETATM 7620 H  H11 . GOL Q 6 .   ? 21.606  -24.337 60.327  1.00 68.12  ? 508  GOL B H11 1 
HETATM 7621 H  H12 . GOL Q 6 .   ? 20.536  -23.286 60.712  1.00 68.12  ? 508  GOL B H12 1 
HETATM 7622 H  HO1 . GOL Q 6 .   ? 21.947  -24.278 62.674  1.00 75.86  ? 508  GOL B HO1 1 
HETATM 7623 H  H2  . GOL Q 6 .   ? 20.526  -26.012 61.433  1.00 70.48  ? 508  GOL B H2  1 
HETATM 7624 H  HO2 . GOL Q 6 .   ? 19.312  -25.372 63.207  1.00 71.33  ? 508  GOL B HO2 1 
HETATM 7625 H  H31 . GOL Q 6 .   ? 18.939  -25.267 59.956  1.00 63.53  ? 508  GOL B H31 1 
HETATM 7626 H  H32 . GOL Q 6 .   ? 18.661  -23.988 60.772  1.00 63.53  ? 508  GOL B H32 1 
HETATM 7627 H  HO3 . GOL Q 6 .   ? 17.246  -25.816 61.072  1.00 60.83  ? 508  GOL B HO3 1 
HETATM 7628 C  C1  . GOL R 6 .   ? -6.019  0.350   63.365  1.00 40.74  ? 509  GOL B C1  1 
HETATM 7629 O  O1  . GOL R 6 .   ? -4.786  -0.186  63.112  1.00 52.44  ? 509  GOL B O1  1 
HETATM 7630 C  C2  . GOL R 6 .   ? -5.909  1.923   63.272  1.00 49.44  ? 509  GOL B C2  1 
HETATM 7631 O  O2  . GOL R 6 .   ? -5.762  2.512   64.520  1.00 60.74  ? 509  GOL B O2  1 
HETATM 7632 C  C3  . GOL R 6 .   ? -4.713  2.198   62.290  1.00 48.55  ? 509  GOL B C3  1 
HETATM 7633 O  O3  . GOL R 6 .   ? -3.491  2.068   63.021  1.00 57.37  ? 509  GOL B O3  1 
HETATM 7634 H  H11 . GOL R 6 .   ? -6.352  0.110   64.244  1.00 48.91  ? 509  GOL B H11 1 
HETATM 7635 H  H12 . GOL R 6 .   ? -6.690  0.044   62.734  1.00 48.91  ? 509  GOL B H12 1 
HETATM 7636 H  HO1 . GOL R 6 .   ? -4.711  -0.874  63.614  1.00 62.95  ? 509  GOL B HO1 1 
HETATM 7637 H  H2  . GOL R 6 .   ? -6.723  2.307   62.910  1.00 59.35  ? 509  GOL B H2  1 
HETATM 7638 H  HO2 . GOL R 6 .   ? -5.815  1.899   65.097  1.00 72.91  ? 509  GOL B HO2 1 
HETATM 7639 H  H31 . GOL R 6 .   ? -4.832  3.078   61.901  1.00 58.28  ? 509  GOL B H31 1 
HETATM 7640 H  H32 . GOL R 6 .   ? -4.778  1.578   61.546  1.00 58.28  ? 509  GOL B H32 1 
HETATM 7641 H  HO3 . GOL R 6 .   ? -3.674  1.667   63.752  1.00 68.87  ? 509  GOL B HO3 1 
HETATM 7642 O  O   . HOH S 7 .   ? -27.766 -23.335 -14.365 1.00 53.64  ? 601  HOH A O   1 
HETATM 7643 O  O   . HOH S 7 .   ? -8.308  12.875  24.352  1.00 60.12  ? 602  HOH A O   1 
HETATM 7644 O  O   . HOH S 7 .   ? -23.951 -9.872  8.104   1.00 43.78  ? 603  HOH A O   1 
HETATM 7645 O  O   . HOH S 7 .   ? -16.433 -6.881  6.392   1.00 43.90  ? 604  HOH A O   1 
HETATM 7646 O  O   . HOH S 7 .   ? -6.255  -11.028 -12.415 1.00 47.54  ? 605  HOH A O   1 
HETATM 7647 O  O   . HOH S 7 .   ? -16.824 -26.919 -0.906  1.00 41.61  ? 606  HOH A O   1 
HETATM 7648 O  O   . HOH S 7 .   ? -8.401  9.759   25.870  1.00 49.05  ? 607  HOH A O   1 
HETATM 7649 O  O   . HOH S 7 .   ? 10.750  -15.705 21.919  1.00 36.65  ? 608  HOH A O   1 
HETATM 7650 O  O   . HOH S 7 .   ? 6.126   -15.151 5.668   1.00 52.25  ? 609  HOH A O   1 
HETATM 7651 O  O   . HOH S 7 .   ? 8.126   -21.277 22.892  1.00 50.47  ? 610  HOH A O   1 
HETATM 7652 O  O   . HOH S 7 .   ? 5.230   -17.691 -0.627  1.00 53.26  ? 611  HOH A O   1 
HETATM 7653 O  O   . HOH S 7 .   ? -33.337 -27.597 10.453  1.00 50.71  ? 612  HOH A O   1 
HETATM 7654 O  O   . HOH S 7 .   ? 9.755   -17.983 12.722  1.00 45.32  ? 613  HOH A O   1 
HETATM 7655 O  O   . HOH S 7 .   ? -11.130 1.673   14.185  1.00 42.02  ? 614  HOH A O   1 
HETATM 7656 O  O   . HOH S 7 .   ? -10.308 -14.350 -14.499 1.00 44.89  ? 615  HOH A O   1 
HETATM 7657 O  O   . HOH S 7 .   ? -2.340  4.694   27.447  1.00 44.81  ? 616  HOH A O   1 
HETATM 7658 O  O   . HOH S 7 .   ? 6.355   -7.337  31.408  1.00 47.63  ? 617  HOH A O   1 
HETATM 7659 O  O   . HOH S 7 .   ? -21.160 8.421   15.326  1.00 58.40  ? 618  HOH A O   1 
HETATM 7660 O  O   . HOH S 7 .   ? -14.182 0.443   32.917  1.00 51.85  ? 619  HOH A O   1 
HETATM 7661 O  O   . HOH S 7 .   ? -1.633  -18.946 32.594  1.00 52.38  ? 620  HOH A O   1 
HETATM 7662 O  O   . HOH S 7 .   ? -4.902  -23.064 -14.509 1.00 51.79  ? 621  HOH A O   1 
HETATM 7663 O  O   . HOH S 7 .   ? -22.206 -17.300 -15.817 1.00 50.87  ? 622  HOH A O   1 
HETATM 7664 O  O   . HOH S 7 .   ? -11.795 -34.871 18.880  1.00 49.45  ? 623  HOH A O   1 
HETATM 7665 O  O   . HOH S 7 .   ? -35.205 -10.408 6.374   1.00 42.81  ? 624  HOH A O   1 
HETATM 7666 O  O   . HOH S 7 .   ? -32.182 -14.764 4.348   1.00 34.91  ? 625  HOH A O   1 
HETATM 7667 O  O   . HOH S 7 .   ? -21.982 -9.207  6.608   1.00 42.30  ? 626  HOH A O   1 
HETATM 7668 O  O   . HOH S 7 .   ? 8.433   -1.509  6.069   1.00 49.63  ? 627  HOH A O   1 
HETATM 7669 O  O   . HOH S 7 .   ? -17.558 -16.652 33.758  1.00 49.33  ? 628  HOH A O   1 
HETATM 7670 O  O   . HOH S 7 .   ? -13.148 -2.542  35.399  1.00 36.63  ? 629  HOH A O   1 
HETATM 7671 O  O   . HOH S 7 .   ? -10.177 -24.510 31.687  1.00 55.86  ? 630  HOH A O   1 
HETATM 7672 O  O   . HOH S 7 .   ? 2.059   9.277   24.007  1.00 49.06  ? 631  HOH A O   1 
HETATM 7673 O  O   . HOH S 7 .   ? -3.645  -14.328 -10.245 1.00 37.73  ? 632  HOH A O   1 
HETATM 7674 O  O   . HOH S 7 .   ? 4.396   1.645   30.457  1.00 40.12  ? 633  HOH A O   1 
HETATM 7675 O  O   . HOH S 7 .   ? 0.978   -26.168 16.530  1.00 47.86  ? 634  HOH A O   1 
HETATM 7676 O  O   . HOH S 7 .   ? -29.289 -18.796 -7.162  1.00 46.98  ? 635  HOH A O   1 
HETATM 7677 O  O   . HOH S 7 .   ? -7.750  -6.900  40.211  1.00 33.31  ? 636  HOH A O   1 
HETATM 7678 O  O   . HOH S 7 .   ? -26.344 -27.938 -14.347 1.00 53.65  ? 637  HOH A O   1 
HETATM 7679 O  O   . HOH S 7 .   ? -33.253 -21.388 9.621   1.00 42.28  ? 638  HOH A O   1 
HETATM 7680 O  O   . HOH S 7 .   ? 0.578   -21.885 23.018  1.00 40.82  ? 639  HOH A O   1 
HETATM 7681 O  O   . HOH S 7 .   ? 1.506   1.713   32.849  1.00 49.08  ? 640  HOH A O   1 
HETATM 7682 O  O   . HOH S 7 .   ? -13.826 -9.615  31.807  1.00 31.12  ? 641  HOH A O   1 
HETATM 7683 O  O   . HOH S 7 .   ? -13.110 -9.530  20.863  1.00 31.88  ? 642  HOH A O   1 
HETATM 7684 O  O   . HOH S 7 .   ? -19.188 -30.171 -12.778 1.00 52.32  ? 643  HOH A O   1 
HETATM 7685 O  O   . HOH S 7 .   ? -22.399 -4.015  27.356  1.00 40.17  ? 644  HOH A O   1 
HETATM 7686 O  O   . HOH S 7 .   ? 2.989   -14.080 31.751  1.00 40.75  ? 645  HOH A O   1 
HETATM 7687 O  O   . HOH S 7 .   ? -15.668 -35.172 5.758   1.00 52.61  ? 646  HOH A O   1 
HETATM 7688 O  O   . HOH S 7 .   ? -14.953 -26.920 29.770  1.00 46.98  ? 647  HOH A O   1 
HETATM 7689 O  O   . HOH S 7 .   ? 8.256   -23.079 18.018  1.00 43.59  ? 648  HOH A O   1 
HETATM 7690 O  O   . HOH S 7 .   ? 0.496   -31.143 1.691   1.00 39.67  ? 649  HOH A O   1 
HETATM 7691 O  O   . HOH S 7 .   ? -18.335 0.774   26.476  1.00 42.86  ? 650  HOH A O   1 
HETATM 7692 O  O   . HOH S 7 .   ? -6.665  -4.717  36.404  1.00 37.03  ? 651  HOH A O   1 
HETATM 7693 O  O   . HOH S 7 .   ? -9.371  12.342  21.989  1.00 47.58  ? 652  HOH A O   1 
HETATM 7694 O  O   . HOH S 7 .   ? -4.426  -0.606  6.175   1.00 44.59  ? 653  HOH A O   1 
HETATM 7695 O  O   . HOH S 7 .   ? 2.598   -16.681 -6.867  1.00 44.45  ? 654  HOH A O   1 
HETATM 7696 O  O   . HOH S 7 .   ? 4.021   -13.484 37.657  1.00 43.32  ? 655  HOH A O   1 
HETATM 7697 O  O   . HOH S 7 .   ? 6.319   -2.338  34.949  1.00 43.07  ? 656  HOH A O   1 
HETATM 7698 O  O   . HOH S 7 .   ? -5.033  -2.135  39.925  1.00 41.82  ? 657  HOH A O   1 
HETATM 7699 O  O   . HOH S 7 .   ? -33.451 -24.102 7.218   1.00 39.66  ? 658  HOH A O   1 
HETATM 7700 O  O   . HOH S 7 .   ? -13.923 -4.521  -5.349  1.00 38.69  ? 659  HOH A O   1 
HETATM 7701 O  O   . HOH S 7 .   ? -17.930 -40.648 -3.951  1.00 58.46  ? 660  HOH A O   1 
HETATM 7702 O  O   . HOH S 7 .   ? -34.624 -22.123 12.365  1.00 56.14  ? 661  HOH A O   1 
HETATM 7703 O  O   . HOH S 7 .   ? -23.656 -27.552 -3.486  1.00 55.92  ? 662  HOH A O   1 
HETATM 7704 O  O   . HOH S 7 .   ? -20.393 -15.495 6.276   1.00 30.46  ? 663  HOH A O   1 
HETATM 7705 O  O   . HOH S 7 .   ? 4.703   -18.124 5.133   1.00 48.36  ? 664  HOH A O   1 
HETATM 7706 O  O   . HOH S 7 .   ? -2.803  -27.961 14.942  1.00 37.88  ? 665  HOH A O   1 
HETATM 7707 O  O   . HOH S 7 .   ? -25.024 -29.131 10.048  1.00 47.50  ? 666  HOH A O   1 
HETATM 7708 O  O   . HOH S 7 .   ? -15.741 -10.021 29.701  1.00 30.43  ? 667  HOH A O   1 
HETATM 7709 O  O   . HOH S 7 .   ? -1.670  -34.129 4.357   1.00 45.87  ? 668  HOH A O   1 
HETATM 7710 O  O   . HOH S 7 .   ? -11.563 -32.366 20.682  1.00 48.99  ? 669  HOH A O   1 
HETATM 7711 O  O   . HOH S 7 .   ? -4.828  2.108   8.382   1.00 42.22  ? 670  HOH A O   1 
HETATM 7712 O  O   . HOH S 7 .   ? -12.898 2.501   30.195  1.00 46.99  ? 671  HOH A O   1 
HETATM 7713 O  O   . HOH S 7 .   ? -26.074 -24.657 20.635  1.00 43.55  ? 672  HOH A O   1 
HETATM 7714 O  O   . HOH S 7 .   ? 3.145   -24.628 11.536  1.00 37.68  ? 673  HOH A O   1 
HETATM 7715 O  O   . HOH S 7 .   ? -18.945 -29.630 -5.997  1.00 40.13  ? 674  HOH A O   1 
HETATM 7716 O  O   . HOH S 7 .   ? -34.481 -9.597  17.709  1.00 41.83  ? 675  HOH A O   1 
HETATM 7717 O  O   . HOH S 7 .   ? -23.470 -19.132 13.245  1.00 33.44  ? 676  HOH A O   1 
HETATM 7718 O  O   . HOH S 7 .   ? -37.333 -20.196 19.718  1.00 49.50  ? 677  HOH A O   1 
HETATM 7719 O  O   . HOH S 7 .   ? -7.702  -1.960  35.493  1.00 40.00  ? 678  HOH A O   1 
HETATM 7720 O  O   . HOH S 7 .   ? 3.474   4.769   6.047   1.00 54.90  ? 679  HOH A O   1 
HETATM 7721 O  O   . HOH S 7 .   ? -3.716  -25.592 -10.920 1.00 38.31  ? 680  HOH A O   1 
HETATM 7722 O  O   . HOH S 7 .   ? -9.229  -31.338 21.754  1.00 55.42  ? 681  HOH A O   1 
HETATM 7723 O  O   . HOH S 7 .   ? -33.050 -21.033 15.181  1.00 41.27  ? 682  HOH A O   1 
HETATM 7724 O  O   . HOH S 7 .   ? -17.488 -39.178 14.436  1.00 57.03  ? 683  HOH A O   1 
HETATM 7725 O  O   . HOH S 7 .   ? -29.992 -2.988  9.368   1.00 49.58  ? 684  HOH A O   1 
HETATM 7726 O  O   . HOH S 7 .   ? -2.372  -21.420 19.882  1.00 41.80  ? 685  HOH A O   1 
HETATM 7727 O  O   . HOH S 7 .   ? 4.183   -17.004 -3.530  1.00 50.90  ? 686  HOH A O   1 
HETATM 7728 O  O   . HOH S 7 .   ? -9.034  -4.848  6.227   1.00 38.72  ? 687  HOH A O   1 
HETATM 7729 O  O   . HOH S 7 .   ? 2.539   -19.155 24.198  1.00 37.88  ? 688  HOH A O   1 
HETATM 7730 O  O   . HOH S 7 .   ? -17.814 -4.481  12.211  1.00 45.59  ? 689  HOH A O   1 
HETATM 7731 O  O   . HOH S 7 .   ? -22.507 0.570   21.475  1.00 40.60  ? 690  HOH A O   1 
HETATM 7732 O  O   . HOH S 7 .   ? 9.647   -9.345  6.476   1.00 46.86  ? 691  HOH A O   1 
HETATM 7733 O  O   . HOH S 7 .   ? -22.136 -13.096 -0.637  1.00 35.26  ? 692  HOH A O   1 
HETATM 7734 O  O   . HOH S 7 .   ? -27.673 -7.895  1.634   1.00 49.81  ? 693  HOH A O   1 
HETATM 7735 O  O   . HOH S 7 .   ? -4.163  8.488   24.361  1.00 43.38  ? 694  HOH A O   1 
HETATM 7736 O  O   . HOH S 7 .   ? -9.638  -27.591 25.302  1.00 48.50  ? 695  HOH A O   1 
HETATM 7737 O  O   . HOH S 7 .   ? -8.167  -2.572  -2.400  1.00 42.77  ? 696  HOH A O   1 
HETATM 7738 O  O   . HOH S 7 .   ? -20.436 -30.803 2.919   1.00 53.18  ? 697  HOH A O   1 
HETATM 7739 O  O   . HOH S 7 .   ? -31.998 -3.967  15.449  1.00 43.73  ? 698  HOH A O   1 
HETATM 7740 O  O   . HOH S 7 .   ? -17.833 -14.470 3.046   1.00 30.97  ? 699  HOH A O   1 
HETATM 7741 O  O   . HOH S 7 .   ? -16.144 -22.463 5.056   1.00 34.71  ? 700  HOH A O   1 
HETATM 7742 O  O   . HOH S 7 .   ? -26.037 -19.719 1.060   1.00 32.96  ? 701  HOH A O   1 
HETATM 7743 O  O   . HOH S 7 .   ? -25.281 -14.267 -3.990  1.00 38.09  ? 702  HOH A O   1 
HETATM 7744 O  O   . HOH S 7 .   ? -14.579 -28.885 -11.912 1.00 47.45  ? 703  HOH A O   1 
HETATM 7745 O  O   . HOH S 7 .   ? -9.901  -18.922 21.756  1.00 45.64  ? 704  HOH A O   1 
HETATM 7746 O  O   . HOH S 7 .   ? -24.526 -12.661 -13.695 1.00 46.37  ? 705  HOH A O   1 
HETATM 7747 O  O   . HOH S 7 .   ? 7.120   -0.538  21.387  1.00 45.57  ? 706  HOH A O   1 
HETATM 7748 O  O   . HOH S 7 .   ? 5.272   -20.323 28.933  1.00 56.15  ? 707  HOH A O   1 
HETATM 7749 O  O   . HOH S 7 .   ? -10.385 -16.145 39.424  1.00 49.62  ? 708  HOH A O   1 
HETATM 7750 O  O   . HOH S 7 .   ? -20.074 -32.233 14.354  1.00 51.45  ? 709  HOH A O   1 
HETATM 7751 O  O   . HOH S 7 .   ? 2.171   -24.932 4.204   1.00 45.59  ? 710  HOH A O   1 
HETATM 7752 O  O   . HOH S 7 .   ? -6.691  -44.151 -5.660  1.00 35.71  ? 711  HOH A O   1 
HETATM 7753 O  O   . HOH S 7 .   ? -1.039  0.161   -1.732  1.00 48.14  ? 712  HOH A O   1 
HETATM 7754 O  O   . HOH S 7 .   ? -5.133  0.403   3.803   1.00 53.28  ? 713  HOH A O   1 
HETATM 7755 O  O   . HOH S 7 .   ? -9.466  -14.812 7.684   1.00 33.07  ? 714  HOH A O   1 
HETATM 7756 O  O   . HOH S 7 .   ? -3.824  -11.738 -3.796  1.00 37.83  ? 715  HOH A O   1 
HETATM 7757 O  O   . HOH S 7 .   ? -17.997 -20.682 3.673   1.00 31.48  ? 716  HOH A O   1 
HETATM 7758 O  O   . HOH S 7 .   ? -10.222 -10.173 33.163  1.00 31.02  ? 717  HOH A O   1 
HETATM 7759 O  O   . HOH S 7 .   ? -0.464  -16.739 30.445  1.00 41.15  ? 718  HOH A O   1 
HETATM 7760 O  O   . HOH S 7 .   ? -14.121 -27.368 -14.182 1.00 44.30  ? 719  HOH A O   1 
HETATM 7761 O  O   . HOH S 7 .   ? -18.649 -17.999 1.767   1.00 31.89  ? 720  HOH A O   1 
HETATM 7762 O  O   . HOH S 7 .   ? -18.437 -42.620 25.462  1.00 65.01  ? 721  HOH A O   1 
HETATM 7763 O  O   . HOH S 7 .   ? -18.616 -34.976 16.426  1.00 55.54  ? 722  HOH A O   1 
HETATM 7764 O  O   . HOH S 7 .   ? 5.328   6.201   12.517  1.00 48.64  ? 723  HOH A O   1 
HETATM 7765 O  O   . HOH S 7 .   ? -29.614 -20.739 -3.855  1.00 48.64  ? 724  HOH A O   1 
HETATM 7766 O  O   . HOH S 7 .   ? -5.174  -23.992 -5.477  1.00 36.54  ? 725  HOH A O   1 
HETATM 7767 O  O   . HOH S 7 .   ? -0.724  -28.558 -11.953 1.00 49.00  ? 726  HOH A O   1 
HETATM 7768 O  O   . HOH S 7 .   ? -12.578 -12.569 16.447  1.00 31.16  ? 727  HOH A O   1 
HETATM 7769 O  O   . HOH S 7 .   ? 14.310  -12.199 16.797  1.00 54.06  ? 728  HOH A O   1 
HETATM 7770 O  O   . HOH S 7 .   ? -11.176 -7.203  1.886   1.00 48.10  ? 729  HOH A O   1 
HETATM 7771 O  O   . HOH S 7 .   ? -13.182 -8.062  33.844  1.00 33.17  ? 730  HOH A O   1 
HETATM 7772 O  O   . HOH S 7 .   ? -0.411  -15.896 33.202  1.00 43.19  ? 731  HOH A O   1 
HETATM 7773 O  O   . HOH S 7 .   ? -39.509 -20.392 15.055  1.00 64.65  ? 732  HOH A O   1 
HETATM 7774 O  O   . HOH S 7 .   ? -8.794  -15.254 -16.646 1.00 51.39  ? 733  HOH A O   1 
HETATM 7775 O  O   . HOH S 7 .   ? -13.391 -15.291 -17.511 1.00 47.80  ? 734  HOH A O   1 
HETATM 7776 O  O   . HOH S 7 .   ? -3.132  -11.523 -11.428 1.00 50.16  ? 735  HOH A O   1 
HETATM 7777 O  O   . HOH S 7 .   ? -10.047 -4.650  24.156  1.00 33.44  ? 736  HOH A O   1 
HETATM 7778 O  O   . HOH S 7 .   ? 5.978   3.908   21.806  1.00 45.50  ? 737  HOH A O   1 
HETATM 7779 O  O   . HOH S 7 .   ? 6.564   9.420   18.364  1.00 52.30  ? 738  HOH A O   1 
HETATM 7780 O  O   . HOH S 7 .   ? -9.922  10.460  14.443  1.00 45.63  ? 739  HOH A O   1 
HETATM 7781 O  O   . HOH S 7 .   ? -7.742  -25.546 10.362  1.00 35.46  ? 740  HOH A O   1 
HETATM 7782 O  O   . HOH S 7 .   ? -17.775 -9.095  -3.949  1.00 41.83  ? 741  HOH A O   1 
HETATM 7783 O  O   . HOH S 7 .   ? -3.202  -12.643 11.271  1.00 34.41  ? 742  HOH A O   1 
HETATM 7784 O  O   . HOH S 7 .   ? -9.998  -48.120 -1.152  1.00 57.10  ? 743  HOH A O   1 
HETATM 7785 O  O   . HOH S 7 .   ? -37.525 -16.600 11.733  1.00 50.52  ? 744  HOH A O   1 
HETATM 7786 O  O   . HOH S 7 .   ? -33.485 -13.851 34.685  1.00 56.74  ? 745  HOH A O   1 
HETATM 7787 O  O   . HOH S 7 .   ? -22.994 -19.220 -11.690 1.00 43.87  ? 746  HOH A O   1 
HETATM 7788 O  O   . HOH S 7 .   ? 1.757   -9.003  -12.348 1.00 58.02  ? 747  HOH A O   1 
HETATM 7789 O  O   . HOH S 7 .   ? 9.177   -7.508  40.435  1.00 53.13  ? 748  HOH A O   1 
HETATM 7790 O  O   . HOH S 7 .   ? -3.545  12.519  19.358  1.00 44.99  ? 749  HOH A O   1 
HETATM 7791 O  O   . HOH S 7 .   ? -17.441 4.202   24.972  1.00 39.94  ? 750  HOH A O   1 
HETATM 7792 O  O   . HOH S 7 .   ? -21.859 2.033   25.908  1.00 56.00  ? 751  HOH A O   1 
HETATM 7793 O  O   . HOH S 7 .   ? 7.764   -9.649  30.074  1.00 44.79  ? 752  HOH A O   1 
HETATM 7794 O  O   . HOH S 7 .   ? 2.967   -5.705  -2.624  1.00 42.61  ? 753  HOH A O   1 
HETATM 7795 O  O   . HOH S 7 .   ? -9.423  -1.543  33.346  1.00 36.71  ? 754  HOH A O   1 
HETATM 7796 O  O   . HOH S 7 .   ? -7.385  -33.393 14.410  1.00 53.89  ? 755  HOH A O   1 
HETATM 7797 O  O   . HOH S 7 .   ? -17.481 -12.374 -12.778 1.00 48.81  ? 756  HOH A O   1 
HETATM 7798 O  O   . HOH S 7 .   ? -15.490 -31.829 21.689  1.00 42.72  ? 757  HOH A O   1 
HETATM 7799 O  O   . HOH S 7 .   ? -10.013 -40.920 5.745   1.00 51.36  ? 758  HOH A O   1 
HETATM 7800 O  O   . HOH S 7 .   ? 8.968   -11.616 9.153   1.00 44.47  ? 759  HOH A O   1 
HETATM 7801 O  O   . HOH S 7 .   ? -7.695  -20.174 22.223  1.00 48.11  ? 760  HOH A O   1 
HETATM 7802 O  O   . HOH S 7 .   ? -28.707 -15.866 11.240  1.00 31.95  ? 761  HOH A O   1 
HETATM 7803 O  O   . HOH S 7 .   ? -20.490 -24.628 -17.271 1.00 52.74  ? 762  HOH A O   1 
HETATM 7804 O  O   . HOH S 7 .   ? 2.256   -21.645 0.526   1.00 45.65  ? 763  HOH A O   1 
HETATM 7805 O  O   . HOH S 7 .   ? -19.584 -14.803 -4.440  1.00 35.05  ? 764  HOH A O   1 
HETATM 7806 O  O   . HOH S 7 .   ? -11.603 -42.243 8.954   1.00 59.46  ? 765  HOH A O   1 
HETATM 7807 O  O   . HOH S 7 .   ? 2.789   -29.027 5.380   1.00 57.06  ? 766  HOH A O   1 
HETATM 7808 O  O   . HOH S 7 .   ? -39.910 -13.964 16.281  1.00 55.98  ? 767  HOH A O   1 
HETATM 7809 O  O   . HOH S 7 .   ? -23.511 -0.834  10.779  1.00 48.83  ? 768  HOH A O   1 
HETATM 7810 O  O   . HOH S 7 .   ? -26.336 -28.943 -11.717 1.00 51.97  ? 769  HOH A O   1 
HETATM 7811 O  O   . HOH S 7 .   ? 10.319  -20.552 21.562  1.00 45.61  ? 770  HOH A O   1 
HETATM 7812 O  O   . HOH S 7 .   ? -18.127 -29.193 -15.036 1.00 53.15  ? 771  HOH A O   1 
HETATM 7813 O  O   . HOH S 7 .   ? 5.518   5.563   24.263  1.00 47.33  ? 772  HOH A O   1 
HETATM 7814 O  O   . HOH S 7 .   ? 1.665   -40.454 0.799   1.00 43.45  ? 773  HOH A O   1 
HETATM 7815 O  O   . HOH S 7 .   ? -14.917 -17.357 -17.933 1.00 49.63  ? 774  HOH A O   1 
HETATM 7816 O  O   . HOH S 7 .   ? -7.419  -17.364 15.253  1.00 34.68  ? 775  HOH A O   1 
HETATM 7817 O  O   . HOH S 7 .   ? 9.055   -13.368 -0.625  1.00 50.46  ? 776  HOH A O   1 
HETATM 7818 O  O   . HOH S 7 .   ? 14.393  1.359   12.253  1.00 64.01  ? 777  HOH A O   1 
HETATM 7819 O  O   . HOH S 7 .   ? -12.416 -9.743  2.968   1.00 33.92  ? 778  HOH A O   1 
HETATM 7820 O  O   . HOH S 7 .   ? 1.217   -14.604 29.757  1.00 37.54  ? 779  HOH A O   1 
HETATM 7821 O  O   . HOH S 7 .   ? -26.527 -8.142  31.341  1.00 44.68  ? 780  HOH A O   1 
HETATM 7822 O  O   . HOH S 7 .   ? 13.896  -9.129  20.000  1.00 46.54  ? 781  HOH A O   1 
HETATM 7823 O  O   . HOH S 7 .   ? -22.435 -6.800  -1.574  1.00 47.17  ? 782  HOH A O   1 
HETATM 7824 O  O   . HOH S 7 .   ? 12.763  -7.715  18.053  1.00 46.33  ? 783  HOH A O   1 
HETATM 7825 O  O   . HOH S 7 .   ? -1.448  -22.356 -11.439 1.00 43.29  ? 784  HOH A O   1 
HETATM 7826 O  O   . HOH S 7 .   ? 0.762   -10.068 36.209  1.00 36.36  ? 785  HOH A O   1 
HETATM 7827 O  O   . HOH S 7 .   ? -8.774  -22.250 19.099  1.00 40.50  ? 786  HOH A O   1 
HETATM 7828 O  O   . HOH S 7 .   ? 14.978  -20.925 18.207  1.00 55.61  ? 787  HOH A O   1 
HETATM 7829 O  O   . HOH S 7 .   ? -18.480 -2.407  33.690  1.00 53.11  ? 788  HOH A O   1 
HETATM 7830 O  O   . HOH S 7 .   ? -4.767  -37.696 -8.258  1.00 47.66  ? 789  HOH A O   1 
HETATM 7831 O  O   . HOH S 7 .   ? -6.988  -7.880  35.629  1.00 33.51  ? 790  HOH A O   1 
HETATM 7832 O  O   . HOH S 7 .   ? -22.748 -28.127 0.601   1.00 51.49  ? 791  HOH A O   1 
HETATM 7833 O  O   . HOH S 7 .   ? 14.176  -10.788 12.774  1.00 50.31  ? 792  HOH A O   1 
HETATM 7834 O  O   . HOH S 7 .   ? -12.426 -28.474 -16.030 1.00 52.86  ? 793  HOH A O   1 
HETATM 7835 O  O   . HOH S 7 .   ? -9.850  -42.286 -5.750  1.00 49.79  ? 794  HOH A O   1 
HETATM 7836 O  O   . HOH S 7 .   ? -23.306 5.275   13.266  1.00 53.29  ? 795  HOH A O   1 
HETATM 7837 O  O   . HOH S 7 .   ? 10.383  -3.063  21.231  1.00 44.14  ? 796  HOH A O   1 
HETATM 7838 O  O   . HOH S 7 .   ? -5.173  -27.084 -15.260 1.00 57.10  ? 797  HOH A O   1 
HETATM 7839 O  O   . HOH S 7 .   ? -39.117 -17.074 21.072  1.00 51.59  ? 798  HOH A O   1 
HETATM 7840 O  O   . HOH S 7 .   ? -35.895 -2.361  16.349  1.00 51.38  ? 799  HOH A O   1 
HETATM 7841 O  O   . HOH S 7 .   ? -16.222 -6.783  -7.641  1.00 43.52  ? 800  HOH A O   1 
HETATM 7842 O  O   . HOH S 7 .   ? -16.206 7.019   13.150  1.00 54.47  ? 801  HOH A O   1 
HETATM 7843 O  O   . HOH S 7 .   ? -24.305 -14.066 -1.425  1.00 36.52  ? 802  HOH A O   1 
HETATM 7844 O  O   . HOH S 7 .   ? -34.314 -15.133 24.543  1.00 57.21  ? 803  HOH A O   1 
HETATM 7845 O  O   . HOH S 7 .   ? -5.772  -22.378 16.295  1.00 37.38  ? 804  HOH A O   1 
HETATM 7846 O  O   . HOH S 7 .   ? -34.537 -19.488 8.942   1.00 41.66  ? 805  HOH A O   1 
HETATM 7847 O  O   . HOH S 7 .   ? -30.693 -4.588  27.160  1.00 48.74  ? 806  HOH A O   1 
HETATM 7848 O  O   . HOH S 7 .   ? -16.191 6.784   22.329  1.00 43.10  ? 807  HOH A O   1 
HETATM 7849 O  O   . HOH S 7 .   ? -11.857 -5.907  -3.968  1.00 37.59  ? 808  HOH A O   1 
HETATM 7850 O  O   . HOH S 7 .   ? -35.241 -19.840 14.912  1.00 43.25  ? 809  HOH A O   1 
HETATM 7851 O  O   . HOH S 7 .   ? -25.496 -10.476 30.547  1.00 43.56  ? 810  HOH A O   1 
HETATM 7852 O  O   . HOH S 7 .   ? -1.150  -7.232  -10.490 1.00 51.65  ? 811  HOH A O   1 
HETATM 7853 O  O   . HOH S 7 .   ? 10.582  -21.864 18.980  1.00 46.12  ? 812  HOH A O   1 
HETATM 7854 O  O   . HOH S 7 .   ? 7.458   -16.520 9.321   1.00 49.99  ? 813  HOH A O   1 
HETATM 7855 O  O   . HOH S 7 .   ? -16.235 2.664   12.995  1.00 58.76  ? 814  HOH A O   1 
HETATM 7856 O  O   . HOH S 7 .   ? -19.842 -14.277 -1.629  1.00 33.98  ? 815  HOH A O   1 
HETATM 7857 O  O   . HOH S 7 .   ? -29.978 -11.031 0.593   1.00 51.94  ? 816  HOH A O   1 
HETATM 7858 O  O   . HOH S 7 .   ? -24.044 -10.490 35.334  1.00 47.30  ? 817  HOH A O   1 
HETATM 7859 O  O   . HOH S 7 .   ? -35.818 -15.677 14.436  1.00 44.31  ? 818  HOH A O   1 
HETATM 7860 O  O   . HOH S 7 .   ? -8.954  -4.854  -3.597  1.00 41.32  ? 819  HOH A O   1 
HETATM 7861 O  O   . HOH S 7 .   ? -7.949  -17.566 31.220  1.00 43.21  ? 820  HOH A O   1 
HETATM 7862 O  O   . HOH S 7 .   ? -13.554 -43.213 10.079  1.00 58.92  ? 821  HOH A O   1 
HETATM 7863 O  O   . HOH S 7 .   ? -35.579 -12.854 6.114   1.00 37.91  ? 822  HOH A O   1 
HETATM 7864 O  O   . HOH S 7 .   ? -31.558 -18.118 30.312  1.00 54.67  ? 823  HOH A O   1 
HETATM 7865 O  O   . HOH S 7 .   ? 9.806   5.959   28.562  1.00 55.68  ? 824  HOH A O   1 
HETATM 7866 O  O   . HOH S 7 .   ? -16.312 -14.932 35.113  1.00 42.64  ? 825  HOH A O   1 
HETATM 7867 O  O   . HOH S 7 .   ? -31.190 -3.084  29.335  1.00 69.57  ? 826  HOH A O   1 
HETATM 7868 O  O   . HOH S 7 .   ? -3.422  -34.256 -11.171 1.00 48.89  ? 827  HOH A O   1 
HETATM 7869 O  O   . HOH S 7 .   ? -27.907 -27.301 6.105   1.00 45.73  ? 828  HOH A O   1 
HETATM 7870 O  O   . HOH S 7 .   ? -5.558  13.639  20.882  1.00 48.48  ? 829  HOH A O   1 
HETATM 7871 O  O   . HOH S 7 .   ? 9.264   -4.098  6.001   1.00 52.62  ? 830  HOH A O   1 
HETATM 7872 O  O   . HOH S 7 .   ? -10.943 -37.449 -10.499 1.00 62.27  ? 831  HOH A O   1 
HETATM 7873 O  O   . HOH S 7 .   ? -1.205  -17.855 -5.131  1.00 43.91  ? 832  HOH A O   1 
HETATM 7874 O  O   . HOH S 7 .   ? -22.055 3.726   10.734  1.00 47.85  ? 833  HOH A O   1 
HETATM 7875 O  O   . HOH S 7 .   ? -29.887 -14.518 -7.631  1.00 63.55  ? 834  HOH A O   1 
HETATM 7876 O  O   . HOH S 7 .   ? -19.011 -6.629  1.703   1.00 49.69  ? 835  HOH A O   1 
HETATM 7877 O  O   . HOH S 7 .   ? 11.966  -1.451  17.301  1.00 51.09  ? 836  HOH A O   1 
HETATM 7878 O  O   . HOH S 7 .   ? -25.020 -32.174 18.089  1.00 59.11  ? 837  HOH A O   1 
HETATM 7879 O  O   . HOH S 7 .   ? -15.531 -20.253 6.569   1.00 32.79  ? 838  HOH A O   1 
HETATM 7880 O  O   . HOH S 7 .   ? -20.390 -9.337  -6.889  1.00 39.61  ? 839  HOH A O   1 
HETATM 7881 O  O   . HOH S 7 .   ? -15.094 -34.464 21.081  1.00 47.15  ? 840  HOH A O   1 
HETATM 7882 O  O   . HOH S 7 .   ? -30.857 -22.648 20.182  1.00 44.58  ? 841  HOH A O   1 
HETATM 7883 O  O   . HOH S 7 .   ? 6.821   -16.282 32.932  1.00 46.67  ? 842  HOH A O   1 
HETATM 7884 O  O   . HOH S 7 .   ? -33.346 -2.990  13.574  1.00 53.29  ? 843  HOH A O   1 
HETATM 7885 O  O   . HOH S 7 .   ? -9.430  -7.270  -2.111  1.00 37.76  ? 844  HOH A O   1 
HETATM 7886 O  O   . HOH S 7 .   ? -19.576 -28.686 1.665   1.00 47.22  ? 845  HOH A O   1 
HETATM 7887 O  O   . HOH S 7 .   ? -10.704 -20.835 34.905  1.00 49.99  ? 846  HOH A O   1 
HETATM 7888 O  O   . HOH S 7 .   ? 1.449   -35.840 2.157   1.00 51.33  ? 847  HOH A O   1 
HETATM 7889 O  O   . HOH S 7 .   ? -4.625  -28.956 16.982  1.00 53.15  ? 848  HOH A O   1 
HETATM 7890 O  O   . HOH S 7 .   ? -0.410  -28.559 15.875  1.00 46.56  ? 849  HOH A O   1 
HETATM 7891 O  O   . HOH S 7 .   ? -8.515  -5.491  -10.509 1.00 34.18  ? 850  HOH A O   1 
HETATM 7892 O  O   . HOH S 7 .   ? -0.713  -1.484  -8.822  1.00 57.33  ? 851  HOH A O   1 
HETATM 7893 O  O   . HOH S 7 .   ? -7.669  -8.022  -11.602 1.00 36.60  ? 852  HOH A O   1 
HETATM 7894 O  O   . HOH S 7 .   ? -16.160 -10.424 -10.611 1.00 48.64  ? 853  HOH A O   1 
HETATM 7895 O  O   . HOH S 7 .   ? -16.393 -8.114  -0.394  1.00 43.51  ? 854  HOH A O   1 
HETATM 7896 O  O   . HOH S 7 .   ? -7.841  -46.580 1.363   1.00 55.88  ? 855  HOH A O   1 
HETATM 7897 O  O   . HOH S 7 .   ? -32.884 -19.122 25.583  1.00 55.54  ? 856  HOH A O   1 
HETATM 7898 O  O   . HOH S 7 .   ? -16.206 -30.459 30.540  1.00 63.29  ? 857  HOH A O   1 
HETATM 7899 O  O   . HOH S 7 .   ? 6.715   -5.531  38.049  1.00 46.16  ? 858  HOH A O   1 
HETATM 7900 O  O   . HOH S 7 .   ? -13.005 -7.170  -1.356  1.00 55.88  ? 859  HOH A O   1 
HETATM 7901 O  O   . HOH S 7 .   ? -13.711 7.940   23.189  1.00 43.37  ? 860  HOH A O   1 
HETATM 7902 O  O   . HOH S 7 .   ? -20.071 -32.227 -3.761  1.00 53.78  ? 861  HOH A O   1 
HETATM 7903 O  O   . HOH S 7 .   ? -29.286 -12.540 -2.067  1.00 55.08  ? 862  HOH A O   1 
HETATM 7904 O  O   . HOH S 7 .   ? -16.118 -31.399 -11.963 1.00 51.62  ? 863  HOH A O   1 
HETATM 7905 O  O   . HOH S 7 .   ? -6.215  -18.082 27.354  1.00 45.29  ? 864  HOH A O   1 
HETATM 7906 O  O   . HOH S 7 .   ? 13.476  -18.948 14.665  1.00 51.96  ? 865  HOH A O   1 
HETATM 7907 O  O   . HOH S 7 .   ? -20.851 -1.913  25.159  1.00 46.35  ? 866  HOH A O   1 
HETATM 7908 O  O   . HOH S 7 .   ? -19.283 -2.425  10.416  1.00 52.77  ? 867  HOH A O   1 
HETATM 7909 O  O   . HOH S 7 .   ? -16.333 -37.726 -5.028  1.00 52.40  ? 868  HOH A O   1 
HETATM 7910 O  O   . HOH S 7 .   ? -39.006 -16.390 14.575  1.00 56.53  ? 869  HOH A O   1 
HETATM 7911 O  O   . HOH S 7 .   ? -0.757  -21.841 -5.658  1.00 50.25  ? 870  HOH A O   1 
HETATM 7912 O  O   . HOH S 7 .   ? -22.582 -0.303  24.196  1.00 45.52  ? 871  HOH A O   1 
HETATM 7913 O  O   . HOH S 7 .   ? -6.149  -9.859  37.602  1.00 33.65  ? 872  HOH A O   1 
HETATM 7914 O  O   . HOH S 7 .   ? 11.036  -18.384 28.273  1.00 51.39  ? 873  HOH A O   1 
HETATM 7915 O  O   . HOH S 7 .   ? -4.063  -13.992 33.990  1.00 40.26  ? 874  HOH A O   1 
HETATM 7916 O  O   . HOH S 7 .   ? -0.263  -16.914 -9.520  1.00 54.33  ? 875  HOH A O   1 
HETATM 7917 O  O   . HOH S 7 .   ? -13.176 10.013  20.940  1.00 44.22  ? 876  HOH A O   1 
HETATM 7918 O  O   . HOH S 7 .   ? -0.587  -5.718  -8.823  1.00 57.41  ? 877  HOH A O   1 
HETATM 7919 O  O   . HOH S 7 .   ? -0.379  -34.915 -3.755  1.00 44.49  ? 878  HOH A O   1 
HETATM 7920 O  O   . HOH S 7 .   ? -26.898 -27.189 19.953  1.00 53.34  ? 879  HOH A O   1 
HETATM 7921 O  O   . HOH S 7 .   ? -22.239 8.081   12.563  1.00 59.58  ? 880  HOH A O   1 
HETATM 7922 O  O   . HOH S 7 .   ? 5.169   -16.415 7.957   1.00 45.69  ? 881  HOH A O   1 
HETATM 7923 O  O   . HOH S 7 .   ? -16.796 -38.097 3.063   1.00 51.70  ? 882  HOH A O   1 
HETATM 7924 O  O   . HOH S 7 .   ? -6.868  9.899   29.533  1.00 53.60  ? 883  HOH A O   1 
HETATM 7925 O  O   . HOH S 7 .   ? -4.473  -42.133 11.910  1.00 60.85  ? 884  HOH A O   1 
HETATM 7926 O  O   . HOH S 7 .   ? -8.904  -12.074 -15.993 1.00 55.78  ? 885  HOH A O   1 
HETATM 7927 O  O   . HOH S 7 .   ? -30.570 -3.281  7.068   1.00 59.34  ? 886  HOH A O   1 
HETATM 7928 O  O   . HOH S 7 .   ? -19.464 -18.108 -17.871 1.00 50.25  ? 887  HOH A O   1 
HETATM 7929 O  O   . HOH S 7 .   ? 12.426  -17.386 13.164  1.00 53.03  ? 888  HOH A O   1 
HETATM 7930 O  O   . HOH S 7 .   ? 11.598  -13.631 38.574  1.00 54.56  ? 889  HOH A O   1 
HETATM 7931 O  O   . HOH S 7 .   ? 6.092   -24.395 19.612  1.00 58.45  ? 890  HOH A O   1 
HETATM 7932 O  O   . HOH S 7 .   ? -16.345 -33.480 -10.756 1.00 62.40  ? 891  HOH A O   1 
HETATM 7933 O  O   . HOH S 7 .   ? -10.542 -15.581 -18.615 1.00 57.45  ? 892  HOH A O   1 
HETATM 7934 O  O   . HOH S 7 .   ? -5.212  6.247   -6.428  1.00 46.88  ? 893  HOH A O   1 
HETATM 7935 O  O   . HOH S 7 .   ? 4.457   -17.020 32.138  1.00 58.28  ? 894  HOH A O   1 
HETATM 7936 O  O   . HOH S 7 .   ? -28.946 -21.484 -6.849  1.00 51.23  ? 895  HOH A O   1 
HETATM 7937 O  O   . HOH S 7 .   ? -7.526  12.060  17.486  1.00 52.75  ? 896  HOH A O   1 
HETATM 7938 O  O   . HOH S 7 .   ? -19.376 4.216   26.618  1.00 56.92  ? 897  HOH A O   1 
HETATM 7939 O  O   . HOH S 7 .   ? -12.323 -15.527 37.637  1.00 52.47  ? 898  HOH A O   1 
HETATM 7940 O  O   . HOH S 7 .   ? -38.937 -13.597 21.483  1.00 65.67  ? 899  HOH A O   1 
HETATM 7941 O  O   . HOH S 7 .   ? -4.797  -2.882  -9.695  1.00 44.09  ? 900  HOH A O   1 
HETATM 7942 O  O   . HOH S 7 .   ? -8.769  -17.737 28.849  1.00 48.37  ? 901  HOH A O   1 
HETATM 7943 O  O   . HOH S 7 .   ? -18.924 -15.535 0.579   1.00 32.85  ? 902  HOH A O   1 
HETATM 7944 O  O   . HOH S 7 .   ? -5.973  -9.073  -15.471 1.00 53.79  ? 903  HOH A O   1 
HETATM 7945 O  O   . HOH S 7 .   ? -15.910 -6.691  3.503   1.00 52.66  ? 904  HOH A O   1 
HETATM 7946 O  O   . HOH S 7 .   ? -28.715 -26.111 -14.468 1.00 55.24  ? 905  HOH A O   1 
HETATM 7947 O  O   . HOH S 7 .   ? -24.344 3.033   21.902  1.00 60.86  ? 906  HOH A O   1 
HETATM 7948 O  O   . HOH S 7 .   ? 14.936  -10.194 15.197  1.00 59.55  ? 907  HOH A O   1 
HETATM 7949 O  O   . HOH S 7 .   ? -3.314  -25.075 -13.388 1.00 45.47  ? 908  HOH A O   1 
HETATM 7950 O  O   . HOH S 7 .   ? -9.006  -44.360 -6.980  1.00 46.06  ? 909  HOH A O   1 
HETATM 7951 O  O   . HOH S 7 .   ? -9.033  12.841  15.169  1.00 56.33  ? 910  HOH A O   1 
HETATM 7952 O  O   . HOH S 7 .   ? -13.309 -13.507 39.070  1.00 43.84  ? 911  HOH A O   1 
HETATM 7953 O  O   . HOH S 7 .   ? -12.120 12.505  21.927  1.00 51.83  ? 912  HOH A O   1 
HETATM 7954 O  O   . HOH S 7 .   ? -2.240  -15.600 -12.025 1.00 48.48  ? 913  HOH A O   1 
HETATM 7955 O  O   . HOH S 7 .   ? 6.068   11.555  19.871  1.00 61.24  ? 914  HOH A O   1 
HETATM 7956 O  O   . HOH S 7 .   ? -24.506 -17.703 -13.566 1.00 51.49  ? 915  HOH A O   1 
HETATM 7957 O  O   . HOH S 7 .   ? 4.354   -20.445 4.092   1.00 56.72  ? 916  HOH A O   1 
HETATM 7958 O  O   . HOH S 7 .   ? -23.286 -1.618  27.869  1.00 55.70  ? 917  HOH A O   1 
HETATM 7959 O  O   . HOH S 7 .   ? 2.379   -23.491 24.720  1.00 62.73  ? 918  HOH A O   1 
HETATM 7960 O  O   . HOH S 7 .   ? -27.958 -27.858 22.592  1.00 61.88  ? 919  HOH A O   1 
HETATM 7961 O  O   . HOH S 7 .   ? 11.220  -3.490  8.033   1.00 53.03  ? 920  HOH A O   1 
HETATM 7962 O  O   . HOH S 7 .   ? -2.122  14.545  18.823  1.00 55.49  ? 921  HOH A O   1 
HETATM 7963 O  O   . HOH S 7 .   ? -0.007  -34.293 -1.065  1.00 47.09  ? 922  HOH A O   1 
HETATM 7964 O  O   . HOH S 7 .   ? -15.654 6.441   25.715  1.00 56.89  ? 923  HOH A O   1 
HETATM 7965 O  O   . HOH S 7 .   ? 18.121  -18.338 22.225  1.00 60.28  ? 924  HOH A O   1 
HETATM 7966 O  O   . HOH S 7 .   ? 3.575   -21.068 25.807  1.00 47.41  ? 925  HOH A O   1 
HETATM 7967 O  O   . HOH S 7 .   ? -4.207  12.787  15.020  1.00 52.04  ? 926  HOH A O   1 
HETATM 7968 O  O   . HOH S 7 .   ? 2.118   -31.788 -0.491  1.00 53.67  ? 927  HOH A O   1 
HETATM 7969 O  O   . HOH S 7 .   ? 11.075  0.519   18.888  1.00 53.55  ? 928  HOH A O   1 
HETATM 7970 O  O   . HOH S 7 .   ? 0.468   -33.175 5.665   1.00 50.97  ? 929  HOH A O   1 
HETATM 7971 O  O   . HOH S 7 .   ? -3.334  -8.678  -11.688 1.00 52.84  ? 930  HOH A O   1 
HETATM 7972 O  O   . HOH S 7 .   ? 4.481   7.877   24.691  1.00 52.98  ? 931  HOH A O   1 
HETATM 7973 O  O   . HOH S 7 .   ? 1.823   -14.739 34.092  1.00 47.93  ? 932  HOH A O   1 
HETATM 7974 O  O   . HOH S 7 .   ? -8.037  13.646  19.823  1.00 48.00  ? 933  HOH A O   1 
HETATM 7975 O  O   . HOH S 7 .   ? -19.544 1.856   28.539  1.00 56.03  ? 934  HOH A O   1 
HETATM 7976 O  O   . HOH S 7 .   ? -37.172 -19.859 9.675   1.00 55.55  ? 935  HOH A O   1 
HETATM 7977 O  O   . HOH S 7 .   ? -4.925  -22.048 18.891  1.00 40.21  ? 936  HOH A O   1 
HETATM 7978 O  O   . HOH S 7 .   ? 3.132   -27.775 7.925   1.00 57.34  ? 937  HOH A O   1 
HETATM 7979 O  O   . HOH S 7 .   ? 18.131  -14.064 18.702  1.00 54.08  ? 938  HOH A O   1 
HETATM 7980 O  O   . HOH S 7 .   ? -34.603 -13.776 3.600   1.00 44.48  ? 939  HOH A O   1 
HETATM 7981 O  O   . HOH S 7 .   ? -7.130  -2.051  2.599   1.00 57.92  ? 940  HOH A O   1 
HETATM 7982 O  O   . HOH S 7 .   ? -5.280  -7.588  -12.792 1.00 51.70  ? 941  HOH A O   1 
HETATM 7983 O  O   . HOH S 7 .   ? -6.952  -22.745 20.592  1.00 48.83  ? 942  HOH A O   1 
HETATM 7984 O  O   . HOH S 7 .   ? -16.026 -18.092 -20.445 1.00 53.68  ? 943  HOH A O   1 
HETATM 7985 O  O   . HOH S 7 .   ? -5.008  11.702  17.189  1.00 46.08  ? 944  HOH A O   1 
HETATM 7986 O  O   . HOH S 7 .   ? 16.246  -9.860  19.754  1.00 56.34  ? 945  HOH A O   1 
HETATM 7987 O  O   . HOH S 7 .   ? -15.371 10.236  19.577  1.00 56.56  ? 946  HOH A O   1 
HETATM 7988 O  O   . HOH S 7 .   ? -12.318 4.963   29.161  1.00 58.26  ? 947  HOH A O   1 
HETATM 7989 O  O   . HOH S 7 .   ? 1.878   5.837   7.474   1.00 60.65  ? 948  HOH A O   1 
HETATM 7990 O  O   . HOH S 7 .   ? -15.991 -19.963 -22.168 1.00 59.75  ? 949  HOH A O   1 
HETATM 7991 O  O   . HOH S 7 .   ? 2.047   -31.355 3.986   1.00 44.46  ? 950  HOH A O   1 
HETATM 7992 O  O   . HOH S 7 .   ? -16.660 -26.999 32.106  1.00 55.67  ? 951  HOH A O   1 
HETATM 7993 O  O   . HOH S 7 .   ? 7.961   6.594   24.505  1.00 52.66  ? 952  HOH A O   1 
HETATM 7994 O  O   . HOH S 7 .   ? -0.503  -33.652 1.752   1.00 44.70  ? 953  HOH A O   1 
HETATM 7995 O  O   . HOH S 7 .   ? -27.256 -29.581 -6.153  1.00 60.86  ? 954  HOH A O   1 
HETATM 7996 O  O   . HOH S 7 .   ? -7.513  -3.622  0.135   1.00 53.76  ? 955  HOH A O   1 
HETATM 7997 O  O   . HOH S 7 .   ? 8.225   8.940   22.711  1.00 59.07  ? 956  HOH A O   1 
HETATM 7998 O  O   . HOH T 7 .   ? 11.399  -17.901 90.833  1.00 51.73  ? 601  HOH B O   1 
HETATM 7999 O  O   . HOH T 7 .   ? 9.237   -31.636 60.528  1.00 46.72  ? 602  HOH B O   1 
HETATM 8000 O  O   . HOH T 7 .   ? -0.234  -14.883 89.460  1.00 45.69  ? 603  HOH B O   1 
HETATM 8001 O  O   . HOH T 7 .   ? 2.954   6.314   62.274  1.00 61.83  ? 604  HOH B O   1 
HETATM 8002 O  O   . HOH T 7 .   ? 1.921   10.627  56.274  1.00 51.75  ? 605  HOH B O   1 
HETATM 8003 O  O   . HOH T 7 .   ? -5.056  -28.827 53.739  1.00 55.87  ? 606  HOH B O   1 
HETATM 8004 O  O   . HOH T 7 .   ? -21.224 -8.655  34.618  1.00 48.32  ? 607  HOH B O   1 
HETATM 8005 O  O   . HOH T 7 .   ? -16.773 -21.241 46.012  1.00 50.39  ? 608  HOH B O   1 
HETATM 8006 O  O   . HOH T 7 .   ? -13.073 -32.236 63.565  1.00 53.01  ? 609  HOH B O   1 
HETATM 8007 O  O   . HOH T 7 .   ? 5.756   -27.225 75.858  1.00 43.19  ? 610  HOH B O   1 
HETATM 8008 O  O   . HOH T 7 .   ? -1.795  1.530   61.305  1.00 45.61  ? 611  HOH B O   1 
HETATM 8009 O  O   . HOH T 7 .   ? 11.145  -7.180  76.803  1.00 53.58  ? 612  HOH B O   1 
HETATM 8010 O  O   . HOH T 7 .   ? -5.519  -23.528 89.792  1.00 50.52  ? 613  HOH B O   1 
HETATM 8011 O  O   . HOH T 7 .   ? 13.920  -14.177 78.783  1.00 37.86  ? 614  HOH B O   1 
HETATM 8012 O  O   . HOH T 7 .   ? 5.398   1.386   48.949  1.00 43.46  ? 615  HOH B O   1 
HETATM 8013 O  O   . HOH T 7 .   ? -4.800  9.860   49.481  1.00 49.59  ? 616  HOH B O   1 
HETATM 8014 O  O   . HOH T 7 .   ? -19.513 -22.700 52.525  1.00 48.42  ? 617  HOH B O   1 
HETATM 8015 O  O   . HOH T 7 .   ? -4.461  12.071  53.801  1.00 47.54  ? 618  HOH B O   1 
HETATM 8016 O  O   . HOH T 7 .   ? -26.006 -11.260 60.099  1.00 48.12  ? 619  HOH B O   1 
HETATM 8017 O  O   . HOH T 7 .   ? 2.368   -49.414 58.638  1.00 54.00  ? 620  HOH B O   1 
HETATM 8018 O  O   . HOH T 7 .   ? -19.933 -9.435  83.473  1.00 54.85  ? 621  HOH B O   1 
HETATM 8019 O  O   . HOH T 7 .   ? 7.661   -43.100 57.890  1.00 47.45  ? 622  HOH B O   1 
HETATM 8020 O  O   . HOH T 7 .   ? 7.184   -35.177 57.726  1.00 50.95  ? 623  HOH B O   1 
HETATM 8021 O  O   . HOH T 7 .   ? -0.771  -20.234 39.472  1.00 52.31  ? 624  HOH B O   1 
HETATM 8022 O  O   . HOH T 7 .   ? -6.112  -4.643  39.009  1.00 37.76  ? 625  HOH B O   1 
HETATM 8023 O  O   . HOH T 7 .   ? -22.210 -1.111  54.517  1.00 44.88  ? 626  HOH B O   1 
HETATM 8024 O  O   . HOH T 7 .   ? -2.286  -36.366 86.630  1.00 52.05  ? 627  HOH B O   1 
HETATM 8025 O  O   . HOH T 7 .   ? 1.480   0.828   42.473  1.00 49.62  ? 628  HOH B O   1 
HETATM 8026 O  O   . HOH T 7 .   ? 8.629   -30.342 87.484  1.00 50.04  ? 629  HOH B O   1 
HETATM 8027 O  O   . HOH T 7 .   ? 17.311  -26.846 56.791  1.00 57.04  ? 630  HOH B O   1 
HETATM 8028 O  O   . HOH T 7 .   ? -16.276 -18.934 76.677  1.00 50.48  ? 631  HOH B O   1 
HETATM 8029 O  O   . HOH T 7 .   ? 22.097  -23.448 67.137  1.00 37.20  ? 632  HOH B O   1 
HETATM 8030 O  O   . HOH T 7 .   ? -21.448 -15.922 36.195  1.00 44.89  ? 633  HOH B O   1 
HETATM 8031 O  O   . HOH T 7 .   ? 7.703   -29.371 89.861  1.00 47.91  ? 634  HOH B O   1 
HETATM 8032 O  O   . HOH T 7 .   ? -13.894 7.831   44.442  1.00 49.97  ? 635  HOH B O   1 
HETATM 8033 O  O   . HOH T 7 .   ? 9.557   -14.962 39.036  1.00 53.29  ? 636  HOH B O   1 
HETATM 8034 O  O   . HOH T 7 .   ? 23.754  -16.903 73.550  1.00 50.41  ? 637  HOH B O   1 
HETATM 8035 O  O   . HOH T 7 .   ? 8.026   -2.031  42.650  1.00 51.04  ? 638  HOH B O   1 
HETATM 8036 O  O   . HOH T 7 .   ? 8.743   -15.408 68.618  1.00 30.14  ? 639  HOH B O   1 
HETATM 8037 O  O   . HOH T 7 .   ? 12.772  -27.512 78.130  1.00 47.82  ? 640  HOH B O   1 
HETATM 8038 O  O   . HOH T 7 .   ? 9.694   -36.876 45.693  1.00 59.77  ? 641  HOH B O   1 
HETATM 8039 O  O   . HOH T 7 .   ? 5.314   -37.290 66.250  1.00 51.10  ? 642  HOH B O   1 
HETATM 8040 O  O   . HOH T 7 .   ? -4.083  -33.603 63.216  1.00 51.42  ? 643  HOH B O   1 
HETATM 8041 O  O   . HOH T 7 .   ? 21.667  -20.907 64.840  1.00 39.83  ? 644  HOH B O   1 
HETATM 8042 O  O   . HOH T 7 .   ? -17.657 -16.465 70.228  1.00 41.84  ? 645  HOH B O   1 
HETATM 8043 O  O   . HOH T 7 .   ? 6.538   -12.946 87.822  1.00 41.95  ? 646  HOH B O   1 
HETATM 8044 O  O   . HOH T 7 .   ? -18.187 -7.525  79.832  1.00 49.96  ? 647  HOH B O   1 
HETATM 8045 O  O   . HOH T 7 .   ? 25.629  -15.455 62.975  1.00 46.96  ? 648  HOH B O   1 
HETATM 8046 O  O   . HOH T 7 .   ? 29.448  -4.389  70.076  1.00 45.43  ? 649  HOH B O   1 
HETATM 8047 O  O   . HOH T 7 .   ? -15.600 7.578   51.363  1.00 42.73  ? 650  HOH B O   1 
HETATM 8048 O  O   . HOH T 7 .   ? -8.525  -28.544 60.326  1.00 36.98  ? 651  HOH B O   1 
HETATM 8049 O  O   . HOH T 7 .   ? 18.450  -2.492  65.612  1.00 55.21  ? 652  HOH B O   1 
HETATM 8050 O  O   . HOH T 7 .   ? -12.102 -27.093 58.768  1.00 43.87  ? 653  HOH B O   1 
HETATM 8051 O  O   . HOH T 7 .   ? -18.612 4.799   62.946  1.00 32.13  ? 654  HOH B O   1 
HETATM 8052 O  O   . HOH T 7 .   ? -21.239 -19.555 62.713  1.00 37.77  ? 655  HOH B O   1 
HETATM 8053 O  O   . HOH T 7 .   ? -22.481 -16.911 53.397  1.00 35.03  ? 656  HOH B O   1 
HETATM 8054 O  O   . HOH T 7 .   ? -14.483 0.953   42.642  1.00 42.78  ? 657  HOH B O   1 
HETATM 8055 O  O   . HOH T 7 .   ? -24.406 -1.528  47.815  1.00 44.63  ? 658  HOH B O   1 
HETATM 8056 O  O   . HOH T 7 .   ? -3.481  -46.541 73.959  1.00 53.49  ? 659  HOH B O   1 
HETATM 8057 O  O   . HOH T 7 .   ? -12.071 -22.483 52.250  1.00 37.65  ? 660  HOH B O   1 
HETATM 8058 O  O   . HOH T 7 .   ? -16.215 -13.915 37.498  1.00 38.24  ? 661  HOH B O   1 
HETATM 8059 O  O   . HOH T 7 .   ? 20.605  -14.266 70.339  1.00 32.75  ? 662  HOH B O   1 
HETATM 8060 O  O   . HOH T 7 .   ? -13.673 7.390   63.818  1.00 44.64  ? 663  HOH B O   1 
HETATM 8061 O  O   . HOH T 7 .   ? -6.348  -12.244 86.749  1.00 45.75  ? 664  HOH B O   1 
HETATM 8062 O  O   . HOH T 7 .   ? 0.863   -9.529  54.364  1.00 31.58  ? 665  HOH B O   1 
HETATM 8063 O  O   . HOH T 7 .   ? -3.713  -33.685 60.840  1.00 49.93  ? 666  HOH B O   1 
HETATM 8064 O  O   . HOH T 7 .   ? -2.442  -18.402 53.666  1.00 35.86  ? 667  HOH B O   1 
HETATM 8065 O  O   . HOH T 7 .   ? 22.234  -8.599  56.951  1.00 38.93  ? 668  HOH B O   1 
HETATM 8066 O  O   . HOH T 7 .   ? -5.799  -24.374 80.743  1.00 34.36  ? 669  HOH B O   1 
HETATM 8067 O  O   . HOH T 7 .   ? -8.229  1.168   67.168  1.00 42.33  ? 670  HOH B O   1 
HETATM 8068 O  O   . HOH T 7 .   ? -4.692  -6.710  35.036  1.00 33.74  ? 671  HOH B O   1 
HETATM 8069 O  O   . HOH T 7 .   ? 7.577   -6.646  72.889  1.00 49.86  ? 672  HOH B O   1 
HETATM 8070 O  O   . HOH T 7 .   ? 9.887   -3.353  47.996  1.00 38.39  ? 673  HOH B O   1 
HETATM 8071 O  O   . HOH T 7 .   ? -4.416  -17.724 59.986  1.00 32.77  ? 674  HOH B O   1 
HETATM 8072 O  O   . HOH T 7 .   ? -1.526  -40.903 62.427  1.00 54.61  ? 675  HOH B O   1 
HETATM 8073 O  O   . HOH T 7 .   ? 13.485  -30.546 50.275  1.00 49.89  ? 676  HOH B O   1 
HETATM 8074 O  O   . HOH T 7 .   ? -17.274 0.784   45.160  1.00 34.44  ? 677  HOH B O   1 
HETATM 8075 O  O   . HOH T 7 .   ? -21.802 -6.494  69.434  1.00 36.50  ? 678  HOH B O   1 
HETATM 8076 O  O   . HOH T 7 .   ? 4.496   -18.138 93.178  1.00 48.35  ? 679  HOH B O   1 
HETATM 8077 O  O   . HOH T 7 .   ? 10.657  -13.011 75.541  1.00 34.11  ? 680  HOH B O   1 
HETATM 8078 O  O   . HOH T 7 .   ? -11.407 8.341   40.823  1.00 55.38  ? 681  HOH B O   1 
HETATM 8079 O  O   . HOH T 7 .   ? 16.433  -26.700 59.642  1.00 46.42  ? 682  HOH B O   1 
HETATM 8080 O  O   . HOH T 7 .   ? -7.089  -26.033 86.229  1.00 35.76  ? 683  HOH B O   1 
HETATM 8081 O  O   . HOH T 7 .   ? -26.952 -0.024  64.339  1.00 47.50  ? 684  HOH B O   1 
HETATM 8082 O  O   . HOH T 7 .   ? -2.353  -41.342 65.253  1.00 53.39  ? 685  HOH B O   1 
HETATM 8083 O  O   . HOH T 7 .   ? 9.660   0.996   53.845  1.00 46.18  ? 686  HOH B O   1 
HETATM 8084 O  O   . HOH T 7 .   ? 3.776   -27.882 89.049  1.00 43.44  ? 687  HOH B O   1 
HETATM 8085 O  O   . HOH T 7 .   ? 18.892  -17.403 43.485  1.00 51.16  ? 688  HOH B O   1 
HETATM 8086 O  O   . HOH T 7 .   ? -1.977  -40.447 68.589  1.00 47.59  ? 689  HOH B O   1 
HETATM 8087 O  O   . HOH T 7 .   ? -3.671  9.999   61.064  1.00 39.62  ? 690  HOH B O   1 
HETATM 8088 O  O   . HOH T 7 .   ? -13.229 -25.496 71.154  1.00 43.74  ? 691  HOH B O   1 
HETATM 8089 O  O   . HOH T 7 .   ? -19.060 -3.359  40.435  1.00 48.09  ? 692  HOH B O   1 
HETATM 8090 O  O   . HOH T 7 .   ? 0.524   -2.095  39.813  1.00 40.10  ? 693  HOH B O   1 
HETATM 8091 O  O   . HOH T 7 .   ? -21.412 9.400   58.271  1.00 48.47  ? 694  HOH B O   1 
HETATM 8092 O  O   . HOH T 7 .   ? -8.634  -11.499 87.057  1.00 49.56  ? 695  HOH B O   1 
HETATM 8093 O  O   . HOH T 7 .   ? 10.368  -9.274  68.693  1.00 37.57  ? 696  HOH B O   1 
HETATM 8094 O  O   . HOH T 7 .   ? -9.382  -23.247 49.238  1.00 56.94  ? 697  HOH B O   1 
HETATM 8095 O  O   . HOH T 7 .   ? 4.993   -10.512 84.378  1.00 49.13  ? 698  HOH B O   1 
HETATM 8096 O  O   . HOH T 7 .   ? -10.600 -18.781 42.359  1.00 54.61  ? 699  HOH B O   1 
HETATM 8097 O  O   . HOH T 7 .   ? 6.294   -14.508 71.985  1.00 30.43  ? 700  HOH B O   1 
HETATM 8098 O  O   . HOH T 7 .   ? -15.001 -14.626 43.516  1.00 42.45  ? 701  HOH B O   1 
HETATM 8099 O  O   . HOH T 7 .   ? -14.565 -25.208 63.828  1.00 36.01  ? 702  HOH B O   1 
HETATM 8100 O  O   . HOH T 7 .   ? -10.488 -28.902 87.217  1.00 44.72  ? 703  HOH B O   1 
HETATM 8101 O  O   . HOH T 7 .   ? 17.084  -23.447 89.057  1.00 43.85  ? 704  HOH B O   1 
HETATM 8102 O  O   . HOH T 7 .   ? 4.117   4.751   50.585  1.00 40.25  ? 705  HOH B O   1 
HETATM 8103 O  O   . HOH T 7 .   ? -15.389 -20.931 73.890  1.00 50.20  ? 706  HOH B O   1 
HETATM 8104 O  O   . HOH T 7 .   ? -14.494 -24.207 67.859  1.00 44.93  ? 707  HOH B O   1 
HETATM 8105 O  O   . HOH T 7 .   ? 11.993  -9.834  66.551  1.00 37.57  ? 708  HOH B O   1 
HETATM 8106 O  O   . HOH T 7 .   ? 9.631   -48.132 54.612  1.00 52.90  ? 709  HOH B O   1 
HETATM 8107 O  O   . HOH T 7 .   ? 8.099   -29.845 80.691  1.00 38.86  ? 710  HOH B O   1 
HETATM 8108 O  O   . HOH T 7 .   ? 15.388  -20.667 91.423  1.00 49.81  ? 711  HOH B O   1 
HETATM 8109 O  O   . HOH T 7 .   ? 1.711   -46.260 63.807  1.00 57.03  ? 712  HOH B O   1 
HETATM 8110 O  O   . HOH T 7 .   ? -15.777 -19.524 70.709  1.00 37.67  ? 713  HOH B O   1 
HETATM 8111 O  O   . HOH T 7 .   ? -19.940 -14.010 68.872  1.00 47.87  ? 714  HOH B O   1 
HETATM 8112 O  O   . HOH T 7 .   ? -10.132 11.622  56.390  1.00 45.27  ? 715  HOH B O   1 
HETATM 8113 O  O   . HOH T 7 .   ? -13.264 8.107   47.301  1.00 46.23  ? 716  HOH B O   1 
HETATM 8114 O  O   . HOH T 7 .   ? 11.789  -18.795 61.608  1.00 31.87  ? 717  HOH B O   1 
HETATM 8115 O  O   . HOH T 7 .   ? 0.612   -12.551 58.760  1.00 30.64  ? 718  HOH B O   1 
HETATM 8116 O  O   . HOH T 7 .   ? -7.076  -14.782 85.766  1.00 35.46  ? 719  HOH B O   1 
HETATM 8117 O  O   . HOH T 7 .   ? -19.925 -1.815  54.060  1.00 40.54  ? 720  HOH B O   1 
HETATM 8118 O  O   . HOH T 7 .   ? -7.241  -12.128 79.389  1.00 35.57  ? 721  HOH B O   1 
HETATM 8119 O  O   . HOH T 7 .   ? -7.511  3.919   44.017  1.00 42.92  ? 722  HOH B O   1 
HETATM 8120 O  O   . HOH T 7 .   ? 3.271   -26.578 45.087  1.00 43.24  ? 723  HOH B O   1 
HETATM 8121 O  O   . HOH T 7 .   ? -26.459 -14.172 58.520  1.00 44.92  ? 724  HOH B O   1 
HETATM 8122 O  O   . HOH T 7 .   ? -13.450 -22.106 74.787  1.00 40.11  ? 725  HOH B O   1 
HETATM 8123 O  O   . HOH T 7 .   ? -0.736  -7.357  73.068  1.00 50.36  ? 726  HOH B O   1 
HETATM 8124 O  O   . HOH T 7 .   ? -2.115  -15.067 67.571  1.00 31.88  ? 727  HOH B O   1 
HETATM 8125 O  O   . HOH T 7 .   ? -3.347  -1.537  42.037  1.00 34.80  ? 728  HOH B O   1 
HETATM 8126 O  O   . HOH T 7 .   ? 4.070   -31.491 53.116  1.00 39.94  ? 729  HOH B O   1 
HETATM 8127 O  O   . HOH T 7 .   ? -2.085  -27.531 49.933  1.00 44.06  ? 730  HOH B O   1 
HETATM 8128 O  O   . HOH T 7 .   ? -1.361  -24.602 43.269  1.00 54.93  ? 731  HOH B O   1 
HETATM 8129 O  O   . HOH T 7 .   ? 12.716  -29.602 83.548  1.00 44.16  ? 732  HOH B O   1 
HETATM 8130 O  O   . HOH T 7 .   ? -26.353 -22.420 57.076  1.00 51.89  ? 733  HOH B O   1 
HETATM 8131 O  O   . HOH T 7 .   ? 8.414   -14.963 79.308  1.00 32.78  ? 734  HOH B O   1 
HETATM 8132 O  O   . HOH T 7 .   ? -9.436  -34.621 70.839  1.00 41.04  ? 735  HOH B O   1 
HETATM 8133 O  O   . HOH T 7 .   ? -9.254  7.724   51.299  1.00 37.24  ? 736  HOH B O   1 
HETATM 8134 O  O   . HOH T 7 .   ? -11.722 -0.093  76.507  1.00 49.70  ? 737  HOH B O   1 
HETATM 8135 O  O   . HOH T 7 .   ? 1.556   -9.339  43.364  1.00 33.54  ? 738  HOH B O   1 
HETATM 8136 O  O   . HOH T 7 .   ? 3.448   -9.750  45.464  1.00 32.73  ? 739  HOH B O   1 
HETATM 8137 O  O   . HOH T 7 .   ? 19.565  -3.087  59.306  1.00 46.07  ? 740  HOH B O   1 
HETATM 8138 O  O   . HOH T 7 .   ? -18.844 4.089   51.331  1.00 39.90  ? 741  HOH B O   1 
HETATM 8139 O  O   . HOH T 7 .   ? -18.988 -8.388  43.883  1.00 47.51  ? 742  HOH B O   1 
HETATM 8140 O  O   . HOH T 7 .   ? 27.837  -0.960  68.418  1.00 53.93  ? 743  HOH B O   1 
HETATM 8141 O  O   . HOH T 7 .   ? -19.579 -24.277 57.192  1.00 39.52  ? 744  HOH B O   1 
HETATM 8142 O  O   . HOH T 7 .   ? 31.651  -10.154 65.558  1.00 50.33  ? 745  HOH B O   1 
HETATM 8143 O  O   . HOH T 7 .   ? -14.711 -6.736  78.018  1.00 38.09  ? 746  HOH B O   1 
HETATM 8144 O  O   . HOH T 7 .   ? 4.668   -35.082 69.164  1.00 44.11  ? 747  HOH B O   1 
HETATM 8145 O  O   . HOH T 7 .   ? -12.454 -9.771  88.162  1.00 47.57  ? 748  HOH B O   1 
HETATM 8146 O  O   . HOH T 7 .   ? -14.628 -35.834 82.249  1.00 55.18  ? 749  HOH B O   1 
HETATM 8147 O  O   . HOH T 7 .   ? 18.573  -20.682 78.291  1.00 51.76  ? 750  HOH B O   1 
HETATM 8148 O  O   . HOH T 7 .   ? -2.049  -10.130 42.055  1.00 30.45  ? 751  HOH B O   1 
HETATM 8149 O  O   . HOH T 7 .   ? 14.765  -19.504 73.605  1.00 34.13  ? 752  HOH B O   1 
HETATM 8150 O  O   . HOH T 7 .   ? 6.086   -38.993 60.740  1.00 46.29  ? 753  HOH B O   1 
HETATM 8151 O  O   . HOH T 7 .   ? 8.306   -4.461  65.436  1.00 47.94  ? 754  HOH B O   1 
HETATM 8152 O  O   . HOH T 7 .   ? -0.334  2.723   45.354  1.00 45.49  ? 755  HOH B O   1 
HETATM 8153 O  O   . HOH T 7 .   ? 0.795   -7.633  41.300  1.00 33.58  ? 756  HOH B O   1 
HETATM 8154 O  O   . HOH T 7 .   ? -11.426 -16.276 41.740  1.00 39.85  ? 757  HOH B O   1 
HETATM 8155 O  O   . HOH T 7 .   ? 20.806  -23.218 86.869  1.00 56.30  ? 758  HOH B O   1 
HETATM 8156 O  O   . HOH T 7 .   ? -11.039 8.840   63.606  1.00 44.37  ? 759  HOH B O   1 
HETATM 8157 O  O   . HOH T 7 .   ? -11.489 -30.402 68.025  1.00 40.61  ? 760  HOH B O   1 
HETATM 8158 O  O   . HOH T 7 .   ? -21.728 -10.953 69.084  1.00 37.70  ? 761  HOH B O   1 
HETATM 8159 O  O   . HOH T 7 .   ? 23.647  -19.051 59.589  1.00 45.18  ? 762  HOH B O   1 
HETATM 8160 O  O   . HOH T 7 .   ? 13.649  -8.100  44.315  1.00 49.89  ? 763  HOH B O   1 
HETATM 8161 O  O   . HOH T 7 .   ? -13.251 -15.122 45.452  1.00 33.33  ? 764  HOH B O   1 
HETATM 8162 O  O   . HOH T 7 .   ? -19.204 2.372   53.828  1.00 40.03  ? 765  HOH B O   1 
HETATM 8163 O  O   . HOH T 7 .   ? 2.843   -16.109 92.405  1.00 48.40  ? 766  HOH B O   1 
HETATM 8164 O  O   . HOH T 7 .   ? -22.770 -17.727 43.815  1.00 47.04  ? 767  HOH B O   1 
HETATM 8165 O  O   . HOH T 7 .   ? 6.646   -20.754 71.273  1.00 30.27  ? 768  HOH B O   1 
HETATM 8166 O  O   . HOH T 7 .   ? -9.178  -21.807 55.279  1.00 37.97  ? 769  HOH B O   1 
HETATM 8167 O  O   . HOH T 7 .   ? 4.854   -22.485 69.949  1.00 31.45  ? 770  HOH B O   1 
HETATM 8168 O  O   . HOH T 7 .   ? 8.707   -31.629 83.529  1.00 50.37  ? 771  HOH B O   1 
HETATM 8169 O  O   . HOH T 7 .   ? 13.887  -28.863 64.490  1.00 46.41  ? 772  HOH B O   1 
HETATM 8170 O  O   . HOH T 7 .   ? 21.429  -20.337 59.258  1.00 40.38  ? 773  HOH B O   1 
HETATM 8171 O  O   . HOH T 7 .   ? 15.667  -29.147 86.081  1.00 46.68  ? 774  HOH B O   1 
HETATM 8172 O  O   . HOH T 7 .   ? -8.190  -1.173  69.024  1.00 40.86  ? 775  HOH B O   1 
HETATM 8173 O  O   . HOH T 7 .   ? -4.674  -1.858  75.309  1.00 57.88  ? 776  HOH B O   1 
HETATM 8174 O  O   . HOH T 7 .   ? -3.179  -5.029  68.946  1.00 43.54  ? 777  HOH B O   1 
HETATM 8175 O  O   . HOH T 7 .   ? 5.317   -16.225 41.466  1.00 46.48  ? 778  HOH B O   1 
HETATM 8176 O  O   . HOH T 7 .   ? -4.707  -44.718 80.674  1.00 34.81  ? 779  HOH B O   1 
HETATM 8177 O  O   . HOH T 7 .   ? 0.126   -34.407 56.087  1.00 46.40  ? 780  HOH B O   1 
HETATM 8178 O  O   . HOH T 7 .   ? 12.880  -14.060 76.342  1.00 36.41  ? 781  HOH B O   1 
HETATM 8179 O  O   . HOH T 7 .   ? 11.353  -7.695  38.879  1.00 53.94  ? 782  HOH B O   1 
HETATM 8180 O  O   . HOH T 7 .   ? 5.571   -1.571  41.873  1.00 55.10  ? 783  HOH B O   1 
HETATM 8181 O  O   . HOH T 7 .   ? -14.259 -19.997 51.167  1.00 35.80  ? 784  HOH B O   1 
HETATM 8182 O  O   . HOH T 7 .   ? -9.562  -18.297 80.935  1.00 40.92  ? 785  HOH B O   1 
HETATM 8183 O  O   . HOH T 7 .   ? -8.732  -13.362 64.067  1.00 33.89  ? 786  HOH B O   1 
HETATM 8184 O  O   . HOH T 7 .   ? -11.007 -29.342 59.475  1.00 46.51  ? 787  HOH B O   1 
HETATM 8185 O  O   . HOH T 7 .   ? 15.891  -7.564  73.357  1.00 50.19  ? 788  HOH B O   1 
HETATM 8186 O  O   . HOH T 7 .   ? 4.063   -29.444 86.888  1.00 46.90  ? 789  HOH B O   1 
HETATM 8187 O  O   . HOH T 7 .   ? -10.870 3.867   48.057  1.00 36.76  ? 790  HOH B O   1 
HETATM 8188 O  O   . HOH T 7 .   ? -13.099 -10.606 39.053  1.00 35.72  ? 791  HOH B O   1 
HETATM 8189 O  O   . HOH T 7 .   ? 18.071  -3.434  47.697  1.00 51.41  ? 792  HOH B O   1 
HETATM 8190 O  O   . HOH T 7 .   ? 23.434  -9.676  68.188  1.00 35.34  ? 793  HOH B O   1 
HETATM 8191 O  O   . HOH T 7 .   ? 12.364  -19.229 86.480  1.00 39.30  ? 794  HOH B O   1 
HETATM 8192 O  O   . HOH T 7 .   ? 21.239  -2.338  61.457  1.00 51.44  ? 795  HOH B O   1 
HETATM 8193 O  O   . HOH T 7 .   ? 4.121   -20.287 68.510  1.00 31.85  ? 796  HOH B O   1 
HETATM 8194 O  O   . HOH T 7 .   ? 18.252  -18.656 81.541  1.00 52.08  ? 797  HOH B O   1 
HETATM 8195 O  O   . HOH T 7 .   ? 0.729   -9.813  72.221  1.00 34.85  ? 798  HOH B O   1 
HETATM 8196 O  O   . HOH T 7 .   ? -14.461 -20.174 78.121  1.00 53.24  ? 799  HOH B O   1 
HETATM 8197 O  O   . HOH T 7 .   ? -22.850 2.403   57.951  1.00 45.55  ? 800  HOH B O   1 
HETATM 8198 O  O   . HOH T 7 .   ? 24.110  -10.105 54.144  1.00 47.41  ? 801  HOH B O   1 
HETATM 8199 O  O   . HOH T 7 .   ? 23.932  -12.293 68.449  1.00 35.16  ? 802  HOH B O   1 
HETATM 8200 O  O   . HOH T 7 .   ? -6.250  -42.109 63.373  1.00 57.27  ? 803  HOH B O   1 
HETATM 8201 O  O   . HOH T 7 .   ? -26.109 -12.887 63.234  1.00 46.96  ? 804  HOH B O   1 
HETATM 8202 O  O   . HOH T 7 .   ? 17.030  -15.321 63.476  1.00 29.97  ? 805  HOH B O   1 
HETATM 8203 O  O   . HOH T 7 .   ? -19.256 -6.445  37.368  1.00 44.21  ? 806  HOH B O   1 
HETATM 8204 O  O   . HOH T 7 .   ? -24.308 -2.635  43.137  1.00 53.76  ? 807  HOH B O   1 
HETATM 8205 O  O   . HOH T 7 .   ? -5.779  -22.671 58.947  1.00 35.93  ? 808  HOH B O   1 
HETATM 8206 O  O   . HOH T 7 .   ? -21.909 -21.984 53.833  1.00 40.90  ? 809  HOH B O   1 
HETATM 8207 O  O   . HOH T 7 .   ? 14.309  -4.783  43.122  1.00 56.37  ? 810  HOH B O   1 
HETATM 8208 O  O   . HOH T 7 .   ? -20.744 -3.522  72.960  1.00 40.60  ? 811  HOH B O   1 
HETATM 8209 O  O   . HOH T 7 .   ? -6.458  -38.338 83.376  1.00 45.33  ? 812  HOH B O   1 
HETATM 8210 O  O   . HOH T 7 .   ? -7.713  14.618  51.239  1.00 60.21  ? 813  HOH B O   1 
HETATM 8211 O  O   . HOH T 7 .   ? 14.403  -24.318 54.005  1.00 40.98  ? 814  HOH B O   1 
HETATM 8212 O  O   . HOH T 7 .   ? -3.581  -25.829 64.778  1.00 31.13  ? 815  HOH B O   1 
HETATM 8213 O  O   . HOH T 7 .   ? 7.259   -17.906 73.131  1.00 30.34  ? 816  HOH B O   1 
HETATM 8214 O  O   . HOH T 7 .   ? 5.496   -4.352  62.844  1.00 44.12  ? 817  HOH B O   1 
HETATM 8215 O  O   . HOH T 7 .   ? 5.394   -38.255 79.831  1.00 50.62  ? 818  HOH B O   1 
HETATM 8216 O  O   . HOH T 7 .   ? -20.112 -10.880 45.263  1.00 42.50  ? 819  HOH B O   1 
HETATM 8217 O  O   . HOH T 7 .   ? 23.077  -18.726 65.465  1.00 35.65  ? 820  HOH B O   1 
HETATM 8218 O  O   . HOH T 7 .   ? 19.151  -21.839 54.475  1.00 42.70  ? 821  HOH B O   1 
HETATM 8219 O  O   . HOH T 7 .   ? -10.705 13.380  46.552  1.00 55.64  ? 822  HOH B O   1 
HETATM 8220 O  O   . HOH T 7 .   ? -19.763 -18.796 70.981  1.00 58.20  ? 823  HOH B O   1 
HETATM 8221 O  O   . HOH T 7 .   ? -24.943 -3.659  58.824  1.00 39.94  ? 824  HOH B O   1 
HETATM 8222 O  O   . HOH T 7 .   ? 25.719  -19.008 54.642  1.00 48.54  ? 825  HOH B O   1 
HETATM 8223 O  O   . HOH T 7 .   ? -1.649  -16.307 35.727  1.00 50.10  ? 826  HOH B O   1 
HETATM 8224 O  O   . HOH T 7 .   ? 4.641   -14.382 39.977  1.00 43.55  ? 827  HOH B O   1 
HETATM 8225 O  O   . HOH T 7 .   ? 8.381   -28.721 73.220  1.00 50.32  ? 828  HOH B O   1 
HETATM 8226 O  O   . HOH T 7 .   ? 8.998   -18.873 92.865  1.00 49.31  ? 829  HOH B O   1 
HETATM 8227 O  O   . HOH T 7 .   ? 8.401   -14.273 76.584  1.00 32.80  ? 830  HOH B O   1 
HETATM 8228 O  O   . HOH T 7 .   ? 15.712  -28.477 88.627  1.00 52.47  ? 831  HOH B O   1 
HETATM 8229 O  O   . HOH T 7 .   ? -19.140 -18.013 66.057  1.00 52.34  ? 832  HOH B O   1 
HETATM 8230 O  O   . HOH T 7 .   ? 18.562  -18.043 84.430  1.00 50.32  ? 833  HOH B O   1 
HETATM 8231 O  O   . HOH T 7 .   ? 12.555  -2.050  55.280  1.00 44.83  ? 834  HOH B O   1 
HETATM 8232 O  O   . HOH T 7 .   ? 20.641  -16.265 50.704  1.00 49.97  ? 835  HOH B O   1 
HETATM 8233 O  O   . HOH T 7 .   ? 3.449   -34.107 53.562  1.00 39.56  ? 836  HOH B O   1 
HETATM 8234 O  O   . HOH T 7 .   ? -20.134 7.793   57.025  1.00 44.20  ? 837  HOH B O   1 
HETATM 8235 O  O   . HOH T 7 .   ? 8.978   -32.817 78.682  1.00 48.77  ? 838  HOH B O   1 
HETATM 8236 O  O   . HOH T 7 .   ? 3.046   7.108   53.217  1.00 48.19  ? 839  HOH B O   1 
HETATM 8237 O  O   . HOH T 7 .   ? -5.349  -7.958  39.590  1.00 32.68  ? 840  HOH B O   1 
HETATM 8238 O  O   . HOH T 7 .   ? 6.813   -42.645 49.285  1.00 56.70  ? 841  HOH B O   1 
HETATM 8239 O  O   . HOH T 7 .   ? -11.578 -31.727 73.608  1.00 37.41  ? 842  HOH B O   1 
HETATM 8240 O  O   . HOH T 7 .   ? -24.581 0.374   65.092  1.00 44.37  ? 843  HOH B O   1 
HETATM 8241 O  O   . HOH T 7 .   ? -7.385  -34.600 86.482  1.00 45.50  ? 844  HOH B O   1 
HETATM 8242 O  O   . HOH T 7 .   ? 22.047  -6.327  70.893  1.00 45.06  ? 845  HOH B O   1 
HETATM 8243 O  O   . HOH T 7 .   ? -8.971  -25.481 52.829  1.00 56.81  ? 846  HOH B O   1 
HETATM 8244 O  O   . HOH T 7 .   ? -13.255 -17.489 82.620  1.00 40.70  ? 847  HOH B O   1 
HETATM 8245 O  O   . HOH T 7 .   ? -8.243  12.978  54.833  1.00 45.75  ? 848  HOH B O   1 
HETATM 8246 O  O   . HOH T 7 .   ? -2.479  -4.646  51.143  1.00 35.77  ? 849  HOH B O   1 
HETATM 8247 O  O   . HOH T 7 .   ? 23.493  -1.470  58.816  1.00 47.30  ? 850  HOH B O   1 
HETATM 8248 O  O   . HOH T 7 .   ? -25.147 -6.762  65.406  1.00 43.11  ? 851  HOH B O   1 
HETATM 8249 O  O   . HOH T 7 .   ? -0.156  -0.470  62.581  1.00 39.96  ? 852  HOH B O   1 
HETATM 8250 O  O   . HOH T 7 .   ? -24.977 -20.898 60.500  1.00 50.74  ? 853  HOH B O   1 
HETATM 8251 O  O   . HOH T 7 .   ? -24.404 -9.058  76.820  1.00 59.96  ? 854  HOH B O   1 
HETATM 8252 O  O   . HOH T 7 .   ? -22.451 -19.536 47.214  1.00 47.07  ? 855  HOH B O   1 
HETATM 8253 O  O   . HOH T 7 .   ? -19.006 -17.147 42.213  1.00 42.88  ? 856  HOH B O   1 
HETATM 8254 O  O   . HOH T 7 .   ? -17.354 10.670  52.908  1.00 53.58  ? 857  HOH B O   1 
HETATM 8255 O  O   . HOH T 7 .   ? 5.574   -38.497 72.132  1.00 48.37  ? 858  HOH B O   1 
HETATM 8256 O  O   . HOH T 7 .   ? 0.353   8.187   52.506  1.00 40.43  ? 859  HOH B O   1 
HETATM 8257 O  O   . HOH T 7 .   ? -22.025 -23.189 56.355  1.00 40.35  ? 860  HOH B O   1 
HETATM 8258 O  O   . HOH T 7 .   ? 11.548  -33.140 68.152  1.00 55.11  ? 861  HOH B O   1 
HETATM 8259 O  O   . HOH T 7 .   ? -3.798  -17.453 43.860  1.00 39.55  ? 862  HOH B O   1 
HETATM 8260 O  O   . HOH T 7 .   ? 24.056  -14.794 60.022  1.00 40.14  ? 863  HOH B O   1 
HETATM 8261 O  O   . HOH T 7 .   ? -13.340 -29.608 69.638  1.00 53.21  ? 864  HOH B O   1 
HETATM 8262 O  O   . HOH T 7 .   ? -10.898 -17.503 84.541  1.00 51.44  ? 865  HOH B O   1 
HETATM 8263 O  O   . HOH T 7 .   ? 10.311  -25.098 92.123  1.00 48.91  ? 866  HOH B O   1 
HETATM 8264 O  O   . HOH T 7 .   ? -10.431 -35.379 79.016  1.00 43.36  ? 867  HOH B O   1 
HETATM 8265 O  O   . HOH T 7 .   ? -1.751  -15.552 91.938  1.00 48.76  ? 868  HOH B O   1 
HETATM 8266 O  O   . HOH T 7 .   ? -1.207  -0.809  65.058  1.00 54.61  ? 869  HOH B O   1 
HETATM 8267 O  O   . HOH T 7 .   ? 3.677   -44.106 52.823  1.00 49.52  ? 870  HOH B O   1 
HETATM 8268 O  O   . HOH T 7 .   ? -9.270  -22.865 87.073  1.00 38.71  ? 871  HOH B O   1 
HETATM 8269 O  O   . HOH T 7 .   ? -4.408  -20.297 53.440  1.00 42.76  ? 872  HOH B O   1 
HETATM 8270 O  O   . HOH T 7 .   ? -0.332  -30.456 44.422  1.00 62.02  ? 873  HOH B O   1 
HETATM 8271 O  O   . HOH T 7 .   ? -1.097  -48.947 76.717  1.00 48.36  ? 874  HOH B O   1 
HETATM 8272 O  O   . HOH T 7 .   ? -24.868 -9.185  57.380  1.00 53.38  ? 875  HOH B O   1 
HETATM 8273 O  O   . HOH T 7 .   ? 4.741   -8.136  75.339  1.00 42.03  ? 876  HOH B O   1 
HETATM 8274 O  O   . HOH T 7 .   ? -0.207  -42.468 66.223  1.00 48.12  ? 877  HOH B O   1 
HETATM 8275 O  O   . HOH T 7 .   ? -2.773  -22.380 56.044  1.00 38.59  ? 878  HOH B O   1 
HETATM 8276 O  O   . HOH T 7 .   ? -1.696  -16.022 47.562  1.00 41.41  ? 879  HOH B O   1 
HETATM 8277 O  O   . HOH T 7 .   ? -6.175  -29.185 58.223  1.00 48.95  ? 880  HOH B O   1 
HETATM 8278 O  O   . HOH T 7 .   ? -7.926  -14.196 41.288  1.00 36.48  ? 881  HOH B O   1 
HETATM 8279 O  O   . HOH T 7 .   ? 25.206  -1.328  62.516  1.00 47.58  ? 882  HOH B O   1 
HETATM 8280 O  O   . HOH T 7 .   ? 16.450  -26.935 68.207  1.00 45.59  ? 883  HOH B O   1 
HETATM 8281 O  O   . HOH T 7 .   ? 10.287  -35.376 55.458  1.00 51.90  ? 884  HOH B O   1 
HETATM 8282 O  O   . HOH T 7 .   ? -11.478 -17.242 44.779  1.00 42.34  ? 885  HOH B O   1 
HETATM 8283 O  O   . HOH T 7 .   ? -16.193 0.286   76.385  1.00 55.96  ? 886  HOH B O   1 
HETATM 8284 O  O   . HOH T 7 .   ? 9.073   -9.426  81.667  1.00 48.87  ? 887  HOH B O   1 
HETATM 8285 O  O   . HOH T 7 .   ? -2.574  -7.066  77.409  1.00 42.85  ? 888  HOH B O   1 
HETATM 8286 O  O   . HOH T 7 .   ? -16.625 -17.624 67.687  1.00 43.98  ? 889  HOH B O   1 
HETATM 8287 O  O   . HOH T 7 .   ? 1.822   -43.339 64.707  1.00 50.69  ? 890  HOH B O   1 
HETATM 8288 O  O   . HOH T 7 .   ? -20.128 -15.144 76.652  1.00 43.65  ? 891  HOH B O   1 
HETATM 8289 O  O   . HOH T 7 .   ? 27.293  -16.140 53.624  1.00 48.67  ? 892  HOH B O   1 
HETATM 8290 O  O   . HOH T 7 .   ? -6.586  9.580   45.879  1.00 48.03  ? 893  HOH B O   1 
HETATM 8291 O  O   . HOH T 7 .   ? 24.787  -1.378  55.717  1.00 57.46  ? 894  HOH B O   1 
HETATM 8292 O  O   . HOH T 7 .   ? 5.712   -31.481 86.953  1.00 51.43  ? 895  HOH B O   1 
HETATM 8293 O  O   . HOH T 7 .   ? -26.088 -10.640 55.504  1.00 44.68  ? 896  HOH B O   1 
HETATM 8294 O  O   . HOH T 7 .   ? -0.097  -32.572 54.626  1.00 48.62  ? 897  HOH B O   1 
HETATM 8295 O  O   . HOH T 7 .   ? 6.661   -8.992  78.884  1.00 51.91  ? 898  HOH B O   1 
HETATM 8296 O  O   . HOH T 7 .   ? -13.832 12.326  60.345  1.00 44.61  ? 899  HOH B O   1 
HETATM 8297 O  O   . HOH T 7 .   ? -9.950  -29.130 56.462  1.00 55.67  ? 900  HOH B O   1 
HETATM 8298 O  O   . HOH T 7 .   ? -2.949  -29.610 51.865  1.00 53.99  ? 901  HOH B O   1 
HETATM 8299 O  O   . HOH T 7 .   ? -19.408 1.778   74.378  1.00 51.28  ? 902  HOH B O   1 
HETATM 8300 O  O   . HOH T 7 .   ? -1.474  -42.743 80.979  1.00 46.14  ? 903  HOH B O   1 
HETATM 8301 O  O   . HOH T 7 .   ? 23.060  -10.692 72.355  1.00 54.33  ? 904  HOH B O   1 
HETATM 8302 O  O   . HOH T 7 .   ? -23.211 -4.461  54.407  1.00 42.27  ? 905  HOH B O   1 
HETATM 8303 O  O   . HOH T 7 .   ? 9.234   -30.422 71.915  1.00 51.17  ? 906  HOH B O   1 
HETATM 8304 O  O   . HOH T 7 .   ? -4.498  -1.403  67.580  1.00 55.34  ? 907  HOH B O   1 
HETATM 8305 O  O   . HOH T 7 .   ? -20.743 -13.369 66.445  1.00 39.63  ? 908  HOH B O   1 
HETATM 8306 O  O   . HOH T 7 .   ? -11.486 -34.941 64.413  1.00 55.36  ? 909  HOH B O   1 
HETATM 8307 O  O   . HOH T 7 .   ? -0.751  -40.071 57.187  1.00 61.40  ? 910  HOH B O   1 
HETATM 8308 O  O   . HOH T 7 .   ? -6.696  -22.376 56.414  1.00 36.19  ? 911  HOH B O   1 
HETATM 8309 O  O   . HOH T 7 .   ? -0.344  10.190  54.826  1.00 41.98  ? 912  HOH B O   1 
HETATM 8310 O  O   . HOH T 7 .   ? -6.569  -19.542 52.182  1.00 43.13  ? 913  HOH B O   1 
HETATM 8311 O  O   . HOH T 7 .   ? 20.848  -18.455 48.974  1.00 53.34  ? 914  HOH B O   1 
HETATM 8312 O  O   . HOH T 7 .   ? -16.734 -24.109 64.764  1.00 54.27  ? 915  HOH B O   1 
HETATM 8313 O  O   . HOH T 7 .   ? -7.343  0.460   36.617  1.00 52.94  ? 916  HOH B O   1 
HETATM 8314 O  O   . HOH T 7 .   ? 31.158  -2.942  58.972  1.00 54.35  ? 917  HOH B O   1 
HETATM 8315 O  O   . HOH T 7 .   ? -5.542  -18.421 47.849  1.00 43.05  ? 918  HOH B O   1 
HETATM 8316 O  O   . HOH T 7 .   ? 0.348   -7.081  77.379  1.00 53.18  ? 919  HOH B O   1 
HETATM 8317 O  O   . HOH T 7 .   ? -10.764 -33.179 80.371  1.00 49.55  ? 920  HOH B O   1 
HETATM 8318 O  O   . HOH T 7 .   ? -21.139 -15.543 65.336  1.00 53.23  ? 921  HOH B O   1 
HETATM 8319 O  O   . HOH T 7 .   ? -13.316 -35.352 79.236  1.00 55.49  ? 922  HOH B O   1 
HETATM 8320 O  O   . HOH T 7 .   ? 6.340   -8.970  82.243  1.00 52.36  ? 923  HOH B O   1 
HETATM 8321 O  O   . HOH T 7 .   ? -9.933  -22.257 81.080  1.00 45.73  ? 924  HOH B O   1 
HETATM 8322 O  O   . HOH T 7 .   ? 20.219  -24.337 54.875  1.00 57.95  ? 925  HOH B O   1 
HETATM 8323 O  O   . HOH T 7 .   ? 30.573  -6.690  58.523  1.00 46.28  ? 926  HOH B O   1 
HETATM 8324 O  O   . HOH T 7 .   ? 21.802  -13.828 49.958  1.00 56.25  ? 927  HOH B O   1 
HETATM 8325 O  O   . HOH T 7 .   ? -12.973 2.840   39.290  1.00 51.82  ? 928  HOH B O   1 
HETATM 8326 O  O   . HOH T 7 .   ? 14.217  -5.878  71.892  1.00 58.66  ? 929  HOH B O   1 
HETATM 8327 O  O   . HOH T 7 .   ? -12.279 -36.023 73.053  1.00 44.91  ? 930  HOH B O   1 
HETATM 8328 O  O   . HOH T 7 .   ? -2.215  -32.795 48.366  1.00 59.43  ? 931  HOH B O   1 
HETATM 8329 O  O   . HOH T 7 .   ? -22.949 -8.846  70.793  1.00 46.92  ? 932  HOH B O   1 
HETATM 8330 O  O   . HOH T 7 .   ? 1.216   -35.347 52.885  1.00 50.95  ? 933  HOH B O   1 
HETATM 8331 O  O   . HOH T 7 .   ? 26.301  -8.653  53.522  1.00 50.30  ? 934  HOH B O   1 
HETATM 8332 O  O   . HOH T 7 .   ? -3.355  -17.847 46.295  1.00 48.33  ? 935  HOH B O   1 
HETATM 8333 O  O   . HOH T 7 .   ? 15.402  -26.487 54.642  1.00 47.40  ? 936  HOH B O   1 
HETATM 8334 O  O   . HOH T 7 .   ? -13.481 -35.772 76.732  1.00 44.47  ? 937  HOH B O   1 
HETATM 8335 O  O   . HOH T 7 .   ? 2.285   -29.054 91.214  1.00 51.57  ? 938  HOH B O   1 
HETATM 8336 O  O   . HOH T 7 .   ? -1.332  6.027   48.781  1.00 54.36  ? 939  HOH B O   1 
HETATM 8337 O  O   . HOH T 7 .   ? -23.982 -19.039 62.300  1.00 45.98  ? 940  HOH B O   1 
HETATM 8338 O  O   . HOH T 7 .   ? 2.690   -7.140  71.723  1.00 56.02  ? 941  HOH B O   1 
HETATM 8339 O  O   . HOH T 7 .   ? 9.888   -20.854 42.197  1.00 50.27  ? 942  HOH B O   1 
HETATM 8340 O  O   . HOH T 7 .   ? 30.486  -2.875  60.986  1.00 53.39  ? 943  HOH B O   1 
HETATM 8341 O  O   . HOH T 7 .   ? 20.109  -2.689  67.811  1.00 57.37  ? 944  HOH B O   1 
HETATM 8342 O  O   . HOH T 7 .   ? 2.584   -7.797  74.112  1.00 57.72  ? 945  HOH B O   1 
HETATM 8343 O  O   . HOH T 7 .   ? 6.367   4.762   48.861  1.00 53.16  ? 946  HOH B O   1 
HETATM 8344 O  O   . HOH T 7 .   ? -24.908 0.768   46.700  1.00 56.74  ? 947  HOH B O   1 
HETATM 8345 O  O   . HOH T 7 .   ? -17.769 -24.860 55.609  1.00 52.59  ? 948  HOH B O   1 
HETATM 8346 O  O   . HOH T 7 .   ? 24.620  -15.493 71.642  1.00 53.09  ? 949  HOH B O   1 
HETATM 8347 O  O   . HOH T 7 .   ? -8.994  14.688  58.323  1.00 54.99  ? 950  HOH B O   1 
HETATM 8348 O  O   . HOH T 7 .   ? -16.818 -26.853 64.422  1.00 65.86  ? 951  HOH B O   1 
HETATM 8349 O  O   . HOH T 7 .   ? 0.383   -16.002 93.827  1.00 58.39  ? 952  HOH B O   1 
HETATM 8350 O  O   . HOH T 7 .   ? -17.322 1.370   40.846  1.00 52.82  ? 953  HOH B O   1 
HETATM 8351 O  O   . HOH T 7 .   ? -21.765 3.364   55.410  1.00 49.03  ? 954  HOH B O   1 
HETATM 8352 O  O   . HOH T 7 .   ? 7.435   -15.487 74.368  1.00 33.67  ? 955  HOH B O   1 
HETATM 8353 O  O   . HOH T 7 .   ? 24.237  -11.112 51.255  1.00 58.02  ? 956  HOH B O   1 
HETATM 8354 O  O   . HOH T 7 .   ? -8.828  -20.366 82.684  1.00 46.90  ? 957  HOH B O   1 
HETATM 8355 O  O   . HOH T 7 .   ? -13.201 5.650   70.295  1.00 52.72  ? 958  HOH B O   1 
HETATM 8356 O  O   . HOH T 7 .   ? -4.937  -23.126 54.760  1.00 43.11  ? 959  HOH B O   1 
HETATM 8357 O  O   . HOH T 7 .   ? 9.891   0.172   51.597  1.00 52.82  ? 960  HOH B O   1 
HETATM 8358 O  O   . HOH T 7 .   ? -7.212  -25.474 88.903  1.00 52.11  ? 961  HOH B O   1 
HETATM 8359 O  O   . HOH T 7 .   ? 4.520   -11.712 87.252  1.00 53.02  ? 962  HOH B O   1 
HETATM 8360 O  O   . HOH T 7 .   ? 1.031   -13.020 36.018  1.00 43.82  ? 963  HOH B O   1 
HETATM 8361 O  O   . HOH T 7 .   ? -1.555  12.460  54.017  1.00 50.37  ? 964  HOH B O   1 
HETATM 8362 O  O   . HOH T 7 .   ? 13.119  -17.646 88.447  1.00 49.21  ? 965  HOH B O   1 
HETATM 8363 O  O   . HOH T 7 .   ? -12.875 -32.430 76.019  1.00 47.53  ? 966  HOH B O   1 
HETATM 8364 O  O   . HOH T 7 .   ? -19.871 -26.386 58.871  1.00 55.79  ? 967  HOH B O   1 
HETATM 8365 O  O   . HOH T 7 .   ? 14.201  -32.095 47.871  1.00 62.89  ? 968  HOH B O   1 
HETATM 8366 O  O   . HOH T 7 .   ? 2.051   6.565   49.846  1.00 53.71  ? 969  HOH B O   1 
HETATM 8367 O  O   . HOH T 7 .   ? 18.442  -25.764 88.995  1.00 56.01  ? 970  HOH B O   1 
HETATM 8368 O  O   . HOH T 7 .   ? 28.032  0.522   66.338  1.00 62.55  ? 971  HOH B O   1 
HETATM 8369 O  O   . HOH T 7 .   ? -11.428 -33.555 69.505  1.00 44.95  ? 972  HOH B O   1 
HETATM 8370 O  O   . HOH T 7 .   ? -8.341  -16.355 87.578  1.00 45.57  ? 973  HOH B O   1 
HETATM 8371 O  O   . HOH T 7 .   ? -12.897 9.279   42.533  1.00 59.33  ? 974  HOH B O   1 
HETATM 8372 O  O   . HOH T 7 .   ? 20.357  -0.786  63.346  1.00 53.56  ? 975  HOH B O   1 
HETATM 8373 O  O   . HOH T 7 .   ? -22.891 3.924   63.251  1.00 42.55  ? 976  HOH B O   1 
HETATM 8374 O  O   . HOH T 7 .   ? -2.435  -45.172 82.139  1.00 43.92  ? 977  HOH B O   1 
HETATM 8375 O  O   . HOH T 7 .   ? 6.476   -50.657 79.604  1.00 53.81  ? 978  HOH B O   1 
HETATM 8376 O  O   . HOH T 7 .   ? -5.562  -20.058 49.907  1.00 42.99  ? 979  HOH B O   1 
HETATM 8377 O  O   . HOH T 7 .   ? 8.194   -4.954  67.966  1.00 58.92  ? 980  HOH B O   1 
HETATM 8378 O  O   . HOH T 7 .   ? -15.175 -21.888 49.517  1.00 43.44  ? 981  HOH B O   1 
HETATM 8379 O  O   . HOH T 7 .   ? 10.004  -6.850  69.435  1.00 53.15  ? 982  HOH B O   1 
HETATM 8380 O  O   . HOH T 7 .   ? -14.760 -1.955  37.407  1.00 59.39  ? 983  HOH B O   1 
HETATM 8381 O  O   . HOH T 7 .   ? 6.492   2.310   46.870  1.00 51.85  ? 984  HOH B O   1 
HETATM 8382 O  O   . HOH T 7 .   ? -11.029 -34.660 76.321  1.00 49.11  ? 985  HOH B O   1 
HETATM 8383 O  O   . HOH T 7 .   ? -17.197 -19.888 68.170  1.00 51.18  ? 986  HOH B O   1 
HETATM 8384 O  O   . HOH T 7 .   ? -2.827  -49.193 78.924  1.00 47.47  ? 987  HOH B O   1 
HETATM 8385 O  O   . HOH T 7 .   ? -20.773 -21.023 65.307  1.00 53.01  ? 988  HOH B O   1 
HETATM 8386 O  O   . HOH T 7 .   ? 30.912  -10.933 68.041  1.00 59.01  ? 989  HOH B O   1 
HETATM 8387 O  O   . HOH T 7 .   ? -3.992  -25.035 49.237  1.00 53.89  ? 990  HOH B O   1 
HETATM 8388 O  O   . HOH T 7 .   ? 23.007  -13.200 71.003  1.00 39.05  ? 991  HOH B O   1 
HETATM 8389 O  O   . HOH T 7 .   ? -24.337 4.991   61.130  1.00 46.48  ? 992  HOH B O   1 
HETATM 8390 O  O   . HOH T 7 .   ? -13.807 -23.416 69.929  1.00 49.37  ? 993  HOH B O   1 
HETATM 8391 O  O   . HOH T 7 .   ? -9.591  -25.352 50.393  1.00 58.80  ? 994  HOH B O   1 
HETATM 8392 O  O   . HOH T 7 .   ? -5.137  3.389   42.763  1.00 50.26  ? 995  HOH B O   1 
HETATM 8393 O  O   . HOH T 7 .   ? -13.559 0.465   40.148  1.00 51.33  ? 996  HOH B O   1 
HETATM 8394 O  O   . HOH T 7 .   ? -15.396 -21.730 71.331  1.00 52.43  ? 997  HOH B O   1 
HETATM 8395 O  O   . HOH T 7 .   ? -2.279  -2.761  68.373  1.00 56.31  ? 998  HOH B O   1 
HETATM 8396 O  O   . HOH T 7 .   ? -13.962 -15.022 41.063  1.00 41.84  ? 999  HOH B O   1 
HETATM 8397 O  O   . HOH T 7 .   ? -7.336  -22.807 48.278  1.00 54.99  ? 1000 HOH B O   1 
HETATM 8398 O  O   . HOH T 7 .   ? -19.086 -3.322  75.158  1.00 50.46  ? 1001 HOH B O   1 
HETATM 8399 O  O   . HOH T 7 .   ? 25.749  -19.033 64.665  1.00 53.94  ? 1002 HOH B O   1 
HETATM 8400 O  O   . HOH T 7 .   ? -27.772 -9.526  58.770  1.00 50.73  ? 1003 HOH B O   1 
HETATM 8401 O  O   . HOH T 7 .   ? -8.806  -14.338 89.796  1.00 61.51  ? 1004 HOH B O   1 
HETATM 8402 O  O   . HOH T 7 .   ? 26.471  -12.461 69.566  1.00 46.44  ? 1005 HOH B O   1 
HETATM 8403 O  O   . HOH T 7 .   ? -18.969 -0.476  75.858  1.00 55.60  ? 1006 HOH B O   1 
HETATM 8404 O  O   . HOH T 7 .   ? -0.075  5.293   46.014  1.00 55.20  ? 1007 HOH B O   1 
HETATM 8405 O  O   . HOH T 7 .   ? -5.859  -1.779  72.815  1.00 49.98  ? 1008 HOH B O   1 
HETATM 8406 O  O   . HOH T 7 .   ? -18.766 12.124  55.944  1.00 54.95  ? 1009 HOH B O   1 
HETATM 8407 O  O   . HOH T 7 .   ? -22.006 5.979   55.718  1.00 53.86  ? 1010 HOH B O   1 
HETATM 8408 O  O   . HOH T 7 .   ? -13.128 -31.924 71.489  1.00 44.82  ? 1011 HOH B O   1 
HETATM 8409 O  O   . HOH T 7 .   ? -25.594 -6.062  57.784  1.00 49.38  ? 1012 HOH B O   1 
HETATM 8410 O  O   . HOH T 7 .   ? -16.656 -22.273 66.659  1.00 53.15  ? 1013 HOH B O   1 
HETATM 8411 O  O   . HOH T 7 .   ? -10.545 -34.193 73.432  1.00 40.68  ? 1014 HOH B O   1 
HETATM 8412 O  O   . HOH T 7 .   ? 4.731   -26.410 42.657  1.00 52.95  ? 1015 HOH B O   1 
HETATM 8413 O  O   . HOH T 7 .   ? -3.093  -32.131 50.709  1.00 58.92  ? 1016 HOH B O   1 
HETATM 8414 O  O   . HOH T 7 .   ? 3.614   9.214   54.899  1.00 53.42  ? 1017 HOH B O   1 
HETATM 8415 O  O   . HOH T 7 .   ? -1.035  -34.067 52.742  1.00 58.25  ? 1018 HOH B O   1 
HETATM 8416 O  O   . HOH T 7 .   ? 22.303  -12.412 47.497  1.00 59.40  ? 1019 HOH B O   1 
HETATM 8417 O  O   . HOH T 7 .   ? 23.952  -10.704 47.733  1.00 65.37  ? 1020 HOH B O   1 
HETATM 8418 O  O   . HOH T 7 .   ? -5.255  -23.065 50.067  1.00 57.18  ? 1021 HOH B O   1 
HETATM 8419 O  O   . HOH T 7 .   ? -22.030 6.862   53.063  1.00 60.62  ? 1022 HOH B O   1 
HETATM 8420 O  O   . HOH T 7 .   ? 2.736   -26.600 40.863  1.00 57.63  ? 1023 HOH B O   1 
# 
