data_3GDP
# 
_entry.id   3GDP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3GDP         
RCSB  RCSB051731   
WWPDB D_1000051731 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1ju2 'triclinic crystal form'    unspecified 
PDB 3gdn 'complex with benzaldehyde' unspecified 
# 
_pdbx_database_status.entry_id                        3GDP 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2009-02-24 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Dreveny, I.' 1 
'Gruber, K.'  2 
'Kratky, C.'  3 
# 
_citation.id                        primary 
_citation.title                     
;Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity.
;
_citation.journal_abbrev            Biochemistry 
_citation.journal_volume            48 
_citation.page_first                3370 
_citation.page_last                 3377 
_citation.year                      2009 
_citation.journal_id_ASTM           BICHAW 
_citation.country                   US 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_id_CSD            0033 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   19256550 
_citation.pdbx_database_id_DOI      10.1021/bi802162s 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Dreveny, I.'        1 
primary 'Andryushkova, A.S.' 2 
primary 'Glieder, A.'        3 
primary 'Gruber, K.'         4 
primary 'Kratky, C.'         5 
# 
_cell.entry_id           3GDP 
_cell.length_a           69.050 
_cell.length_b           93.710 
_cell.length_c           87.260 
_cell.angle_alpha        90.00 
_cell.angle_beta         106.39 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         3GDP 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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     nat 'R-oxynitrile lyase isoenzyme 1'            56535.785 2    4.1.2.10 ? ? ? 
2  non-polymer syn 'ISOPROPYL ALCOHOL'                         60.095    2    ?        ? ? ? 
3  non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'               785.550   2    ?        ? ? ? 
4  non-polymer man N-ACETYL-D-GLUCOSAMINE                      221.208   11   ?        ? ? ? 
5  non-polymer man BETA-L-FUCOSE                               164.156   1    ?        ? ? ? 
6  non-polymer man ALPHA-D-MANNOSE                             180.156   4    ?        ? ? ? 
7  non-polymer man ALPHA-L-FUCOSE                              164.156   2    ?        ? ? ? 
8  non-polymer man BETA-D-MANNOSE                              180.156   2    ?        ? ? ? 
9  non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208   1    ?        ? ? ? 
10 water       nat water                                       18.015    1589 ?        ? ? ? 
# 
_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       
;LATTSDHDFSYLSFAYDATDLELEGSYDYVIVGGGTSGCPLAATLSEKYKVLVLERGSLPTAYPNVLTADGFVYNLQQED
DGKTPVERFVSEDGIDNVRGRVLGGTSIINAGVYARANTSIYSASGVDWDMDLVNQTYEWVEDTIVYKPNSQSWQSVTKT
AFLEAGVHPNHGFSLDHEEGTRITGSTFDNKGTRHAADELLNKGNSNNLRVGVHASVEKIIFSNAPGLTATGVIYRDSNG
TPHQAFVRSKGEVIVSAGTIGTPQLLLLSGVGPESYLSSLNIPVVLSHPYVGQFLHDNPRNFINILPPNPIEPTIVTVLG
ISNDFYQCSFSSLPFTTPPFGFFPSSSYPLPNSTFAHFASKVAGPLSYGSLTLKSSSNVRVSPNVKFNYYSNLTDLSHCV
SGMKKIGELLSTDALKPYKVEDLPGVEGFNILGIPLPKDQTDDAAFETFCRESVASYWHYHGGCLVGKVLDGDFRVTGIN
ALRVVDGSTFPYTPASHPQGFYLMLGRYVGIKILQERSASD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;LATTSDHDFSYLSFAYDATDLELEGSYDYVIVGGGTSGCPLAATLSEKYKVLVLERGSLPTAYPNVLTADGFVYNLQQED
DGKTPVERFVSEDGIDNVRGRVLGGTSIINAGVYARANTSIYSASGVDWDMDLVNQTYEWVEDTIVYKPNSQSWQSVTKT
AFLEAGVHPNHGFSLDHEEGTRITGSTFDNKGTRHAADELLNKGNSNNLRVGVHASVEKIIFSNAPGLTATGVIYRDSNG
TPHQAFVRSKGEVIVSAGTIGTPQLLLLSGVGPESYLSSLNIPVVLSHPYVGQFLHDNPRNFINILPPNPIEPTIVTVLG
ISNDFYQCSFSSLPFTTPPFGFFPSSSYPLPNSTFAHFASKVAGPLSYGSLTLKSSSNVRVSPNVKFNYYSNLTDLSHCV
SGMKKIGELLSTDALKPYKVEDLPGVEGFNILGIPLPKDQTDDAAFETFCRESVASYWHYHGGCLVGKVLDGDFRVTGIN
ALRVVDGSTFPYTPASHPQGFYLMLGRYVGIKILQERSASD
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LEU n 
1 2   ALA n 
1 3   THR n 
1 4   THR n 
1 5   SER n 
1 6   ASP n 
1 7   HIS n 
1 8   ASP n 
1 9   PHE n 
1 10  SER n 
1 11  TYR n 
1 12  LEU n 
1 13  SER n 
1 14  PHE n 
1 15  ALA n 
1 16  TYR n 
1 17  ASP n 
1 18  ALA n 
1 19  THR n 
1 20  ASP n 
1 21  LEU n 
1 22  GLU n 
1 23  LEU n 
1 24  GLU n 
1 25  GLY n 
1 26  SER n 
1 27  TYR n 
1 28  ASP n 
1 29  TYR n 
1 30  VAL n 
1 31  ILE n 
1 32  VAL n 
1 33  GLY n 
1 34  GLY n 
1 35  GLY n 
1 36  THR n 
1 37  SER n 
1 38  GLY n 
1 39  CYS n 
1 40  PRO n 
1 41  LEU n 
1 42  ALA n 
1 43  ALA n 
1 44  THR n 
1 45  LEU n 
1 46  SER n 
1 47  GLU n 
1 48  LYS n 
1 49  TYR n 
1 50  LYS n 
1 51  VAL n 
1 52  LEU n 
1 53  VAL n 
1 54  LEU n 
1 55  GLU n 
1 56  ARG n 
1 57  GLY n 
1 58  SER n 
1 59  LEU n 
1 60  PRO n 
1 61  THR n 
1 62  ALA n 
1 63  TYR n 
1 64  PRO n 
1 65  ASN n 
1 66  VAL n 
1 67  LEU n 
1 68  THR n 
1 69  ALA n 
1 70  ASP n 
1 71  GLY n 
1 72  PHE n 
1 73  VAL n 
1 74  TYR n 
1 75  ASN n 
1 76  LEU n 
1 77  GLN n 
1 78  GLN n 
1 79  GLU n 
1 80  ASP n 
1 81  ASP n 
1 82  GLY n 
1 83  LYS n 
1 84  THR n 
1 85  PRO n 
1 86  VAL n 
1 87  GLU n 
1 88  ARG n 
1 89  PHE n 
1 90  VAL n 
1 91  SER n 
1 92  GLU n 
1 93  ASP n 
1 94  GLY n 
1 95  ILE n 
1 96  ASP n 
1 97  ASN n 
1 98  VAL n 
1 99  ARG n 
1 100 GLY n 
1 101 ARG n 
1 102 VAL n 
1 103 LEU n 
1 104 GLY n 
1 105 GLY n 
1 106 THR n 
1 107 SER n 
1 108 ILE n 
1 109 ILE n 
1 110 ASN n 
1 111 ALA n 
1 112 GLY n 
1 113 VAL n 
1 114 TYR n 
1 115 ALA n 
1 116 ARG n 
1 117 ALA n 
1 118 ASN n 
1 119 THR n 
1 120 SER n 
1 121 ILE n 
1 122 TYR n 
1 123 SER n 
1 124 ALA n 
1 125 SER n 
1 126 GLY n 
1 127 VAL n 
1 128 ASP n 
1 129 TRP n 
1 130 ASP n 
1 131 MET n 
1 132 ASP n 
1 133 LEU n 
1 134 VAL n 
1 135 ASN n 
1 136 GLN n 
1 137 THR n 
1 138 TYR n 
1 139 GLU n 
1 140 TRP n 
1 141 VAL n 
1 142 GLU n 
1 143 ASP n 
1 144 THR n 
1 145 ILE n 
1 146 VAL n 
1 147 TYR n 
1 148 LYS n 
1 149 PRO n 
1 150 ASN n 
1 151 SER n 
1 152 GLN n 
1 153 SER n 
1 154 TRP n 
1 155 GLN n 
1 156 SER n 
1 157 VAL n 
1 158 THR n 
1 159 LYS n 
1 160 THR n 
1 161 ALA n 
1 162 PHE n 
1 163 LEU n 
1 164 GLU n 
1 165 ALA n 
1 166 GLY n 
1 167 VAL n 
1 168 HIS n 
1 169 PRO n 
1 170 ASN n 
1 171 HIS n 
1 172 GLY n 
1 173 PHE n 
1 174 SER n 
1 175 LEU n 
1 176 ASP n 
1 177 HIS n 
1 178 GLU n 
1 179 GLU n 
1 180 GLY n 
1 181 THR n 
1 182 ARG n 
1 183 ILE n 
1 184 THR n 
1 185 GLY n 
1 186 SER n 
1 187 THR n 
1 188 PHE n 
1 189 ASP n 
1 190 ASN n 
1 191 LYS n 
1 192 GLY n 
1 193 THR n 
1 194 ARG n 
1 195 HIS n 
1 196 ALA n 
1 197 ALA n 
1 198 ASP n 
1 199 GLU n 
1 200 LEU n 
1 201 LEU n 
1 202 ASN n 
1 203 LYS n 
1 204 GLY n 
1 205 ASN n 
1 206 SER n 
1 207 ASN n 
1 208 ASN n 
1 209 LEU n 
1 210 ARG n 
1 211 VAL n 
1 212 GLY n 
1 213 VAL n 
1 214 HIS n 
1 215 ALA n 
1 216 SER n 
1 217 VAL n 
1 218 GLU n 
1 219 LYS n 
1 220 ILE n 
1 221 ILE n 
1 222 PHE n 
1 223 SER n 
1 224 ASN n 
1 225 ALA n 
1 226 PRO n 
1 227 GLY n 
1 228 LEU n 
1 229 THR n 
1 230 ALA n 
1 231 THR n 
1 232 GLY n 
1 233 VAL n 
1 234 ILE n 
1 235 TYR n 
1 236 ARG n 
1 237 ASP n 
1 238 SER n 
1 239 ASN n 
1 240 GLY n 
1 241 THR n 
1 242 PRO n 
1 243 HIS n 
1 244 GLN n 
1 245 ALA n 
1 246 PHE n 
1 247 VAL n 
1 248 ARG n 
1 249 SER n 
1 250 LYS n 
1 251 GLY n 
1 252 GLU n 
1 253 VAL n 
1 254 ILE n 
1 255 VAL n 
1 256 SER n 
1 257 ALA n 
1 258 GLY n 
1 259 THR n 
1 260 ILE n 
1 261 GLY n 
1 262 THR n 
1 263 PRO n 
1 264 GLN n 
1 265 LEU n 
1 266 LEU n 
1 267 LEU n 
1 268 LEU n 
1 269 SER n 
1 270 GLY n 
1 271 VAL n 
1 272 GLY n 
1 273 PRO n 
1 274 GLU n 
1 275 SER n 
1 276 TYR n 
1 277 LEU n 
1 278 SER n 
1 279 SER n 
1 280 LEU n 
1 281 ASN n 
1 282 ILE n 
1 283 PRO n 
1 284 VAL n 
1 285 VAL n 
1 286 LEU n 
1 287 SER n 
1 288 HIS n 
1 289 PRO n 
1 290 TYR n 
1 291 VAL n 
1 292 GLY n 
1 293 GLN n 
1 294 PHE n 
1 295 LEU n 
1 296 HIS n 
1 297 ASP n 
1 298 ASN n 
1 299 PRO n 
1 300 ARG n 
1 301 ASN n 
1 302 PHE n 
1 303 ILE n 
1 304 ASN n 
1 305 ILE n 
1 306 LEU n 
1 307 PRO n 
1 308 PRO n 
1 309 ASN n 
1 310 PRO n 
1 311 ILE n 
1 312 GLU n 
1 313 PRO n 
1 314 THR n 
1 315 ILE n 
1 316 VAL n 
1 317 THR n 
1 318 VAL n 
1 319 LEU n 
1 320 GLY n 
1 321 ILE n 
1 322 SER n 
1 323 ASN n 
1 324 ASP n 
1 325 PHE n 
1 326 TYR n 
1 327 GLN n 
1 328 CYS n 
1 329 SER n 
1 330 PHE n 
1 331 SER n 
1 332 SER n 
1 333 LEU n 
1 334 PRO n 
1 335 PHE n 
1 336 THR n 
1 337 THR n 
1 338 PRO n 
1 339 PRO n 
1 340 PHE n 
1 341 GLY n 
1 342 PHE n 
1 343 PHE n 
1 344 PRO n 
1 345 SER n 
1 346 SER n 
1 347 SER n 
1 348 TYR n 
1 349 PRO n 
1 350 LEU n 
1 351 PRO n 
1 352 ASN n 
1 353 SER n 
1 354 THR n 
1 355 PHE n 
1 356 ALA n 
1 357 HIS n 
1 358 PHE n 
1 359 ALA n 
1 360 SER n 
1 361 LYS n 
1 362 VAL n 
1 363 ALA n 
1 364 GLY n 
1 365 PRO n 
1 366 LEU n 
1 367 SER n 
1 368 TYR n 
1 369 GLY n 
1 370 SER n 
1 371 LEU n 
1 372 THR n 
1 373 LEU n 
1 374 LYS n 
1 375 SER n 
1 376 SER n 
1 377 SER n 
1 378 ASN n 
1 379 VAL n 
1 380 ARG n 
1 381 VAL n 
1 382 SER n 
1 383 PRO n 
1 384 ASN n 
1 385 VAL n 
1 386 LYS n 
1 387 PHE n 
1 388 ASN n 
1 389 TYR n 
1 390 TYR n 
1 391 SER n 
1 392 ASN n 
1 393 LEU n 
1 394 THR n 
1 395 ASP n 
1 396 LEU n 
1 397 SER n 
1 398 HIS n 
1 399 CYS n 
1 400 VAL n 
1 401 SER n 
1 402 GLY n 
1 403 MET n 
1 404 LYS n 
1 405 LYS n 
1 406 ILE n 
1 407 GLY n 
1 408 GLU n 
1 409 LEU n 
1 410 LEU n 
1 411 SER n 
1 412 THR n 
1 413 ASP n 
1 414 ALA n 
1 415 LEU n 
1 416 LYS n 
1 417 PRO n 
1 418 TYR n 
1 419 LYS n 
1 420 VAL n 
1 421 GLU n 
1 422 ASP n 
1 423 LEU n 
1 424 PRO n 
1 425 GLY n 
1 426 VAL n 
1 427 GLU n 
1 428 GLY n 
1 429 PHE n 
1 430 ASN n 
1 431 ILE n 
1 432 LEU n 
1 433 GLY n 
1 434 ILE n 
1 435 PRO n 
1 436 LEU n 
1 437 PRO n 
1 438 LYS n 
1 439 ASP n 
1 440 GLN n 
1 441 THR n 
1 442 ASP n 
1 443 ASP n 
1 444 ALA n 
1 445 ALA n 
1 446 PHE n 
1 447 GLU n 
1 448 THR n 
1 449 PHE n 
1 450 CYS n 
1 451 ARG n 
1 452 GLU n 
1 453 SER n 
1 454 VAL n 
1 455 ALA n 
1 456 SER n 
1 457 TYR n 
1 458 TRP n 
1 459 HIS n 
1 460 TYR n 
1 461 HIS n 
1 462 GLY n 
1 463 GLY n 
1 464 CYS n 
1 465 LEU n 
1 466 VAL n 
1 467 GLY n 
1 468 LYS n 
1 469 VAL n 
1 470 LEU n 
1 471 ASP n 
1 472 GLY n 
1 473 ASP n 
1 474 PHE n 
1 475 ARG n 
1 476 VAL n 
1 477 THR n 
1 478 GLY n 
1 479 ILE n 
1 480 ASN n 
1 481 ALA n 
1 482 LEU n 
1 483 ARG n 
1 484 VAL n 
1 485 VAL n 
1 486 ASP n 
1 487 GLY n 
1 488 SER n 
1 489 THR n 
1 490 PHE n 
1 491 PRO n 
1 492 TYR n 
1 493 THR n 
1 494 PRO n 
1 495 ALA n 
1 496 SER n 
1 497 HIS n 
1 498 PRO n 
1 499 GLN n 
1 500 GLY n 
1 501 PHE n 
1 502 TYR n 
1 503 LEU n 
1 504 MET n 
1 505 LEU n 
1 506 GLY n 
1 507 ARG n 
1 508 TYR n 
1 509 VAL n 
1 510 GLY n 
1 511 ILE n 
1 512 LYS n 
1 513 ILE n 
1 514 LEU n 
1 515 GLN n 
1 516 GLU n 
1 517 ARG n 
1 518 SER n 
1 519 ALA n 
1 520 SER n 
1 521 ASP n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                'sweet almond' 
_entity_src_nat.pdbx_organism_scientific   'Prunus dulcis' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      3755 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q945K2_PRUDU 
_struct_ref.pdbx_db_accession          Q945K2 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LATTSDHDFSYLSFAYDATDLELEGSYDYVIVGGGTSGCPLAATLSEKYKVLVLERGSLPTAYPNVLTADGFVYNLQQED
DGKTPVERFVSEDGIDNVRGRVLGGTSIINAGVYARANTSIYSASGVDWDMDLVNQTYEWVEDTIVYKPNSQSWQSVTKT
AFLEAGVHPNHGFSLDHEEGTRITGSTFDNKGTRHAADELLNKGNSNNLRVGVHASVEKIIFSNAPGLTATGVIYRDSNG
TPHQAFVRSKGEVIVSAGTIGTPQLLLLSGVGPESYLSSLNIPVVLSHPYVGQFLHDNPRNFINILPPNPIEPTIVTVLG
ISNDFYQCSFSSLPFTTPPFGFFPSASYPLPNSTFAHFASKVAGPLSYGSLTLKSSSNVRVSPNVKFNYYSNLTDLSHCV
SGMKKIGELLSTDALKPYKVEDLPGVEGFNILGIPLPKDQTDDAAFETFCRESVASYWHYHGGCLVGKVLDGDFRVTGIN
ALRVVDGSTFPYTPASHPQGFYLMLGRYVGIKILQERSASD
;
_struct_ref.pdbx_align_begin           28 
_struct_ref.pdbx_db_isoform            ? 
# 
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 3GDP A 1 ? 521 ? Q945K2 28 ? 548 ? 1 521 
2 1 3GDP B 1 ? 521 ? Q945K2 28 ? 548 ? 1 521 
# 
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 3GDP SER A 346 ? UNP Q945K2 ALA 373 'SEE REMARK 999' 346 1 
2 3GDP SER B 346 ? UNP Q945K2 ALA 373 'SEE REMARK 999' 346 2 
# 
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 
BMA D-saccharide        . BETA-D-MANNOSE                              ?                        'C6 H12 O6'         180.156 
CYS 'L-peptide linking' y CYSTEINE                                    ?                        'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'               ?                        'C27 H33 N9 O15 P2' 785.550 
FUC saccharide          . ALPHA-L-FUCOSE                              ?                        'C6 H12 O5'         164.156 
FUL L-saccharide        . BETA-L-FUCOSE                               6-DEOXY-BETA-L-GALACTOSE 'C6 H12 O5'         164.156 
GLN 'L-peptide linking' y GLUTAMINE                                   ?                        'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                             ?                        'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                     ?                        'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                   ?                        'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                       ?                        'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                  ?                        'C6 H13 N O2'       131.173 
IPA non-polymer         . 'ISOPROPYL ALCOHOL'                         2-PROPANOL               'C3 H8 O'           60.095  
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 
MAN D-saccharide        . ALPHA-D-MANNOSE                             ?                        'C6 H12 O6'         180.156 
MET 'L-peptide linking' y METHIONINE                                  ?                        'C5 H11 N O2 S'     149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE                      ?                        'C8 H15 N O6'       221.208 
NDG D-saccharide        . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ?                        'C8 H15 N O6'       221.208 
PHE 'L-peptide linking' y PHENYLALANINE                               ?                        'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                     ?                        'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                      ?                        'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                   ?                        'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                  ?                        'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                    ?                        'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                      ?                        'C5 H11 N O2'       117.146 
# 
_exptl.crystals_number   1 
_exptl.entry_id          3GDP 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.40 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   48.65 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    '20% w/v PEG-4000, 16% v/v isopropanol, pH 7.0, VAPOR DIFFUSION, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR scanner 345 mm plate' 
_diffrn_detector.pdbx_collection_date   2001-06-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8439 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X11' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.8439 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, Hamburg' 
_diffrn_source.pdbx_synchrotron_beamline   X11 
# 
_reflns.entry_id                     3GDP 
_reflns.B_iso_Wilson_estimate        15.300 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.d_resolution_high            1.57 
_reflns.d_resolution_low             39.0 
_reflns.number_all                   143518 
_reflns.number_obs                   143518 
_reflns.percent_possible_obs         96.7 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.058 
_reflns.pdbx_netI_over_sigmaI        11.2 
_reflns.pdbx_redundancy              3.4 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.57 
_reflns_shell.d_res_low              1.67 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.percent_possible_all   89.9 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.meanI_over_sigI_obs    2.6 
_reflns_shell.pdbx_Rsym_value        0.385 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3GDP 
_refine.ls_d_res_high                            1.570 
_refine.ls_d_res_low                             38.250 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               2001043.000 
_refine.pdbx_data_cutoff_low_absF                0.000 
_refine.ls_percent_reflns_obs                    95.600 
_refine.ls_number_reflns_obs                     142082 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'BULK SOLVENT MODEL USED' 
_refine.ls_R_factor_R_work                       0.186 
_refine.ls_R_factor_R_free                       0.210 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  14166 
_refine.ls_R_factor_R_free_error                 0.002 
_refine.B_iso_mean                               15.642 
_refine.solvent_model_param_bsol                 46.627 
_refine.solvent_model_param_ksol                 0.350 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.aniso_B[1][1]                            -1.250 
_refine.aniso_B[2][2]                            4.900 
_refine.aniso_B[3][3]                            -3.660 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            1.130 
_refine.aniso_B[2][3]                            0.000 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.pdbx_method_to_determine_struct          ? 
_refine.B_iso_max                                53.42 
_refine.B_iso_min                                4.39 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'pdb entry 1ju2' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        3GDP 
_refine_analyze.Luzzati_coordinate_error_obs    0.170 
_refine_analyze.Luzzati_sigma_a_obs             0.160 
_refine_analyze.Luzzati_d_res_low_obs           5.000 
_refine_analyze.Luzzati_coordinate_error_free   0.200 
_refine_analyze.Luzzati_sigma_a_free            0.170 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        7988 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         378 
_refine_hist.number_atoms_solvent             1589 
_refine_hist.number_atoms_total               9955 
_refine_hist.d_res_high                       1.570 
_refine_hist.d_res_low                        38.250 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d           ? 0.006  ?     ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        ? 1.400  ?     ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d ? 24.400 ?     ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d ? 0.870  ?     ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it        ? 0.950  1.500 ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it       ? 1.370  2.000 ? 'X-RAY DIFFRACTION' ? 
c_scbond_it        ? 1.640  2.000 ? 'X-RAY DIFFRACTION' ? 
c_scangle_it       ? 2.370  2.500 ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.570 
_refine_ls_shell.d_res_low                        1.670 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.percent_reflns_obs               91.700 
_refine_ls_shell.number_reflns_R_work             20323 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.257 
_refine_ls_shell.R_factor_R_free                  0.280 
_refine_ls_shell.percent_reflns_R_free            9.900 
_refine_ls_shell.number_reflns_R_free             2238 
_refine_ls_shell.R_factor_R_free_error            0.006 
_refine_ls_shell.number_reflns_all                22561 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 protein_rep.param  protein.top      'X-RAY DIFFRACTION' 
2 carbohydrate.param iso.top          'X-RAY DIFFRACTION' 
3 water_rep.param    fad.top          'X-RAY DIFFRACTION' 
4 iso.par            water.top        'X-RAY DIFFRACTION' 
5 fad.par            carbohydrate.top 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3GDP 
_struct.title                     'Hydroxynitrile lyase from almond, monoclinic crystal form' 
_struct.pdbx_descriptor           'R-oxynitrile lyase isoenzyme 1 (E.C.4.1.2.10)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            N 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3GDP 
_struct_keywords.pdbx_keywords   LYASE 
_struct_keywords.text            'HYDROXYNITRILE LYASE, FLAVIN, GMC OXIDOREDUCTASE, ALMOND, CYANOGENESIS, Flavoprotein, Lyase' 
# 
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 4  ? 
G  N N 4  ? 
H  N N 5  ? 
I  N N 6  ? 
J  N N 6  ? 
K  N N 4  ? 
L  N N 4  ? 
M  N N 7  ? 
N  N N 4  ? 
O  N N 2  ? 
P  N N 3  ? 
Q  N N 4  ? 
R  N N 4  ? 
S  N N 7  ? 
T  N N 8  ? 
U  N N 6  ? 
V  N N 4  ? 
W  N N 4  ? 
X  N N 8  ? 
Y  N N 6  ? 
Z  N N 9  ? 
AA N N 4  ? 
BA N N 10 ? 
CA N N 10 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  PHE A 9   ? SER A 13  ? PHE A 9   SER A 13  5 ? 5  
HELX_P HELX_P2  2  THR A 19  ? LEU A 21  ? THR A 19  LEU A 21  5 ? 3  
HELX_P HELX_P3  3  SER A 37  ? SER A 46  ? SER A 37  SER A 46  1 ? 10 
HELX_P HELX_P4  4  LEU A 59  ? ASP A 70  ? LEU A 59  ASP A 70  5 ? 12 
HELX_P HELX_P5  5  GLY A 71  ? GLN A 78  ? GLY A 71  GLN A 78  1 ? 8  
HELX_P HELX_P6  6  GLY A 104 ? ILE A 109 ? GLY A 104 ILE A 109 5 ? 6  
HELX_P HELX_P7  7  ASP A 130 ? VAL A 146 ? ASP A 130 VAL A 146 1 ? 17 
HELX_P HELX_P8  8  GLN A 152 ? ALA A 165 ? GLN A 152 ALA A 165 1 ? 14 
HELX_P HELX_P9  9  ALA A 196 ? GLY A 204 ? ALA A 196 GLY A 204 5 ? 9  
HELX_P HELX_P10 10 ALA A 257 ? SER A 269 ? ALA A 257 SER A 269 1 ? 13 
HELX_P HELX_P11 11 PRO A 273 ? LEU A 280 ? PRO A 273 LEU A 280 1 ? 8  
HELX_P HELX_P12 12 ASN A 392 ? SER A 411 ? ASN A 392 SER A 411 1 ? 20 
HELX_P HELX_P13 13 THR A 412 ? LYS A 419 ? THR A 412 LYS A 419 5 ? 8  
HELX_P HELX_P14 14 ASP A 442 ? VAL A 454 ? ASP A 442 VAL A 454 1 ? 13 
HELX_P HELX_P15 15 ASP A 486 ? PHE A 490 ? ASP A 486 PHE A 490 5 ? 5  
HELX_P HELX_P16 16 PRO A 498 ? SER A 520 ? PRO A 498 SER A 520 1 ? 23 
HELX_P HELX_P17 17 PHE B 9   ? SER B 13  ? PHE B 9   SER B 13  5 ? 5  
HELX_P HELX_P18 18 THR B 19  ? LEU B 21  ? THR B 19  LEU B 21  5 ? 3  
HELX_P HELX_P19 19 SER B 37  ? SER B 46  ? SER B 37  SER B 46  1 ? 10 
HELX_P HELX_P20 20 LEU B 59  ? ASP B 70  ? LEU B 59  ASP B 70  5 ? 12 
HELX_P HELX_P21 21 GLY B 71  ? GLN B 78  ? GLY B 71  GLN B 78  1 ? 8  
HELX_P HELX_P22 22 GLY B 104 ? ILE B 109 ? GLY B 104 ILE B 109 5 ? 6  
HELX_P HELX_P23 23 ASP B 130 ? VAL B 146 ? ASP B 130 VAL B 146 1 ? 17 
HELX_P HELX_P24 24 GLN B 152 ? ALA B 165 ? GLN B 152 ALA B 165 1 ? 14 
HELX_P HELX_P25 25 ALA B 196 ? GLY B 204 ? ALA B 196 GLY B 204 5 ? 9  
HELX_P HELX_P26 26 ALA B 257 ? SER B 269 ? ALA B 257 SER B 269 1 ? 13 
HELX_P HELX_P27 27 PRO B 273 ? LEU B 280 ? PRO B 273 LEU B 280 1 ? 8  
HELX_P HELX_P28 28 ASN B 392 ? SER B 411 ? ASN B 392 SER B 411 1 ? 20 
HELX_P HELX_P29 29 THR B 412 ? LYS B 419 ? THR B 412 LYS B 419 5 ? 8  
HELX_P HELX_P30 30 ASP B 442 ? VAL B 454 ? ASP B 442 VAL B 454 1 ? 13 
HELX_P HELX_P31 31 PRO B 498 ? ASP B 521 ? PRO B 498 ASP B 521 1 ? 24 
# 
_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 
disulf1  disulf ? ? A CYS 399 SG  ? ? ? 1_555 A  CYS 450 SG ? ? A CYS 399 A CYS 450 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf2  disulf ? ? B CYS 399 SG  ? ? ? 1_555 B  CYS 450 SG ? ? B CYS 399 B CYS 450 1_555 ? ? ? ? ? ? ? 2.029 ? 
covale1  covale ? ? A ASN 118 ND2 ? ? ? 1_555 E  NAG .   C1 ? ? A ASN 118 A NAG 524 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale2  covale ? ? A ASN 135 ND2 ? ? ? 1_555 F  NAG .   C1 ? ? A ASN 135 A NAG 525 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale3  covale ? ? A ASN 352 ND2 ? ? ? 1_555 N  NAG .   C1 ? ? A ASN 352 A NAG 533 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale4  covale ? ? A ASN 392 ND2 ? ? ? 1_555 K  NAG .   C1 ? ? A ASN 392 A NAG 530 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale5  covale ? ? B ASN 118 ND2 ? ? ? 1_555 AA NAG .   C1 ? ? B ASN 118 B NAG 534 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale6  covale ? ? B ASN 135 ND2 ? ? ? 1_555 V  NAG .   C1 ? ? B ASN 135 B NAG 529 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale7  covale ? ? B ASN 392 ND2 ? ? ? 1_555 R  NAG .   C1 ? ? B ASN 392 B NAG 525 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale8  covale ? ? F NAG .   O3  ? ? ? 1_555 H  FUL .   C1 ? ? A NAG 525 A FUL 527 1_555 ? ? ? ? ? ? ? 1.399 ? 
covale9  covale ? ? F NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? A NAG 525 A NAG 526 1_555 ? ? ? ? ? ? ? 1.393 ? 
covale10 covale ? ? G NAG .   O4  ? ? ? 1_555 I  MAN .   C1 ? ? A NAG 526 A MAN 528 1_555 ? ? ? ? ? ? ? 1.390 ? 
covale11 covale ? ? I MAN .   O6  ? ? ? 1_555 J  MAN .   C1 ? ? A MAN 528 A MAN 529 1_555 ? ? ? ? ? ? ? 1.396 ? 
covale12 covale ? ? K NAG .   O3  ? ? ? 1_555 M  FUC .   C1 ? ? A NAG 530 A FUC 532 1_555 ? ? ? ? ? ? ? 1.403 ? 
covale13 covale ? ? K NAG .   O4  ? ? ? 1_555 L  NAG .   C1 ? ? A NAG 530 A NAG 531 1_555 ? ? ? ? ? ? ? 1.390 ? 
covale14 covale ? ? Q NAG .   C1  ? ? ? 1_555 R  NAG .   O4 ? ? B NAG 524 B NAG 525 1_555 ? ? ? ? ? ? ? 1.384 ? 
covale15 covale ? ? Q NAG .   O4  ? ? ? 1_555 T  BMA .   C1 ? ? B NAG 524 B BMA 527 1_555 ? ? ? ? ? ? ? 1.385 ? 
covale16 covale ? ? R NAG .   O3  ? ? ? 1_555 S  FUC .   C1 ? ? B NAG 525 B FUC 526 1_555 ? ? ? ? ? ? ? 1.401 ? 
covale17 covale ? ? T BMA .   O3  ? ? ? 1_555 U  MAN .   C1 ? ? B BMA 527 B MAN 528 1_555 ? ? ? ? ? ? ? 1.399 ? 
covale18 covale ? ? V NAG .   O4  ? ? ? 1_555 W  NAG .   C1 ? ? B NAG 529 B NAG 530 1_555 ? ? ? ? ? ? ? 1.389 ? 
covale19 covale ? ? W NAG .   O4  ? ? ? 1_555 X  BMA .   C1 ? ? B NAG 530 B BMA 531 1_555 ? ? ? ? ? ? ? 1.389 ? 
covale20 covale ? ? X BMA .   O6  ? ? ? 1_555 Y  MAN .   C1 ? ? B BMA 531 B MAN 532 1_555 ? ? ? ? ? ? ? 1.397 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 HIS 168 A . ? HIS 168 A PRO 169 A ? PRO 169 A 1 0.00  
2 ALA 225 A . ? ALA 225 A PRO 226 A ? PRO 226 A 1 -2.26 
3 GLY 364 A . ? GLY 364 A PRO 365 A ? PRO 365 A 1 -0.15 
4 HIS 168 B . ? HIS 168 B PRO 169 B ? PRO 169 B 1 -0.64 
5 ALA 225 B . ? ALA 225 B PRO 226 B ? PRO 226 B 1 -0.13 
6 GLY 364 B . ? GLY 364 B PRO 365 B ? PRO 365 B 1 -0.43 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 7 ? 
B ? 6 ? 
C ? 2 ? 
D ? 2 ? 
E ? 7 ? 
F ? 7 ? 
G ? 2 ? 
H ? 4 ? 
I ? 7 ? 
J ? 6 ? 
K ? 2 ? 
L ? 2 ? 
M ? 7 ? 
N ? 7 ? 
O ? 2 ? 
P ? 4 ? 
# 
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 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
A 5 6 ? anti-parallel 
A 6 7 ? anti-parallel 
B 1 2 ? parallel      
B 2 3 ? parallel      
B 3 4 ? parallel      
B 4 5 ? parallel      
B 5 6 ? parallel      
C 1 2 ? anti-parallel 
D 1 2 ? anti-parallel 
E 1 2 ? parallel      
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
E 5 6 ? anti-parallel 
E 6 7 ? anti-parallel 
F 1 2 ? parallel      
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
F 4 5 ? anti-parallel 
F 5 6 ? anti-parallel 
F 6 7 ? anti-parallel 
G 1 2 ? parallel      
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
I 1 2 ? parallel      
I 2 3 ? parallel      
I 3 4 ? parallel      
I 4 5 ? parallel      
I 5 6 ? anti-parallel 
I 6 7 ? anti-parallel 
J 1 2 ? parallel      
J 2 3 ? parallel      
J 3 4 ? parallel      
J 4 5 ? parallel      
J 5 6 ? parallel      
K 1 2 ? anti-parallel 
L 1 2 ? anti-parallel 
M 1 2 ? parallel      
M 2 3 ? anti-parallel 
M 3 4 ? anti-parallel 
M 4 5 ? anti-parallel 
M 5 6 ? anti-parallel 
M 6 7 ? anti-parallel 
N 1 2 ? parallel      
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
N 4 5 ? anti-parallel 
N 5 6 ? anti-parallel 
N 6 7 ? anti-parallel 
O 1 2 ? parallel      
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? 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 
A 1 ALA A 15  ? ASP A 17  ? ALA A 15  ASP A 17  
A 2 LEU A 209 ? VAL A 213 ? LEU A 209 VAL A 213 
A 3 VAL A 51  ? LEU A 54  ? VAL A 51  LEU A 54  
A 4 GLU A 24  ? VAL A 32  ? GLU A 24  VAL A 32  
A 5 PRO A 242 ? VAL A 255 ? PRO A 242 VAL A 255 
A 6 LEU A 228 ? ARG A 236 ? LEU A 228 ARG A 236 
A 7 SER A 216 ? ASN A 224 ? SER A 216 ASN A 224 
B 1 ALA A 15  ? ASP A 17  ? ALA A 15  ASP A 17  
B 2 LEU A 209 ? VAL A 213 ? LEU A 209 VAL A 213 
B 3 VAL A 51  ? LEU A 54  ? VAL A 51  LEU A 54  
B 4 GLU A 24  ? VAL A 32  ? GLU A 24  VAL A 32  
B 5 PRO A 242 ? VAL A 255 ? PRO A 242 VAL A 255 
B 6 LEU A 482 ? VAL A 484 ? LEU A 482 VAL A 484 
C 1 VAL A 86  ? VAL A 90  ? VAL A 86  VAL A 90  
C 2 ASP A 96  ? GLY A 100 ? ASP A 96  GLY A 100 
D 1 VAL A 113 ? TYR A 114 ? VAL A 113 TYR A 114 
D 2 GLY A 185 ? SER A 186 ? GLY A 185 SER A 186 
E 1 ASN A 170 ? PHE A 173 ? ASN A 170 PHE A 173 
E 2 GLY A 180 ? ILE A 183 ? GLY A 180 ILE A 183 
E 3 VAL A 318 ? ILE A 321 ? VAL A 318 ILE A 321 
E 4 PHE A 325 ? SER A 332 ? PHE A 325 SER A 332 
E 5 PHE A 355 ? VAL A 362 ? PHE A 355 VAL A 362 
E 6 PRO A 299 ? ILE A 305 ? PRO A 299 ILE A 305 
E 7 ILE A 431 ? LEU A 432 ? ILE A 431 LEU A 432 
F 1 ASN A 170 ? PHE A 173 ? ASN A 170 PHE A 173 
F 2 GLY A 180 ? ILE A 183 ? GLY A 180 ILE A 183 
F 3 VAL A 318 ? ILE A 321 ? VAL A 318 ILE A 321 
F 4 PHE A 325 ? SER A 332 ? PHE A 325 SER A 332 
F 5 PHE A 355 ? VAL A 362 ? PHE A 355 VAL A 362 
F 6 PRO A 299 ? ILE A 305 ? PRO A 299 ILE A 305 
F 7 ALA A 455 ? SER A 456 ? ALA A 455 SER A 456 
G 1 VAL A 271 ? GLY A 272 ? VAL A 271 GLY A 272 
G 2 LEU A 286 ? SER A 287 ? LEU A 286 SER A 287 
H 1 ASN A 384 ? VAL A 385 ? ASN A 384 VAL A 385 
H 2 GLY A 369 ? THR A 372 ? GLY A 369 THR A 372 
H 3 GLN A 293 ? HIS A 296 ? GLN A 293 HIS A 296 
H 4 HIS A 461 ? GLY A 462 ? HIS A 461 GLY A 462 
I 1 ALA B 15  ? ASP B 17  ? ALA B 15  ASP B 17  
I 2 LEU B 209 ? VAL B 213 ? LEU B 209 VAL B 213 
I 3 VAL B 51  ? LEU B 54  ? VAL B 51  LEU B 54  
I 4 GLU B 24  ? VAL B 32  ? GLU B 24  VAL B 32  
I 5 PRO B 242 ? VAL B 255 ? PRO B 242 VAL B 255 
I 6 ALA B 230 ? ARG B 236 ? ALA B 230 ARG B 236 
I 7 SER B 216 ? PHE B 222 ? SER B 216 PHE B 222 
J 1 ALA B 15  ? ASP B 17  ? ALA B 15  ASP B 17  
J 2 LEU B 209 ? VAL B 213 ? LEU B 209 VAL B 213 
J 3 VAL B 51  ? LEU B 54  ? VAL B 51  LEU B 54  
J 4 GLU B 24  ? VAL B 32  ? GLU B 24  VAL B 32  
J 5 PRO B 242 ? VAL B 255 ? PRO B 242 VAL B 255 
J 6 LEU B 482 ? VAL B 484 ? LEU B 482 VAL B 484 
K 1 VAL B 86  ? VAL B 90  ? VAL B 86  VAL B 90  
K 2 ASP B 96  ? GLY B 100 ? ASP B 96  GLY B 100 
L 1 VAL B 113 ? TYR B 114 ? VAL B 113 TYR B 114 
L 2 GLY B 185 ? SER B 186 ? GLY B 185 SER B 186 
M 1 ASN B 170 ? PHE B 173 ? ASN B 170 PHE B 173 
M 2 GLY B 180 ? ILE B 183 ? GLY B 180 ILE B 183 
M 3 VAL B 318 ? ILE B 321 ? VAL B 318 ILE B 321 
M 4 PHE B 325 ? SER B 332 ? PHE B 325 SER B 332 
M 5 PHE B 355 ? VAL B 362 ? PHE B 355 VAL B 362 
M 6 PRO B 299 ? ILE B 305 ? PRO B 299 ILE B 305 
M 7 ILE B 431 ? LEU B 432 ? ILE B 431 LEU B 432 
N 1 ASN B 170 ? PHE B 173 ? ASN B 170 PHE B 173 
N 2 GLY B 180 ? ILE B 183 ? GLY B 180 ILE B 183 
N 3 VAL B 318 ? ILE B 321 ? VAL B 318 ILE B 321 
N 4 PHE B 325 ? SER B 332 ? PHE B 325 SER B 332 
N 5 PHE B 355 ? VAL B 362 ? PHE B 355 VAL B 362 
N 6 PRO B 299 ? ILE B 305 ? PRO B 299 ILE B 305 
N 7 ALA B 455 ? SER B 456 ? ALA B 455 SER B 456 
O 1 VAL B 271 ? GLY B 272 ? VAL B 271 GLY B 272 
O 2 LEU B 286 ? SER B 287 ? LEU B 286 SER B 287 
P 1 ASN B 384 ? VAL B 385 ? ASN B 384 VAL B 385 
P 2 GLY B 369 ? THR B 372 ? GLY B 369 THR B 372 
P 3 GLN B 293 ? HIS B 296 ? GLN B 293 HIS B 296 
P 4 HIS B 461 ? GLY B 462 ? HIS B 461 GLY B 462 
# 
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 
A 1 2 N TYR A 16  ? N TYR A 16  O VAL A 211 ? O VAL A 211 
A 2 3 O GLY A 212 ? O GLY A 212 N VAL A 53  ? N VAL A 53  
A 3 4 O LEU A 52  ? O LEU A 52  N ILE A 31  ? N ILE A 31  
A 4 5 N TYR A 27  ? N TYR A 27  O PHE A 246 ? O PHE A 246 
A 5 6 O HIS A 243 ? O HIS A 243 N TYR A 235 ? N TYR A 235 
A 6 7 O GLY A 232 ? O GLY A 232 N ILE A 221 ? N ILE A 221 
B 1 2 N TYR A 16  ? N TYR A 16  O VAL A 211 ? O VAL A 211 
B 2 3 O GLY A 212 ? O GLY A 212 N VAL A 53  ? N VAL A 53  
B 3 4 O LEU A 52  ? O LEU A 52  N ILE A 31  ? N ILE A 31  
B 4 5 N TYR A 27  ? N TYR A 27  O PHE A 246 ? O PHE A 246 
B 5 6 N VAL A 255 ? N VAL A 255 O ARG A 483 ? O ARG A 483 
C 1 2 N GLU A 87  ? N GLU A 87  O ARG A 99  ? O ARG A 99  
D 1 2 N TYR A 114 ? N TYR A 114 O GLY A 185 ? O GLY A 185 
E 1 2 N HIS A 171 ? N HIS A 171 O THR A 181 ? O THR A 181 
E 2 3 N GLY A 180 ? N GLY A 180 O ILE A 321 ? O ILE A 321 
E 3 4 N GLY A 320 ? N GLY A 320 O GLN A 327 ? O GLN A 327 
E 4 5 N TYR A 326 ? N TYR A 326 O LYS A 361 ? O LYS A 361 
E 5 6 O PHE A 358 ? O PHE A 358 N ILE A 303 ? N ILE A 303 
E 6 7 N ASN A 304 ? N ASN A 304 O LEU A 432 ? O LEU A 432 
F 1 2 N HIS A 171 ? N HIS A 171 O THR A 181 ? O THR A 181 
F 2 3 N GLY A 180 ? N GLY A 180 O ILE A 321 ? O ILE A 321 
F 3 4 N GLY A 320 ? N GLY A 320 O GLN A 327 ? O GLN A 327 
F 4 5 N TYR A 326 ? N TYR A 326 O LYS A 361 ? O LYS A 361 
F 5 6 O PHE A 358 ? O PHE A 358 N ILE A 303 ? N ILE A 303 
F 6 7 N ARG A 300 ? N ARG A 300 O ALA A 455 ? O ALA A 455 
G 1 2 N GLY A 272 ? N GLY A 272 O LEU A 286 ? O LEU A 286 
H 1 2 O ASN A 384 ? O ASN A 384 N THR A 372 ? N THR A 372 
H 2 3 O GLY A 369 ? O GLY A 369 N LEU A 295 ? N LEU A 295 
H 3 4 N HIS A 296 ? N HIS A 296 O HIS A 461 ? O HIS A 461 
I 1 2 N TYR B 16  ? N TYR B 16  O VAL B 211 ? O VAL B 211 
I 2 3 O GLY B 212 ? O GLY B 212 N VAL B 53  ? N VAL B 53  
I 3 4 O LEU B 52  ? O LEU B 52  N ILE B 31  ? N ILE B 31  
I 4 5 N GLY B 25  ? N GLY B 25  O PHE B 246 ? O PHE B 246 
I 5 6 O HIS B 243 ? O HIS B 243 N TYR B 235 ? N TYR B 235 
I 6 7 O GLY B 232 ? O GLY B 232 N ILE B 221 ? N ILE B 221 
J 1 2 N TYR B 16  ? N TYR B 16  O VAL B 211 ? O VAL B 211 
J 2 3 O GLY B 212 ? O GLY B 212 N VAL B 53  ? N VAL B 53  
J 3 4 O LEU B 52  ? O LEU B 52  N ILE B 31  ? N ILE B 31  
J 4 5 N GLY B 25  ? N GLY B 25  O PHE B 246 ? O PHE B 246 
J 5 6 N VAL B 255 ? N VAL B 255 O ARG B 483 ? O ARG B 483 
K 1 2 N GLU B 87  ? N GLU B 87  O ARG B 99  ? O ARG B 99  
L 1 2 N TYR B 114 ? N TYR B 114 O GLY B 185 ? O GLY B 185 
M 1 2 N HIS B 171 ? N HIS B 171 O THR B 181 ? O THR B 181 
M 2 3 N GLY B 180 ? N GLY B 180 O ILE B 321 ? O ILE B 321 
M 3 4 N GLY B 320 ? N GLY B 320 O GLN B 327 ? O GLN B 327 
M 4 5 N TYR B 326 ? N TYR B 326 O LYS B 361 ? O LYS B 361 
M 5 6 O PHE B 358 ? O PHE B 358 N ILE B 303 ? N ILE B 303 
M 6 7 N ASN B 304 ? N ASN B 304 O LEU B 432 ? O LEU B 432 
N 1 2 N HIS B 171 ? N HIS B 171 O THR B 181 ? O THR B 181 
N 2 3 N GLY B 180 ? N GLY B 180 O ILE B 321 ? O ILE B 321 
N 3 4 N GLY B 320 ? N GLY B 320 O GLN B 327 ? O GLN B 327 
N 4 5 N TYR B 326 ? N TYR B 326 O LYS B 361 ? O LYS B 361 
N 5 6 O PHE B 358 ? O PHE B 358 N ILE B 303 ? N ILE B 303 
N 6 7 N ARG B 300 ? N ARG B 300 O ALA B 455 ? O ALA B 455 
O 1 2 N GLY B 272 ? N GLY B 272 O LEU B 286 ? O LEU B 286 
P 1 2 O ASN B 384 ? O ASN B 384 N THR B 372 ? N THR B 372 
P 2 3 O GLY B 369 ? O GLY B 369 N LEU B 295 ? N LEU B 295 
P 3 4 N HIS B 296 ? N HIS B 296 O HIS B 461 ? O HIS B 461 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE IPA A 522' 
AC2 Software ? ? ? ? 39 'BINDING SITE FOR RESIDUE FAD A 523' 
AC3 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG A 524' 
AC4 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE NAG A 525' 
AC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG A 526' 
AC6 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE FUL A 527' 
AC7 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE MAN A 528' 
AC8 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE MAN A 529' 
AC9 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG A 530' 
BC1 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 531' 
BC2 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE FUC A 532' 
BC3 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG A 533' 
BC4 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE IPA B 522' 
BC5 Software ? ? ? ? 39 'BINDING SITE FOR RESIDUE FAD B 523' 
BC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B 524' 
BC7 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG B 525' 
BC8 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE FUC B 526' 
BC9 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE BMA B 527' 
CC1 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE MAN B 528' 
CC2 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG B 529' 
CC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG B 530' 
CC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE BMA B 531' 
CC5 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE MAN B 532' 
CC6 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NDG B 533' 
CC7 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG B 534' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 7  ILE A  121 ? ILE A 121  . ? 1_555 ? 
2   AC1 7  SER A  125 ? SER A 125  . ? 1_555 ? 
3   AC1 7  PHE A  490 ? PHE A 490  . ? 1_555 ? 
4   AC1 7  TYR A  492 ? TYR A 492  . ? 1_555 ? 
5   AC1 7  HOH BA .   ? HOH A 866  . ? 1_555 ? 
6   AC1 7  HOH BA .   ? HOH A 1156 . ? 1_555 ? 
7   AC1 7  HOH BA .   ? HOH A 1176 . ? 1_555 ? 
8   AC2 39 GLY A  33  ? GLY A 33   . ? 1_555 ? 
9   AC2 39 GLY A  35  ? GLY A 35   . ? 1_555 ? 
10  AC2 39 THR A  36  ? THR A 36   . ? 1_555 ? 
11  AC2 39 SER A  37  ? SER A 37   . ? 1_555 ? 
12  AC2 39 LEU A  54  ? LEU A 54   . ? 1_555 ? 
13  AC2 39 GLU A  55  ? GLU A 55   . ? 1_555 ? 
14  AC2 39 ARG A  56  ? ARG A 56   . ? 1_555 ? 
15  AC2 39 VAL A  98  ? VAL A 98   . ? 1_555 ? 
16  AC2 39 GLY A  100 ? GLY A 100  . ? 1_555 ? 
17  AC2 39 ARG A  101 ? ARG A 101  . ? 1_555 ? 
18  AC2 39 VAL A  102 ? VAL A 102  . ? 1_555 ? 
19  AC2 39 GLY A  105 ? GLY A 105  . ? 1_555 ? 
20  AC2 39 THR A  106 ? THR A 106  . ? 1_555 ? 
21  AC2 39 ASN A  110 ? ASN A 110  . ? 1_555 ? 
22  AC2 39 ALA A  111 ? ALA A 111  . ? 1_555 ? 
23  AC2 39 GLY A  112 ? GLY A 112  . ? 1_555 ? 
24  AC2 39 VAL A  113 ? VAL A 113  . ? 1_555 ? 
25  AC2 39 ALA A  215 ? ALA A 215  . ? 1_555 ? 
26  AC2 39 VAL A  217 ? VAL A 217  . ? 1_555 ? 
27  AC2 39 SER A  256 ? SER A 256  . ? 1_555 ? 
28  AC2 39 ALA A  257 ? ALA A 257  . ? 1_555 ? 
29  AC2 39 VAL A  379 ? VAL A 379  . ? 1_555 ? 
30  AC2 39 TRP A  458 ? TRP A 458  . ? 1_555 ? 
31  AC2 39 HIS A  459 ? HIS A 459  . ? 1_555 ? 
32  AC2 39 ASP A  486 ? ASP A 486  . ? 1_555 ? 
33  AC2 39 GLY A  487 ? GLY A 487  . ? 1_555 ? 
34  AC2 39 HIS A  497 ? HIS A 497  . ? 1_555 ? 
35  AC2 39 PRO A  498 ? PRO A 498  . ? 1_555 ? 
36  AC2 39 GLN A  499 ? GLN A 499  . ? 1_555 ? 
37  AC2 39 TYR A  502 ? TYR A 502  . ? 1_555 ? 
38  AC2 39 HOH BA .   ? HOH A 593  . ? 1_555 ? 
39  AC2 39 HOH BA .   ? HOH A 694  . ? 1_555 ? 
40  AC2 39 HOH BA .   ? HOH A 777  . ? 1_555 ? 
41  AC2 39 HOH BA .   ? HOH A 831  . ? 1_555 ? 
42  AC2 39 HOH BA .   ? HOH A 835  . ? 1_555 ? 
43  AC2 39 HOH BA .   ? HOH A 845  . ? 1_555 ? 
44  AC2 39 HOH BA .   ? HOH A 853  . ? 1_555 ? 
45  AC2 39 HOH BA .   ? HOH A 879  . ? 1_555 ? 
46  AC2 39 HOH BA .   ? HOH A 920  . ? 1_555 ? 
47  AC3 10 ASN A  118 ? ASN A 118  . ? 1_555 ? 
48  AC3 10 HIS A  177 ? HIS A 177  . ? 1_555 ? 
49  AC3 10 GLU A  179 ? GLU A 179  . ? 1_555 ? 
50  AC3 10 ASN A  323 ? ASN A 323  . ? 1_555 ? 
51  AC3 10 HOH BA .   ? HOH A 632  . ? 1_555 ? 
52  AC3 10 HOH BA .   ? HOH A 827  . ? 1_555 ? 
53  AC3 10 HOH BA .   ? HOH A 925  . ? 1_555 ? 
54  AC3 10 HOH BA .   ? HOH A 1202 . ? 1_555 ? 
55  AC3 10 HOH BA .   ? HOH A 1299 . ? 1_555 ? 
56  AC3 10 HOH BA .   ? HOH A 1349 . ? 1_555 ? 
57  AC4 12 ARG A  116 ? ARG A 116  . ? 1_555 ? 
58  AC4 12 ASP A  132 ? ASP A 132  . ? 1_555 ? 
59  AC4 12 ASN A  135 ? ASN A 135  . ? 1_555 ? 
60  AC4 12 ASP A  176 ? ASP A 176  . ? 1_555 ? 
61  AC4 12 NAG G  .   ? NAG A 526  . ? 1_555 ? 
62  AC4 12 FUL H  .   ? FUL A 527  . ? 1_555 ? 
63  AC4 12 HOH BA .   ? HOH A 568  . ? 1_555 ? 
64  AC4 12 HOH BA .   ? HOH A 877  . ? 1_555 ? 
65  AC4 12 HOH BA .   ? HOH A 1088 . ? 1_555 ? 
66  AC4 12 HOH BA .   ? HOH A 1208 . ? 1_555 ? 
67  AC4 12 HOH BA .   ? HOH A 1213 . ? 1_555 ? 
68  AC4 12 HOH BA .   ? HOH A 1250 . ? 1_555 ? 
69  AC5 6  THR A  119 ? THR A 119  . ? 1_555 ? 
70  AC5 6  ASP A  176 ? ASP A 176  . ? 1_555 ? 
71  AC5 6  NAG F  .   ? NAG A 525  . ? 1_555 ? 
72  AC5 6  FUL H  .   ? FUL A 527  . ? 1_555 ? 
73  AC5 6  MAN I  .   ? MAN A 528  . ? 1_555 ? 
74  AC5 6  HOH BA .   ? HOH A 538  . ? 1_555 ? 
75  AC6 3  NAG F  .   ? NAG A 525  . ? 1_555 ? 
76  AC6 3  NAG G  .   ? NAG A 526  . ? 1_555 ? 
77  AC6 3  HOH BA .   ? HOH A 568  . ? 1_555 ? 
78  AC7 3  NAG G  .   ? NAG A 526  . ? 1_555 ? 
79  AC7 3  MAN J  .   ? MAN A 529  . ? 1_555 ? 
80  AC7 3  HOH BA .   ? HOH A 554  . ? 1_555 ? 
81  AC8 4  HIS A  171 ? HIS A 171  . ? 1_555 ? 
82  AC8 4  GLU A  178 ? GLU A 178  . ? 1_555 ? 
83  AC8 4  MAN I  .   ? MAN A 528  . ? 1_555 ? 
84  AC8 4  HOH BA .   ? HOH A 588  . ? 1_555 ? 
85  AC9 7  LEU A  366 ? LEU A 366  . ? 1_555 ? 
86  AC9 7  ASN A  392 ? ASN A 392  . ? 1_555 ? 
87  AC9 7  NAG L  .   ? NAG A 531  . ? 1_555 ? 
88  AC9 7  FUC M  .   ? FUC A 532  . ? 1_555 ? 
89  AC9 7  HOH BA .   ? HOH A 587  . ? 1_555 ? 
90  AC9 7  HOH BA .   ? HOH A 683  . ? 1_555 ? 
91  AC9 7  HOH BA .   ? HOH A 784  . ? 1_555 ? 
92  BC1 3  NAG K  .   ? NAG A 530  . ? 1_555 ? 
93  BC1 3  FUC M  .   ? FUC A 532  . ? 1_555 ? 
94  BC1 3  HOH BA .   ? HOH A 686  . ? 1_555 ? 
95  BC2 3  NAG K  .   ? NAG A 530  . ? 1_555 ? 
96  BC2 3  NAG L  .   ? NAG A 531  . ? 1_555 ? 
97  BC2 3  HOH BA .   ? HOH A 683  . ? 1_555 ? 
98  BC3 6  ASN A  352 ? ASN A 352  . ? 1_555 ? 
99  BC3 6  ASN A  430 ? ASN A 430  . ? 1_555 ? 
100 BC3 6  HOH BA .   ? HOH A 570  . ? 1_555 ? 
101 BC3 6  HOH BA .   ? HOH A 650  . ? 1_555 ? 
102 BC3 6  HOH BA .   ? HOH A 824  . ? 1_555 ? 
103 BC3 6  HOH BA .   ? HOH A 1301 . ? 1_555 ? 
104 BC4 6  ILE B  121 ? ILE B 121  . ? 1_555 ? 
105 BC4 6  PHE B  490 ? PHE B 490  . ? 1_555 ? 
106 BC4 6  TYR B  492 ? TYR B 492  . ? 1_555 ? 
107 BC4 6  HOH CA .   ? HOH B 850  . ? 1_555 ? 
108 BC4 6  HOH CA .   ? HOH B 1002 . ? 1_555 ? 
109 BC4 6  HOH CA .   ? HOH B 1381 . ? 1_555 ? 
110 BC5 39 GLY B  33  ? GLY B 33   . ? 1_555 ? 
111 BC5 39 GLY B  35  ? GLY B 35   . ? 1_555 ? 
112 BC5 39 THR B  36  ? THR B 36   . ? 1_555 ? 
113 BC5 39 SER B  37  ? SER B 37   . ? 1_555 ? 
114 BC5 39 LEU B  54  ? LEU B 54   . ? 1_555 ? 
115 BC5 39 GLU B  55  ? GLU B 55   . ? 1_555 ? 
116 BC5 39 ARG B  56  ? ARG B 56   . ? 1_555 ? 
117 BC5 39 VAL B  98  ? VAL B 98   . ? 1_555 ? 
118 BC5 39 GLY B  100 ? GLY B 100  . ? 1_555 ? 
119 BC5 39 ARG B  101 ? ARG B 101  . ? 1_555 ? 
120 BC5 39 VAL B  102 ? VAL B 102  . ? 1_555 ? 
121 BC5 39 GLY B  105 ? GLY B 105  . ? 1_555 ? 
122 BC5 39 THR B  106 ? THR B 106  . ? 1_555 ? 
123 BC5 39 ASN B  110 ? ASN B 110  . ? 1_555 ? 
124 BC5 39 ALA B  111 ? ALA B 111  . ? 1_555 ? 
125 BC5 39 GLY B  112 ? GLY B 112  . ? 1_555 ? 
126 BC5 39 VAL B  113 ? VAL B 113  . ? 1_555 ? 
127 BC5 39 ALA B  215 ? ALA B 215  . ? 1_555 ? 
128 BC5 39 VAL B  217 ? VAL B 217  . ? 1_555 ? 
129 BC5 39 SER B  256 ? SER B 256  . ? 1_555 ? 
130 BC5 39 ALA B  257 ? ALA B 257  . ? 1_555 ? 
131 BC5 39 VAL B  379 ? VAL B 379  . ? 1_555 ? 
132 BC5 39 TRP B  458 ? TRP B 458  . ? 1_555 ? 
133 BC5 39 HIS B  459 ? HIS B 459  . ? 1_555 ? 
134 BC5 39 ASP B  486 ? ASP B 486  . ? 1_555 ? 
135 BC5 39 GLY B  487 ? GLY B 487  . ? 1_555 ? 
136 BC5 39 HIS B  497 ? HIS B 497  . ? 1_555 ? 
137 BC5 39 PRO B  498 ? PRO B 498  . ? 1_555 ? 
138 BC5 39 GLN B  499 ? GLN B 499  . ? 1_555 ? 
139 BC5 39 TYR B  502 ? TYR B 502  . ? 1_555 ? 
140 BC5 39 HOH CA .   ? HOH B 831  . ? 1_555 ? 
141 BC5 39 HOH CA .   ? HOH B 841  . ? 1_555 ? 
142 BC5 39 HOH CA .   ? HOH B 847  . ? 1_555 ? 
143 BC5 39 HOH CA .   ? HOH B 848  . ? 1_555 ? 
144 BC5 39 HOH CA .   ? HOH B 851  . ? 1_555 ? 
145 BC5 39 HOH CA .   ? HOH B 861  . ? 1_555 ? 
146 BC5 39 HOH CA .   ? HOH B 885  . ? 1_555 ? 
147 BC5 39 HOH CA .   ? HOH B 976  . ? 1_555 ? 
148 BC5 39 HOH CA .   ? HOH B 1058 . ? 1_555 ? 
149 BC6 4  NAG R  .   ? NAG B 525  . ? 1_555 ? 
150 BC6 4  FUC S  .   ? FUC B 526  . ? 1_555 ? 
151 BC6 4  BMA T  .   ? BMA B 527  . ? 1_555 ? 
152 BC6 4  HOH CA .   ? HOH B 1432 . ? 1_555 ? 
153 BC7 6  LEU B  366 ? LEU B 366  . ? 1_555 ? 
154 BC7 6  ASN B  392 ? ASN B 392  . ? 1_555 ? 
155 BC7 6  NAG Q  .   ? NAG B 524  . ? 1_555 ? 
156 BC7 6  FUC S  .   ? FUC B 526  . ? 1_555 ? 
157 BC7 6  HOH CA .   ? HOH B 1007 . ? 1_555 ? 
158 BC7 6  HOH CA .   ? HOH B 1245 . ? 1_555 ? 
159 BC8 3  NAG Q  .   ? NAG B 524  . ? 1_555 ? 
160 BC8 3  NAG R  .   ? NAG B 525  . ? 1_555 ? 
161 BC8 3  HOH CA .   ? HOH B 1277 . ? 1_555 ? 
162 BC9 3  ASP A  422 ? ASP A 422  . ? 1_555 ? 
163 BC9 3  NAG Q  .   ? NAG B 524  . ? 1_555 ? 
164 BC9 3  MAN U  .   ? MAN B 528  . ? 1_555 ? 
165 CC1 9  LYS A  416 ? LYS A 416  . ? 1_555 ? 
166 CC1 9  PRO A  417 ? PRO A 417  . ? 1_555 ? 
167 CC1 9  LYS A  419 ? LYS A 419  . ? 1_555 ? 
168 CC1 9  ASP A  422 ? ASP A 422  . ? 1_555 ? 
169 CC1 9  HOH BA .   ? HOH A 607  . ? 1_555 ? 
170 CC1 9  BMA T  .   ? BMA B 527  . ? 1_555 ? 
171 CC1 9  HOH CA .   ? HOH B 535  . ? 1_555 ? 
172 CC1 9  HOH CA .   ? HOH B 590  . ? 1_555 ? 
173 CC1 9  HOH CA .   ? HOH B 625  . ? 1_555 ? 
174 CC2 10 ARG B  116 ? ARG B 116  . ? 1_555 ? 
175 CC2 10 ASP B  132 ? ASP B 132  . ? 1_555 ? 
176 CC2 10 ASN B  135 ? ASN B 135  . ? 1_555 ? 
177 CC2 10 ASP B  176 ? ASP B 176  . ? 1_555 ? 
178 CC2 10 NAG W  .   ? NAG B 530  . ? 1_555 ? 
179 CC2 10 HOH CA .   ? HOH B 866  . ? 1_555 ? 
180 CC2 10 HOH CA .   ? HOH B 880  . ? 1_555 ? 
181 CC2 10 HOH CA .   ? HOH B 1276 . ? 1_555 ? 
182 CC2 10 HOH CA .   ? HOH B 1283 . ? 1_555 ? 
183 CC2 10 HOH CA .   ? HOH B 1323 . ? 1_555 ? 
184 CC3 5  GLU B  178 ? GLU B 178  . ? 1_555 ? 
185 CC3 5  NAG V  .   ? NAG B 529  . ? 1_555 ? 
186 CC3 5  BMA X  .   ? BMA B 531  . ? 1_555 ? 
187 CC3 5  HOH CA .   ? HOH B 1341 . ? 1_555 ? 
188 CC3 5  HOH CA .   ? HOH B 1373 . ? 1_555 ? 
189 CC4 4  NAG W  .   ? NAG B 530  . ? 1_555 ? 
190 CC4 4  MAN Y  .   ? MAN B 532  . ? 1_555 ? 
191 CC4 4  HOH CA .   ? HOH B 1291 . ? 1_555 ? 
192 CC4 4  HOH CA .   ? HOH B 1380 . ? 1_555 ? 
193 CC5 5  HIS B  171 ? HIS B 171  . ? 1_555 ? 
194 CC5 5  GLU B  178 ? GLU B 178  . ? 1_555 ? 
195 CC5 5  BMA X  .   ? BMA B 531  . ? 1_555 ? 
196 CC5 5  HOH CA .   ? HOH B 1097 . ? 1_555 ? 
197 CC5 5  HOH CA .   ? HOH B 1370 . ? 1_555 ? 
198 CC6 7  ALA A  519 ? ALA A 519  . ? 1_465 ? 
199 CC6 7  HOH BA .   ? HOH A 1267 . ? 1_465 ? 
200 CC6 7  ASN B  352 ? ASN B 352  . ? 1_555 ? 
201 CC6 7  ASN B  430 ? ASN B 430  . ? 1_555 ? 
202 CC6 7  HOH CA .   ? HOH B 1232 . ? 1_555 ? 
203 CC6 7  HOH CA .   ? HOH B 1502 . ? 1_555 ? 
204 CC6 7  HOH CA .   ? HOH B 1597 . ? 1_555 ? 
205 CC7 6  ASN B  118 ? ASN B 118  . ? 1_555 ? 
206 CC7 6  SER B  120 ? SER B 120  . ? 1_555 ? 
207 CC7 6  HIS B  177 ? HIS B 177  . ? 1_555 ? 
208 CC7 6  ASN B  323 ? ASN B 323  . ? 1_555 ? 
209 CC7 6  HOH CA .   ? HOH B 911  . ? 1_555 ? 
210 CC7 6  HOH CA .   ? HOH B 921  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3GDP 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.000000 
_database_PDB_matrix.origx_vector[2]   0.000000 
_database_PDB_matrix.origx_vector[3]   0.000000 
# 
_atom_sites.entry_id                    3GDP 
_atom_sites.fract_transf_matrix[1][1]   0.014482 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004260 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010671 
_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]   0.011945 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
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     . LEU A  1  1   ? 73.998  -4.750  -10.138 1.00 17.36 ? 1    LEU A N     1 
ATOM   2     C CA    . LEU A  1  1   ? 73.520  -3.492  -10.785 1.00 16.58 ? 1    LEU A CA    1 
ATOM   3     C C     . LEU A  1  1   ? 74.540  -2.367  -10.644 1.00 15.74 ? 1    LEU A C     1 
ATOM   4     O O     . LEU A  1  1   ? 75.341  -2.349  -9.706  1.00 16.78 ? 1    LEU A O     1 
ATOM   5     C CB    . LEU A  1  1   ? 72.184  -3.062  -10.175 1.00 19.17 ? 1    LEU A CB    1 
ATOM   6     C CG    . LEU A  1  1   ? 71.026  -4.046  -10.356 1.00 19.58 ? 1    LEU A CG    1 
ATOM   7     C CD1   . LEU A  1  1   ? 69.804  -3.548  -9.607  1.00 22.23 ? 1    LEU A CD1   1 
ATOM   8     C CD2   . LEU A  1  1   ? 70.724  -4.204  -11.836 1.00 21.15 ? 1    LEU A CD2   1 
ATOM   9     N N     . ALA A  1  2   ? 74.498  -1.424  -11.580 1.00 13.93 ? 2    ALA A N     1 
ATOM   10    C CA    . ALA A  1  2   ? 75.421  -0.297  -11.583 1.00 14.09 ? 2    ALA A CA    1 
ATOM   11    C C     . ALA A  1  2   ? 74.831  0.939   -10.919 1.00 14.65 ? 2    ALA A C     1 
ATOM   12    O O     . ALA A  1  2   ? 73.645  0.980   -10.591 1.00 14.86 ? 2    ALA A O     1 
ATOM   13    C CB    . ALA A  1  2   ? 75.825  0.033   -13.016 1.00 13.90 ? 2    ALA A CB    1 
ATOM   14    N N     . THR A  1  3   ? 75.678  1.943   -10.723 1.00 14.42 ? 3    THR A N     1 
ATOM   15    C CA    . THR A  1  3   ? 75.263  3.198   -10.115 1.00 16.71 ? 3    THR A CA    1 
ATOM   16    C C     . THR A  1  3   ? 75.373  4.306   -11.155 1.00 15.46 ? 3    THR A C     1 
ATOM   17    O O     . THR A  1  3   ? 76.358  4.387   -11.887 1.00 14.88 ? 3    THR A O     1 
ATOM   18    C CB    . THR A  1  3   ? 76.151  3.548   -8.906  1.00 18.55 ? 3    THR A CB    1 
ATOM   19    O OG1   . THR A  1  3   ? 76.065  2.499   -7.934  1.00 21.26 ? 3    THR A OG1   1 
ATOM   20    C CG2   . THR A  1  3   ? 75.700  4.857   -8.271  1.00 21.08 ? 3    THR A CG2   1 
ATOM   21    N N     . THR A  1  4   ? 74.349  5.150   -11.221 1.00 15.71 ? 4    THR A N     1 
ATOM   22    C CA    . THR A  1  4   ? 74.307  6.258   -12.172 1.00 16.15 ? 4    THR A CA    1 
ATOM   23    C C     . THR A  1  4   ? 75.652  6.970   -12.319 1.00 16.62 ? 4    THR A C     1 
ATOM   24    O O     . THR A  1  4   ? 76.296  7.316   -11.328 1.00 16.21 ? 4    THR A O     1 
ATOM   25    C CB    . THR A  1  4   ? 73.227  7.277   -11.750 1.00 17.41 ? 4    THR A CB    1 
ATOM   26    O OG1   . THR A  1  4   ? 71.935  6.660   -11.841 1.00 18.68 ? 4    THR A OG1   1 
ATOM   27    C CG2   . THR A  1  4   ? 73.268  8.512   -12.637 1.00 16.01 ? 4    THR A CG2   1 
ATOM   28    N N     . SER A  1  5   ? 76.068  7.180   -13.565 1.00 16.27 ? 5    SER A N     1 
ATOM   29    C CA    . SER A  1  5   ? 77.334  7.848   -13.862 1.00 16.95 ? 5    SER A CA    1 
ATOM   30    C C     . SER A  1  5   ? 77.373  8.234   -15.337 1.00 16.27 ? 5    SER A C     1 
ATOM   31    O O     . SER A  1  5   ? 76.519  7.807   -16.117 1.00 15.04 ? 5    SER A O     1 
ATOM   32    C CB    . SER A  1  5   ? 78.508  6.916   -13.564 1.00 17.87 ? 5    SER A CB    1 
ATOM   33    O OG    . SER A  1  5   ? 78.596  5.891   -14.542 1.00 20.28 ? 5    SER A OG    1 
ATOM   34    N N     . ASP A  1  6   ? 78.362  9.037   -15.720 1.00 15.62 ? 6    ASP A N     1 
ATOM   35    C CA    . ASP A  1  6   ? 78.495  9.442   -17.114 1.00 15.37 ? 6    ASP A CA    1 
ATOM   36    C C     . ASP A  1  6   ? 78.836  8.220   -17.958 1.00 13.85 ? 6    ASP A C     1 
ATOM   37    O O     . ASP A  1  6   ? 79.359  7.229   -17.446 1.00 12.70 ? 6    ASP A O     1 
ATOM   38    C CB    . ASP A  1  6   ? 79.617  10.471  -17.296 1.00 17.74 ? 6    ASP A CB    1 
ATOM   39    C CG    . ASP A  1  6   ? 79.406  11.728  -16.479 1.00 21.28 ? 6    ASP A CG    1 
ATOM   40    O OD1   . ASP A  1  6   ? 78.242  12.135  -16.286 1.00 22.09 ? 6    ASP A OD1   1 
ATOM   41    O OD2   . ASP A  1  6   ? 80.419  12.319  -16.049 1.00 21.90 ? 6    ASP A OD2   1 
ATOM   42    N N     . HIS A  1  7   ? 78.534  8.293   -19.249 1.00 13.01 ? 7    HIS A N     1 
ATOM   43    C CA    . HIS A  1  7   ? 78.851  7.197   -20.159 1.00 13.79 ? 7    HIS A CA    1 
ATOM   44    C C     . HIS A  1  7   ? 80.379  7.100   -20.134 1.00 13.77 ? 7    HIS A C     1 
ATOM   45    O O     . HIS A  1  7   ? 81.069  8.095   -20.360 1.00 14.37 ? 7    HIS A O     1 
ATOM   46    C CB    . HIS A  1  7   ? 78.366  7.528   -21.571 1.00 12.00 ? 7    HIS A CB    1 
ATOM   47    C CG    . HIS A  1  7   ? 78.432  6.372   -22.521 1.00 12.13 ? 7    HIS A CG    1 
ATOM   48    N ND1   . HIS A  1  7   ? 77.368  5.525   -22.736 1.00 10.61 ? 7    HIS A ND1   1 
ATOM   49    C CD2   . HIS A  1  7   ? 79.440  5.920   -23.304 1.00 11.47 ? 7    HIS A CD2   1 
ATOM   50    C CE1   . HIS A  1  7   ? 77.717  4.599   -23.614 1.00 8.79  ? 7    HIS A CE1   1 
ATOM   51    N NE2   . HIS A  1  7   ? 78.968  4.817   -23.973 1.00 9.87  ? 7    HIS A NE2   1 
ATOM   52    N N     . ASP A  1  8   ? 80.902  5.910   -19.859 1.00 13.45 ? 8    ASP A N     1 
ATOM   53    C CA    . ASP A  1  8   ? 82.349  5.704   -19.763 1.00 13.99 ? 8    ASP A CA    1 
ATOM   54    C C     . ASP A  1  8   ? 83.063  5.514   -21.104 1.00 14.58 ? 8    ASP A C     1 
ATOM   55    O O     . ASP A  1  8   ? 82.995  4.442   -21.703 1.00 13.33 ? 8    ASP A O     1 
ATOM   56    C CB    . ASP A  1  8   ? 82.626  4.499   -18.862 1.00 15.32 ? 8    ASP A CB    1 
ATOM   57    C CG    . ASP A  1  8   ? 84.092  4.357   -18.505 1.00 14.55 ? 8    ASP A CG    1 
ATOM   58    O OD1   . ASP A  1  8   ? 84.930  5.063   -19.104 1.00 15.74 ? 8    ASP A OD1   1 
ATOM   59    O OD2   . ASP A  1  8   ? 84.400  3.526   -17.626 1.00 16.79 ? 8    ASP A OD2   1 
ATOM   60    N N     . PHE A  1  9   ? 83.758  6.554   -21.561 1.00 12.66 ? 9    PHE A N     1 
ATOM   61    C CA    . PHE A  1  9   ? 84.490  6.501   -22.824 1.00 12.93 ? 9    PHE A CA    1 
ATOM   62    C C     . PHE A  1  9   ? 85.995  6.309   -22.636 1.00 12.55 ? 9    PHE A C     1 
ATOM   63    O O     . PHE A  1  9   ? 86.790  6.756   -23.465 1.00 12.57 ? 9    PHE A O     1 
ATOM   64    C CB    . PHE A  1  9   ? 84.256  7.778   -23.641 1.00 14.05 ? 9    PHE A CB    1 
ATOM   65    C CG    . PHE A  1  9   ? 82.901  7.854   -24.292 1.00 14.68 ? 9    PHE A CG    1 
ATOM   66    C CD1   . PHE A  1  9   ? 81.959  8.787   -23.867 1.00 13.07 ? 9    PHE A CD1   1 
ATOM   67    C CD2   . PHE A  1  9   ? 82.579  7.012   -25.353 1.00 13.05 ? 9    PHE A CD2   1 
ATOM   68    C CE1   . PHE A  1  9   ? 80.716  8.883   -24.491 1.00 14.42 ? 9    PHE A CE1   1 
ATOM   69    C CE2   . PHE A  1  9   ? 81.341  7.098   -25.984 1.00 13.51 ? 9    PHE A CE2   1 
ATOM   70    C CZ    . PHE A  1  9   ? 80.406  8.039   -25.553 1.00 14.08 ? 9    PHE A CZ    1 
ATOM   71    N N     . SER A  1  10  ? 86.391  5.645   -21.555 1.00 13.59 ? 10   SER A N     1 
ATOM   72    C CA    . SER A  1  10  ? 87.810  5.415   -21.298 1.00 14.00 ? 10   SER A CA    1 
ATOM   73    C C     . SER A  1  10  ? 88.459  4.608   -22.420 1.00 14.12 ? 10   SER A C     1 
ATOM   74    O O     . SER A  1  10  ? 89.637  4.790   -22.729 1.00 13.98 ? 10   SER A O     1 
ATOM   75    C CB    . SER A  1  10  ? 87.998  4.680   -19.968 1.00 14.72 ? 10   SER A CB    1 
ATOM   76    O OG    . SER A  1  10  ? 87.539  5.463   -18.880 1.00 16.00 ? 10   SER A OG    1 
ATOM   77    N N     . TYR A  1  11  ? 87.677  3.723   -23.033 1.00 12.15 ? 11   TYR A N     1 
ATOM   78    C CA    . TYR A  1  11  ? 88.165  2.873   -24.112 1.00 12.75 ? 11   TYR A CA    1 
ATOM   79    C C     . TYR A  1  11  ? 88.630  3.641   -25.347 1.00 12.06 ? 11   TYR A C     1 
ATOM   80    O O     . TYR A  1  11  ? 89.262  3.071   -26.234 1.00 12.33 ? 11   TYR A O     1 
ATOM   81    C CB    . TYR A  1  11  ? 87.080  1.860   -24.503 1.00 10.24 ? 11   TYR A CB    1 
ATOM   82    C CG    . TYR A  1  11  ? 85.864  2.463   -25.180 1.00 10.13 ? 11   TYR A CG    1 
ATOM   83    C CD1   . TYR A  1  11  ? 85.900  2.827   -26.522 1.00 8.96  ? 11   TYR A CD1   1 
ATOM   84    C CD2   . TYR A  1  11  ? 84.675  2.658   -24.477 1.00 9.55  ? 11   TYR A CD2   1 
ATOM   85    C CE1   . TYR A  1  11  ? 84.782  3.370   -27.158 1.00 10.00 ? 11   TYR A CE1   1 
ATOM   86    C CE2   . TYR A  1  11  ? 83.549  3.201   -25.103 1.00 9.18  ? 11   TYR A CE2   1 
ATOM   87    C CZ    . TYR A  1  11  ? 83.611  3.551   -26.441 1.00 8.76  ? 11   TYR A CZ    1 
ATOM   88    O OH    . TYR A  1  11  ? 82.501  4.066   -27.074 1.00 10.05 ? 11   TYR A OH    1 
ATOM   89    N N     . LEU A  1  12  ? 88.322  4.932   -25.414 1.00 12.19 ? 12   LEU A N     1 
ATOM   90    C CA    . LEU A  1  12  ? 88.737  5.728   -26.561 1.00 12.59 ? 12   LEU A CA    1 
ATOM   91    C C     . LEU A  1  12  ? 90.255  5.730   -26.726 1.00 12.61 ? 12   LEU A C     1 
ATOM   92    O O     . LEU A  1  12  ? 90.764  6.010   -27.811 1.00 13.10 ? 12   LEU A O     1 
ATOM   93    C CB    . LEU A  1  12  ? 88.230  7.165   -26.427 1.00 14.14 ? 12   LEU A CB    1 
ATOM   94    C CG    . LEU A  1  12  ? 86.714  7.340   -26.567 1.00 14.77 ? 12   LEU A CG    1 
ATOM   95    C CD1   . LEU A  1  12  ? 86.357  8.810   -26.430 1.00 16.53 ? 12   LEU A CD1   1 
ATOM   96    C CD2   . LEU A  1  12  ? 86.254  6.802   -27.918 1.00 13.78 ? 12   LEU A CD2   1 
ATOM   97    N N     . SER A  1  13  ? 90.971  5.407   -25.651 1.00 12.48 ? 13   SER A N     1 
ATOM   98    C CA    . SER A  1  13  ? 92.431  5.383   -25.693 1.00 13.74 ? 13   SER A CA    1 
ATOM   99    C C     . SER A  1  13  ? 92.944  4.332   -26.672 1.00 13.13 ? 13   SER A C     1 
ATOM   100   O O     . SER A  1  13  ? 94.056  4.450   -27.192 1.00 13.23 ? 13   SER A O     1 
ATOM   101   C CB    . SER A  1  13  ? 93.005  5.116   -24.299 1.00 14.38 ? 13   SER A CB    1 
ATOM   102   O OG    . SER A  1  13  ? 92.693  3.811   -23.853 1.00 16.51 ? 13   SER A OG    1 
ATOM   103   N N     . PHE A  1  14  ? 92.141  3.300   -26.917 1.00 11.50 ? 14   PHE A N     1 
ATOM   104   C CA    . PHE A  1  14  ? 92.538  2.261   -27.855 1.00 9.82  ? 14   PHE A CA    1 
ATOM   105   C C     . PHE A  1  14  ? 91.570  2.113   -29.028 1.00 10.14 ? 14   PHE A C     1 
ATOM   106   O O     . PHE A  1  14  ? 91.448  1.042   -29.620 1.00 10.45 ? 14   PHE A O     1 
ATOM   107   C CB    . PHE A  1  14  ? 92.754  0.912   -27.134 1.00 10.98 ? 14   PHE A CB    1 
ATOM   108   C CG    . PHE A  1  14  ? 91.590  0.449   -26.291 1.00 10.82 ? 14   PHE A CG    1 
ATOM   109   C CD1   . PHE A  1  14  ? 90.465  -0.123  -26.878 1.00 9.81  ? 14   PHE A CD1   1 
ATOM   110   C CD2   . PHE A  1  14  ? 91.648  0.535   -24.903 1.00 11.96 ? 14   PHE A CD2   1 
ATOM   111   C CE1   . PHE A  1  14  ? 89.415  -0.610  -26.089 1.00 10.26 ? 14   PHE A CE1   1 
ATOM   112   C CE2   . PHE A  1  14  ? 90.605  0.053   -24.107 1.00 12.97 ? 14   PHE A CE2   1 
ATOM   113   C CZ    . PHE A  1  14  ? 89.488  -0.522  -24.703 1.00 11.51 ? 14   PHE A CZ    1 
ATOM   114   N N     . ALA A  1  15  ? 90.898  3.209   -29.368 1.00 9.77  ? 15   ALA A N     1 
ATOM   115   C CA    . ALA A  1  15  ? 89.967  3.220   -30.492 1.00 12.07 ? 15   ALA A CA    1 
ATOM   116   C C     . ALA A  1  15  ? 90.631  4.004   -31.619 1.00 14.40 ? 15   ALA A C     1 
ATOM   117   O O     . ALA A  1  15  ? 91.203  5.072   -31.391 1.00 16.44 ? 15   ALA A O     1 
ATOM   118   C CB    . ALA A  1  15  ? 88.651  3.882   -30.090 1.00 12.55 ? 15   ALA A CB    1 
ATOM   119   N N     . TYR A  1  16  ? 90.564  3.467   -32.831 1.00 13.45 ? 16   TYR A N     1 
ATOM   120   C CA    . TYR A  1  16  ? 91.177  4.117   -33.981 1.00 13.98 ? 16   TYR A CA    1 
ATOM   121   C C     . TYR A  1  16  ? 90.259  4.097   -35.183 1.00 13.67 ? 16   TYR A C     1 
ATOM   122   O O     . TYR A  1  16  ? 89.394  3.231   -35.302 1.00 12.24 ? 16   TYR A O     1 
ATOM   123   C CB    . TYR A  1  16  ? 92.470  3.401   -34.379 1.00 15.66 ? 16   TYR A CB    1 
ATOM   124   C CG    . TYR A  1  16  ? 93.446  3.186   -33.253 1.00 16.85 ? 16   TYR A CG    1 
ATOM   125   C CD1   . TYR A  1  16  ? 93.242  2.178   -32.311 1.00 15.53 ? 16   TYR A CD1   1 
ATOM   126   C CD2   . TYR A  1  16  ? 94.567  4.004   -33.115 1.00 18.26 ? 16   TYR A CD2   1 
ATOM   127   C CE1   . TYR A  1  16  ? 94.130  1.991   -31.255 1.00 17.12 ? 16   TYR A CE1   1 
ATOM   128   C CE2   . TYR A  1  16  ? 95.461  3.827   -32.063 1.00 19.75 ? 16   TYR A CE2   1 
ATOM   129   C CZ    . TYR A  1  16  ? 95.235  2.820   -31.137 1.00 19.69 ? 16   TYR A CZ    1 
ATOM   130   O OH    . TYR A  1  16  ? 96.105  2.654   -30.083 1.00 22.16 ? 16   TYR A OH    1 
ATOM   131   N N     . ASP A  1  17  ? 90.451  5.056   -36.079 1.00 14.33 ? 17   ASP A N     1 
ATOM   132   C CA    . ASP A  1  17  ? 89.671  5.082   -37.303 1.00 14.28 ? 17   ASP A CA    1 
ATOM   133   C C     . ASP A  1  17  ? 90.422  4.097   -38.189 1.00 14.27 ? 17   ASP A C     1 
ATOM   134   O O     . ASP A  1  17  ? 91.648  3.999   -38.107 1.00 14.36 ? 17   ASP A O     1 
ATOM   135   C CB    . ASP A  1  17  ? 89.677  6.478   -37.928 1.00 14.50 ? 17   ASP A CB    1 
ATOM   136   C CG    . ASP A  1  17  ? 88.802  6.564   -39.165 1.00 14.44 ? 17   ASP A CG    1 
ATOM   137   O OD1   . ASP A  1  17  ? 89.205  6.042   -40.225 1.00 15.25 ? 17   ASP A OD1   1 
ATOM   138   O OD2   . ASP A  1  17  ? 87.702  7.144   -39.072 1.00 17.70 ? 17   ASP A OD2   1 
ATOM   139   N N     . ALA A  1  18  ? 89.699  3.351   -39.016 1.00 14.56 ? 18   ALA A N     1 
ATOM   140   C CA    . ALA A  1  18  ? 90.331  2.364   -39.885 1.00 13.78 ? 18   ALA A CA    1 
ATOM   141   C C     . ALA A  1  18  ? 91.481  2.944   -40.707 1.00 15.48 ? 18   ALA A C     1 
ATOM   142   O O     . ALA A  1  18  ? 92.456  2.246   -40.991 1.00 15.19 ? 18   ALA A O     1 
ATOM   143   C CB    . ALA A  1  18  ? 89.292  1.736   -40.807 1.00 15.08 ? 18   ALA A CB    1 
ATOM   144   N N     . THR A  1  19  ? 91.370  4.216   -41.084 1.00 15.76 ? 19   THR A N     1 
ATOM   145   C CA    . THR A  1  19  ? 92.414  4.862   -41.876 1.00 17.66 ? 19   THR A CA    1 
ATOM   146   C C     . THR A  1  19  ? 93.736  4.936   -41.123 1.00 19.35 ? 19   THR A C     1 
ATOM   147   O O     . THR A  1  19  ? 94.794  5.101   -41.730 1.00 20.14 ? 19   THR A O     1 
ATOM   148   C CB    . THR A  1  19  ? 92.022  6.302   -42.281 1.00 16.34 ? 19   THR A CB    1 
ATOM   149   O OG1   . THR A  1  19  ? 91.742  7.071   -41.104 1.00 18.24 ? 19   THR A OG1   1 
ATOM   150   C CG2   . THR A  1  19  ? 90.807  6.293   -43.189 1.00 16.32 ? 19   THR A CG2   1 
ATOM   151   N N     . ASP A  1  20  ? 93.609  4.768   -39.899 1.00 20.06 ? 20   ASP A N     1 
ATOM   152   C CA    . ASP A  1  20  ? 94.787  4.870   -39.048 1.00 20.30 ? 20   ASP A CA    1 
ATOM   153   C C     . ASP A  1  20  ? 95.355  3.517   -38.625 1.00 20.54 ? 20   ASP A C     1 
ATOM   154   O O     . ASP A  1  20  ? 96.404  3.454   -37.985 1.00 20.59 ? 20   ASP A O     1 
ATOM   155   C CB    . ASP A  1  20  ? 94.457  5.723   -37.819 1.00 21.82 ? 20   ASP A CB    1 
ATOM   156   C CG    . ASP A  1  20  ? 94.310  7.200   -38.160 1.00 24.29 ? 20   ASP A CG    1 
ATOM   157   O OD1   . ASP A  1  20  ? 94.691  7.604   -39.278 1.00 25.52 ? 20   ASP A OD1   1 
ATOM   158   O OD2   . ASP A  1  20  ? 93.804  7.960   -37.305 1.00 27.40 ? 20   ASP A OD2   1 
ATOM   159   N N     . LEU A  1  21  ? 94.684  2.457   -38.897 1.00 19.39 ? 21   LEU A N     1 
ATOM   160   C CA    . LEU A  1  21  ? 95.112  1.100   -38.569 1.00 17.98 ? 21   LEU A CA    1 
ATOM   161   C C     . LEU A  1  21  ? 96.111  0.619   -39.611 1.00 18.48 ? 21   LEU A C     1 
ATOM   162   O O     . LEU A  1  21  ? 96.079  1.064   -40.758 1.00 20.41 ? 21   LEU A O     1 
ATOM   163   C CB    . LEU A  1  21  ? 93.912  0.149   -38.543 1.00 17.00 ? 21   LEU A CB    1 
ATOM   164   C CG    . LEU A  1  21  ? 92.899  0.365   -37.419 1.00 17.47 ? 21   LEU A CG    1 
ATOM   165   C CD1   . LEU A  1  21  ? 91.735  -0.596  -37.591 1.00 16.58 ? 21   LEU A CD1   1 
ATOM   166   C CD2   . LEU A  1  21  ? 93.575  0.151   -36.074 1.00 17.82 ? 21   LEU A CD2   1 
ATOM   167   N N     . GLU A  1  22  ? 96.991  -0.296  -39.215 1.00 19.23 ? 22   GLU A N     1 
ATOM   168   C CA    . GLU A  1  22  ? 97.993  -0.823  -40.134 1.00 18.69 ? 22   GLU A CA    1 
ATOM   169   C C     . GLU A  1  22  ? 97.319  -1.496  -41.328 1.00 19.14 ? 22   GLU A C     1 
ATOM   170   O O     . GLU A  1  22  ? 96.196  -1.991  -41.215 1.00 18.75 ? 22   GLU A O     1 
ATOM   171   C CB    . GLU A  1  22  ? 98.906  -1.825  -39.412 1.00 19.44 ? 22   GLU A CB    1 
ATOM   172   C CG    . GLU A  1  22  ? 98.248  -3.135  -38.967 1.00 20.03 ? 22   GLU A CG    1 
ATOM   173   C CD    . GLU A  1  22  ? 97.196  -2.955  -37.885 1.00 21.54 ? 22   GLU A CD    1 
ATOM   174   O OE1   . GLU A  1  22  ? 97.366  -2.070  -37.018 1.00 19.84 ? 22   GLU A OE1   1 
ATOM   175   O OE2   . GLU A  1  22  ? 96.204  -3.718  -37.890 1.00 21.97 ? 22   GLU A OE2   1 
ATOM   176   N N     . LEU A  1  23  ? 98.001  -1.505  -42.472 1.00 17.86 ? 23   LEU A N     1 
ATOM   177   C CA    . LEU A  1  23  ? 97.458  -2.118  -43.681 1.00 17.30 ? 23   LEU A CA    1 
ATOM   178   C C     . LEU A  1  23  ? 97.385  -3.635  -43.537 1.00 17.39 ? 23   LEU A C     1 
ATOM   179   O O     . LEU A  1  23  ? 96.515  -4.280  -44.123 1.00 17.68 ? 23   LEU A O     1 
ATOM   180   C CB    . LEU A  1  23  ? 98.316  -1.757  -44.896 1.00 19.12 ? 23   LEU A CB    1 
ATOM   181   C CG    . LEU A  1  23  ? 98.389  -0.276  -45.273 1.00 20.81 ? 23   LEU A CG    1 
ATOM   182   C CD1   . LEU A  1  23  ? 99.305  -0.114  -46.479 1.00 21.73 ? 23   LEU A CD1   1 
ATOM   183   C CD2   . LEU A  1  23  ? 96.999  0.257   -45.584 1.00 20.54 ? 23   LEU A CD2   1 
ATOM   184   N N     . GLU A  1  24  ? 98.312  -4.214  -42.757 1.00 15.97 ? 24   GLU A N     1 
ATOM   185   C CA    . GLU A  1  24  ? 98.334  -5.655  -42.519 1.00 17.50 ? 24   GLU A CA    1 
ATOM   186   C C     . GLU A  1  24  ? 98.706  -5.930  -41.066 1.00 17.24 ? 24   GLU A C     1 
ATOM   187   O O     . GLU A  1  24  ? 99.858  -5.748  -40.664 1.00 18.14 ? 24   GLU A O     1 
ATOM   188   C CB    . GLU A  1  24  ? 99.333  -6.345  -43.450 1.00 19.80 ? 24   GLU A CB    1 
ATOM   189   C CG    . GLU A  1  24  ? 99.358  -7.860  -43.299 1.00 24.10 ? 24   GLU A CG    1 
ATOM   190   C CD    . GLU A  1  24  ? 100.316 -8.534  -44.264 1.00 28.47 ? 24   GLU A CD    1 
ATOM   191   O OE1   . GLU A  1  24  ? 100.962 -7.816  -45.058 1.00 31.42 ? 24   GLU A OE1   1 
ATOM   192   O OE2   . GLU A  1  24  ? 100.430 -9.779  -44.227 1.00 30.37 ? 24   GLU A OE2   1 
ATOM   193   N N     . GLY A  1  25  ? 97.720  -6.355  -40.297 1.00 14.21 ? 25   GLY A N     1 
ATOM   194   C CA    . GLY A  1  25  ? 97.958  -6.633  -38.894 1.00 13.59 ? 25   GLY A CA    1 
ATOM   195   C C     . GLY A  1  25  ? 97.846  -8.099  -38.525 1.00 12.56 ? 25   GLY A C     1 
ATOM   196   O O     . GLY A  1  25  ? 97.281  -8.901  -39.269 1.00 13.03 ? 25   GLY A O     1 
ATOM   197   N N     . SER A  1  26  ? 98.391  -8.439  -37.362 1.00 11.81 ? 26   SER A N     1 
ATOM   198   C CA    . SER A  1  26  ? 98.378  -9.807  -36.854 1.00 12.05 ? 26   SER A CA    1 
ATOM   199   C C     . SER A  1  26  ? 97.887  -9.795  -35.406 1.00 12.22 ? 26   SER A C     1 
ATOM   200   O O     . SER A  1  26  ? 98.428  -9.071  -34.573 1.00 12.75 ? 26   SER A O     1 
ATOM   201   C CB    . SER A  1  26  ? 99.794  -10.387 -36.916 1.00 12.28 ? 26   SER A CB    1 
ATOM   202   O OG    . SER A  1  26  ? 99.828  -11.716 -36.439 1.00 12.70 ? 26   SER A OG    1 
ATOM   203   N N     . TYR A  1  27  ? 96.864  -10.596 -35.113 1.00 11.00 ? 27   TYR A N     1 
ATOM   204   C CA    . TYR A  1  27  ? 96.296  -10.667 -33.765 1.00 9.28  ? 27   TYR A CA    1 
ATOM   205   C C     . TYR A  1  27  ? 95.951  -12.099 -33.390 1.00 9.61  ? 27   TYR A C     1 
ATOM   206   O O     . TYR A  1  27  ? 96.106  -13.010 -34.197 1.00 10.66 ? 27   TYR A O     1 
ATOM   207   C CB    . TYR A  1  27  ? 95.014  -9.831  -33.679 1.00 9.46  ? 27   TYR A CB    1 
ATOM   208   C CG    . TYR A  1  27  ? 95.188  -8.389  -34.085 1.00 9.42  ? 27   TYR A CG    1 
ATOM   209   C CD1   . TYR A  1  27  ? 95.211  -8.021  -35.430 1.00 10.55 ? 27   TYR A CD1   1 
ATOM   210   C CD2   . TYR A  1  27  ? 95.365  -7.394  -33.125 1.00 8.66  ? 27   TYR A CD2   1 
ATOM   211   C CE1   . TYR A  1  27  ? 95.410  -6.698  -35.807 1.00 11.90 ? 27   TYR A CE1   1 
ATOM   212   C CE2   . TYR A  1  27  ? 95.566  -6.067  -33.491 1.00 11.06 ? 27   TYR A CE2   1 
ATOM   213   C CZ    . TYR A  1  27  ? 95.588  -5.728  -34.832 1.00 11.68 ? 27   TYR A CZ    1 
ATOM   214   O OH    . TYR A  1  27  ? 95.793  -4.419  -35.203 1.00 14.38 ? 27   TYR A OH    1 
ATOM   215   N N     . ASP A  1  28  ? 95.490  -12.294 -32.158 1.00 9.27  ? 28   ASP A N     1 
ATOM   216   C CA    . ASP A  1  28  ? 95.075  -13.620 -31.719 1.00 8.17  ? 28   ASP A CA    1 
ATOM   217   C C     . ASP A  1  28  ? 93.614  -13.785 -32.126 1.00 9.45  ? 28   ASP A C     1 
ATOM   218   O O     . ASP A  1  28  ? 93.209  -14.852 -32.589 1.00 9.47  ? 28   ASP A O     1 
ATOM   219   C CB    . ASP A  1  28  ? 95.207  -13.771 -30.201 1.00 10.21 ? 28   ASP A CB    1 
ATOM   220   C CG    . ASP A  1  28  ? 96.650  -13.852 -29.748 1.00 10.29 ? 28   ASP A CG    1 
ATOM   221   O OD1   . ASP A  1  28  ? 97.383  -14.740 -30.237 1.00 11.82 ? 28   ASP A OD1   1 
ATOM   222   O OD2   . ASP A  1  28  ? 97.053  -13.032 -28.899 1.00 11.19 ? 28   ASP A OD2   1 
ATOM   223   N N     . TYR A  1  29  ? 92.828  -12.724 -31.960 1.00 7.02  ? 29   TYR A N     1 
ATOM   224   C CA    . TYR A  1  29  ? 91.417  -12.765 -32.330 1.00 8.21  ? 29   TYR A CA    1 
ATOM   225   C C     . TYR A  1  29  ? 90.976  -11.509 -33.055 1.00 7.30  ? 29   TYR A C     1 
ATOM   226   O O     . TYR A  1  29  ? 91.403  -10.399 -32.727 1.00 8.74  ? 29   TYR A O     1 
ATOM   227   C CB    . TYR A  1  29  ? 90.523  -12.954 -31.095 1.00 8.29  ? 29   TYR A CB    1 
ATOM   228   C CG    . TYR A  1  29  ? 90.788  -14.236 -30.352 1.00 8.30  ? 29   TYR A CG    1 
ATOM   229   C CD1   . TYR A  1  29  ? 91.722  -14.282 -29.322 1.00 9.15  ? 29   TYR A CD1   1 
ATOM   230   C CD2   . TYR A  1  29  ? 90.154  -15.419 -30.724 1.00 9.36  ? 29   TYR A CD2   1 
ATOM   231   C CE1   . TYR A  1  29  ? 92.024  -15.477 -28.681 1.00 8.62  ? 29   TYR A CE1   1 
ATOM   232   C CE2   . TYR A  1  29  ? 90.449  -16.623 -30.089 1.00 9.12  ? 29   TYR A CE2   1 
ATOM   233   C CZ    . TYR A  1  29  ? 91.389  -16.640 -29.070 1.00 8.48  ? 29   TYR A CZ    1 
ATOM   234   O OH    . TYR A  1  29  ? 91.707  -17.822 -28.454 1.00 9.84  ? 29   TYR A OH    1 
ATOM   235   N N     . VAL A  1  30  ? 90.127  -11.701 -34.057 1.00 7.81  ? 30   VAL A N     1 
ATOM   236   C CA    . VAL A  1  30  ? 89.572  -10.595 -34.823 1.00 7.69  ? 30   VAL A CA    1 
ATOM   237   C C     . VAL A  1  30  ? 88.061  -10.731 -34.708 1.00 8.57  ? 30   VAL A C     1 
ATOM   238   O O     . VAL A  1  30  ? 87.500  -11.764 -35.067 1.00 8.86  ? 30   VAL A O     1 
ATOM   239   C CB    . VAL A  1  30  ? 89.976  -10.667 -36.313 1.00 8.20  ? 30   VAL A CB    1 
ATOM   240   C CG1   . VAL A  1  30  ? 89.200  -9.625  -37.113 1.00 10.77 ? 30   VAL A CG1   1 
ATOM   241   C CG2   . VAL A  1  30  ? 91.478  -10.439 -36.455 1.00 10.56 ? 30   VAL A CG2   1 
ATOM   242   N N     . ILE A  1  31  ? 87.412  -9.695  -34.187 1.00 8.10  ? 31   ILE A N     1 
ATOM   243   C CA    . ILE A  1  31  ? 85.965  -9.703  -34.015 1.00 9.30  ? 31   ILE A CA    1 
ATOM   244   C C     . ILE A  1  31  ? 85.319  -8.773  -35.041 1.00 8.95  ? 31   ILE A C     1 
ATOM   245   O O     . ILE A  1  31  ? 85.650  -7.587  -35.108 1.00 9.31  ? 31   ILE A O     1 
ATOM   246   C CB    . ILE A  1  31  ? 85.572  -9.217  -32.593 1.00 10.37 ? 31   ILE A CB    1 
ATOM   247   C CG1   . ILE A  1  31  ? 86.322  -10.022 -31.526 1.00 12.80 ? 31   ILE A CG1   1 
ATOM   248   C CG2   . ILE A  1  31  ? 84.072  -9.323  -32.401 1.00 11.02 ? 31   ILE A CG2   1 
ATOM   249   C CD1   . ILE A  1  31  ? 86.085  -11.511 -31.583 1.00 15.64 ? 31   ILE A CD1   1 
ATOM   250   N N     . VAL A  1  32  ? 84.402  -9.310  -35.840 1.00 7.28  ? 32   VAL A N     1 
ATOM   251   C CA    . VAL A  1  32  ? 83.717  -8.504  -36.846 1.00 7.40  ? 32   VAL A CA    1 
ATOM   252   C C     . VAL A  1  32  ? 82.409  -7.992  -36.260 1.00 6.87  ? 32   VAL A C     1 
ATOM   253   O O     . VAL A  1  32  ? 81.494  -8.771  -35.979 1.00 7.44  ? 32   VAL A O     1 
ATOM   254   C CB    . VAL A  1  32  ? 83.410  -9.323  -38.121 1.00 4.99  ? 32   VAL A CB    1 
ATOM   255   C CG1   . VAL A  1  32  ? 82.723  -8.434  -39.159 1.00 8.07  ? 32   VAL A CG1   1 
ATOM   256   C CG2   . VAL A  1  32  ? 84.699  -9.900  -38.684 1.00 7.65  ? 32   VAL A CG2   1 
ATOM   257   N N     . GLY A  1  33  ? 82.330  -6.678  -36.067 1.00 7.23  ? 33   GLY A N     1 
ATOM   258   C CA    . GLY A  1  33  ? 81.132  -6.081  -35.507 1.00 7.13  ? 33   GLY A CA    1 
ATOM   259   C C     . GLY A  1  33  ? 81.292  -5.780  -34.027 1.00 8.22  ? 33   GLY A C     1 
ATOM   260   O O     . GLY A  1  33  ? 81.279  -6.690  -33.200 1.00 9.03  ? 33   GLY A O     1 
ATOM   261   N N     . GLY A  1  34  ? 81.454  -4.503  -33.693 1.00 7.29  ? 34   GLY A N     1 
ATOM   262   C CA    . GLY A  1  34  ? 81.603  -4.121  -32.301 1.00 6.11  ? 34   GLY A CA    1 
ATOM   263   C C     . GLY A  1  34  ? 80.234  -3.812  -31.736 1.00 6.95  ? 34   GLY A C     1 
ATOM   264   O O     . GLY A  1  34  ? 79.961  -2.688  -31.308 1.00 7.62  ? 34   GLY A O     1 
ATOM   265   N N     . GLY A  1  35  ? 79.367  -4.820  -31.744 1.00 7.28  ? 35   GLY A N     1 
ATOM   266   C CA    . GLY A  1  35  ? 78.011  -4.635  -31.263 1.00 6.39  ? 35   GLY A CA    1 
ATOM   267   C C     . GLY A  1  35  ? 77.705  -5.147  -29.871 1.00 6.42  ? 35   GLY A C     1 
ATOM   268   O O     . GLY A  1  35  ? 78.587  -5.256  -29.016 1.00 6.58  ? 35   GLY A O     1 
ATOM   269   N N     . THR A  1  36  ? 76.433  -5.476  -29.663 1.00 6.12  ? 36   THR A N     1 
ATOM   270   C CA    . THR A  1  36  ? 75.920  -5.966  -28.393 1.00 6.12  ? 36   THR A CA    1 
ATOM   271   C C     . THR A  1  36  ? 76.697  -7.174  -27.870 1.00 6.26  ? 36   THR A C     1 
ATOM   272   O O     . THR A  1  36  ? 77.137  -7.175  -26.721 1.00 7.52  ? 36   THR A O     1 
ATOM   273   C CB    . THR A  1  36  ? 74.422  -6.303  -28.530 1.00 7.29  ? 36   THR A CB    1 
ATOM   274   O OG1   . THR A  1  36  ? 73.736  -5.159  -29.062 1.00 6.54  ? 36   THR A OG1   1 
ATOM   275   C CG2   . THR A  1  36  ? 73.818  -6.650  -27.177 1.00 6.60  ? 36   THR A CG2   1 
ATOM   276   N N     . SER A  1  37  ? 76.870  -8.197  -28.702 1.00 6.77  ? 37   SER A N     1 
ATOM   277   C CA    . SER A  1  37  ? 77.634  -9.374  -28.286 1.00 6.29  ? 37   SER A CA    1 
ATOM   278   C C     . SER A  1  37  ? 79.131  -9.173  -28.532 1.00 6.05  ? 37   SER A C     1 
ATOM   279   O O     . SER A  1  37  ? 79.964  -9.593  -27.729 1.00 6.96  ? 37   SER A O     1 
ATOM   280   C CB    . SER A  1  37  ? 77.184  -10.626 -29.052 1.00 5.19  ? 37   SER A CB    1 
ATOM   281   O OG    . SER A  1  37  ? 75.867  -11.023 -28.712 1.00 6.78  ? 37   SER A OG    1 
ATOM   282   N N     . GLY A  1  38  ? 79.460  -8.529  -29.649 1.00 5.87  ? 38   GLY A N     1 
ATOM   283   C CA    . GLY A  1  38  ? 80.850  -8.308  -30.013 1.00 5.92  ? 38   GLY A CA    1 
ATOM   284   C C     . GLY A  1  38  ? 81.732  -7.585  -29.009 1.00 7.06  ? 38   GLY A C     1 
ATOM   285   O O     . GLY A  1  38  ? 82.880  -7.977  -28.801 1.00 7.19  ? 38   GLY A O     1 
ATOM   286   N N     . CYS A  1  39  ? 81.216  -6.528  -28.392 1.00 7.61  ? 39   CYS A N     1 
ATOM   287   C CA    . CYS A  1  39  ? 82.015  -5.774  -27.428 1.00 7.57  ? 39   CYS A CA    1 
ATOM   288   C C     . CYS A  1  39  ? 82.413  -6.586  -26.190 1.00 8.66  ? 39   CYS A C     1 
ATOM   289   O O     . CYS A  1  39  ? 83.597  -6.667  -25.858 1.00 8.88  ? 39   CYS A O     1 
ATOM   290   C CB    . CYS A  1  39  ? 81.280  -4.488  -27.032 1.00 8.90  ? 39   CYS A CB    1 
ATOM   291   S SG    . CYS A  1  39  ? 81.274  -3.249  -28.361 1.00 9.78  ? 39   CYS A SG    1 
ATOM   292   N N     . PRO A  1  40  ? 81.442  -7.191  -25.484 1.00 7.50  ? 40   PRO A N     1 
ATOM   293   C CA    . PRO A  1  40  ? 81.834  -7.974  -24.305 1.00 8.56  ? 40   PRO A CA    1 
ATOM   294   C C     . PRO A  1  40  ? 82.698  -9.186  -24.663 1.00 8.94  ? 40   PRO A C     1 
ATOM   295   O O     . PRO A  1  40  ? 83.520  -9.627  -23.861 1.00 8.26  ? 40   PRO A O     1 
ATOM   296   C CB    . PRO A  1  40  ? 80.495  -8.355  -23.665 1.00 7.85  ? 40   PRO A CB    1 
ATOM   297   C CG    . PRO A  1  40  ? 79.508  -8.264  -24.811 1.00 6.31  ? 40   PRO A CG    1 
ATOM   298   C CD    . PRO A  1  40  ? 79.977  -7.053  -25.564 1.00 7.89  ? 40   PRO A CD    1 
ATOM   299   N N     . LEU A  1  41  ? 82.508  -9.721  -25.864 1.00 8.34  ? 41   LEU A N     1 
ATOM   300   C CA    . LEU A  1  41  ? 83.311  -10.851 -26.326 1.00 8.77  ? 41   LEU A CA    1 
ATOM   301   C C     . LEU A  1  41  ? 84.756  -10.376 -26.480 1.00 9.26  ? 41   LEU A C     1 
ATOM   302   O O     . LEU A  1  41  ? 85.692  -11.009 -25.992 1.00 9.36  ? 41   LEU A O     1 
ATOM   303   C CB    . LEU A  1  41  ? 82.798  -11.354 -27.681 1.00 8.65  ? 41   LEU A CB    1 
ATOM   304   C CG    . LEU A  1  41  ? 83.708  -12.339 -28.427 1.00 10.16 ? 41   LEU A CG    1 
ATOM   305   C CD1   . LEU A  1  41  ? 83.838  -13.646 -27.642 1.00 9.62  ? 41   LEU A CD1   1 
ATOM   306   C CD2   . LEU A  1  41  ? 83.132  -12.599 -29.811 1.00 9.57  ? 41   LEU A CD2   1 
ATOM   307   N N     . ALA A  1  42  ? 84.927  -9.249  -27.161 1.00 8.81  ? 42   ALA A N     1 
ATOM   308   C CA    . ALA A  1  42  ? 86.251  -8.684  -27.388 1.00 9.03  ? 42   ALA A CA    1 
ATOM   309   C C     . ALA A  1  42  ? 86.962  -8.350  -26.078 1.00 9.97  ? 42   ALA A C     1 
ATOM   310   O O     . ALA A  1  42  ? 88.137  -8.672  -25.895 1.00 10.46 ? 42   ALA A O     1 
ATOM   311   C CB    . ALA A  1  42  ? 86.131  -7.438  -28.244 1.00 10.03 ? 42   ALA A CB    1 
ATOM   312   N N     . ALA A  1  43  ? 86.253  -7.692  -25.170 1.00 8.10  ? 43   ALA A N     1 
ATOM   313   C CA    . ALA A  1  43  ? 86.840  -7.319  -23.890 1.00 8.71  ? 43   ALA A CA    1 
ATOM   314   C C     . ALA A  1  43  ? 87.304  -8.553  -23.123 1.00 8.67  ? 43   ALA A C     1 
ATOM   315   O O     . ALA A  1  43  ? 88.403  -8.576  -22.565 1.00 8.73  ? 43   ALA A O     1 
ATOM   316   C CB    . ALA A  1  43  ? 85.829  -6.537  -23.060 1.00 7.30  ? 43   ALA A CB    1 
ATOM   317   N N     . THR A  1  44  ? 86.466  -9.583  -23.106 1.00 7.99  ? 44   THR A N     1 
ATOM   318   C CA    . THR A  1  44  ? 86.794  -10.811 -22.398 1.00 8.37  ? 44   THR A CA    1 
ATOM   319   C C     . THR A  1  44  ? 88.049  -11.474 -22.957 1.00 9.68  ? 44   THR A C     1 
ATOM   320   O O     . THR A  1  44  ? 88.966  -11.814 -22.208 1.00 9.40  ? 44   THR A O     1 
ATOM   321   C CB    . THR A  1  44  ? 85.609  -11.789 -22.452 1.00 9.54  ? 44   THR A CB    1 
ATOM   322   O OG1   . THR A  1  44  ? 84.491  -11.203 -21.773 1.00 8.12  ? 44   THR A OG1   1 
ATOM   323   C CG2   . THR A  1  44  ? 85.964  -13.111 -21.784 1.00 10.59 ? 44   THR A CG2   1 
ATOM   324   N N     . LEU A  1  45  ? 88.095  -11.652 -24.272 1.00 7.16  ? 45   LEU A N     1 
ATOM   325   C CA    . LEU A  1  45  ? 89.259  -12.268 -24.895 1.00 8.16  ? 45   LEU A CA    1 
ATOM   326   C C     . LEU A  1  45  ? 90.527  -11.451 -24.651 1.00 9.65  ? 45   LEU A C     1 
ATOM   327   O O     . LEU A  1  45  ? 91.603  -12.019 -24.479 1.00 9.46  ? 45   LEU A O     1 
ATOM   328   C CB    . LEU A  1  45  ? 89.034  -12.435 -26.402 1.00 6.93  ? 45   LEU A CB    1 
ATOM   329   C CG    . LEU A  1  45  ? 88.007  -13.496 -26.811 1.00 6.52  ? 45   LEU A CG    1 
ATOM   330   C CD1   . LEU A  1  45  ? 87.747  -13.410 -28.304 1.00 8.16  ? 45   LEU A CD1   1 
ATOM   331   C CD2   . LEU A  1  45  ? 88.508  -14.881 -26.430 1.00 9.09  ? 45   LEU A CD2   1 
ATOM   332   N N     . SER A  1  46  ? 90.398  -10.124 -24.619 1.00 9.65  ? 46   SER A N     1 
ATOM   333   C CA    . SER A  1  46  ? 91.560  -9.255  -24.423 1.00 9.80  ? 46   SER A CA    1 
ATOM   334   C C     . SER A  1  46  ? 92.197  -9.393  -23.043 1.00 10.00 ? 46   SER A C     1 
ATOM   335   O O     . SER A  1  46  ? 93.291  -8.881  -22.807 1.00 10.34 ? 46   SER A O     1 
ATOM   336   C CB    . SER A  1  46  ? 91.188  -7.784  -24.670 1.00 9.14  ? 46   SER A CB    1 
ATOM   337   O OG    . SER A  1  46  ? 90.481  -7.226  -23.575 1.00 9.37  ? 46   SER A OG    1 
ATOM   338   N N     . GLU A  1  47  ? 91.517  -10.075 -22.128 1.00 10.32 ? 47   GLU A N     1 
ATOM   339   C CA    . GLU A  1  47  ? 92.067  -10.264 -20.793 1.00 11.23 ? 47   GLU A CA    1 
ATOM   340   C C     . GLU A  1  47  ? 93.382  -11.034 -20.875 1.00 11.92 ? 47   GLU A C     1 
ATOM   341   O O     . GLU A  1  47  ? 94.265  -10.872 -20.026 1.00 12.85 ? 47   GLU A O     1 
ATOM   342   C CB    . GLU A  1  47  ? 91.070  -11.019 -19.910 1.00 13.27 ? 47   GLU A CB    1 
ATOM   343   C CG    . GLU A  1  47  ? 89.896  -10.165 -19.443 1.00 15.70 ? 47   GLU A CG    1 
ATOM   344   C CD    . GLU A  1  47  ? 88.891  -10.948 -18.621 1.00 18.72 ? 47   GLU A CD    1 
ATOM   345   O OE1   . GLU A  1  47  ? 89.314  -11.854 -17.871 1.00 20.87 ? 47   GLU A OE1   1 
ATOM   346   O OE2   . GLU A  1  47  ? 87.680  -10.651 -18.709 1.00 18.21 ? 47   GLU A OE2   1 
ATOM   347   N N     . LYS A  1  48  ? 93.519  -11.855 -21.912 1.00 11.35 ? 48   LYS A N     1 
ATOM   348   C CA    . LYS A  1  48  ? 94.722  -12.660 -22.095 1.00 11.20 ? 48   LYS A CA    1 
ATOM   349   C C     . LYS A  1  48  ? 95.367  -12.566 -23.475 1.00 11.62 ? 48   LYS A C     1 
ATOM   350   O O     . LYS A  1  48  ? 96.581  -12.744 -23.607 1.00 11.40 ? 48   LYS A O     1 
ATOM   351   C CB    . LYS A  1  48  ? 94.410  -14.131 -21.806 1.00 12.21 ? 48   LYS A CB    1 
ATOM   352   C CG    . LYS A  1  48  ? 94.119  -14.439 -20.348 1.00 18.48 ? 48   LYS A CG    1 
ATOM   353   C CD    . LYS A  1  48  ? 93.771  -15.908 -20.166 1.00 22.98 ? 48   LYS A CD    1 
ATOM   354   C CE    . LYS A  1  48  ? 93.807  -16.310 -18.699 1.00 26.11 ? 48   LYS A CE    1 
ATOM   355   N NZ    . LYS A  1  48  ? 92.956  -15.437 -17.849 1.00 29.23 ? 48   LYS A NZ    1 
ATOM   356   N N     . TYR A  1  49  ? 94.569  -12.285 -24.502 1.00 10.37 ? 49   TYR A N     1 
ATOM   357   C CA    . TYR A  1  49  ? 95.105  -12.239 -25.858 1.00 9.56  ? 49   TYR A CA    1 
ATOM   358   C C     . TYR A  1  49  ? 94.938  -10.925 -26.610 1.00 9.40  ? 49   TYR A C     1 
ATOM   359   O O     . TYR A  1  49  ? 94.202  -10.039 -26.179 1.00 9.41  ? 49   TYR A O     1 
ATOM   360   C CB    . TYR A  1  49  ? 94.500  -13.386 -26.674 1.00 10.47 ? 49   TYR A CB    1 
ATOM   361   C CG    . TYR A  1  49  ? 94.845  -14.752 -26.123 1.00 11.82 ? 49   TYR A CG    1 
ATOM   362   C CD1   . TYR A  1  49  ? 93.938  -15.466 -25.336 1.00 13.46 ? 49   TYR A CD1   1 
ATOM   363   C CD2   . TYR A  1  49  ? 96.094  -15.318 -26.367 1.00 14.28 ? 49   TYR A CD2   1 
ATOM   364   C CE1   . TYR A  1  49  ? 94.274  -16.718 -24.806 1.00 14.57 ? 49   TYR A CE1   1 
ATOM   365   C CE2   . TYR A  1  49  ? 96.440  -16.559 -25.842 1.00 15.22 ? 49   TYR A CE2   1 
ATOM   366   C CZ    . TYR A  1  49  ? 95.529  -17.254 -25.066 1.00 15.23 ? 49   TYR A CZ    1 
ATOM   367   O OH    . TYR A  1  49  ? 95.884  -18.486 -24.559 1.00 17.38 ? 49   TYR A OH    1 
ATOM   368   N N     . LYS A  1  50  ? 95.638  -10.812 -27.740 1.00 9.27  ? 50   LYS A N     1 
ATOM   369   C CA    . LYS A  1  50  ? 95.589  -9.613  -28.573 1.00 7.31  ? 50   LYS A CA    1 
ATOM   370   C C     . LYS A  1  50  ? 94.349  -9.670  -29.450 1.00 8.82  ? 50   LYS A C     1 
ATOM   371   O O     . LYS A  1  50  ? 94.192  -10.574 -30.271 1.00 8.80  ? 50   LYS A O     1 
ATOM   372   C CB    . LYS A  1  50  ? 96.849  -9.519  -29.432 1.00 8.38  ? 50   LYS A CB    1 
ATOM   373   C CG    . LYS A  1  50  ? 98.137  -9.442  -28.616 1.00 9.24  ? 50   LYS A CG    1 
ATOM   374   C CD    . LYS A  1  50  ? 98.217  -8.152  -27.816 1.00 9.26  ? 50   LYS A CD    1 
ATOM   375   C CE    . LYS A  1  50  ? 99.509  -8.090  -27.008 1.00 10.72 ? 50   LYS A CE    1 
ATOM   376   N NZ    . LYS A  1  50  ? 99.642  -6.794  -26.281 1.00 10.15 ? 50   LYS A NZ    1 
ATOM   377   N N     . VAL A  1  51  ? 93.481  -8.680  -29.274 1.00 8.73  ? 51   VAL A N     1 
ATOM   378   C CA    . VAL A  1  51  ? 92.218  -8.625  -29.992 1.00 9.37  ? 51   VAL A CA    1 
ATOM   379   C C     . VAL A  1  51  ? 92.016  -7.356  -30.802 1.00 9.79  ? 51   VAL A C     1 
ATOM   380   O O     . VAL A  1  51  ? 92.405  -6.267  -30.381 1.00 9.56  ? 51   VAL A O     1 
ATOM   381   C CB    . VAL A  1  51  ? 91.042  -8.740  -28.989 1.00 8.40  ? 51   VAL A CB    1 
ATOM   382   C CG1   . VAL A  1  51  ? 89.712  -8.734  -29.727 1.00 8.75  ? 51   VAL A CG1   1 
ATOM   383   C CG2   . VAL A  1  51  ? 91.194  -10.001 -28.151 1.00 8.74  ? 51   VAL A CG2   1 
ATOM   384   N N     . LEU A  1  52  ? 91.404  -7.514  -31.972 1.00 8.70  ? 52   LEU A N     1 
ATOM   385   C CA    . LEU A  1  52  ? 91.076  -6.389  -32.832 1.00 8.66  ? 52   LEU A CA    1 
ATOM   386   C C     . LEU A  1  52  ? 89.588  -6.489  -33.133 1.00 9.37  ? 52   LEU A C     1 
ATOM   387   O O     . LEU A  1  52  ? 89.109  -7.533  -33.574 1.00 8.29  ? 52   LEU A O     1 
ATOM   388   C CB    . LEU A  1  52  ? 91.851  -6.438  -34.153 1.00 8.27  ? 52   LEU A CB    1 
ATOM   389   C CG    . LEU A  1  52  ? 91.430  -5.343  -35.144 1.00 8.88  ? 52   LEU A CG    1 
ATOM   390   C CD1   . LEU A  1  52  ? 91.803  -3.978  -34.577 1.00 10.03 ? 52   LEU A CD1   1 
ATOM   391   C CD2   . LEU A  1  52  ? 92.094  -5.561  -36.499 1.00 10.44 ? 52   LEU A CD2   1 
ATOM   392   N N     . VAL A  1  53  ? 88.859  -5.413  -32.862 1.00 9.85  ? 53   VAL A N     1 
ATOM   393   C CA    . VAL A  1  53  ? 87.430  -5.358  -33.145 1.00 10.54 ? 53   VAL A CA    1 
ATOM   394   C C     . VAL A  1  53  ? 87.284  -4.408  -34.323 1.00 10.59 ? 53   VAL A C     1 
ATOM   395   O O     . VAL A  1  53  ? 87.887  -3.331  -34.333 1.00 12.77 ? 53   VAL A O     1 
ATOM   396   C CB    . VAL A  1  53  ? 86.624  -4.776  -31.970 1.00 13.55 ? 53   VAL A CB    1 
ATOM   397   C CG1   . VAL A  1  53  ? 85.142  -4.737  -32.327 1.00 14.64 ? 53   VAL A CG1   1 
ATOM   398   C CG2   . VAL A  1  53  ? 86.852  -5.595  -30.725 1.00 15.42 ? 53   VAL A CG2   1 
ATOM   399   N N     . LEU A  1  54  ? 86.489  -4.805  -35.310 1.00 8.07  ? 54   LEU A N     1 
ATOM   400   C CA    . LEU A  1  54  ? 86.266  -3.981  -36.494 1.00 8.36  ? 54   LEU A CA    1 
ATOM   401   C C     . LEU A  1  54  ? 84.784  -3.641  -36.613 1.00 8.89  ? 54   LEU A C     1 
ATOM   402   O O     . LEU A  1  54  ? 83.949  -4.523  -36.817 1.00 8.61  ? 54   LEU A O     1 
ATOM   403   C CB    . LEU A  1  54  ? 86.746  -4.721  -37.745 1.00 9.00  ? 54   LEU A CB    1 
ATOM   404   C CG    . LEU A  1  54  ? 88.251  -5.009  -37.792 1.00 9.99  ? 54   LEU A CG    1 
ATOM   405   C CD1   . LEU A  1  54  ? 88.549  -6.019  -38.889 1.00 11.71 ? 54   LEU A CD1   1 
ATOM   406   C CD2   . LEU A  1  54  ? 89.012  -3.710  -38.029 1.00 10.96 ? 54   LEU A CD2   1 
ATOM   407   N N     . GLU A  1  55  ? 84.470  -2.354  -36.493 1.00 7.11  ? 55   GLU A N     1 
ATOM   408   C CA    . GLU A  1  55  ? 83.093  -1.867  -36.556 1.00 9.34  ? 55   GLU A CA    1 
ATOM   409   C C     . GLU A  1  55  ? 82.908  -0.900  -37.718 1.00 8.68  ? 55   GLU A C     1 
ATOM   410   O O     . GLU A  1  55  ? 83.670  0.050   -37.862 1.00 8.82  ? 55   GLU A O     1 
ATOM   411   C CB    . GLU A  1  55  ? 82.750  -1.166  -35.237 1.00 9.46  ? 55   GLU A CB    1 
ATOM   412   C CG    . GLU A  1  55  ? 81.465  -0.349  -35.251 1.00 8.82  ? 55   GLU A CG    1 
ATOM   413   C CD    . GLU A  1  55  ? 80.256  -1.170  -35.633 1.00 9.34  ? 55   GLU A CD    1 
ATOM   414   O OE1   . GLU A  1  55  ? 80.139  -2.306  -35.131 1.00 8.69  ? 55   GLU A OE1   1 
ATOM   415   O OE2   . GLU A  1  55  ? 79.422  -0.677  -36.424 1.00 8.38  ? 55   GLU A OE2   1 
ATOM   416   N N     . ARG A  1  56  ? 81.885  -1.136  -38.534 1.00 8.09  ? 56   ARG A N     1 
ATOM   417   C CA    . ARG A  1  56  ? 81.619  -0.286  -39.691 1.00 8.51  ? 56   ARG A CA    1 
ATOM   418   C C     . ARG A  1  56  ? 81.146  1.121   -39.326 1.00 8.35  ? 56   ARG A C     1 
ATOM   419   O O     . ARG A  1  56  ? 81.403  2.072   -40.066 1.00 9.00  ? 56   ARG A O     1 
ATOM   420   C CB    . ARG A  1  56  ? 80.574  -0.948  -40.595 1.00 7.83  ? 56   ARG A CB    1 
ATOM   421   C CG    . ARG A  1  56  ? 79.240  -1.157  -39.907 1.00 7.40  ? 56   ARG A CG    1 
ATOM   422   C CD    . ARG A  1  56  ? 78.177  -1.721  -40.834 1.00 7.21  ? 56   ARG A CD    1 
ATOM   423   N NE    . ARG A  1  56  ? 76.896  -1.754  -40.135 1.00 6.96  ? 56   ARG A NE    1 
ATOM   424   C CZ    . ARG A  1  56  ? 75.706  -1.817  -40.723 1.00 4.71  ? 56   ARG A CZ    1 
ATOM   425   N NH1   . ARG A  1  56  ? 75.605  -1.866  -42.047 1.00 6.11  ? 56   ARG A NH1   1 
ATOM   426   N NH2   . ARG A  1  56  ? 74.612  -1.790  -39.976 1.00 6.16  ? 56   ARG A NH2   1 
ATOM   427   N N     . GLY A  1  57  ? 80.457  1.252   -38.194 1.00 8.66  ? 57   GLY A N     1 
ATOM   428   C CA    . GLY A  1  57  ? 79.951  2.552   -37.776 1.00 9.47  ? 57   GLY A CA    1 
ATOM   429   C C     . GLY A  1  57  ? 80.928  3.460   -37.045 1.00 9.50  ? 57   GLY A C     1 
ATOM   430   O O     . GLY A  1  57  ? 82.099  3.124   -36.866 1.00 10.51 ? 57   GLY A O     1 
ATOM   431   N N     . SER A  1  58  ? 80.432  4.620   -36.617 1.00 9.09  ? 58   SER A N     1 
ATOM   432   C CA    . SER A  1  58  ? 81.244  5.605   -35.899 1.00 10.07 ? 58   SER A CA    1 
ATOM   433   C C     . SER A  1  58  ? 81.254  5.372   -34.391 1.00 9.64  ? 58   SER A C     1 
ATOM   434   O O     . SER A  1  58  ? 80.618  4.451   -33.881 1.00 9.61  ? 58   SER A O     1 
ATOM   435   C CB    . SER A  1  58  ? 80.701  7.020   -36.147 1.00 10.03 ? 58   SER A CB    1 
ATOM   436   O OG    . SER A  1  58  ? 80.596  7.321   -37.525 1.00 12.04 ? 58   SER A OG    1 
ATOM   437   N N     . LEU A  1  59  ? 81.996  6.215   -33.680 1.00 11.03 ? 59   LEU A N     1 
ATOM   438   C CA    . LEU A  1  59  ? 82.042  6.154   -32.225 1.00 10.96 ? 59   LEU A CA    1 
ATOM   439   C C     . LEU A  1  59  ? 80.728  6.800   -31.786 1.00 11.18 ? 59   LEU A C     1 
ATOM   440   O O     . LEU A  1  59  ? 80.166  7.623   -32.515 1.00 11.65 ? 59   LEU A O     1 
ATOM   441   C CB    . LEU A  1  59  ? 83.219  6.977   -31.689 1.00 12.53 ? 59   LEU A CB    1 
ATOM   442   C CG    . LEU A  1  59  ? 84.634  6.497   -32.021 1.00 14.37 ? 59   LEU A CG    1 
ATOM   443   C CD1   . LEU A  1  59  ? 85.641  7.584   -31.670 1.00 16.16 ? 59   LEU A CD1   1 
ATOM   444   C CD2   . LEU A  1  59  ? 84.935  5.222   -31.253 1.00 15.08 ? 59   LEU A CD2   1 
ATOM   445   N N     . PRO A  1  60  ? 80.212  6.433   -30.603 1.00 11.00 ? 60   PRO A N     1 
ATOM   446   C CA    . PRO A  1  60  ? 78.953  7.028   -30.142 1.00 11.15 ? 60   PRO A CA    1 
ATOM   447   C C     . PRO A  1  60  ? 79.056  8.549   -30.008 1.00 11.14 ? 60   PRO A C     1 
ATOM   448   O O     . PRO A  1  60  ? 78.060  9.262   -30.119 1.00 11.04 ? 60   PRO A O     1 
ATOM   449   C CB    . PRO A  1  60  ? 78.722  6.348   -28.794 1.00 10.83 ? 60   PRO A CB    1 
ATOM   450   C CG    . PRO A  1  60  ? 79.366  5.004   -28.978 1.00 11.26 ? 60   PRO A CG    1 
ATOM   451   C CD    . PRO A  1  60  ? 80.652  5.364   -29.690 1.00 11.75 ? 60   PRO A CD    1 
ATOM   452   N N     . THR A  1  61  ? 80.268  9.037   -29.771 1.00 10.55 ? 61   THR A N     1 
ATOM   453   C CA    . THR A  1  61  ? 80.488  10.471  -29.614 1.00 12.36 ? 61   THR A CA    1 
ATOM   454   C C     . THR A  1  61  ? 80.175  11.275  -30.878 1.00 12.94 ? 61   THR A C     1 
ATOM   455   O O     . THR A  1  61  ? 79.944  12.485  -30.807 1.00 13.83 ? 61   THR A O     1 
ATOM   456   C CB    . THR A  1  61  ? 81.939  10.761  -29.182 1.00 12.35 ? 61   THR A CB    1 
ATOM   457   O OG1   . THR A  1  61  ? 82.846  10.126  -30.090 1.00 13.87 ? 61   THR A OG1   1 
ATOM   458   C CG2   . THR A  1  61  ? 82.190  10.237  -27.773 1.00 14.57 ? 61   THR A CG2   1 
ATOM   459   N N     . ALA A  1  62  ? 80.166  10.608  -32.030 1.00 12.61 ? 62   ALA A N     1 
ATOM   460   C CA    . ALA A  1  62  ? 79.874  11.276  -33.296 1.00 12.29 ? 62   ALA A CA    1 
ATOM   461   C C     . ALA A  1  62  ? 78.392  11.622  -33.419 1.00 12.55 ? 62   ALA A C     1 
ATOM   462   O O     . ALA A  1  62  ? 78.006  12.459  -34.239 1.00 12.77 ? 62   ALA A O     1 
ATOM   463   C CB    . ALA A  1  62  ? 80.296  10.397  -34.460 1.00 13.53 ? 62   ALA A CB    1 
ATOM   464   N N     . TYR A  1  63  ? 77.566  10.969  -32.606 1.00 12.03 ? 63   TYR A N     1 
ATOM   465   C CA    . TYR A  1  63  ? 76.126  11.209  -32.619 1.00 12.88 ? 63   TYR A CA    1 
ATOM   466   C C     . TYR A  1  63  ? 75.620  11.288  -31.182 1.00 13.75 ? 63   TYR A C     1 
ATOM   467   O O     . TYR A  1  63  ? 75.035  10.342  -30.658 1.00 12.21 ? 63   TYR A O     1 
ATOM   468   C CB    . TYR A  1  63  ? 75.411  10.090  -33.384 1.00 11.85 ? 63   TYR A CB    1 
ATOM   469   C CG    . TYR A  1  63  ? 75.826  10.010  -34.833 1.00 10.60 ? 63   TYR A CG    1 
ATOM   470   C CD1   . TYR A  1  63  ? 76.916  9.236   -35.227 1.00 9.84  ? 63   TYR A CD1   1 
ATOM   471   C CD2   . TYR A  1  63  ? 75.159  10.753  -35.806 1.00 11.74 ? 63   TYR A CD2   1 
ATOM   472   C CE1   . TYR A  1  63  ? 77.336  9.205   -36.557 1.00 9.23  ? 63   TYR A CE1   1 
ATOM   473   C CE2   . TYR A  1  63  ? 75.570  10.732  -37.136 1.00 10.15 ? 63   TYR A CE2   1 
ATOM   474   C CZ    . TYR A  1  63  ? 76.660  9.958   -37.505 1.00 9.91  ? 63   TYR A CZ    1 
ATOM   475   O OH    . TYR A  1  63  ? 77.075  9.954   -38.818 1.00 11.81 ? 63   TYR A OH    1 
ATOM   476   N N     . PRO A  1  64  ? 75.831  12.442  -30.533 1.00 13.73 ? 64   PRO A N     1 
ATOM   477   C CA    . PRO A  1  64  ? 75.444  12.738  -29.151 1.00 14.14 ? 64   PRO A CA    1 
ATOM   478   C C     . PRO A  1  64  ? 74.072  12.262  -28.681 1.00 13.43 ? 64   PRO A C     1 
ATOM   479   O O     . PRO A  1  64  ? 73.919  11.865  -27.528 1.00 14.48 ? 64   PRO A O     1 
ATOM   480   C CB    . PRO A  1  64  ? 75.575  14.256  -29.080 1.00 15.71 ? 64   PRO A CB    1 
ATOM   481   C CG    . PRO A  1  64  ? 76.715  14.523  -29.997 1.00 15.94 ? 64   PRO A CG    1 
ATOM   482   C CD    . PRO A  1  64  ? 76.391  13.644  -31.180 1.00 15.53 ? 64   PRO A CD    1 
ATOM   483   N N     . ASN A  1  65  ? 73.077  12.298  -29.560 1.00 13.21 ? 65   ASN A N     1 
ATOM   484   C CA    . ASN A  1  65  ? 71.739  11.887  -29.161 1.00 12.85 ? 65   ASN A CA    1 
ATOM   485   C C     . ASN A  1  65  ? 71.528  10.397  -28.906 1.00 12.97 ? 65   ASN A C     1 
ATOM   486   O O     . ASN A  1  65  ? 70.438  9.984   -28.513 1.00 11.07 ? 65   ASN A O     1 
ATOM   487   C CB    . ASN A  1  65  ? 70.709  12.420  -30.158 1.00 15.23 ? 65   ASN A CB    1 
ATOM   488   C CG    . ASN A  1  65  ? 70.569  13.929  -30.079 1.00 16.68 ? 65   ASN A CG    1 
ATOM   489   O OD1   . ASN A  1  65  ? 70.424  14.487  -28.992 1.00 17.89 ? 65   ASN A OD1   1 
ATOM   490   N ND2   . ASN A  1  65  ? 70.614  14.595  -31.225 1.00 17.13 ? 65   ASN A ND2   1 
ATOM   491   N N     . VAL A  1  66  ? 72.557  9.584   -29.120 1.00 12.03 ? 66   VAL A N     1 
ATOM   492   C CA    . VAL A  1  66  ? 72.416  8.159   -28.830 1.00 11.21 ? 66   VAL A CA    1 
ATOM   493   C C     . VAL A  1  66  ? 72.814  7.958   -27.370 1.00 11.16 ? 66   VAL A C     1 
ATOM   494   O O     . VAL A  1  66  ? 72.766  6.845   -26.849 1.00 12.58 ? 66   VAL A O     1 
ATOM   495   C CB    . VAL A  1  66  ? 73.340  7.271   -29.712 1.00 10.65 ? 66   VAL A CB    1 
ATOM   496   C CG1   . VAL A  1  66  ? 73.030  7.482   -31.184 1.00 9.49  ? 66   VAL A CG1   1 
ATOM   497   C CG2   . VAL A  1  66  ? 74.810  7.576   -29.417 1.00 12.92 ? 66   VAL A CG2   1 
ATOM   498   N N     . LEU A  1  67  ? 73.192  9.047   -26.706 1.00 10.75 ? 67   LEU A N     1 
ATOM   499   C CA    . LEU A  1  67  ? 73.641  8.972   -25.319 1.00 10.99 ? 67   LEU A CA    1 
ATOM   500   C C     . LEU A  1  67  ? 72.636  9.376   -24.242 1.00 10.32 ? 67   LEU A C     1 
ATOM   501   O O     . LEU A  1  67  ? 72.983  9.430   -23.063 1.00 12.10 ? 67   LEU A O     1 
ATOM   502   C CB    . LEU A  1  67  ? 74.923  9.794   -25.162 1.00 11.26 ? 67   LEU A CB    1 
ATOM   503   C CG    . LEU A  1  67  ? 76.078  9.375   -26.080 1.00 12.94 ? 67   LEU A CG    1 
ATOM   504   C CD1   . LEU A  1  67  ? 77.254  10.330  -25.917 1.00 13.94 ? 67   LEU A CD1   1 
ATOM   505   C CD2   . LEU A  1  67  ? 76.493  7.949   -25.746 1.00 12.86 ? 67   LEU A CD2   1 
ATOM   506   N N     . THR A  1  68  ? 71.395  9.649   -24.632 1.00 11.34 ? 68   THR A N     1 
ATOM   507   C CA    . THR A  1  68  ? 70.369  10.030  -23.662 1.00 11.23 ? 68   THR A CA    1 
ATOM   508   C C     . THR A  1  68  ? 69.035  9.388   -24.011 1.00 11.20 ? 68   THR A C     1 
ATOM   509   O O     . THR A  1  68  ? 68.771  9.083   -25.179 1.00 11.59 ? 68   THR A O     1 
ATOM   510   C CB    . THR A  1  68  ? 70.158  11.554  -23.634 1.00 13.08 ? 68   THR A CB    1 
ATOM   511   O OG1   . THR A  1  68  ? 69.645  11.982  -24.901 1.00 14.21 ? 68   THR A OG1   1 
ATOM   512   C CG2   . THR A  1  68  ? 71.470  12.276  -23.349 1.00 13.55 ? 68   THR A CG2   1 
ATOM   513   N N     . ALA A  1  69  ? 68.195  9.191   -23.000 1.00 10.29 ? 69   ALA A N     1 
ATOM   514   C CA    . ALA A  1  69  ? 66.887  8.605   -23.227 1.00 12.21 ? 69   ALA A CA    1 
ATOM   515   C C     . ALA A  1  69  ? 66.030  9.510   -24.101 1.00 12.53 ? 69   ALA A C     1 
ATOM   516   O O     . ALA A  1  69  ? 65.273  9.029   -24.936 1.00 13.00 ? 69   ALA A O     1 
ATOM   517   C CB    . ALA A  1  69  ? 66.184  8.339   -21.894 1.00 11.75 ? 69   ALA A CB    1 
ATOM   518   N N     . ASP A  1  70  ? 66.136  10.823  -23.930 1.00 14.74 ? 70   ASP A N     1 
ATOM   519   C CA    . ASP A  1  70  ? 65.312  11.700  -24.753 1.00 15.25 ? 70   ASP A CA    1 
ATOM   520   C C     . ASP A  1  70  ? 65.796  11.795  -26.193 1.00 15.37 ? 70   ASP A C     1 
ATOM   521   O O     . ASP A  1  70  ? 65.236  12.540  -26.996 1.00 16.53 ? 70   ASP A O     1 
ATOM   522   C CB    . ASP A  1  70  ? 65.201  13.103  -24.155 1.00 18.50 ? 70   ASP A CB    1 
ATOM   523   C CG    . ASP A  1  70  ? 66.539  13.701  -23.790 0.50 17.40 ? 70   ASP A CG    1 
ATOM   524   O OD1   . ASP A  1  70  ? 67.504  13.552  -24.565 0.50 19.65 ? 70   ASP A OD1   1 
ATOM   525   O OD2   . ASP A  1  70  ? 66.618  14.352  -22.727 0.50 20.10 ? 70   ASP A OD2   1 
ATOM   526   N N     . GLY A  1  71  ? 66.826  11.022  -26.523 1.00 13.84 ? 71   GLY A N     1 
ATOM   527   C CA    . GLY A  1  71  ? 67.340  11.007  -27.880 1.00 12.80 ? 71   GLY A CA    1 
ATOM   528   C C     . GLY A  1  71  ? 66.863  9.784   -28.648 1.00 11.03 ? 71   GLY A C     1 
ATOM   529   O O     . GLY A  1  71  ? 67.086  9.679   -29.849 1.00 11.04 ? 71   GLY A O     1 
ATOM   530   N N     . PHE A  1  72  ? 66.206  8.856   -27.956 1.00 12.14 ? 72   PHE A N     1 
ATOM   531   C CA    . PHE A  1  72  ? 65.714  7.621   -28.574 1.00 10.10 ? 72   PHE A CA    1 
ATOM   532   C C     . PHE A  1  72  ? 64.932  7.841   -29.872 1.00 10.30 ? 72   PHE A C     1 
ATOM   533   O O     . PHE A  1  72  ? 65.301  7.331   -30.934 1.00 10.52 ? 72   PHE A O     1 
ATOM   534   C CB    . PHE A  1  72  ? 64.841  6.841   -27.578 1.00 10.92 ? 72   PHE A CB    1 
ATOM   535   C CG    . PHE A  1  72  ? 64.201  5.620   -28.165 1.00 10.57 ? 72   PHE A CG    1 
ATOM   536   C CD1   . PHE A  1  72  ? 64.983  4.581   -28.659 1.00 9.31  ? 72   PHE A CD1   1 
ATOM   537   C CD2   . PHE A  1  72  ? 62.816  5.513   -28.239 1.00 9.71  ? 72   PHE A CD2   1 
ATOM   538   C CE1   . PHE A  1  72  ? 64.397  3.458   -29.215 1.00 9.41  ? 72   PHE A CE1   1 
ATOM   539   C CE2   . PHE A  1  72  ? 62.216  4.390   -28.794 1.00 10.64 ? 72   PHE A CE2   1 
ATOM   540   C CZ    . PHE A  1  72  ? 63.009  3.360   -29.284 1.00 10.34 ? 72   PHE A CZ    1 
ATOM   541   N N     . VAL A  1  73  ? 63.839  8.589   -29.786 1.00 10.25 ? 73   VAL A N     1 
ATOM   542   C CA    . VAL A  1  73  ? 63.024  8.866   -30.960 1.00 10.06 ? 73   VAL A CA    1 
ATOM   543   C C     . VAL A  1  73  ? 63.833  9.635   -32.002 1.00 10.55 ? 73   VAL A C     1 
ATOM   544   O O     . VAL A  1  73  ? 63.737  9.362   -33.196 1.00 10.24 ? 73   VAL A O     1 
ATOM   545   C CB    . VAL A  1  73  ? 61.762  9.674   -30.573 1.00 10.42 ? 73   VAL A CB    1 
ATOM   546   C CG1   . VAL A  1  73  ? 61.036  10.151  -31.819 1.00 11.69 ? 73   VAL A CG1   1 
ATOM   547   C CG2   . VAL A  1  73  ? 60.838  8.801   -29.734 1.00 12.94 ? 73   VAL A CG2   1 
ATOM   548   N N     . TYR A  1  74  ? 64.641  10.586  -31.543 1.00 10.80 ? 74   TYR A N     1 
ATOM   549   C CA    . TYR A  1  74  ? 65.464  11.389  -32.438 1.00 12.17 ? 74   TYR A CA    1 
ATOM   550   C C     . TYR A  1  74  ? 66.280  10.549  -33.420 1.00 11.06 ? 74   TYR A C     1 
ATOM   551   O O     . TYR A  1  74  ? 66.262  10.801  -34.622 1.00 11.19 ? 74   TYR A O     1 
ATOM   552   C CB    . TYR A  1  74  ? 66.422  12.268  -31.627 1.00 15.65 ? 74   TYR A CB    1 
ATOM   553   C CG    . TYR A  1  74  ? 67.315  13.148  -32.477 1.00 17.22 ? 74   TYR A CG    1 
ATOM   554   C CD1   . TYR A  1  74  ? 66.908  14.426  -32.863 1.00 20.74 ? 74   TYR A CD1   1 
ATOM   555   C CD2   . TYR A  1  74  ? 68.557  12.693  -32.919 1.00 19.79 ? 74   TYR A CD2   1 
ATOM   556   C CE1   . TYR A  1  74  ? 67.717  15.229  -33.668 1.00 21.81 ? 74   TYR A CE1   1 
ATOM   557   C CE2   . TYR A  1  74  ? 69.373  13.485  -33.726 1.00 21.98 ? 74   TYR A CE2   1 
ATOM   558   C CZ    . TYR A  1  74  ? 68.946  14.751  -34.095 1.00 23.01 ? 74   TYR A CZ    1 
ATOM   559   O OH    . TYR A  1  74  ? 69.751  15.533  -34.895 1.00 24.86 ? 74   TYR A OH    1 
ATOM   560   N N     . ASN A  1  75  ? 67.002  9.555   -32.910 1.00 10.28 ? 75   ASN A N     1 
ATOM   561   C CA    . ASN A  1  75  ? 67.834  8.721   -33.770 1.00 9.47  ? 75   ASN A CA    1 
ATOM   562   C C     . ASN A  1  75  ? 67.020  8.038   -34.865 1.00 9.88  ? 75   ASN A C     1 
ATOM   563   O O     . ASN A  1  75  ? 67.474  7.924   -36.005 1.00 10.63 ? 75   ASN A O     1 
ATOM   564   C CB    . ASN A  1  75  ? 68.569  7.676   -32.927 1.00 11.02 ? 75   ASN A CB    1 
ATOM   565   C CG    . ASN A  1  75  ? 69.364  8.299   -31.796 1.00 11.74 ? 75   ASN A CG    1 
ATOM   566   O OD1   . ASN A  1  75  ? 69.385  7.781   -30.679 1.00 12.97 ? 75   ASN A OD1   1 
ATOM   567   N ND2   . ASN A  1  75  ? 70.025  9.417   -32.081 1.00 9.56  ? 75   ASN A ND2   1 
ATOM   568   N N     . LEU A  1  76  ? 65.814  7.593   -34.520 1.00 9.45  ? 76   LEU A N     1 
ATOM   569   C CA    . LEU A  1  76  ? 64.944  6.922   -35.482 1.00 9.67  ? 76   LEU A CA    1 
ATOM   570   C C     . LEU A  1  76  ? 64.406  7.898   -36.531 1.00 10.12 ? 76   LEU A C     1 
ATOM   571   O O     . LEU A  1  76  ? 64.128  7.512   -37.665 1.00 9.49  ? 76   LEU A O     1 
ATOM   572   C CB    . LEU A  1  76  ? 63.770  6.250   -34.758 1.00 9.52  ? 76   LEU A CB    1 
ATOM   573   C CG    . LEU A  1  76  ? 64.112  5.188   -33.709 1.00 10.10 ? 76   LEU A CG    1 
ATOM   574   C CD1   . LEU A  1  76  ? 62.831  4.667   -33.069 1.00 11.09 ? 76   LEU A CD1   1 
ATOM   575   C CD2   . LEU A  1  76  ? 64.878  4.049   -34.364 1.00 12.13 ? 76   LEU A CD2   1 
ATOM   576   N N     . GLN A  1  77  ? 64.272  9.165   -36.149 1.00 10.41 ? 77   GLN A N     1 
ATOM   577   C CA    . GLN A  1  77  ? 63.760  10.190  -37.055 1.00 11.49 ? 77   GLN A CA    1 
ATOM   578   C C     . GLN A  1  77  ? 64.794  10.702  -38.048 1.00 12.40 ? 77   GLN A C     1 
ATOM   579   O O     . GLN A  1  77  ? 64.438  11.206  -39.111 1.00 13.06 ? 77   GLN A O     1 
ATOM   580   C CB    . GLN A  1  77  ? 63.244  11.393  -36.265 1.00 11.00 ? 77   GLN A CB    1 
ATOM   581   C CG    . GLN A  1  77  ? 62.056  11.132  -35.366 1.00 12.92 ? 77   GLN A CG    1 
ATOM   582   C CD    . GLN A  1  77  ? 61.760  12.329  -34.491 1.00 12.44 ? 77   GLN A CD    1 
ATOM   583   O OE1   . GLN A  1  77  ? 62.644  12.827  -33.797 1.00 12.08 ? 77   GLN A OE1   1 
ATOM   584   N NE2   . GLN A  1  77  ? 60.519  12.801  -34.518 1.00 13.26 ? 77   GLN A NE2   1 
ATOM   585   N N     . GLN A  1  78  ? 66.072  10.580  -37.703 1.00 12.89 ? 78   GLN A N     1 
ATOM   586   C CA    . GLN A  1  78  ? 67.130  11.081  -38.567 1.00 12.90 ? 78   GLN A CA    1 
ATOM   587   C C     . GLN A  1  78  ? 67.262  10.379  -39.908 1.00 13.11 ? 78   GLN A C     1 
ATOM   588   O O     . GLN A  1  78  ? 67.185  9.155   -40.006 1.00 12.54 ? 78   GLN A O     1 
ATOM   589   C CB    . GLN A  1  78  ? 68.466  11.065  -37.821 1.00 13.44 ? 78   GLN A CB    1 
ATOM   590   C CG    A GLN A  1  78  ? 68.431  11.913  -36.559 0.50 12.67 ? 78   GLN A CG    1 
ATOM   591   C CG    B GLN A  1  78  ? 69.701  11.154  -38.723 0.50 12.69 ? 78   GLN A CG    1 
ATOM   592   C CD    A GLN A  1  78  ? 67.704  13.237  -36.767 0.50 13.31 ? 78   GLN A CD    1 
ATOM   593   C CD    B GLN A  1  78  ? 70.980  11.408  -37.951 0.50 13.33 ? 78   GLN A CD    1 
ATOM   594   O OE1   A GLN A  1  78  ? 68.186  14.124  -37.476 0.50 13.46 ? 78   GLN A OE1   1 
ATOM   595   O OE1   B GLN A  1  78  ? 71.332  10.648  -37.048 0.50 13.50 ? 78   GLN A OE1   1 
ATOM   596   N NE2   A GLN A  1  78  ? 66.531  13.368  -36.156 0.50 8.69  ? 78   GLN A NE2   1 
ATOM   597   N NE2   B GLN A  1  78  ? 71.827  12.414  -38.137 0.50 8.86  ? 78   GLN A NE2   1 
ATOM   598   N N     . GLU A  1  79  ? 67.455  11.176  -40.951 1.00 14.15 ? 79   GLU A N     1 
ATOM   599   C CA    . GLU A  1  79  ? 67.593  10.645  -42.294 1.00 15.73 ? 79   GLU A CA    1 
ATOM   600   C C     . GLU A  1  79  ? 68.831  9.757   -42.379 1.00 14.31 ? 79   GLU A C     1 
ATOM   601   O O     . GLU A  1  79  ? 69.881  10.066  -41.812 1.00 13.61 ? 79   GLU A O     1 
ATOM   602   C CB    . GLU A  1  79  ? 67.677  11.799  -43.295 1.00 20.40 ? 79   GLU A CB    1 
ATOM   603   C CG    . GLU A  1  79  ? 66.586  12.841  -43.074 1.00 28.00 ? 79   GLU A CG    1 
ATOM   604   C CD    . GLU A  1  79  ? 66.653  13.999  -44.053 1.00 32.01 ? 79   GLU A CD    1 
ATOM   605   O OE1   . GLU A  1  79  ? 67.774  14.468  -44.347 1.00 34.58 ? 79   GLU A OE1   1 
ATOM   606   O OE2   . GLU A  1  79  ? 65.581  14.449  -44.514 1.00 35.34 ? 79   GLU A OE2   1 
ATOM   607   N N     . ASP A  1  80  ? 68.686  8.643   -43.084 1.00 13.89 ? 80   ASP A N     1 
ATOM   608   C CA    . ASP A  1  80  ? 69.762  7.676   -43.253 1.00 12.60 ? 80   ASP A CA    1 
ATOM   609   C C     . ASP A  1  80  ? 70.694  8.120   -44.375 1.00 13.19 ? 80   ASP A C     1 
ATOM   610   O O     . ASP A  1  80  ? 70.355  7.991   -45.552 1.00 13.90 ? 80   ASP A O     1 
ATOM   611   C CB    . ASP A  1  80  ? 69.160  6.309   -43.591 1.00 12.37 ? 80   ASP A CB    1 
ATOM   612   C CG    . ASP A  1  80  ? 70.191  5.203   -43.626 1.00 12.24 ? 80   ASP A CG    1 
ATOM   613   O OD1   . ASP A  1  80  ? 71.401  5.503   -43.715 1.00 13.34 ? 80   ASP A OD1   1 
ATOM   614   O OD2   . ASP A  1  80  ? 69.783  4.022   -43.577 1.00 13.33 ? 80   ASP A OD2   1 
ATOM   615   N N     . ASP A  1  81  ? 71.862  8.646   -44.013 1.00 12.05 ? 81   ASP A N     1 
ATOM   616   C CA    . ASP A  1  81  ? 72.823  9.096   -45.015 1.00 12.84 ? 81   ASP A CA    1 
ATOM   617   C C     . ASP A  1  81  ? 73.916  8.059   -45.246 1.00 12.10 ? 81   ASP A C     1 
ATOM   618   O O     . ASP A  1  81  ? 74.925  8.340   -45.894 1.00 12.59 ? 81   ASP A O     1 
ATOM   619   C CB    . ASP A  1  81  ? 73.454  10.433  -44.602 1.00 12.68 ? 81   ASP A CB    1 
ATOM   620   C CG    . ASP A  1  81  ? 74.279  10.333  -43.331 1.00 15.31 ? 81   ASP A CG    1 
ATOM   621   O OD1   . ASP A  1  81  ? 74.469  9.212   -42.817 1.00 14.18 ? 81   ASP A OD1   1 
ATOM   622   O OD2   . ASP A  1  81  ? 74.745  11.386  -42.844 1.00 16.24 ? 81   ASP A OD2   1 
ATOM   623   N N     . GLY A  1  82  ? 73.705  6.858   -44.715 1.00 12.34 ? 82   GLY A N     1 
ATOM   624   C CA    . GLY A  1  82  ? 74.682  5.797   -44.875 1.00 11.23 ? 82   GLY A CA    1 
ATOM   625   C C     . GLY A  1  82  ? 75.744  5.771   -43.791 1.00 11.38 ? 82   GLY A C     1 
ATOM   626   O O     . GLY A  1  82  ? 76.539  4.832   -43.721 1.00 11.62 ? 82   GLY A O     1 
ATOM   627   N N     . LYS A  1  83  ? 75.761  6.793   -42.941 1.00 12.01 ? 83   LYS A N     1 
ATOM   628   C CA    . LYS A  1  83  ? 76.750  6.872   -41.871 1.00 12.69 ? 83   LYS A CA    1 
ATOM   629   C C     . LYS A  1  83  ? 76.107  6.969   -40.495 1.00 10.70 ? 83   LYS A C     1 
ATOM   630   O O     . LYS A  1  83  ? 76.743  6.676   -39.482 1.00 11.10 ? 83   LYS A O     1 
ATOM   631   C CB    . LYS A  1  83  ? 77.662  8.082   -42.094 1.00 15.44 ? 83   LYS A CB    1 
ATOM   632   C CG    . LYS A  1  83  ? 78.273  8.139   -43.487 1.00 22.22 ? 83   LYS A CG    1 
ATOM   633   C CD    . LYS A  1  83  ? 79.159  9.363   -43.667 1.00 26.26 ? 83   LYS A CD    1 
ATOM   634   C CE    . LYS A  1  83  ? 79.705  9.439   -45.088 1.00 30.19 ? 83   LYS A CE    1 
ATOM   635   N NZ    . LYS A  1  83  ? 80.562  10.639  -45.304 1.00 32.70 ? 83   LYS A NZ    1 
ATOM   636   N N     . THR A  1  84  ? 74.846  7.386   -40.463 1.00 10.19 ? 84   THR A N     1 
ATOM   637   C CA    . THR A  1  84  ? 74.114  7.536   -39.210 1.00 9.55  ? 84   THR A CA    1 
ATOM   638   C C     . THR A  1  84  ? 74.007  6.220   -38.435 1.00 9.32  ? 84   THR A C     1 
ATOM   639   O O     . THR A  1  84  ? 74.063  5.136   -39.018 1.00 9.56  ? 84   THR A O     1 
ATOM   640   C CB    . THR A  1  84  ? 72.711  8.106   -39.476 1.00 10.74 ? 84   THR A CB    1 
ATOM   641   O OG1   . THR A  1  84  ? 72.107  7.397   -40.562 1.00 10.17 ? 84   THR A OG1   1 
ATOM   642   C CG2   . THR A  1  84  ? 72.804  9.587   -39.834 1.00 11.55 ? 84   THR A CG2   1 
ATOM   643   N N     . PRO A  1  85  ? 73.847  6.301   -37.103 1.00 9.46  ? 85   PRO A N     1 
ATOM   644   C CA    . PRO A  1  85  ? 73.743  5.113   -36.247 1.00 8.69  ? 85   PRO A CA    1 
ATOM   645   C C     . PRO A  1  85  ? 72.520  4.227   -36.453 1.00 8.86  ? 85   PRO A C     1 
ATOM   646   O O     . PRO A  1  85  ? 72.508  3.069   -36.028 1.00 8.62  ? 85   PRO A O     1 
ATOM   647   C CB    . PRO A  1  85  ? 73.819  5.695   -34.836 1.00 8.26  ? 85   PRO A CB    1 
ATOM   648   C CG    . PRO A  1  85  ? 73.205  7.063   -34.999 1.00 8.62  ? 85   PRO A CG    1 
ATOM   649   C CD    . PRO A  1  85  ? 73.815  7.536   -36.294 1.00 8.20  ? 85   PRO A CD    1 
ATOM   650   N N     . VAL A  1  86  ? 71.492  4.772   -37.093 1.00 7.86  ? 86   VAL A N     1 
ATOM   651   C CA    . VAL A  1  86  ? 70.281  4.012   -37.364 1.00 8.14  ? 86   VAL A CA    1 
ATOM   652   C C     . VAL A  1  86  ? 70.178  3.726   -38.858 1.00 8.64  ? 86   VAL A C     1 
ATOM   653   O O     . VAL A  1  86  ? 69.962  4.641   -39.660 1.00 10.69 ? 86   VAL A O     1 
ATOM   654   C CB    . VAL A  1  86  ? 69.016  4.778   -36.914 1.00 8.79  ? 86   VAL A CB    1 
ATOM   655   C CG1   . VAL A  1  86  ? 67.768  3.981   -37.279 1.00 10.16 ? 86   VAL A CG1   1 
ATOM   656   C CG2   . VAL A  1  86  ? 69.064  5.023   -35.408 1.00 10.12 ? 86   VAL A CG2   1 
ATOM   657   N N     . GLU A  1  87  ? 70.354  2.460   -39.233 1.00 7.31  ? 87   GLU A N     1 
ATOM   658   C CA    . GLU A  1  87  ? 70.255  2.075   -40.634 1.00 6.80  ? 87   GLU A CA    1 
ATOM   659   C C     . GLU A  1  87  ? 68.842  1.589   -40.913 1.00 8.09  ? 87   GLU A C     1 
ATOM   660   O O     . GLU A  1  87  ? 68.335  0.686   -40.241 1.00 9.30  ? 87   GLU A O     1 
ATOM   661   C CB    . GLU A  1  87  ? 71.250  0.964   -40.993 1.00 8.85  ? 87   GLU A CB    1 
ATOM   662   C CG    . GLU A  1  87  ? 71.044  0.462   -42.423 1.00 8.78  ? 87   GLU A CG    1 
ATOM   663   C CD    . GLU A  1  87  ? 72.090  -0.535  -42.892 1.00 10.47 ? 87   GLU A CD    1 
ATOM   664   O OE1   . GLU A  1  87  ? 72.956  -0.937  -42.088 1.00 10.35 ? 87   GLU A OE1   1 
ATOM   665   O OE2   . GLU A  1  87  ? 72.042  -0.916  -44.082 1.00 13.21 ? 87   GLU A OE2   1 
ATOM   666   N N     . ARG A  1  88  ? 68.210  2.193   -41.910 1.00 6.92  ? 88   ARG A N     1 
ATOM   667   C CA    . ARG A  1  88  ? 66.849  1.835   -42.279 1.00 7.79  ? 88   ARG A CA    1 
ATOM   668   C C     . ARG A  1  88  ? 66.793  0.712   -43.301 1.00 7.94  ? 88   ARG A C     1 
ATOM   669   O O     . ARG A  1  88  ? 67.674  0.589   -44.151 1.00 10.20 ? 88   ARG A O     1 
ATOM   670   C CB    . ARG A  1  88  ? 66.131  3.049   -42.873 1.00 9.02  ? 88   ARG A CB    1 
ATOM   671   C CG    . ARG A  1  88  ? 66.061  4.256   -41.966 1.00 8.04  ? 88   ARG A CG    1 
ATOM   672   C CD    . ARG A  1  88  ? 65.304  5.395   -42.647 1.00 10.58 ? 88   ARG A CD    1 
ATOM   673   N NE    . ARG A  1  88  ? 65.137  6.542   -41.763 1.00 12.74 ? 88   ARG A NE    1 
ATOM   674   C CZ    . ARG A  1  88  ? 64.363  7.589   -42.036 1.00 13.24 ? 88   ARG A CZ    1 
ATOM   675   N NH1   . ARG A  1  88  ? 63.683  7.635   -43.174 1.00 13.16 ? 88   ARG A NH1   1 
ATOM   676   N NH2   . ARG A  1  88  ? 64.264  8.586   -41.167 1.00 14.55 ? 88   ARG A NH2   1 
ATOM   677   N N     . PHE A  1  89  ? 65.755  -0.112  -43.201 1.00 8.62  ? 89   PHE A N     1 
ATOM   678   C CA    . PHE A  1  89  ? 65.526  -1.174  -44.171 1.00 8.80  ? 89   PHE A CA    1 
ATOM   679   C C     . PHE A  1  89  ? 64.065  -1.582  -44.128 1.00 7.83  ? 89   PHE A C     1 
ATOM   680   O O     . PHE A  1  89  ? 63.349  -1.263  -43.179 1.00 8.30  ? 89   PHE A O     1 
ATOM   681   C CB    . PHE A  1  89  ? 66.482  -2.370  -43.961 1.00 9.63  ? 89   PHE A CB    1 
ATOM   682   C CG    . PHE A  1  89  ? 66.191  -3.227  -42.755 1.00 9.94  ? 89   PHE A CG    1 
ATOM   683   C CD1   . PHE A  1  89  ? 65.374  -4.351  -42.861 1.00 9.07  ? 89   PHE A CD1   1 
ATOM   684   C CD2   . PHE A  1  89  ? 66.807  -2.963  -41.536 1.00 9.90  ? 89   PHE A CD2   1 
ATOM   685   C CE1   . PHE A  1  89  ? 65.185  -5.202  -41.774 1.00 8.92  ? 89   PHE A CE1   1 
ATOM   686   C CE2   . PHE A  1  89  ? 66.622  -3.806  -40.444 1.00 9.65  ? 89   PHE A CE2   1 
ATOM   687   C CZ    . PHE A  1  89  ? 65.812  -4.928  -40.563 1.00 9.53  ? 89   PHE A CZ    1 
ATOM   688   N N     . VAL A  1  90  ? 63.605  -2.234  -45.186 1.00 7.53  ? 90   VAL A N     1 
ATOM   689   C CA    . VAL A  1  90  ? 62.218  -2.663  -45.258 1.00 7.65  ? 90   VAL A CA    1 
ATOM   690   C C     . VAL A  1  90  ? 62.227  -4.135  -45.624 1.00 8.58  ? 90   VAL A C     1 
ATOM   691   O O     . VAL A  1  90  ? 62.879  -4.523  -46.596 1.00 8.63  ? 90   VAL A O     1 
ATOM   692   C CB    . VAL A  1  90  ? 61.446  -1.889  -46.350 1.00 8.71  ? 90   VAL A CB    1 
ATOM   693   C CG1   . VAL A  1  90  ? 59.965  -2.223  -46.276 1.00 10.00 ? 90   VAL A CG1   1 
ATOM   694   C CG2   . VAL A  1  90  ? 61.660  -0.396  -46.185 1.00 10.00 ? 90   VAL A CG2   1 
ATOM   695   N N     . SER A  1  91  ? 61.519  -4.957  -44.853 1.00 6.89  ? 91   SER A N     1 
ATOM   696   C CA    . SER A  1  91  ? 61.484  -6.381  -45.160 1.00 7.65  ? 91   SER A CA    1 
ATOM   697   C C     . SER A  1  91  ? 60.667  -6.583  -46.433 1.00 7.57  ? 91   SER A C     1 
ATOM   698   O O     . SER A  1  91  ? 59.931  -5.687  -46.862 1.00 7.25  ? 91   SER A O     1 
ATOM   699   C CB    . SER A  1  91  ? 60.860  -7.182  -44.011 1.00 7.54  ? 91   SER A CB    1 
ATOM   700   O OG    . SER A  1  91  ? 59.453  -7.015  -43.944 1.00 9.05  ? 91   SER A OG    1 
ATOM   701   N N     . GLU A  1  92  ? 60.811  -7.756  -47.040 1.00 6.59  ? 92   GLU A N     1 
ATOM   702   C CA    . GLU A  1  92  ? 60.086  -8.078  -48.262 1.00 7.50  ? 92   GLU A CA    1 
ATOM   703   C C     . GLU A  1  92  ? 58.590  -8.135  -47.955 1.00 8.61  ? 92   GLU A C     1 
ATOM   704   O O     . GLU A  1  92  ? 57.760  -8.097  -48.867 1.00 10.13 ? 92   GLU A O     1 
ATOM   705   C CB    . GLU A  1  92  ? 60.569  -9.424  -48.818 1.00 8.12  ? 92   GLU A CB    1 
ATOM   706   C CG    A GLU A  1  92  ? 60.097  -9.734  -50.232 0.50 10.25 ? 92   GLU A CG    1 
ATOM   707   C CG    B GLU A  1  92  ? 61.975  -9.347  -49.394 0.50 10.41 ? 92   GLU A CG    1 
ATOM   708   C CD    A GLU A  1  92  ? 60.593  -11.084 -50.722 0.50 12.51 ? 92   GLU A CD    1 
ATOM   709   C CD    B GLU A  1  92  ? 62.398  -10.653 -50.036 0.50 13.25 ? 92   GLU A CD    1 
ATOM   710   O OE1   A GLU A  1  92  ? 61.713  -11.480 -50.335 0.50 12.72 ? 92   GLU A OE1   1 
ATOM   711   O OE1   B GLU A  1  92  ? 61.571  -11.588 -50.080 0.50 12.84 ? 92   GLU A OE1   1 
ATOM   712   O OE2   A GLU A  1  92  ? 59.869  -11.741 -51.502 0.50 13.35 ? 92   GLU A OE2   1 
ATOM   713   O OE2   B GLU A  1  92  ? 63.556  -10.743 -50.495 0.50 13.25 ? 92   GLU A OE2   1 
ATOM   714   N N     . ASP A  1  93  ? 58.253  -8.215  -46.666 1.00 8.33  ? 93   ASP A N     1 
ATOM   715   C CA    . ASP A  1  93  ? 56.856  -8.260  -46.232 1.00 7.38  ? 93   ASP A CA    1 
ATOM   716   C C     . ASP A  1  93  ? 56.242  -6.866  -46.337 1.00 7.66  ? 93   ASP A C     1 
ATOM   717   O O     . ASP A  1  93  ? 55.018  -6.717  -46.311 1.00 9.04  ? 93   ASP A O     1 
ATOM   718   C CB    . ASP A  1  93  ? 56.734  -8.718  -44.773 1.00 7.69  ? 93   ASP A CB    1 
ATOM   719   C CG    . ASP A  1  93  ? 57.602  -9.914  -44.451 1.00 8.87  ? 93   ASP A CG    1 
ATOM   720   O OD1   . ASP A  1  93  ? 58.777  -9.709  -44.077 1.00 8.61  ? 93   ASP A OD1   1 
ATOM   721   O OD2   . ASP A  1  93  ? 57.108  -11.057 -44.570 1.00 10.07 ? 93   ASP A OD2   1 
ATOM   722   N N     . GLY A  1  94  ? 57.104  -5.855  -46.435 1.00 8.92  ? 94   GLY A N     1 
ATOM   723   C CA    . GLY A  1  94  ? 56.655  -4.475  -46.531 1.00 8.59  ? 94   GLY A CA    1 
ATOM   724   C C     . GLY A  1  94  ? 56.668  -3.742  -45.198 1.00 9.80  ? 94   GLY A C     1 
ATOM   725   O O     . GLY A  1  94  ? 56.073  -2.673  -45.070 1.00 12.14 ? 94   GLY A O     1 
ATOM   726   N N     . ILE A  1  95  ? 57.367  -4.303  -44.214 1.00 8.28  ? 95   ILE A N     1 
ATOM   727   C CA    . ILE A  1  95  ? 57.434  -3.718  -42.875 1.00 7.94  ? 95   ILE A CA    1 
ATOM   728   C C     . ILE A  1  95  ? 58.739  -2.960  -42.619 1.00 8.06  ? 95   ILE A C     1 
ATOM   729   O O     . ILE A  1  95  ? 59.828  -3.530  -42.701 1.00 7.84  ? 95   ILE A O     1 
ATOM   730   C CB    . ILE A  1  95  ? 57.259  -4.821  -41.802 1.00 6.92  ? 95   ILE A CB    1 
ATOM   731   C CG1   . ILE A  1  95  ? 55.929  -5.550  -42.023 1.00 7.08  ? 95   ILE A CG1   1 
ATOM   732   C CG2   . ILE A  1  95  ? 57.301  -4.221  -40.400 1.00 6.59  ? 95   ILE A CG2   1 
ATOM   733   C CD1   . ILE A  1  95  ? 54.698  -4.649  -41.946 1.00 9.74  ? 95   ILE A CD1   1 
ATOM   734   N N     . ASP A  1  96  ? 58.617  -1.669  -42.318 1.00 7.95  ? 96   ASP A N     1 
ATOM   735   C CA    . ASP A  1  96  ? 59.777  -0.825  -42.044 1.00 6.95  ? 96   ASP A CA    1 
ATOM   736   C C     . ASP A  1  96  ? 60.516  -1.338  -40.812 1.00 8.42  ? 96   ASP A C     1 
ATOM   737   O O     . ASP A  1  96  ? 59.903  -1.851  -39.868 1.00 7.73  ? 96   ASP A O     1 
ATOM   738   C CB    . ASP A  1  96  ? 59.353  0.630   -41.819 1.00 7.94  ? 96   ASP A CB    1 
ATOM   739   C CG    . ASP A  1  96  ? 58.847  1.301   -43.085 1.00 11.72 ? 96   ASP A CG    1 
ATOM   740   O OD1   . ASP A  1  96  ? 59.043  0.741   -44.188 1.00 12.33 ? 96   ASP A OD1   1 
ATOM   741   O OD2   . ASP A  1  96  ? 58.262  2.404   -42.973 1.00 11.88 ? 96   ASP A OD2   1 
ATOM   742   N N     . ASN A  1  97  ? 61.833  -1.182  -40.817 1.00 7.17  ? 97   ASN A N     1 
ATOM   743   C CA    . ASN A  1  97  ? 62.652  -1.670  -39.716 1.00 7.33  ? 97   ASN A CA    1 
ATOM   744   C C     . ASN A  1  97  ? 63.984  -0.922  -39.668 1.00 8.32  ? 97   ASN A C     1 
ATOM   745   O O     . ASN A  1  97  ? 64.297  -0.126  -40.562 1.00 8.34  ? 97   ASN A O     1 
ATOM   746   C CB    . ASN A  1  97  ? 62.910  -3.168  -39.917 1.00 6.75  ? 97   ASN A CB    1 
ATOM   747   C CG    . ASN A  1  97  ? 62.927  -3.941  -38.615 1.00 7.25  ? 97   ASN A CG    1 
ATOM   748   O OD1   . ASN A  1  97  ? 63.406  -3.451  -37.599 1.00 7.95  ? 97   ASN A OD1   1 
ATOM   749   N ND2   . ASN A  1  97  ? 62.415  -5.171  -38.648 1.00 8.23  ? 97   ASN A ND2   1 
ATOM   750   N N     . VAL A  1  98  ? 64.764  -1.175  -38.620 1.00 7.15  ? 98   VAL A N     1 
ATOM   751   C CA    . VAL A  1  98  ? 66.069  -0.544  -38.462 1.00 7.85  ? 98   VAL A CA    1 
ATOM   752   C C     . VAL A  1  98  ? 67.055  -1.455  -37.734 1.00 7.33  ? 98   VAL A C     1 
ATOM   753   O O     . VAL A  1  98  ? 66.660  -2.402  -37.056 1.00 8.24  ? 98   VAL A O     1 
ATOM   754   C CB    . VAL A  1  98  ? 65.993  0.783   -37.648 1.00 8.30  ? 98   VAL A CB    1 
ATOM   755   C CG1   . VAL A  1  98  ? 65.014  1.746   -38.293 1.00 7.64  ? 98   VAL A CG1   1 
ATOM   756   C CG2   . VAL A  1  98  ? 65.591  0.496   -36.200 1.00 9.20  ? 98   VAL A CG2   1 
ATOM   757   N N     . ARG A  1  99  ? 68.341  -1.170  -37.910 1.00 8.19  ? 99   ARG A N     1 
ATOM   758   C CA    . ARG A  1  99  ? 69.403  -1.901  -37.228 1.00 6.97  ? 99   ARG A CA    1 
ATOM   759   C C     . ARG A  1  99  ? 70.511  -0.908  -36.911 1.00 7.42  ? 99   ARG A C     1 
ATOM   760   O O     . ARG A  1  99  ? 70.634  0.126   -37.569 1.00 7.70  ? 99   ARG A O     1 
ATOM   761   C CB    . ARG A  1  99  ? 69.950  -3.062  -38.071 1.00 7.96  ? 99   ARG A CB    1 
ATOM   762   C CG    . ARG A  1  99  ? 70.618  -2.687  -39.379 1.00 6.82  ? 99   ARG A CG    1 
ATOM   763   C CD    . ARG A  1  99  ? 71.411  -3.883  -39.907 1.00 7.39  ? 99   ARG A CD    1 
ATOM   764   N NE    . ARG A  1  99  ? 71.705  -3.749  -41.325 1.00 8.55  ? 99   ARG A NE    1 
ATOM   765   C CZ    . ARG A  1  99  ? 72.770  -4.265  -41.930 1.00 7.79  ? 99   ARG A CZ    1 
ATOM   766   N NH1   . ARG A  1  99  ? 73.669  -4.962  -41.243 1.00 7.65  ? 99   ARG A NH1   1 
ATOM   767   N NH2   . ARG A  1  99  ? 72.937  -4.070  -43.230 1.00 9.36  ? 99   ARG A NH2   1 
ATOM   768   N N     . GLY A  1  100 ? 71.303  -1.214  -35.892 1.00 7.23  ? 100  GLY A N     1 
ATOM   769   C CA    . GLY A  1  100 ? 72.378  -0.320  -35.510 1.00 6.93  ? 100  GLY A CA    1 
ATOM   770   C C     . GLY A  1  100 ? 73.572  -0.318  -36.445 1.00 7.94  ? 100  GLY A C     1 
ATOM   771   O O     . GLY A  1  100 ? 73.861  -1.306  -37.116 1.00 6.38  ? 100  GLY A O     1 
ATOM   772   N N     . ARG A  1  101 ? 74.271  0.810   -36.474 1.00 6.49  ? 101  ARG A N     1 
ATOM   773   C CA    . ARG A  1  101 ? 75.460  0.988   -37.306 1.00 6.96  ? 101  ARG A CA    1 
ATOM   774   C C     . ARG A  1  101 ? 76.314  1.994   -36.541 1.00 8.01  ? 101  ARG A C     1 
ATOM   775   O O     . ARG A  1  101 ? 76.401  3.165   -36.905 1.00 8.29  ? 101  ARG A O     1 
ATOM   776   C CB    . ARG A  1  101 ? 75.058  1.543   -38.676 1.00 8.25  ? 101  ARG A CB    1 
ATOM   777   C CG    . ARG A  1  101 ? 76.213  1.711   -39.656 1.00 8.46  ? 101  ARG A CG    1 
ATOM   778   C CD    . ARG A  1  101 ? 75.690  2.029   -41.040 1.00 10.57 ? 101  ARG A CD    1 
ATOM   779   N NE    . ARG A  1  101 ? 74.816  3.195   -41.008 1.00 11.68 ? 101  ARG A NE    1 
ATOM   780   C CZ    . ARG A  1  101 ? 73.964  3.523   -41.972 1.00 11.56 ? 101  ARG A CZ    1 
ATOM   781   N NH1   . ARG A  1  101 ? 73.863  2.773   -43.063 1.00 12.23 ? 101  ARG A NH1   1 
ATOM   782   N NH2   . ARG A  1  101 ? 73.202  4.596   -41.836 1.00 11.72 ? 101  ARG A NH2   1 
ATOM   783   N N     . VAL A  1  102 ? 76.934  1.516   -35.466 1.00 8.13  ? 102  VAL A N     1 
ATOM   784   C CA    . VAL A  1  102 ? 77.728  2.363   -34.587 1.00 9.04  ? 102  VAL A CA    1 
ATOM   785   C C     . VAL A  1  102 ? 78.421  1.453   -33.570 1.00 9.59  ? 102  VAL A C     1 
ATOM   786   O O     . VAL A  1  102 ? 77.982  0.324   -33.352 1.00 8.26  ? 102  VAL A O     1 
ATOM   787   C CB    . VAL A  1  102 ? 76.781  3.355   -33.850 1.00 9.33  ? 102  VAL A CB    1 
ATOM   788   C CG1   . VAL A  1  102 ? 75.700  2.575   -33.112 1.00 9.30  ? 102  VAL A CG1   1 
ATOM   789   C CG2   . VAL A  1  102 ? 77.559  4.243   -32.889 1.00 8.94  ? 102  VAL A CG2   1 
ATOM   790   N N     . LEU A  1  103 ? 79.507  1.923   -32.963 1.00 8.89  ? 103  LEU A N     1 
ATOM   791   C CA    . LEU A  1  103 ? 80.194  1.115   -31.961 1.00 8.79  ? 103  LEU A CA    1 
ATOM   792   C C     . LEU A  1  103 ? 79.237  0.962   -30.782 1.00 8.80  ? 103  LEU A C     1 
ATOM   793   O O     . LEU A  1  103 ? 78.703  1.947   -30.272 1.00 8.83  ? 103  LEU A O     1 
ATOM   794   C CB    . LEU A  1  103 ? 81.491  1.790   -31.510 1.00 8.75  ? 103  LEU A CB    1 
ATOM   795   C CG    . LEU A  1  103 ? 82.345  0.968   -30.539 1.00 8.64  ? 103  LEU A CG    1 
ATOM   796   C CD1   . LEU A  1  103 ? 82.759  -0.342  -31.205 1.00 8.31  ? 103  LEU A CD1   1 
ATOM   797   C CD2   . LEU A  1  103 ? 83.573  1.765   -30.123 1.00 8.55  ? 103  LEU A CD2   1 
ATOM   798   N N     . GLY A  1  104 ? 79.032  -0.278  -30.353 1.00 6.63  ? 104  GLY A N     1 
ATOM   799   C CA    . GLY A  1  104 ? 78.102  -0.557  -29.277 1.00 7.67  ? 104  GLY A CA    1 
ATOM   800   C C     . GLY A  1  104 ? 76.922  -1.268  -29.920 1.00 6.56  ? 104  GLY A C     1 
ATOM   801   O O     . GLY A  1  104 ? 76.080  -1.869  -29.250 1.00 8.82  ? 104  GLY A O     1 
ATOM   802   N N     . GLY A  1  105 ? 76.863  -1.188  -31.245 1.00 6.60  ? 105  GLY A N     1 
ATOM   803   C CA    . GLY A  1  105 ? 75.798  -1.842  -31.978 1.00 7.06  ? 105  GLY A CA    1 
ATOM   804   C C     . GLY A  1  105 ? 74.409  -1.305  -31.708 1.00 7.14  ? 105  GLY A C     1 
ATOM   805   O O     . GLY A  1  105 ? 74.223  -0.128  -31.389 1.00 6.97  ? 105  GLY A O     1 
ATOM   806   N N     . THR A  1  106 ? 73.421  -2.180  -31.834 1.00 6.31  ? 106  THR A N     1 
ATOM   807   C CA    . THR A  1  106 ? 72.043  -1.786  -31.631 1.00 5.63  ? 106  THR A CA    1 
ATOM   808   C C     . THR A  1  106 ? 71.716  -1.462  -30.173 1.00 6.95  ? 106  THR A C     1 
ATOM   809   O O     . THR A  1  106 ? 70.681  -0.856  -29.887 1.00 5.68  ? 106  THR A O     1 
ATOM   810   C CB    . THR A  1  106 ? 71.105  -2.876  -32.214 1.00 5.60  ? 106  THR A CB    1 
ATOM   811   O OG1   . THR A  1  106 ? 71.413  -3.046  -33.606 1.00 6.42  ? 106  THR A OG1   1 
ATOM   812   C CG2   . THR A  1  106 ? 69.650  -2.478  -32.085 1.00 6.82  ? 106  THR A CG2   1 
ATOM   813   N N     . SER A  1  107 ? 72.599  -1.838  -29.248 1.00 6.77  ? 107  SER A N     1 
ATOM   814   C CA    . SER A  1  107 ? 72.355  -1.526  -27.839 1.00 7.71  ? 107  SER A CA    1 
ATOM   815   C C     . SER A  1  107 ? 72.511  -0.014  -27.647 1.00 8.58  ? 107  SER A C     1 
ATOM   816   O O     . SER A  1  107 ? 72.106  0.536   -26.623 1.00 8.98  ? 107  SER A O     1 
ATOM   817   C CB    . SER A  1  107 ? 73.336  -2.271  -26.921 1.00 8.16  ? 107  SER A CB    1 
ATOM   818   O OG    . SER A  1  107 ? 74.638  -1.715  -26.971 1.00 8.77  ? 107  SER A OG    1 
ATOM   819   N N     . ILE A  1  108 ? 73.089  0.646   -28.649 1.00 10.08 ? 108  ILE A N     1 
ATOM   820   C CA    . ILE A  1  108 ? 73.312  2.095   -28.620 1.00 11.20 ? 108  ILE A CA    1 
ATOM   821   C C     . ILE A  1  108 ? 72.091  2.897   -29.089 1.00 11.23 ? 108  ILE A C     1 
ATOM   822   O O     . ILE A  1  108 ? 71.993  4.102   -28.834 1.00 10.95 ? 108  ILE A O     1 
ATOM   823   C CB    . ILE A  1  108 ? 74.547  2.473   -29.505 1.00 14.15 ? 108  ILE A CB    1 
ATOM   824   C CG1   . ILE A  1  108 ? 75.845  2.095   -28.786 1.00 17.45 ? 108  ILE A CG1   1 
ATOM   825   C CG2   . ILE A  1  108 ? 74.551  3.963   -29.828 1.00 16.10 ? 108  ILE A CG2   1 
ATOM   826   C CD1   . ILE A  1  108 ? 76.159  2.960   -27.569 1.00 20.61 ? 108  ILE A CD1   1 
ATOM   827   N N     . ILE A  1  109 ? 71.152  2.235   -29.760 1.00 10.31 ? 109  ILE A N     1 
ATOM   828   C CA    . ILE A  1  109 ? 69.966  2.926   -30.266 1.00 8.99  ? 109  ILE A CA    1 
ATOM   829   C C     . ILE A  1  109 ? 68.639  2.333   -29.803 1.00 8.14  ? 109  ILE A C     1 
ATOM   830   O O     . ILE A  1  109 ? 67.575  2.776   -30.248 1.00 8.26  ? 109  ILE A O     1 
ATOM   831   C CB    . ILE A  1  109 ? 69.938  2.936   -31.818 1.00 9.11  ? 109  ILE A CB    1 
ATOM   832   C CG1   . ILE A  1  109 ? 69.896  1.496   -32.350 1.00 8.51  ? 109  ILE A CG1   1 
ATOM   833   C CG2   . ILE A  1  109 ? 71.156  3.671   -32.364 1.00 10.28 ? 109  ILE A CG2   1 
ATOM   834   C CD1   . ILE A  1  109 ? 69.490  1.396   -33.807 1.00 7.42  ? 109  ILE A CD1   1 
ATOM   835   N N     . ASN A  1  110 ? 68.686  1.350   -28.909 1.00 7.80  ? 110  ASN A N     1 
ATOM   836   C CA    . ASN A  1  110 ? 67.459  0.694   -28.467 1.00 7.98  ? 110  ASN A CA    1 
ATOM   837   C C     . ASN A  1  110 ? 66.651  1.369   -27.358 1.00 8.38  ? 110  ASN A C     1 
ATOM   838   O O     . ASN A  1  110 ? 66.990  2.461   -26.901 1.00 8.10  ? 110  ASN A O     1 
ATOM   839   C CB    . ASN A  1  110 ? 67.749  -0.772  -28.106 1.00 8.02  ? 110  ASN A CB    1 
ATOM   840   C CG    . ASN A  1  110 ? 68.614  -0.930  -26.875 1.00 8.18  ? 110  ASN A CG    1 
ATOM   841   O OD1   . ASN A  1  110 ? 68.697  -0.041  -26.031 1.00 9.70  ? 110  ASN A OD1   1 
ATOM   842   N ND2   . ASN A  1  110 ? 69.248  -2.094  -26.756 1.00 6.92  ? 110  ASN A ND2   1 
ATOM   843   N N     . ALA A  1  111 ? 65.570  0.717   -26.940 1.00 6.68  ? 111  ALA A N     1 
ATOM   844   C CA    . ALA A  1  111 ? 64.691  1.265   -25.906 1.00 7.45  ? 111  ALA A CA    1 
ATOM   845   C C     . ALA A  1  111 ? 65.191  1.095   -24.470 1.00 6.83  ? 111  ALA A C     1 
ATOM   846   O O     . ALA A  1  111 ? 64.489  1.453   -23.517 1.00 8.21  ? 111  ALA A O     1 
ATOM   847   C CB    . ALA A  1  111 ? 63.291  0.676   -26.050 1.00 8.74  ? 111  ALA A CB    1 
ATOM   848   N N     . GLY A  1  112 ? 66.392  0.540   -24.323 1.00 6.56  ? 112  GLY A N     1 
ATOM   849   C CA    . GLY A  1  112 ? 66.998  0.365   -23.012 1.00 7.18  ? 112  GLY A CA    1 
ATOM   850   C C     . GLY A  1  112 ? 66.463  -0.690  -22.056 1.00 7.23  ? 112  GLY A C     1 
ATOM   851   O O     . GLY A  1  112 ? 67.015  -0.870  -20.972 1.00 7.93  ? 112  GLY A O     1 
ATOM   852   N N     . VAL A  1  113 ? 65.406  -1.397  -22.432 1.00 6.80  ? 113  VAL A N     1 
ATOM   853   C CA    . VAL A  1  113 ? 64.847  -2.410  -21.536 1.00 6.61  ? 113  VAL A CA    1 
ATOM   854   C C     . VAL A  1  113 ? 65.812  -3.583  -21.335 1.00 6.03  ? 113  VAL A C     1 
ATOM   855   O O     . VAL A  1  113 ? 66.320  -4.149  -22.299 1.00 7.64  ? 113  VAL A O     1 
ATOM   856   C CB    . VAL A  1  113 ? 63.503  -2.940  -22.075 1.00 6.63  ? 113  VAL A CB    1 
ATOM   857   C CG1   . VAL A  1  113 ? 62.888  -3.922  -21.081 1.00 7.39  ? 113  VAL A CG1   1 
ATOM   858   C CG2   . VAL A  1  113 ? 62.553  -1.776  -22.316 1.00 6.26  ? 113  VAL A CG2   1 
ATOM   859   N N     . TYR A  1  114 ? 66.064  -3.937  -20.075 1.00 6.67  ? 114  TYR A N     1 
ATOM   860   C CA    . TYR A  1  114 ? 66.967  -5.040  -19.761 1.00 7.21  ? 114  TYR A CA    1 
ATOM   861   C C     . TYR A  1  114 ? 66.286  -6.163  -18.991 1.00 8.38  ? 114  TYR A C     1 
ATOM   862   O O     . TYR A  1  114 ? 65.636  -5.926  -17.970 1.00 9.23  ? 114  TYR A O     1 
ATOM   863   C CB    . TYR A  1  114 ? 68.158  -4.546  -18.934 1.00 7.41  ? 114  TYR A CB    1 
ATOM   864   C CG    . TYR A  1  114 ? 69.139  -5.649  -18.584 1.00 7.23  ? 114  TYR A CG    1 
ATOM   865   C CD1   . TYR A  1  114 ? 70.266  -5.881  -19.370 1.00 7.41  ? 114  TYR A CD1   1 
ATOM   866   C CD2   . TYR A  1  114 ? 68.920  -6.482  -17.484 1.00 7.38  ? 114  TYR A CD2   1 
ATOM   867   C CE1   . TYR A  1  114 ? 71.154  -6.916  -19.072 1.00 8.45  ? 114  TYR A CE1   1 
ATOM   868   C CE2   . TYR A  1  114 ? 69.798  -7.520  -17.179 1.00 7.07  ? 114  TYR A CE2   1 
ATOM   869   C CZ    . TYR A  1  114 ? 70.914  -7.731  -17.976 1.00 7.93  ? 114  TYR A CZ    1 
ATOM   870   O OH    . TYR A  1  114 ? 71.795  -8.749  -17.678 1.00 8.07  ? 114  TYR A OH    1 
ATOM   871   N N     . ALA A  1  115 ? 66.458  -7.389  -19.477 1.00 7.87  ? 115  ALA A N     1 
ATOM   872   C CA    . ALA A  1  115 ? 65.885  -8.558  -18.827 1.00 8.66  ? 115  ALA A CA    1 
ATOM   873   C C     . ALA A  1  115 ? 66.810  -9.747  -19.024 1.00 8.58  ? 115  ALA A C     1 
ATOM   874   O O     . ALA A  1  115 ? 67.524  -9.824  -20.022 1.00 7.72  ? 115  ALA A O     1 
ATOM   875   C CB    . ALA A  1  115 ? 64.516  -8.873  -19.421 1.00 9.28  ? 115  ALA A CB    1 
ATOM   876   N N     . ARG A  1  116 ? 66.821  -10.658 -18.058 1.00 9.01  ? 116  ARG A N     1 
ATOM   877   C CA    . ARG A  1  116 ? 67.622  -11.863 -18.185 1.00 9.09  ? 116  ARG A CA    1 
ATOM   878   C C     . ARG A  1  116 ? 66.741  -12.838 -18.951 1.00 9.53  ? 116  ARG A C     1 
ATOM   879   O O     . ARG A  1  116 ? 65.513  -12.737 -18.912 1.00 9.99  ? 116  ARG A O     1 
ATOM   880   C CB    . ARG A  1  116 ? 67.965  -12.455 -16.815 1.00 9.72  ? 116  ARG A CB    1 
ATOM   881   C CG    . ARG A  1  116 ? 69.017  -11.687 -16.043 1.00 9.22  ? 116  ARG A CG    1 
ATOM   882   C CD    . ARG A  1  116 ? 69.416  -12.444 -14.789 1.00 10.60 ? 116  ARG A CD    1 
ATOM   883   N NE    . ARG A  1  116 ? 70.472  -11.763 -14.047 1.00 9.82  ? 116  ARG A NE    1 
ATOM   884   C CZ    . ARG A  1  116 ? 71.069  -12.266 -12.971 1.00 12.46 ? 116  ARG A CZ    1 
ATOM   885   N NH1   . ARG A  1  116 ? 70.715  -13.461 -12.508 1.00 11.69 ? 116  ARG A NH1   1 
ATOM   886   N NH2   . ARG A  1  116 ? 72.021  -11.575 -12.357 1.00 13.68 ? 116  ARG A NH2   1 
ATOM   887   N N     . ALA A  1  117 ? 67.360  -13.786 -19.638 1.00 9.18  ? 117  ALA A N     1 
ATOM   888   C CA    . ALA A  1  117 ? 66.600  -14.755 -20.408 1.00 8.96  ? 117  ALA A CA    1 
ATOM   889   C C     . ALA A  1  117 ? 65.753  -15.677 -19.536 1.00 10.07 ? 117  ALA A C     1 
ATOM   890   O O     . ALA A  1  117 ? 66.073  -15.931 -18.372 1.00 11.87 ? 117  ALA A O     1 
ATOM   891   C CB    . ALA A  1  117 ? 67.544  -15.588 -21.270 1.00 9.00  ? 117  ALA A CB    1 
ATOM   892   N N     . ASN A  1  118 ? 64.662  -16.160 -20.121 1.00 10.50 ? 118  ASN A N     1 
ATOM   893   C CA    . ASN A  1  118 ? 63.760  -17.108 -19.472 1.00 10.82 ? 118  ASN A CA    1 
ATOM   894   C C     . ASN A  1  118 ? 64.684  -18.243 -19.003 1.00 12.71 ? 118  ASN A C     1 
ATOM   895   O O     . ASN A  1  118 ? 65.389  -18.840 -19.815 1.00 13.67 ? 118  ASN A O     1 
ATOM   896   C CB    . ASN A  1  118 ? 62.769  -17.622 -20.522 1.00 10.24 ? 118  ASN A CB    1 
ATOM   897   C CG    . ASN A  1  118 ? 61.773  -18.619 -19.966 1.00 11.95 ? 118  ASN A CG    1 
ATOM   898   O OD1   . ASN A  1  118 ? 62.063  -19.355 -19.027 1.00 14.94 ? 118  ASN A OD1   1 
ATOM   899   N ND2   . ASN A  1  118 ? 60.593  -18.656 -20.575 1.00 13.45 ? 118  ASN A ND2   1 
ATOM   900   N N     . THR A  1  119 ? 64.692  -18.537 -17.706 1.00 13.18 ? 119  THR A N     1 
ATOM   901   C CA    . THR A  1  119 ? 65.575  -19.581 -17.180 1.00 14.07 ? 119  THR A CA    1 
ATOM   902   C C     . THR A  1  119 ? 65.281  -20.997 -17.668 1.00 15.34 ? 119  THR A C     1 
ATOM   903   O O     . THR A  1  119 ? 66.062  -21.913 -17.411 1.00 16.24 ? 119  THR A O     1 
ATOM   904   C CB    . THR A  1  119 ? 65.566  -19.603 -15.633 1.00 15.32 ? 119  THR A CB    1 
ATOM   905   O OG1   . THR A  1  119 ? 64.235  -19.843 -15.162 1.00 16.28 ? 119  THR A OG1   1 
ATOM   906   C CG2   . THR A  1  119 ? 66.074  -18.284 -15.078 1.00 15.22 ? 119  THR A CG2   1 
ATOM   907   N N     . SER A  1  120 ? 64.172  -21.175 -18.378 1.00 15.93 ? 120  SER A N     1 
ATOM   908   C CA    . SER A  1  120 ? 63.787  -22.497 -18.870 1.00 17.84 ? 120  SER A CA    1 
ATOM   909   C C     . SER A  1  120 ? 64.178  -22.787 -20.318 1.00 18.17 ? 120  SER A C     1 
ATOM   910   O O     . SER A  1  120 ? 63.994  -23.906 -20.795 1.00 18.82 ? 120  SER A O     1 
ATOM   911   C CB    . SER A  1  120 ? 62.272  -22.683 -18.727 1.00 17.69 ? 120  SER A CB    1 
ATOM   912   O OG    . SER A  1  120 ? 61.856  -22.512 -17.384 1.00 19.93 ? 120  SER A OG    1 
ATOM   913   N N     . ILE A  1  121 ? 64.726  -21.796 -21.015 1.00 18.25 ? 121  ILE A N     1 
ATOM   914   C CA    . ILE A  1  121 ? 65.092  -21.981 -22.417 1.00 18.61 ? 121  ILE A CA    1 
ATOM   915   C C     . ILE A  1  121 ? 66.485  -22.540 -22.697 1.00 18.41 ? 121  ILE A C     1 
ATOM   916   O O     . ILE A  1  121 ? 66.779  -22.919 -23.829 1.00 18.07 ? 121  ILE A O     1 
ATOM   917   C CB    . ILE A  1  121 ? 64.941  -20.659 -23.198 1.00 19.39 ? 121  ILE A CB    1 
ATOM   918   C CG1   . ILE A  1  121 ? 65.901  -19.608 -22.638 1.00 21.43 ? 121  ILE A CG1   1 
ATOM   919   C CG2   . ILE A  1  121 ? 63.504  -20.170 -23.107 1.00 19.14 ? 121  ILE A CG2   1 
ATOM   920   C CD1   . ILE A  1  121 ? 65.793  -18.253 -23.306 1.00 23.20 ? 121  ILE A CD1   1 
ATOM   921   N N     . TYR A  1  122 ? 67.341  -22.601 -21.682 1.00 17.83 ? 122  TYR A N     1 
ATOM   922   C CA    . TYR A  1  122 ? 68.696  -23.103 -21.884 1.00 17.54 ? 122  TYR A CA    1 
ATOM   923   C C     . TYR A  1  122 ? 68.781  -24.592 -22.218 1.00 19.36 ? 122  TYR A C     1 
ATOM   924   O O     . TYR A  1  122 ? 69.583  -24.999 -23.056 1.00 19.43 ? 122  TYR A O     1 
ATOM   925   C CB    . TYR A  1  122 ? 69.566  -22.817 -20.654 1.00 15.22 ? 122  TYR A CB    1 
ATOM   926   C CG    . TYR A  1  122 ? 69.696  -21.347 -20.323 1.00 13.74 ? 122  TYR A CG    1 
ATOM   927   C CD1   . TYR A  1  122 ? 68.803  -20.726 -19.451 1.00 13.11 ? 122  TYR A CD1   1 
ATOM   928   C CD2   . TYR A  1  122 ? 70.705  -20.572 -20.894 1.00 13.03 ? 122  TYR A CD2   1 
ATOM   929   C CE1   . TYR A  1  122 ? 68.910  -19.365 -19.153 1.00 13.81 ? 122  TYR A CE1   1 
ATOM   930   C CE2   . TYR A  1  122 ? 70.820  -19.210 -20.606 1.00 13.93 ? 122  TYR A CE2   1 
ATOM   931   C CZ    . TYR A  1  122 ? 69.921  -18.615 -19.735 1.00 12.46 ? 122  TYR A CZ    1 
ATOM   932   O OH    . TYR A  1  122 ? 70.029  -17.274 -19.448 1.00 11.38 ? 122  TYR A OH    1 
ATOM   933   N N     . SER A  1  123 ? 67.949  -25.402 -21.572 1.00 21.03 ? 123  SER A N     1 
ATOM   934   C CA    . SER A  1  123 ? 67.974  -26.845 -21.803 1.00 23.63 ? 123  SER A CA    1 
ATOM   935   C C     . SER A  1  123 ? 67.738  -27.353 -23.222 1.00 24.22 ? 123  SER A C     1 
ATOM   936   O O     . SER A  1  123 ? 68.365  -28.322 -23.635 1.00 25.56 ? 123  SER A O     1 
ATOM   937   C CB    . SER A  1  123 ? 67.005  -27.547 -20.851 1.00 24.52 ? 123  SER A CB    1 
ATOM   938   O OG    . SER A  1  123 ? 67.667  -27.926 -19.655 1.00 29.68 ? 123  SER A OG    1 
ATOM   939   N N     . ALA A  1  124 ? 66.857  -26.708 -23.974 1.00 24.65 ? 124  ALA A N     1 
ATOM   940   C CA    . ALA A  1  124 ? 66.563  -27.160 -25.331 1.00 25.81 ? 124  ALA A CA    1 
ATOM   941   C C     . ALA A  1  124 ? 67.205  -26.323 -26.429 1.00 25.48 ? 124  ALA A C     1 
ATOM   942   O O     . ALA A  1  124 ? 66.847  -26.445 -27.592 1.00 26.92 ? 124  ALA A O     1 
ATOM   943   C CB    . ALA A  1  124 ? 65.049  -27.200 -25.527 1.00 26.24 ? 124  ALA A CB    1 
ATOM   944   N N     . SER A  1  125 ? 68.162  -25.482 -26.057 1.00 23.37 ? 125  SER A N     1 
ATOM   945   C CA    . SER A  1  125 ? 68.833  -24.593 -27.007 1.00 21.33 ? 125  SER A CA    1 
ATOM   946   C C     . SER A  1  125 ? 69.847  -25.229 -27.964 1.00 19.97 ? 125  SER A C     1 
ATOM   947   O O     . SER A  1  125 ? 70.160  -24.657 -29.009 1.00 18.86 ? 125  SER A O     1 
ATOM   948   C CB    . SER A  1  125 ? 69.537  -23.471 -26.243 1.00 21.05 ? 125  SER A CB    1 
ATOM   949   O OG    . SER A  1  125 ? 70.546  -24.018 -25.417 1.00 20.25 ? 125  SER A OG    1 
ATOM   950   N N     . GLY A  1  126 ? 70.369  -26.398 -27.614 1.00 18.96 ? 126  GLY A N     1 
ATOM   951   C CA    . GLY A  1  126 ? 71.356  -27.038 -28.468 1.00 17.25 ? 126  GLY A CA    1 
ATOM   952   C C     . GLY A  1  126 ? 72.756  -26.723 -27.968 1.00 15.88 ? 126  GLY A C     1 
ATOM   953   O O     . GLY A  1  126 ? 73.754  -27.071 -28.598 1.00 14.74 ? 126  GLY A O     1 
ATOM   954   N N     . VAL A  1  127 ? 72.818  -26.044 -26.828 1.00 15.21 ? 127  VAL A N     1 
ATOM   955   C CA    . VAL A  1  127 ? 74.082  -25.675 -26.196 1.00 14.54 ? 127  VAL A CA    1 
ATOM   956   C C     . VAL A  1  127 ? 74.078  -26.219 -24.769 1.00 15.51 ? 127  VAL A C     1 
ATOM   957   O O     . VAL A  1  127 ? 73.062  -26.149 -24.081 1.00 14.89 ? 127  VAL A O     1 
ATOM   958   C CB    . VAL A  1  127 ? 74.255  -24.131 -26.134 1.00 13.45 ? 127  VAL A CB    1 
ATOM   959   C CG1   . VAL A  1  127 ? 75.445  -23.768 -25.250 1.00 13.28 ? 127  VAL A CG1   1 
ATOM   960   C CG2   . VAL A  1  127 ? 74.448  -23.571 -27.533 1.00 14.16 ? 127  VAL A CG2   1 
ATOM   961   N N     . ASP A  1  128 ? 75.206  -26.771 -24.333 1.00 16.13 ? 128  ASP A N     1 
ATOM   962   C CA    . ASP A  1  128 ? 75.321  -27.298 -22.975 1.00 18.66 ? 128  ASP A CA    1 
ATOM   963   C C     . ASP A  1  128 ? 75.799  -26.128 -22.124 1.00 16.83 ? 128  ASP A C     1 
ATOM   964   O O     . ASP A  1  128 ? 77.000  -25.898 -21.988 1.00 18.60 ? 128  ASP A O     1 
ATOM   965   C CB    . ASP A  1  128 ? 76.344  -28.437 -22.927 1.00 21.41 ? 128  ASP A CB    1 
ATOM   966   C CG    . ASP A  1  128 ? 76.427  -29.092 -21.559 1.00 27.40 ? 128  ASP A CG    1 
ATOM   967   O OD1   . ASP A  1  128 ? 75.827  -28.559 -20.601 1.00 30.42 ? 128  ASP A OD1   1 
ATOM   968   O OD2   . ASP A  1  128 ? 77.099  -30.140 -21.440 1.00 30.30 ? 128  ASP A OD2   1 
ATOM   969   N N     . TRP A  1  129 ? 74.853  -25.389 -21.557 1.00 16.37 ? 129  TRP A N     1 
ATOM   970   C CA    . TRP A  1  129 ? 75.176  -24.213 -20.758 1.00 15.10 ? 129  TRP A CA    1 
ATOM   971   C C     . TRP A  1  129 ? 75.733  -24.458 -19.365 1.00 15.53 ? 129  TRP A C     1 
ATOM   972   O O     . TRP A  1  129 ? 75.289  -25.354 -18.648 1.00 16.42 ? 129  TRP A O     1 
ATOM   973   C CB    . TRP A  1  129 ? 73.943  -23.313 -20.613 1.00 15.51 ? 129  TRP A CB    1 
ATOM   974   C CG    . TRP A  1  129 ? 73.392  -22.792 -21.902 1.00 14.24 ? 129  TRP A CG    1 
ATOM   975   C CD1   . TRP A  1  129 ? 72.455  -23.387 -22.695 1.00 14.45 ? 129  TRP A CD1   1 
ATOM   976   C CD2   . TRP A  1  129 ? 73.743  -21.563 -22.545 1.00 14.17 ? 129  TRP A CD2   1 
ATOM   977   N NE1   . TRP A  1  129 ? 72.198  -22.603 -23.796 1.00 13.96 ? 129  TRP A NE1   1 
ATOM   978   C CE2   . TRP A  1  129 ? 72.976  -21.477 -23.728 1.00 13.96 ? 129  TRP A CE2   1 
ATOM   979   C CE3   . TRP A  1  129 ? 74.633  -20.525 -22.238 1.00 14.79 ? 129  TRP A CE3   1 
ATOM   980   C CZ2   . TRP A  1  129 ? 73.072  -20.392 -24.607 1.00 14.13 ? 129  TRP A CZ2   1 
ATOM   981   C CZ3   . TRP A  1  129 ? 74.729  -19.445 -23.112 1.00 14.19 ? 129  TRP A CZ3   1 
ATOM   982   C CH2   . TRP A  1  129 ? 73.952  -19.389 -24.282 1.00 13.36 ? 129  TRP A CH2   1 
ATOM   983   N N     . ASP A  1  130 ? 76.711  -23.636 -18.997 1.00 15.35 ? 130  ASP A N     1 
ATOM   984   C CA    . ASP A  1  130 ? 77.323  -23.665 -17.674 1.00 14.82 ? 130  ASP A CA    1 
ATOM   985   C C     . ASP A  1  130 ? 76.532  -22.567 -16.967 1.00 15.49 ? 130  ASP A C     1 
ATOM   986   O O     . ASP A  1  130 ? 76.850  -21.384 -17.103 1.00 13.47 ? 130  ASP A O     1 
ATOM   987   C CB    . ASP A  1  130 ? 78.800  -23.265 -17.763 1.00 16.27 ? 130  ASP A CB    1 
ATOM   988   C CG    . ASP A  1  130 ? 79.493  -23.261 -16.411 1.00 17.39 ? 130  ASP A CG    1 
ATOM   989   O OD1   . ASP A  1  130 ? 78.812  -23.049 -15.386 1.00 17.91 ? 130  ASP A OD1   1 
ATOM   990   O OD2   . ASP A  1  130 ? 80.728  -23.454 -16.377 1.00 20.39 ? 130  ASP A OD2   1 
ATOM   991   N N     . MET A  1  131 ? 75.493  -22.949 -16.230 1.00 15.28 ? 131  MET A N     1 
ATOM   992   C CA    . MET A  1  131 ? 74.654  -21.962 -15.561 1.00 16.03 ? 131  MET A CA    1 
ATOM   993   C C     . MET A  1  131 ? 75.358  -21.089 -14.532 1.00 15.48 ? 131  MET A C     1 
ATOM   994   O O     . MET A  1  131 ? 74.974  -19.934 -14.340 1.00 14.96 ? 131  MET A O     1 
ATOM   995   C CB    . MET A  1  131 ? 73.429  -22.635 -14.938 1.00 17.79 ? 131  MET A CB    1 
ATOM   996   C CG    . MET A  1  131 ? 72.463  -23.216 -15.970 1.00 20.04 ? 131  MET A CG    1 
ATOM   997   S SD    . MET A  1  131 ? 72.106  -22.094 -17.361 1.00 23.73 ? 131  MET A SD    1 
ATOM   998   C CE    . MET A  1  131 ? 71.238  -20.763 -16.539 1.00 18.83 ? 131  MET A CE    1 
ATOM   999   N N     . ASP A  1  132 ? 76.376  -21.619 -13.862 1.00 15.12 ? 132  ASP A N     1 
ATOM   1000  C CA    . ASP A  1  132 ? 77.099  -20.801 -12.897 1.00 15.73 ? 132  ASP A CA    1 
ATOM   1001  C C     . ASP A  1  132 ? 77.768  -19.662 -13.660 1.00 13.73 ? 132  ASP A C     1 
ATOM   1002  O O     . ASP A  1  132 ? 77.773  -18.515 -13.206 1.00 14.47 ? 132  ASP A O     1 
ATOM   1003  C CB    . ASP A  1  132 ? 78.168  -21.614 -12.159 1.00 18.65 ? 132  ASP A CB    1 
ATOM   1004  C CG    . ASP A  1  132 ? 77.576  -22.658 -11.232 1.00 21.60 ? 132  ASP A CG    1 
ATOM   1005  O OD1   . ASP A  1  132 ? 76.548  -22.373 -10.585 1.00 22.05 ? 132  ASP A OD1   1 
ATOM   1006  O OD2   . ASP A  1  132 ? 78.151  -23.763 -11.137 1.00 25.81 ? 132  ASP A OD2   1 
ATOM   1007  N N     . LEU A  1  133 ? 78.326  -19.986 -14.826 1.00 13.11 ? 133  LEU A N     1 
ATOM   1008  C CA    . LEU A  1  133 ? 78.999  -18.996 -15.659 1.00 11.46 ? 133  LEU A CA    1 
ATOM   1009  C C     . LEU A  1  133 ? 77.992  -18.014 -16.247 1.00 10.05 ? 133  LEU A C     1 
ATOM   1010  O O     . LEU A  1  133 ? 78.259  -16.817 -16.332 1.00 10.42 ? 133  LEU A O     1 
ATOM   1011  C CB    . LEU A  1  133 ? 79.780  -19.687 -16.784 1.00 12.47 ? 133  LEU A CB    1 
ATOM   1012  C CG    . LEU A  1  133 ? 80.536  -18.779 -17.761 1.00 12.66 ? 133  LEU A CG    1 
ATOM   1013  C CD1   . LEU A  1  133 ? 81.478  -17.844 -16.998 1.00 13.12 ? 133  LEU A CD1   1 
ATOM   1014  C CD2   . LEU A  1  133 ? 81.306  -19.642 -18.755 1.00 14.68 ? 133  LEU A CD2   1 
ATOM   1015  N N     . VAL A  1  134 ? 76.834  -18.523 -16.655 1.00 10.19 ? 134  VAL A N     1 
ATOM   1016  C CA    . VAL A  1  134 ? 75.799  -17.663 -17.211 1.00 10.46 ? 134  VAL A CA    1 
ATOM   1017  C C     . VAL A  1  134 ? 75.441  -16.559 -16.220 1.00 10.87 ? 134  VAL A C     1 
ATOM   1018  O O     . VAL A  1  134 ? 75.460  -15.378 -16.564 1.00 11.78 ? 134  VAL A O     1 
ATOM   1019  C CB    . VAL A  1  134 ? 74.520  -18.464 -17.555 1.00 11.05 ? 134  VAL A CB    1 
ATOM   1020  C CG1   . VAL A  1  134 ? 73.369  -17.509 -17.860 1.00 9.83  ? 134  VAL A CG1   1 
ATOM   1021  C CG2   . VAL A  1  134 ? 74.783  -19.368 -18.755 1.00 10.76 ? 134  VAL A CG2   1 
ATOM   1022  N N     . ASN A  1  135 ? 75.129  -16.938 -14.984 1.00 11.26 ? 135  ASN A N     1 
ATOM   1023  C CA    . ASN A  1  135 ? 74.764  -15.944 -13.983 1.00 11.38 ? 135  ASN A CA    1 
ATOM   1024  C C     . ASN A  1  135 ? 75.918  -15.018 -13.618 1.00 10.87 ? 135  ASN A C     1 
ATOM   1025  O O     . ASN A  1  135 ? 75.711  -13.828 -13.377 1.00 10.35 ? 135  ASN A O     1 
ATOM   1026  C CB    . ASN A  1  135 ? 74.206  -16.626 -12.736 1.00 11.64 ? 135  ASN A CB    1 
ATOM   1027  C CG    . ASN A  1  135 ? 72.797  -17.144 -12.944 1.00 13.40 ? 135  ASN A CG    1 
ATOM   1028  O OD1   . ASN A  1  135 ? 72.226  -17.007 -14.025 1.00 12.41 ? 135  ASN A OD1   1 
ATOM   1029  N ND2   . ASN A  1  135 ? 72.238  -17.742 -11.898 1.00 15.04 ? 135  ASN A ND2   1 
ATOM   1030  N N     . GLN A  1  136 ? 77.134  -15.553 -13.578 1.00 11.24 ? 136  GLN A N     1 
ATOM   1031  C CA    . GLN A  1  136 ? 78.297  -14.728 -13.271 1.00 11.35 ? 136  GLN A CA    1 
ATOM   1032  C C     . GLN A  1  136 ? 78.450  -13.671 -14.356 1.00 10.67 ? 136  GLN A C     1 
ATOM   1033  O O     . GLN A  1  136 ? 78.824  -12.530 -14.082 1.00 10.15 ? 136  GLN A O     1 
ATOM   1034  C CB    . GLN A  1  136 ? 79.564  -15.581 -13.223 1.00 11.05 ? 136  GLN A CB    1 
ATOM   1035  C CG    . GLN A  1  136 ? 79.708  -16.415 -11.968 1.00 15.13 ? 136  GLN A CG    1 
ATOM   1036  C CD    . GLN A  1  136 ? 80.750  -17.498 -12.126 1.00 17.85 ? 136  GLN A CD    1 
ATOM   1037  O OE1   . GLN A  1  136 ? 81.580  -17.447 -13.037 1.00 19.47 ? 136  GLN A OE1   1 
ATOM   1038  N NE2   . GLN A  1  136 ? 80.720  -18.484 -11.237 1.00 17.71 ? 136  GLN A NE2   1 
ATOM   1039  N N     . THR A  1  137 ? 78.146  -14.061 -15.592 1.00 9.90  ? 137  THR A N     1 
ATOM   1040  C CA    . THR A  1  137 ? 78.258  -13.156 -16.726 1.00 9.48  ? 137  THR A CA    1 
ATOM   1041  C C     . THR A  1  137 ? 77.158  -12.096 -16.701 1.00 9.88  ? 137  THR A C     1 
ATOM   1042  O O     . THR A  1  137 ? 77.405  -10.936 -17.027 1.00 8.44  ? 137  THR A O     1 
ATOM   1043  C CB    . THR A  1  137 ? 78.232  -13.945 -18.051 1.00 10.38 ? 137  THR A CB    1 
ATOM   1044  O OG1   . THR A  1  137 ? 79.311  -14.892 -18.052 1.00 10.77 ? 137  THR A OG1   1 
ATOM   1045  C CG2   . THR A  1  137 ? 78.400  -13.006 -19.239 1.00 10.85 ? 137  THR A CG2   1 
ATOM   1046  N N     . TYR A  1  138 ? 75.947  -12.485 -16.313 1.00 9.07  ? 138  TYR A N     1 
ATOM   1047  C CA    . TYR A  1  138 ? 74.858  -11.516 -16.213 1.00 9.40  ? 138  TYR A CA    1 
ATOM   1048  C C     . TYR A  1  138 ? 75.268  -10.452 -15.190 1.00 9.56  ? 138  TYR A C     1 
ATOM   1049  O O     . TYR A  1  138 ? 75.095  -9.255  -15.420 1.00 8.99  ? 138  TYR A O     1 
ATOM   1050  C CB    . TYR A  1  138 ? 73.561  -12.193 -15.752 1.00 8.65  ? 138  TYR A CB    1 
ATOM   1051  C CG    . TYR A  1  138 ? 72.739  -12.831 -16.857 1.00 9.03  ? 138  TYR A CG    1 
ATOM   1052  C CD1   . TYR A  1  138 ? 72.248  -14.130 -16.724 1.00 9.83  ? 138  TYR A CD1   1 
ATOM   1053  C CD2   . TYR A  1  138 ? 72.425  -12.125 -18.016 1.00 9.23  ? 138  TYR A CD2   1 
ATOM   1054  C CE1   . TYR A  1  138 ? 71.462  -14.712 -17.719 1.00 10.21 ? 138  TYR A CE1   1 
ATOM   1055  C CE2   . TYR A  1  138 ? 71.636  -12.698 -19.021 1.00 8.70  ? 138  TYR A CE2   1 
ATOM   1056  C CZ    . TYR A  1  138 ? 71.160  -13.990 -18.864 1.00 9.57  ? 138  TYR A CZ    1 
ATOM   1057  O OH    . TYR A  1  138 ? 70.380  -14.559 -19.846 1.00 10.35 ? 138  TYR A OH    1 
ATOM   1058  N N     . GLU A  1  139 ? 75.820  -10.899 -14.062 1.00 10.39 ? 139  GLU A N     1 
ATOM   1059  C CA    . GLU A  1  139 ? 76.253  -9.993  -13.000 1.00 11.35 ? 139  GLU A CA    1 
ATOM   1060  C C     . GLU A  1  139 ? 77.340  -9.037  -13.496 1.00 9.51  ? 139  GLU A C     1 
ATOM   1061  O O     . GLU A  1  139 ? 77.316  -7.846  -13.196 1.00 11.64 ? 139  GLU A O     1 
ATOM   1062  C CB    . GLU A  1  139 ? 76.766  -10.806 -11.803 1.00 12.36 ? 139  GLU A CB    1 
ATOM   1063  C CG    . GLU A  1  139 ? 75.689  -11.666 -11.145 1.00 16.94 ? 139  GLU A CG    1 
ATOM   1064  C CD    . GLU A  1  139 ? 76.255  -12.714 -10.201 1.00 22.11 ? 139  GLU A CD    1 
ATOM   1065  O OE1   . GLU A  1  139 ? 75.455  -13.424 -9.552  1.00 24.98 ? 139  GLU A OE1   1 
ATOM   1066  O OE2   . GLU A  1  139 ? 77.494  -12.832 -10.110 1.00 23.69 ? 139  GLU A OE2   1 
ATOM   1067  N N     . TRP A  1  140 ? 78.283  -9.572  -14.267 1.00 9.88  ? 140  TRP A N     1 
ATOM   1068  C CA    . TRP A  1  140 ? 79.387  -8.796  -14.832 1.00 9.94  ? 140  TRP A CA    1 
ATOM   1069  C C     . TRP A  1  140 ? 78.844  -7.654  -15.703 1.00 9.54  ? 140  TRP A C     1 
ATOM   1070  O O     . TRP A  1  140 ? 79.311  -6.515  -15.621 1.00 11.20 ? 140  TRP A O     1 
ATOM   1071  C CB    . TRP A  1  140 ? 80.259  -9.738  -15.666 1.00 10.38 ? 140  TRP A CB    1 
ATOM   1072  C CG    . TRP A  1  140 ? 81.524  -9.171  -16.256 1.00 11.24 ? 140  TRP A CG    1 
ATOM   1073  C CD1   . TRP A  1  140 ? 82.767  -9.152  -15.682 1.00 11.66 ? 140  TRP A CD1   1 
ATOM   1074  C CD2   . TRP A  1  140 ? 81.694  -8.680  -17.590 1.00 10.50 ? 140  TRP A CD2   1 
ATOM   1075  N NE1   . TRP A  1  140 ? 83.701  -8.695  -16.585 1.00 10.80 ? 140  TRP A NE1   1 
ATOM   1076  C CE2   . TRP A  1  140 ? 83.067  -8.398  -17.764 1.00 10.72 ? 140  TRP A CE2   1 
ATOM   1077  C CE3   . TRP A  1  140 ? 80.816  -8.459  -18.661 1.00 10.73 ? 140  TRP A CE3   1 
ATOM   1078  C CZ2   . TRP A  1  140 ? 83.584  -7.909  -18.968 1.00 12.54 ? 140  TRP A CZ2   1 
ATOM   1079  C CZ3   . TRP A  1  140 ? 81.332  -7.973  -19.858 1.00 12.40 ? 140  TRP A CZ3   1 
ATOM   1080  C CH2   . TRP A  1  140 ? 82.703  -7.705  -20.000 1.00 11.39 ? 140  TRP A CH2   1 
ATOM   1081  N N     . VAL A  1  141 ? 77.857  -7.964  -16.539 1.00 9.07  ? 141  VAL A N     1 
ATOM   1082  C CA    . VAL A  1  141 ? 77.244  -6.964  -17.405 1.00 9.88  ? 141  VAL A CA    1 
ATOM   1083  C C     . VAL A  1  141 ? 76.411  -5.974  -16.592 1.00 9.12  ? 141  VAL A C     1 
ATOM   1084  O O     . VAL A  1  141 ? 76.534  -4.760  -16.750 1.00 9.81  ? 141  VAL A O     1 
ATOM   1085  C CB    . VAL A  1  141 ? 76.318  -7.625  -18.455 1.00 8.47  ? 141  VAL A CB    1 
ATOM   1086  C CG1   . VAL A  1  141 ? 75.568  -6.554  -19.247 1.00 9.22  ? 141  VAL A CG1   1 
ATOM   1087  C CG2   . VAL A  1  141 ? 77.133  -8.501  -19.388 1.00 10.33 ? 141  VAL A CG2   1 
ATOM   1088  N N     . GLU A  1  142 ? 75.566  -6.507  -15.715 1.00 9.50  ? 142  GLU A N     1 
ATOM   1089  C CA    . GLU A  1  142 ? 74.684  -5.688  -14.895 1.00 9.49  ? 142  GLU A CA    1 
ATOM   1090  C C     . GLU A  1  142 ? 75.403  -4.712  -13.975 1.00 9.41  ? 142  GLU A C     1 
ATOM   1091  O O     . GLU A  1  142 ? 74.940  -3.590  -13.772 1.00 10.13 ? 142  GLU A O     1 
ATOM   1092  C CB    . GLU A  1  142 ? 73.750  -6.598  -14.095 1.00 10.54 ? 142  GLU A CB    1 
ATOM   1093  C CG    . GLU A  1  142 ? 72.761  -7.329  -14.995 1.00 8.97  ? 142  GLU A CG    1 
ATOM   1094  C CD    . GLU A  1  142 ? 72.225  -8.601  -14.384 1.00 10.20 ? 142  GLU A CD    1 
ATOM   1095  O OE1   . GLU A  1  142 ? 71.555  -9.369  -15.112 1.00 9.27  ? 142  GLU A OE1   1 
ATOM   1096  O OE2   . GLU A  1  142 ? 72.468  -8.834  -13.181 1.00 11.97 ? 142  GLU A OE2   1 
ATOM   1097  N N     . ASP A  1  143 ? 76.539  -5.128  -13.430 1.00 9.64  ? 143  ASP A N     1 
ATOM   1098  C CA    . ASP A  1  143 ? 77.293  -4.254  -12.546 1.00 12.01 ? 143  ASP A CA    1 
ATOM   1099  C C     . ASP A  1  143 ? 77.940  -3.105  -13.311 1.00 11.67 ? 143  ASP A C     1 
ATOM   1100  O O     . ASP A  1  143 ? 78.433  -2.152  -12.706 1.00 11.86 ? 143  ASP A O     1 
ATOM   1101  C CB    . ASP A  1  143 ? 78.371  -5.044  -11.796 1.00 14.02 ? 143  ASP A CB    1 
ATOM   1102  C CG    . ASP A  1  143 ? 77.790  -5.964  -10.735 1.00 17.56 ? 143  ASP A CG    1 
ATOM   1103  O OD1   . ASP A  1  143 ? 76.598  -5.807  -10.389 1.00 20.71 ? 143  ASP A OD1   1 
ATOM   1104  O OD2   . ASP A  1  143 ? 78.530  -6.838  -10.238 1.00 19.75 ? 143  ASP A OD2   1 
ATOM   1105  N N     . THR A  1  144 ? 77.921  -3.181  -14.640 1.00 11.11 ? 144  THR A N     1 
ATOM   1106  C CA    . THR A  1  144 ? 78.533  -2.140  -15.455 1.00 10.71 ? 144  THR A CA    1 
ATOM   1107  C C     . THR A  1  144 ? 77.554  -1.208  -16.172 1.00 11.38 ? 144  THR A C     1 
ATOM   1108  O O     . THR A  1  144 ? 77.789  0.003   -16.228 1.00 12.44 ? 144  THR A O     1 
ATOM   1109  C CB    . THR A  1  144 ? 79.478  -2.753  -16.521 1.00 12.94 ? 144  THR A CB    1 
ATOM   1110  O OG1   . THR A  1  144 ? 80.360  -3.699  -15.900 1.00 14.28 ? 144  THR A OG1   1 
ATOM   1111  C CG2   . THR A  1  144 ? 80.316  -1.662  -17.185 1.00 12.14 ? 144  THR A CG2   1 
ATOM   1112  N N     . ILE A  1  145 ? 76.462  -1.755  -16.709 1.00 10.52 ? 145  ILE A N     1 
ATOM   1113  C CA    . ILE A  1  145 ? 75.507  -0.934  -17.460 1.00 10.06 ? 145  ILE A CA    1 
ATOM   1114  C C     . ILE A  1  145 ? 74.004  -1.115  -17.212 1.00 9.15  ? 145  ILE A C     1 
ATOM   1115  O O     . ILE A  1  145 ? 73.199  -0.665  -18.029 1.00 9.30  ? 145  ILE A O     1 
ATOM   1116  C CB    . ILE A  1  145 ? 75.724  -1.099  -18.988 1.00 9.00  ? 145  ILE A CB    1 
ATOM   1117  C CG1   . ILE A  1  145 ? 75.504  -2.562  -19.389 1.00 9.27  ? 145  ILE A CG1   1 
ATOM   1118  C CG2   . ILE A  1  145 ? 77.128  -0.647  -19.375 1.00 11.21 ? 145  ILE A CG2   1 
ATOM   1119  C CD1   . ILE A  1  145 ? 75.549  -2.806  -20.893 1.00 8.97  ? 145  ILE A CD1   1 
ATOM   1120  N N     . VAL A  1  146 ? 73.610  -1.746  -16.109 1.00 8.51  ? 146  VAL A N     1 
ATOM   1121  C CA    . VAL A  1  146 ? 72.183  -1.937  -15.840 1.00 9.00  ? 146  VAL A CA    1 
ATOM   1122  C C     . VAL A  1  146 ? 71.774  -1.242  -14.544 1.00 10.64 ? 146  VAL A C     1 
ATOM   1123  O O     . VAL A  1  146 ? 72.473  -1.334  -13.530 1.00 10.33 ? 146  VAL A O     1 
ATOM   1124  C CB    . VAL A  1  146 ? 71.825  -3.437  -15.773 1.00 9.28  ? 146  VAL A CB    1 
ATOM   1125  C CG1   . VAL A  1  146 ? 70.326  -3.611  -15.546 1.00 9.21  ? 146  VAL A CG1   1 
ATOM   1126  C CG2   . VAL A  1  146 ? 72.242  -4.118  -17.077 1.00 10.53 ? 146  VAL A CG2   1 
ATOM   1127  N N     . TYR A  1  147 ? 70.635  -0.554  -14.579 1.00 10.02 ? 147  TYR A N     1 
ATOM   1128  C CA    . TYR A  1  147 ? 70.167  0.203   -13.421 1.00 11.18 ? 147  TYR A CA    1 
ATOM   1129  C C     . TYR A  1  147 ? 68.735  -0.062  -13.000 1.00 12.22 ? 147  TYR A C     1 
ATOM   1130  O O     . TYR A  1  147 ? 67.893  -0.436  -13.814 1.00 12.68 ? 147  TYR A O     1 
ATOM   1131  C CB    . TYR A  1  147 ? 70.296  1.705   -13.705 1.00 11.50 ? 147  TYR A CB    1 
ATOM   1132  C CG    . TYR A  1  147 ? 71.620  2.076   -14.309 1.00 10.65 ? 147  TYR A CG    1 
ATOM   1133  C CD1   . TYR A  1  147 ? 71.896  1.800   -15.647 1.00 11.08 ? 147  TYR A CD1   1 
ATOM   1134  C CD2   . TYR A  1  147 ? 72.638  2.603   -13.519 1.00 10.59 ? 147  TYR A CD2   1 
ATOM   1135  C CE1   . TYR A  1  147 ? 73.154  2.023   -16.180 1.00 12.00 ? 147  TYR A CE1   1 
ATOM   1136  C CE2   . TYR A  1  147 ? 73.901  2.831   -14.043 1.00 11.09 ? 147  TYR A CE2   1 
ATOM   1137  C CZ    . TYR A  1  147 ? 74.154  2.535   -15.371 1.00 11.58 ? 147  TYR A CZ    1 
ATOM   1138  O OH    . TYR A  1  147 ? 75.418  2.713   -15.874 1.00 12.88 ? 147  TYR A OH    1 
ATOM   1139  N N     . LYS A  1  148 ? 68.474  0.138   -11.711 1.00 12.62 ? 148  LYS A N     1 
ATOM   1140  C CA    . LYS A  1  148 ? 67.131  0.006   -11.168 1.00 12.78 ? 148  LYS A CA    1 
ATOM   1141  C C     . LYS A  1  148 ? 66.554  1.376   -11.519 1.00 12.43 ? 148  LYS A C     1 
ATOM   1142  O O     . LYS A  1  148 ? 67.059  2.404   -11.070 1.00 13.02 ? 148  LYS A O     1 
ATOM   1143  C CB    . LYS A  1  148 ? 67.187  -0.182  -9.650  1.00 13.49 ? 148  LYS A CB    1 
ATOM   1144  C CG    . LYS A  1  148 ? 65.822  -0.314  -8.989  1.00 16.38 ? 148  LYS A CG    1 
ATOM   1145  C CD    . LYS A  1  148 ? 65.955  -0.347  -7.474  1.00 19.88 ? 148  LYS A CD    1 
ATOM   1146  C CE    . LYS A  1  148 ? 64.596  -0.404  -6.791  1.00 22.43 ? 148  LYS A CE    1 
ATOM   1147  N NZ    . LYS A  1  148 ? 63.868  -1.659  -7.103  1.00 25.93 ? 148  LYS A NZ    1 
ATOM   1148  N N     . PRO A  1  149 ? 65.491  1.412   -12.335 1.00 12.91 ? 149  PRO A N     1 
ATOM   1149  C CA    . PRO A  1  149 ? 64.861  2.667   -12.757 1.00 13.26 ? 149  PRO A CA    1 
ATOM   1150  C C     . PRO A  1  149 ? 64.151  3.519   -11.709 1.00 13.95 ? 149  PRO A C     1 
ATOM   1151  O O     . PRO A  1  149 ? 63.752  3.038   -10.648 1.00 14.04 ? 149  PRO A O     1 
ATOM   1152  C CB    . PRO A  1  149 ? 63.902  2.209   -13.848 1.00 12.66 ? 149  PRO A CB    1 
ATOM   1153  C CG    . PRO A  1  149 ? 63.447  0.891   -13.329 1.00 14.28 ? 149  PRO A CG    1 
ATOM   1154  C CD    . PRO A  1  149 ? 64.742  0.253   -12.857 1.00 12.87 ? 149  PRO A CD    1 
ATOM   1155  N N     . ASN A  1  150 ? 64.009  4.798   -12.039 1.00 16.62 ? 150  ASN A N     1 
ATOM   1156  C CA    . ASN A  1  150 ? 63.312  5.759   -11.194 1.00 17.35 ? 150  ASN A CA    1 
ATOM   1157  C C     . ASN A  1  150 ? 61.845  5.422   -11.364 1.00 16.50 ? 150  ASN A C     1 
ATOM   1158  O O     . ASN A  1  150 ? 61.460  4.812   -12.362 1.00 15.17 ? 150  ASN A O     1 
ATOM   1159  C CB    . ASN A  1  150 ? 63.503  7.185   -11.716 1.00 19.66 ? 150  ASN A CB    1 
ATOM   1160  C CG    . ASN A  1  150 ? 64.910  7.702   -11.537 1.00 21.16 ? 150  ASN A CG    1 
ATOM   1161  O OD1   . ASN A  1  150 ? 65.363  8.557   -12.300 1.00 24.08 ? 150  ASN A OD1   1 
ATOM   1162  N ND2   . ASN A  1  150 ? 65.602  7.212   -10.518 1.00 21.87 ? 150  ASN A ND2   1 
ATOM   1163  N N     . SER A  1  151 ? 61.019  5.817   -10.406 1.00 16.20 ? 151  SER A N     1 
ATOM   1164  C CA    . SER A  1  151 ? 59.595  5.577   -10.549 1.00 15.69 ? 151  SER A CA    1 
ATOM   1165  C C     . SER A  1  151 ? 59.150  6.612   -11.584 1.00 13.65 ? 151  SER A C     1 
ATOM   1166  O O     . SER A  1  151 ? 59.707  7.709   -11.650 1.00 13.20 ? 151  SER A O     1 
ATOM   1167  C CB    . SER A  1  151 ? 58.873  5.808   -9.219  1.00 16.99 ? 151  SER A CB    1 
ATOM   1168  O OG    . SER A  1  151 ? 59.000  7.152   -8.795  1.00 20.51 ? 151  SER A OG    1 
ATOM   1169  N N     . GLN A  1  152 ? 58.176  6.253   -12.413 1.00 12.43 ? 152  GLN A N     1 
ATOM   1170  C CA    . GLN A  1  152 ? 57.665  7.162   -13.434 1.00 10.94 ? 152  GLN A CA    1 
ATOM   1171  C C     . GLN A  1  152 ? 56.153  7.038   -13.462 1.00 11.76 ? 152  GLN A C     1 
ATOM   1172  O O     . GLN A  1  152 ? 55.619  5.934   -13.565 1.00 11.02 ? 152  GLN A O     1 
ATOM   1173  C CB    . GLN A  1  152 ? 58.222  6.802   -14.809 1.00 9.68  ? 152  GLN A CB    1 
ATOM   1174  C CG    . GLN A  1  152 ? 59.736  6.796   -14.898 1.00 11.43 ? 152  GLN A CG    1 
ATOM   1175  C CD    . GLN A  1  152 ? 60.212  6.302   -16.245 1.00 11.68 ? 152  GLN A CD    1 
ATOM   1176  O OE1   . GLN A  1  152 ? 60.464  7.087   -17.161 1.00 10.88 ? 152  GLN A OE1   1 
ATOM   1177  N NE2   . GLN A  1  152 ? 60.314  4.985   -16.382 1.00 12.44 ? 152  GLN A NE2   1 
ATOM   1178  N N     . SER A  1  153 ? 55.466  8.173   -13.390 1.00 12.00 ? 153  SER A N     1 
ATOM   1179  C CA    . SER A  1  153 ? 54.011  8.180   -13.375 1.00 11.22 ? 153  SER A CA    1 
ATOM   1180  C C     . SER A  1  153 ? 53.327  7.306   -14.420 1.00 10.14 ? 153  SER A C     1 
ATOM   1181  O O     . SER A  1  153 ? 52.504  6.457   -14.069 1.00 10.78 ? 153  SER A O     1 
ATOM   1182  C CB    . SER A  1  153 ? 53.483  9.607   -13.501 1.00 12.28 ? 153  SER A CB    1 
ATOM   1183  O OG    . SER A  1  153 ? 52.068  9.603   -13.470 1.00 12.96 ? 153  SER A OG    1 
ATOM   1184  N N     . TRP A  1  154 ? 53.646  7.496   -15.699 1.00 10.07 ? 154  TRP A N     1 
ATOM   1185  C CA    . TRP A  1  154 ? 52.979  6.689   -16.712 1.00 8.54  ? 154  TRP A CA    1 
ATOM   1186  C C     . TRP A  1  154 ? 53.283  5.201   -16.594 1.00 8.58  ? 154  TRP A C     1 
ATOM   1187  O O     . TRP A  1  154 ? 52.416  4.368   -16.858 1.00 8.44  ? 154  TRP A O     1 
ATOM   1188  C CB    . TRP A  1  154 ? 53.304  7.162   -18.127 1.00 9.25  ? 154  TRP A CB    1 
ATOM   1189  C CG    . TRP A  1  154 ? 52.506  6.392   -19.127 1.00 9.69  ? 154  TRP A CG    1 
ATOM   1190  C CD1   . TRP A  1  154 ? 52.962  5.425   -19.976 1.00 10.06 ? 154  TRP A CD1   1 
ATOM   1191  C CD2   . TRP A  1  154 ? 51.084  6.427   -19.285 1.00 10.57 ? 154  TRP A CD2   1 
ATOM   1192  N NE1   . TRP A  1  154 ? 51.909  4.849   -20.647 1.00 11.80 ? 154  TRP A NE1   1 
ATOM   1193  C CE2   . TRP A  1  154 ? 50.744  5.447   -20.241 1.00 10.42 ? 154  TRP A CE2   1 
ATOM   1194  C CE3   . TRP A  1  154 ? 50.061  7.192   -18.706 1.00 10.82 ? 154  TRP A CE3   1 
ATOM   1195  C CZ2   . TRP A  1  154 ? 49.422  5.209   -20.635 1.00 10.29 ? 154  TRP A CZ2   1 
ATOM   1196  C CZ3   . TRP A  1  154 ? 48.747  6.956   -19.096 1.00 11.73 ? 154  TRP A CZ3   1 
ATOM   1197  C CH2   . TRP A  1  154 ? 48.441  5.971   -20.053 1.00 12.52 ? 154  TRP A CH2   1 
ATOM   1198  N N     . GLN A  1  155 ? 54.506  4.858   -16.206 1.00 8.91  ? 155  GLN A N     1 
ATOM   1199  C CA    . GLN A  1  155 ? 54.841  3.448   -16.058 1.00 9.46  ? 155  GLN A CA    1 
ATOM   1200  C C     . GLN A  1  155 ? 54.050  2.870   -14.888 1.00 10.10 ? 155  GLN A C     1 
ATOM   1201  O O     . GLN A  1  155 ? 53.630  1.712   -14.924 1.00 9.55  ? 155  GLN A O     1 
ATOM   1202  C CB    . GLN A  1  155 ? 56.347  3.263   -15.841 1.00 8.37  ? 155  GLN A CB    1 
ATOM   1203  C CG    . GLN A  1  155 ? 57.191  3.612   -17.069 1.00 8.05  ? 155  GLN A CG    1 
ATOM   1204  C CD    . GLN A  1  155 ? 56.835  2.773   -18.286 1.00 8.76  ? 155  GLN A CD    1 
ATOM   1205  O OE1   . GLN A  1  155 ? 56.953  1.547   -18.264 1.00 8.81  ? 155  GLN A OE1   1 
ATOM   1206  N NE2   . GLN A  1  155 ? 56.398  3.431   -19.355 1.00 8.42  ? 155  GLN A NE2   1 
ATOM   1207  N N     . SER A  1  156 ? 53.835  3.680   -13.856 1.00 10.37 ? 156  SER A N     1 
ATOM   1208  C CA    . SER A  1  156 ? 53.068  3.230   -12.702 1.00 10.48 ? 156  SER A CA    1 
ATOM   1209  C C     . SER A  1  156 ? 51.608  3.033   -13.098 1.00 10.43 ? 156  SER A C     1 
ATOM   1210  O O     . SER A  1  156 ? 50.957  2.098   -12.636 1.00 10.54 ? 156  SER A O     1 
ATOM   1211  C CB    . SER A  1  156 ? 53.173  4.240   -11.556 1.00 10.64 ? 156  SER A CB    1 
ATOM   1212  O OG    . SER A  1  156 ? 54.488  4.265   -11.028 1.00 12.61 ? 156  SER A OG    1 
ATOM   1213  N N     . VAL A  1  157 ? 51.086  3.913   -13.949 1.00 9.24  ? 157  VAL A N     1 
ATOM   1214  C CA    . VAL A  1  157 ? 49.706  3.767   -14.399 1.00 10.49 ? 157  VAL A CA    1 
ATOM   1215  C C     . VAL A  1  157 ? 49.592  2.448   -15.155 1.00 9.55  ? 157  VAL A C     1 
ATOM   1216  O O     . VAL A  1  157 ? 48.645  1.687   -14.962 1.00 10.92 ? 157  VAL A O     1 
ATOM   1217  C CB    . VAL A  1  157 ? 49.282  4.923   -15.334 1.00 11.47 ? 157  VAL A CB    1 
ATOM   1218  C CG1   . VAL A  1  157 ? 47.930  4.619   -15.965 1.00 14.51 ? 157  VAL A CG1   1 
ATOM   1219  C CG2   . VAL A  1  157 ? 49.206  6.218   -14.545 1.00 12.42 ? 157  VAL A CG2   1 
ATOM   1220  N N     . THR A  1  158 ? 50.577  2.179   -16.009 1.00 8.94  ? 158  THR A N     1 
ATOM   1221  C CA    . THR A  1  158 ? 50.605  0.953   -16.796 1.00 8.12  ? 158  THR A CA    1 
ATOM   1222  C C     . THR A  1  158 ? 50.668  -0.267  -15.879 1.00 8.25  ? 158  THR A C     1 
ATOM   1223  O O     . THR A  1  158 ? 50.004  -1.275  -16.126 1.00 7.86  ? 158  THR A O     1 
ATOM   1224  C CB    . THR A  1  158 ? 51.815  0.957   -17.761 1.00 9.47  ? 158  THR A CB    1 
ATOM   1225  O OG1   . THR A  1  158 ? 51.705  2.081   -18.644 1.00 9.27  ? 158  THR A OG1   1 
ATOM   1226  C CG2   . THR A  1  158 ? 51.850  -0.317  -18.594 1.00 10.65 ? 158  THR A CG2   1 
ATOM   1227  N N     . LYS A  1  159 ? 51.464  -0.177  -14.819 1.00 8.11  ? 159  LYS A N     1 
ATOM   1228  C CA    . LYS A  1  159 ? 51.576  -1.280  -13.870 1.00 8.15  ? 159  LYS A CA    1 
ATOM   1229  C C     . LYS A  1  159 ? 50.212  -1.564  -13.235 1.00 8.03  ? 159  LYS A C     1 
ATOM   1230  O O     . LYS A  1  159 ? 49.827  -2.724  -13.075 1.00 7.48  ? 159  LYS A O     1 
ATOM   1231  C CB    . LYS A  1  159 ? 52.612  -0.940  -12.794 1.00 8.99  ? 159  LYS A CB    1 
ATOM   1232  C CG    . LYS A  1  159 ? 52.715  -1.938  -11.644 1.00 9.23  ? 159  LYS A CG    1 
ATOM   1233  C CD    . LYS A  1  159 ? 53.947  -1.639  -10.788 1.00 8.44  ? 159  LYS A CD    1 
ATOM   1234  C CE    . LYS A  1  159 ? 53.956  -2.450  -9.499  1.00 9.97  ? 159  LYS A CE    1 
ATOM   1235  N NZ    . LYS A  1  159 ? 55.236  -2.253  -8.754  1.00 10.24 ? 159  LYS A NZ    1 
ATOM   1236  N N     . THR A  1  160 ? 49.473  -0.512  -12.884 1.00 7.74  ? 160  THR A N     1 
ATOM   1237  C CA    . THR A  1  160 ? 48.158  -0.711  -12.274 1.00 8.12  ? 160  THR A CA    1 
ATOM   1238  C C     . THR A  1  160 ? 47.192  -1.340  -13.274 1.00 7.99  ? 160  THR A C     1 
ATOM   1239  O O     . THR A  1  160 ? 46.336  -2.145  -12.901 1.00 8.99  ? 160  THR A O     1 
ATOM   1240  C CB    . THR A  1  160 ? 47.540  0.619   -11.741 1.00 10.64 ? 160  THR A CB    1 
ATOM   1241  O OG1   . THR A  1  160 ? 47.250  1.504   -12.830 1.00 13.97 ? 160  THR A OG1   1 
ATOM   1242  C CG2   . THR A  1  160 ? 48.497  1.302   -10.783 1.00 10.21 ? 160  THR A CG2   1 
ATOM   1243  N N     . ALA A  1  161 ? 47.336  -0.982  -14.547 1.00 7.57  ? 161  ALA A N     1 
ATOM   1244  C CA    . ALA A  1  161 ? 46.467  -1.530  -15.580 1.00 7.63  ? 161  ALA A CA    1 
ATOM   1245  C C     . ALA A  1  161 ? 46.735  -3.025  -15.757 1.00 7.50  ? 161  ALA A C     1 
ATOM   1246  O O     . ALA A  1  161 ? 45.801  -3.818  -15.837 1.00 7.07  ? 161  ALA A O     1 
ATOM   1247  C CB    . ALA A  1  161 ? 46.685  -0.793  -16.895 1.00 8.87  ? 161  ALA A CB    1 
ATOM   1248  N N     . PHE A  1  162 ? 48.009  -3.407  -15.822 1.00 7.90  ? 162  PHE A N     1 
ATOM   1249  C CA    . PHE A  1  162 ? 48.370  -4.817  -15.976 1.00 7.38  ? 162  PHE A CA    1 
ATOM   1250  C C     . PHE A  1  162 ? 47.835  -5.652  -14.812 1.00 7.65  ? 162  PHE A C     1 
ATOM   1251  O O     . PHE A  1  162 ? 47.275  -6.730  -15.014 1.00 8.73  ? 162  PHE A O     1 
ATOM   1252  C CB    . PHE A  1  162 ? 49.895  -4.983  -16.055 1.00 7.47  ? 162  PHE A CB    1 
ATOM   1253  C CG    . PHE A  1  162 ? 50.473  -4.753  -17.430 1.00 7.86  ? 162  PHE A CG    1 
ATOM   1254  C CD1   . PHE A  1  162 ? 51.575  -3.922  -17.601 1.00 9.22  ? 162  PHE A CD1   1 
ATOM   1255  C CD2   . PHE A  1  162 ? 49.931  -5.384  -18.551 1.00 10.08 ? 162  PHE A CD2   1 
ATOM   1256  C CE1   . PHE A  1  162 ? 52.137  -3.717  -18.866 1.00 8.28  ? 162  PHE A CE1   1 
ATOM   1257  C CE2   . PHE A  1  162 ? 50.487  -5.185  -19.822 1.00 9.43  ? 162  PHE A CE2   1 
ATOM   1258  C CZ    . PHE A  1  162 ? 51.591  -4.351  -19.977 1.00 9.87  ? 162  PHE A CZ    1 
ATOM   1259  N N     . LEU A  1  163 ? 48.004  -5.154  -13.591 1.00 8.23  ? 163  LEU A N     1 
ATOM   1260  C CA    . LEU A  1  163 ? 47.534  -5.881  -12.415 1.00 7.65  ? 163  LEU A CA    1 
ATOM   1261  C C     . LEU A  1  163 ? 46.011  -5.990  -12.377 1.00 9.05  ? 163  LEU A C     1 
ATOM   1262  O O     . LEU A  1  163 ? 45.464  -7.019  -11.977 1.00 8.85  ? 163  LEU A O     1 
ATOM   1263  C CB    . LEU A  1  163 ? 48.073  -5.215  -11.140 1.00 9.15  ? 163  LEU A CB    1 
ATOM   1264  C CG    . LEU A  1  163 ? 49.600  -5.323  -11.012 1.00 8.44  ? 163  LEU A CG    1 
ATOM   1265  C CD1   . LEU A  1  163 ? 50.095  -4.480  -9.849  1.00 10.61 ? 163  LEU A CD1   1 
ATOM   1266  C CD2   . LEU A  1  163 ? 49.993  -6.786  -10.826 1.00 10.02 ? 163  LEU A CD2   1 
ATOM   1267  N N     . GLU A  1  164 ? 45.328  -4.936  -12.809 1.00 9.12  ? 164  GLU A N     1 
ATOM   1268  C CA    . GLU A  1  164 ? 43.876  -4.951  -12.839 1.00 8.92  ? 164  GLU A CA    1 
ATOM   1269  C C     . GLU A  1  164 ? 43.411  -5.938  -13.913 1.00 9.89  ? 164  GLU A C     1 
ATOM   1270  O O     . GLU A  1  164 ? 42.382  -6.600  -13.760 1.00 9.57  ? 164  GLU A O     1 
ATOM   1271  C CB    . GLU A  1  164 ? 43.342  -3.548  -13.148 1.00 11.14 ? 164  GLU A CB    1 
ATOM   1272  C CG    . GLU A  1  164 ? 41.955  -3.287  -12.598 1.00 14.09 ? 164  GLU A CG    1 
ATOM   1273  C CD    . GLU A  1  164 ? 41.417  -1.920  -12.972 1.00 10.64 ? 164  GLU A CD    1 
ATOM   1274  O OE1   . GLU A  1  164 ? 42.157  -0.924  -12.831 1.00 12.09 ? 164  GLU A OE1   1 
ATOM   1275  O OE2   . GLU A  1  164 ? 40.248  -1.845  -13.399 1.00 14.31 ? 164  GLU A OE2   1 
ATOM   1276  N N     . ALA A  1  165 ? 44.187  -6.046  -14.992 1.00 7.78  ? 165  ALA A N     1 
ATOM   1277  C CA    . ALA A  1  165 ? 43.848  -6.938  -16.098 1.00 8.65  ? 165  ALA A CA    1 
ATOM   1278  C C     . ALA A  1  165 ? 44.308  -8.388  -15.928 1.00 9.77  ? 165  ALA A C     1 
ATOM   1279  O O     . ALA A  1  165 ? 44.344  -9.151  -16.894 1.00 10.27 ? 165  ALA A O     1 
ATOM   1280  C CB    . ALA A  1  165 ? 44.386  -6.369  -17.406 1.00 6.59  ? 165  ALA A CB    1 
ATOM   1281  N N     . GLY A  1  166 ? 44.681  -8.760  -14.707 1.00 8.31  ? 166  GLY A N     1 
ATOM   1282  C CA    . GLY A  1  166 ? 45.081  -10.132 -14.445 1.00 8.55  ? 166  GLY A CA    1 
ATOM   1283  C C     . GLY A  1  166 ? 46.452  -10.624 -14.871 1.00 9.60  ? 166  GLY A C     1 
ATOM   1284  O O     . GLY A  1  166 ? 46.680  -11.835 -14.913 1.00 10.82 ? 166  GLY A O     1 
ATOM   1285  N N     . VAL A  1  167 ? 47.371  -9.723  -15.194 1.00 8.40  ? 167  VAL A N     1 
ATOM   1286  C CA    . VAL A  1  167 ? 48.707  -10.170 -15.577 1.00 8.68  ? 167  VAL A CA    1 
ATOM   1287  C C     . VAL A  1  167 ? 49.421  -10.368 -14.241 1.00 9.12  ? 167  VAL A C     1 
ATOM   1288  O O     . VAL A  1  167 ? 50.099  -9.476  -13.729 1.00 8.94  ? 167  VAL A O     1 
ATOM   1289  C CB    . VAL A  1  167 ? 49.420  -9.125  -16.448 1.00 9.81  ? 167  VAL A CB    1 
ATOM   1290  C CG1   . VAL A  1  167 ? 50.763  -9.674  -16.914 1.00 10.16 ? 167  VAL A CG1   1 
ATOM   1291  C CG2   . VAL A  1  167 ? 48.548  -8.787  -17.659 1.00 11.95 ? 167  VAL A CG2   1 
ATOM   1292  N N     . HIS A  1  168 ? 49.232  -11.562 -13.686 1.00 9.27  ? 168  HIS A N     1 
ATOM   1293  C CA    . HIS A  1  168 ? 49.760  -11.931 -12.379 1.00 10.17 ? 168  HIS A CA    1 
ATOM   1294  C C     . HIS A  1  168 ? 50.820  -13.028 -12.417 1.00 9.52  ? 168  HIS A C     1 
ATOM   1295  O O     . HIS A  1  168 ? 50.907  -13.793 -13.377 1.00 8.72  ? 168  HIS A O     1 
ATOM   1296  C CB    . HIS A  1  168 ? 48.586  -12.372 -11.501 1.00 9.35  ? 168  HIS A CB    1 
ATOM   1297  C CG    . HIS A  1  168 ? 47.533  -11.319 -11.334 1.00 9.90  ? 168  HIS A CG    1 
ATOM   1298  N ND1   . HIS A  1  168 ? 46.244  -11.607 -10.943 1.00 9.52  ? 168  HIS A ND1   1 
ATOM   1299  C CD2   . HIS A  1  168 ? 47.592  -9.973  -11.483 1.00 9.79  ? 168  HIS A CD2   1 
ATOM   1300  C CE1   . HIS A  1  168 ? 45.553  -10.483 -10.856 1.00 9.24  ? 168  HIS A CE1   1 
ATOM   1301  N NE2   . HIS A  1  168 ? 46.347  -9.478  -11.177 1.00 8.53  ? 168  HIS A NE2   1 
ATOM   1302  N N     . PRO A  1  169 ? 51.640  -13.121 -11.358 1.00 10.31 ? 169  PRO A N     1 
ATOM   1303  C CA    . PRO A  1  169 ? 51.623  -12.272 -10.160 1.00 10.13 ? 169  PRO A CA    1 
ATOM   1304  C C     . PRO A  1  169 ? 52.454  -11.005 -10.337 1.00 10.62 ? 169  PRO A C     1 
ATOM   1305  O O     . PRO A  1  169 ? 52.960  -10.729 -11.424 1.00 10.13 ? 169  PRO A O     1 
ATOM   1306  C CB    . PRO A  1  169 ? 52.223  -13.183 -9.100  1.00 10.71 ? 169  PRO A CB    1 
ATOM   1307  C CG    . PRO A  1  169 ? 53.285  -13.899 -9.887  1.00 9.96  ? 169  PRO A CG    1 
ATOM   1308  C CD    . PRO A  1  169 ? 52.555  -14.262 -11.172 1.00 9.93  ? 169  PRO A CD    1 
ATOM   1309  N N     . ASN A  1  170 ? 52.584  -10.236 -9.260  1.00 9.07  ? 170  ASN A N     1 
ATOM   1310  C CA    . ASN A  1  170 ? 53.397  -9.023  -9.276  1.00 9.41  ? 170  ASN A CA    1 
ATOM   1311  C C     . ASN A  1  170 ? 54.762  -9.438  -8.738  1.00 11.78 ? 170  ASN A C     1 
ATOM   1312  O O     . ASN A  1  170 ? 54.849  -10.057 -7.679  1.00 13.16 ? 170  ASN A O     1 
ATOM   1313  C CB    . ASN A  1  170 ? 52.783  -7.946  -8.376  1.00 8.94  ? 170  ASN A CB    1 
ATOM   1314  C CG    . ASN A  1  170 ? 53.668  -6.720  -8.240  1.00 9.69  ? 170  ASN A CG    1 
ATOM   1315  O OD1   . ASN A  1  170 ? 54.494  -6.433  -9.108  1.00 10.85 ? 170  ASN A OD1   1 
ATOM   1316  N ND2   . ASN A  1  170 ? 53.487  -5.980  -7.154  1.00 9.43  ? 170  ASN A ND2   1 
ATOM   1317  N N     . HIS A  1  171 ? 55.821  -9.113  -9.472  1.00 10.34 ? 171  HIS A N     1 
ATOM   1318  C CA    . HIS A  1  171 ? 57.175  -9.481  -9.060  1.00 10.23 ? 171  HIS A CA    1 
ATOM   1319  C C     . HIS A  1  171 ? 57.959  -8.326  -8.444  1.00 10.66 ? 171  HIS A C     1 
ATOM   1320  O O     . HIS A  1  171 ? 59.113  -8.505  -8.057  1.00 12.47 ? 171  HIS A O     1 
ATOM   1321  C CB    . HIS A  1  171 ? 57.958  -10.014 -10.264 1.00 9.65  ? 171  HIS A CB    1 
ATOM   1322  C CG    . HIS A  1  171 ? 57.399  -11.275 -10.842 1.00 10.15 ? 171  HIS A CG    1 
ATOM   1323  N ND1   . HIS A  1  171 ? 57.606  -12.512 -10.271 1.00 11.52 ? 171  HIS A ND1   1 
ATOM   1324  C CD2   . HIS A  1  171 ? 56.625  -11.488 -11.932 1.00 11.24 ? 171  HIS A CD2   1 
ATOM   1325  C CE1   . HIS A  1  171 ? 56.984  -13.433 -10.985 1.00 11.51 ? 171  HIS A CE1   1 
ATOM   1326  N NE2   . HIS A  1  171 ? 56.380  -12.837 -11.998 1.00 12.43 ? 171  HIS A NE2   1 
ATOM   1327  N N     . GLY A  1  172 ? 57.339  -7.152  -8.347  1.00 9.99  ? 172  GLY A N     1 
ATOM   1328  C CA    . GLY A  1  172 ? 58.035  -5.996  -7.804  1.00 10.34 ? 172  GLY A CA    1 
ATOM   1329  C C     . GLY A  1  172 ? 59.128  -5.619  -8.784  1.00 10.56 ? 172  GLY A C     1 
ATOM   1330  O O     . GLY A  1  172 ? 58.872  -5.552  -9.986  1.00 10.67 ? 172  GLY A O     1 
ATOM   1331  N N     . PHE A  1  173 ? 60.334  -5.348  -8.291  1.00 9.46  ? 173  PHE A N     1 
ATOM   1332  C CA    . PHE A  1  173 ? 61.449  -5.041  -9.184  1.00 10.70 ? 173  PHE A CA    1 
ATOM   1333  C C     . PHE A  1  173 ? 62.220  -6.338  -9.373  1.00 10.58 ? 173  PHE A C     1 
ATOM   1334  O O     . PHE A  1  173 ? 62.707  -6.923  -8.400  1.00 11.31 ? 173  PHE A O     1 
ATOM   1335  C CB    . PHE A  1  173 ? 62.399  -3.998  -8.592  1.00 10.91 ? 173  PHE A CB    1 
ATOM   1336  C CG    . PHE A  1  173 ? 63.678  -3.842  -9.379  1.00 10.31 ? 173  PHE A CG    1 
ATOM   1337  C CD1   . PHE A  1  173 ? 63.656  -3.323  -10.671 1.00 12.96 ? 173  PHE A CD1   1 
ATOM   1338  C CD2   . PHE A  1  173 ? 64.896  -4.253  -8.845  1.00 12.28 ? 173  PHE A CD2   1 
ATOM   1339  C CE1   . PHE A  1  173 ? 64.830  -3.217  -11.424 1.00 13.25 ? 173  PHE A CE1   1 
ATOM   1340  C CE2   . PHE A  1  173 ? 66.077  -4.153  -9.586  1.00 12.47 ? 173  PHE A CE2   1 
ATOM   1341  C CZ    . PHE A  1  173 ? 66.043  -3.633  -10.880 1.00 12.79 ? 173  PHE A CZ    1 
ATOM   1342  N N     . SER A  1  174 ? 62.337  -6.787  -10.617 1.00 8.75  ? 174  SER A N     1 
ATOM   1343  C CA    . SER A  1  174 ? 63.045  -8.029  -10.906 1.00 8.47  ? 174  SER A CA    1 
ATOM   1344  C C     . SER A  1  174 ? 63.542  -8.043  -12.343 1.00 9.29  ? 174  SER A C     1 
ATOM   1345  O O     . SER A  1  174 ? 62.850  -7.582  -13.249 1.00 10.75 ? 174  SER A O     1 
ATOM   1346  C CB    . SER A  1  174 ? 62.120  -9.226  -10.670 1.00 10.95 ? 174  SER A CB    1 
ATOM   1347  O OG    . SER A  1  174 ? 62.763  -10.444 -11.006 1.00 11.08 ? 174  SER A OG    1 
ATOM   1348  N N     . LEU A  1  175 ? 64.740  -8.584  -12.546 1.00 9.99  ? 175  LEU A N     1 
ATOM   1349  C CA    . LEU A  1  175 ? 65.342  -8.651  -13.875 1.00 9.54  ? 175  LEU A CA    1 
ATOM   1350  C C     . LEU A  1  175 ? 64.915  -9.878  -14.669 1.00 9.79  ? 175  LEU A C     1 
ATOM   1351  O O     . LEU A  1  175 ? 65.083  -9.926  -15.889 1.00 9.98  ? 175  LEU A O     1 
ATOM   1352  C CB    . LEU A  1  175 ? 66.866  -8.671  -13.755 1.00 9.72  ? 175  LEU A CB    1 
ATOM   1353  C CG    . LEU A  1  175 ? 67.515  -7.519  -12.993 1.00 10.27 ? 175  LEU A CG    1 
ATOM   1354  C CD1   . LEU A  1  175 ? 69.015  -7.735  -12.928 1.00 12.40 ? 175  LEU A CD1   1 
ATOM   1355  C CD2   . LEU A  1  175 ? 67.182  -6.210  -13.686 1.00 9.76  ? 175  LEU A CD2   1 
ATOM   1356  N N     . ASP A  1  176 ? 64.361  -10.864 -13.976 1.00 9.32  ? 176  ASP A N     1 
ATOM   1357  C CA    . ASP A  1  176 ? 63.965  -12.113 -14.611 1.00 8.94  ? 176  ASP A CA    1 
ATOM   1358  C C     . ASP A  1  176 ? 62.676  -12.142 -15.418 1.00 9.05  ? 176  ASP A C     1 
ATOM   1359  O O     . ASP A  1  176 ? 61.640  -11.621 -15.001 1.00 9.63  ? 176  ASP A O     1 
ATOM   1360  C CB    . ASP A  1  176 ? 63.920  -13.219 -13.562 1.00 9.95  ? 176  ASP A CB    1 
ATOM   1361  C CG    . ASP A  1  176 ? 65.291  -13.564 -13.033 1.00 11.61 ? 176  ASP A CG    1 
ATOM   1362  O OD1   . ASP A  1  176 ? 66.128  -14.036 -13.829 1.00 12.12 ? 176  ASP A OD1   1 
ATOM   1363  O OD2   . ASP A  1  176 ? 65.532  -13.360 -11.827 1.00 13.53 ? 176  ASP A OD2   1 
ATOM   1364  N N     . HIS A  1  177 ? 62.767  -12.782 -16.578 1.00 8.72  ? 177  HIS A N     1 
ATOM   1365  C CA    . HIS A  1  177 ? 61.638  -12.943 -17.481 1.00 8.95  ? 177  HIS A CA    1 
ATOM   1366  C C     . HIS A  1  177 ? 60.709  -14.009 -16.906 1.00 9.23  ? 177  HIS A C     1 
ATOM   1367  O O     . HIS A  1  177 ? 60.956  -15.208 -17.062 1.00 11.59 ? 177  HIS A O     1 
ATOM   1368  C CB    . HIS A  1  177 ? 62.130  -13.392 -18.857 1.00 8.26  ? 177  HIS A CB    1 
ATOM   1369  C CG    . HIS A  1  177 ? 61.029  -13.636 -19.838 1.00 7.59  ? 177  HIS A CG    1 
ATOM   1370  N ND1   . HIS A  1  177 ? 60.511  -12.640 -20.640 1.00 8.02  ? 177  HIS A ND1   1 
ATOM   1371  C CD2   . HIS A  1  177 ? 60.317  -14.753 -20.119 1.00 10.03 ? 177  HIS A CD2   1 
ATOM   1372  C CE1   . HIS A  1  177 ? 59.529  -13.135 -21.372 1.00 8.18  ? 177  HIS A CE1   1 
ATOM   1373  N NE2   . HIS A  1  177 ? 59.390  -14.415 -21.074 1.00 9.45  ? 177  HIS A NE2   1 
ATOM   1374  N N     . GLU A  1  178 ? 59.652  -13.570 -16.234 1.00 8.78  ? 178  GLU A N     1 
ATOM   1375  C CA    . GLU A  1  178 ? 58.685  -14.481 -15.637 1.00 9.67  ? 178  GLU A CA    1 
ATOM   1376  C C     . GLU A  1  178 ? 57.270  -13.993 -15.892 1.00 8.48  ? 178  GLU A C     1 
ATOM   1377  O O     . GLU A  1  178 ? 57.023  -12.790 -15.987 1.00 9.84  ? 178  GLU A O     1 
ATOM   1378  C CB    . GLU A  1  178 ? 58.885  -14.574 -14.127 1.00 12.25 ? 178  GLU A CB    1 
ATOM   1379  C CG    . GLU A  1  178 ? 60.259  -15.004 -13.671 1.00 14.51 ? 178  GLU A CG    1 
ATOM   1380  C CD    . GLU A  1  178 ? 60.319  -15.148 -12.163 1.00 16.76 ? 178  GLU A CD    1 
ATOM   1381  O OE1   . GLU A  1  178 ? 59.834  -16.176 -11.643 1.00 19.48 ? 178  GLU A OE1   1 
ATOM   1382  O OE2   . GLU A  1  178 ? 60.831  -14.223 -11.497 1.00 16.92 ? 178  GLU A OE2   1 
ATOM   1383  N N     . GLU A  1  179 ? 56.340  -14.935 -15.987 1.00 9.79  ? 179  GLU A N     1 
ATOM   1384  C CA    . GLU A  1  179 ? 54.939  -14.602 -16.200 1.00 9.72  ? 179  GLU A CA    1 
ATOM   1385  C C     . GLU A  1  179 ? 54.489  -13.649 -15.097 1.00 10.12 ? 179  GLU A C     1 
ATOM   1386  O O     . GLU A  1  179 ? 54.816  -13.848 -13.925 1.00 10.21 ? 179  GLU A O     1 
ATOM   1387  C CB    . GLU A  1  179 ? 54.095  -15.876 -16.164 1.00 12.44 ? 179  GLU A CB    1 
ATOM   1388  C CG    . GLU A  1  179 ? 52.611  -15.650 -16.380 1.00 17.58 ? 179  GLU A CG    1 
ATOM   1389  C CD    . GLU A  1  179 ? 51.834  -16.951 -16.405 1.00 20.98 ? 179  GLU A CD    1 
ATOM   1390  O OE1   . GLU A  1  179 ? 52.450  -18.011 -16.168 1.00 24.13 ? 179  GLU A OE1   1 
ATOM   1391  O OE2   . GLU A  1  179 ? 50.612  -16.914 -16.658 1.00 22.88 ? 179  GLU A OE2   1 
ATOM   1392  N N     . GLY A  1  180 ? 53.741  -12.615 -15.477 1.00 8.55  ? 180  GLY A N     1 
ATOM   1393  C CA    . GLY A  1  180 ? 53.263  -11.645 -14.509 1.00 8.70  ? 180  GLY A CA    1 
ATOM   1394  C C     . GLY A  1  180 ? 53.756  -10.239 -14.807 1.00 6.81  ? 180  GLY A C     1 
ATOM   1395  O O     . GLY A  1  180 ? 54.358  -9.988  -15.855 1.00 7.49  ? 180  GLY A O     1 
ATOM   1396  N N     . THR A  1  181 ? 53.505  -9.327  -13.875 1.00 6.31  ? 181  THR A N     1 
ATOM   1397  C CA    . THR A  1  181 ? 53.898  -7.929  -14.014 1.00 7.14  ? 181  THR A CA    1 
ATOM   1398  C C     . THR A  1  181 ? 55.088  -7.585  -13.129 1.00 7.94  ? 181  THR A C     1 
ATOM   1399  O O     . THR A  1  181 ? 55.175  -8.041  -11.992 1.00 8.17  ? 181  THR A O     1 
ATOM   1400  C CB    . THR A  1  181 ? 52.733  -7.004  -13.628 1.00 8.68  ? 181  THR A CB    1 
ATOM   1401  O OG1   . THR A  1  181 ? 51.615  -7.272  -14.481 1.00 7.88  ? 181  THR A OG1   1 
ATOM   1402  C CG2   . THR A  1  181 ? 53.134  -5.545  -13.757 1.00 8.87  ? 181  THR A CG2   1 
ATOM   1403  N N     . ARG A  1  182 ? 55.995  -6.766  -13.649 1.00 8.01  ? 182  ARG A N     1 
ATOM   1404  C CA    . ARG A  1  182 ? 57.166  -6.362  -12.882 1.00 6.71  ? 182  ARG A CA    1 
ATOM   1405  C C     . ARG A  1  182 ? 57.794  -5.101  -13.453 1.00 7.47  ? 182  ARG A C     1 
ATOM   1406  O O     . ARG A  1  182 ? 57.444  -4.654  -14.545 1.00 8.05  ? 182  ARG A O     1 
ATOM   1407  C CB    . ARG A  1  182 ? 58.227  -7.469  -12.900 1.00 6.21  ? 182  ARG A CB    1 
ATOM   1408  C CG    . ARG A  1  182 ? 59.082  -7.514  -14.178 1.00 8.88  ? 182  ARG A CG    1 
ATOM   1409  C CD    . ARG A  1  182 ? 60.058  -8.686  -14.135 1.00 6.35  ? 182  ARG A CD    1 
ATOM   1410  N NE    . ARG A  1  182 ? 61.099  -8.621  -15.161 1.00 6.91  ? 182  ARG A NE    1 
ATOM   1411  C CZ    . ARG A  1  182 ? 60.951  -9.009  -16.426 1.00 7.17  ? 182  ARG A CZ    1 
ATOM   1412  N NH1   . ARG A  1  182 ? 59.791  -9.496  -16.851 1.00 9.11  ? 182  ARG A NH1   1 
ATOM   1413  N NH2   . ARG A  1  182 ? 61.980  -8.931  -17.264 1.00 8.77  ? 182  ARG A NH2   1 
ATOM   1414  N N     . ILE A  1  183 ? 58.710  -4.527  -12.680 1.00 7.35  ? 183  ILE A N     1 
ATOM   1415  C CA    . ILE A  1  183 ? 59.484  -3.375  -13.115 1.00 8.30  ? 183  ILE A CA    1 
ATOM   1416  C C     . ILE A  1  183 ? 60.835  -4.041  -13.328 1.00 8.88  ? 183  ILE A C     1 
ATOM   1417  O O     . ILE A  1  183 ? 61.363  -4.679  -12.417 1.00 9.63  ? 183  ILE A O     1 
ATOM   1418  C CB    . ILE A  1  183 ? 59.621  -2.301  -12.016 1.00 9.91  ? 183  ILE A CB    1 
ATOM   1419  C CG1   . ILE A  1  183 ? 58.254  -1.676  -11.732 1.00 11.39 ? 183  ILE A CG1   1 
ATOM   1420  C CG2   . ILE A  1  183 ? 60.615  -1.222  -12.459 1.00 11.16 ? 183  ILE A CG2   1 
ATOM   1421  C CD1   . ILE A  1  183 ? 58.280  -0.621  -10.643 1.00 14.44 ? 183  ILE A CD1   1 
ATOM   1422  N N     . THR A  1  184 ? 61.381  -3.927  -14.532 1.00 8.98  ? 184  THR A N     1 
ATOM   1423  C CA    . THR A  1  184 ? 62.658  -4.559  -14.821 1.00 8.76  ? 184  THR A CA    1 
ATOM   1424  C C     . THR A  1  184 ? 63.784  -3.526  -14.874 1.00 8.26  ? 184  THR A C     1 
ATOM   1425  O O     . THR A  1  184 ? 63.567  -2.350  -14.587 1.00 9.52  ? 184  THR A O     1 
ATOM   1426  C CB    . THR A  1  184 ? 62.577  -5.354  -16.150 1.00 7.94  ? 184  THR A CB    1 
ATOM   1427  O OG1   . THR A  1  184 ? 63.675  -6.268  -16.226 1.00 10.39 ? 184  THR A OG1   1 
ATOM   1428  C CG2   . THR A  1  184 ? 62.613  -4.415  -17.354 1.00 9.43  ? 184  THR A CG2   1 
ATOM   1429  N N     . GLY A  1  185 ? 64.986  -3.967  -15.228 1.00 8.50  ? 185  GLY A N     1 
ATOM   1430  C CA    . GLY A  1  185 ? 66.106  -3.047  -15.299 1.00 8.74  ? 185  GLY A CA    1 
ATOM   1431  C C     . GLY A  1  185 ? 66.169  -2.297  -16.616 1.00 8.15  ? 185  GLY A C     1 
ATOM   1432  O O     . GLY A  1  185 ? 65.448  -2.620  -17.560 1.00 7.79  ? 185  GLY A O     1 
ATOM   1433  N N     . SER A  1  186 ? 67.026  -1.285  -16.682 1.00 8.87  ? 186  SER A N     1 
ATOM   1434  C CA    . SER A  1  186 ? 67.182  -0.502  -17.904 1.00 8.90  ? 186  SER A CA    1 
ATOM   1435  C C     . SER A  1  186 ? 68.644  -0.132  -18.101 1.00 8.32  ? 186  SER A C     1 
ATOM   1436  O O     . SER A  1  186 ? 69.396  -0.033  -17.130 1.00 7.14  ? 186  SER A O     1 
ATOM   1437  C CB    . SER A  1  186 ? 66.336  0.775   -17.822 1.00 9.68  ? 186  SER A CB    1 
ATOM   1438  O OG    . SER A  1  186 ? 66.559  1.621   -18.936 1.00 9.96  ? 186  SER A OG    1 
ATOM   1439  N N     . THR A  1  187 ? 69.057  0.047   -19.352 1.00 8.33  ? 187  THR A N     1 
ATOM   1440  C CA    . THR A  1  187 ? 70.429  0.444   -19.615 1.00 8.60  ? 187  THR A CA    1 
ATOM   1441  C C     . THR A  1  187 ? 70.533  1.972   -19.595 1.00 9.76  ? 187  THR A C     1 
ATOM   1442  O O     . THR A  1  187 ? 71.594  2.543   -19.847 1.00 8.99  ? 187  THR A O     1 
ATOM   1443  C CB    . THR A  1  187 ? 70.975  -0.158  -20.943 1.00 8.27  ? 187  THR A CB    1 
ATOM   1444  O OG1   . THR A  1  187 ? 69.976  -0.097  -21.968 1.00 7.65  ? 187  THR A OG1   1 
ATOM   1445  C CG2   . THR A  1  187 ? 71.384  -1.618  -20.724 1.00 8.54  ? 187  THR A CG2   1 
ATOM   1446  N N     . PHE A  1  188 ? 69.412  2.628   -19.307 1.00 9.06  ? 188  PHE A N     1 
ATOM   1447  C CA    . PHE A  1  188 ? 69.393  4.084   -19.156 1.00 8.94  ? 188  PHE A CA    1 
ATOM   1448  C C     . PHE A  1  188 ? 69.505  4.267   -17.642 1.00 10.20 ? 188  PHE A C     1 
ATOM   1449  O O     . PHE A  1  188 ? 68.793  3.590   -16.895 1.00 11.05 ? 188  PHE A O     1 
ATOM   1450  C CB    . PHE A  1  188 ? 68.056  4.691   -19.597 1.00 10.14 ? 188  PHE A CB    1 
ATOM   1451  C CG    . PHE A  1  188 ? 67.853  4.728   -21.082 1.00 8.19  ? 188  PHE A CG    1 
ATOM   1452  C CD1   . PHE A  1  188 ? 66.792  4.040   -21.663 1.00 9.24  ? 188  PHE A CD1   1 
ATOM   1453  C CD2   . PHE A  1  188 ? 68.703  5.470   -21.900 1.00 8.77  ? 188  PHE A CD2   1 
ATOM   1454  C CE1   . PHE A  1  188 ? 66.579  4.088   -23.041 1.00 9.56  ? 188  PHE A CE1   1 
ATOM   1455  C CE2   . PHE A  1  188 ? 68.500  5.523   -23.277 1.00 9.33  ? 188  PHE A CE2   1 
ATOM   1456  C CZ    . PHE A  1  188 ? 67.434  4.831   -23.849 1.00 8.82  ? 188  PHE A CZ    1 
ATOM   1457  N N     . ASP A  1  189 ? 70.382  5.151   -17.170 1.00 9.89  ? 189  ASP A N     1 
ATOM   1458  C CA    . ASP A  1  189 ? 70.472  5.337   -15.728 1.00 10.58 ? 189  ASP A CA    1 
ATOM   1459  C C     . ASP A  1  189 ? 69.458  6.365   -15.230 1.00 10.71 ? 189  ASP A C     1 
ATOM   1460  O O     . ASP A  1  189 ? 68.693  6.932   -16.014 1.00 11.37 ? 189  ASP A O     1 
ATOM   1461  C CB    . ASP A  1  189 ? 71.901  5.695   -15.269 1.00 11.24 ? 189  ASP A CB    1 
ATOM   1462  C CG    . ASP A  1  189 ? 72.361  7.067   -15.719 1.00 11.95 ? 189  ASP A CG    1 
ATOM   1463  O OD1   . ASP A  1  189 ? 71.520  7.958   -15.964 1.00 12.71 ? 189  ASP A OD1   1 
ATOM   1464  O OD2   . ASP A  1  189 ? 73.594  7.255   -15.800 1.00 11.12 ? 189  ASP A OD2   1 
ATOM   1465  N N     . ASN A  1  190 ? 69.459  6.605   -13.926 1.00 12.44 ? 190  ASN A N     1 
ATOM   1466  C CA    . ASN A  1  190 ? 68.499  7.512   -13.312 1.00 14.25 ? 190  ASN A CA    1 
ATOM   1467  C C     . ASN A  1  190 ? 68.545  8.979   -13.733 1.00 14.75 ? 190  ASN A C     1 
ATOM   1468  O O     . ASN A  1  190 ? 67.678  9.765   -13.344 1.00 15.39 ? 190  ASN A O     1 
ATOM   1469  C CB    . ASN A  1  190 ? 68.598  7.365   -11.796 1.00 16.36 ? 190  ASN A CB    1 
ATOM   1470  C CG    . ASN A  1  190 ? 68.533  5.911   -11.363 1.00 19.22 ? 190  ASN A CG    1 
ATOM   1471  O OD1   . ASN A  1  190 ? 69.450  5.134   -11.630 1.00 22.89 ? 190  ASN A OD1   1 
ATOM   1472  N ND2   . ASN A  1  190 ? 67.442  5.529   -10.714 1.00 22.06 ? 190  ASN A ND2   1 
ATOM   1473  N N     . LYS A  1  191 ? 69.540  9.347   -14.534 1.00 14.42 ? 191  LYS A N     1 
ATOM   1474  C CA    . LYS A  1  191 ? 69.645  10.717  -15.025 1.00 15.00 ? 191  LYS A CA    1 
ATOM   1475  C C     . LYS A  1  191 ? 69.312  10.734  -16.512 1.00 14.30 ? 191  LYS A C     1 
ATOM   1476  O O     . LYS A  1  191 ? 69.380  11.774  -17.165 1.00 16.02 ? 191  LYS A O     1 
ATOM   1477  C CB    . LYS A  1  191 ? 71.051  11.275  -14.793 1.00 16.90 ? 191  LYS A CB    1 
ATOM   1478  C CG    . LYS A  1  191 ? 71.369  11.516  -13.326 1.00 21.10 ? 191  LYS A CG    1 
ATOM   1479  C CD    . LYS A  1  191 ? 72.742  12.142  -13.140 1.00 23.69 ? 191  LYS A CD    1 
ATOM   1480  C CE    . LYS A  1  191 ? 73.060  12.319  -11.661 1.00 26.08 ? 191  LYS A CE    1 
ATOM   1481  N NZ    . LYS A  1  191 ? 74.398  12.937  -11.438 1.00 30.55 ? 191  LYS A NZ    1 
ATOM   1482  N N     . GLY A  1  192 ? 68.950  9.569   -17.040 1.00 13.50 ? 192  GLY A N     1 
ATOM   1483  C CA    . GLY A  1  192 ? 68.604  9.470   -18.446 1.00 11.90 ? 192  GLY A CA    1 
ATOM   1484  C C     . GLY A  1  192 ? 69.782  9.211   -19.364 1.00 11.29 ? 192  GLY A C     1 
ATOM   1485  O O     . GLY A  1  192 ? 69.632  9.206   -20.585 1.00 12.06 ? 192  GLY A O     1 
ATOM   1486  N N     . THR A  1  193 ? 70.959  8.998   -18.786 1.00 11.43 ? 193  THR A N     1 
ATOM   1487  C CA    . THR A  1  193 ? 72.151  8.735   -19.585 1.00 10.30 ? 193  THR A CA    1 
ATOM   1488  C C     . THR A  1  193 ? 72.131  7.303   -20.101 1.00 10.61 ? 193  THR A C     1 
ATOM   1489  O O     . THR A  1  193 ? 71.921  6.369   -19.333 1.00 10.33 ? 193  THR A O     1 
ATOM   1490  C CB    . THR A  1  193 ? 73.429  8.927   -18.755 1.00 11.33 ? 193  THR A CB    1 
ATOM   1491  O OG1   . THR A  1  193 ? 73.504  10.287  -18.309 1.00 14.93 ? 193  THR A OG1   1 
ATOM   1492  C CG2   . THR A  1  193 ? 74.661  8.598   -19.588 1.00 10.73 ? 193  THR A CG2   1 
ATOM   1493  N N     . ARG A  1  194 ? 72.347  7.128   -21.401 1.00 10.22 ? 194  ARG A N     1 
ATOM   1494  C CA    . ARG A  1  194 ? 72.359  5.785   -21.959 1.00 9.94  ? 194  ARG A CA    1 
ATOM   1495  C C     . ARG A  1  194 ? 73.705  5.112   -21.763 1.00 10.35 ? 194  ARG A C     1 
ATOM   1496  O O     . ARG A  1  194 ? 74.757  5.704   -22.003 1.00 12.13 ? 194  ARG A O     1 
ATOM   1497  C CB    . ARG A  1  194 ? 72.054  5.781   -23.460 1.00 10.63 ? 194  ARG A CB    1 
ATOM   1498  C CG    . ARG A  1  194 ? 71.981  4.353   -24.018 1.00 9.61  ? 194  ARG A CG    1 
ATOM   1499  C CD    . ARG A  1  194 ? 72.113  4.304   -25.528 1.00 9.31  ? 194  ARG A CD    1 
ATOM   1500  N NE    . ARG A  1  194 ? 70.937  4.799   -26.237 1.00 8.96  ? 194  ARG A NE    1 
ATOM   1501  C CZ    . ARG A  1  194 ? 69.809  4.113   -26.390 1.00 7.71  ? 194  ARG A CZ    1 
ATOM   1502  N NH1   . ARG A  1  194 ? 69.694  2.896   -25.872 1.00 8.86  ? 194  ARG A NH1   1 
ATOM   1503  N NH2   . ARG A  1  194 ? 68.807  4.629   -27.088 1.00 9.15  ? 194  ARG A NH2   1 
ATOM   1504  N N     . HIS A  1  195 ? 73.656  3.867   -21.314 1.00 9.74  ? 195  HIS A N     1 
ATOM   1505  C CA    . HIS A  1  195 ? 74.849  3.065   -21.136 1.00 8.68  ? 195  HIS A CA    1 
ATOM   1506  C C     . HIS A  1  195 ? 74.638  1.920   -22.117 1.00 9.83  ? 195  HIS A C     1 
ATOM   1507  O O     . HIS A  1  195 ? 73.501  1.529   -22.382 1.00 9.93  ? 195  HIS A O     1 
ATOM   1508  C CB    . HIS A  1  195 ? 74.956  2.604   -19.683 1.00 9.83  ? 195  HIS A CB    1 
ATOM   1509  C CG    . HIS A  1  195 ? 75.239  3.728   -18.733 1.00 11.05 ? 195  HIS A CG    1 
ATOM   1510  N ND1   . HIS A  1  195 ? 76.514  4.201   -18.498 1.00 10.19 ? 195  HIS A ND1   1 
ATOM   1511  C CD2   . HIS A  1  195 ? 74.408  4.524   -18.021 1.00 10.97 ? 195  HIS A CD2   1 
ATOM   1512  C CE1   . HIS A  1  195 ? 76.453  5.238   -17.682 1.00 13.04 ? 195  HIS A CE1   1 
ATOM   1513  N NE2   . HIS A  1  195 ? 75.186  5.455   -17.377 1.00 10.79 ? 195  HIS A NE2   1 
ATOM   1514  N N     . ALA A  1  196 ? 75.717  1.407   -22.690 1.00 9.39  ? 196  ALA A N     1 
ATOM   1515  C CA    . ALA A  1  196 ? 75.569  0.355   -23.685 1.00 9.71  ? 196  ALA A CA    1 
ATOM   1516  C C     . ALA A  1  196 ? 76.752  -0.587  -23.771 1.00 8.46  ? 196  ALA A C     1 
ATOM   1517  O O     . ALA A  1  196 ? 77.698  -0.495  -22.989 1.00 7.57  ? 196  ALA A O     1 
ATOM   1518  C CB    . ALA A  1  196 ? 75.308  0.982   -25.050 1.00 8.44  ? 196  ALA A CB    1 
ATOM   1519  N N     . ALA A  1  197 ? 76.693  -1.484  -24.750 1.00 7.37  ? 197  ALA A N     1 
ATOM   1520  C CA    . ALA A  1  197 ? 77.737  -2.479  -24.949 1.00 8.01  ? 197  ALA A CA    1 
ATOM   1521  C C     . ALA A  1  197 ? 79.146  -1.917  -25.132 1.00 7.49  ? 197  ALA A C     1 
ATOM   1522  O O     . ALA A  1  197 ? 80.121  -2.570  -24.758 1.00 9.04  ? 197  ALA A O     1 
ATOM   1523  C CB    . ALA A  1  197 ? 77.378  -3.373  -26.134 1.00 8.42  ? 197  ALA A CB    1 
ATOM   1524  N N     . ASP A  1  198 ? 79.267  -0.720  -25.700 1.00 8.75  ? 198  ASP A N     1 
ATOM   1525  C CA    . ASP A  1  198 ? 80.587  -0.140  -25.904 1.00 8.81  ? 198  ASP A CA    1 
ATOM   1526  C C     . ASP A  1  198 ? 81.338  0.024   -24.589 1.00 8.92  ? 198  ASP A C     1 
ATOM   1527  O O     . ASP A  1  198 ? 82.555  -0.138  -24.540 1.00 8.88  ? 198  ASP A O     1 
ATOM   1528  C CB    . ASP A  1  198 ? 80.484  1.207   -26.639 1.00 9.38  ? 198  ASP A CB    1 
ATOM   1529  C CG    . ASP A  1  198 ? 79.728  2.261   -25.849 1.00 10.33 ? 198  ASP A CG    1 
ATOM   1530  O OD1   . ASP A  1  198 ? 78.611  1.972   -25.374 1.00 11.10 ? 198  ASP A OD1   1 
ATOM   1531  O OD2   . ASP A  1  198 ? 80.247  3.393   -25.722 1.00 10.15 ? 198  ASP A OD2   1 
ATOM   1532  N N     . GLU A  1  199 ? 80.614  0.322   -23.516 1.00 9.67  ? 199  GLU A N     1 
ATOM   1533  C CA    . GLU A  1  199 ? 81.251  0.502   -22.219 1.00 9.43  ? 199  GLU A CA    1 
ATOM   1534  C C     . GLU A  1  199 ? 81.836  -0.785  -21.660 1.00 10.24 ? 199  GLU A C     1 
ATOM   1535  O O     . GLU A  1  199 ? 82.684  -0.747  -20.772 1.00 11.68 ? 199  GLU A O     1 
ATOM   1536  C CB    . GLU A  1  199 ? 80.260  1.086   -21.219 1.00 9.84  ? 199  GLU A CB    1 
ATOM   1537  C CG    . GLU A  1  199 ? 79.995  2.560   -21.430 1.00 9.35  ? 199  GLU A CG    1 
ATOM   1538  C CD    . GLU A  1  199 ? 78.835  3.045   -20.606 1.00 11.89 ? 199  GLU A CD    1 
ATOM   1539  O OE1   . GLU A  1  199 ? 77.685  2.736   -20.977 1.00 12.63 ? 199  GLU A OE1   1 
ATOM   1540  O OE2   . GLU A  1  199 ? 79.070  3.721   -19.583 1.00 11.54 ? 199  GLU A OE2   1 
ATOM   1541  N N     . LEU A  1  200 ? 81.382  -1.926  -22.167 1.00 9.64  ? 200  LEU A N     1 
ATOM   1542  C CA    . LEU A  1  200 ? 81.911  -3.193  -21.687 1.00 9.52  ? 200  LEU A CA    1 
ATOM   1543  C C     . LEU A  1  200 ? 83.342  -3.371  -22.208 1.00 10.67 ? 200  LEU A C     1 
ATOM   1544  O O     . LEU A  1  200 ? 84.092  -4.224  -21.728 1.00 9.79  ? 200  LEU A O     1 
ATOM   1545  C CB    . LEU A  1  200 ? 80.997  -4.351  -22.117 1.00 10.46 ? 200  LEU A CB    1 
ATOM   1546  C CG    . LEU A  1  200 ? 79.593  -4.286  -21.486 1.00 10.12 ? 200  LEU A CG    1 
ATOM   1547  C CD1   . LEU A  1  200 ? 78.723  -5.423  -22.011 1.00 11.02 ? 200  LEU A CD1   1 
ATOM   1548  C CD2   . LEU A  1  200 ? 79.703  -4.363  -19.967 1.00 10.43 ? 200  LEU A CD2   1 
ATOM   1549  N N     . LEU A  1  201 ? 83.723  -2.543  -23.178 1.00 9.80  ? 201  LEU A N     1 
ATOM   1550  C CA    . LEU A  1  201 ? 85.078  -2.583  -23.729 1.00 10.43 ? 201  LEU A CA    1 
ATOM   1551  C C     . LEU A  1  201 ? 86.053  -2.124  -22.643 1.00 11.72 ? 201  LEU A C     1 
ATOM   1552  O O     . LEU A  1  201 ? 87.227  -2.493  -22.651 1.00 11.91 ? 201  LEU A O     1 
ATOM   1553  C CB    . LEU A  1  201 ? 85.197  -1.655  -24.944 1.00 9.87  ? 201  LEU A CB    1 
ATOM   1554  C CG    . LEU A  1  201 ? 84.409  -2.025  -26.207 1.00 10.15 ? 201  LEU A CG    1 
ATOM   1555  C CD1   . LEU A  1  201 ? 84.487  -0.882  -27.210 1.00 10.16 ? 201  LEU A CD1   1 
ATOM   1556  C CD2   . LEU A  1  201 ? 84.967  -3.309  -26.815 1.00 9.26  ? 201  LEU A CD2   1 
ATOM   1557  N N     . ASN A  1  202 ? 85.555  -1.320  -21.706 1.00 11.47 ? 202  ASN A N     1 
ATOM   1558  C CA    . ASN A  1  202 ? 86.379  -0.807  -20.610 1.00 11.90 ? 202  ASN A CA    1 
ATOM   1559  C C     . ASN A  1  202 ? 86.814  -1.910  -19.658 1.00 13.40 ? 202  ASN A C     1 
ATOM   1560  O O     . ASN A  1  202 ? 87.726  -1.721  -18.852 1.00 13.29 ? 202  ASN A O     1 
ATOM   1561  C CB    . ASN A  1  202 ? 85.618  0.264   -19.820 1.00 11.84 ? 202  ASN A CB    1 
ATOM   1562  C CG    . ASN A  1  202 ? 85.367  1.515   -20.632 1.00 11.69 ? 202  ASN A CG    1 
ATOM   1563  O OD1   . ASN A  1  202 ? 86.285  2.066   -21.239 1.00 13.33 ? 202  ASN A OD1   1 
ATOM   1564  N ND2   . ASN A  1  202 ? 84.121  1.979   -20.641 1.00 11.45 ? 202  ASN A ND2   1 
ATOM   1565  N N     . LYS A  1  203 ? 86.154  -3.059  -19.754 1.00 12.97 ? 203  LYS A N     1 
ATOM   1566  C CA    . LYS A  1  203 ? 86.464  -4.205  -18.907 1.00 14.61 ? 203  LYS A CA    1 
ATOM   1567  C C     . LYS A  1  203 ? 87.612  -5.009  -19.510 1.00 13.25 ? 203  LYS A C     1 
ATOM   1568  O O     . LYS A  1  203 ? 88.130  -5.931  -18.883 1.00 15.12 ? 203  LYS A O     1 
ATOM   1569  C CB    . LYS A  1  203 ? 85.230  -5.098  -18.766 1.00 15.81 ? 203  LYS A CB    1 
ATOM   1570  C CG    . LYS A  1  203 ? 83.996  -4.379  -18.236 1.00 19.69 ? 203  LYS A CG    1 
ATOM   1571  C CD    . LYS A  1  203 ? 84.063  -4.159  -16.733 1.00 21.39 ? 203  LYS A CD    1 
ATOM   1572  C CE    . LYS A  1  203 ? 83.908  -5.469  -15.973 1.00 21.77 ? 203  LYS A CE    1 
ATOM   1573  N NZ    . LYS A  1  203 ? 83.905  -5.260  -14.497 1.00 22.21 ? 203  LYS A NZ    1 
ATOM   1574  N N     . GLY A  1  204 ? 87.999  -4.658  -20.733 1.00 13.28 ? 204  GLY A N     1 
ATOM   1575  C CA    . GLY A  1  204 ? 89.086  -5.356  -21.396 1.00 12.28 ? 204  GLY A CA    1 
ATOM   1576  C C     . GLY A  1  204 ? 90.433  -4.796  -20.983 1.00 13.08 ? 204  GLY A C     1 
ATOM   1577  O O     . GLY A  1  204 ? 90.498  -3.823  -20.231 1.00 14.24 ? 204  GLY A O     1 
ATOM   1578  N N     . ASN A  1  205 ? 91.506  -5.410  -21.473 1.00 13.04 ? 205  ASN A N     1 
ATOM   1579  C CA    . ASN A  1  205 ? 92.863  -4.966  -21.157 1.00 13.44 ? 205  ASN A CA    1 
ATOM   1580  C C     . ASN A  1  205 ? 93.277  -3.925  -22.195 1.00 13.65 ? 205  ASN A C     1 
ATOM   1581  O O     . ASN A  1  205 ? 93.352  -4.223  -23.388 1.00 13.16 ? 205  ASN A O     1 
ATOM   1582  C CB    . ASN A  1  205 ? 93.824  -6.158  -21.189 1.00 14.17 ? 205  ASN A CB    1 
ATOM   1583  C CG    . ASN A  1  205 ? 95.219  -5.796  -20.719 1.00 15.67 ? 205  ASN A CG    1 
ATOM   1584  O OD1   . ASN A  1  205 ? 95.824  -4.848  -21.215 1.00 16.36 ? 205  ASN A OD1   1 
ATOM   1585  N ND2   . ASN A  1  205 ? 95.739  -6.555  -19.760 1.00 17.71 ? 205  ASN A ND2   1 
ATOM   1586  N N     . SER A  1  206 ? 93.548  -2.708  -21.735 1.00 12.79 ? 206  SER A N     1 
ATOM   1587  C CA    . SER A  1  206 ? 93.915  -1.608  -22.621 1.00 14.45 ? 206  SER A CA    1 
ATOM   1588  C C     . SER A  1  206 ? 95.222  -1.775  -23.392 1.00 13.89 ? 206  SER A C     1 
ATOM   1589  O O     . SER A  1  206 ? 95.533  -0.961  -24.259 1.00 13.85 ? 206  SER A O     1 
ATOM   1590  C CB    . SER A  1  206 ? 93.951  -0.293  -21.836 1.00 16.46 ? 206  SER A CB    1 
ATOM   1591  O OG    . SER A  1  206 ? 94.934  -0.325  -20.818 1.00 19.66 ? 206  SER A OG    1 
ATOM   1592  N N     . ASN A  1  207 ? 95.987  -2.818  -23.079 1.00 12.03 ? 207  ASN A N     1 
ATOM   1593  C CA    . ASN A  1  207 ? 97.243  -3.064  -23.779 1.00 11.89 ? 207  ASN A CA    1 
ATOM   1594  C C     . ASN A  1  207 ? 97.075  -4.195  -24.792 1.00 10.37 ? 207  ASN A C     1 
ATOM   1595  O O     . ASN A  1  207 ? 97.957  -4.428  -25.619 1.00 11.72 ? 207  ASN A O     1 
ATOM   1596  C CB    . ASN A  1  207 ? 98.349  -3.440  -22.788 1.00 11.80 ? 207  ASN A CB    1 
ATOM   1597  C CG    . ASN A  1  207 ? 99.722  -3.505  -23.440 1.00 14.12 ? 207  ASN A CG    1 
ATOM   1598  O OD1   . ASN A  1  207 ? 100.445 -4.492  -23.299 1.00 15.77 ? 207  ASN A OD1   1 
ATOM   1599  N ND2   . ASN A  1  207 ? 100.090 -2.444  -24.149 1.00 12.60 ? 207  ASN A ND2   1 
ATOM   1600  N N     . ASN A  1  208 ? 95.941  -4.890  -24.731 1.00 11.47 ? 208  ASN A N     1 
ATOM   1601  C CA    . ASN A  1  208 ? 95.677  -6.009  -25.639 1.00 10.43 ? 208  ASN A CA    1 
ATOM   1602  C C     . ASN A  1  208 ? 94.509  -5.795  -26.595 1.00 10.81 ? 208  ASN A C     1 
ATOM   1603  O O     . ASN A  1  208 ? 94.403  -6.488  -27.603 1.00 11.11 ? 208  ASN A O     1 
ATOM   1604  C CB    . ASN A  1  208 ? 95.399  -7.295  -24.851 1.00 10.50 ? 208  ASN A CB    1 
ATOM   1605  C CG    . ASN A  1  208 ? 96.544  -7.687  -23.940 1.00 11.68 ? 208  ASN A CG    1 
ATOM   1606  O OD1   . ASN A  1  208 ? 97.692  -7.300  -24.158 1.00 12.84 ? 208  ASN A OD1   1 
ATOM   1607  N ND2   . ASN A  1  208 ? 96.238  -8.477  -22.920 1.00 11.80 ? 208  ASN A ND2   1 
ATOM   1608  N N     . LEU A  1  209 ? 93.637  -4.842  -26.281 1.00 10.02 ? 209  LEU A N     1 
ATOM   1609  C CA    . LEU A  1  209 ? 92.460  -4.588  -27.107 1.00 10.29 ? 209  LEU A CA    1 
ATOM   1610  C C     . LEU A  1  209 ? 92.576  -3.348  -27.984 1.00 11.64 ? 209  LEU A C     1 
ATOM   1611  O O     . LEU A  1  209 ? 92.953  -2.277  -27.514 1.00 12.15 ? 209  LEU A O     1 
ATOM   1612  C CB    . LEU A  1  209 ? 91.221  -4.467  -26.206 1.00 9.77  ? 209  LEU A CB    1 
ATOM   1613  C CG    . LEU A  1  209 ? 89.844  -4.214  -26.832 1.00 9.41  ? 209  LEU A CG    1 
ATOM   1614  C CD1   . LEU A  1  209 ? 89.481  -5.343  -27.793 1.00 11.02 ? 209  LEU A CD1   1 
ATOM   1615  C CD2   . LEU A  1  209 ? 88.804  -4.111  -25.719 1.00 12.05 ? 209  LEU A CD2   1 
ATOM   1616  N N     . ARG A  1  210 ? 92.255  -3.512  -29.264 1.00 11.60 ? 210  ARG A N     1 
ATOM   1617  C CA    . ARG A  1  210 ? 92.277  -2.413  -30.220 1.00 11.42 ? 210  ARG A CA    1 
ATOM   1618  C C     . ARG A  1  210 ? 90.942  -2.432  -30.948 1.00 12.35 ? 210  ARG A C     1 
ATOM   1619  O O     . ARG A  1  210 ? 90.460  -3.491  -31.358 1.00 11.71 ? 210  ARG A O     1 
ATOM   1620  C CB    . ARG A  1  210 ? 93.428  -2.570  -31.221 1.00 13.48 ? 210  ARG A CB    1 
ATOM   1621  C CG    . ARG A  1  210 ? 94.810  -2.346  -30.617 1.00 15.05 ? 210  ARG A CG    1 
ATOM   1622  C CD    . ARG A  1  210 ? 95.920  -2.699  -31.601 1.00 18.30 ? 210  ARG A CD    1 
ATOM   1623  N NE    A ARG A  1  210 ? 96.003  -1.777  -32.731 0.50 20.25 ? 210  ARG A NE    1 
ATOM   1624  N NE    B ARG A  1  210 ? 97.070  -1.802  -31.518 0.50 21.57 ? 210  ARG A NE    1 
ATOM   1625  C CZ    A ARG A  1  210 ? 96.531  -0.559  -32.667 0.50 21.15 ? 210  ARG A CZ    1 
ATOM   1626  C CZ    B ARG A  1  210 ? 97.819  -1.643  -30.432 0.50 22.74 ? 210  ARG A CZ    1 
ATOM   1627  N NH1   A ARG A  1  210 ? 97.032  -0.107  -31.524 0.50 21.66 ? 210  ARG A NH1   1 
ATOM   1628  N NH1   B ARG A  1  210 ? 97.546  -2.324  -29.326 0.50 23.37 ? 210  ARG A NH1   1 
ATOM   1629  N NH2   A ARG A  1  210 ? 96.558  0.210   -33.747 0.50 21.28 ? 210  ARG A NH2   1 
ATOM   1630  N NH2   B ARG A  1  210 ? 98.843  -0.800  -30.450 0.50 23.14 ? 210  ARG A NH2   1 
ATOM   1631  N N     . VAL A  1  211 ? 90.337  -1.258  -31.084 1.00 11.09 ? 211  VAL A N     1 
ATOM   1632  C CA    . VAL A  1  211 ? 89.050  -1.133  -31.752 1.00 10.89 ? 211  VAL A CA    1 
ATOM   1633  C C     . VAL A  1  211 ? 89.172  -0.239  -32.974 1.00 11.61 ? 211  VAL A C     1 
ATOM   1634  O O     . VAL A  1  211 ? 89.740  0.853   -32.907 1.00 12.04 ? 211  VAL A O     1 
ATOM   1635  C CB    . VAL A  1  211 ? 87.981  -0.524  -30.812 1.00 11.35 ? 211  VAL A CB    1 
ATOM   1636  C CG1   . VAL A  1  211 ? 86.678  -0.320  -31.571 1.00 12.17 ? 211  VAL A CG1   1 
ATOM   1637  C CG2   . VAL A  1  211 ? 87.766  -1.426  -29.605 1.00 10.56 ? 211  VAL A CG2   1 
ATOM   1638  N N     . GLY A  1  212 ? 88.644  -0.712  -34.095 1.00 10.40 ? 212  GLY A N     1 
ATOM   1639  C CA    . GLY A  1  212 ? 88.684  0.081   -35.303 1.00 11.10 ? 212  GLY A CA    1 
ATOM   1640  C C     . GLY A  1  212 ? 87.271  0.472   -35.683 1.00 10.84 ? 212  GLY A C     1 
ATOM   1641  O O     . GLY A  1  212 ? 86.381  -0.380  -35.726 1.00 12.29 ? 212  GLY A O     1 
ATOM   1642  N N     . VAL A  1  213 ? 87.045  1.758   -35.923 1.00 9.67  ? 213  VAL A N     1 
ATOM   1643  C CA    . VAL A  1  213 ? 85.722  2.213   -36.331 1.00 8.94  ? 213  VAL A CA    1 
ATOM   1644  C C     . VAL A  1  213 ? 85.785  2.636   -37.794 1.00 9.17  ? 213  VAL A C     1 
ATOM   1645  O O     . VAL A  1  213 ? 86.872  2.829   -38.345 1.00 9.13  ? 213  VAL A O     1 
ATOM   1646  C CB    . VAL A  1  213 ? 85.206  3.381   -35.452 1.00 10.50 ? 213  VAL A CB    1 
ATOM   1647  C CG1   . VAL A  1  213 ? 84.942  2.879   -34.038 1.00 9.67  ? 213  VAL A CG1   1 
ATOM   1648  C CG2   . VAL A  1  213 ? 86.215  4.520   -35.432 1.00 10.91 ? 213  VAL A CG2   1 
ATOM   1649  N N     . HIS A  1  214 ? 84.623  2.767   -38.426 1.00 9.81  ? 214  HIS A N     1 
ATOM   1650  C CA    . HIS A  1  214 ? 84.563  3.124   -39.840 1.00 10.84 ? 214  HIS A CA    1 
ATOM   1651  C C     . HIS A  1  214 ? 85.340  2.057   -40.607 1.00 10.43 ? 214  HIS A C     1 
ATOM   1652  O O     . HIS A  1  214 ? 86.044  2.350   -41.575 1.00 9.78  ? 214  HIS A O     1 
ATOM   1653  C CB    . HIS A  1  214 ? 85.187  4.504   -40.069 1.00 12.41 ? 214  HIS A CB    1 
ATOM   1654  C CG    . HIS A  1  214 ? 84.437  5.618   -39.410 1.00 13.78 ? 214  HIS A CG    1 
ATOM   1655  N ND1   . HIS A  1  214 ? 85.053  6.771   -38.969 1.00 17.01 ? 214  HIS A ND1   1 
ATOM   1656  C CD2   . HIS A  1  214 ? 83.122  5.763   -39.125 1.00 15.48 ? 214  HIS A CD2   1 
ATOM   1657  C CE1   . HIS A  1  214 ? 84.149  7.576   -38.441 1.00 16.58 ? 214  HIS A CE1   1 
ATOM   1658  N NE2   . HIS A  1  214 ? 82.968  6.988   -38.522 1.00 15.13 ? 214  HIS A NE2   1 
ATOM   1659  N N     . ALA A  1  215 ? 85.201  0.814   -40.153 1.00 10.44 ? 215  ALA A N     1 
ATOM   1660  C CA    . ALA A  1  215 ? 85.875  -0.329  -40.762 1.00 10.00 ? 215  ALA A CA    1 
ATOM   1661  C C     . ALA A  1  215 ? 84.833  -1.291  -41.313 1.00 9.94  ? 215  ALA A C     1 
ATOM   1662  O O     . ALA A  1  215 ? 84.153  -1.991  -40.558 1.00 10.40 ? 215  ALA A O     1 
ATOM   1663  C CB    . ALA A  1  215 ? 86.742  -1.032  -39.728 1.00 10.38 ? 215  ALA A CB    1 
ATOM   1664  N N     . SER A  1  216 ? 84.709  -1.319  -42.636 1.00 9.36  ? 216  SER A N     1 
ATOM   1665  C CA    . SER A  1  216 ? 83.739  -2.179  -43.300 1.00 9.51  ? 216  SER A CA    1 
ATOM   1666  C C     . SER A  1  216 ? 84.364  -3.519  -43.668 1.00 9.04  ? 216  SER A C     1 
ATOM   1667  O O     . SER A  1  216 ? 85.167  -3.596  -44.597 1.00 10.49 ? 216  SER A O     1 
ATOM   1668  C CB    . SER A  1  216 ? 83.210  -1.481  -44.559 1.00 10.74 ? 216  SER A CB    1 
ATOM   1669  O OG    . SER A  1  216 ? 82.247  -2.273  -45.234 1.00 10.48 ? 216  SER A OG    1 
ATOM   1670  N N     . VAL A  1  217 ? 84.001  -4.568  -42.933 1.00 8.64  ? 217  VAL A N     1 
ATOM   1671  C CA    . VAL A  1  217 ? 84.530  -5.904  -43.197 1.00 7.83  ? 217  VAL A CA    1 
ATOM   1672  C C     . VAL A  1  217 ? 83.779  -6.486  -44.390 1.00 7.99  ? 217  VAL A C     1 
ATOM   1673  O O     . VAL A  1  217 ? 82.563  -6.690  -44.340 1.00 7.51  ? 217  VAL A O     1 
ATOM   1674  C CB    . VAL A  1  217 ? 84.375  -6.814  -41.966 1.00 7.75  ? 217  VAL A CB    1 
ATOM   1675  C CG1   . VAL A  1  217 ? 84.919  -8.200  -42.272 1.00 8.50  ? 217  VAL A CG1   1 
ATOM   1676  C CG2   . VAL A  1  217 ? 85.121  -6.205  -40.778 1.00 8.48  ? 217  VAL A CG2   1 
ATOM   1677  N N     . GLU A  1  218 ? 84.521  -6.757  -45.459 1.00 8.66  ? 218  GLU A N     1 
ATOM   1678  C CA    . GLU A  1  218 ? 83.940  -7.246  -46.701 1.00 9.49  ? 218  GLU A CA    1 
ATOM   1679  C C     . GLU A  1  218 ? 84.054  -8.735  -46.968 1.00 10.40 ? 218  GLU A C     1 
ATOM   1680  O O     . GLU A  1  218 ? 83.233  -9.296  -47.695 1.00 12.17 ? 218  GLU A O     1 
ATOM   1681  C CB    . GLU A  1  218 ? 84.569  -6.509  -47.885 1.00 10.97 ? 218  GLU A CB    1 
ATOM   1682  C CG    . GLU A  1  218 ? 84.667  -5.006  -47.711 1.00 14.69 ? 218  GLU A CG    1 
ATOM   1683  C CD    . GLU A  1  218 ? 85.194  -4.322  -48.955 1.00 16.65 ? 218  GLU A CD    1 
ATOM   1684  O OE1   . GLU A  1  218 ? 86.086  -4.898  -49.614 1.00 17.96 ? 218  GLU A OE1   1 
ATOM   1685  O OE2   . GLU A  1  218 ? 84.727  -3.206  -49.267 1.00 19.29 ? 218  GLU A OE2   1 
ATOM   1686  N N     . LYS A  1  219 ? 85.057  -9.383  -46.391 1.00 9.94  ? 219  LYS A N     1 
ATOM   1687  C CA    . LYS A  1  219 ? 85.242  -10.799 -46.662 1.00 12.14 ? 219  LYS A CA    1 
ATOM   1688  C C     . LYS A  1  219 ? 86.132  -11.505 -45.648 1.00 12.04 ? 219  LYS A C     1 
ATOM   1689  O O     . LYS A  1  219 ? 87.061  -10.912 -45.099 1.00 10.94 ? 219  LYS A O     1 
ATOM   1690  C CB    . LYS A  1  219 ? 85.840  -10.945 -48.066 1.00 16.22 ? 219  LYS A CB    1 
ATOM   1691  C CG    . LYS A  1  219 ? 85.973  -12.361 -48.594 1.00 21.00 ? 219  LYS A CG    1 
ATOM   1692  C CD    . LYS A  1  219 ? 86.507  -12.329 -50.021 1.00 23.61 ? 219  LYS A CD    1 
ATOM   1693  C CE    . LYS A  1  219 ? 86.538  -13.712 -50.649 1.00 25.12 ? 219  LYS A CE    1 
ATOM   1694  N NZ    . LYS A  1  219 ? 86.980  -13.654 -52.073 1.00 28.30 ? 219  LYS A NZ    1 
ATOM   1695  N N     . ILE A  1  220 ? 85.825  -12.772 -45.391 1.00 10.24 ? 220  ILE A N     1 
ATOM   1696  C CA    . ILE A  1  220 ? 86.628  -13.583 -44.484 1.00 10.79 ? 220  ILE A CA    1 
ATOM   1697  C C     . ILE A  1  220 ? 87.642  -14.289 -45.381 1.00 11.19 ? 220  ILE A C     1 
ATOM   1698  O O     . ILE A  1  220 ? 87.293  -14.746 -46.469 1.00 12.49 ? 220  ILE A O     1 
ATOM   1699  C CB    . ILE A  1  220 ? 85.778  -14.649 -43.768 1.00 9.73  ? 220  ILE A CB    1 
ATOM   1700  C CG1   . ILE A  1  220 ? 84.690  -13.972 -42.928 1.00 10.98 ? 220  ILE A CG1   1 
ATOM   1701  C CG2   . ILE A  1  220 ? 86.670  -15.514 -42.881 1.00 10.59 ? 220  ILE A CG2   1 
ATOM   1702  C CD1   . ILE A  1  220 ? 83.620  -14.922 -42.442 1.00 12.63 ? 220  ILE A CD1   1 
ATOM   1703  N N     . ILE A  1  221 ? 88.893  -14.359 -44.936 1.00 10.91 ? 221  ILE A N     1 
ATOM   1704  C CA    . ILE A  1  221 ? 89.948  -15.008 -45.710 1.00 12.83 ? 221  ILE A CA    1 
ATOM   1705  C C     . ILE A  1  221 ? 90.133  -16.433 -45.206 1.00 12.27 ? 221  ILE A C     1 
ATOM   1706  O O     . ILE A  1  221 ? 90.118  -16.670 -44.001 1.00 12.05 ? 221  ILE A O     1 
ATOM   1707  C CB    . ILE A  1  221 ? 91.291  -14.256 -45.564 1.00 14.46 ? 221  ILE A CB    1 
ATOM   1708  C CG1   . ILE A  1  221 ? 91.109  -12.786 -45.945 1.00 15.34 ? 221  ILE A CG1   1 
ATOM   1709  C CG2   . ILE A  1  221 ? 92.352  -14.907 -46.446 1.00 14.93 ? 221  ILE A CG2   1 
ATOM   1710  C CD1   . ILE A  1  221 ? 92.341  -11.931 -45.709 1.00 17.38 ? 221  ILE A CD1   1 
ATOM   1711  N N     . PHE A  1  222 ? 90.302  -17.378 -46.126 1.00 12.64 ? 222  PHE A N     1 
ATOM   1712  C CA    . PHE A  1  222 ? 90.489  -18.776 -45.744 1.00 13.27 ? 222  PHE A CA    1 
ATOM   1713  C C     . PHE A  1  222 ? 91.755  -19.383 -46.329 1.00 15.97 ? 222  PHE A C     1 
ATOM   1714  O O     . PHE A  1  222 ? 92.395  -18.808 -47.210 1.00 14.73 ? 222  PHE A O     1 
ATOM   1715  C CB    . PHE A  1  222 ? 89.307  -19.638 -46.201 1.00 12.71 ? 222  PHE A CB    1 
ATOM   1716  C CG    . PHE A  1  222 ? 87.982  -19.210 -45.648 1.00 12.67 ? 222  PHE A CG    1 
ATOM   1717  C CD1   . PHE A  1  222 ? 87.185  -18.303 -46.340 1.00 12.10 ? 222  PHE A CD1   1 
ATOM   1718  C CD2   . PHE A  1  222 ? 87.525  -19.718 -44.438 1.00 12.54 ? 222  PHE A CD2   1 
ATOM   1719  C CE1   . PHE A  1  222 ? 85.947  -17.910 -45.834 1.00 12.79 ? 222  PHE A CE1   1 
ATOM   1720  C CE2   . PHE A  1  222 ? 86.290  -19.332 -43.922 1.00 13.08 ? 222  PHE A CE2   1 
ATOM   1721  C CZ    . PHE A  1  222 ? 85.498  -18.424 -44.623 1.00 13.11 ? 222  PHE A CZ    1 
ATOM   1722  N N     . SER A  1  223 ? 92.092  -20.563 -45.823 1.00 18.27 ? 223  SER A N     1 
ATOM   1723  C CA    . SER A  1  223 ? 93.247  -21.318 -46.278 1.00 21.06 ? 223  SER A CA    1 
ATOM   1724  C C     . SER A  1  223 ? 93.106  -22.730 -45.735 1.00 22.28 ? 223  SER A C     1 
ATOM   1725  O O     . SER A  1  223 ? 92.310  -22.985 -44.837 1.00 22.85 ? 223  SER A O     1 
ATOM   1726  C CB    . SER A  1  223 ? 94.547  -20.708 -45.753 1.00 22.31 ? 223  SER A CB    1 
ATOM   1727  O OG    . SER A  1  223 ? 94.730  -21.022 -44.384 1.00 25.70 ? 223  SER A OG    1 
ATOM   1728  N N     . ASN A  1  224 ? 93.880  -23.645 -46.296 1.00 24.03 ? 224  ASN A N     1 
ATOM   1729  C CA    . ASN A  1  224 ? 93.866  -25.032 -45.854 1.00 25.87 ? 224  ASN A CA    1 
ATOM   1730  C C     . ASN A  1  224 ? 95.172  -25.186 -45.093 1.00 26.15 ? 224  ASN A C     1 
ATOM   1731  O O     . ASN A  1  224 ? 96.237  -25.265 -45.707 1.00 27.07 ? 224  ASN A O     1 
ATOM   1732  C CB    . ASN A  1  224 ? 93.811  -25.969 -47.068 1.00 27.32 ? 224  ASN A CB    1 
ATOM   1733  C CG    . ASN A  1  224 ? 92.558  -25.764 -47.906 1.00 29.52 ? 224  ASN A CG    1 
ATOM   1734  O OD1   . ASN A  1  224 ? 92.591  -25.855 -49.135 1.00 32.35 ? 224  ASN A OD1   1 
ATOM   1735  N ND2   . ASN A  1  224 ? 91.443  -25.508 -47.241 1.00 30.29 ? 224  ASN A ND2   1 
ATOM   1736  N N     . ALA A  1  225 ? 95.092  -25.202 -43.761 1.00 26.81 ? 225  ALA A N     1 
ATOM   1737  C CA    . ALA A  1  225 ? 96.297  -25.303 -42.932 1.00 27.19 ? 225  ALA A CA    1 
ATOM   1738  C C     . ALA A  1  225 ? 96.324  -26.358 -41.807 1.00 26.81 ? 225  ALA A C     1 
ATOM   1739  O O     . ALA A  1  225 ? 96.538  -26.024 -40.638 1.00 27.78 ? 225  ALA A O     1 
ATOM   1740  C CB    . ALA A  1  225 ? 96.594  -23.946 -42.338 1.00 26.86 ? 225  ALA A CB    1 
ATOM   1741  N N     . PRO A  1  226 ? 96.160  -27.640 -42.158 1.00 25.60 ? 226  PRO A N     1 
ATOM   1742  C CA    . PRO A  1  226 ? 95.907  -28.210 -43.489 1.00 24.81 ? 226  PRO A CA    1 
ATOM   1743  C C     . PRO A  1  226 ? 94.430  -28.194 -43.882 1.00 23.06 ? 226  PRO A C     1 
ATOM   1744  O O     . PRO A  1  226 ? 94.092  -28.193 -45.064 1.00 23.86 ? 226  PRO A O     1 
ATOM   1745  C CB    . PRO A  1  226 ? 96.446  -29.631 -43.347 1.00 24.88 ? 226  PRO A CB    1 
ATOM   1746  C CG    . PRO A  1  226 ? 96.040  -29.968 -41.944 1.00 25.02 ? 226  PRO A CG    1 
ATOM   1747  C CD    . PRO A  1  226 ? 96.415  -28.717 -41.176 1.00 26.44 ? 226  PRO A CD    1 
ATOM   1748  N N     . GLY A  1  227 ? 93.555  -28.201 -42.878 1.00 21.67 ? 227  GLY A N     1 
ATOM   1749  C CA    . GLY A  1  227 ? 92.124  -28.193 -43.142 1.00 19.02 ? 227  GLY A CA    1 
ATOM   1750  C C     . GLY A  1  227 ? 91.605  -26.791 -43.388 1.00 17.78 ? 227  GLY A C     1 
ATOM   1751  O O     . GLY A  1  227 ? 92.303  -25.813 -43.111 1.00 17.06 ? 227  GLY A O     1 
ATOM   1752  N N     . LEU A  1  228 ? 90.388  -26.690 -43.915 1.00 15.44 ? 228  LEU A N     1 
ATOM   1753  C CA    . LEU A  1  228 ? 89.787  -25.388 -44.190 1.00 13.04 ? 228  LEU A CA    1 
ATOM   1754  C C     . LEU A  1  228 ? 89.775  -24.582 -42.897 1.00 11.92 ? 228  LEU A C     1 
ATOM   1755  O O     . LEU A  1  228 ? 89.193  -25.003 -41.897 1.00 10.85 ? 228  LEU A O     1 
ATOM   1756  C CB    . LEU A  1  228 ? 88.363  -25.560 -44.727 1.00 13.86 ? 228  LEU A CB    1 
ATOM   1757  C CG    . LEU A  1  228 ? 87.610  -24.267 -45.060 1.00 14.64 ? 228  LEU A CG    1 
ATOM   1758  C CD1   . LEU A  1  228 ? 88.419  -23.420 -46.030 1.00 12.54 ? 228  LEU A CD1   1 
ATOM   1759  C CD2   . LEU A  1  228 ? 86.250  -24.612 -45.652 1.00 14.09 ? 228  LEU A CD2   1 
ATOM   1760  N N     . THR A  1  229 ? 90.416  -23.417 -42.931 1.00 12.33 ? 229  THR A N     1 
ATOM   1761  C CA    . THR A  1  229 ? 90.526  -22.563 -41.754 1.00 12.61 ? 229  THR A CA    1 
ATOM   1762  C C     . THR A  1  229 ? 90.409  -21.077 -42.088 1.00 10.97 ? 229  THR A C     1 
ATOM   1763  O O     . THR A  1  229 ? 90.911  -20.627 -43.113 1.00 12.74 ? 229  THR A O     1 
ATOM   1764  C CB    . THR A  1  229 ? 91.897  -22.775 -41.070 1.00 13.74 ? 229  THR A CB    1 
ATOM   1765  O OG1   . THR A  1  229 ? 92.087  -24.167 -40.792 1.00 15.90 ? 229  THR A OG1   1 
ATOM   1766  C CG2   . THR A  1  229 ? 91.981  -21.989 -39.777 1.00 13.38 ? 229  THR A CG2   1 
ATOM   1767  N N     . ALA A  1  230 ? 89.742  -20.320 -41.219 1.00 9.78  ? 230  ALA A N     1 
ATOM   1768  C CA    . ALA A  1  230 ? 89.622  -18.877 -41.413 1.00 10.36 ? 230  ALA A CA    1 
ATOM   1769  C C     . ALA A  1  230 ? 90.951  -18.295 -40.930 1.00 10.91 ? 230  ALA A C     1 
ATOM   1770  O O     . ALA A  1  230 ? 91.417  -18.627 -39.838 1.00 12.44 ? 230  ALA A O     1 
ATOM   1771  C CB    . ALA A  1  230 ? 88.464  -18.324 -40.586 1.00 9.30  ? 230  ALA A CB    1 
ATOM   1772  N N     . THR A  1  231 ? 91.569  -17.439 -41.738 1.00 11.70 ? 231  THR A N     1 
ATOM   1773  C CA    . THR A  1  231 ? 92.861  -16.866 -41.369 1.00 11.11 ? 231  THR A CA    1 
ATOM   1774  C C     . THR A  1  231 ? 92.832  -15.370 -41.090 1.00 11.21 ? 231  THR A C     1 
ATOM   1775  O O     . THR A  1  231 ? 93.783  -14.820 -40.534 1.00 11.28 ? 231  THR A O     1 
ATOM   1776  C CB    . THR A  1  231 ? 93.904  -17.124 -42.467 1.00 13.20 ? 231  THR A CB    1 
ATOM   1777  O OG1   . THR A  1  231 ? 93.488  -16.482 -43.677 1.00 14.34 ? 231  THR A OG1   1 
ATOM   1778  C CG2   . THR A  1  231 ? 94.050  -18.617 -42.715 1.00 15.93 ? 231  THR A CG2   1 
ATOM   1779  N N     . GLY A  1  232 ? 91.749  -14.711 -41.476 1.00 9.03  ? 232  GLY A N     1 
ATOM   1780  C CA    . GLY A  1  232 ? 91.652  -13.281 -41.246 1.00 10.34 ? 232  GLY A CA    1 
ATOM   1781  C C     . GLY A  1  232 ? 90.495  -12.675 -42.003 1.00 10.24 ? 232  GLY A C     1 
ATOM   1782  O O     . GLY A  1  232 ? 89.600  -13.388 -42.449 1.00 10.38 ? 232  GLY A O     1 
ATOM   1783  N N     . VAL A  1  233 ? 90.509  -11.354 -42.149 1.00 10.51 ? 233  VAL A N     1 
ATOM   1784  C CA    . VAL A  1  233 ? 89.447  -10.665 -42.865 1.00 10.44 ? 233  VAL A CA    1 
ATOM   1785  C C     . VAL A  1  233 ? 89.989  -9.476  -43.635 1.00 10.79 ? 233  VAL A C     1 
ATOM   1786  O O     . VAL A  1  233 ? 91.080  -8.977  -43.356 1.00 9.98  ? 233  VAL A O     1 
ATOM   1787  C CB    . VAL A  1  233 ? 88.346  -10.136 -41.904 1.00 10.59 ? 233  VAL A CB    1 
ATOM   1788  C CG1   . VAL A  1  233 ? 87.803  -11.269 -41.053 1.00 11.36 ? 233  VAL A CG1   1 
ATOM   1789  C CG2   . VAL A  1  233 ? 88.904  -9.018  -41.024 1.00 11.71 ? 233  VAL A CG2   1 
ATOM   1790  N N     . ILE A  1  234 ? 89.214  -9.036  -44.617 1.00 11.17 ? 234  ILE A N     1 
ATOM   1791  C CA    . ILE A  1  234 ? 89.565  -7.871  -45.412 1.00 11.11 ? 234  ILE A CA    1 
ATOM   1792  C C     . ILE A  1  234 ? 88.544  -6.808  -45.040 1.00 9.36  ? 234  ILE A C     1 
ATOM   1793  O O     . ILE A  1  234 ? 87.342  -7.074  -45.047 1.00 10.96 ? 234  ILE A O     1 
ATOM   1794  C CB    . ILE A  1  234 ? 89.442  -8.148  -46.923 1.00 12.44 ? 234  ILE A CB    1 
ATOM   1795  C CG1   . ILE A  1  234 ? 90.434  -9.232  -47.337 1.00 13.12 ? 234  ILE A CG1   1 
ATOM   1796  C CG2   . ILE A  1  234 ? 89.691  -6.862  -47.710 1.00 12.02 ? 234  ILE A CG2   1 
ATOM   1797  C CD1   . ILE A  1  234 ? 90.306  -9.656  -48.790 1.00 15.29 ? 234  ILE A CD1   1 
ATOM   1798  N N     . TYR A  1  235 ? 89.015  -5.617  -44.689 1.00 9.81  ? 235  TYR A N     1 
ATOM   1799  C CA    . TYR A  1  235 ? 88.104  -4.532  -44.352 1.00 10.39 ? 235  TYR A CA    1 
ATOM   1800  C C     . TYR A  1  235 ? 88.547  -3.279  -45.091 1.00 11.67 ? 235  TYR A C     1 
ATOM   1801  O O     . TYR A  1  235 ? 89.709  -3.160  -45.482 1.00 12.53 ? 235  TYR A O     1 
ATOM   1802  C CB    . TYR A  1  235 ? 88.056  -4.309  -42.831 1.00 10.40 ? 235  TYR A CB    1 
ATOM   1803  C CG    . TYR A  1  235 ? 89.354  -3.882  -42.177 1.00 10.15 ? 235  TYR A CG    1 
ATOM   1804  C CD1   . TYR A  1  235 ? 89.646  -2.533  -41.982 1.00 11.33 ? 235  TYR A CD1   1 
ATOM   1805  C CD2   . TYR A  1  235 ? 90.271  -4.828  -41.720 1.00 10.48 ? 235  TYR A CD2   1 
ATOM   1806  C CE1   . TYR A  1  235 ? 90.818  -2.132  -41.341 1.00 11.72 ? 235  TYR A CE1   1 
ATOM   1807  C CE2   . TYR A  1  235 ? 91.449  -4.441  -41.080 1.00 10.45 ? 235  TYR A CE2   1 
ATOM   1808  C CZ    . TYR A  1  235 ? 91.714  -3.089  -40.894 1.00 12.36 ? 235  TYR A CZ    1 
ATOM   1809  O OH    . TYR A  1  235 ? 92.876  -2.691  -40.274 1.00 12.57 ? 235  TYR A OH    1 
ATOM   1810  N N     . ARG A  1  236 ? 87.621  -2.350  -45.299 1.00 10.44 ? 236  ARG A N     1 
ATOM   1811  C CA    . ARG A  1  236 ? 87.942  -1.130  -46.031 1.00 13.59 ? 236  ARG A CA    1 
ATOM   1812  C C     . ARG A  1  236 ? 87.692  0.121   -45.195 1.00 13.49 ? 236  ARG A C     1 
ATOM   1813  O O     . ARG A  1  236 ? 86.759  0.157   -44.389 1.00 12.73 ? 236  ARG A O     1 
ATOM   1814  C CB    . ARG A  1  236 ? 87.108  -1.083  -47.317 1.00 15.56 ? 236  ARG A CB    1 
ATOM   1815  C CG    . ARG A  1  236 ? 87.605  -0.099  -48.364 1.00 18.92 ? 236  ARG A CG    1 
ATOM   1816  C CD    . ARG A  1  236 ? 86.816  -0.251  -49.654 1.00 20.09 ? 236  ARG A CD    1 
ATOM   1817  N NE    . ARG A  1  236 ? 86.917  -1.604  -50.198 1.00 22.38 ? 236  ARG A NE    1 
ATOM   1818  C CZ    . ARG A  1  236 ? 87.978  -2.082  -50.843 1.00 24.27 ? 236  ARG A CZ    1 
ATOM   1819  N NH1   . ARG A  1  236 ? 89.046  -1.317  -51.039 1.00 24.49 ? 236  ARG A NH1   1 
ATOM   1820  N NH2   . ARG A  1  236 ? 87.973  -3.330  -51.291 1.00 25.81 ? 236  ARG A NH2   1 
ATOM   1821  N N     . ASP A  1  237 ? 88.530  1.141   -45.378 1.00 14.54 ? 237  ASP A N     1 
ATOM   1822  C CA    . ASP A  1  237 ? 88.370  2.387   -44.633 1.00 15.36 ? 237  ASP A CA    1 
ATOM   1823  C C     . ASP A  1  237 ? 87.649  3.449   -45.457 1.00 16.33 ? 237  ASP A C     1 
ATOM   1824  O O     . ASP A  1  237 ? 87.291  3.213   -46.613 1.00 15.84 ? 237  ASP A O     1 
ATOM   1825  C CB    . ASP A  1  237 ? 89.727  2.925   -44.135 1.00 15.76 ? 237  ASP A CB    1 
ATOM   1826  C CG    . ASP A  1  237 ? 90.692  3.267   -45.265 1.00 17.83 ? 237  ASP A CG    1 
ATOM   1827  O OD1   . ASP A  1  237 ? 90.240  3.713   -46.339 1.00 17.00 ? 237  ASP A OD1   1 
ATOM   1828  O OD2   . ASP A  1  237 ? 91.917  3.113   -45.060 1.00 17.96 ? 237  ASP A OD2   1 
ATOM   1829  N N     . SER A  1  238 ? 87.435  4.617   -44.857 1.00 17.08 ? 238  SER A N     1 
ATOM   1830  C CA    . SER A  1  238 ? 86.729  5.707   -45.523 1.00 18.18 ? 238  SER A CA    1 
ATOM   1831  C C     . SER A  1  238 ? 87.421  6.258   -46.769 1.00 19.13 ? 238  SER A C     1 
ATOM   1832  O O     . SER A  1  238 ? 86.809  7.002   -47.537 1.00 19.54 ? 238  SER A O     1 
ATOM   1833  C CB    . SER A  1  238 ? 86.462  6.846   -44.530 1.00 15.67 ? 238  SER A CB    1 
ATOM   1834  O OG    . SER A  1  238 ? 87.659  7.314   -43.945 1.00 16.08 ? 238  SER A OG    1 
ATOM   1835  N N     . ASN A  1  239 ? 88.688  5.905   -46.972 1.00 19.88 ? 239  ASN A N     1 
ATOM   1836  C CA    . ASN A  1  239 ? 89.416  6.367   -48.153 1.00 21.34 ? 239  ASN A CA    1 
ATOM   1837  C C     . ASN A  1  239 ? 89.269  5.357   -49.278 1.00 21.00 ? 239  ASN A C     1 
ATOM   1838  O O     . ASN A  1  239 ? 89.670  5.614   -50.414 1.00 21.29 ? 239  ASN A O     1 
ATOM   1839  C CB    . ASN A  1  239 ? 90.906  6.555   -47.850 1.00 22.00 ? 239  ASN A CB    1 
ATOM   1840  C CG    . ASN A  1  239 ? 91.178  7.749   -46.963 1.00 23.24 ? 239  ASN A CG    1 
ATOM   1841  O OD1   . ASN A  1  239 ? 90.587  8.815   -47.142 1.00 27.09 ? 239  ASN A OD1   1 
ATOM   1842  N ND2   . ASN A  1  239 ? 92.090  7.586   -46.011 1.00 23.80 ? 239  ASN A ND2   1 
ATOM   1843  N N     . GLY A  1  240 ? 88.687  4.207   -48.954 1.00 20.37 ? 240  GLY A N     1 
ATOM   1844  C CA    . GLY A  1  240 ? 88.503  3.160   -49.942 1.00 19.80 ? 240  GLY A CA    1 
ATOM   1845  C C     . GLY A  1  240 ? 89.678  2.202   -49.933 1.00 17.81 ? 240  GLY A C     1 
ATOM   1846  O O     . GLY A  1  240 ? 89.740  1.275   -50.738 1.00 18.64 ? 240  GLY A O     1 
ATOM   1847  N N     . THR A  1  241 ? 90.613  2.432   -49.015 1.00 17.61 ? 241  THR A N     1 
ATOM   1848  C CA    . THR A  1  241 ? 91.806  1.602   -48.891 1.00 16.99 ? 241  THR A CA    1 
ATOM   1849  C C     . THR A  1  241 ? 91.510  0.314   -48.124 1.00 17.05 ? 241  THR A C     1 
ATOM   1850  O O     . THR A  1  241 ? 90.990  0.351   -47.010 1.00 14.78 ? 241  THR A O     1 
ATOM   1851  C CB    . THR A  1  241 ? 92.934  2.362   -48.157 1.00 19.41 ? 241  THR A CB    1 
ATOM   1852  O OG1   . THR A  1  241 ? 93.252  3.565   -48.872 1.00 19.77 ? 241  THR A OG1   1 
ATOM   1853  C CG2   . THR A  1  241 ? 94.179  1.499   -48.054 1.00 19.44 ? 241  THR A CG2   1 
ATOM   1854  N N     . PRO A  1  242 ? 91.829  -0.845  -48.721 1.00 16.19 ? 242  PRO A N     1 
ATOM   1855  C CA    . PRO A  1  242 ? 91.578  -2.120  -48.046 1.00 16.27 ? 242  PRO A CA    1 
ATOM   1856  C C     . PRO A  1  242 ? 92.729  -2.541  -47.137 1.00 16.32 ? 242  PRO A C     1 
ATOM   1857  O O     . PRO A  1  242 ? 93.901  -2.383  -47.484 1.00 17.44 ? 242  PRO A O     1 
ATOM   1858  C CB    . PRO A  1  242 ? 91.381  -3.083  -49.207 1.00 15.63 ? 242  PRO A CB    1 
ATOM   1859  C CG    . PRO A  1  242 ? 92.383  -2.567  -50.209 1.00 16.26 ? 242  PRO A CG    1 
ATOM   1860  C CD    . PRO A  1  242 ? 92.165  -1.061  -50.142 1.00 16.77 ? 242  PRO A CD    1 
ATOM   1861  N N     . HIS A  1  243 ? 92.379  -3.066  -45.968 1.00 14.04 ? 243  HIS A N     1 
ATOM   1862  C CA    . HIS A  1  243 ? 93.354  -3.537  -44.997 1.00 13.68 ? 243  HIS A CA    1 
ATOM   1863  C C     . HIS A  1  243 ? 93.080  -5.016  -44.770 1.00 13.98 ? 243  HIS A C     1 
ATOM   1864  O O     . HIS A  1  243 ? 92.036  -5.535  -45.171 1.00 14.33 ? 243  HIS A O     1 
ATOM   1865  C CB    . HIS A  1  243 ? 93.180  -2.849  -43.643 1.00 12.32 ? 243  HIS A CB    1 
ATOM   1866  C CG    . HIS A  1  243 ? 93.375  -1.367  -43.660 1.00 13.86 ? 243  HIS A CG    1 
ATOM   1867  N ND1   . HIS A  1  243 ? 92.659  -0.525  -44.485 1.00 16.71 ? 243  HIS A ND1   1 
ATOM   1868  C CD2   . HIS A  1  243 ? 94.148  -0.567  -42.888 1.00 14.23 ? 243  HIS A CD2   1 
ATOM   1869  C CE1   . HIS A  1  243 ? 92.981  0.727   -44.217 1.00 13.61 ? 243  HIS A CE1   1 
ATOM   1870  N NE2   . HIS A  1  243 ? 93.882  0.730   -43.251 1.00 16.28 ? 243  HIS A NE2   1 
ATOM   1871  N N     . GLN A  1  244 ? 94.015  -5.682  -44.107 1.00 13.53 ? 244  GLN A N     1 
ATOM   1872  C CA    . GLN A  1  244 ? 93.859  -7.090  -43.776 1.00 14.20 ? 244  GLN A CA    1 
ATOM   1873  C C     . GLN A  1  244 ? 94.277  -7.298  -42.329 1.00 12.99 ? 244  GLN A C     1 
ATOM   1874  O O     . GLN A  1  244 ? 95.252  -6.710  -41.869 1.00 13.40 ? 244  GLN A O     1 
ATOM   1875  C CB    . GLN A  1  244 ? 94.729  -7.968  -44.677 1.00 15.90 ? 244  GLN A CB    1 
ATOM   1876  C CG    . GLN A  1  244 ? 94.348  -7.945  -46.138 1.00 19.96 ? 244  GLN A CG    1 
ATOM   1877  C CD    . GLN A  1  244 ? 95.206  -8.881  -46.968 1.00 22.55 ? 244  GLN A CD    1 
ATOM   1878  O OE1   . GLN A  1  244 ? 96.432  -8.756  -47.001 1.00 24.76 ? 244  GLN A OE1   1 
ATOM   1879  N NE2   . GLN A  1  244 ? 94.565  -9.827  -47.643 1.00 25.02 ? 244  GLN A NE2   1 
ATOM   1880  N N     . ALA A  1  245 ? 93.525  -8.123  -41.613 1.00 12.02 ? 245  ALA A N     1 
ATOM   1881  C CA    . ALA A  1  245 ? 93.829  -8.444  -40.226 1.00 11.74 ? 245  ALA A CA    1 
ATOM   1882  C C     . ALA A  1  245 ? 93.815  -9.962  -40.147 1.00 12.44 ? 245  ALA A C     1 
ATOM   1883  O O     . ALA A  1  245 ? 92.805  -10.592 -40.462 1.00 13.27 ? 245  ALA A O     1 
ATOM   1884  C CB    . ALA A  1  245 ? 92.774  -7.856  -39.299 1.00 12.02 ? 245  ALA A CB    1 
ATOM   1885  N N     . PHE A  1  246 ? 94.940  -10.547 -39.750 1.00 11.68 ? 246  PHE A N     1 
ATOM   1886  C CA    . PHE A  1  246 ? 95.049  -11.996 -39.649 1.00 12.00 ? 246  PHE A CA    1 
ATOM   1887  C C     . PHE A  1  246 ? 95.152  -12.456 -38.204 1.00 12.15 ? 246  PHE A C     1 
ATOM   1888  O O     . PHE A  1  246 ? 95.531  -11.687 -37.320 1.00 11.87 ? 246  PHE A O     1 
ATOM   1889  C CB    . PHE A  1  246 ? 96.281  -12.505 -40.405 1.00 12.63 ? 246  PHE A CB    1 
ATOM   1890  C CG    . PHE A  1  246 ? 96.261  -12.219 -41.877 1.00 13.07 ? 246  PHE A CG    1 
ATOM   1891  C CD1   . PHE A  1  246 ? 96.755  -11.019 -42.375 1.00 15.55 ? 246  PHE A CD1   1 
ATOM   1892  C CD2   . PHE A  1  246 ? 95.754  -13.157 -42.769 1.00 15.14 ? 246  PHE A CD2   1 
ATOM   1893  C CE1   . PHE A  1  246 ? 96.746  -10.759 -43.747 1.00 17.15 ? 246  PHE A CE1   1 
ATOM   1894  C CE2   . PHE A  1  246 ? 95.740  -12.907 -44.139 1.00 16.43 ? 246  PHE A CE2   1 
ATOM   1895  C CZ    . PHE A  1  246 ? 96.236  -11.707 -44.627 1.00 15.88 ? 246  PHE A CZ    1 
ATOM   1896  N N     . VAL A  1  247 ? 94.819  -13.722 -37.975 1.00 12.91 ? 247  VAL A N     1 
ATOM   1897  C CA    . VAL A  1  247 ? 94.900  -14.304 -36.642 1.00 12.69 ? 247  VAL A CA    1 
ATOM   1898  C C     . VAL A  1  247 ? 96.033  -15.324 -36.625 1.00 13.01 ? 247  VAL A C     1 
ATOM   1899  O O     . VAL A  1  247 ? 96.291  -15.998 -37.623 1.00 15.13 ? 247  VAL A O     1 
ATOM   1900  C CB    . VAL A  1  247 ? 93.575  -14.991 -36.238 1.00 13.27 ? 247  VAL A CB    1 
ATOM   1901  C CG1   . VAL A  1  247 ? 92.467  -13.948 -36.138 1.00 13.07 ? 247  VAL A CG1   1 
ATOM   1902  C CG2   . VAL A  1  247 ? 93.204  -16.063 -37.247 1.00 13.19 ? 247  VAL A CG2   1 
ATOM   1903  N N     . ARG A  1  248 ? 96.711  -15.428 -35.488 1.00 13.18 ? 248  ARG A N     1 
ATOM   1904  C CA    . ARG A  1  248 ? 97.826  -16.351 -35.347 1.00 13.44 ? 248  ARG A CA    1 
ATOM   1905  C C     . ARG A  1  248 ? 97.397  -17.734 -34.864 1.00 14.26 ? 248  ARG A C     1 
ATOM   1906  O O     . ARG A  1  248 ? 96.217  -17.984 -34.629 1.00 16.04 ? 248  ARG A O     1 
ATOM   1907  C CB    . ARG A  1  248 ? 98.870  -15.755 -34.400 1.00 13.32 ? 248  ARG A CB    1 
ATOM   1908  C CG    . ARG A  1  248 ? 99.468  -14.445 -34.915 1.00 15.15 ? 248  ARG A CG    1 
ATOM   1909  C CD    . ARG A  1  248 ? 100.752 -14.071 -34.186 1.00 14.82 ? 248  ARG A CD    1 
ATOM   1910  N NE    . ARG A  1  248 ? 100.524 -13.576 -32.829 1.00 16.20 ? 248  ARG A NE    1 
ATOM   1911  C CZ    . ARG A  1  248 ? 100.305 -12.301 -32.518 1.00 15.26 ? 248  ARG A CZ    1 
ATOM   1912  N NH1   . ARG A  1  248 ? 100.280 -11.373 -33.464 1.00 13.74 ? 248  ARG A NH1   1 
ATOM   1913  N NH2   . ARG A  1  248 ? 100.118 -11.949 -31.254 1.00 15.75 ? 248  ARG A NH2   1 
ATOM   1914  N N     . SER A  1  249 ? 98.367  -18.632 -34.728 1.00 15.65 ? 249  SER A N     1 
ATOM   1915  C CA    . SER A  1  249 ? 98.097  -19.997 -34.287 1.00 16.80 ? 249  SER A CA    1 
ATOM   1916  C C     . SER A  1  249 ? 97.140  -20.060 -33.100 1.00 16.86 ? 249  SER A C     1 
ATOM   1917  O O     . SER A  1  249 ? 97.308  -19.341 -32.112 1.00 17.91 ? 249  SER A O     1 
ATOM   1918  C CB    . SER A  1  249 ? 99.410  -20.699 -33.925 1.00 18.11 ? 249  SER A CB    1 
ATOM   1919  O OG    . SER A  1  249 ? 99.178  -22.045 -33.544 1.00 21.11 ? 249  SER A OG    1 
ATOM   1920  N N     . LYS A  1  250 ? 96.139  -20.932 -33.213 1.00 16.16 ? 250  LYS A N     1 
ATOM   1921  C CA    . LYS A  1  250 ? 95.127  -21.137 -32.179 1.00 16.75 ? 250  LYS A CA    1 
ATOM   1922  C C     . LYS A  1  250 ? 94.126  -19.992 -32.061 1.00 14.99 ? 250  LYS A C     1 
ATOM   1923  O O     . LYS A  1  250 ? 93.149  -20.096 -31.320 1.00 15.70 ? 250  LYS A O     1 
ATOM   1924  C CB    . LYS A  1  250 ? 95.785  -21.374 -30.815 1.00 19.51 ? 250  LYS A CB    1 
ATOM   1925  C CG    . LYS A  1  250 ? 96.586  -22.664 -30.719 1.00 23.72 ? 250  LYS A CG    1 
ATOM   1926  C CD    . LYS A  1  250 ? 97.026  -22.914 -29.285 1.00 26.53 ? 250  LYS A CD    1 
ATOM   1927  C CE    . LYS A  1  250 ? 97.786  -24.219 -29.148 1.00 29.23 ? 250  LYS A CE    1 
ATOM   1928  N NZ    . LYS A  1  250 ? 98.126  -24.494 -27.724 1.00 31.80 ? 250  LYS A NZ    1 
ATOM   1929  N N     . GLY A  1  251 ? 94.374  -18.907 -32.789 1.00 13.90 ? 251  GLY A N     1 
ATOM   1930  C CA    . GLY A  1  251 ? 93.477  -17.763 -32.751 1.00 12.53 ? 251  GLY A CA    1 
ATOM   1931  C C     . GLY A  1  251 ? 92.265  -17.972 -33.639 1.00 11.43 ? 251  GLY A C     1 
ATOM   1932  O O     . GLY A  1  251 ? 92.219  -18.928 -34.411 1.00 11.39 ? 251  GLY A O     1 
ATOM   1933  N N     . GLU A  1  252 ? 91.286  -17.075 -33.554 1.00 10.24 ? 252  GLU A N     1 
ATOM   1934  C CA    . GLU A  1  252 ? 90.081  -17.237 -34.358 1.00 9.50  ? 252  GLU A CA    1 
ATOM   1935  C C     . GLU A  1  252 ? 89.440  -15.943 -34.824 1.00 9.49  ? 252  GLU A C     1 
ATOM   1936  O O     . GLU A  1  252 ? 89.673  -14.869 -34.267 1.00 8.73  ? 252  GLU A O     1 
ATOM   1937  C CB    . GLU A  1  252 ? 89.029  -18.018 -33.563 1.00 11.53 ? 252  GLU A CB    1 
ATOM   1938  C CG    . GLU A  1  252 ? 89.542  -19.295 -32.920 1.00 13.48 ? 252  GLU A CG    1 
ATOM   1939  C CD    . GLU A  1  252 ? 88.468  -20.018 -32.137 1.00 15.63 ? 252  GLU A CD    1 
ATOM   1940  O OE1   . GLU A  1  252 ? 87.396  -20.288 -32.717 1.00 16.46 ? 252  GLU A OE1   1 
ATOM   1941  O OE2   . GLU A  1  252 ? 88.694  -20.321 -30.946 1.00 14.10 ? 252  GLU A OE2   1 
ATOM   1942  N N     . VAL A  1  253 ? 88.638  -16.069 -35.873 1.00 8.28  ? 253  VAL A N     1 
ATOM   1943  C CA    . VAL A  1  253 ? 87.876  -14.955 -36.406 1.00 8.67  ? 253  VAL A CA    1 
ATOM   1944  C C     . VAL A  1  253 ? 86.477  -15.233 -35.873 1.00 9.14  ? 253  VAL A C     1 
ATOM   1945  O O     . VAL A  1  253 ? 85.962  -16.345 -36.018 1.00 8.69  ? 253  VAL A O     1 
ATOM   1946  C CB    . VAL A  1  253 ? 87.824  -14.967 -37.949 1.00 7.97  ? 253  VAL A CB    1 
ATOM   1947  C CG1   . VAL A  1  253 ? 86.791  -13.955 -38.441 1.00 9.97  ? 253  VAL A CG1   1 
ATOM   1948  C CG2   . VAL A  1  253 ? 89.198  -14.639 -38.523 1.00 9.36  ? 253  VAL A CG2   1 
ATOM   1949  N N     . ILE A  1  254 ? 85.871  -14.244 -35.232 1.00 8.00  ? 254  ILE A N     1 
ATOM   1950  C CA    . ILE A  1  254 ? 84.528  -14.418 -34.702 1.00 7.81  ? 254  ILE A CA    1 
ATOM   1951  C C     . ILE A  1  254 ? 83.652  -13.339 -35.307 1.00 7.71  ? 254  ILE A C     1 
ATOM   1952  O O     . ILE A  1  254 ? 83.971  -12.150 -35.225 1.00 8.47  ? 254  ILE A O     1 
ATOM   1953  C CB    . ILE A  1  254 ? 84.509  -14.300 -33.167 1.00 8.35  ? 254  ILE A CB    1 
ATOM   1954  C CG1   . ILE A  1  254 ? 85.489  -15.314 -32.565 1.00 11.40 ? 254  ILE A CG1   1 
ATOM   1955  C CG2   . ILE A  1  254 ? 83.102  -14.556 -32.649 1.00 10.97 ? 254  ILE A CG2   1 
ATOM   1956  C CD1   . ILE A  1  254 ? 85.777  -15.110 -31.095 1.00 12.84 ? 254  ILE A CD1   1 
ATOM   1957  N N     . VAL A  1  255 ? 82.559  -13.764 -35.932 1.00 7.16  ? 255  VAL A N     1 
ATOM   1958  C CA    . VAL A  1  255 ? 81.631  -12.841 -36.566 1.00 6.99  ? 255  VAL A CA    1 
ATOM   1959  C C     . VAL A  1  255 ? 80.497  -12.506 -35.602 1.00 5.81  ? 255  VAL A C     1 
ATOM   1960  O O     . VAL A  1  255 ? 79.775  -13.391 -35.142 1.00 6.88  ? 255  VAL A O     1 
ATOM   1961  C CB    . VAL A  1  255 ? 81.052  -13.452 -37.861 1.00 6.21  ? 255  VAL A CB    1 
ATOM   1962  C CG1   . VAL A  1  255 ? 80.223  -12.404 -38.607 1.00 7.47  ? 255  VAL A CG1   1 
ATOM   1963  C CG2   . VAL A  1  255 ? 82.189  -13.956 -38.746 1.00 8.43  ? 255  VAL A CG2   1 
ATOM   1964  N N     . SER A  1  256 ? 80.364  -11.218 -35.294 1.00 5.89  ? 256  SER A N     1 
ATOM   1965  C CA    . SER A  1  256 ? 79.335  -10.720 -34.387 1.00 5.90  ? 256  SER A CA    1 
ATOM   1966  C C     . SER A  1  256 ? 78.679  -9.532  -35.079 1.00 6.51  ? 256  SER A C     1 
ATOM   1967  O O     . SER A  1  256 ? 78.392  -8.508  -34.452 1.00 6.59  ? 256  SER A O     1 
ATOM   1968  C CB    . SER A  1  256 ? 79.975  -10.267 -33.070 1.00 7.24  ? 256  SER A CB    1 
ATOM   1969  O OG    . SER A  1  256 ? 80.664  -11.339 -32.443 1.00 7.66  ? 256  SER A OG    1 
ATOM   1970  N N     . ALA A  1  257 ? 78.438  -9.689  -36.378 1.00 5.95  ? 257  ALA A N     1 
ATOM   1971  C CA    . ALA A  1  257 ? 77.860  -8.636  -37.207 1.00 5.42  ? 257  ALA A CA    1 
ATOM   1972  C C     . ALA A  1  257 ? 76.338  -8.546  -37.161 1.00 7.49  ? 257  ALA A C     1 
ATOM   1973  O O     . ALA A  1  257 ? 75.737  -7.782  -37.919 1.00 7.81  ? 257  ALA A O     1 
ATOM   1974  C CB    . ALA A  1  257 ? 78.330  -8.808  -38.646 1.00 5.91  ? 257  ALA A CB    1 
ATOM   1975  N N     . GLY A  1  258 ? 75.719  -9.328  -36.281 1.00 5.75  ? 258  GLY A N     1 
ATOM   1976  C CA    . GLY A  1  258 ? 74.274  -9.291  -36.141 1.00 7.39  ? 258  GLY A CA    1 
ATOM   1977  C C     . GLY A  1  258 ? 73.473  -10.207 -37.044 1.00 7.52  ? 258  GLY A C     1 
ATOM   1978  O O     . GLY A  1  258 ? 74.001  -10.799 -37.986 1.00 7.48  ? 258  GLY A O     1 
ATOM   1979  N N     . THR A  1  259 ? 72.183  -10.312 -36.741 1.00 6.93  ? 259  THR A N     1 
ATOM   1980  C CA    . THR A  1  259 ? 71.245  -11.137 -37.495 1.00 6.88  ? 259  THR A CA    1 
ATOM   1981  C C     . THR A  1  259 ? 71.298  -10.843 -38.993 1.00 7.42  ? 259  THR A C     1 
ATOM   1982  O O     . THR A  1  259 ? 71.192  -11.750 -39.818 1.00 7.57  ? 259  THR A O     1 
ATOM   1983  C CB    . THR A  1  259 ? 69.804  -10.903 -36.984 1.00 7.52  ? 259  THR A CB    1 
ATOM   1984  O OG1   . THR A  1  259 ? 69.719  -11.320 -35.615 1.00 9.10  ? 259  THR A OG1   1 
ATOM   1985  C CG2   . THR A  1  259 ? 68.791  -11.676 -37.817 1.00 6.44  ? 259  THR A CG2   1 
ATOM   1986  N N     . ILE A  1  260 ? 71.462  -9.572  -39.344 1.00 6.93  ? 260  ILE A N     1 
ATOM   1987  C CA    . ILE A  1  260 ? 71.519  -9.188  -40.747 1.00 7.62  ? 260  ILE A CA    1 
ATOM   1988  C C     . ILE A  1  260 ? 72.942  -9.244  -41.304 1.00 8.37  ? 260  ILE A C     1 
ATOM   1989  O O     . ILE A  1  260 ? 73.173  -9.800  -42.377 1.00 9.19  ? 260  ILE A O     1 
ATOM   1990  C CB    . ILE A  1  260 ? 70.964  -7.752  -40.955 1.00 9.38  ? 260  ILE A CB    1 
ATOM   1991  C CG1   . ILE A  1  260 ? 69.533  -7.651  -40.415 1.00 11.06 ? 260  ILE A CG1   1 
ATOM   1992  C CG2   . ILE A  1  260 ? 71.015  -7.382  -42.427 1.00 8.95  ? 260  ILE A CG2   1 
ATOM   1993  C CD1   . ILE A  1  260 ? 68.530  -8.544  -41.112 1.00 15.12 ? 260  ILE A CD1   1 
ATOM   1994  N N     . GLY A  1  261 ? 73.891  -8.681  -40.559 1.00 7.91  ? 261  GLY A N     1 
ATOM   1995  C CA    . GLY A  1  261 ? 75.272  -8.639  -41.008 1.00 7.28  ? 261  GLY A CA    1 
ATOM   1996  C C     . GLY A  1  261 ? 76.079  -9.925  -41.052 1.00 6.98  ? 261  GLY A C     1 
ATOM   1997  O O     . GLY A  1  261 ? 76.942  -10.076 -41.915 1.00 7.53  ? 261  GLY A O     1 
ATOM   1998  N N     . THR A  1  262 ? 75.824  -10.846 -40.132 1.00 7.47  ? 262  THR A N     1 
ATOM   1999  C CA    . THR A  1  262 ? 76.581  -12.093 -40.115 1.00 6.63  ? 262  THR A CA    1 
ATOM   2000  C C     . THR A  1  262 ? 76.285  -12.991 -41.317 1.00 7.42  ? 262  THR A C     1 
ATOM   2001  O O     . THR A  1  262 ? 77.209  -13.399 -42.024 1.00 8.09  ? 262  THR A O     1 
ATOM   2002  C CB    . THR A  1  262 ? 76.361  -12.839 -38.786 1.00 6.51  ? 262  THR A CB    1 
ATOM   2003  O OG1   . THR A  1  262 ? 77.019  -12.112 -37.741 1.00 7.32  ? 262  THR A OG1   1 
ATOM   2004  C CG2   . THR A  1  262 ? 76.929  -14.252 -38.845 1.00 8.47  ? 262  THR A CG2   1 
ATOM   2005  N N     . PRO A  1  263 ? 75.005  -13.304 -41.579 1.00 7.12  ? 263  PRO A N     1 
ATOM   2006  C CA    . PRO A  1  263 ? 74.729  -14.159 -42.739 1.00 7.43  ? 263  PRO A CA    1 
ATOM   2007  C C     . PRO A  1  263 ? 75.222  -13.502 -44.032 1.00 7.84  ? 263  PRO A C     1 
ATOM   2008  O O     . PRO A  1  263 ? 75.714  -14.176 -44.934 1.00 8.10  ? 263  PRO A O     1 
ATOM   2009  C CB    . PRO A  1  263 ? 73.206  -14.303 -42.712 1.00 8.48  ? 263  PRO A CB    1 
ATOM   2010  C CG    . PRO A  1  263 ? 72.878  -14.188 -41.253 1.00 8.72  ? 263  PRO A CG    1 
ATOM   2011  C CD    . PRO A  1  263 ? 73.779  -13.058 -40.799 1.00 7.83  ? 263  PRO A CD    1 
ATOM   2012  N N     . GLN A  1  264 ? 75.088  -12.180 -44.117 1.00 8.47  ? 264  GLN A N     1 
ATOM   2013  C CA    . GLN A  1  264 ? 75.534  -11.449 -45.300 1.00 7.44  ? 264  GLN A CA    1 
ATOM   2014  C C     . GLN A  1  264 ? 77.028  -11.637 -45.545 1.00 7.41  ? 264  GLN A C     1 
ATOM   2015  O O     . GLN A  1  264 ? 77.452  -11.909 -46.671 1.00 7.80  ? 264  GLN A O     1 
ATOM   2016  C CB    . GLN A  1  264 ? 75.233  -9.955  -45.154 1.00 6.18  ? 264  GLN A CB    1 
ATOM   2017  C CG    . GLN A  1  264 ? 75.821  -9.110  -46.274 1.00 8.02  ? 264  GLN A CG    1 
ATOM   2018  C CD    . GLN A  1  264 ? 75.645  -7.622  -46.038 1.00 10.48 ? 264  GLN A CD    1 
ATOM   2019  O OE1   . GLN A  1  264 ? 75.844  -7.132  -44.928 1.00 10.23 ? 264  GLN A OE1   1 
ATOM   2020  N NE2   . GLN A  1  264 ? 75.288  -6.893  -47.090 1.00 8.99  ? 264  GLN A NE2   1 
ATOM   2021  N N     . LEU A  1  265 ? 77.827  -11.484 -44.491 1.00 6.65  ? 265  LEU A N     1 
ATOM   2022  C CA    . LEU A  1  265 ? 79.271  -11.635 -44.616 1.00 7.51  ? 265  LEU A CA    1 
ATOM   2023  C C     . LEU A  1  265 ? 79.656  -13.069 -44.977 1.00 6.70  ? 265  LEU A C     1 
ATOM   2024  O O     . LEU A  1  265 ? 80.556  -13.282 -45.788 1.00 7.23  ? 265  LEU A O     1 
ATOM   2025  C CB    . LEU A  1  265 ? 79.970  -11.219 -43.318 1.00 7.55  ? 265  LEU A CB    1 
ATOM   2026  C CG    . LEU A  1  265 ? 81.495  -11.364 -43.344 1.00 7.66  ? 265  LEU A CG    1 
ATOM   2027  C CD1   . LEU A  1  265 ? 82.086  -10.517 -44.461 1.00 9.03  ? 265  LEU A CD1   1 
ATOM   2028  C CD2   . LEU A  1  265 ? 82.070  -10.948 -41.999 1.00 9.14  ? 265  LEU A CD2   1 
ATOM   2029  N N     . LEU A  1  266 ? 78.980  -14.047 -44.378 1.00 8.11  ? 266  LEU A N     1 
ATOM   2030  C CA    . LEU A  1  266 ? 79.268  -15.446 -44.673 1.00 7.17  ? 266  LEU A CA    1 
ATOM   2031  C C     . LEU A  1  266 ? 78.997  -15.732 -46.150 1.00 6.62  ? 266  LEU A C     1 
ATOM   2032  O O     . LEU A  1  266 ? 79.823  -16.332 -46.831 1.00 7.61  ? 266  LEU A O     1 
ATOM   2033  C CB    . LEU A  1  266 ? 78.423  -16.369 -43.787 1.00 7.61  ? 266  LEU A CB    1 
ATOM   2034  C CG    . LEU A  1  266 ? 78.849  -16.429 -42.315 1.00 8.26  ? 266  LEU A CG    1 
ATOM   2035  C CD1   . LEU A  1  266 ? 77.846  -17.255 -41.521 1.00 8.41  ? 266  LEU A CD1   1 
ATOM   2036  C CD2   . LEU A  1  266 ? 80.249  -17.035 -42.209 1.00 8.90  ? 266  LEU A CD2   1 
ATOM   2037  N N     . LEU A  1  267 ? 77.845  -15.288 -46.646 1.00 7.33  ? 267  LEU A N     1 
ATOM   2038  C CA    . LEU A  1  267 ? 77.501  -15.496 -48.048 1.00 7.78  ? 267  LEU A CA    1 
ATOM   2039  C C     . LEU A  1  267 ? 78.536  -14.833 -48.955 1.00 8.21  ? 267  LEU A C     1 
ATOM   2040  O O     . LEU A  1  267 ? 79.034  -15.448 -49.894 1.00 9.71  ? 267  LEU A O     1 
ATOM   2041  C CB    . LEU A  1  267 ? 76.110  -14.928 -48.346 1.00 7.92  ? 267  LEU A CB    1 
ATOM   2042  C CG    . LEU A  1  267 ? 74.942  -15.639 -47.655 1.00 7.07  ? 267  LEU A CG    1 
ATOM   2043  C CD1   . LEU A  1  267 ? 73.639  -14.898 -47.942 1.00 8.92  ? 267  LEU A CD1   1 
ATOM   2044  C CD2   . LEU A  1  267 ? 74.854  -17.082 -48.145 1.00 8.61  ? 267  LEU A CD2   1 
ATOM   2045  N N     . LEU A  1  268 ? 78.859  -13.577 -48.669 1.00 8.03  ? 268  LEU A N     1 
ATOM   2046  C CA    . LEU A  1  268 ? 79.834  -12.847 -49.467 1.00 8.52  ? 268  LEU A CA    1 
ATOM   2047  C C     . LEU A  1  268 ? 81.210  -13.505 -49.438 1.00 9.52  ? 268  LEU A C     1 
ATOM   2048  O O     . LEU A  1  268 ? 82.020  -13.307 -50.346 1.00 11.68 ? 268  LEU A O     1 
ATOM   2049  C CB    . LEU A  1  268 ? 79.946  -11.401 -48.974 1.00 8.20  ? 268  LEU A CB    1 
ATOM   2050  C CG    . LEU A  1  268 ? 78.799  -10.460 -49.347 1.00 8.79  ? 268  LEU A CG    1 
ATOM   2051  C CD1   . LEU A  1  268 ? 78.925  -9.154  -48.571 1.00 8.88  ? 268  LEU A CD1   1 
ATOM   2052  C CD2   . LEU A  1  268 ? 78.825  -10.205 -50.855 1.00 8.50  ? 268  LEU A CD2   1 
ATOM   2053  N N     . SER A  1  269 ? 81.463  -14.292 -48.395 1.00 8.23  ? 269  SER A N     1 
ATOM   2054  C CA    . SER A  1  269 ? 82.742  -14.975 -48.231 1.00 8.73  ? 269  SER A CA    1 
ATOM   2055  C C     . SER A  1  269 ? 82.745  -16.400 -48.777 1.00 10.03 ? 269  SER A C     1 
ATOM   2056  O O     . SER A  1  269 ? 83.724  -17.129 -48.617 1.00 11.49 ? 269  SER A O     1 
ATOM   2057  C CB    . SER A  1  269 ? 83.133  -14.995 -46.752 1.00 9.50  ? 269  SER A CB    1 
ATOM   2058  O OG    . SER A  1  269 ? 83.230  -13.673 -46.253 1.00 8.29  ? 269  SER A OG    1 
ATOM   2059  N N     . GLY A  1  270 ? 81.646  -16.801 -49.406 1.00 9.66  ? 270  GLY A N     1 
ATOM   2060  C CA    . GLY A  1  270 ? 81.582  -18.135 -49.977 1.00 9.57  ? 270  GLY A CA    1 
ATOM   2061  C C     . GLY A  1  270 ? 81.114  -19.252 -49.064 1.00 10.18 ? 270  GLY A C     1 
ATOM   2062  O O     . GLY A  1  270 ? 81.335  -20.427 -49.363 1.00 10.65 ? 270  GLY A O     1 
ATOM   2063  N N     . VAL A  1  271 ? 80.479  -18.907 -47.950 1.00 8.15  ? 271  VAL A N     1 
ATOM   2064  C CA    . VAL A  1  271 ? 79.970  -19.922 -47.033 1.00 9.54  ? 271  VAL A CA    1 
ATOM   2065  C C     . VAL A  1  271 ? 78.448  -19.833 -47.034 1.00 10.56 ? 271  VAL A C     1 
ATOM   2066  O O     . VAL A  1  271 ? 77.864  -18.928 -46.433 1.00 10.61 ? 271  VAL A O     1 
ATOM   2067  C CB    . VAL A  1  271 ? 80.505  -19.712 -45.598 1.00 8.75  ? 271  VAL A CB    1 
ATOM   2068  C CG1   . VAL A  1  271 ? 79.950  -20.782 -44.672 1.00 9.63  ? 271  VAL A CG1   1 
ATOM   2069  C CG2   . VAL A  1  271 ? 82.022  -19.764 -45.599 1.00 8.86  ? 271  VAL A CG2   1 
ATOM   2070  N N     . GLY A  1  272 ? 77.812  -20.770 -47.731 1.00 9.46  ? 272  GLY A N     1 
ATOM   2071  C CA    . GLY A  1  272 ? 76.365  -20.777 -47.821 1.00 10.62 ? 272  GLY A CA    1 
ATOM   2072  C C     . GLY A  1  272 ? 75.882  -21.794 -48.838 1.00 10.26 ? 272  GLY A C     1 
ATOM   2073  O O     . GLY A  1  272 ? 76.665  -22.641 -49.272 1.00 9.93  ? 272  GLY A O     1 
ATOM   2074  N N     . PRO A  1  273 ? 74.602  -21.733 -49.245 1.00 11.61 ? 273  PRO A N     1 
ATOM   2075  C CA    . PRO A  1  273 ? 74.020  -22.662 -50.220 1.00 12.40 ? 273  PRO A CA    1 
ATOM   2076  C C     . PRO A  1  273 ? 74.825  -22.690 -51.516 1.00 13.21 ? 273  PRO A C     1 
ATOM   2077  O O     . PRO A  1  273 ? 74.957  -21.678 -52.200 1.00 11.39 ? 273  PRO A O     1 
ATOM   2078  C CB    . PRO A  1  273 ? 72.613  -22.108 -50.423 1.00 13.91 ? 273  PRO A CB    1 
ATOM   2079  C CG    . PRO A  1  273 ? 72.308  -21.480 -49.094 1.00 12.67 ? 273  PRO A CG    1 
ATOM   2080  C CD    . PRO A  1  273 ? 73.594  -20.756 -48.799 1.00 13.00 ? 273  PRO A CD    1 
ATOM   2081  N N     . GLU A  1  274 ? 75.351  -23.861 -51.850 1.00 13.13 ? 274  GLU A N     1 
ATOM   2082  C CA    . GLU A  1  274 ? 76.163  -24.025 -53.046 1.00 14.18 ? 274  GLU A CA    1 
ATOM   2083  C C     . GLU A  1  274 ? 75.515  -23.499 -54.329 1.00 13.35 ? 274  GLU A C     1 
ATOM   2084  O O     . GLU A  1  274 ? 76.120  -22.706 -55.048 1.00 12.48 ? 274  GLU A O     1 
ATOM   2085  C CB    . GLU A  1  274 ? 76.535  -25.503 -53.203 1.00 18.33 ? 274  GLU A CB    1 
ATOM   2086  C CG    . GLU A  1  274 ? 77.518  -25.793 -54.317 1.00 24.73 ? 274  GLU A CG    1 
ATOM   2087  C CD    . GLU A  1  274 ? 78.258  -27.097 -54.098 1.00 29.50 ? 274  GLU A CD    1 
ATOM   2088  O OE1   . GLU A  1  274 ? 77.592  -28.132 -53.874 1.00 32.54 ? 274  GLU A OE1   1 
ATOM   2089  O OE2   . GLU A  1  274 ? 79.507  -27.084 -54.149 1.00 32.62 ? 274  GLU A OE2   1 
ATOM   2090  N N     . SER A  1  275 ? 74.291  -23.928 -54.620 1.00 12.58 ? 275  SER A N     1 
ATOM   2091  C CA    . SER A  1  275 ? 73.618  -23.480 -55.838 1.00 12.05 ? 275  SER A CA    1 
ATOM   2092  C C     . SER A  1  275 ? 73.358  -21.974 -55.835 1.00 12.04 ? 275  SER A C     1 
ATOM   2093  O O     . SER A  1  275 ? 73.425  -21.323 -56.878 1.00 12.26 ? 275  SER A O     1 
ATOM   2094  C CB    . SER A  1  275 ? 72.304  -24.244 -56.034 1.00 15.86 ? 275  SER A CB    1 
ATOM   2095  O OG    . SER A  1  275 ? 71.450  -24.099 -54.917 1.00 20.38 ? 275  SER A OG    1 
ATOM   2096  N N     . TYR A  1  276 ? 73.063  -21.419 -54.665 1.00 10.66 ? 276  TYR A N     1 
ATOM   2097  C CA    . TYR A  1  276 ? 72.814  -19.986 -54.559 1.00 9.52  ? 276  TYR A CA    1 
ATOM   2098  C C     . TYR A  1  276 ? 74.091  -19.202 -54.853 1.00 8.55  ? 276  TYR A C     1 
ATOM   2099  O O     . TYR A  1  276 ? 74.096  -18.294 -55.684 1.00 10.02 ? 276  TYR A O     1 
ATOM   2100  C CB    . TYR A  1  276 ? 72.307  -19.633 -53.160 1.00 8.85  ? 276  TYR A CB    1 
ATOM   2101  C CG    . TYR A  1  276 ? 72.157  -18.145 -52.935 1.00 10.00 ? 276  TYR A CG    1 
ATOM   2102  C CD1   . TYR A  1  276 ? 71.120  -17.428 -53.529 1.00 11.46 ? 276  TYR A CD1   1 
ATOM   2103  C CD2   . TYR A  1  276 ? 73.071  -17.450 -52.146 1.00 10.96 ? 276  TYR A CD2   1 
ATOM   2104  C CE1   . TYR A  1  276 ? 70.997  -16.049 -53.340 1.00 11.04 ? 276  TYR A CE1   1 
ATOM   2105  C CE2   . TYR A  1  276 ? 72.960  -16.079 -51.954 1.00 12.39 ? 276  TYR A CE2   1 
ATOM   2106  C CZ    . TYR A  1  276 ? 71.923  -15.385 -52.551 1.00 12.39 ? 276  TYR A CZ    1 
ATOM   2107  O OH    . TYR A  1  276 ? 71.815  -14.029 -52.356 1.00 13.86 ? 276  TYR A OH    1 
ATOM   2108  N N     . LEU A  1  277 ? 75.177  -19.558 -54.174 1.00 8.14  ? 277  LEU A N     1 
ATOM   2109  C CA    . LEU A  1  277 ? 76.447  -18.870 -54.380 1.00 8.69  ? 277  LEU A CA    1 
ATOM   2110  C C     . LEU A  1  277 ? 76.904  -18.972 -55.832 1.00 9.58  ? 277  LEU A C     1 
ATOM   2111  O O     . LEU A  1  277 ? 77.303  -17.978 -56.434 1.00 10.44 ? 277  LEU A O     1 
ATOM   2112  C CB    . LEU A  1  277 ? 77.526  -19.443 -53.454 1.00 7.95  ? 277  LEU A CB    1 
ATOM   2113  C CG    . LEU A  1  277 ? 77.298  -19.234 -51.952 1.00 9.53  ? 277  LEU A CG    1 
ATOM   2114  C CD1   . LEU A  1  277 ? 78.416  -19.908 -51.167 1.00 11.83 ? 277  LEU A CD1   1 
ATOM   2115  C CD2   . LEU A  1  277 ? 77.255  -17.744 -51.641 1.00 10.38 ? 277  LEU A CD2   1 
ATOM   2116  N N     . SER A  1  278 ? 76.842  -20.174 -56.393 1.00 9.52  ? 278  SER A N     1 
ATOM   2117  C CA    . SER A  1  278 ? 77.259  -20.374 -57.777 1.00 10.31 ? 278  SER A CA    1 
ATOM   2118  C C     . SER A  1  278 ? 76.445  -19.523 -58.744 1.00 9.52  ? 278  SER A C     1 
ATOM   2119  O O     . SER A  1  278 ? 76.988  -18.990 -59.712 1.00 11.30 ? 278  SER A O     1 
ATOM   2120  C CB    . SER A  1  278 ? 77.136  -21.850 -58.163 1.00 12.23 ? 278  SER A CB    1 
ATOM   2121  O OG    A SER A  1  278 ? 78.038  -22.646 -57.414 0.50 12.79 ? 278  SER A OG    1 
ATOM   2122  O OG    B SER A  1  278 ? 77.574  -22.059 -59.494 0.50 12.80 ? 278  SER A OG    1 
ATOM   2123  N N     . SER A  1  279 ? 75.147  -19.390 -58.483 1.00 9.70  ? 279  SER A N     1 
ATOM   2124  C CA    . SER A  1  279 ? 74.284  -18.602 -59.362 1.00 10.79 ? 279  SER A CA    1 
ATOM   2125  C C     . SER A  1  279 ? 74.752  -17.158 -59.440 1.00 10.49 ? 279  SER A C     1 
ATOM   2126  O O     . SER A  1  279 ? 74.484  -16.464 -60.420 1.00 10.88 ? 279  SER A O     1 
ATOM   2127  C CB    . SER A  1  279 ? 72.834  -18.625 -58.872 1.00 10.40 ? 279  SER A CB    1 
ATOM   2128  O OG    . SER A  1  279 ? 72.660  -17.783 -57.742 1.00 12.58 ? 279  SER A OG    1 
ATOM   2129  N N     . LEU A  1  280 ? 75.452  -16.707 -58.405 1.00 9.76  ? 280  LEU A N     1 
ATOM   2130  C CA    . LEU A  1  280 ? 75.942  -15.335 -58.362 1.00 10.28 ? 280  LEU A CA    1 
ATOM   2131  C C     . LEU A  1  280 ? 77.437  -15.250 -58.650 1.00 10.50 ? 280  LEU A C     1 
ATOM   2132  O O     . LEU A  1  280 ? 78.035  -14.176 -58.564 1.00 11.01 ? 280  LEU A O     1 
ATOM   2133  C CB    . LEU A  1  280 ? 75.636  -14.715 -56.993 1.00 9.59  ? 280  LEU A CB    1 
ATOM   2134  C CG    . LEU A  1  280 ? 74.155  -14.609 -56.615 1.00 11.62 ? 280  LEU A CG    1 
ATOM   2135  C CD1   . LEU A  1  280 ? 74.031  -14.016 -55.218 1.00 10.82 ? 280  LEU A CD1   1 
ATOM   2136  C CD2   . LEU A  1  280 ? 73.420  -13.742 -57.633 1.00 11.33 ? 280  LEU A CD2   1 
ATOM   2137  N N     . ASN A  1  281 ? 78.033  -16.387 -58.992 1.00 10.29 ? 281  ASN A N     1 
ATOM   2138  C CA    . ASN A  1  281 ? 79.456  -16.451 -59.301 1.00 12.51 ? 281  ASN A CA    1 
ATOM   2139  C C     . ASN A  1  281 ? 80.344  -16.172 -58.095 1.00 12.41 ? 281  ASN A C     1 
ATOM   2140  O O     . ASN A  1  281 ? 81.459  -15.672 -58.234 1.00 13.75 ? 281  ASN A O     1 
ATOM   2141  C CB    . ASN A  1  281 ? 79.791  -15.484 -60.438 1.00 12.92 ? 281  ASN A CB    1 
ATOM   2142  C CG    . ASN A  1  281 ? 79.160  -15.901 -61.747 1.00 14.04 ? 281  ASN A CG    1 
ATOM   2143  O OD1   . ASN A  1  281 ? 78.873  -15.069 -62.607 1.00 17.85 ? 281  ASN A OD1   1 
ATOM   2144  N ND2   . ASN A  1  281 ? 78.949  -17.201 -61.909 1.00 13.84 ? 281  ASN A ND2   1 
ATOM   2145  N N     . ILE A  1  282 ? 79.834  -16.477 -56.907 1.00 10.68 ? 282  ILE A N     1 
ATOM   2146  C CA    . ILE A  1  282 ? 80.616  -16.308 -55.691 1.00 10.69 ? 282  ILE A CA    1 
ATOM   2147  C C     . ILE A  1  282 ? 81.266  -17.675 -55.464 1.00 11.18 ? 282  ILE A C     1 
ATOM   2148  O O     . ILE A  1  282 ? 80.573  -18.685 -55.334 1.00 11.44 ? 282  ILE A O     1 
ATOM   2149  C CB    . ILE A  1  282 ? 79.720  -15.954 -54.482 1.00 9.58  ? 282  ILE A CB    1 
ATOM   2150  C CG1   . ILE A  1  282 ? 79.103  -14.564 -54.677 1.00 9.72  ? 282  ILE A CG1   1 
ATOM   2151  C CG2   . ILE A  1  282 ? 80.541  -15.998 -53.196 1.00 10.24 ? 282  ILE A CG2   1 
ATOM   2152  C CD1   . ILE A  1  282 ? 78.084  -14.184 -53.607 1.00 10.66 ? 282  ILE A CD1   1 
ATOM   2153  N N     . PRO A  1  283 ? 82.609  -17.731 -55.447 1.00 12.52 ? 283  PRO A N     1 
ATOM   2154  C CA    . PRO A  1  283 ? 83.282  -19.015 -55.235 1.00 12.28 ? 283  PRO A CA    1 
ATOM   2155  C C     . PRO A  1  283 ? 82.817  -19.677 -53.948 1.00 12.22 ? 283  PRO A C     1 
ATOM   2156  O O     . PRO A  1  283 ? 82.698  -19.021 -52.912 1.00 13.60 ? 283  PRO A O     1 
ATOM   2157  C CB    . PRO A  1  283 ? 84.756  -18.627 -55.182 1.00 13.19 ? 283  PRO A CB    1 
ATOM   2158  C CG    . PRO A  1  283 ? 84.819  -17.439 -56.086 1.00 14.92 ? 283  PRO A CG    1 
ATOM   2159  C CD    . PRO A  1  283 ? 83.592  -16.659 -55.675 1.00 12.75 ? 283  PRO A CD    1 
ATOM   2160  N N     . VAL A  1  284 ? 82.554  -20.976 -54.017 1.00 12.55 ? 284  VAL A N     1 
ATOM   2161  C CA    . VAL A  1  284 ? 82.101  -21.716 -52.848 1.00 12.75 ? 284  VAL A CA    1 
ATOM   2162  C C     . VAL A  1  284 ? 83.276  -22.201 -51.999 1.00 14.30 ? 284  VAL A C     1 
ATOM   2163  O O     . VAL A  1  284 ? 84.085  -23.016 -52.447 1.00 15.18 ? 284  VAL A O     1 
ATOM   2164  C CB    . VAL A  1  284 ? 81.254  -22.944 -53.255 1.00 12.68 ? 284  VAL A CB    1 
ATOM   2165  C CG1   . VAL A  1  284 ? 80.770  -23.675 -52.016 1.00 12.49 ? 284  VAL A CG1   1 
ATOM   2166  C CG2   . VAL A  1  284 ? 80.074  -22.504 -54.110 1.00 14.28 ? 284  VAL A CG2   1 
ATOM   2167  N N     . VAL A  1  285 ? 83.370  -21.685 -50.778 1.00 12.69 ? 285  VAL A N     1 
ATOM   2168  C CA    . VAL A  1  285 ? 84.426  -22.088 -49.858 1.00 12.64 ? 285  VAL A CA    1 
ATOM   2169  C C     . VAL A  1  285 ? 83.950  -23.362 -49.170 1.00 12.68 ? 285  VAL A C     1 
ATOM   2170  O O     . VAL A  1  285 ? 84.708  -24.321 -49.017 1.00 13.39 ? 285  VAL A O     1 
ATOM   2171  C CB    . VAL A  1  285 ? 84.705  -20.991 -48.809 1.00 12.81 ? 285  VAL A CB    1 
ATOM   2172  C CG1   . VAL A  1  285 ? 85.623  -21.527 -47.715 1.00 13.82 ? 285  VAL A CG1   1 
ATOM   2173  C CG2   . VAL A  1  285 ? 85.349  -19.789 -49.490 1.00 12.87 ? 285  VAL A CG2   1 
ATOM   2174  N N     . LEU A  1  286 ? 82.683  -23.366 -48.769 1.00 11.59 ? 286  LEU A N     1 
ATOM   2175  C CA    . LEU A  1  286 ? 82.076  -24.527 -48.129 1.00 11.86 ? 286  LEU A CA    1 
ATOM   2176  C C     . LEU A  1  286 ? 80.562  -24.455 -48.255 1.00 13.11 ? 286  LEU A C     1 
ATOM   2177  O O     . LEU A  1  286 ? 79.944  -23.456 -47.880 1.00 12.87 ? 286  LEU A O     1 
ATOM   2178  C CB    . LEU A  1  286 ? 82.456  -24.606 -46.645 1.00 12.19 ? 286  LEU A CB    1 
ATOM   2179  C CG    . LEU A  1  286 ? 81.886  -25.822 -45.902 1.00 13.04 ? 286  LEU A CG    1 
ATOM   2180  C CD1   . LEU A  1  286 ? 82.460  -27.093 -46.507 1.00 13.84 ? 286  LEU A CD1   1 
ATOM   2181  C CD2   . LEU A  1  286 ? 82.223  -25.747 -44.417 1.00 12.77 ? 286  LEU A CD2   1 
ATOM   2182  N N     . SER A  1  287 ? 79.969  -25.512 -48.801 1.00 12.20 ? 287  SER A N     1 
ATOM   2183  C CA    . SER A  1  287 ? 78.524  -25.569 -48.956 1.00 12.73 ? 287  SER A CA    1 
ATOM   2184  C C     . SER A  1  287 ? 77.906  -25.606 -47.563 1.00 12.28 ? 287  SER A C     1 
ATOM   2185  O O     . SER A  1  287 ? 78.191  -26.504 -46.772 1.00 13.71 ? 287  SER A O     1 
ATOM   2186  C CB    . SER A  1  287 ? 78.121  -26.819 -49.739 1.00 15.66 ? 287  SER A CB    1 
ATOM   2187  O OG    . SER A  1  287 ? 76.715  -26.884 -49.892 1.00 18.37 ? 287  SER A OG    1 
ATOM   2188  N N     . HIS A  1  288 ? 77.072  -24.614 -47.269 1.00 11.62 ? 288  HIS A N     1 
ATOM   2189  C CA    . HIS A  1  288 ? 76.405  -24.496 -45.974 1.00 11.49 ? 288  HIS A CA    1 
ATOM   2190  C C     . HIS A  1  288 ? 74.979  -24.062 -46.278 1.00 11.56 ? 288  HIS A C     1 
ATOM   2191  O O     . HIS A  1  288 ? 74.671  -22.871 -46.316 1.00 11.04 ? 288  HIS A O     1 
ATOM   2192  C CB    . HIS A  1  288 ? 77.118  -23.445 -45.119 1.00 12.70 ? 288  HIS A CB    1 
ATOM   2193  C CG    . HIS A  1  288 ? 77.731  -24.000 -43.871 1.00 13.78 ? 288  HIS A CG    1 
ATOM   2194  N ND1   . HIS A  1  288 ? 76.978  -24.455 -42.813 1.00 15.06 ? 288  HIS A ND1   1 
ATOM   2195  C CD2   . HIS A  1  288 ? 79.027  -24.182 -43.519 1.00 14.14 ? 288  HIS A CD2   1 
ATOM   2196  C CE1   . HIS A  1  288 ? 77.782  -24.895 -41.859 1.00 14.58 ? 288  HIS A CE1   1 
ATOM   2197  N NE2   . HIS A  1  288 ? 79.029  -24.740 -42.263 1.00 13.84 ? 288  HIS A NE2   1 
ATOM   2198  N N     . PRO A  1  289 ? 74.085  -25.036 -46.492 1.00 11.16 ? 289  PRO A N     1 
ATOM   2199  C CA    . PRO A  1  289 ? 72.678  -24.788 -46.815 1.00 11.94 ? 289  PRO A CA    1 
ATOM   2200  C C     . PRO A  1  289 ? 71.840  -23.879 -45.927 1.00 10.96 ? 289  PRO A C     1 
ATOM   2201  O O     . PRO A  1  289 ? 70.901  -23.249 -46.415 1.00 11.46 ? 289  PRO A O     1 
ATOM   2202  C CB    . PRO A  1  289 ? 72.093  -26.200 -46.911 1.00 13.75 ? 289  PRO A CB    1 
ATOM   2203  C CG    . PRO A  1  289 ? 72.941  -26.986 -45.971 1.00 14.84 ? 289  PRO A CG    1 
ATOM   2204  C CD    . PRO A  1  289 ? 74.325  -26.476 -46.293 1.00 13.77 ? 289  PRO A CD    1 
ATOM   2205  N N     . TYR A  1  290 ? 72.171  -23.784 -44.645 1.00 10.09 ? 290  TYR A N     1 
ATOM   2206  C CA    . TYR A  1  290 ? 71.358  -22.975 -43.749 1.00 9.98  ? 290  TYR A CA    1 
ATOM   2207  C C     . TYR A  1  290 ? 71.813  -21.552 -43.444 1.00 9.36  ? 290  TYR A C     1 
ATOM   2208  O O     . TYR A  1  290 ? 71.190  -20.871 -42.631 1.00 9.43  ? 290  TYR A O     1 
ATOM   2209  C CB    . TYR A  1  290 ? 71.117  -23.752 -42.452 1.00 11.11 ? 290  TYR A CB    1 
ATOM   2210  C CG    . TYR A  1  290 ? 70.455  -25.088 -42.713 1.00 13.57 ? 290  TYR A CG    1 
ATOM   2211  C CD1   . TYR A  1  290 ? 71.102  -26.284 -42.409 1.00 14.38 ? 290  TYR A CD1   1 
ATOM   2212  C CD2   . TYR A  1  290 ? 69.199  -25.154 -43.314 1.00 13.67 ? 290  TYR A CD2   1 
ATOM   2213  C CE1   . TYR A  1  290 ? 70.515  -27.516 -42.703 1.00 16.65 ? 290  TYR A CE1   1 
ATOM   2214  C CE2   . TYR A  1  290 ? 68.604  -26.378 -43.613 1.00 17.19 ? 290  TYR A CE2   1 
ATOM   2215  C CZ    . TYR A  1  290 ? 69.268  -27.553 -43.307 1.00 18.34 ? 290  TYR A CZ    1 
ATOM   2216  O OH    . TYR A  1  290 ? 68.692  -28.764 -43.620 1.00 20.37 ? 290  TYR A OH    1 
ATOM   2217  N N     . VAL A  1  291 ? 72.885  -21.094 -44.087 1.00 8.81  ? 291  VAL A N     1 
ATOM   2218  C CA    . VAL A  1  291 ? 73.338  -19.723 -43.867 1.00 8.03  ? 291  VAL A CA    1 
ATOM   2219  C C     . VAL A  1  291 ? 72.277  -18.793 -44.460 1.00 9.71  ? 291  VAL A C     1 
ATOM   2220  O O     . VAL A  1  291 ? 71.929  -18.905 -45.636 1.00 8.91  ? 291  VAL A O     1 
ATOM   2221  C CB    . VAL A  1  291 ? 74.694  -19.442 -44.562 1.00 7.17  ? 291  VAL A CB    1 
ATOM   2222  C CG1   . VAL A  1  291 ? 75.025  -17.949 -44.484 1.00 6.91  ? 291  VAL A CG1   1 
ATOM   2223  C CG2   . VAL A  1  291 ? 75.802  -20.246 -43.890 1.00 7.73  ? 291  VAL A CG2   1 
ATOM   2224  N N     . GLY A  1  292 ? 71.756  -17.885 -43.640 1.00 8.64  ? 292  GLY A N     1 
ATOM   2225  C CA    . GLY A  1  292 ? 70.738  -16.967 -44.117 1.00 9.56  ? 292  GLY A CA    1 
ATOM   2226  C C     . GLY A  1  292 ? 69.338  -17.539 -44.005 1.00 10.20 ? 292  GLY A C     1 
ATOM   2227  O O     . GLY A  1  292 ? 68.367  -16.895 -44.389 1.00 10.47 ? 292  GLY A O     1 
ATOM   2228  N N     . GLN A  1  293 ? 69.229  -18.759 -43.490 1.00 8.84  ? 293  GLN A N     1 
ATOM   2229  C CA    . GLN A  1  293 ? 67.925  -19.390 -43.335 1.00 8.33  ? 293  GLN A CA    1 
ATOM   2230  C C     . GLN A  1  293 ? 67.438  -19.247 -41.903 1.00 9.00  ? 293  GLN A C     1 
ATOM   2231  O O     . GLN A  1  293 ? 68.229  -19.020 -40.988 1.00 8.97  ? 293  GLN A O     1 
ATOM   2232  C CB    . GLN A  1  293 ? 68.001  -20.875 -43.707 1.00 11.30 ? 293  GLN A CB    1 
ATOM   2233  C CG    . GLN A  1  293 ? 68.426  -21.127 -45.147 1.00 14.38 ? 293  GLN A CG    1 
ATOM   2234  C CD    . GLN A  1  293 ? 67.493  -20.478 -46.151 1.00 15.83 ? 293  GLN A CD    1 
ATOM   2235  O OE1   . GLN A  1  293 ? 66.302  -20.781 -46.193 1.00 20.42 ? 293  GLN A OE1   1 
ATOM   2236  N NE2   . GLN A  1  293 ? 68.034  -19.580 -46.967 1.00 19.01 ? 293  GLN A NE2   1 
ATOM   2237  N N     . PHE A  1  294 ? 66.128  -19.379 -41.722 1.00 9.52  ? 294  PHE A N     1 
ATOM   2238  C CA    . PHE A  1  294 ? 65.509  -19.288 -40.407 1.00 9.58  ? 294  PHE A CA    1 
ATOM   2239  C C     . PHE A  1  294 ? 65.666  -17.913 -39.760 1.00 9.16  ? 294  PHE A C     1 
ATOM   2240  O O     . PHE A  1  294 ? 66.198  -17.786 -38.656 1.00 10.55 ? 294  PHE A O     1 
ATOM   2241  C CB    . PHE A  1  294 ? 66.080  -20.376 -39.492 1.00 11.46 ? 294  PHE A CB    1 
ATOM   2242  C CG    . PHE A  1  294 ? 65.993  -21.757 -40.079 1.00 13.76 ? 294  PHE A CG    1 
ATOM   2243  C CD1   . PHE A  1  294 ? 67.141  -22.518 -40.273 1.00 15.74 ? 294  PHE A CD1   1 
ATOM   2244  C CD2   . PHE A  1  294 ? 64.765  -22.283 -40.471 1.00 17.75 ? 294  PHE A CD2   1 
ATOM   2245  C CE1   . PHE A  1  294 ? 67.071  -23.782 -40.855 1.00 17.91 ? 294  PHE A CE1   1 
ATOM   2246  C CE2   . PHE A  1  294 ? 64.684  -23.549 -41.054 1.00 18.65 ? 294  PHE A CE2   1 
ATOM   2247  C CZ    . PHE A  1  294 ? 65.840  -24.299 -41.247 1.00 19.09 ? 294  PHE A CZ    1 
ATOM   2248  N N     . LEU A  1  295 ? 65.204  -16.888 -40.471 1.00 8.95  ? 295  LEU A N     1 
ATOM   2249  C CA    . LEU A  1  295 ? 65.232  -15.508 -39.980 1.00 8.05  ? 295  LEU A CA    1 
ATOM   2250  C C     . LEU A  1  295 ? 63.869  -15.258 -39.337 1.00 7.79  ? 295  LEU A C     1 
ATOM   2251  O O     . LEU A  1  295 ? 62.840  -15.343 -40.012 1.00 8.83  ? 295  LEU A O     1 
ATOM   2252  C CB    . LEU A  1  295 ? 65.437  -14.526 -41.138 1.00 10.64 ? 295  LEU A CB    1 
ATOM   2253  C CG    A LEU A  1  295 ? 66.852  -14.122 -41.562 0.50 11.50 ? 295  LEU A CG    1 
ATOM   2254  C CG    B LEU A  1  295 ? 65.706  -13.085 -40.714 0.50 11.31 ? 295  LEU A CG    1 
ATOM   2255  C CD1   A LEU A  1  295 ? 67.457  -13.223 -40.507 0.50 9.18  ? 295  LEU A CD1   1 
ATOM   2256  C CD1   B LEU A  1  295 ? 67.045  -12.928 -40.010 0.50 8.89  ? 295  LEU A CD1   1 
ATOM   2257  C CD2   A LEU A  1  295 ? 67.709  -15.355 -41.790 0.50 10.01 ? 295  LEU A CD2   1 
ATOM   2258  C CD2   B LEU A  1  295 ? 65.632  -12.175 -41.931 0.50 9.86  ? 295  LEU A CD2   1 
ATOM   2259  N N     . HIS A  1  296 ? 63.869  -14.938 -38.044 1.00 7.52  ? 296  HIS A N     1 
ATOM   2260  C CA    . HIS A  1  296 ? 62.637  -14.707 -37.287 1.00 8.03  ? 296  HIS A CA    1 
ATOM   2261  C C     . HIS A  1  296 ? 62.492  -13.270 -36.792 1.00 8.76  ? 296  HIS A C     1 
ATOM   2262  O O     . HIS A  1  296 ? 63.456  -12.682 -36.301 1.00 10.42 ? 296  HIS A O     1 
ATOM   2263  C CB    . HIS A  1  296 ? 62.595  -15.598 -36.036 1.00 8.25  ? 296  HIS A CB    1 
ATOM   2264  C CG    . HIS A  1  296 ? 62.643  -17.068 -36.312 1.00 8.66  ? 296  HIS A CG    1 
ATOM   2265  N ND1   . HIS A  1  296 ? 61.589  -17.912 -36.020 1.00 8.71  ? 296  HIS A ND1   1 
ATOM   2266  C CD2   . HIS A  1  296 ? 63.630  -17.858 -36.794 1.00 8.12  ? 296  HIS A CD2   1 
ATOM   2267  C CE1   . HIS A  1  296 ? 61.929  -19.153 -36.308 1.00 9.26  ? 296  HIS A CE1   1 
ATOM   2268  N NE2   . HIS A  1  296 ? 63.165  -19.149 -36.782 1.00 10.79 ? 296  HIS A NE2   1 
ATOM   2269  N N     . ASP A  1  297 ? 61.293  -12.705 -36.910 1.00 6.43  ? 297  ASP A N     1 
ATOM   2270  C CA    . ASP A  1  297 ? 61.054  -11.367 -36.380 1.00 5.84  ? 297  ASP A CA    1 
ATOM   2271  C C     . ASP A  1  297 ? 59.729  -11.366 -35.631 1.00 4.91  ? 297  ASP A C     1 
ATOM   2272  O O     . ASP A  1  297 ? 58.663  -11.483 -36.234 1.00 7.40  ? 297  ASP A O     1 
ATOM   2273  C CB    . ASP A  1  297 ? 61.025  -10.297 -37.476 1.00 6.12  ? 297  ASP A CB    1 
ATOM   2274  C CG    . ASP A  1  297 ? 61.009  -8.889  -36.898 1.00 7.81  ? 297  ASP A CG    1 
ATOM   2275  O OD1   . ASP A  1  297 ? 61.755  -8.643  -35.920 1.00 8.56  ? 297  ASP A OD1   1 
ATOM   2276  O OD2   . ASP A  1  297 ? 60.263  -8.028  -37.415 1.00 9.09  ? 297  ASP A OD2   1 
ATOM   2277  N N     . ASN A  1  298 ? 59.797  -11.250 -34.308 1.00 5.55  ? 298  ASN A N     1 
ATOM   2278  C CA    . ASN A  1  298 ? 58.584  -11.234 -33.501 1.00 4.39  ? 298  ASN A CA    1 
ATOM   2279  C C     . ASN A  1  298 ? 57.725  -10.052 -33.905 1.00 5.92  ? 298  ASN A C     1 
ATOM   2280  O O     . ASN A  1  298 ? 58.202  -8.921  -33.961 1.00 7.59  ? 298  ASN A O     1 
ATOM   2281  C CB    . ASN A  1  298 ? 58.912  -11.111 -32.011 1.00 6.38  ? 298  ASN A CB    1 
ATOM   2282  C CG    . ASN A  1  298 ? 59.856  -12.188 -31.535 1.00 6.99  ? 298  ASN A CG    1 
ATOM   2283  O OD1   . ASN A  1  298 ? 61.045  -12.169 -31.853 1.00 9.21  ? 298  ASN A OD1   1 
ATOM   2284  N ND2   . ASN A  1  298 ? 59.332  -13.136 -30.768 1.00 6.97  ? 298  ASN A ND2   1 
ATOM   2285  N N     . PRO A  1  299 ? 56.445  -10.298 -34.206 1.00 6.83  ? 299  PRO A N     1 
ATOM   2286  C CA    . PRO A  1  299 ? 55.580  -9.186  -34.597 1.00 6.95  ? 299  PRO A CA    1 
ATOM   2287  C C     . PRO A  1  299 ? 55.156  -8.314  -33.424 1.00 7.97  ? 299  PRO A C     1 
ATOM   2288  O O     . PRO A  1  299 ? 55.013  -8.783  -32.293 1.00 8.71  ? 299  PRO A O     1 
ATOM   2289  C CB    . PRO A  1  299 ? 54.391  -9.887  -35.254 1.00 7.29  ? 299  PRO A CB    1 
ATOM   2290  C CG    . PRO A  1  299 ? 54.308  -11.182 -34.504 1.00 8.40  ? 299  PRO A CG    1 
ATOM   2291  C CD    . PRO A  1  299 ? 55.762  -11.593 -34.389 1.00 6.73  ? 299  PRO A CD    1 
ATOM   2292  N N     . ARG A  1  300 ? 54.982  -7.030  -33.707 1.00 6.78  ? 300  ARG A N     1 
ATOM   2293  C CA    . ARG A  1  300 ? 54.530  -6.079  -32.711 1.00 7.16  ? 300  ARG A CA    1 
ATOM   2294  C C     . ARG A  1  300 ? 53.186  -5.554  -33.174 1.00 7.28  ? 300  ARG A C     1 
ATOM   2295  O O     . ARG A  1  300 ? 53.038  -5.123  -34.314 1.00 8.39  ? 300  ARG A O     1 
ATOM   2296  C CB    . ARG A  1  300 ? 55.497  -4.895  -32.578 1.00 8.40  ? 300  ARG A CB    1 
ATOM   2297  C CG    . ARG A  1  300 ? 54.941  -3.728  -31.736 1.00 8.13  ? 300  ARG A CG    1 
ATOM   2298  C CD    . ARG A  1  300 ? 56.030  -2.722  -31.365 1.00 10.54 ? 300  ARG A CD    1 
ATOM   2299  N NE    . ARG A  1  300 ? 56.774  -2.276  -32.540 1.00 10.45 ? 300  ARG A NE    1 
ATOM   2300  C CZ    . ARG A  1  300 ? 56.580  -1.122  -33.172 1.00 8.73  ? 300  ARG A CZ    1 
ATOM   2301  N NH1   . ARG A  1  300 ? 55.665  -0.262  -32.743 1.00 9.83  ? 300  ARG A NH1   1 
ATOM   2302  N NH2   . ARG A  1  300 ? 57.282  -0.845  -34.260 1.00 9.31  ? 300  ARG A NH2   1 
ATOM   2303  N N     . ASN A  1  301 ? 52.193  -5.635  -32.301 1.00 7.30  ? 301  ASN A N     1 
ATOM   2304  C CA    . ASN A  1  301 ? 50.887  -5.087  -32.611 1.00 7.37  ? 301  ASN A CA    1 
ATOM   2305  C C     . ASN A  1  301 ? 50.657  -4.114  -31.470 1.00 8.37  ? 301  ASN A C     1 
ATOM   2306  O O     . ASN A  1  301 ? 51.194  -4.298  -30.370 1.00 8.19  ? 301  ASN A O     1 
ATOM   2307  C CB    . ASN A  1  301 ? 49.831  -6.184  -32.721 1.00 8.79  ? 301  ASN A CB    1 
ATOM   2308  C CG    . ASN A  1  301 ? 50.008  -7.013  -33.990 1.00 8.75  ? 301  ASN A CG    1 
ATOM   2309  O OD1   . ASN A  1  301 ? 50.789  -7.963  -34.026 1.00 10.82 ? 301  ASN A OD1   1 
ATOM   2310  N ND2   . ASN A  1  301 ? 49.298  -6.632  -35.046 1.00 11.26 ? 301  ASN A ND2   1 
ATOM   2311  N N     . PHE A  1  302 ? 49.865  -3.081  -31.714 1.00 7.61  ? 302  PHE A N     1 
ATOM   2312  C CA    . PHE A  1  302 ? 49.735  -2.044  -30.706 1.00 8.87  ? 302  PHE A CA    1 
ATOM   2313  C C     . PHE A  1  302 ? 48.506  -1.159  -30.816 1.00 8.08  ? 302  PHE A C     1 
ATOM   2314  O O     . PHE A  1  302 ? 47.751  -1.224  -31.784 1.00 8.49  ? 302  PHE A O     1 
ATOM   2315  C CB    . PHE A  1  302 ? 50.956  -1.150  -30.854 1.00 8.74  ? 302  PHE A CB    1 
ATOM   2316  C CG    . PHE A  1  302 ? 51.095  -0.580  -32.248 1.00 9.61  ? 302  PHE A CG    1 
ATOM   2317  C CD1   . PHE A  1  302 ? 50.362  0.540   -32.633 1.00 7.68  ? 302  PHE A CD1   1 
ATOM   2318  C CD2   . PHE A  1  302 ? 51.887  -1.217  -33.199 1.00 9.57  ? 302  PHE A CD2   1 
ATOM   2319  C CE1   . PHE A  1  302 ? 50.413  1.015   -33.950 1.00 7.56  ? 302  PHE A CE1   1 
ATOM   2320  C CE2   . PHE A  1  302 ? 51.945  -0.753  -34.514 1.00 10.13 ? 302  PHE A CE2   1 
ATOM   2321  C CZ    . PHE A  1  302 ? 51.204  0.366   -34.890 1.00 9.32  ? 302  PHE A CZ    1 
ATOM   2322  N N     . ILE A  1  303 ? 48.345  -0.313  -29.802 1.00 8.52  ? 303  ILE A N     1 
ATOM   2323  C CA    . ILE A  1  303 ? 47.278  0.674   -29.759 1.00 8.49  ? 303  ILE A CA    1 
ATOM   2324  C C     . ILE A  1  303 ? 47.881  1.963   -29.209 1.00 8.46  ? 303  ILE A C     1 
ATOM   2325  O O     . ILE A  1  303 ? 48.532  1.959   -28.157 1.00 9.18  ? 303  ILE A O     1 
ATOM   2326  C CB    . ILE A  1  303 ? 46.104  0.250   -28.844 1.00 8.43  ? 303  ILE A CB    1 
ATOM   2327  C CG1   . ILE A  1  303 ? 45.352  -0.937  -29.454 1.00 7.43  ? 303  ILE A CG1   1 
ATOM   2328  C CG2   . ILE A  1  303 ? 45.150  1.431   -28.649 1.00 9.06  ? 303  ILE A CG2   1 
ATOM   2329  C CD1   . ILE A  1  303 ? 44.645  -0.624  -30.772 1.00 8.60  ? 303  ILE A CD1   1 
ATOM   2330  N N     . ASN A  1  304 ? 47.688  3.057   -29.940 1.00 8.57  ? 304  ASN A N     1 
ATOM   2331  C CA    . ASN A  1  304 ? 48.179  4.362   -29.515 1.00 8.72  ? 304  ASN A CA    1 
ATOM   2332  C C     . ASN A  1  304 ? 46.988  5.183   -29.037 1.00 9.64  ? 304  ASN A C     1 
ATOM   2333  O O     . ASN A  1  304 ? 46.031  5.377   -29.789 1.00 10.36 ? 304  ASN A O     1 
ATOM   2334  C CB    . ASN A  1  304 ? 48.832  5.118   -30.681 1.00 11.44 ? 304  ASN A CB    1 
ATOM   2335  C CG    . ASN A  1  304 ? 50.009  4.382   -31.279 1.00 12.44 ? 304  ASN A CG    1 
ATOM   2336  O OD1   . ASN A  1  304 ? 50.980  4.074   -30.590 1.00 12.94 ? 304  ASN A OD1   1 
ATOM   2337  N ND2   . ASN A  1  304 ? 49.933  4.105   -32.576 1.00 15.67 ? 304  ASN A ND2   1 
ATOM   2338  N N     . ILE A  1  305 ? 47.026  5.644   -27.791 1.00 8.84  ? 305  ILE A N     1 
ATOM   2339  C CA    . ILE A  1  305 ? 45.946  6.482   -27.288 1.00 9.06  ? 305  ILE A CA    1 
ATOM   2340  C C     . ILE A  1  305 ? 46.460  7.907   -27.112 1.00 9.55  ? 305  ILE A C     1 
ATOM   2341  O O     . ILE A  1  305 ? 47.630  8.126   -26.787 1.00 8.82  ? 305  ILE A O     1 
ATOM   2342  C CB    . ILE A  1  305 ? 45.371  5.977   -25.935 1.00 7.97  ? 305  ILE A CB    1 
ATOM   2343  C CG1   . ILE A  1  305 ? 46.441  6.014   -24.842 1.00 9.01  ? 305  ILE A CG1   1 
ATOM   2344  C CG2   . ILE A  1  305 ? 44.806  4.576   -26.107 1.00 8.29  ? 305  ILE A CG2   1 
ATOM   2345  C CD1   . ILE A  1  305 ? 45.892  5.733   -23.446 1.00 12.29 ? 305  ILE A CD1   1 
ATOM   2346  N N     . LEU A  1  306 ? 45.574  8.866   -27.353 1.00 10.14 ? 306  LEU A N     1 
ATOM   2347  C CA    . LEU A  1  306 ? 45.881  10.287  -27.225 1.00 10.59 ? 306  LEU A CA    1 
ATOM   2348  C C     . LEU A  1  306 ? 45.024  10.834  -26.089 1.00 10.28 ? 306  LEU A C     1 
ATOM   2349  O O     . LEU A  1  306 ? 43.878  11.221  -26.302 1.00 12.07 ? 306  LEU A O     1 
ATOM   2350  C CB    . LEU A  1  306 ? 45.539  11.011  -28.527 1.00 10.89 ? 306  LEU A CB    1 
ATOM   2351  C CG    . LEU A  1  306 ? 46.366  10.603  -29.748 1.00 10.64 ? 306  LEU A CG    1 
ATOM   2352  C CD1   . LEU A  1  306 ? 45.623  10.963  -31.025 1.00 12.86 ? 306  LEU A CD1   1 
ATOM   2353  C CD2   . LEU A  1  306 ? 47.719  11.284  -29.687 1.00 14.29 ? 306  LEU A CD2   1 
ATOM   2354  N N     . PRO A  1  307 ? 45.568  10.859  -24.863 1.00 10.86 ? 307  PRO A N     1 
ATOM   2355  C CA    . PRO A  1  307 ? 44.852  11.353  -23.681 1.00 12.24 ? 307  PRO A CA    1 
ATOM   2356  C C     . PRO A  1  307 ? 44.424  12.813  -23.789 1.00 14.47 ? 307  PRO A C     1 
ATOM   2357  O O     . PRO A  1  307 ? 45.151  13.641  -24.337 1.00 13.39 ? 307  PRO A O     1 
ATOM   2358  C CB    . PRO A  1  307 ? 45.860  11.141  -22.552 1.00 12.79 ? 307  PRO A CB    1 
ATOM   2359  C CG    . PRO A  1  307 ? 46.672  9.974   -23.032 1.00 13.57 ? 307  PRO A CG    1 
ATOM   2360  C CD    . PRO A  1  307 ? 46.887  10.324  -24.483 1.00 11.72 ? 307  PRO A CD    1 
ATOM   2361  N N     . PRO A  1  308 ? 43.230  13.143  -23.266 1.00 14.54 ? 308  PRO A N     1 
ATOM   2362  C CA    . PRO A  1  308 ? 42.735  14.522  -23.315 1.00 16.45 ? 308  PRO A CA    1 
ATOM   2363  C C     . PRO A  1  308 ? 43.598  15.396  -22.409 1.00 17.16 ? 308  PRO A C     1 
ATOM   2364  O O     . PRO A  1  308 ? 43.688  16.613  -22.582 1.00 17.95 ? 308  PRO A O     1 
ATOM   2365  C CB    . PRO A  1  308 ? 41.297  14.386  -22.819 1.00 16.17 ? 308  PRO A CB    1 
ATOM   2366  C CG    . PRO A  1  308 ? 41.384  13.245  -21.854 1.00 16.47 ? 308  PRO A CG    1 
ATOM   2367  C CD    . PRO A  1  308 ? 42.255  12.257  -22.603 1.00 15.31 ? 308  PRO A CD    1 
ATOM   2368  N N     . ASN A  1  309 ? 44.231  14.757  -21.433 1.00 19.33 ? 309  ASN A N     1 
ATOM   2369  C CA    . ASN A  1  309 ? 45.118  15.451  -20.515 1.00 20.87 ? 309  ASN A CA    1 
ATOM   2370  C C     . ASN A  1  309 ? 46.522  14.926  -20.769 1.00 21.71 ? 309  ASN A C     1 
ATOM   2371  O O     . ASN A  1  309 ? 46.768  13.721  -20.715 1.00 22.72 ? 309  ASN A O     1 
ATOM   2372  C CB    . ASN A  1  309 ? 44.701  15.201  -19.067 1.00 23.53 ? 309  ASN A CB    1 
ATOM   2373  C CG    . ASN A  1  309 ? 43.392  15.874  -18.722 1.00 24.96 ? 309  ASN A CG    1 
ATOM   2374  O OD1   . ASN A  1  309 ? 43.246  17.086  -18.886 1.00 27.31 ? 309  ASN A OD1   1 
ATOM   2375  N ND2   . ASN A  1  309 ? 42.431  15.095  -18.241 1.00 26.94 ? 309  ASN A ND2   1 
ATOM   2376  N N     . PRO A  1  310 ? 47.463  15.831  -21.056 1.00 19.58 ? 310  PRO A N     1 
ATOM   2377  C CA    . PRO A  1  310 ? 48.857  15.481  -21.332 1.00 19.10 ? 310  PRO A CA    1 
ATOM   2378  C C     . PRO A  1  310 ? 49.494  14.522  -20.334 1.00 18.31 ? 310  PRO A C     1 
ATOM   2379  O O     . PRO A  1  310 ? 49.221  14.584  -19.136 1.00 17.76 ? 310  PRO A O     1 
ATOM   2380  C CB    . PRO A  1  310 ? 49.556  16.836  -21.334 1.00 20.42 ? 310  PRO A CB    1 
ATOM   2381  C CG    . PRO A  1  310 ? 48.486  17.763  -21.824 1.00 20.34 ? 310  PRO A CG    1 
ATOM   2382  C CD    . PRO A  1  310 ? 47.281  17.295  -21.059 1.00 19.95 ? 310  PRO A CD    1 
ATOM   2383  N N     . ILE A  1  311 ? 50.332  13.625  -20.846 1.00 16.68 ? 311  ILE A N     1 
ATOM   2384  C CA    . ILE A  1  311 ? 51.064  12.688  -20.006 1.00 15.03 ? 311  ILE A CA    1 
ATOM   2385  C C     . ILE A  1  311 ? 52.538  12.933  -20.304 1.00 14.82 ? 311  ILE A C     1 
ATOM   2386  O O     . ILE A  1  311 ? 52.887  13.410  -21.388 1.00 15.21 ? 311  ILE A O     1 
ATOM   2387  C CB    . ILE A  1  311 ? 50.699  11.208  -20.300 1.00 14.58 ? 311  ILE A CB    1 
ATOM   2388  C CG1   . ILE A  1  311 ? 50.902  10.885  -21.780 1.00 14.28 ? 311  ILE A CG1   1 
ATOM   2389  C CG2   . ILE A  1  311 ? 49.265  10.938  -19.878 1.00 14.72 ? 311  ILE A CG2   1 
ATOM   2390  C CD1   . ILE A  1  311 ? 50.678  9.416   -22.107 1.00 14.82 ? 311  ILE A CD1   1 
ATOM   2391  N N     . GLU A  1  312 ? 53.401  12.622  -19.346 1.00 14.48 ? 312  GLU A N     1 
ATOM   2392  C CA    . GLU A  1  312 ? 54.828  12.854  -19.524 1.00 15.05 ? 312  GLU A CA    1 
ATOM   2393  C C     . GLU A  1  312 ? 55.549  11.685  -20.188 1.00 15.41 ? 312  GLU A C     1 
ATOM   2394  O O     . GLU A  1  312 ? 55.160  10.527  -20.021 1.00 14.10 ? 312  GLU A O     1 
ATOM   2395  C CB    . GLU A  1  312 ? 55.473  13.173  -18.170 1.00 17.85 ? 312  GLU A CB    1 
ATOM   2396  C CG    . GLU A  1  312 ? 55.864  11.973  -17.302 1.00 19.91 ? 312  GLU A CG    1 
ATOM   2397  C CD    . GLU A  1  312 ? 54.715  11.028  -16.976 1.00 21.04 ? 312  GLU A CD    1 
ATOM   2398  O OE1   . GLU A  1  312 ? 53.537  11.455  -16.988 1.00 22.80 ? 312  GLU A OE1   1 
ATOM   2399  O OE2   . GLU A  1  312 ? 55.002  9.848   -16.682 1.00 18.29 ? 312  GLU A OE2   1 
ATOM   2400  N N     . PRO A  1  313 ? 56.601  11.979  -20.971 1.00 14.03 ? 313  PRO A N     1 
ATOM   2401  C CA    . PRO A  1  313 ? 57.353  10.916  -21.643 1.00 13.71 ? 313  PRO A CA    1 
ATOM   2402  C C     . PRO A  1  313 ? 58.086  10.051  -20.623 1.00 13.06 ? 313  PRO A C     1 
ATOM   2403  O O     . PRO A  1  313 ? 58.558  10.543  -19.598 1.00 13.01 ? 313  PRO A O     1 
ATOM   2404  C CB    . PRO A  1  313 ? 58.303  11.689  -22.558 1.00 15.29 ? 313  PRO A CB    1 
ATOM   2405  C CG    . PRO A  1  313 ? 58.524  12.971  -21.811 1.00 16.96 ? 313  PRO A CG    1 
ATOM   2406  C CD    . PRO A  1  313 ? 57.136  13.306  -21.325 1.00 15.22 ? 313  PRO A CD    1 
ATOM   2407  N N     . THR A  1  314 ? 58.179  8.758   -20.908 1.00 11.63 ? 314  THR A N     1 
ATOM   2408  C CA    . THR A  1  314 ? 58.834  7.832   -19.995 1.00 11.79 ? 314  THR A CA    1 
ATOM   2409  C C     . THR A  1  314 ? 59.644  6.794   -20.746 1.00 11.17 ? 314  THR A C     1 
ATOM   2410  O O     . THR A  1  314 ? 59.469  6.605   -21.950 1.00 12.13 ? 314  THR A O     1 
ATOM   2411  C CB    . THR A  1  314 ? 57.803  7.053   -19.161 1.00 12.09 ? 314  THR A CB    1 
ATOM   2412  O OG1   . THR A  1  314 ? 56.892  6.385   -20.045 1.00 10.85 ? 314  THR A OG1   1 
ATOM   2413  C CG2   . THR A  1  314 ? 57.024  7.986   -18.253 1.00 11.19 ? 314  THR A CG2   1 
ATOM   2414  N N     . ILE A  1  315 ? 60.538  6.129   -20.024 1.00 10.61 ? 315  ILE A N     1 
ATOM   2415  C CA    . ILE A  1  315 ? 61.318  5.049   -20.611 1.00 11.30 ? 315  ILE A CA    1 
ATOM   2416  C C     . ILE A  1  315 ? 60.589  3.784   -20.158 1.00 10.43 ? 315  ILE A C     1 
ATOM   2417  O O     . ILE A  1  315 ? 60.049  3.732   -19.052 1.00 9.92  ? 315  ILE A O     1 
ATOM   2418  C CB    . ILE A  1  315 ? 62.776  5.019   -20.093 1.00 14.65 ? 315  ILE A CB    1 
ATOM   2419  C CG1   . ILE A  1  315 ? 62.797  4.910   -18.570 1.00 16.29 ? 315  ILE A CG1   1 
ATOM   2420  C CG2   . ILE A  1  315 ? 63.517  6.263   -20.562 1.00 15.59 ? 315  ILE A CG2   1 
ATOM   2421  C CD1   . ILE A  1  315 ? 64.187  4.684   -17.994 1.00 17.88 ? 315  ILE A CD1   1 
ATOM   2422  N N     . VAL A  1  316 ? 60.549  2.773   -21.014 1.00 9.14  ? 316  VAL A N     1 
ATOM   2423  C CA    . VAL A  1  316 ? 59.861  1.534   -20.675 1.00 8.53  ? 316  VAL A CA    1 
ATOM   2424  C C     . VAL A  1  316 ? 60.545  0.793   -19.533 1.00 7.62  ? 316  VAL A C     1 
ATOM   2425  O O     . VAL A  1  316 ? 61.741  0.503   -19.602 1.00 8.78  ? 316  VAL A O     1 
ATOM   2426  C CB    . VAL A  1  316 ? 59.782  0.598   -21.895 1.00 8.82  ? 316  VAL A CB    1 
ATOM   2427  C CG1   . VAL A  1  316 ? 59.168  -0.737  -21.490 1.00 10.60 ? 316  VAL A CG1   1 
ATOM   2428  C CG2   . VAL A  1  316 ? 58.947  1.250   -22.990 1.00 13.10 ? 316  VAL A CG2   1 
ATOM   2429  N N     . THR A  1  317 ? 59.783  0.497   -18.484 1.00 7.36  ? 317  THR A N     1 
ATOM   2430  C CA    . THR A  1  317 ? 60.316  -0.233  -17.334 1.00 8.60  ? 317  THR A CA    1 
ATOM   2431  C C     . THR A  1  317 ? 59.341  -1.297  -16.824 1.00 9.13  ? 317  THR A C     1 
ATOM   2432  O O     . THR A  1  317 ? 59.760  -2.300  -16.239 1.00 8.26  ? 317  THR A O     1 
ATOM   2433  C CB    . THR A  1  317 ? 60.655  0.712   -16.161 1.00 8.60  ? 317  THR A CB    1 
ATOM   2434  O OG1   . THR A  1  317 ? 59.452  1.306   -15.658 1.00 9.26  ? 317  THR A OG1   1 
ATOM   2435  C CG2   . THR A  1  317 ? 61.617  1.805   -16.614 1.00 8.73  ? 317  THR A CG2   1 
ATOM   2436  N N     . VAL A  1  318 ? 58.049  -1.082  -17.049 1.00 8.75  ? 318  VAL A N     1 
ATOM   2437  C CA    . VAL A  1  318 ? 57.032  -2.030  -16.599 1.00 9.09  ? 318  VAL A CA    1 
ATOM   2438  C C     . VAL A  1  318 ? 56.660  -3.026  -17.695 1.00 8.66  ? 318  VAL A C     1 
ATOM   2439  O O     . VAL A  1  318 ? 56.253  -2.643  -18.794 1.00 9.03  ? 318  VAL A O     1 
ATOM   2440  C CB    . VAL A  1  318 ? 55.760  -1.286  -16.113 1.00 8.54  ? 318  VAL A CB    1 
ATOM   2441  C CG1   . VAL A  1  318 ? 54.620  -2.273  -15.882 1.00 9.99  ? 318  VAL A CG1   1 
ATOM   2442  C CG2   . VAL A  1  318 ? 56.071  -0.543  -14.824 1.00 9.05  ? 318  VAL A CG2   1 
ATOM   2443  N N     . LEU A  1  319 ? 56.807  -4.310  -17.386 1.00 8.36  ? 319  LEU A N     1 
ATOM   2444  C CA    . LEU A  1  319 ? 56.492  -5.356  -18.346 1.00 7.06  ? 319  LEU A CA    1 
ATOM   2445  C C     . LEU A  1  319 ? 55.354  -6.257  -17.876 1.00 7.04  ? 319  LEU A C     1 
ATOM   2446  O O     . LEU A  1  319 ? 55.301  -6.645  -16.706 1.00 8.79  ? 319  LEU A O     1 
ATOM   2447  C CB    . LEU A  1  319 ? 57.733  -6.212  -18.616 1.00 6.50  ? 319  LEU A CB    1 
ATOM   2448  C CG    . LEU A  1  319 ? 58.996  -5.458  -19.035 1.00 7.43  ? 319  LEU A CG    1 
ATOM   2449  C CD1   . LEU A  1  319 ? 60.084  -6.464  -19.377 1.00 7.02  ? 319  LEU A CD1   1 
ATOM   2450  C CD2   . LEU A  1  319 ? 58.692  -4.566  -20.242 1.00 8.60  ? 319  LEU A CD2   1 
ATOM   2451  N N     . GLY A  1  320 ? 54.448  -6.569  -18.802 1.00 7.89  ? 320  GLY A N     1 
ATOM   2452  C CA    . GLY A  1  320 ? 53.320  -7.442  -18.524 1.00 7.93  ? 320  GLY A CA    1 
ATOM   2453  C C     . GLY A  1  320 ? 53.585  -8.693  -19.338 1.00 8.81  ? 320  GLY A C     1 
ATOM   2454  O O     . GLY A  1  320 ? 53.336  -8.732  -20.548 1.00 7.92  ? 320  GLY A O     1 
ATOM   2455  N N     . ILE A  1  321 ? 54.088  -9.723  -18.669 1.00 7.39  ? 321  ILE A N     1 
ATOM   2456  C CA    . ILE A  1  321 ? 54.468  -10.964 -19.331 1.00 8.12  ? 321  ILE A CA    1 
ATOM   2457  C C     . ILE A  1  321 ? 53.482  -12.123 -19.271 1.00 8.48  ? 321  ILE A C     1 
ATOM   2458  O O     . ILE A  1  321 ? 53.083  -12.561 -18.199 1.00 9.13  ? 321  ILE A O     1 
ATOM   2459  C CB    . ILE A  1  321 ? 55.827  -11.467 -18.763 1.00 8.02  ? 321  ILE A CB    1 
ATOM   2460  C CG1   . ILE A  1  321 ? 56.884  -10.364 -18.891 1.00 8.30  ? 321  ILE A CG1   1 
ATOM   2461  C CG2   . ILE A  1  321 ? 56.273  -12.735 -19.483 1.00 7.37  ? 321  ILE A CG2   1 
ATOM   2462  C CD1   . ILE A  1  321 ? 57.167  -9.930  -20.325 1.00 8.17  ? 321  ILE A CD1   1 
ATOM   2463  N N     . SER A  1  322 ? 53.088  -12.608 -20.442 1.00 8.66  ? 322  SER A N     1 
ATOM   2464  C CA    . SER A  1  322 ? 52.212  -13.767 -20.531 1.00 11.25 ? 322  SER A CA    1 
ATOM   2465  C C     . SER A  1  322 ? 53.075  -14.820 -21.219 1.00 10.54 ? 322  SER A C     1 
ATOM   2466  O O     . SER A  1  322 ? 54.141  -14.500 -21.748 1.00 11.37 ? 322  SER A O     1 
ATOM   2467  C CB    . SER A  1  322 ? 50.964  -13.446 -21.359 1.00 12.72 ? 322  SER A CB    1 
ATOM   2468  O OG    . SER A  1  322 ? 50.132  -12.520 -20.674 1.00 17.32 ? 322  SER A OG    1 
ATOM   2469  N N     . ASN A  1  323 ? 52.644  -16.075 -21.218 1.00 12.98 ? 323  ASN A N     1 
ATOM   2470  C CA    . ASN A  1  323 ? 53.450  -17.114 -21.846 1.00 13.26 ? 323  ASN A CA    1 
ATOM   2471  C C     . ASN A  1  323 ? 53.568  -16.989 -23.360 1.00 12.53 ? 323  ASN A C     1 
ATOM   2472  O O     . ASN A  1  323 ? 54.605  -17.317 -23.935 1.00 14.09 ? 323  ASN A O     1 
ATOM   2473  C CB    . ASN A  1  323 ? 52.904  -18.503 -21.502 1.00 16.23 ? 323  ASN A CB    1 
ATOM   2474  C CG    . ASN A  1  323 ? 53.146  -18.879 -20.054 1.00 20.34 ? 323  ASN A CG    1 
ATOM   2475  O OD1   . ASN A  1  323 ? 52.229  -18.865 -19.235 1.00 23.95 ? 323  ASN A OD1   1 
ATOM   2476  N ND2   . ASN A  1  323 ? 54.390  -19.208 -19.731 1.00 21.54 ? 323  ASN A ND2   1 
ATOM   2477  N N     . ASP A  1  324 ? 52.515  -16.501 -24.008 1.00 10.66 ? 324  ASP A N     1 
ATOM   2478  C CA    . ASP A  1  324 ? 52.528  -16.391 -25.461 1.00 10.21 ? 324  ASP A CA    1 
ATOM   2479  C C     . ASP A  1  324 ? 52.751  -14.996 -26.040 1.00 8.66  ? 324  ASP A C     1 
ATOM   2480  O O     . ASP A  1  324 ? 52.924  -14.850 -27.253 1.00 9.23  ? 324  ASP A O     1 
ATOM   2481  C CB    . ASP A  1  324 ? 51.230  -16.971 -26.025 1.00 14.11 ? 324  ASP A CB    1 
ATOM   2482  C CG    . ASP A  1  324 ? 50.950  -18.370 -25.513 1.00 16.40 ? 324  ASP A CG    1 
ATOM   2483  O OD1   . ASP A  1  324 ? 51.874  -19.209 -25.546 1.00 16.54 ? 324  ASP A OD1   1 
ATOM   2484  O OD2   . ASP A  1  324 ? 49.806  -18.629 -25.085 1.00 20.36 ? 324  ASP A OD2   1 
ATOM   2485  N N     . PHE A  1  325 ? 52.749  -13.979 -25.185 1.00 7.73  ? 325  PHE A N     1 
ATOM   2486  C CA    . PHE A  1  325 ? 52.956  -12.606 -25.634 1.00 6.83  ? 325  PHE A CA    1 
ATOM   2487  C C     . PHE A  1  325 ? 53.476  -11.741 -24.489 1.00 7.50  ? 325  PHE A C     1 
ATOM   2488  O O     . PHE A  1  325 ? 53.190  -12.010 -23.323 1.00 7.61  ? 325  PHE A O     1 
ATOM   2489  C CB    . PHE A  1  325 ? 51.657  -12.031 -26.221 1.00 6.59  ? 325  PHE A CB    1 
ATOM   2490  C CG    . PHE A  1  325 ? 50.466  -12.139 -25.306 1.00 6.61  ? 325  PHE A CG    1 
ATOM   2491  C CD1   . PHE A  1  325 ? 50.247  -11.193 -24.307 1.00 6.08  ? 325  PHE A CD1   1 
ATOM   2492  C CD2   . PHE A  1  325 ? 49.562  -13.189 -25.445 1.00 8.01  ? 325  PHE A CD2   1 
ATOM   2493  C CE1   . PHE A  1  325 ? 49.141  -11.293 -23.459 1.00 6.83  ? 325  PHE A CE1   1 
ATOM   2494  C CE2   . PHE A  1  325 ? 48.455  -13.297 -24.602 1.00 8.37  ? 325  PHE A CE2   1 
ATOM   2495  C CZ    . PHE A  1  325 ? 48.245  -12.351 -23.610 1.00 7.42  ? 325  PHE A CZ    1 
ATOM   2496  N N     . TYR A  1  326 ? 54.242  -10.710 -24.834 1.00 6.83  ? 326  TYR A N     1 
ATOM   2497  C CA    . TYR A  1  326 ? 54.853  -9.817  -23.847 1.00 7.40  ? 326  TYR A CA    1 
ATOM   2498  C C     . TYR A  1  326 ? 54.396  -8.393  -24.129 1.00 7.05  ? 326  TYR A C     1 
ATOM   2499  O O     . TYR A  1  326 ? 54.372  -7.968  -25.286 1.00 8.03  ? 326  TYR A O     1 
ATOM   2500  C CB    . TYR A  1  326 ? 56.371  -9.908  -23.960 1.00 8.84  ? 326  TYR A CB    1 
ATOM   2501  C CG    . TYR A  1  326 ? 56.878  -11.306 -24.251 1.00 7.24  ? 326  TYR A CG    1 
ATOM   2502  C CD1   . TYR A  1  326 ? 57.747  -11.537 -25.315 1.00 9.07  ? 326  TYR A CD1   1 
ATOM   2503  C CD2   . TYR A  1  326 ? 56.489  -12.393 -23.470 1.00 10.09 ? 326  TYR A CD2   1 
ATOM   2504  C CE1   . TYR A  1  326 ? 58.218  -12.814 -25.597 1.00 10.38 ? 326  TYR A CE1   1 
ATOM   2505  C CE2   . TYR A  1  326 ? 56.955  -13.682 -23.745 1.00 10.00 ? 326  TYR A CE2   1 
ATOM   2506  C CZ    . TYR A  1  326 ? 57.821  -13.879 -24.814 1.00 10.45 ? 326  TYR A CZ    1 
ATOM   2507  O OH    . TYR A  1  326 ? 58.289  -15.142 -25.110 1.00 13.01 ? 326  TYR A OH    1 
ATOM   2508  N N     . GLN A  1  327 ? 54.068  -7.641  -23.079 1.00 5.65  ? 327  GLN A N     1 
ATOM   2509  C CA    . GLN A  1  327 ? 53.545  -6.297  -23.287 1.00 5.62  ? 327  GLN A CA    1 
ATOM   2510  C C     . GLN A  1  327 ? 54.158  -5.184  -22.444 1.00 7.30  ? 327  GLN A C     1 
ATOM   2511  O O     . GLN A  1  327 ? 54.780  -5.428  -21.411 1.00 6.34  ? 327  GLN A O     1 
ATOM   2512  C CB    . GLN A  1  327 ? 52.024  -6.344  -23.084 1.00 6.56  ? 327  GLN A CB    1 
ATOM   2513  C CG    . GLN A  1  327 ? 51.393  -7.567  -23.757 1.00 9.07  ? 327  GLN A CG    1 
ATOM   2514  C CD    . GLN A  1  327 ? 49.883  -7.619  -23.651 1.00 7.51  ? 327  GLN A CD    1 
ATOM   2515  O OE1   . GLN A  1  327 ? 49.314  -7.506  -22.562 1.00 9.40  ? 327  GLN A OE1   1 
ATOM   2516  N NE2   . GLN A  1  327 ? 49.222  -7.808  -24.788 1.00 9.28  ? 327  GLN A NE2   1 
ATOM   2517  N N     . CYS A  1  328 ? 53.977  -3.951  -22.903 1.00 8.17  ? 328  CYS A N     1 
ATOM   2518  C CA    . CYS A  1  328 ? 54.497  -2.787  -22.201 1.00 9.99  ? 328  CYS A CA    1 
ATOM   2519  C C     . CYS A  1  328 ? 53.891  -1.526  -22.802 1.00 10.34 ? 328  CYS A C     1 
ATOM   2520  O O     . CYS A  1  328 ? 53.136  -1.591  -23.776 1.00 10.11 ? 328  CYS A O     1 
ATOM   2521  C CB    . CYS A  1  328 ? 56.020  -2.731  -22.316 1.00 10.58 ? 328  CYS A CB    1 
ATOM   2522  S SG    . CYS A  1  328 ? 56.614  -2.461  -24.002 1.00 17.12 ? 328  CYS A SG    1 
ATOM   2523  N N     . SER A  1  329 ? 54.219  -0.379  -22.219 1.00 10.35 ? 329  SER A N     1 
ATOM   2524  C CA    . SER A  1  329 ? 53.699  0.884   -22.715 1.00 10.65 ? 329  SER A CA    1 
ATOM   2525  C C     . SER A  1  329 ? 54.777  1.951   -22.695 1.00 10.90 ? 329  SER A C     1 
ATOM   2526  O O     . SER A  1  329 ? 55.572  2.039   -21.758 1.00 13.36 ? 329  SER A O     1 
ATOM   2527  C CB    . SER A  1  329 ? 52.501  1.337   -21.883 1.00 10.73 ? 329  SER A CB    1 
ATOM   2528  O OG    . SER A  1  329 ? 51.899  2.477   -22.466 1.00 12.17 ? 329  SER A OG    1 
ATOM   2529  N N     . PHE A  1  330 ? 54.788  2.755   -23.748 1.00 11.99 ? 330  PHE A N     1 
ATOM   2530  C CA    . PHE A  1  330 ? 55.755  3.827   -23.926 1.00 13.36 ? 330  PHE A CA    1 
ATOM   2531  C C     . PHE A  1  330 ? 54.990  5.135   -24.120 1.00 12.34 ? 330  PHE A C     1 
ATOM   2532  O O     . PHE A  1  330 ? 54.102  5.211   -24.963 1.00 12.70 ? 330  PHE A O     1 
ATOM   2533  C CB    . PHE A  1  330 ? 56.603  3.506   -25.170 1.00 15.87 ? 330  PHE A CB    1 
ATOM   2534  C CG    . PHE A  1  330 ? 57.544  4.601   -25.583 1.00 16.59 ? 330  PHE A CG    1 
ATOM   2535  C CD1   . PHE A  1  330 ? 58.542  5.047   -24.724 1.00 19.74 ? 330  PHE A CD1   1 
ATOM   2536  C CD2   . PHE A  1  330 ? 57.459  5.156   -26.858 1.00 18.55 ? 330  PHE A CD2   1 
ATOM   2537  C CE1   . PHE A  1  330 ? 59.446  6.029   -25.130 1.00 19.83 ? 330  PHE A CE1   1 
ATOM   2538  C CE2   . PHE A  1  330 ? 58.358  6.138   -27.274 1.00 18.75 ? 330  PHE A CE2   1 
ATOM   2539  C CZ    . PHE A  1  330 ? 59.352  6.575   -26.409 1.00 20.41 ? 330  PHE A CZ    1 
ATOM   2540  N N     . SER A  1  331 ? 55.305  6.152   -23.323 1.00 11.41 ? 331  SER A N     1 
ATOM   2541  C CA    . SER A  1  331 ? 54.644  7.446   -23.476 1.00 11.37 ? 331  SER A CA    1 
ATOM   2542  C C     . SER A  1  331 ? 55.668  8.389   -24.093 1.00 11.30 ? 331  SER A C     1 
ATOM   2543  O O     . SER A  1  331 ? 56.847  8.355   -23.736 1.00 10.71 ? 331  SER A O     1 
ATOM   2544  C CB    . SER A  1  331 ? 54.148  7.983   -22.127 1.00 11.22 ? 331  SER A CB    1 
ATOM   2545  O OG    . SER A  1  331 ? 55.205  8.152   -21.199 1.00 10.72 ? 331  SER A OG    1 
ATOM   2546  N N     . SER A  1  332 ? 55.224  9.233   -25.016 1.00 10.53 ? 332  SER A N     1 
ATOM   2547  C CA    . SER A  1  332 ? 56.153  10.128  -25.687 1.00 12.68 ? 332  SER A CA    1 
ATOM   2548  C C     . SER A  1  332 ? 55.536  11.448  -26.125 1.00 12.88 ? 332  SER A C     1 
ATOM   2549  O O     . SER A  1  332 ? 54.323  11.634  -26.062 1.00 12.61 ? 332  SER A O     1 
ATOM   2550  C CB    . SER A  1  332 ? 56.734  9.408   -26.904 1.00 16.21 ? 332  SER A CB    1 
ATOM   2551  O OG    . SER A  1  332 ? 57.716  10.196  -27.551 1.00 21.97 ? 332  SER A OG    1 
ATOM   2552  N N     . LEU A  1  333 ? 56.394  12.357  -26.578 1.00 14.22 ? 333  LEU A N     1 
ATOM   2553  C CA    . LEU A  1  333 ? 55.975  13.670  -27.054 1.00 14.20 ? 333  LEU A CA    1 
ATOM   2554  C C     . LEU A  1  333 ? 55.489  13.575  -28.496 1.00 15.46 ? 333  LEU A C     1 
ATOM   2555  O O     . LEU A  1  333 ? 55.772  12.599  -29.194 1.00 13.92 ? 333  LEU A O     1 
ATOM   2556  C CB    . LEU A  1  333 ? 57.152  14.645  -26.989 1.00 14.75 ? 333  LEU A CB    1 
ATOM   2557  C CG    . LEU A  1  333 ? 57.729  14.959  -25.609 1.00 14.67 ? 333  LEU A CG    1 
ATOM   2558  C CD1   . LEU A  1  333 ? 58.934  15.875  -25.764 1.00 17.81 ? 333  LEU A CD1   1 
ATOM   2559  C CD2   . LEU A  1  333 ? 56.664  15.617  -24.740 1.00 16.53 ? 333  LEU A CD2   1 
ATOM   2560  N N     . PRO A  1  334 ? 54.746  14.592  -28.962 1.00 15.71 ? 334  PRO A N     1 
ATOM   2561  C CA    . PRO A  1  334 ? 54.227  14.623  -30.332 1.00 16.81 ? 334  PRO A CA    1 
ATOM   2562  C C     . PRO A  1  334 ? 55.355  14.952  -31.309 1.00 18.03 ? 334  PRO A C     1 
ATOM   2563  O O     . PRO A  1  334 ? 56.434  15.372  -30.892 1.00 18.88 ? 334  PRO A O     1 
ATOM   2564  C CB    . PRO A  1  334 ? 53.173  15.725  -30.269 1.00 17.04 ? 334  PRO A CB    1 
ATOM   2565  C CG    . PRO A  1  334 ? 53.763  16.678  -29.282 1.00 17.26 ? 334  PRO A CG    1 
ATOM   2566  C CD    . PRO A  1  334 ? 54.256  15.750  -28.190 1.00 17.17 ? 334  PRO A CD    1 
ATOM   2567  N N     . PHE A  1  335 ? 55.107  14.770  -32.602 1.00 18.31 ? 335  PHE A N     1 
ATOM   2568  C CA    . PHE A  1  335 ? 56.126  15.056  -33.612 1.00 18.82 ? 335  PHE A CA    1 
ATOM   2569  C C     . PHE A  1  335 ? 55.553  15.101  -35.025 1.00 18.61 ? 335  PHE A C     1 
ATOM   2570  O O     . PHE A  1  335 ? 54.482  14.558  -35.284 1.00 19.57 ? 335  PHE A O     1 
ATOM   2571  C CB    . PHE A  1  335 ? 57.238  14.003  -33.539 1.00 19.16 ? 335  PHE A CB    1 
ATOM   2572  C CG    . PHE A  1  335 ? 56.745  12.581  -33.636 1.00 19.52 ? 335  PHE A CG    1 
ATOM   2573  C CD1   . PHE A  1  335 ? 56.168  12.103  -34.810 1.00 20.11 ? 335  PHE A CD1   1 
ATOM   2574  C CD2   . PHE A  1  335 ? 56.856  11.720  -32.549 1.00 21.01 ? 335  PHE A CD2   1 
ATOM   2575  C CE1   . PHE A  1  335 ? 55.710  10.792  -34.900 1.00 21.81 ? 335  PHE A CE1   1 
ATOM   2576  C CE2   . PHE A  1  335 ? 56.400  10.404  -32.629 1.00 21.34 ? 335  PHE A CE2   1 
ATOM   2577  C CZ    . PHE A  1  335 ? 55.826  9.940   -33.806 1.00 19.67 ? 335  PHE A CZ    1 
ATOM   2578  N N     . THR A  1  336 ? 56.263  15.763  -35.936 1.00 19.65 ? 336  THR A N     1 
ATOM   2579  C CA    . THR A  1  336 ? 55.821  15.841  -37.326 1.00 19.97 ? 336  THR A CA    1 
ATOM   2580  C C     . THR A  1  336 ? 56.739  15.009  -38.215 1.00 20.00 ? 336  THR A C     1 
ATOM   2581  O O     . THR A  1  336 ? 56.411  14.724  -39.367 1.00 20.77 ? 336  THR A O     1 
ATOM   2582  C CB    . THR A  1  336 ? 55.785  17.296  -37.848 1.00 20.51 ? 336  THR A CB    1 
ATOM   2583  O OG1   . THR A  1  336 ? 57.014  17.957  -37.530 1.00 21.60 ? 336  THR A OG1   1 
ATOM   2584  C CG2   . THR A  1  336 ? 54.620  18.051  -37.231 1.00 20.59 ? 336  THR A CG2   1 
ATOM   2585  N N     . THR A  1  337 ? 57.894  14.628  -37.675 1.00 18.71 ? 337  THR A N     1 
ATOM   2586  C CA    . THR A  1  337 ? 58.843  13.791  -38.403 1.00 16.87 ? 337  THR A CA    1 
ATOM   2587  C C     . THR A  1  337 ? 58.709  12.402  -37.794 1.00 15.87 ? 337  THR A C     1 
ATOM   2588  O O     . THR A  1  337 ? 58.973  12.206  -36.609 1.00 14.40 ? 337  THR A O     1 
ATOM   2589  C CB    . THR A  1  337 ? 60.289  14.281  -38.231 1.00 18.21 ? 337  THR A CB    1 
ATOM   2590  O OG1   . THR A  1  337 ? 60.429  15.571  -38.841 1.00 21.37 ? 337  THR A OG1   1 
ATOM   2591  C CG2   . THR A  1  337 ? 61.259  13.312  -38.884 1.00 17.53 ? 337  THR A CG2   1 
ATOM   2592  N N     . PRO A  1  338 ? 58.295  11.416  -38.599 1.00 15.49 ? 338  PRO A N     1 
ATOM   2593  C CA    . PRO A  1  338 ? 58.128  10.056  -38.090 1.00 16.31 ? 338  PRO A CA    1 
ATOM   2594  C C     . PRO A  1  338 ? 59.411  9.292   -37.779 1.00 14.29 ? 338  PRO A C     1 
ATOM   2595  O O     . PRO A  1  338 ? 60.391  9.374   -38.519 1.00 13.62 ? 338  PRO A O     1 
ATOM   2596  C CB    . PRO A  1  338 ? 57.320  9.384   -39.193 1.00 17.46 ? 338  PRO A CB    1 
ATOM   2597  C CG    . PRO A  1  338 ? 57.872  10.019  -40.420 1.00 18.66 ? 338  PRO A CG    1 
ATOM   2598  C CD    . PRO A  1  338 ? 57.949  11.486  -40.031 1.00 16.45 ? 338  PRO A CD    1 
ATOM   2599  N N     . PRO A  1  339 ? 59.423  8.565   -36.652 1.00 13.85 ? 339  PRO A N     1 
ATOM   2600  C CA    . PRO A  1  339 ? 60.598  7.777   -36.265 1.00 13.58 ? 339  PRO A CA    1 
ATOM   2601  C C     . PRO A  1  339 ? 60.490  6.521   -37.127 1.00 12.97 ? 339  PRO A C     1 
ATOM   2602  O O     . PRO A  1  339 ? 59.567  5.730   -36.949 1.00 11.52 ? 339  PRO A O     1 
ATOM   2603  C CB    . PRO A  1  339 ? 60.349  7.471   -34.787 1.00 14.12 ? 339  PRO A CB    1 
ATOM   2604  C CG    . PRO A  1  339 ? 59.374  8.542   -34.352 1.00 17.11 ? 339  PRO A CG    1 
ATOM   2605  C CD    . PRO A  1  339 ? 58.468  8.659   -35.536 1.00 14.15 ? 339  PRO A CD    1 
ATOM   2606  N N     . PHE A  1  340 ? 61.411  6.350   -38.069 1.00 11.59 ? 340  PHE A N     1 
ATOM   2607  C CA    . PHE A  1  340 ? 61.364  5.199   -38.963 1.00 11.04 ? 340  PHE A CA    1 
ATOM   2608  C C     . PHE A  1  340 ? 61.340  3.877   -38.208 1.00 10.34 ? 340  PHE A C     1 
ATOM   2609  O O     . PHE A  1  340 ? 62.137  3.659   -37.297 1.00 10.94 ? 340  PHE A O     1 
ATOM   2610  C CB    . PHE A  1  340 ? 62.558  5.214   -39.917 1.00 10.22 ? 340  PHE A CB    1 
ATOM   2611  C CG    . PHE A  1  340 ? 62.370  4.347   -41.128 1.00 10.09 ? 340  PHE A CG    1 
ATOM   2612  C CD1   . PHE A  1  340 ? 61.657  4.816   -42.226 1.00 10.63 ? 340  PHE A CD1   1 
ATOM   2613  C CD2   . PHE A  1  340 ? 62.881  3.052   -41.161 1.00 9.96  ? 340  PHE A CD2   1 
ATOM   2614  C CE1   . PHE A  1  340 ? 61.453  4.011   -43.340 1.00 10.91 ? 340  PHE A CE1   1 
ATOM   2615  C CE2   . PHE A  1  340 ? 62.681  2.236   -42.275 1.00 9.59  ? 340  PHE A CE2   1 
ATOM   2616  C CZ    . PHE A  1  340 ? 61.965  2.716   -43.366 1.00 9.78  ? 340  PHE A CZ    1 
ATOM   2617  N N     . GLY A  1  341 ? 60.421  2.999   -38.598 1.00 9.62  ? 341  GLY A N     1 
ATOM   2618  C CA    . GLY A  1  341 ? 60.312  1.704   -37.957 1.00 11.03 ? 341  GLY A CA    1 
ATOM   2619  C C     . GLY A  1  341 ? 59.315  1.653   -36.814 1.00 11.52 ? 341  GLY A C     1 
ATOM   2620  O O     . GLY A  1  341 ? 58.862  0.570   -36.442 1.00 12.14 ? 341  GLY A O     1 
ATOM   2621  N N     . PHE A  1  342 ? 58.971  2.809   -36.250 1.00 13.28 ? 342  PHE A N     1 
ATOM   2622  C CA    . PHE A  1  342 ? 58.018  2.847   -35.142 1.00 13.22 ? 342  PHE A CA    1 
ATOM   2623  C C     . PHE A  1  342 ? 56.672  2.362   -35.656 1.00 14.12 ? 342  PHE A C     1 
ATOM   2624  O O     . PHE A  1  342 ? 56.051  1.469   -35.081 1.00 14.36 ? 342  PHE A O     1 
ATOM   2625  C CB    . PHE A  1  342 ? 57.882  4.263   -34.585 1.00 15.01 ? 342  PHE A CB    1 
ATOM   2626  C CG    . PHE A  1  342 ? 57.205  4.314   -33.249 1.00 18.29 ? 342  PHE A CG    1 
ATOM   2627  C CD1   . PHE A  1  342 ? 57.844  3.817   -32.116 1.00 20.61 ? 342  PHE A CD1   1 
ATOM   2628  C CD2   . PHE A  1  342 ? 55.916  4.819   -33.125 1.00 20.28 ? 342  PHE A CD2   1 
ATOM   2629  C CE1   . PHE A  1  342 ? 57.206  3.820   -30.877 1.00 22.91 ? 342  PHE A CE1   1 
ATOM   2630  C CE2   . PHE A  1  342 ? 55.267  4.828   -31.890 1.00 22.45 ? 342  PHE A CE2   1 
ATOM   2631  C CZ    . PHE A  1  342 ? 55.915  4.326   -30.765 1.00 22.75 ? 342  PHE A CZ    1 
ATOM   2632  N N     . PHE A  1  343 ? 56.214  2.979   -36.736 1.00 14.41 ? 343  PHE A N     1 
ATOM   2633  C CA    . PHE A  1  343 ? 54.977  2.572   -37.373 1.00 14.84 ? 343  PHE A CA    1 
ATOM   2634  C C     . PHE A  1  343 ? 55.481  1.759   -38.568 1.00 13.78 ? 343  PHE A C     1 
ATOM   2635  O O     . PHE A  1  343 ? 56.561  2.032   -39.092 1.00 12.53 ? 343  PHE A O     1 
ATOM   2636  C CB    . PHE A  1  343 ? 54.174  3.814   -37.756 1.00 17.14 ? 343  PHE A CB    1 
ATOM   2637  C CG    . PHE A  1  343 ? 53.709  4.602   -36.557 1.00 20.81 ? 343  PHE A CG    1 
ATOM   2638  C CD1   . PHE A  1  343 ? 53.810  5.988   -36.522 1.00 23.15 ? 343  PHE A CD1   1 
ATOM   2639  C CD2   . PHE A  1  343 ? 53.184  3.941   -35.446 1.00 22.01 ? 343  PHE A CD2   1 
ATOM   2640  C CE1   . PHE A  1  343 ? 53.397  6.706   -35.394 1.00 25.68 ? 343  PHE A CE1   1 
ATOM   2641  C CE2   . PHE A  1  343 ? 52.770  4.646   -34.318 1.00 24.53 ? 343  PHE A CE2   1 
ATOM   2642  C CZ    . PHE A  1  343 ? 52.876  6.032   -34.292 1.00 24.52 ? 343  PHE A CZ    1 
ATOM   2643  N N     . PRO A  1  344 ? 54.724  0.739   -38.998 1.00 13.77 ? 344  PRO A N     1 
ATOM   2644  C CA    . PRO A  1  344 ? 55.134  -0.114  -40.122 1.00 12.53 ? 344  PRO A CA    1 
ATOM   2645  C C     . PRO A  1  344 ? 55.396  0.514   -41.490 1.00 13.23 ? 344  PRO A C     1 
ATOM   2646  O O     . PRO A  1  344 ? 56.091  -0.079  -42.308 1.00 11.40 ? 344  PRO A O     1 
ATOM   2647  C CB    . PRO A  1  344 ? 54.040  -1.178  -40.160 1.00 13.55 ? 344  PRO A CB    1 
ATOM   2648  C CG    . PRO A  1  344 ? 52.831  -0.423  -39.717 1.00 12.01 ? 344  PRO A CG    1 
ATOM   2649  C CD    . PRO A  1  344 ? 53.355  0.408   -38.561 1.00 14.22 ? 344  PRO A CD    1 
ATOM   2650  N N     . SER A  1  345 ? 54.847  1.696   -41.743 1.00 14.73 ? 345  SER A N     1 
ATOM   2651  C CA    . SER A  1  345 ? 55.067  2.362   -43.023 1.00 18.22 ? 345  SER A CA    1 
ATOM   2652  C C     . SER A  1  345 ? 55.027  3.875   -42.863 1.00 19.09 ? 345  SER A C     1 
ATOM   2653  O O     . SER A  1  345 ? 54.637  4.392   -41.820 1.00 17.63 ? 345  SER A O     1 
ATOM   2654  C CB    . SER A  1  345 ? 54.024  1.913   -44.051 1.00 19.74 ? 345  SER A CB    1 
ATOM   2655  O OG    . SER A  1  345 ? 52.728  2.348   -43.695 1.00 24.08 ? 345  SER A OG    1 
ATOM   2656  N N     . SER A  1  346 ? 55.434  4.582   -43.908 1.00 21.48 ? 346  SER A N     1 
ATOM   2657  C CA    . SER A  1  346 ? 55.472  6.034   -43.888 1.00 24.73 ? 346  SER A CA    1 
ATOM   2658  C C     . SER A  1  346 ? 54.101  6.707   -43.941 1.00 26.02 ? 346  SER A C     1 
ATOM   2659  O O     . SER A  1  346 ? 53.950  7.845   -43.507 1.00 28.04 ? 346  SER A O     1 
ATOM   2660  C CB    . SER A  1  346 ? 56.359  6.537   -45.033 1.00 25.24 ? 346  SER A CB    1 
ATOM   2661  O OG    . SER A  1  346 ? 56.001  5.941   -46.262 0.50 23.27 ? 346  SER A OG    1 
ATOM   2662  N N     . SER A  1  347 ? 53.101  6.013   -44.466 1.00 25.99 ? 347  SER A N     1 
ATOM   2663  C CA    . SER A  1  347 ? 51.769  6.596   -44.541 1.00 27.54 ? 347  SER A CA    1 
ATOM   2664  C C     . SER A  1  347 ? 51.000  6.265   -43.270 1.00 27.03 ? 347  SER A C     1 
ATOM   2665  O O     . SER A  1  347 ? 50.109  5.410   -43.266 1.00 28.54 ? 347  SER A O     1 
ATOM   2666  C CB    . SER A  1  347 ? 51.022  6.076   -45.771 1.00 28.68 ? 347  SER A CB    1 
ATOM   2667  O OG    . SER A  1  347 ? 50.750  4.697   -45.654 1.00 32.61 ? 347  SER A OG    1 
ATOM   2668  N N     . TYR A  1  348 ? 51.367  6.947   -42.190 1.00 24.97 ? 348  TYR A N     1 
ATOM   2669  C CA    . TYR A  1  348 ? 50.742  6.751   -40.888 1.00 22.58 ? 348  TYR A CA    1 
ATOM   2670  C C     . TYR A  1  348 ? 50.523  8.136   -40.279 1.00 21.29 ? 348  TYR A C     1 
ATOM   2671  O O     . TYR A  1  348 ? 51.351  9.027   -40.450 1.00 21.94 ? 348  TYR A O     1 
ATOM   2672  C CB    . TYR A  1  348 ? 51.675  5.941   -39.986 1.00 22.49 ? 348  TYR A CB    1 
ATOM   2673  C CG    . TYR A  1  348 ? 50.982  5.280   -38.823 1.00 21.51 ? 348  TYR A CG    1 
ATOM   2674  C CD1   . TYR A  1  348 ? 50.449  3.997   -38.945 1.00 22.05 ? 348  TYR A CD1   1 
ATOM   2675  C CD2   . TYR A  1  348 ? 50.843  5.939   -37.602 1.00 20.01 ? 348  TYR A CD2   1 
ATOM   2676  C CE1   . TYR A  1  348 ? 49.794  3.386   -37.876 1.00 20.26 ? 348  TYR A CE1   1 
ATOM   2677  C CE2   . TYR A  1  348 ? 50.191  5.337   -36.527 1.00 19.10 ? 348  TYR A CE2   1 
ATOM   2678  C CZ    . TYR A  1  348 ? 49.668  4.062   -36.673 1.00 20.55 ? 348  TYR A CZ    1 
ATOM   2679  O OH    . TYR A  1  348 ? 49.001  3.470   -35.626 1.00 18.81 ? 348  TYR A OH    1 
ATOM   2680  N N     . PRO A  1  349 ? 49.405  8.337   -39.565 1.00 19.98 ? 349  PRO A N     1 
ATOM   2681  C CA    . PRO A  1  349 ? 49.133  9.644   -38.953 1.00 19.57 ? 349  PRO A CA    1 
ATOM   2682  C C     . PRO A  1  349 ? 50.130  10.034  -37.859 1.00 19.15 ? 349  PRO A C     1 
ATOM   2683  O O     . PRO A  1  349 ? 50.614  9.187   -37.111 1.00 18.20 ? 349  PRO A O     1 
ATOM   2684  C CB    . PRO A  1  349 ? 47.707  9.485   -38.428 1.00 19.38 ? 349  PRO A CB    1 
ATOM   2685  C CG    . PRO A  1  349 ? 47.632  8.023   -38.107 1.00 18.12 ? 349  PRO A CG    1 
ATOM   2686  C CD    . PRO A  1  349 ? 48.306  7.393   -39.301 1.00 19.87 ? 349  PRO A CD    1 
ATOM   2687  N N     . LEU A  1  350 ? 50.425  11.328  -37.776 1.00 19.03 ? 350  LEU A N     1 
ATOM   2688  C CA    . LEU A  1  350 ? 51.364  11.860  -36.795 1.00 20.54 ? 350  LEU A CA    1 
ATOM   2689  C C     . LEU A  1  350 ? 50.643  12.396  -35.558 1.00 18.90 ? 350  LEU A C     1 
ATOM   2690  O O     . LEU A  1  350 ? 49.563  12.976  -35.660 1.00 20.96 ? 350  LEU A O     1 
ATOM   2691  C CB    . LEU A  1  350 ? 52.178  12.986  -37.432 1.00 22.96 ? 350  LEU A CB    1 
ATOM   2692  C CG    . LEU A  1  350 ? 53.010  12.590  -38.654 1.00 25.52 ? 350  LEU A CG    1 
ATOM   2693  C CD1   . LEU A  1  350 ? 53.028  13.735  -39.652 1.00 27.20 ? 350  LEU A CD1   1 
ATOM   2694  C CD2   . LEU A  1  350 ? 54.416  12.213  -38.220 1.00 25.78 ? 350  LEU A CD2   1 
ATOM   2695  N N     . PRO A  1  351 ? 51.232  12.197  -34.369 1.00 18.35 ? 351  PRO A N     1 
ATOM   2696  C CA    . PRO A  1  351 ? 50.610  12.683  -33.135 1.00 17.42 ? 351  PRO A CA    1 
ATOM   2697  C C     . PRO A  1  351 ? 50.949  14.151  -32.889 1.00 17.48 ? 351  PRO A C     1 
ATOM   2698  O O     . PRO A  1  351 ? 52.124  14.522  -32.886 1.00 16.78 ? 351  PRO A O     1 
ATOM   2699  C CB    . PRO A  1  351 ? 51.212  11.770  -32.074 1.00 17.05 ? 351  PRO A CB    1 
ATOM   2700  C CG    . PRO A  1  351 ? 52.606  11.572  -32.582 1.00 17.32 ? 351  PRO A CG    1 
ATOM   2701  C CD    . PRO A  1  351 ? 52.390  11.335  -34.070 1.00 17.08 ? 351  PRO A CD    1 
ATOM   2702  N N     . ASN A  1  352 ? 49.927  14.984  -32.700 1.00 18.09 ? 352  ASN A N     1 
ATOM   2703  C CA    . ASN A  1  352 ? 50.160  16.401  -32.445 1.00 19.23 ? 352  ASN A CA    1 
ATOM   2704  C C     . ASN A  1  352 ? 50.033  16.734  -30.958 1.00 18.40 ? 352  ASN A C     1 
ATOM   2705  O O     . ASN A  1  352 ? 50.031  17.902  -30.564 1.00 17.94 ? 352  ASN A O     1 
ATOM   2706  C CB    . ASN A  1  352 ? 49.227  17.287  -33.302 1.00 22.89 ? 352  ASN A CB    1 
ATOM   2707  C CG    . ASN A  1  352 ? 47.746  16.960  -33.128 1.00 28.42 ? 352  ASN A CG    1 
ATOM   2708  O OD1   . ASN A  1  352 ? 47.193  17.099  -32.036 1.00 29.23 ? 352  ASN A OD1   1 
ATOM   2709  N ND2   . ASN A  1  352 ? 47.110  16.541  -34.222 1.00 32.92 ? 352  ASN A ND2   1 
ATOM   2710  N N     . SER A  1  353 ? 49.945  15.687  -30.140 1.00 15.68 ? 353  SER A N     1 
ATOM   2711  C CA    . SER A  1  353 ? 49.850  15.815  -28.686 1.00 15.33 ? 353  SER A CA    1 
ATOM   2712  C C     . SER A  1  353 ? 50.583  14.618  -28.079 1.00 15.22 ? 353  SER A C     1 
ATOM   2713  O O     . SER A  1  353 ? 50.997  13.718  -28.811 1.00 14.14 ? 353  SER A O     1 
ATOM   2714  C CB    . SER A  1  353 ? 48.383  15.815  -28.237 1.00 17.38 ? 353  SER A CB    1 
ATOM   2715  O OG    . SER A  1  353 ? 47.710  14.638  -28.651 1.00 19.17 ? 353  SER A OG    1 
ATOM   2716  N N     . THR A  1  354 ? 50.755  14.602  -26.758 1.00 13.32 ? 354  THR A N     1 
ATOM   2717  C CA    . THR A  1  354 ? 51.443  13.477  -26.120 1.00 13.27 ? 354  THR A CA    1 
ATOM   2718  C C     . THR A  1  354 ? 50.608  12.215  -26.301 1.00 11.47 ? 354  THR A C     1 
ATOM   2719  O O     . THR A  1  354 ? 49.381  12.279  -26.386 1.00 12.51 ? 354  THR A O     1 
ATOM   2720  C CB    . THR A  1  354 ? 51.685  13.716  -24.606 1.00 13.53 ? 354  THR A CB    1 
ATOM   2721  O OG1   . THR A  1  354 ? 50.438  13.960  -23.945 1.00 13.96 ? 354  THR A OG1   1 
ATOM   2722  C CG2   . THR A  1  354 ? 52.612  14.908  -24.394 1.00 14.80 ? 354  THR A CG2   1 
ATOM   2723  N N     . PHE A  1  355 ? 51.265  11.062  -26.368 1.00 10.75 ? 355  PHE A N     1 
ATOM   2724  C CA    . PHE A  1  355 ? 50.533  9.818   -26.559 1.00 10.69 ? 355  PHE A CA    1 
ATOM   2725  C C     . PHE A  1  355 ? 51.174  8.646   -25.836 1.00 8.90  ? 355  PHE A C     1 
ATOM   2726  O O     . PHE A  1  355 ? 52.309  8.735   -25.369 1.00 8.25  ? 355  PHE A O     1 
ATOM   2727  C CB    . PHE A  1  355 ? 50.416  9.500   -28.057 1.00 12.95 ? 355  PHE A CB    1 
ATOM   2728  C CG    . PHE A  1  355 ? 51.707  9.063   -28.697 1.00 13.93 ? 355  PHE A CG    1 
ATOM   2729  C CD1   . PHE A  1  355 ? 51.942  7.717   -28.967 1.00 16.24 ? 355  PHE A CD1   1 
ATOM   2730  C CD2   . PHE A  1  355 ? 52.685  9.993   -29.034 1.00 14.98 ? 355  PHE A CD2   1 
ATOM   2731  C CE1   . PHE A  1  355 ? 53.134  7.304   -29.566 1.00 17.03 ? 355  PHE A CE1   1 
ATOM   2732  C CE2   . PHE A  1  355 ? 53.880  9.593   -29.631 1.00 17.47 ? 355  PHE A CE2   1 
ATOM   2733  C CZ    . PHE A  1  355 ? 54.104  8.245   -29.898 1.00 18.40 ? 355  PHE A CZ    1 
ATOM   2734  N N     . ALA A  1  356 ? 50.419  7.558   -25.737 1.00 10.19 ? 356  ALA A N     1 
ATOM   2735  C CA    . ALA A  1  356 ? 50.885  6.336   -25.099 1.00 9.31  ? 356  ALA A CA    1 
ATOM   2736  C C     . ALA A  1  356 ? 50.780  5.219   -26.125 1.00 8.90  ? 356  ALA A C     1 
ATOM   2737  O O     . ALA A  1  356 ? 49.759  5.077   -26.804 1.00 8.40  ? 356  ALA A O     1 
ATOM   2738  C CB    . ALA A  1  356 ? 50.030  6.012   -23.883 1.00 10.62 ? 356  ALA A CB    1 
ATOM   2739  N N     . HIS A  1  357 ? 51.846  4.436   -26.228 1.00 9.34  ? 357  HIS A N     1 
ATOM   2740  C CA    . HIS A  1  357 ? 51.932  3.322   -27.164 1.00 8.84  ? 357  HIS A CA    1 
ATOM   2741  C C     . HIS A  1  357 ? 51.880  2.007   -26.386 1.00 10.02 ? 357  HIS A C     1 
ATOM   2742  O O     . HIS A  1  357 ? 52.836  1.665   -25.698 1.00 12.29 ? 357  HIS A O     1 
ATOM   2743  C CB    . HIS A  1  357 ? 53.263  3.431   -27.920 1.00 9.44  ? 357  HIS A CB    1 
ATOM   2744  C CG    . HIS A  1  357 ? 53.501  2.353   -28.933 1.00 9.43  ? 357  HIS A CG    1 
ATOM   2745  N ND1   . HIS A  1  357 ? 52.881  2.335   -30.164 1.00 10.17 ? 357  HIS A ND1   1 
ATOM   2746  C CD2   . HIS A  1  357 ? 54.365  1.310   -28.933 1.00 11.31 ? 357  HIS A CD2   1 
ATOM   2747  C CE1   . HIS A  1  357 ? 53.360  1.333   -30.882 1.00 12.22 ? 357  HIS A CE1   1 
ATOM   2748  N NE2   . HIS A  1  357 ? 54.262  0.696   -30.159 1.00 10.19 ? 357  HIS A NE2   1 
ATOM   2749  N N     . PHE A  1  358 ? 50.764  1.287   -26.471 1.00 8.87  ? 358  PHE A N     1 
ATOM   2750  C CA    . PHE A  1  358 ? 50.646  -0.004  -25.794 1.00 8.91  ? 358  PHE A CA    1 
ATOM   2751  C C     . PHE A  1  358 ? 51.057  -1.056  -26.819 1.00 9.65  ? 358  PHE A C     1 
ATOM   2752  O O     . PHE A  1  358 ? 50.385  -1.241  -27.835 1.00 9.50  ? 358  PHE A O     1 
ATOM   2753  C CB    . PHE A  1  358 ? 49.210  -0.256  -25.316 1.00 9.77  ? 358  PHE A CB    1 
ATOM   2754  C CG    . PHE A  1  358 ? 48.826  0.545   -24.099 1.00 8.59  ? 358  PHE A CG    1 
ATOM   2755  C CD1   . PHE A  1  358 ? 48.310  1.830   -24.228 1.00 11.14 ? 358  PHE A CD1   1 
ATOM   2756  C CD2   . PHE A  1  358 ? 49.016  0.025   -22.822 1.00 12.12 ? 358  PHE A CD2   1 
ATOM   2757  C CE1   . PHE A  1  358 ? 47.989  2.589   -23.098 1.00 11.11 ? 358  PHE A CE1   1 
ATOM   2758  C CE2   . PHE A  1  358 ? 48.699  0.774   -21.687 1.00 11.45 ? 358  PHE A CE2   1 
ATOM   2759  C CZ    . PHE A  1  358 ? 48.184  2.060   -21.828 1.00 11.81 ? 358  PHE A CZ    1 
ATOM   2760  N N     . ALA A  1  359 ? 52.166  -1.739  -26.548 1.00 8.34  ? 359  ALA A N     1 
ATOM   2761  C CA    . ALA A  1  359 ? 52.694  -2.731  -27.478 1.00 8.78  ? 359  ALA A CA    1 
ATOM   2762  C C     . ALA A  1  359 ? 52.595  -4.172  -26.993 1.00 9.28  ? 359  ALA A C     1 
ATOM   2763  O O     . ALA A  1  359 ? 52.656  -4.450  -25.794 1.00 8.77  ? 359  ALA A O     1 
ATOM   2764  C CB    . ALA A  1  359 ? 54.145  -2.392  -27.806 1.00 9.09  ? 359  ALA A CB    1 
ATOM   2765  N N     . SER A  1  360 ? 52.450  -5.086  -27.947 1.00 7.90  ? 360  SER A N     1 
ATOM   2766  C CA    . SER A  1  360 ? 52.337  -6.509  -27.647 1.00 8.16  ? 360  SER A CA    1 
ATOM   2767  C C     . SER A  1  360 ? 53.228  -7.314  -28.597 1.00 8.83  ? 360  SER A C     1 
ATOM   2768  O O     . SER A  1  360 ? 53.084  -7.235  -29.820 1.00 8.96  ? 360  SER A O     1 
ATOM   2769  C CB    . SER A  1  360 ? 50.876  -6.950  -27.784 1.00 8.98  ? 360  SER A CB    1 
ATOM   2770  O OG    . SER A  1  360 ? 50.699  -8.292  -27.358 1.00 8.14  ? 360  SER A OG    1 
ATOM   2771  N N     . LYS A  1  361 ? 54.153  -8.075  -28.019 1.00 7.71  ? 361  LYS A N     1 
ATOM   2772  C CA    . LYS A  1  361 ? 55.096  -8.894  -28.777 1.00 7.64  ? 361  LYS A CA    1 
ATOM   2773  C C     . LYS A  1  361 ? 54.732  -10.375 -28.691 1.00 7.17  ? 361  LYS A C     1 
ATOM   2774  O O     . LYS A  1  361 ? 54.611  -10.923 -27.601 1.00 7.73  ? 361  LYS A O     1 
ATOM   2775  C CB    . LYS A  1  361 ? 56.516  -8.692  -28.223 1.00 8.29  ? 361  LYS A CB    1 
ATOM   2776  C CG    . LYS A  1  361 ? 57.604  -9.555  -28.866 1.00 9.56  ? 361  LYS A CG    1 
ATOM   2777  C CD    . LYS A  1  361 ? 58.943  -9.373  -28.148 1.00 10.26 ? 361  LYS A CD    1 
ATOM   2778  C CE    . LYS A  1  361 ? 60.028  -10.247 -28.757 1.00 10.35 ? 361  LYS A CE    1 
ATOM   2779  N NZ    . LYS A  1  361 ? 61.306  -10.209 -27.978 1.00 8.93  ? 361  LYS A NZ    1 
ATOM   2780  N N     . VAL A  1  362 ? 54.550  -11.020 -29.839 1.00 7.27  ? 362  VAL A N     1 
ATOM   2781  C CA    . VAL A  1  362 ? 54.232  -12.443 -29.848 1.00 7.67  ? 362  VAL A CA    1 
ATOM   2782  C C     . VAL A  1  362 ? 55.504  -13.238 -29.554 1.00 8.77  ? 362  VAL A C     1 
ATOM   2783  O O     . VAL A  1  362 ? 56.575  -12.929 -30.079 1.00 8.20  ? 362  VAL A O     1 
ATOM   2784  C CB    . VAL A  1  362 ? 53.653  -12.882 -31.217 1.00 8.62  ? 362  VAL A CB    1 
ATOM   2785  C CG1   . VAL A  1  362 ? 53.559  -14.400 -31.287 1.00 9.66  ? 362  VAL A CG1   1 
ATOM   2786  C CG2   . VAL A  1  362 ? 52.275  -12.266 -31.414 1.00 9.76  ? 362  VAL A CG2   1 
ATOM   2787  N N     . ALA A  1  363 ? 55.380  -14.248 -28.699 1.00 7.53  ? 363  ALA A N     1 
ATOM   2788  C CA    . ALA A  1  363 ? 56.508  -15.103 -28.328 1.00 8.24  ? 363  ALA A CA    1 
ATOM   2789  C C     . ALA A  1  363 ? 57.030  -15.895 -29.530 1.00 9.02  ? 363  ALA A C     1 
ATOM   2790  O O     . ALA A  1  363 ? 56.295  -16.145 -30.483 1.00 8.53  ? 363  ALA A O     1 
ATOM   2791  C CB    . ALA A  1  363 ? 56.081  -16.062 -27.222 1.00 8.99  ? 363  ALA A CB    1 
ATOM   2792  N N     . GLY A  1  364 ? 58.299  -16.293 -29.474 1.00 8.69  ? 364  GLY A N     1 
ATOM   2793  C CA    . GLY A  1  364 ? 58.887  -17.058 -30.561 1.00 8.36  ? 364  GLY A CA    1 
ATOM   2794  C C     . GLY A  1  364 ? 59.716  -16.205 -31.501 1.00 7.98  ? 364  GLY A C     1 
ATOM   2795  O O     . GLY A  1  364 ? 60.814  -15.780 -31.141 1.00 9.04  ? 364  GLY A O     1 
ATOM   2796  N N     . PRO A  1  365 ? 59.231  -15.946 -32.726 1.00 7.08  ? 365  PRO A N     1 
ATOM   2797  C CA    . PRO A  1  365 ? 57.955  -16.406 -33.285 1.00 7.21  ? 365  PRO A CA    1 
ATOM   2798  C C     . PRO A  1  365 ? 58.174  -17.737 -33.993 1.00 7.30  ? 365  PRO A C     1 
ATOM   2799  O O     . PRO A  1  365 ? 59.314  -18.115 -34.267 1.00 8.74  ? 365  PRO A O     1 
ATOM   2800  C CB    . PRO A  1  365 ? 57.611  -15.302 -34.267 1.00 7.83  ? 365  PRO A CB    1 
ATOM   2801  C CG    . PRO A  1  365 ? 58.964  -15.000 -34.858 1.00 7.54  ? 365  PRO A CG    1 
ATOM   2802  C CD    . PRO A  1  365 ? 59.877  -14.981 -33.636 1.00 7.91  ? 365  PRO A CD    1 
ATOM   2803  N N     . LEU A  1  366 ? 57.090  -18.441 -34.297 1.00 8.37  ? 366  LEU A N     1 
ATOM   2804  C CA    . LEU A  1  366 ? 57.209  -19.716 -34.994 1.00 9.21  ? 366  LEU A CA    1 
ATOM   2805  C C     . LEU A  1  366 ? 57.443  -19.478 -36.485 1.00 8.63  ? 366  LEU A C     1 
ATOM   2806  O O     . LEU A  1  366 ? 58.101  -20.276 -37.153 1.00 8.70  ? 366  LEU A O     1 
ATOM   2807  C CB    . LEU A  1  366 ? 55.945  -20.559 -34.776 1.00 10.01 ? 366  LEU A CB    1 
ATOM   2808  C CG    . LEU A  1  366 ? 55.746  -21.071 -33.345 1.00 11.19 ? 366  LEU A CG    1 
ATOM   2809  C CD1   . LEU A  1  366 ? 54.424  -21.804 -33.233 1.00 10.46 ? 366  LEU A CD1   1 
ATOM   2810  C CD2   . LEU A  1  366 ? 56.900  -21.994 -32.969 1.00 13.58 ? 366  LEU A CD2   1 
ATOM   2811  N N     . SER A  1  367 ? 56.905  -18.371 -36.996 1.00 8.02  ? 367  SER A N     1 
ATOM   2812  C CA    . SER A  1  367 ? 57.043  -18.007 -38.404 1.00 6.30  ? 367  SER A CA    1 
ATOM   2813  C C     . SER A  1  367 ? 58.463  -17.546 -38.684 1.00 6.93  ? 367  SER A C     1 
ATOM   2814  O O     . SER A  1  367 ? 59.102  -16.935 -37.828 1.00 6.10  ? 367  SER A O     1 
ATOM   2815  C CB    . SER A  1  367 ? 56.084  -16.866 -38.757 1.00 7.23  ? 367  SER A CB    1 
ATOM   2816  O OG    . SER A  1  367 ? 54.740  -17.223 -38.506 1.00 6.91  ? 367  SER A OG    1 
ATOM   2817  N N     . TYR A  1  368 ? 58.953  -17.830 -39.884 1.00 6.15  ? 368  TYR A N     1 
ATOM   2818  C CA    . TYR A  1  368 ? 60.295  -17.416 -40.254 1.00 7.83  ? 368  TYR A CA    1 
ATOM   2819  C C     . TYR A  1  368 ? 60.455  -17.245 -41.757 1.00 7.70  ? 368  TYR A C     1 
ATOM   2820  O O     . TYR A  1  368 ? 59.627  -17.713 -42.548 1.00 7.26  ? 368  TYR A O     1 
ATOM   2821  C CB    . TYR A  1  368 ? 61.328  -18.419 -39.728 1.00 7.87  ? 368  TYR A CB    1 
ATOM   2822  C CG    . TYR A  1  368 ? 61.244  -19.792 -40.355 1.00 9.96  ? 368  TYR A CG    1 
ATOM   2823  C CD1   . TYR A  1  368 ? 61.843  -20.059 -41.589 1.00 11.09 ? 368  TYR A CD1   1 
ATOM   2824  C CD2   . TYR A  1  368 ? 60.559  -20.823 -39.720 1.00 13.61 ? 368  TYR A CD2   1 
ATOM   2825  C CE1   . TYR A  1  368 ? 61.758  -21.329 -42.172 1.00 13.89 ? 368  TYR A CE1   1 
ATOM   2826  C CE2   . TYR A  1  368 ? 60.466  -22.090 -40.291 1.00 14.69 ? 368  TYR A CE2   1 
ATOM   2827  C CZ    . TYR A  1  368 ? 61.065  -22.336 -41.512 1.00 15.24 ? 368  TYR A CZ    1 
ATOM   2828  O OH    . TYR A  1  368 ? 60.961  -23.590 -42.070 1.00 17.64 ? 368  TYR A OH    1 
ATOM   2829  N N     . GLY A  1  369 ? 61.527  -16.552 -42.131 1.00 8.28  ? 369  GLY A N     1 
ATOM   2830  C CA    . GLY A  1  369 ? 61.840  -16.313 -43.528 1.00 7.93  ? 369  GLY A CA    1 
ATOM   2831  C C     . GLY A  1  369 ? 63.329  -16.494 -43.752 1.00 9.92  ? 369  GLY A C     1 
ATOM   2832  O O     . GLY A  1  369 ? 63.996  -17.221 -43.008 1.00 11.14 ? 369  GLY A O     1 
ATOM   2833  N N     . SER A  1  370 ? 63.864  -15.834 -44.773 1.00 8.78  ? 370  SER A N     1 
ATOM   2834  C CA    . SER A  1  370 ? 65.282  -15.956 -45.069 1.00 9.61  ? 370  SER A CA    1 
ATOM   2835  C C     . SER A  1  370 ? 65.912  -14.649 -45.512 1.00 9.30  ? 370  SER A C     1 
ATOM   2836  O O     . SER A  1  370 ? 65.223  -13.664 -45.802 1.00 9.15  ? 370  SER A O     1 
ATOM   2837  C CB    . SER A  1  370 ? 65.511  -17.012 -46.155 1.00 10.90 ? 370  SER A CB    1 
ATOM   2838  O OG    . SER A  1  370 ? 64.973  -16.588 -47.394 1.00 13.60 ? 370  SER A OG    1 
ATOM   2839  N N     . LEU A  1  371 ? 67.238  -14.660 -45.563 1.00 9.20  ? 371  LEU A N     1 
ATOM   2840  C CA    . LEU A  1  371 ? 68.013  -13.505 -45.978 1.00 9.66  ? 371  LEU A CA    1 
ATOM   2841  C C     . LEU A  1  371 ? 68.788  -13.861 -47.242 1.00 10.28 ? 371  LEU A C     1 
ATOM   2842  O O     . LEU A  1  371 ? 69.342  -14.955 -47.349 1.00 11.51 ? 371  LEU A O     1 
ATOM   2843  C CB    . LEU A  1  371 ? 68.982  -13.097 -44.858 1.00 9.59  ? 371  LEU A CB    1 
ATOM   2844  C CG    . LEU A  1  371 ? 69.955  -11.936 -45.101 1.00 7.31  ? 371  LEU A CG    1 
ATOM   2845  C CD1   . LEU A  1  371 ? 70.368  -11.345 -43.762 1.00 8.52  ? 371  LEU A CD1   1 
ATOM   2846  C CD2   . LEU A  1  371 ? 71.177  -12.409 -45.884 1.00 6.50  ? 371  LEU A CD2   1 
ATOM   2847  N N     . THR A  1  372 ? 68.807  -12.937 -48.196 1.00 10.14 ? 372  THR A N     1 
ATOM   2848  C CA    . THR A  1  372 ? 69.523  -13.121 -49.455 1.00 11.68 ? 372  THR A CA    1 
ATOM   2849  C C     . THR A  1  372 ? 70.252  -11.819 -49.766 1.00 10.85 ? 372  THR A C     1 
ATOM   2850  O O     . THR A  1  372 ? 69.886  -10.759 -49.258 1.00 10.72 ? 372  THR A O     1 
ATOM   2851  C CB    . THR A  1  372 ? 68.557  -13.445 -50.620 1.00 14.87 ? 372  THR A CB    1 
ATOM   2852  O OG1   . THR A  1  372 ? 67.546  -12.431 -50.702 1.00 17.06 ? 372  THR A OG1   1 
ATOM   2853  C CG2   . THR A  1  372 ? 67.898  -14.810 -50.412 1.00 17.40 ? 372  THR A CG2   1 
ATOM   2854  N N     . LEU A  1  373 ? 71.282  -11.892 -50.598 1.00 10.47 ? 373  LEU A N     1 
ATOM   2855  C CA    . LEU A  1  373 ? 72.040  -10.695 -50.948 1.00 9.98  ? 373  LEU A CA    1 
ATOM   2856  C C     . LEU A  1  373 ? 71.340  -9.837  -51.995 1.00 10.89 ? 373  LEU A C     1 
ATOM   2857  O O     . LEU A  1  373 ? 70.668  -10.357 -52.889 1.00 12.21 ? 373  LEU A O     1 
ATOM   2858  C CB    . LEU A  1  373 ? 73.416  -11.085 -51.490 1.00 9.72  ? 373  LEU A CB    1 
ATOM   2859  C CG    . LEU A  1  373 ? 74.348  -11.889 -50.585 1.00 9.93  ? 373  LEU A CG    1 
ATOM   2860  C CD1   . LEU A  1  373 ? 75.591  -12.298 -51.368 1.00 9.69  ? 373  LEU A CD1   1 
ATOM   2861  C CD2   . LEU A  1  373 ? 74.722  -11.054 -49.373 1.00 9.39  ? 373  LEU A CD2   1 
ATOM   2862  N N     . LYS A  1  374 ? 71.483  -8.519  -51.873 1.00 11.37 ? 374  LYS A N     1 
ATOM   2863  C CA    . LYS A  1  374 ? 70.920  -7.615  -52.868 1.00 13.24 ? 374  LYS A CA    1 
ATOM   2864  C C     . LYS A  1  374 ? 72.082  -7.304  -53.807 1.00 14.01 ? 374  LYS A C     1 
ATOM   2865  O O     . LYS A  1  374 ? 71.893  -7.066  -55.000 1.00 17.25 ? 374  LYS A O     1 
ATOM   2866  C CB    . LYS A  1  374 ? 70.412  -6.313  -52.255 1.00 15.61 ? 374  LYS A CB    1 
ATOM   2867  C CG    . LYS A  1  374 ? 69.814  -5.407  -53.324 1.00 19.57 ? 374  LYS A CG    1 
ATOM   2868  C CD    . LYS A  1  374 ? 70.040  -3.936  -53.044 1.00 24.14 ? 374  LYS A CD    1 
ATOM   2869  C CE    . LYS A  1  374 ? 69.728  -3.099  -54.277 1.00 25.09 ? 374  LYS A CE    1 
ATOM   2870  N NZ    . LYS A  1  374 ? 68.339  -3.328  -54.767 1.00 27.43 ? 374  LYS A NZ    1 
ATOM   2871  N N     . SER A  1  375 ? 73.288  -7.300  -53.247 1.00 11.77 ? 375  SER A N     1 
ATOM   2872  C CA    . SER A  1  375 ? 74.505  -7.072  -54.020 1.00 11.07 ? 375  SER A CA    1 
ATOM   2873  C C     . SER A  1  375 ? 75.409  -8.275  -53.797 1.00 11.10 ? 375  SER A C     1 
ATOM   2874  O O     . SER A  1  375 ? 75.619  -8.696  -52.663 1.00 11.08 ? 375  SER A O     1 
ATOM   2875  C CB    . SER A  1  375 ? 75.234  -5.812  -53.558 1.00 10.57 ? 375  SER A CB    1 
ATOM   2876  O OG    . SER A  1  375 ? 76.469  -5.684  -54.246 1.00 11.89 ? 375  SER A OG    1 
ATOM   2877  N N     . SER A  1  376 ? 75.949  -8.826  -54.876 1.00 12.85 ? 376  SER A N     1 
ATOM   2878  C CA    . SER A  1  376 ? 76.816  -9.991  -54.759 1.00 13.48 ? 376  SER A CA    1 
ATOM   2879  C C     . SER A  1  376 ? 78.248  -9.610  -54.406 1.00 12.75 ? 376  SER A C     1 
ATOM   2880  O O     . SER A  1  376 ? 79.093  -10.485 -54.213 1.00 12.84 ? 376  SER A O     1 
ATOM   2881  C CB    . SER A  1  376 ? 76.815  -10.778 -56.074 1.00 14.48 ? 376  SER A CB    1 
ATOM   2882  O OG    . SER A  1  376 ? 77.398  -10.014 -57.121 1.00 16.20 ? 376  SER A OG    1 
ATOM   2883  N N     . SER A  1  377 ? 78.520  -8.311  -54.295 1.00 13.41 ? 377  SER A N     1 
ATOM   2884  C CA    . SER A  1  377 ? 79.880  -7.863  -54.010 1.00 13.72 ? 377  SER A CA    1 
ATOM   2885  C C     . SER A  1  377 ? 80.055  -6.731  -53.005 1.00 14.20 ? 377  SER A C     1 
ATOM   2886  O O     . SER A  1  377 ? 81.138  -6.571  -52.446 1.00 16.33 ? 377  SER A O     1 
ATOM   2887  C CB    . SER A  1  377 ? 80.550  -7.435  -55.316 1.00 14.48 ? 377  SER A CB    1 
ATOM   2888  O OG    . SER A  1  377 ? 79.900  -6.293  -55.856 1.00 15.40 ? 377  SER A OG    1 
ATOM   2889  N N     . ASN A  1  378 ? 79.009  -5.943  -52.780 1.00 12.48 ? 378  ASN A N     1 
ATOM   2890  C CA    . ASN A  1  378 ? 79.107  -4.802  -51.871 1.00 11.72 ? 378  ASN A CA    1 
ATOM   2891  C C     . ASN A  1  378 ? 78.430  -5.046  -50.528 1.00 11.13 ? 378  ASN A C     1 
ATOM   2892  O O     . ASN A  1  378 ? 77.204  -5.101  -50.447 1.00 10.39 ? 378  ASN A O     1 
ATOM   2893  C CB    . ASN A  1  378 ? 78.483  -3.575  -52.534 1.00 12.49 ? 378  ASN A CB    1 
ATOM   2894  C CG    . ASN A  1  378 ? 78.869  -2.280  -51.850 1.00 14.77 ? 378  ASN A CG    1 
ATOM   2895  O OD1   . ASN A  1  378 ? 79.214  -2.263  -50.669 1.00 14.24 ? 378  ASN A OD1   1 
ATOM   2896  N ND2   . ASN A  1  378 ? 78.800  -1.180  -52.592 1.00 15.76 ? 378  ASN A ND2   1 
ATOM   2897  N N     . VAL A  1  379 ? 79.235  -5.166  -49.475 1.00 9.79  ? 379  VAL A N     1 
ATOM   2898  C CA    . VAL A  1  379 ? 78.717  -5.411  -48.133 1.00 8.27  ? 379  VAL A CA    1 
ATOM   2899  C C     . VAL A  1  379 ? 77.968  -4.203  -47.558 1.00 9.20  ? 379  VAL A C     1 
ATOM   2900  O O     . VAL A  1  379 ? 77.254  -4.329  -46.561 1.00 8.11  ? 379  VAL A O     1 
ATOM   2901  C CB    . VAL A  1  379 ? 79.865  -5.817  -47.162 1.00 8.50  ? 379  VAL A CB    1 
ATOM   2902  C CG1   . VAL A  1  379 ? 80.725  -4.605  -46.820 1.00 8.35  ? 379  VAL A CG1   1 
ATOM   2903  C CG2   . VAL A  1  379 ? 79.288  -6.457  -45.907 1.00 7.67  ? 379  VAL A CG2   1 
ATOM   2904  N N     . ARG A  1  380 ? 78.125  -3.036  -48.182 1.00 10.69 ? 380  ARG A N     1 
ATOM   2905  C CA    . ARG A  1  380 ? 77.438  -1.838  -47.705 1.00 11.96 ? 380  ARG A CA    1 
ATOM   2906  C C     . ARG A  1  380 ? 76.004  -1.762  -48.231 1.00 10.94 ? 380  ARG A C     1 
ATOM   2907  O O     . ARG A  1  380 ? 75.245  -0.857  -47.869 1.00 11.05 ? 380  ARG A O     1 
ATOM   2908  C CB    . ARG A  1  380 ? 78.197  -0.575  -48.115 1.00 14.68 ? 380  ARG A CB    1 
ATOM   2909  C CG    . ARG A  1  380 ? 79.578  -0.428  -47.499 1.00 20.05 ? 380  ARG A CG    1 
ATOM   2910  C CD    . ARG A  1  380 ? 80.245  0.829   -48.040 1.00 25.12 ? 380  ARG A CD    1 
ATOM   2911  N NE    . ARG A  1  380 ? 81.664  0.910   -47.706 1.00 29.29 ? 380  ARG A NE    1 
ATOM   2912  C CZ    . ARG A  1  380 ? 82.144  1.381   -46.559 1.00 31.74 ? 380  ARG A CZ    1 
ATOM   2913  N NH1   . ARG A  1  380 ? 81.318  1.825   -45.618 1.00 32.31 ? 380  ARG A NH1   1 
ATOM   2914  N NH2   . ARG A  1  380 ? 83.454  1.407   -46.357 1.00 32.39 ? 380  ARG A NH2   1 
ATOM   2915  N N     . VAL A  1  381 ? 75.637  -2.704  -49.095 1.00 10.37 ? 381  VAL A N     1 
ATOM   2916  C CA    . VAL A  1  381 ? 74.285  -2.743  -49.638 1.00 10.86 ? 381  VAL A CA    1 
ATOM   2917  C C     . VAL A  1  381 ? 73.462  -3.697  -48.774 1.00 11.14 ? 381  VAL A C     1 
ATOM   2918  O O     . VAL A  1  381 ? 73.766  -4.883  -48.685 1.00 12.01 ? 381  VAL A O     1 
ATOM   2919  C CB    . VAL A  1  381 ? 74.275  -3.239  -51.097 1.00 10.08 ? 381  VAL A CB    1 
ATOM   2920  C CG1   . VAL A  1  381 ? 72.846  -3.423  -51.570 1.00 11.96 ? 381  VAL A CG1   1 
ATOM   2921  C CG2   . VAL A  1  381 ? 74.987  -2.240  -51.994 1.00 12.31 ? 381  VAL A CG2   1 
ATOM   2922  N N     . SER A  1  382 ? 72.421  -3.171  -48.139 1.00 11.29 ? 382  SER A N     1 
ATOM   2923  C CA    . SER A  1  382 ? 71.576  -3.974  -47.261 1.00 11.86 ? 382  SER A CA    1 
ATOM   2924  C C     . SER A  1  382 ? 71.030  -5.231  -47.928 1.00 11.17 ? 382  SER A C     1 
ATOM   2925  O O     . SER A  1  382 ? 70.591  -5.200  -49.079 1.00 11.16 ? 382  SER A O     1 
ATOM   2926  C CB    . SER A  1  382 ? 70.407  -3.133  -46.744 1.00 14.58 ? 382  SER A CB    1 
ATOM   2927  O OG    A SER A  1  382 ? 70.871  -1.986  -46.058 0.50 16.50 ? 382  SER A OG    1 
ATOM   2928  O OG    B SER A  1  382 ? 69.596  -3.860  -45.835 0.50 16.59 ? 382  SER A OG    1 
ATOM   2929  N N     . PRO A  1  383 ? 71.067  -6.363  -47.209 1.00 11.23 ? 383  PRO A N     1 
ATOM   2930  C CA    . PRO A  1  383 ? 70.565  -7.636  -47.733 1.00 11.01 ? 383  PRO A CA    1 
ATOM   2931  C C     . PRO A  1  383 ? 69.041  -7.618  -47.787 1.00 11.58 ? 383  PRO A C     1 
ATOM   2932  O O     . PRO A  1  383 ? 68.398  -6.790  -47.136 1.00 12.10 ? 383  PRO A O     1 
ATOM   2933  C CB    . PRO A  1  383 ? 71.054  -8.656  -46.705 1.00 11.66 ? 383  PRO A CB    1 
ATOM   2934  C CG    . PRO A  1  383 ? 72.257  -8.010  -46.099 1.00 14.26 ? 383  PRO A CG    1 
ATOM   2935  C CD    . PRO A  1  383 ? 71.820  -6.575  -45.960 1.00 11.73 ? 383  PRO A CD    1 
ATOM   2936  N N     . ASN A  1  384 ? 68.470  -8.532  -48.564 1.00 10.12 ? 384  ASN A N     1 
ATOM   2937  C CA    . ASN A  1  384 ? 67.024  -8.650  -48.651 1.00 12.14 ? 384  ASN A CA    1 
ATOM   2938  C C     . ASN A  1  384 ? 66.621  -9.591  -47.521 1.00 10.88 ? 384  ASN A C     1 
ATOM   2939  O O     . ASN A  1  384 ? 67.286  -10.601 -47.284 1.00 11.87 ? 384  ASN A O     1 
ATOM   2940  C CB    . ASN A  1  384 ? 66.617  -9.268  -49.989 1.00 13.54 ? 384  ASN A CB    1 
ATOM   2941  C CG    . ASN A  1  384 ? 65.113  -9.415  -50.131 0.50 14.42 ? 384  ASN A CG    1 
ATOM   2942  O OD1   . ASN A  1  384 ? 64.393  -8.432  -50.306 0.50 15.89 ? 384  ASN A OD1   1 
ATOM   2943  N ND2   . ASN A  1  384 ? 64.630  -10.650 -50.047 0.50 15.41 ? 384  ASN A ND2   1 
ATOM   2944  N N     . VAL A  1  385 ? 65.551  -9.263  -46.809 1.00 9.17  ? 385  VAL A N     1 
ATOM   2945  C CA    . VAL A  1  385 ? 65.091  -10.129 -45.732 1.00 7.98  ? 385  VAL A CA    1 
ATOM   2946  C C     . VAL A  1  385 ? 63.575  -10.214 -45.711 1.00 7.93  ? 385  VAL A C     1 
ATOM   2947  O O     . VAL A  1  385 ? 62.890  -9.215  -45.919 1.00 9.09  ? 385  VAL A O     1 
ATOM   2948  C CB    . VAL A  1  385 ? 65.573  -9.638  -44.336 1.00 8.78  ? 385  VAL A CB    1 
ATOM   2949  C CG1   A VAL A  1  385 ? 67.084  -9.718  -44.248 0.50 5.77  ? 385  VAL A CG1   1 
ATOM   2950  C CG1   B VAL A  1  385 ? 65.018  -8.309  -43.992 0.50 5.95  ? 385  VAL A CG1   1 
ATOM   2951  C CG2   A VAL A  1  385 ? 65.103  -8.214  -44.083 0.50 4.80  ? 385  VAL A CG2   1 
ATOM   2952  C CG2   B VAL A  1  385 ? 65.355  -10.690 -43.291 0.50 4.78  ? 385  VAL A CG2   1 
ATOM   2953  N N     . LYS A  1  386 ? 63.059  -11.418 -45.485 1.00 7.42  ? 386  LYS A N     1 
ATOM   2954  C CA    . LYS A  1  386 ? 61.617  -11.624 -45.393 1.00 9.18  ? 386  LYS A CA    1 
ATOM   2955  C C     . LYS A  1  386 ? 61.353  -12.409 -44.116 1.00 9.83  ? 386  LYS A C     1 
ATOM   2956  O O     . LYS A  1  386 ? 62.066  -13.364 -43.817 1.00 9.81  ? 386  LYS A O     1 
ATOM   2957  C CB    . LYS A  1  386 ? 61.081  -12.389 -46.606 1.00 10.09 ? 386  LYS A CB    1 
ATOM   2958  C CG    . LYS A  1  386 ? 59.560  -12.462 -46.608 1.00 11.46 ? 386  LYS A CG    1 
ATOM   2959  C CD    . LYS A  1  386 ? 58.989  -12.853 -47.958 1.00 13.05 ? 386  LYS A CD    1 
ATOM   2960  C CE    . LYS A  1  386 ? 57.475  -12.697 -47.958 1.00 13.21 ? 386  LYS A CE    1 
ATOM   2961  N NZ    . LYS A  1  386 ? 56.868  -13.062 -49.271 1.00 14.95 ? 386  LYS A NZ    1 
ATOM   2962  N N     . PHE A  1  387 ? 60.335  -12.007 -43.360 1.00 7.84  ? 387  PHE A N     1 
ATOM   2963  C CA    . PHE A  1  387 ? 60.030  -12.676 -42.102 1.00 7.90  ? 387  PHE A CA    1 
ATOM   2964  C C     . PHE A  1  387 ? 58.767  -13.534 -42.097 1.00 7.70  ? 387  PHE A C     1 
ATOM   2965  O O     . PHE A  1  387 ? 58.578  -14.355 -41.200 1.00 8.82  ? 387  PHE A O     1 
ATOM   2966  C CB    . PHE A  1  387 ? 59.962  -11.634 -40.982 1.00 7.24  ? 387  PHE A CB    1 
ATOM   2967  C CG    . PHE A  1  387 ? 61.259  -10.906 -40.758 1.00 7.94  ? 387  PHE A CG    1 
ATOM   2968  C CD1   . PHE A  1  387 ? 61.343  -9.529  -40.937 1.00 7.07  ? 387  PHE A CD1   1 
ATOM   2969  C CD2   . PHE A  1  387 ? 62.395  -11.598 -40.345 1.00 6.73  ? 387  PHE A CD2   1 
ATOM   2970  C CE1   . PHE A  1  387 ? 62.543  -8.849  -40.702 1.00 6.59  ? 387  PHE A CE1   1 
ATOM   2971  C CE2   . PHE A  1  387 ? 63.594  -10.933 -40.109 1.00 6.98  ? 387  PHE A CE2   1 
ATOM   2972  C CZ    . PHE A  1  387 ? 63.671  -9.555  -40.285 1.00 7.49  ? 387  PHE A CZ    1 
ATOM   2973  N N     . ASN A  1  388 ? 57.911  -13.341 -43.097 1.00 7.07  ? 388  ASN A N     1 
ATOM   2974  C CA    . ASN A  1  388 ? 56.665  -14.095 -43.229 1.00 6.18  ? 388  ASN A CA    1 
ATOM   2975  C C     . ASN A  1  388 ? 55.784  -14.042 -41.989 1.00 5.67  ? 388  ASN A C     1 
ATOM   2976  O O     . ASN A  1  388 ? 55.350  -15.071 -41.471 1.00 7.57  ? 388  ASN A O     1 
ATOM   2977  C CB    . ASN A  1  388 ? 56.972  -15.550 -43.599 1.00 6.27  ? 388  ASN A CB    1 
ATOM   2978  C CG    . ASN A  1  388 ? 57.643  -15.668 -44.954 1.00 8.73  ? 388  ASN A CG    1 
ATOM   2979  O OD1   . ASN A  1  388 ? 57.151  -15.133 -45.945 1.00 10.38 ? 388  ASN A OD1   1 
ATOM   2980  N ND2   . ASN A  1  388 ? 58.772  -16.364 -45.003 1.00 9.99  ? 388  ASN A ND2   1 
ATOM   2981  N N     . TYR A  1  389 ? 55.515  -12.827 -41.526 1.00 6.54  ? 389  TYR A N     1 
ATOM   2982  C CA    . TYR A  1  389 ? 54.689  -12.629 -40.348 1.00 6.42  ? 389  TYR A CA    1 
ATOM   2983  C C     . TYR A  1  389 ? 53.388  -13.407 -40.457 1.00 7.47  ? 389  TYR A C     1 
ATOM   2984  O O     . TYR A  1  389 ? 52.735  -13.411 -41.507 1.00 8.07  ? 389  TYR A O     1 
ATOM   2985  C CB    . TYR A  1  389 ? 54.359  -11.144 -40.154 1.00 6.54  ? 389  TYR A CB    1 
ATOM   2986  C CG    . TYR A  1  389 ? 55.561  -10.241 -40.003 1.00 6.47  ? 389  TYR A CG    1 
ATOM   2987  C CD1   . TYR A  1  389 ? 56.076  -9.544  -41.094 1.00 7.53  ? 389  TYR A CD1   1 
ATOM   2988  C CD2   . TYR A  1  389 ? 56.187  -10.085 -38.765 1.00 5.53  ? 389  TYR A CD2   1 
ATOM   2989  C CE1   . TYR A  1  389 ? 57.187  -8.709  -40.962 1.00 6.55  ? 389  TYR A CE1   1 
ATOM   2990  C CE2   . TYR A  1  389 ? 57.301  -9.253  -38.618 1.00 8.22  ? 389  TYR A CE2   1 
ATOM   2991  C CZ    . TYR A  1  389 ? 57.793  -8.568  -39.724 1.00 6.81  ? 389  TYR A CZ    1 
ATOM   2992  O OH    . TYR A  1  389 ? 58.884  -7.735  -39.592 1.00 6.86  ? 389  TYR A OH    1 
ATOM   2993  N N     . TYR A  1  390 ? 53.033  -14.073 -39.364 1.00 7.40  ? 390  TYR A N     1 
ATOM   2994  C CA    . TYR A  1  390 ? 51.802  -14.840 -39.267 1.00 7.20  ? 390  TYR A CA    1 
ATOM   2995  C C     . TYR A  1  390 ? 51.613  -15.978 -40.271 1.00 9.66  ? 390  TYR A C     1 
ATOM   2996  O O     . TYR A  1  390 ? 50.492  -16.448 -40.477 1.00 10.86 ? 390  TYR A O     1 
ATOM   2997  C CB    . TYR A  1  390 ? 50.611  -13.867 -39.293 1.00 8.35  ? 390  TYR A CB    1 
ATOM   2998  C CG    . TYR A  1  390 ? 50.642  -12.920 -38.107 1.00 8.30  ? 390  TYR A CG    1 
ATOM   2999  C CD1   . TYR A  1  390 ? 50.488  -11.538 -38.269 1.00 11.13 ? 390  TYR A CD1   1 
ATOM   3000  C CD2   . TYR A  1  390 ? 50.886  -13.406 -36.825 1.00 9.55  ? 390  TYR A CD2   1 
ATOM   3001  C CE1   . TYR A  1  390 ? 50.588  -10.668 -37.170 1.00 11.86 ? 390  TYR A CE1   1 
ATOM   3002  C CE2   . TYR A  1  390 ? 50.986  -12.553 -35.732 1.00 10.85 ? 390  TYR A CE2   1 
ATOM   3003  C CZ    . TYR A  1  390 ? 50.841  -11.193 -35.905 1.00 12.58 ? 390  TYR A CZ    1 
ATOM   3004  O OH    . TYR A  1  390 ? 50.980  -10.375 -34.800 1.00 12.51 ? 390  TYR A OH    1 
ATOM   3005  N N     . SER A  1  391 ? 52.702  -16.435 -40.885 1.00 9.23  ? 391  SER A N     1 
ATOM   3006  C CA    . SER A  1  391 ? 52.603  -17.552 -41.824 1.00 10.39 ? 391  SER A CA    1 
ATOM   3007  C C     . SER A  1  391 ? 52.257  -18.797 -41.002 1.00 11.87 ? 391  SER A C     1 
ATOM   3008  O O     . SER A  1  391 ? 51.613  -19.729 -41.493 1.00 12.62 ? 391  SER A O     1 
ATOM   3009  C CB    . SER A  1  391 ? 53.920  -17.744 -42.589 1.00 11.89 ? 391  SER A CB    1 
ATOM   3010  O OG    . SER A  1  391 ? 55.021  -17.915 -41.715 1.00 12.49 ? 391  SER A OG    1 
ATOM   3011  N N     . ASN A  1  392 ? 52.695  -18.805 -39.746 1.00 9.89  ? 392  ASN A N     1 
ATOM   3012  C CA    . ASN A  1  392 ? 52.379  -19.897 -38.834 1.00 10.96 ? 392  ASN A CA    1 
ATOM   3013  C C     . ASN A  1  392 ? 51.178  -19.392 -38.039 1.00 11.64 ? 392  ASN A C     1 
ATOM   3014  O O     . ASN A  1  392 ? 51.278  -18.411 -37.302 1.00 10.73 ? 392  ASN A O     1 
ATOM   3015  C CB    . ASN A  1  392 ? 53.546  -20.187 -37.893 1.00 11.98 ? 392  ASN A CB    1 
ATOM   3016  C CG    . ASN A  1  392 ? 53.327  -21.447 -37.076 1.00 14.45 ? 392  ASN A CG    1 
ATOM   3017  O OD1   . ASN A  1  392 ? 52.437  -21.497 -36.228 1.00 11.76 ? 392  ASN A OD1   1 
ATOM   3018  N ND2   . ASN A  1  392 ? 54.136  -22.469 -37.346 1.00 17.52 ? 392  ASN A ND2   1 
ATOM   3019  N N     . LEU A  1  393 ? 50.041  -20.059 -38.194 1.00 10.32 ? 393  LEU A N     1 
ATOM   3020  C CA    . LEU A  1  393 ? 48.817  -19.631 -37.527 1.00 9.96  ? 393  LEU A CA    1 
ATOM   3021  C C     . LEU A  1  393 ? 48.857  -19.585 -36.005 1.00 9.33  ? 393  LEU A C     1 
ATOM   3022  O O     . LEU A  1  393 ? 48.042  -18.896 -35.389 1.00 10.35 ? 393  LEU A O     1 
ATOM   3023  C CB    . LEU A  1  393 ? 47.644  -20.495 -37.996 1.00 11.02 ? 393  LEU A CB    1 
ATOM   3024  C CG    . LEU A  1  393 ? 47.347  -20.372 -39.494 1.00 13.38 ? 393  LEU A CG    1 
ATOM   3025  C CD1   . LEU A  1  393 ? 46.217  -21.317 -39.869 1.00 14.65 ? 393  LEU A CD1   1 
ATOM   3026  C CD2   . LEU A  1  393 ? 46.981  -18.934 -39.834 1.00 13.88 ? 393  LEU A CD2   1 
ATOM   3027  N N     . THR A  1  394 ? 49.782  -20.312 -35.387 1.00 8.80  ? 394  THR A N     1 
ATOM   3028  C CA    . THR A  1  394 ? 49.869  -20.279 -33.934 1.00 9.56  ? 394  THR A CA    1 
ATOM   3029  C C     . THR A  1  394 ? 50.315  -18.878 -33.506 1.00 9.10  ? 394  THR A C     1 
ATOM   3030  O O     . THR A  1  394 ? 49.885  -18.377 -32.465 1.00 8.63  ? 394  THR A O     1 
ATOM   3031  C CB    . THR A  1  394 ? 50.845  -21.345 -33.398 1.00 11.64 ? 394  THR A CB    1 
ATOM   3032  O OG1   . THR A  1  394 ? 50.352  -22.650 -33.731 1.00 14.18 ? 394  THR A OG1   1 
ATOM   3033  C CG2   . THR A  1  394 ? 50.961  -21.245 -31.885 1.00 13.33 ? 394  THR A CG2   1 
ATOM   3034  N N     . ASP A  1  395 ? 51.161  -18.239 -34.314 1.00 8.41  ? 395  ASP A N     1 
ATOM   3035  C CA    . ASP A  1  395 ? 51.608  -16.881 -34.000 1.00 8.21  ? 395  ASP A CA    1 
ATOM   3036  C C     . ASP A  1  395 ? 50.391  -15.959 -34.018 1.00 7.18  ? 395  ASP A C     1 
ATOM   3037  O O     . ASP A  1  395 ? 50.253  -15.071 -33.177 1.00 9.01  ? 395  ASP A O     1 
ATOM   3038  C CB    . ASP A  1  395 ? 52.608  -16.348 -35.036 1.00 8.23  ? 395  ASP A CB    1 
ATOM   3039  C CG    . ASP A  1  395 ? 54.001  -16.945 -34.899 1.00 6.20  ? 395  ASP A CG    1 
ATOM   3040  O OD1   . ASP A  1  395 ? 54.328  -17.523 -33.837 1.00 8.16  ? 395  ASP A OD1   1 
ATOM   3041  O OD2   . ASP A  1  395 ? 54.782  -16.809 -35.867 1.00 7.46  ? 395  ASP A OD2   1 
ATOM   3042  N N     . LEU A  1  396 ? 49.518  -16.165 -34.999 1.00 7.13  ? 396  LEU A N     1 
ATOM   3043  C CA    . LEU A  1  396 ? 48.323  -15.343 -35.136 1.00 7.20  ? 396  LEU A CA    1 
ATOM   3044  C C     . LEU A  1  396 ? 47.389  -15.520 -33.943 1.00 8.86  ? 396  LEU A C     1 
ATOM   3045  O O     . LEU A  1  396 ? 46.821  -14.550 -33.449 1.00 8.12  ? 396  LEU A O     1 
ATOM   3046  C CB    . LEU A  1  396 ? 47.592  -15.694 -36.437 1.00 6.82  ? 396  LEU A CB    1 
ATOM   3047  C CG    . LEU A  1  396 ? 46.373  -14.838 -36.792 1.00 9.34  ? 396  LEU A CG    1 
ATOM   3048  C CD1   . LEU A  1  396 ? 46.773  -13.371 -36.892 1.00 10.29 ? 396  LEU A CD1   1 
ATOM   3049  C CD2   . LEU A  1  396 ? 45.786  -15.320 -38.111 1.00 10.87 ? 396  LEU A CD2   1 
ATOM   3050  N N     . SER A  1  397 ? 47.233  -16.758 -33.480 1.00 8.03  ? 397  SER A N     1 
ATOM   3051  C CA    . SER A  1  397 ? 46.367  -17.021 -32.337 1.00 9.10  ? 397  SER A CA    1 
ATOM   3052  C C     . SER A  1  397 ? 46.917  -16.283 -31.120 1.00 8.34  ? 397  SER A C     1 
ATOM   3053  O O     . SER A  1  397 ? 46.161  -15.749 -30.309 1.00 8.39  ? 397  SER A O     1 
ATOM   3054  C CB    . SER A  1  397 ? 46.293  -18.526 -32.051 1.00 11.31 ? 397  SER A CB    1 
ATOM   3055  O OG    . SER A  1  397 ? 47.554  -19.038 -31.656 0.50 13.21 ? 397  SER A OG    1 
ATOM   3056  N N     . HIS A  1  398 ? 48.239  -16.247 -31.003 1.00 8.47  ? 398  HIS A N     1 
ATOM   3057  C CA    . HIS A  1  398 ? 48.873  -15.558 -29.886 1.00 8.26  ? 398  HIS A CA    1 
ATOM   3058  C C     . HIS A  1  398 ? 48.698  -14.045 -30.005 1.00 9.34  ? 398  HIS A C     1 
ATOM   3059  O O     . HIS A  1  398 ? 48.552  -13.360 -28.991 1.00 10.10 ? 398  HIS A O     1 
ATOM   3060  C CB    . HIS A  1  398 ? 50.352  -15.950 -29.799 1.00 7.70  ? 398  HIS A CB    1 
ATOM   3061  C CG    . HIS A  1  398 ? 50.560  -17.384 -29.419 1.00 8.51  ? 398  HIS A CG    1 
ATOM   3062  N ND1   . HIS A  1  398 ? 51.766  -18.037 -29.580 1.00 10.56 ? 398  HIS A ND1   1 
ATOM   3063  C CD2   . HIS A  1  398 ? 49.714  -18.295 -28.881 1.00 10.89 ? 398  HIS A CD2   1 
ATOM   3064  C CE1   . HIS A  1  398 ? 51.650  -19.283 -29.161 1.00 9.87  ? 398  HIS A CE1   1 
ATOM   3065  N NE2   . HIS A  1  398 ? 50.413  -19.467 -28.731 1.00 10.87 ? 398  HIS A NE2   1 
ATOM   3066  N N     . CYS A  1  399 ? 48.693  -13.522 -31.231 1.00 8.96  ? 399  CYS A N     1 
ATOM   3067  C CA    . CYS A  1  399 ? 48.490  -12.082 -31.423 1.00 7.93  ? 399  CYS A CA    1 
ATOM   3068  C C     . CYS A  1  399 ? 47.087  -11.727 -30.964 1.00 7.69  ? 399  CYS A C     1 
ATOM   3069  O O     . CYS A  1  399 ? 46.873  -10.730 -30.273 1.00 7.28  ? 399  CYS A O     1 
ATOM   3070  C CB    . CYS A  1  399 ? 48.621  -11.671 -32.897 1.00 9.26  ? 399  CYS A CB    1 
ATOM   3071  S SG    . CYS A  1  399 ? 48.222  -9.902  -33.146 1.00 14.08 ? 399  CYS A SG    1 
ATOM   3072  N N     . VAL A  1  400 ? 46.121  -12.547 -31.362 1.00 7.90  ? 400  VAL A N     1 
ATOM   3073  C CA    . VAL A  1  400 ? 44.741  -12.306 -30.985 1.00 7.04  ? 400  VAL A CA    1 
ATOM   3074  C C     . VAL A  1  400 ? 44.604  -12.256 -29.468 1.00 7.87  ? 400  VAL A C     1 
ATOM   3075  O O     . VAL A  1  400 ? 44.020  -11.318 -28.928 1.00 7.22  ? 400  VAL A O     1 
ATOM   3076  C CB    . VAL A  1  400 ? 43.809  -13.390 -31.565 1.00 6.79  ? 400  VAL A CB    1 
ATOM   3077  C CG1   . VAL A  1  400 ? 42.402  -13.222 -31.009 1.00 6.94  ? 400  VAL A CG1   1 
ATOM   3078  C CG2   . VAL A  1  400 ? 43.784  -13.278 -33.089 1.00 7.17  ? 400  VAL A CG2   1 
ATOM   3079  N N     . SER A  1  401 ? 45.157  -13.252 -28.779 1.00 7.25  ? 401  SER A N     1 
ATOM   3080  C CA    . SER A  1  401 ? 45.092  -13.286 -27.321 1.00 6.73  ? 401  SER A CA    1 
ATOM   3081  C C     . SER A  1  401 ? 45.767  -12.046 -26.745 1.00 6.97  ? 401  SER A C     1 
ATOM   3082  O O     . SER A  1  401 ? 45.261  -11.424 -25.806 1.00 7.35  ? 401  SER A O     1 
ATOM   3083  C CB    . SER A  1  401 ? 45.779  -14.544 -26.789 1.00 8.17  ? 401  SER A CB    1 
ATOM   3084  O OG    . SER A  1  401 ? 45.108  -15.707 -27.240 0.50 5.83  ? 401  SER A OG    1 
ATOM   3085  N N     . GLY A  1  402 ? 46.911  -11.690 -27.319 1.00 7.44  ? 402  GLY A N     1 
ATOM   3086  C CA    . GLY A  1  402 ? 47.637  -10.521 -26.862 1.00 6.06  ? 402  GLY A CA    1 
ATOM   3087  C C     . GLY A  1  402 ? 46.852  -9.232  -27.013 1.00 6.79  ? 402  GLY A C     1 
ATOM   3088  O O     . GLY A  1  402 ? 46.804  -8.423  -26.087 1.00 6.82  ? 402  GLY A O     1 
ATOM   3089  N N     . MET A  1  403 ? 46.230  -9.025  -28.170 1.00 6.90  ? 403  MET A N     1 
ATOM   3090  C CA    . MET A  1  403 ? 45.469  -7.798  -28.365 1.00 7.03  ? 403  MET A CA    1 
ATOM   3091  C C     . MET A  1  403 ? 44.197  -7.776  -27.520 1.00 8.24  ? 403  MET A C     1 
ATOM   3092  O O     . MET A  1  403 ? 43.704  -6.706  -27.169 1.00 7.98  ? 403  MET A O     1 
ATOM   3093  C CB    . MET A  1  403 ? 45.160  -7.576  -29.850 1.00 7.77  ? 403  MET A CB    1 
ATOM   3094  C CG    . MET A  1  403 ? 46.405  -7.248  -30.685 1.00 7.85  ? 403  MET A CG    1 
ATOM   3095  S SD    . MET A  1  403 ? 47.625  -6.164  -29.856 1.00 9.35  ? 403  MET A SD    1 
ATOM   3096  C CE    . MET A  1  403 ? 46.711  -4.606  -29.757 1.00 9.34  ? 403  MET A CE    1 
ATOM   3097  N N     . LYS A  1  404 ? 43.667  -8.950  -27.185 1.00 6.93  ? 404  LYS A N     1 
ATOM   3098  C CA    . LYS A  1  404 ? 42.492  -9.003  -26.323 1.00 7.63  ? 404  LYS A CA    1 
ATOM   3099  C C     . LYS A  1  404 ? 42.937  -8.537  -24.935 1.00 8.08  ? 404  LYS A C     1 
ATOM   3100  O O     . LYS A  1  404 ? 42.188  -7.866  -24.228 1.00 7.34  ? 404  LYS A O     1 
ATOM   3101  C CB    . LYS A  1  404 ? 41.935  -10.426 -26.244 1.00 6.94  ? 404  LYS A CB    1 
ATOM   3102  C CG    . LYS A  1  404 ? 41.057  -10.810 -27.427 1.00 6.98  ? 404  LYS A CG    1 
ATOM   3103  C CD    . LYS A  1  404 ? 40.583  -12.247 -27.288 1.00 8.89  ? 404  LYS A CD    1 
ATOM   3104  C CE    . LYS A  1  404 ? 39.605  -12.624 -28.390 1.00 10.02 ? 404  LYS A CE    1 
ATOM   3105  N NZ    . LYS A  1  404 ? 39.203  -14.058 -28.276 1.00 11.01 ? 404  LYS A NZ    1 
ATOM   3106  N N     . LYS A  1  405 ? 44.162  -8.886  -24.547 1.00 7.58  ? 405  LYS A N     1 
ATOM   3107  C CA    . LYS A  1  405 ? 44.663  -8.467  -23.243 1.00 7.30  ? 405  LYS A CA    1 
ATOM   3108  C C     . LYS A  1  405 ? 44.835  -6.949  -23.248 1.00 7.17  ? 405  LYS A C     1 
ATOM   3109  O O     . LYS A  1  405 ? 44.566  -6.292  -22.245 1.00 7.39  ? 405  LYS A O     1 
ATOM   3110  C CB    . LYS A  1  405 ? 45.986  -9.172  -22.908 1.00 6.91  ? 405  LYS A CB    1 
ATOM   3111  C CG    . LYS A  1  405 ? 46.551  -8.825  -21.520 1.00 6.66  ? 405  LYS A CG    1 
ATOM   3112  C CD    . LYS A  1  405 ? 45.574  -9.141  -20.375 1.00 6.75  ? 405  LYS A CD    1 
ATOM   3113  C CE    . LYS A  1  405 ? 45.393  -10.644 -20.163 1.00 6.91  ? 405  LYS A CE    1 
ATOM   3114  N NZ    . LYS A  1  405 ? 44.442  -10.956 -19.043 1.00 8.39  ? 405  LYS A NZ    1 
ATOM   3115  N N     . ILE A  1  406 ? 45.282  -6.391  -24.373 1.00 6.72  ? 406  ILE A N     1 
ATOM   3116  C CA    . ILE A  1  406 ? 45.424  -4.938  -24.474 1.00 6.74  ? 406  ILE A CA    1 
ATOM   3117  C C     . ILE A  1  406 ? 44.022  -4.339  -24.313 1.00 7.58  ? 406  ILE A C     1 
ATOM   3118  O O     . ILE A  1  406 ? 43.845  -3.306  -23.667 1.00 7.29  ? 406  ILE A O     1 
ATOM   3119  C CB    . ILE A  1  406 ? 46.018  -4.507  -25.844 1.00 8.03  ? 406  ILE A CB    1 
ATOM   3120  C CG1   . ILE A  1  406 ? 47.471  -4.973  -25.956 1.00 9.48  ? 406  ILE A CG1   1 
ATOM   3121  C CG2   . ILE A  1  406 ? 45.949  -2.989  -25.995 1.00 8.47  ? 406  ILE A CG2   1 
ATOM   3122  C CD1   . ILE A  1  406 ? 48.381  -4.457  -24.843 1.00 10.48 ? 406  ILE A CD1   1 
ATOM   3123  N N     . GLY A  1  407 ? 43.026  -4.999  -24.900 1.00 8.32  ? 407  GLY A N     1 
ATOM   3124  C CA    . GLY A  1  407 ? 41.656  -4.527  -24.771 1.00 7.77  ? 407  GLY A CA    1 
ATOM   3125  C C     . GLY A  1  407 ? 41.250  -4.484  -23.307 1.00 9.34  ? 407  GLY A C     1 
ATOM   3126  O O     . GLY A  1  407 ? 40.534  -3.576  -22.877 1.00 9.19  ? 407  GLY A O     1 
ATOM   3127  N N     . GLU A  1  408 ? 41.702  -5.469  -22.536 1.00 8.45  ? 408  GLU A N     1 
ATOM   3128  C CA    . GLU A  1  408 ? 41.397  -5.505  -21.110 1.00 9.08  ? 408  GLU A CA    1 
ATOM   3129  C C     . GLU A  1  408 ? 42.022  -4.298  -20.425 1.00 9.59  ? 408  GLU A C     1 
ATOM   3130  O O     . GLU A  1  408 ? 41.384  -3.652  -19.590 1.00 8.97  ? 408  GLU A O     1 
ATOM   3131  C CB    . GLU A  1  408 ? 41.935  -6.784  -20.467 1.00 8.71  ? 408  GLU A CB    1 
ATOM   3132  C CG    . GLU A  1  408 ? 41.095  -8.018  -20.736 1.00 11.62 ? 408  GLU A CG    1 
ATOM   3133  C CD    . GLU A  1  408 ? 41.504  -9.182  -19.852 1.00 12.48 ? 408  GLU A CD    1 
ATOM   3134  O OE1   . GLU A  1  408 ? 42.156  -10.120 -20.353 1.00 13.67 ? 408  GLU A OE1   1 
ATOM   3135  O OE2   . GLU A  1  408 ? 41.178  -9.148  -18.646 1.00 16.07 ? 408  GLU A OE2   1 
ATOM   3136  N N     . LEU A  1  409 ? 43.273  -4.002  -20.775 1.00 9.06  ? 409  LEU A N     1 
ATOM   3137  C CA    . LEU A  1  409 ? 43.968  -2.857  -20.198 1.00 8.11  ? 409  LEU A CA    1 
ATOM   3138  C C     . LEU A  1  409 ? 43.177  -1.586  -20.477 1.00 8.51  ? 409  LEU A C     1 
ATOM   3139  O O     . LEU A  1  409 ? 43.002  -0.747  -19.597 1.00 8.34  ? 409  LEU A O     1 
ATOM   3140  C CB    . LEU A  1  409 ? 45.373  -2.717  -20.795 1.00 7.78  ? 409  LEU A CB    1 
ATOM   3141  C CG    A LEU A  1  409 ? 46.529  -3.520  -20.188 0.50 7.92  ? 409  LEU A CG    1 
ATOM   3142  C CG    B LEU A  1  409 ? 46.322  -3.904  -20.495 0.50 7.88  ? 409  LEU A CG    1 
ATOM   3143  C CD1   A LEU A  1  409 ? 46.195  -4.996  -20.125 0.50 9.36  ? 409  LEU A CD1   1 
ATOM   3144  C CD1   B LEU A  1  409 ? 47.689  -3.646  -21.110 0.50 9.30  ? 409  LEU A CD1   1 
ATOM   3145  C CD2   A LEU A  1  409 ? 47.775  -3.290  -21.032 0.50 6.90  ? 409  LEU A CD2   1 
ATOM   3146  C CD2   B LEU A  1  409 ? 46.448  -4.164  -19.002 0.50 6.88  ? 409  LEU A CD2   1 
ATOM   3147  N N     . LEU A  1  410 ? 42.691  -1.457  -21.707 1.00 8.37  ? 410  LEU A N     1 
ATOM   3148  C CA    . LEU A  1  410 ? 41.924  -0.282  -22.106 1.00 8.35  ? 410  LEU A CA    1 
ATOM   3149  C C     . LEU A  1  410 ? 40.582  -0.174  -21.392 1.00 8.49  ? 410  LEU A C     1 
ATOM   3150  O O     . LEU A  1  410 ? 39.985  0.900   -21.350 1.00 10.20 ? 410  LEU A O     1 
ATOM   3151  C CB    . LEU A  1  410 ? 41.693  -0.300  -23.618 1.00 8.62  ? 410  LEU A CB    1 
ATOM   3152  C CG    . LEU A  1  410 ? 42.966  -0.186  -24.459 1.00 8.98  ? 410  LEU A CG    1 
ATOM   3153  C CD1   . LEU A  1  410 ? 42.626  -0.304  -25.938 1.00 12.79 ? 410  LEU A CD1   1 
ATOM   3154  C CD2   . LEU A  1  410 ? 43.648  1.145   -24.168 1.00 10.70 ? 410  LEU A CD2   1 
ATOM   3155  N N     . SER A  1  411 ? 40.116  -1.283  -20.826 1.00 6.79  ? 411  SER A N     1 
ATOM   3156  C CA    . SER A  1  411 ? 38.833  -1.308  -20.126 1.00 7.63  ? 411  SER A CA    1 
ATOM   3157  C C     . SER A  1  411 ? 38.956  -1.205  -18.602 1.00 9.26  ? 411  SER A C     1 
ATOM   3158  O O     . SER A  1  411 ? 37.949  -1.249  -17.889 1.00 10.54 ? 411  SER A O     1 
ATOM   3159  C CB    . SER A  1  411 ? 38.083  -2.593  -20.485 1.00 8.16  ? 411  SER A CB    1 
ATOM   3160  O OG    . SER A  1  411 ? 38.018  -2.758  -21.892 1.00 10.34 ? 411  SER A OG    1 
ATOM   3161  N N     . THR A  1  412 ? 40.181  -1.053  -18.106 1.00 9.79  ? 412  THR A N     1 
ATOM   3162  C CA    . THR A  1  412 ? 40.430  -0.963  -16.666 1.00 8.65  ? 412  THR A CA    1 
ATOM   3163  C C     . THR A  1  412 ? 40.074  0.391   -16.056 1.00 9.07  ? 412  THR A C     1 
ATOM   3164  O O     . THR A  1  412 ? 40.000  1.400   -16.757 1.00 9.28  ? 412  THR A O     1 
ATOM   3165  C CB    . THR A  1  412 ? 41.921  -1.201  -16.337 1.00 8.16  ? 412  THR A CB    1 
ATOM   3166  O OG1   . THR A  1  412 ? 42.711  -0.199  -16.989 1.00 9.12  ? 412  THR A OG1   1 
ATOM   3167  C CG2   . THR A  1  412 ? 42.373  -2.580  -16.797 1.00 7.99  ? 412  THR A CG2   1 
ATOM   3168  N N     . ASP A  1  413 ? 39.863  0.406   -14.741 1.00 9.74  ? 413  ASP A N     1 
ATOM   3169  C CA    . ASP A  1  413 ? 39.576  1.656   -14.040 1.00 9.08  ? 413  ASP A CA    1 
ATOM   3170  C C     . ASP A  1  413 ? 40.811  2.538   -14.223 1.00 10.14 ? 413  ASP A C     1 
ATOM   3171  O O     . ASP A  1  413 ? 40.713  3.758   -14.379 1.00 9.46  ? 413  ASP A O     1 
ATOM   3172  C CB    . ASP A  1  413 ? 39.377  1.420   -12.535 1.00 10.06 ? 413  ASP A CB    1 
ATOM   3173  C CG    . ASP A  1  413 ? 38.101  0.671   -12.211 1.00 11.65 ? 413  ASP A CG    1 
ATOM   3174  O OD1   . ASP A  1  413 ? 37.293  0.414   -13.128 1.00 13.14 ? 413  ASP A OD1   1 
ATOM   3175  O OD2   . ASP A  1  413 ? 37.907  0.346   -11.016 1.00 14.90 ? 413  ASP A OD2   1 
ATOM   3176  N N     . ALA A  1  414 ? 41.978  1.900   -14.202 1.00 9.90  ? 414  ALA A N     1 
ATOM   3177  C CA    . ALA A  1  414 ? 43.256  2.593   -14.338 1.00 10.30 ? 414  ALA A CA    1 
ATOM   3178  C C     . ALA A  1  414 ? 43.379  3.458   -15.589 1.00 10.26 ? 414  ALA A C     1 
ATOM   3179  O O     . ALA A  1  414 ? 43.962  4.538   -15.541 1.00 10.96 ? 414  ALA A O     1 
ATOM   3180  C CB    . ALA A  1  414 ? 44.403  1.580   -14.295 1.00 11.30 ? 414  ALA A CB    1 
ATOM   3181  N N     . LEU A  1  415 ? 42.831  3.001   -16.708 1.00 9.24  ? 415  LEU A N     1 
ATOM   3182  C CA    . LEU A  1  415 ? 42.939  3.781   -17.933 1.00 9.78  ? 415  LEU A CA    1 
ATOM   3183  C C     . LEU A  1  415 ? 41.734  4.672   -18.246 1.00 10.13 ? 415  LEU A C     1 
ATOM   3184  O O     . LEU A  1  415 ? 41.757  5.411   -19.225 1.00 10.14 ? 415  LEU A O     1 
ATOM   3185  C CB    . LEU A  1  415 ? 43.251  2.860   -19.123 1.00 13.26 ? 415  LEU A CB    1 
ATOM   3186  C CG    . LEU A  1  415 ? 44.554  2.045   -19.012 1.00 14.28 ? 415  LEU A CG    1 
ATOM   3187  C CD1   . LEU A  1  415 ? 44.916  1.481   -20.377 1.00 17.21 ? 415  LEU A CD1   1 
ATOM   3188  C CD2   . LEU A  1  415 ? 45.692  2.911   -18.493 1.00 15.94 ? 415  LEU A CD2   1 
ATOM   3189  N N     . LYS A  1  416 ? 40.699  4.629   -17.409 1.00 9.93  ? 416  LYS A N     1 
ATOM   3190  C CA    . LYS A  1  416 ? 39.512  5.459   -17.633 1.00 12.35 ? 416  LYS A CA    1 
ATOM   3191  C C     . LYS A  1  416 ? 39.823  6.943   -17.777 1.00 12.01 ? 416  LYS A C     1 
ATOM   3192  O O     . LYS A  1  416 ? 39.285  7.612   -18.666 1.00 12.31 ? 416  LYS A O     1 
ATOM   3193  C CB    . LYS A  1  416 ? 38.504  5.306   -16.486 1.00 15.02 ? 416  LYS A CB    1 
ATOM   3194  C CG    . LYS A  1  416 ? 38.054  3.902   -16.201 1.00 20.16 ? 416  LYS A CG    1 
ATOM   3195  C CD    . LYS A  1  416 ? 37.174  3.895   -14.959 1.00 23.30 ? 416  LYS A CD    1 
ATOM   3196  C CE    . LYS A  1  416 ? 35.705  4.021   -15.312 1.00 25.90 ? 416  LYS A CE    1 
ATOM   3197  N NZ    . LYS A  1  416 ? 35.165  2.720   -15.815 1.00 28.95 ? 416  LYS A NZ    1 
ATOM   3198  N N     . PRO A  1  417 ? 40.675  7.488   -16.889 1.00 12.25 ? 417  PRO A N     1 
ATOM   3199  C CA    . PRO A  1  417 ? 41.019  8.913   -16.954 1.00 12.38 ? 417  PRO A CA    1 
ATOM   3200  C C     . PRO A  1  417 ? 41.655  9.364   -18.256 1.00 13.05 ? 417  PRO A C     1 
ATOM   3201  O O     . PRO A  1  417 ? 41.802  10.564  -18.496 1.00 13.28 ? 417  PRO A O     1 
ATOM   3202  C CB    . PRO A  1  417 ? 41.972  9.098   -15.771 1.00 13.35 ? 417  PRO A CB    1 
ATOM   3203  C CG    . PRO A  1  417 ? 41.538  8.052   -14.805 1.00 13.65 ? 417  PRO A CG    1 
ATOM   3204  C CD    . PRO A  1  417 ? 41.305  6.860   -15.713 1.00 12.41 ? 417  PRO A CD    1 
ATOM   3205  N N     . TYR A  1  418 ? 42.029  8.410   -19.099 1.00 11.49 ? 418  TYR A N     1 
ATOM   3206  C CA    . TYR A  1  418 ? 42.684  8.752   -20.349 1.00 11.46 ? 418  TYR A CA    1 
ATOM   3207  C C     . TYR A  1  418 ? 41.798  8.648   -21.586 1.00 12.41 ? 418  TYR A C     1 
ATOM   3208  O O     . TYR A  1  418 ? 42.267  8.789   -22.715 1.00 11.48 ? 418  TYR A O     1 
ATOM   3209  C CB    . TYR A  1  418 ? 43.965  7.923   -20.477 1.00 11.28 ? 418  TYR A CB    1 
ATOM   3210  C CG    . TYR A  1  418 ? 44.833  8.098   -19.249 1.00 10.80 ? 418  TYR A CG    1 
ATOM   3211  C CD1   . TYR A  1  418 ? 44.810  7.165   -18.212 1.00 9.82  ? 418  TYR A CD1   1 
ATOM   3212  C CD2   . TYR A  1  418 ? 45.588  9.257   -19.071 1.00 11.58 ? 418  TYR A CD2   1 
ATOM   3213  C CE1   . TYR A  1  418 ? 45.512  7.385   -17.027 1.00 11.04 ? 418  TYR A CE1   1 
ATOM   3214  C CE2   . TYR A  1  418 ? 46.290  9.489   -17.891 1.00 12.52 ? 418  TYR A CE2   1 
ATOM   3215  C CZ    . TYR A  1  418 ? 46.245  8.550   -16.872 1.00 12.24 ? 418  TYR A CZ    1 
ATOM   3216  O OH    . TYR A  1  418 ? 46.917  8.784   -15.692 1.00 15.10 ? 418  TYR A OH    1 
ATOM   3217  N N     . LYS A  1  419 ? 40.508  8.416   -21.362 1.00 12.29 ? 419  LYS A N     1 
ATOM   3218  C CA    . LYS A  1  419 ? 39.540  8.351   -22.449 1.00 14.01 ? 419  LYS A CA    1 
ATOM   3219  C C     . LYS A  1  419 ? 39.062  9.781   -22.682 1.00 15.37 ? 419  LYS A C     1 
ATOM   3220  O O     . LYS A  1  419 ? 39.127  10.615  -21.779 1.00 15.70 ? 419  LYS A O     1 
ATOM   3221  C CB    . LYS A  1  419 ? 38.331  7.496   -22.062 1.00 13.75 ? 419  LYS A CB    1 
ATOM   3222  C CG    . LYS A  1  419 ? 38.572  6.000   -22.015 1.00 13.27 ? 419  LYS A CG    1 
ATOM   3223  C CD    . LYS A  1  419 ? 37.253  5.264   -21.832 1.00 13.54 ? 419  LYS A CD    1 
ATOM   3224  C CE    . LYS A  1  419 ? 37.431  3.755   -21.920 1.00 13.89 ? 419  LYS A CE    1 
ATOM   3225  N NZ    . LYS A  1  419 ? 36.115  3.057   -21.923 1.00 16.10 ? 419  LYS A NZ    1 
ATOM   3226  N N     . VAL A  1  420 ? 38.588  10.068  -23.889 1.00 16.32 ? 420  VAL A N     1 
ATOM   3227  C CA    . VAL A  1  420 ? 38.077  11.400  -24.191 1.00 19.46 ? 420  VAL A CA    1 
ATOM   3228  C C     . VAL A  1  420 ? 36.580  11.415  -23.892 1.00 21.45 ? 420  VAL A C     1 
ATOM   3229  O O     . VAL A  1  420 ? 36.001  12.460  -23.594 1.00 21.61 ? 420  VAL A O     1 
ATOM   3230  C CB    . VAL A  1  420 ? 38.306  11.767  -25.674 1.00 20.28 ? 420  VAL A CB    1 
ATOM   3231  C CG1   . VAL A  1  420 ? 37.641  13.101  -25.990 1.00 21.78 ? 420  VAL A CG1   1 
ATOM   3232  C CG2   . VAL A  1  420 ? 39.796  11.847  -25.962 1.00 21.22 ? 420  VAL A CG2   1 
ATOM   3233  N N     . GLU A  1  421 ? 35.968  10.236  -23.967 1.00 23.51 ? 421  GLU A N     1 
ATOM   3234  C CA    . GLU A  1  421 ? 34.540  10.063  -23.714 1.00 26.90 ? 421  GLU A CA    1 
ATOM   3235  C C     . GLU A  1  421 ? 34.351  8.804   -22.874 1.00 27.44 ? 421  GLU A C     1 
ATOM   3236  O O     . GLU A  1  421 ? 35.030  7.803   -23.096 1.00 26.16 ? 421  GLU A O     1 
ATOM   3237  C CB    . GLU A  1  421 ? 33.791  9.889   -25.034 1.00 29.70 ? 421  GLU A CB    1 
ATOM   3238  C CG    . GLU A  1  421 ? 34.203  10.856  -26.127 1.00 34.93 ? 421  GLU A CG    1 
ATOM   3239  C CD    . GLU A  1  421 ? 33.563  10.520  -27.459 1.00 37.78 ? 421  GLU A CD    1 
ATOM   3240  O OE1   . GLU A  1  421 ? 32.316  10.462  -27.521 1.00 40.18 ? 421  GLU A OE1   1 
ATOM   3241  O OE2   . GLU A  1  421 ? 34.304  10.311  -28.444 1.00 40.35 ? 421  GLU A OE2   1 
ATOM   3242  N N     . ASP A  1  422 ? 33.427  8.842   -21.921 1.00 28.61 ? 422  ASP A N     1 
ATOM   3243  C CA    . ASP A  1  422 ? 33.185  7.678   -21.074 1.00 29.66 ? 422  ASP A CA    1 
ATOM   3244  C C     . ASP A  1  422 ? 32.247  6.680   -21.754 1.00 29.63 ? 422  ASP A C     1 
ATOM   3245  O O     . ASP A  1  422 ? 31.075  6.562   -21.393 1.00 30.98 ? 422  ASP A O     1 
ATOM   3246  C CB    . ASP A  1  422 ? 32.613  8.119   -19.720 1.00 30.89 ? 422  ASP A CB    1 
ATOM   3247  C CG    A ASP A  1  422 ? 31.264  8.799   -19.846 0.50 31.62 ? 422  ASP A CG    1 
ATOM   3248  C CG    B ASP A  1  422 ? 32.541  6.918   -18.765 0.50 32.31 ? 422  ASP A CG    1 
ATOM   3249  O OD1   A ASP A  1  422 ? 31.079  9.587   -20.797 0.50 32.63 ? 422  ASP A OD1   1 
ATOM   3250  O OD1   B ASP A  1  422 ? 33.027  5.824   -19.122 0.50 33.34 ? 422  ASP A OD1   1 
ATOM   3251  O OD2   A ASP A  1  422 ? 30.392  8.553   -18.985 0.50 31.76 ? 422  ASP A OD2   1 
ATOM   3252  O OD2   B ASP A  1  422 ? 32.012  7.100   -17.650 0.50 32.45 ? 422  ASP A OD2   1 
ATOM   3253  N N     . LEU A  1  423 ? 32.774  5.968   -22.748 1.00 27.53 ? 423  LEU A N     1 
ATOM   3254  C CA    . LEU A  1  423 ? 32.002  4.971   -23.483 1.00 25.15 ? 423  LEU A CA    1 
ATOM   3255  C C     . LEU A  1  423 ? 32.303  3.583   -22.920 1.00 23.49 ? 423  LEU A C     1 
ATOM   3256  O O     . LEU A  1  423 ? 33.334  3.379   -22.280 1.00 23.00 ? 423  LEU A O     1 
ATOM   3257  C CB    . LEU A  1  423 ? 32.348  5.024   -24.975 1.00 25.31 ? 423  LEU A CB    1 
ATOM   3258  C CG    . LEU A  1  423 ? 32.090  6.361   -25.679 1.00 26.23 ? 423  LEU A CG    1 
ATOM   3259  C CD1   . LEU A  1  423 ? 32.442  6.242   -27.152 1.00 25.22 ? 423  LEU A CD1   1 
ATOM   3260  C CD2   . LEU A  1  423 ? 30.632  6.758   -25.513 1.00 26.76 ? 423  LEU A CD2   1 
ATOM   3261  N N     . PRO A  1  424 ? 31.408  2.610   -23.154 1.00 22.21 ? 424  PRO A N     1 
ATOM   3262  C CA    . PRO A  1  424 ? 31.607  1.246   -22.650 1.00 20.69 ? 424  PRO A CA    1 
ATOM   3263  C C     . PRO A  1  424 ? 32.760  0.481   -23.299 1.00 19.52 ? 424  PRO A C     1 
ATOM   3264  O O     . PRO A  1  424 ? 33.181  0.792   -24.413 1.00 18.93 ? 424  PRO A O     1 
ATOM   3265  C CB    . PRO A  1  424 ? 30.257  0.587   -22.914 1.00 21.15 ? 424  PRO A CB    1 
ATOM   3266  C CG    . PRO A  1  424 ? 29.816  1.254   -24.175 1.00 22.82 ? 424  PRO A CG    1 
ATOM   3267  C CD    . PRO A  1  424 ? 30.146  2.708   -23.910 1.00 21.23 ? 424  PRO A CD    1 
ATOM   3268  N N     . GLY A  1  425 ? 33.263  -0.521  -22.584 1.00 18.06 ? 425  GLY A N     1 
ATOM   3269  C CA    . GLY A  1  425 ? 34.349  -1.338  -23.096 1.00 16.44 ? 425  GLY A CA    1 
ATOM   3270  C C     . GLY A  1  425 ? 35.629  -0.595  -23.425 1.00 15.17 ? 425  GLY A C     1 
ATOM   3271  O O     . GLY A  1  425 ? 36.116  0.208   -22.628 1.00 15.57 ? 425  GLY A O     1 
ATOM   3272  N N     . VAL A  1  426 ? 36.172  -0.869  -24.608 1.00 13.05 ? 426  VAL A N     1 
ATOM   3273  C CA    . VAL A  1  426 ? 37.413  -0.251  -25.060 1.00 12.33 ? 426  VAL A CA    1 
ATOM   3274  C C     . VAL A  1  426 ? 37.181  1.058   -25.806 1.00 11.77 ? 426  VAL A C     1 
ATOM   3275  O O     . VAL A  1  426 ? 38.127  1.685   -26.274 1.00 12.66 ? 426  VAL A O     1 
ATOM   3276  C CB    . VAL A  1  426 ? 38.194  -1.193  -26.006 1.00 10.86 ? 426  VAL A CB    1 
ATOM   3277  C CG1   . VAL A  1  426 ? 38.423  -2.529  -25.332 1.00 10.14 ? 426  VAL A CG1   1 
ATOM   3278  C CG2   . VAL A  1  426 ? 37.432  -1.375  -27.314 1.00 10.29 ? 426  VAL A CG2   1 
ATOM   3279  N N     . GLU A  1  427 ? 35.923  1.467   -25.916 1.00 14.33 ? 427  GLU A N     1 
ATOM   3280  C CA    . GLU A  1  427 ? 35.589  2.693   -26.631 1.00 14.89 ? 427  GLU A CA    1 
ATOM   3281  C C     . GLU A  1  427 ? 35.751  3.951   -25.788 1.00 14.72 ? 427  GLU A C     1 
ATOM   3282  O O     . GLU A  1  427 ? 35.752  3.893   -24.559 1.00 14.97 ? 427  GLU A O     1 
ATOM   3283  C CB    . GLU A  1  427 ? 34.155  2.608   -27.157 1.00 16.86 ? 427  GLU A CB    1 
ATOM   3284  C CG    . GLU A  1  427 ? 33.961  1.562   -28.243 1.00 20.89 ? 427  GLU A CG    1 
ATOM   3285  C CD    . GLU A  1  427 ? 32.539  1.521   -28.763 1.00 24.67 ? 427  GLU A CD    1 
ATOM   3286  O OE1   . GLU A  1  427 ? 31.680  0.882   -28.120 1.00 24.20 ? 427  GLU A OE1   1 
ATOM   3287  O OE2   . GLU A  1  427 ? 32.279  2.144   -29.814 1.00 26.95 ? 427  GLU A OE2   1 
ATOM   3288  N N     . GLY A  1  428 ? 35.896  5.091   -26.459 1.00 14.15 ? 428  GLY A N     1 
ATOM   3289  C CA    . GLY A  1  428 ? 36.037  6.346   -25.742 1.00 14.04 ? 428  GLY A CA    1 
ATOM   3290  C C     . GLY A  1  428 ? 37.393  7.016   -25.854 1.00 13.88 ? 428  GLY A C     1 
ATOM   3291  O O     . GLY A  1  428 ? 37.534  8.189   -25.507 1.00 14.48 ? 428  GLY A O     1 
ATOM   3292  N N     . PHE A  1  429 ? 38.394  6.282   -26.327 1.00 13.41 ? 429  PHE A N     1 
ATOM   3293  C CA    . PHE A  1  429 ? 39.731  6.844   -26.475 1.00 13.90 ? 429  PHE A CA    1 
ATOM   3294  C C     . PHE A  1  429 ? 39.904  7.540   -27.813 1.00 14.10 ? 429  PHE A C     1 
ATOM   3295  O O     . PHE A  1  429 ? 39.211  7.236   -28.782 1.00 16.10 ? 429  PHE A O     1 
ATOM   3296  C CB    . PHE A  1  429 ? 40.813  5.758   -26.396 1.00 11.93 ? 429  PHE A CB    1 
ATOM   3297  C CG    . PHE A  1  429 ? 40.914  5.078   -25.065 1.00 11.38 ? 429  PHE A CG    1 
ATOM   3298  C CD1   . PHE A  1  429 ? 40.231  3.891   -24.818 1.00 11.71 ? 429  PHE A CD1   1 
ATOM   3299  C CD2   . PHE A  1  429 ? 41.712  5.612   -24.062 1.00 10.75 ? 429  PHE A CD2   1 
ATOM   3300  C CE1   . PHE A  1  429 ? 40.347  3.247   -23.591 1.00 11.07 ? 429  PHE A CE1   1 
ATOM   3301  C CE2   . PHE A  1  429 ? 41.833  4.976   -22.832 1.00 11.83 ? 429  PHE A CE2   1 
ATOM   3302  C CZ    . PHE A  1  429 ? 41.151  3.792   -22.596 1.00 11.24 ? 429  PHE A CZ    1 
ATOM   3303  N N     . ASN A  1  430 ? 40.840  8.479   -27.852 1.00 14.84 ? 430  ASN A N     1 
ATOM   3304  C CA    . ASN A  1  430 ? 41.179  9.166   -29.086 1.00 15.65 ? 430  ASN A CA    1 
ATOM   3305  C C     . ASN A  1  430 ? 42.322  8.274   -29.567 1.00 15.29 ? 430  ASN A C     1 
ATOM   3306  O O     . ASN A  1  430 ? 43.391  8.248   -28.957 1.00 15.12 ? 430  ASN A O     1 
ATOM   3307  C CB    . ASN A  1  430 ? 41.685  10.579  -28.792 1.00 17.40 ? 430  ASN A CB    1 
ATOM   3308  C CG    . ASN A  1  430 ? 42.053  11.346  -30.049 1.00 20.04 ? 430  ASN A CG    1 
ATOM   3309  O OD1   . ASN A  1  430 ? 42.453  12.509  -29.982 1.00 21.77 ? 430  ASN A OD1   1 
ATOM   3310  N ND2   . ASN A  1  430 ? 41.921  10.700  -31.203 1.00 20.37 ? 430  ASN A ND2   1 
ATOM   3311  N N     . ILE A  1  431 ? 42.089  7.526   -30.639 1.00 14.12 ? 431  ILE A N     1 
ATOM   3312  C CA    . ILE A  1  431 ? 43.096  6.604   -31.155 1.00 14.48 ? 431  ILE A CA    1 
ATOM   3313  C C     . ILE A  1  431 ? 43.911  7.129   -32.329 1.00 15.06 ? 431  ILE A C     1 
ATOM   3314  O O     . ILE A  1  431 ? 43.366  7.723   -33.260 1.00 16.94 ? 431  ILE A O     1 
ATOM   3315  C CB    . ILE A  1  431 ? 42.436  5.268   -31.601 1.00 14.66 ? 431  ILE A CB    1 
ATOM   3316  C CG1   . ILE A  1  431 ? 41.679  4.635   -30.428 1.00 16.28 ? 431  ILE A CG1   1 
ATOM   3317  C CG2   . ILE A  1  431 ? 43.490  4.315   -32.151 1.00 14.98 ? 431  ILE A CG2   1 
ATOM   3318  C CD1   . ILE A  1  431 ? 42.548  4.278   -29.239 1.00 15.17 ? 431  ILE A CD1   1 
ATOM   3319  N N     . LEU A  1  432 ? 45.221  6.910   -32.276 1.00 14.30 ? 432  LEU A N     1 
ATOM   3320  C CA    . LEU A  1  432 ? 46.105  7.306   -33.368 1.00 14.39 ? 432  LEU A CA    1 
ATOM   3321  C C     . LEU A  1  432 ? 46.380  6.022   -34.144 1.00 14.88 ? 432  LEU A C     1 
ATOM   3322  O O     . LEU A  1  432 ? 47.087  5.140   -33.660 1.00 15.60 ? 432  LEU A O     1 
ATOM   3323  C CB    . LEU A  1  432 ? 47.429  7.869   -32.839 1.00 14.43 ? 432  LEU A CB    1 
ATOM   3324  C CG    . LEU A  1  432 ? 48.441  8.264   -33.924 1.00 15.20 ? 432  LEU A CG    1 
ATOM   3325  C CD1   . LEU A  1  432 ? 47.986  9.557   -34.595 1.00 16.20 ? 432  LEU A CD1   1 
ATOM   3326  C CD2   . LEU A  1  432 ? 49.825  8.446   -33.314 1.00 14.86 ? 432  LEU A CD2   1 
ATOM   3327  N N     . GLY A  1  433 ? 45.812  5.907   -35.339 1.00 14.15 ? 433  GLY A N     1 
ATOM   3328  C CA    . GLY A  1  433 ? 46.029  4.706   -36.123 1.00 13.46 ? 433  GLY A CA    1 
ATOM   3329  C C     . GLY A  1  433 ? 44.849  3.753   -36.085 1.00 11.51 ? 433  GLY A C     1 
ATOM   3330  O O     . GLY A  1  433 ? 43.720  4.155   -35.808 1.00 12.39 ? 433  GLY A O     1 
ATOM   3331  N N     . ILE A  1  434 ? 45.116  2.478   -36.347 1.00 10.25 ? 434  ILE A N     1 
ATOM   3332  C CA    . ILE A  1  434 ? 44.066  1.463   -36.378 1.00 11.09 ? 434  ILE A CA    1 
ATOM   3333  C C     . ILE A  1  434 ? 43.567  1.065   -34.993 1.00 10.66 ? 434  ILE A C     1 
ATOM   3334  O O     . ILE A  1  434 ? 44.335  0.608   -34.152 1.00 11.04 ? 434  ILE A O     1 
ATOM   3335  C CB    . ILE A  1  434 ? 44.557  0.205   -37.116 1.00 12.19 ? 434  ILE A CB    1 
ATOM   3336  C CG1   . ILE A  1  434 ? 45.018  0.594   -38.525 1.00 11.98 ? 434  ILE A CG1   1 
ATOM   3337  C CG2   . ILE A  1  434 ? 43.442  -0.841  -37.170 1.00 11.92 ? 434  ILE A CG2   1 
ATOM   3338  C CD1   . ILE A  1  434 ? 45.690  -0.518  -39.285 1.00 12.15 ? 434  ILE A CD1   1 
ATOM   3339  N N     . PRO A  1  435 ? 42.259  1.233   -34.743 1.00 11.48 ? 435  PRO A N     1 
ATOM   3340  C CA    . PRO A  1  435 ? 41.669  0.886   -33.447 1.00 11.13 ? 435  PRO A CA    1 
ATOM   3341  C C     . PRO A  1  435 ? 41.332  -0.599  -33.310 1.00 9.89  ? 435  PRO A C     1 
ATOM   3342  O O     . PRO A  1  435 ? 41.226  -1.318  -34.304 1.00 10.19 ? 435  PRO A O     1 
ATOM   3343  C CB    . PRO A  1  435 ? 40.421  1.756   -33.407 1.00 12.20 ? 435  PRO A CB    1 
ATOM   3344  C CG    . PRO A  1  435 ? 39.970  1.706   -34.837 1.00 12.34 ? 435  PRO A CG    1 
ATOM   3345  C CD    . PRO A  1  435 ? 41.267  1.903   -35.607 1.00 12.90 ? 435  PRO A CD    1 
ATOM   3346  N N     . LEU A  1  436 ? 41.174  -1.056  -32.072 1.00 9.65  ? 436  LEU A N     1 
ATOM   3347  C CA    . LEU A  1  436 ? 40.816  -2.446  -31.819 1.00 9.54  ? 436  LEU A CA    1 
ATOM   3348  C C     . LEU A  1  436 ? 39.368  -2.660  -32.210 1.00 9.84  ? 436  LEU A C     1 
ATOM   3349  O O     . LEU A  1  436 ? 38.585  -1.711  -32.260 1.00 10.28 ? 436  LEU A O     1 
ATOM   3350  C CB    . LEU A  1  436 ? 40.910  -2.787  -30.330 1.00 11.62 ? 436  LEU A CB    1 
ATOM   3351  C CG    . LEU A  1  436 ? 42.230  -3.008  -29.604 1.00 13.12 ? 436  LEU A CG    1 
ATOM   3352  C CD1   . LEU A  1  436 ? 41.919  -3.372  -28.153 1.00 14.34 ? 436  LEU A CD1   1 
ATOM   3353  C CD2   . LEU A  1  436 ? 43.020  -4.124  -30.274 1.00 14.82 ? 436  LEU A CD2   1 
ATOM   3354  N N     . PRO A  1  437 ? 38.996  -3.911  -32.516 1.00 10.22 ? 437  PRO A N     1 
ATOM   3355  C CA    . PRO A  1  437 ? 37.602  -4.178  -32.872 1.00 10.40 ? 437  PRO A CA    1 
ATOM   3356  C C     . PRO A  1  437 ? 36.832  -3.875  -31.581 1.00 10.20 ? 437  PRO A C     1 
ATOM   3357  O O     . PRO A  1  437 ? 37.357  -4.102  -30.490 1.00 10.11 ? 437  PRO A O     1 
ATOM   3358  C CB    . PRO A  1  437 ? 37.611  -5.670  -33.191 1.00 11.38 ? 437  PRO A CB    1 
ATOM   3359  C CG    . PRO A  1  437 ? 38.986  -5.884  -33.763 1.00 12.17 ? 437  PRO A CG    1 
ATOM   3360  C CD    . PRO A  1  437 ? 39.857  -5.069  -32.823 1.00 10.27 ? 437  PRO A CD    1 
ATOM   3361  N N     . LYS A  1  438 ? 35.612  -3.360  -31.685 1.00 11.73 ? 438  LYS A N     1 
ATOM   3362  C CA    . LYS A  1  438 ? 34.829  -3.042  -30.488 1.00 12.06 ? 438  LYS A CA    1 
ATOM   3363  C C     . LYS A  1  438 ? 34.461  -4.305  -29.708 1.00 11.11 ? 438  LYS A C     1 
ATOM   3364  O O     . LYS A  1  438 ? 34.583  -4.355  -28.478 1.00 10.28 ? 438  LYS A O     1 
ATOM   3365  C CB    . LYS A  1  438 ? 33.550  -2.299  -30.878 1.00 14.47 ? 438  LYS A CB    1 
ATOM   3366  C CG    . LYS A  1  438 ? 33.783  -1.068  -31.738 1.00 19.07 ? 438  LYS A CG    1 
ATOM   3367  C CD    . LYS A  1  438 ? 32.465  -0.470  -32.208 1.00 21.89 ? 438  LYS A CD    1 
ATOM   3368  C CE    . LYS A  1  438 ? 32.692  0.650   -33.211 1.00 25.33 ? 438  LYS A CE    1 
ATOM   3369  N NZ    . LYS A  1  438 ? 33.514  1.754   -32.641 1.00 28.06 ? 438  LYS A NZ    1 
ATOM   3370  N N     . ASP A  1  439 ? 34.002  -5.316  -30.438 1.00 10.46 ? 439  ASP A N     1 
ATOM   3371  C CA    . ASP A  1  439 ? 33.595  -6.598  -29.864 1.00 10.40 ? 439  ASP A CA    1 
ATOM   3372  C C     . ASP A  1  439 ? 34.829  -7.404  -29.464 1.00 9.60  ? 439  ASP A C     1 
ATOM   3373  O O     . ASP A  1  439 ? 35.550  -7.907  -30.324 1.00 10.99 ? 439  ASP A O     1 
ATOM   3374  C CB    . ASP A  1  439 ? 32.780  -7.370  -30.904 1.00 10.82 ? 439  ASP A CB    1 
ATOM   3375  C CG    . ASP A  1  439 ? 32.230  -8.679  -30.376 1.00 11.42 ? 439  ASP A CG    1 
ATOM   3376  O OD1   . ASP A  1  439 ? 32.666  -9.136  -29.299 1.00 10.49 ? 439  ASP A OD1   1 
ATOM   3377  O OD2   . ASP A  1  439 ? 31.358  -9.260  -31.056 1.00 12.11 ? 439  ASP A OD2   1 
ATOM   3378  N N     . GLN A  1  440 ? 35.061  -7.541  -28.161 1.00 9.60  ? 440  GLN A N     1 
ATOM   3379  C CA    . GLN A  1  440 ? 36.231  -8.270  -27.679 1.00 9.66  ? 440  GLN A CA    1 
ATOM   3380  C C     . GLN A  1  440 ? 36.154  -9.788  -27.847 1.00 9.88  ? 440  GLN A C     1 
ATOM   3381  O O     . GLN A  1  440 ? 37.101  -10.497 -27.508 1.00 11.48 ? 440  GLN A O     1 
ATOM   3382  C CB    . GLN A  1  440 ? 36.504  -7.915  -26.212 1.00 9.29  ? 440  GLN A CB    1 
ATOM   3383  C CG    . GLN A  1  440 ? 36.766  -6.426  -25.985 1.00 9.56  ? 440  GLN A CG    1 
ATOM   3384  C CD    . GLN A  1  440 ? 37.926  -5.898  -26.819 1.00 9.82  ? 440  GLN A CD    1 
ATOM   3385  O OE1   . GLN A  1  440 ? 39.090  -6.205  -26.553 1.00 8.65  ? 440  GLN A OE1   1 
ATOM   3386  N NE2   . GLN A  1  440 ? 37.608  -5.107  -27.840 1.00 10.89 ? 440  GLN A NE2   1 
ATOM   3387  N N     . THR A  1  441 ? 35.037  -10.285 -28.375 1.00 10.11 ? 441  THR A N     1 
ATOM   3388  C CA    . THR A  1  441 ? 34.875  -11.720 -28.592 1.00 10.27 ? 441  THR A CA    1 
ATOM   3389  C C     . THR A  1  441 ? 34.885  -12.065 -30.086 1.00 11.26 ? 441  THR A C     1 
ATOM   3390  O O     . THR A  1  441 ? 34.722  -13.227 -30.461 1.00 13.41 ? 441  THR A O     1 
ATOM   3391  C CB    . THR A  1  441 ? 33.553  -12.243 -27.975 1.00 11.04 ? 441  THR A CB    1 
ATOM   3392  O OG1   . THR A  1  441 ? 32.436  -11.646 -28.652 1.00 10.56 ? 441  THR A OG1   1 
ATOM   3393  C CG2   . THR A  1  441 ? 33.487  -11.908 -26.490 1.00 11.02 ? 441  THR A CG2   1 
ATOM   3394  N N     . ASP A  1  442 ? 35.078  -11.059 -30.934 1.00 10.57 ? 442  ASP A N     1 
ATOM   3395  C CA    . ASP A  1  442 ? 35.101  -11.274 -32.384 1.00 11.33 ? 442  ASP A CA    1 
ATOM   3396  C C     . ASP A  1  442 ? 36.510  -11.658 -32.836 1.00 10.00 ? 442  ASP A C     1 
ATOM   3397  O O     . ASP A  1  442 ? 37.291  -10.809 -33.270 1.00 10.32 ? 442  ASP A O     1 
ATOM   3398  C CB    . ASP A  1  442 ? 34.653  -10.004 -33.117 1.00 12.41 ? 442  ASP A CB    1 
ATOM   3399  C CG    . ASP A  1  442 ? 34.379  -10.240 -34.596 1.00 14.39 ? 442  ASP A CG    1 
ATOM   3400  O OD1   . ASP A  1  442 ? 34.906  -11.221 -35.161 1.00 15.93 ? 442  ASP A OD1   1 
ATOM   3401  O OD2   . ASP A  1  442 ? 33.644  -9.429  -35.197 1.00 16.40 ? 442  ASP A OD2   1 
ATOM   3402  N N     . ASP A  1  443 ? 36.826  -12.945 -32.740 1.00 10.67 ? 443  ASP A N     1 
ATOM   3403  C CA    . ASP A  1  443 ? 38.142  -13.445 -33.117 1.00 11.39 ? 443  ASP A CA    1 
ATOM   3404  C C     . ASP A  1  443 ? 38.546  -13.109 -34.549 1.00 9.70  ? 443  ASP A C     1 
ATOM   3405  O O     . ASP A  1  443 ? 39.673  -12.683 -34.796 1.00 9.50  ? 443  ASP A O     1 
ATOM   3406  C CB    . ASP A  1  443 ? 38.206  -14.963 -32.905 1.00 12.58 ? 443  ASP A CB    1 
ATOM   3407  C CG    . ASP A  1  443 ? 38.175  -15.349 -31.435 1.00 14.66 ? 443  ASP A CG    1 
ATOM   3408  O OD1   . ASP A  1  443 ? 37.963  -14.459 -30.587 1.00 14.80 ? 443  ASP A OD1   1 
ATOM   3409  O OD2   . ASP A  1  443 ? 38.358  -16.547 -31.129 1.00 18.89 ? 443  ASP A OD2   1 
ATOM   3410  N N     . ALA A  1  444 ? 37.633  -13.298 -35.497 1.00 9.86  ? 444  ALA A N     1 
ATOM   3411  C CA    . ALA A  1  444 ? 37.942  -13.008 -36.892 1.00 9.64  ? 444  ALA A CA    1 
ATOM   3412  C C     . ALA A  1  444 ? 38.349  -11.550 -37.084 1.00 9.87  ? 444  ALA A C     1 
ATOM   3413  O O     . ALA A  1  444 ? 39.254  -11.246 -37.866 1.00 10.94 ? 444  ALA A O     1 
ATOM   3414  C CB    . ALA A  1  444 ? 36.748  -13.340 -37.775 1.00 11.65 ? 444  ALA A CB    1 
ATOM   3415  N N     . ALA A  1  445 ? 37.680  -10.649 -36.371 1.00 9.72  ? 445  ALA A N     1 
ATOM   3416  C CA    . ALA A  1  445 ? 37.996  -9.232  -36.471 1.00 7.93  ? 445  ALA A CA    1 
ATOM   3417  C C     . ALA A  1  445 ? 39.390  -8.974  -35.903 1.00 9.24  ? 445  ALA A C     1 
ATOM   3418  O O     . ALA A  1  445 ? 40.134  -8.140  -36.423 1.00 9.25  ? 445  ALA A O     1 
ATOM   3419  C CB    . ALA A  1  445 ? 36.961  -8.405  -35.720 1.00 9.26  ? 445  ALA A CB    1 
ATOM   3420  N N     . PHE A  1  446 ? 39.741  -9.690  -34.839 1.00 8.58  ? 446  PHE A N     1 
ATOM   3421  C CA    . PHE A  1  446 ? 41.056  -9.521  -34.235 1.00 8.17  ? 446  PHE A CA    1 
ATOM   3422  C C     . PHE A  1  446 ? 42.148  -10.076 -35.137 1.00 7.47  ? 446  PHE A C     1 
ATOM   3423  O O     . PHE A  1  446 ? 43.250  -9.545  -35.169 1.00 7.27  ? 446  PHE A O     1 
ATOM   3424  C CB    . PHE A  1  446 ? 41.124  -10.181 -32.852 1.00 8.09  ? 446  PHE A CB    1 
ATOM   3425  C CG    . PHE A  1  446 ? 40.672  -9.283  -31.733 1.00 7.93  ? 446  PHE A CG    1 
ATOM   3426  C CD1   . PHE A  1  446 ? 39.321  -9.059  -31.502 1.00 8.44  ? 446  PHE A CD1   1 
ATOM   3427  C CD2   . PHE A  1  446 ? 41.605  -8.636  -30.926 1.00 6.91  ? 446  PHE A CD2   1 
ATOM   3428  C CE1   . PHE A  1  446 ? 38.903  -8.205  -30.486 1.00 8.70  ? 446  PHE A CE1   1 
ATOM   3429  C CE2   . PHE A  1  446 ? 41.199  -7.781  -29.907 1.00 7.39  ? 446  PHE A CE2   1 
ATOM   3430  C CZ    . PHE A  1  446 ? 39.845  -7.563  -29.685 1.00 7.95  ? 446  PHE A CZ    1 
ATOM   3431  N N     . GLU A  1  447 ? 41.848  -11.144 -35.872 1.00 7.63  ? 447  GLU A N     1 
ATOM   3432  C CA    . GLU A  1  447 ? 42.842  -11.705 -36.781 1.00 8.71  ? 447  GLU A CA    1 
ATOM   3433  C C     . GLU A  1  447 ? 43.133  -10.689 -37.880 1.00 9.46  ? 447  GLU A C     1 
ATOM   3434  O O     . GLU A  1  447 ? 44.284  -10.498 -38.273 1.00 9.11  ? 447  GLU A O     1 
ATOM   3435  C CB    . GLU A  1  447 ? 42.344  -13.023 -37.387 1.00 9.26  ? 447  GLU A CB    1 
ATOM   3436  C CG    . GLU A  1  447 ? 42.332  -14.175 -36.396 1.00 10.95 ? 447  GLU A CG    1 
ATOM   3437  C CD    . GLU A  1  447 ? 42.035  -15.508 -37.050 1.00 14.49 ? 447  GLU A CD    1 
ATOM   3438  O OE1   . GLU A  1  447 ? 41.995  -15.564 -38.302 1.00 15.15 ? 447  GLU A OE1   1 
ATOM   3439  O OE2   . GLU A  1  447 ? 41.853  -16.503 -36.314 1.00 16.12 ? 447  GLU A OE2   1 
ATOM   3440  N N     . THR A  1  448 ? 42.087  -10.031 -38.373 1.00 9.56  ? 448  THR A N     1 
ATOM   3441  C CA    . THR A  1  448 ? 42.257  -9.022  -39.409 1.00 10.24 ? 448  THR A CA    1 
ATOM   3442  C C     . THR A  1  448 ? 43.057  -7.845  -38.854 1.00 9.37  ? 448  THR A C     1 
ATOM   3443  O O     . THR A  1  448 ? 43.930  -7.304  -39.532 1.00 9.51  ? 448  THR A O     1 
ATOM   3444  C CB    . THR A  1  448 ? 40.898  -8.524  -39.925 1.00 10.65 ? 448  THR A CB    1 
ATOM   3445  O OG1   . THR A  1  448 ? 40.248  -9.588  -40.631 1.00 13.29 ? 448  THR A OG1   1 
ATOM   3446  C CG2   . THR A  1  448 ? 41.081  -7.336  -40.858 1.00 12.13 ? 448  THR A CG2   1 
ATOM   3447  N N     . PHE A  1  449 ? 42.755  -7.450  -37.621 1.00 9.83  ? 449  PHE A N     1 
ATOM   3448  C CA    . PHE A  1  449 ? 43.484  -6.353  -36.986 1.00 8.99  ? 449  PHE A CA    1 
ATOM   3449  C C     . PHE A  1  449 ? 44.964  -6.717  -36.884 1.00 9.62  ? 449  PHE A C     1 
ATOM   3450  O O     . PHE A  1  449 ? 45.836  -5.912  -37.207 1.00 9.57  ? 449  PHE A O     1 
ATOM   3451  C CB    . PHE A  1  449 ? 42.948  -6.084  -35.576 1.00 9.33  ? 449  PHE A CB    1 
ATOM   3452  C CG    . PHE A  1  449 ? 43.811  -5.148  -34.774 1.00 9.29  ? 449  PHE A CG    1 
ATOM   3453  C CD1   . PHE A  1  449 ? 43.624  -3.770  -34.848 1.00 10.29 ? 449  PHE A CD1   1 
ATOM   3454  C CD2   . PHE A  1  449 ? 44.851  -5.643  -33.986 1.00 8.97  ? 449  PHE A CD2   1 
ATOM   3455  C CE1   . PHE A  1  449 ? 44.462  -2.897  -34.150 1.00 10.52 ? 449  PHE A CE1   1 
ATOM   3456  C CE2   . PHE A  1  449 ? 45.696  -4.782  -33.286 1.00 7.81  ? 449  PHE A CE2   1 
ATOM   3457  C CZ    . PHE A  1  449 ? 45.503  -3.405  -33.367 1.00 9.29  ? 449  PHE A CZ    1 
ATOM   3458  N N     . CYS A  1  450 ? 45.240  -7.933  -36.421 1.00 7.86  ? 450  CYS A N     1 
ATOM   3459  C CA    . CYS A  1  450 ? 46.611  -8.396  -36.268 1.00 8.53  ? 450  CYS A CA    1 
ATOM   3460  C C     . CYS A  1  450 ? 47.390  -8.368  -37.572 1.00 9.19  ? 450  CYS A C     1 
ATOM   3461  O O     . CYS A  1  450 ? 48.511  -7.865  -37.621 1.00 10.50 ? 450  CYS A O     1 
ATOM   3462  C CB    . CYS A  1  450 ? 46.625  -9.813  -35.692 1.00 9.56  ? 450  CYS A CB    1 
ATOM   3463  S SG    . CYS A  1  450 ? 46.328  -9.844  -33.897 1.00 11.00 ? 450  CYS A SG    1 
ATOM   3464  N N     . ARG A  1  451 ? 46.790  -8.902  -38.630 1.00 7.64  ? 451  ARG A N     1 
ATOM   3465  C CA    . ARG A  1  451 ? 47.450  -8.949  -39.927 1.00 9.18  ? 451  ARG A CA    1 
ATOM   3466  C C     . ARG A  1  451 ? 47.694  -7.590  -40.575 1.00 9.38  ? 451  ARG A C     1 
ATOM   3467  O O     . ARG A  1  451 ? 48.788  -7.319  -41.061 1.00 10.35 ? 451  ARG A O     1 
ATOM   3468  C CB    . ARG A  1  451 ? 46.640  -9.810  -40.901 1.00 8.18  ? 451  ARG A CB    1 
ATOM   3469  C CG    . ARG A  1  451 ? 46.673  -11.308 -40.619 1.00 8.79  ? 451  ARG A CG    1 
ATOM   3470  C CD    . ARG A  1  451 ? 45.860  -12.055 -41.677 1.00 8.12  ? 451  ARG A CD    1 
ATOM   3471  N NE    . ARG A  1  451 ? 45.820  -13.502 -41.476 1.00 8.86  ? 451  ARG A NE    1 
ATOM   3472  C CZ    . ARG A  1  451 ? 46.821  -14.334 -41.754 1.00 8.26  ? 451  ARG A CZ    1 
ATOM   3473  N NH1   . ARG A  1  451 ? 47.965  -13.872 -42.247 1.00 11.10 ? 451  ARG A NH1   1 
ATOM   3474  N NH2   . ARG A  1  451 ? 46.665  -15.638 -41.561 1.00 10.22 ? 451  ARG A NH2   1 
ATOM   3475  N N     . GLU A  1  452 ? 46.672  -6.740  -40.585 1.00 10.20 ? 452  GLU A N     1 
ATOM   3476  C CA    . GLU A  1  452 ? 46.780  -5.437  -41.229 1.00 11.00 ? 452  GLU A CA    1 
ATOM   3477  C C     . GLU A  1  452 ? 47.499  -4.333  -40.469 1.00 10.68 ? 452  GLU A C     1 
ATOM   3478  O O     . GLU A  1  452 ? 47.920  -3.350  -41.073 1.00 12.95 ? 452  GLU A O     1 
ATOM   3479  C CB    . GLU A  1  452 ? 45.389  -4.928  -41.616 1.00 12.88 ? 452  GLU A CB    1 
ATOM   3480  C CG    . GLU A  1  452 ? 44.599  -5.886  -42.488 1.00 19.70 ? 452  GLU A CG    1 
ATOM   3481  C CD    . GLU A  1  452 ? 43.417  -5.216  -43.158 1.00 22.06 ? 452  GLU A CD    1 
ATOM   3482  O OE1   . GLU A  1  452 ? 42.653  -4.519  -42.459 1.00 20.99 ? 452  GLU A OE1   1 
ATOM   3483  O OE2   . GLU A  1  452 ? 43.253  -5.390  -44.385 1.00 24.79 ? 452  GLU A OE2   1 
ATOM   3484  N N     . SER A  1  453 ? 47.655  -4.486  -39.159 1.00 8.89  ? 453  SER A N     1 
ATOM   3485  C CA    . SER A  1  453 ? 48.302  -3.442  -38.369 1.00 8.59  ? 453  SER A CA    1 
ATOM   3486  C C     . SER A  1  453 ? 49.692  -3.806  -37.860 1.00 8.64  ? 453  SER A C     1 
ATOM   3487  O O     . SER A  1  453 ? 50.340  -2.996  -37.200 1.00 9.23  ? 453  SER A O     1 
ATOM   3488  C CB    . SER A  1  453 ? 47.420  -3.080  -37.170 1.00 7.47  ? 453  SER A CB    1 
ATOM   3489  O OG    . SER A  1  453 ? 47.432  -4.121  -36.203 1.00 9.13  ? 453  SER A OG    1 
ATOM   3490  N N     . VAL A  1  454 ? 50.150  -5.013  -38.179 1.00 8.40  ? 454  VAL A N     1 
ATOM   3491  C CA    . VAL A  1  454 ? 51.447  -5.496  -37.710 1.00 8.04  ? 454  VAL A CA    1 
ATOM   3492  C C     . VAL A  1  454 ? 52.656  -4.621  -38.037 1.00 8.88  ? 454  VAL A C     1 
ATOM   3493  O O     . VAL A  1  454 ? 52.705  -3.958  -39.073 1.00 8.48  ? 454  VAL A O     1 
ATOM   3494  C CB    . VAL A  1  454 ? 51.725  -6.932  -38.238 1.00 8.15  ? 454  VAL A CB    1 
ATOM   3495  C CG1   . VAL A  1  454 ? 52.094  -6.896  -39.719 1.00 8.28  ? 454  VAL A CG1   1 
ATOM   3496  C CG2   . VAL A  1  454 ? 52.832  -7.587  -37.411 1.00 10.05 ? 454  VAL A CG2   1 
ATOM   3497  N N     . ALA A  1  455 ? 53.626  -4.633  -37.125 1.00 7.29  ? 455  ALA A N     1 
ATOM   3498  C CA    . ALA A  1  455 ? 54.877  -3.893  -37.271 1.00 7.27  ? 455  ALA A CA    1 
ATOM   3499  C C     . ALA A  1  455 ? 55.966  -4.780  -36.679 1.00 7.25  ? 455  ALA A C     1 
ATOM   3500  O O     . ALA A  1  455 ? 55.675  -5.869  -36.196 1.00 7.07  ? 455  ALA A O     1 
ATOM   3501  C CB    . ALA A  1  455 ? 54.806  -2.577  -36.510 1.00 8.53  ? 455  ALA A CB    1 
ATOM   3502  N N     . SER A  1  456 ? 57.218  -4.332  -36.724 1.00 6.57  ? 456  SER A N     1 
ATOM   3503  C CA    . SER A  1  456 ? 58.304  -5.118  -36.145 1.00 6.93  ? 456  SER A CA    1 
ATOM   3504  C C     . SER A  1  456 ? 58.586  -4.668  -34.717 1.00 8.78  ? 456  SER A C     1 
ATOM   3505  O O     . SER A  1  456 ? 58.469  -3.483  -34.399 1.00 9.52  ? 456  SER A O     1 
ATOM   3506  C CB    . SER A  1  456 ? 59.586  -4.968  -36.967 1.00 7.60  ? 456  SER A CB    1 
ATOM   3507  O OG    . SER A  1  456 ? 60.674  -5.613  -36.316 1.00 6.82  ? 456  SER A OG    1 
ATOM   3508  N N     . TYR A  1  457 ? 58.944  -5.614  -33.854 1.00 8.70  ? 457  TYR A N     1 
ATOM   3509  C CA    . TYR A  1  457 ? 59.280  -5.274  -32.476 1.00 10.13 ? 457  TYR A CA    1 
ATOM   3510  C C     . TYR A  1  457 ? 60.784  -4.987  -32.438 1.00 10.59 ? 457  TYR A C     1 
ATOM   3511  O O     . TYR A  1  457 ? 61.340  -4.662  -31.389 1.00 10.42 ? 457  TYR A O     1 
ATOM   3512  C CB    . TYR A  1  457 ? 58.944  -6.427  -31.516 1.00 10.70 ? 457  TYR A CB    1 
ATOM   3513  C CG    . TYR A  1  457 ? 58.480  -5.936  -30.160 1.00 12.82 ? 457  TYR A CG    1 
ATOM   3514  C CD1   . TYR A  1  457 ? 57.121  -5.797  -29.875 1.00 11.93 ? 457  TYR A CD1   1 
ATOM   3515  C CD2   . TYR A  1  457 ? 59.399  -5.526  -29.194 1.00 14.35 ? 457  TYR A CD2   1 
ATOM   3516  C CE1   . TYR A  1  457 ? 56.688  -5.254  -28.665 1.00 15.06 ? 457  TYR A CE1   1 
ATOM   3517  C CE2   . TYR A  1  457 ? 58.979  -4.983  -27.984 1.00 16.86 ? 457  TYR A CE2   1 
ATOM   3518  C CZ    . TYR A  1  457 ? 57.624  -4.847  -27.727 1.00 16.86 ? 457  TYR A CZ    1 
ATOM   3519  O OH    . TYR A  1  457 ? 57.208  -4.284  -26.543 1.00 20.98 ? 457  TYR A OH    1 
ATOM   3520  N N     . TRP A  1  458 ? 61.424  -5.115  -33.601 1.00 9.49  ? 458  TRP A N     1 
ATOM   3521  C CA    . TRP A  1  458 ? 62.857  -4.869  -33.776 1.00 9.48  ? 458  TRP A CA    1 
ATOM   3522  C C     . TRP A  1  458 ? 63.742  -5.903  -33.092 1.00 8.14  ? 458  TRP A C     1 
ATOM   3523  O O     . TRP A  1  458 ? 64.948  -5.695  -32.942 1.00 8.06  ? 458  TRP A O     1 
ATOM   3524  C CB    . TRP A  1  458 ? 63.242  -3.486  -33.245 1.00 10.95 ? 458  TRP A CB    1 
ATOM   3525  C CG    . TRP A  1  458 ? 62.349  -2.367  -33.681 1.00 13.43 ? 458  TRP A CG    1 
ATOM   3526  C CD1   . TRP A  1  458 ? 62.028  -2.017  -34.961 1.00 13.25 ? 458  TRP A CD1   1 
ATOM   3527  C CD2   . TRP A  1  458 ? 61.684  -1.429  -32.828 1.00 14.90 ? 458  TRP A CD2   1 
ATOM   3528  N NE1   . TRP A  1  458 ? 61.206  -0.914  -34.956 1.00 14.85 ? 458  TRP A NE1   1 
ATOM   3529  C CE2   . TRP A  1  458 ? 60.980  -0.533  -33.660 1.00 15.81 ? 458  TRP A CE2   1 
ATOM   3530  C CE3   . TRP A  1  458 ? 61.615  -1.257  -31.438 1.00 15.16 ? 458  TRP A CE3   1 
ATOM   3531  C CZ2   . TRP A  1  458 ? 60.215  0.523   -33.148 1.00 17.02 ? 458  TRP A CZ2   1 
ATOM   3532  C CZ3   . TRP A  1  458 ? 60.856  -0.209  -30.929 1.00 16.76 ? 458  TRP A CZ3   1 
ATOM   3533  C CH2   . TRP A  1  458 ? 60.167  0.667   -31.784 1.00 17.94 ? 458  TRP A CH2   1 
ATOM   3534  N N     . HIS A  1  459 ? 63.153  -7.019  -32.679 1.00 7.50  ? 459  HIS A N     1 
ATOM   3535  C CA    . HIS A  1  459 ? 63.923  -8.053  -32.004 1.00 7.34  ? 459  HIS A CA    1 
ATOM   3536  C C     . HIS A  1  459 ? 64.218  -9.249  -32.901 1.00 8.72  ? 459  HIS A C     1 
ATOM   3537  O O     . HIS A  1  459 ? 64.317  -10.383 -32.423 1.00 9.09  ? 459  HIS A O     1 
ATOM   3538  C CB    . HIS A  1  459 ? 63.183  -8.511  -30.741 1.00 6.64  ? 459  HIS A CB    1 
ATOM   3539  C CG    . HIS A  1  459 ? 63.008  -7.432  -29.720 1.00 7.38  ? 459  HIS A CG    1 
ATOM   3540  N ND1   . HIS A  1  459 ? 62.338  -7.633  -28.529 1.00 9.30  ? 459  HIS A ND1   1 
ATOM   3541  C CD2   . HIS A  1  459 ? 63.420  -6.142  -29.701 1.00 8.61  ? 459  HIS A CD2   1 
ATOM   3542  C CE1   . HIS A  1  459 ? 62.345  -6.516  -27.827 1.00 9.03  ? 459  HIS A CE1   1 
ATOM   3543  N NE2   . HIS A  1  459 ? 62.996  -5.593  -28.515 1.00 8.24  ? 459  HIS A NE2   1 
ATOM   3544  N N     . TYR A  1  460 ? 64.357  -8.997  -34.200 1.00 6.24  ? 460  TYR A N     1 
ATOM   3545  C CA    . TYR A  1  460 ? 64.653  -10.066 -35.151 1.00 7.59  ? 460  TYR A CA    1 
ATOM   3546  C C     . TYR A  1  460 ? 65.934  -10.787 -34.754 1.00 7.79  ? 460  TYR A C     1 
ATOM   3547  O O     . TYR A  1  460 ? 66.840  -10.203 -34.155 1.00 8.04  ? 460  TYR A O     1 
ATOM   3548  C CB    . TYR A  1  460 ? 64.764  -9.496  -36.569 1.00 6.20  ? 460  TYR A CB    1 
ATOM   3549  C CG    . TYR A  1  460 ? 65.557  -8.213  -36.634 1.00 4.98  ? 460  TYR A CG    1 
ATOM   3550  C CD1   . TYR A  1  460 ? 66.951  -8.232  -36.646 1.00 7.53  ? 460  TYR A CD1   1 
ATOM   3551  C CD2   . TYR A  1  460 ? 64.912  -6.973  -36.620 1.00 6.16  ? 460  TYR A CD2   1 
ATOM   3552  C CE1   . TYR A  1  460 ? 67.689  -7.046  -36.636 1.00 7.67  ? 460  TYR A CE1   1 
ATOM   3553  C CE2   . TYR A  1  460 ? 65.640  -5.782  -36.609 1.00 5.93  ? 460  TYR A CE2   1 
ATOM   3554  C CZ    . TYR A  1  460 ? 67.029  -5.829  -36.614 1.00 8.99  ? 460  TYR A CZ    1 
ATOM   3555  O OH    . TYR A  1  460 ? 67.762  -4.663  -36.553 1.00 9.51  ? 460  TYR A OH    1 
ATOM   3556  N N     . HIS A  1  461 ? 65.997  -12.067 -35.098 1.00 6.94  ? 461  HIS A N     1 
ATOM   3557  C CA    . HIS A  1  461 ? 67.126  -12.912 -34.748 1.00 7.43  ? 461  HIS A CA    1 
ATOM   3558  C C     . HIS A  1  461 ? 67.156  -14.108 -35.691 1.00 7.73  ? 461  HIS A C     1 
ATOM   3559  O O     . HIS A  1  461 ? 66.268  -14.267 -36.529 1.00 7.73  ? 461  HIS A O     1 
ATOM   3560  C CB    . HIS A  1  461 ? 66.952  -13.409 -33.311 1.00 7.42  ? 461  HIS A CB    1 
ATOM   3561  C CG    . HIS A  1  461 ? 65.604  -14.008 -33.048 1.00 6.43  ? 461  HIS A CG    1 
ATOM   3562  N ND1   . HIS A  1  461 ? 64.478  -13.242 -32.821 1.00 7.03  ? 461  HIS A ND1   1 
ATOM   3563  C CD2   . HIS A  1  461 ? 65.188  -15.296 -33.037 1.00 7.99  ? 461  HIS A CD2   1 
ATOM   3564  C CE1   . HIS A  1  461 ? 63.429  -14.033 -32.684 1.00 6.95  ? 461  HIS A CE1   1 
ATOM   3565  N NE2   . HIS A  1  461 ? 63.833  -15.286 -32.811 1.00 7.39  ? 461  HIS A NE2   1 
ATOM   3566  N N     . GLY A  1  462 ? 68.174  -14.949 -35.541 1.00 7.65  ? 462  GLY A N     1 
ATOM   3567  C CA    . GLY A  1  462 ? 68.296  -16.126 -36.385 1.00 7.87  ? 462  GLY A CA    1 
ATOM   3568  C C     . GLY A  1  462 ? 69.133  -15.879 -37.624 1.00 7.71  ? 462  GLY A C     1 
ATOM   3569  O O     . GLY A  1  462 ? 69.755  -14.827 -37.756 1.00 8.95  ? 462  GLY A O     1 
ATOM   3570  N N     . GLY A  1  463 ? 69.157  -16.855 -38.530 1.00 8.68  ? 463  GLY A N     1 
ATOM   3571  C CA    . GLY A  1  463 ? 69.924  -16.718 -39.759 1.00 7.37  ? 463  GLY A CA    1 
ATOM   3572  C C     . GLY A  1  463 ? 71.235  -17.488 -39.806 1.00 8.15  ? 463  GLY A C     1 
ATOM   3573  O O     . GLY A  1  463 ? 71.824  -17.656 -40.876 1.00 9.96  ? 463  GLY A O     1 
ATOM   3574  N N     . CYS A  1  464 ? 71.701  -17.947 -38.649 1.00 7.43  ? 464  CYS A N     1 
ATOM   3575  C CA    . CYS A  1  464 ? 72.949  -18.707 -38.551 1.00 7.16  ? 464  CYS A CA    1 
ATOM   3576  C C     . CYS A  1  464 ? 72.807  -19.555 -37.289 1.00 8.12  ? 464  CYS A C     1 
ATOM   3577  O O     . CYS A  1  464 ? 73.601  -19.458 -36.350 1.00 6.63  ? 464  CYS A O     1 
ATOM   3578  C CB    . CYS A  1  464 ? 74.127  -17.743 -38.420 1.00 9.76  ? 464  CYS A CB    1 
ATOM   3579  S SG    . CYS A  1  464 ? 75.734  -18.513 -38.644 1.00 10.91 ? 464  CYS A SG    1 
ATOM   3580  N N     . LEU A  1  465 ? 71.786  -20.404 -37.296 1.00 7.61  ? 465  LEU A N     1 
ATOM   3581  C CA    . LEU A  1  465 ? 71.436  -21.224 -36.142 1.00 9.46  ? 465  LEU A CA    1 
ATOM   3582  C C     . LEU A  1  465 ? 72.371  -22.311 -35.636 1.00 9.63  ? 465  LEU A C     1 
ATOM   3583  O O     . LEU A  1  465 ? 73.051  -22.995 -36.401 1.00 9.62  ? 465  LEU A O     1 
ATOM   3584  C CB    . LEU A  1  465 ? 70.063  -21.873 -36.369 1.00 9.53  ? 465  LEU A CB    1 
ATOM   3585  C CG    . LEU A  1  465 ? 68.865  -20.992 -36.728 1.00 11.30 ? 465  LEU A CG    1 
ATOM   3586  C CD1   . LEU A  1  465 ? 67.615  -21.861 -36.755 1.00 10.16 ? 465  LEU A CD1   1 
ATOM   3587  C CD2   . LEU A  1  465 ? 68.706  -19.873 -35.717 1.00 11.05 ? 465  LEU A CD2   1 
ATOM   3588  N N     . VAL A  1  466 ? 72.386  -22.451 -34.315 1.00 9.97  ? 466  VAL A N     1 
ATOM   3589  C CA    . VAL A  1  466 ? 73.145  -23.503 -33.663 1.00 9.36  ? 466  VAL A CA    1 
ATOM   3590  C C     . VAL A  1  466 ? 72.364  -24.750 -34.067 1.00 10.70 ? 466  VAL A C     1 
ATOM   3591  O O     . VAL A  1  466 ? 71.136  -24.777 -33.960 1.00 11.58 ? 466  VAL A O     1 
ATOM   3592  C CB    . VAL A  1  466 ? 73.098  -23.361 -32.128 1.00 10.26 ? 466  VAL A CB    1 
ATOM   3593  C CG1   . VAL A  1  466 ? 73.508  -24.673 -31.468 1.00 10.26 ? 466  VAL A CG1   1 
ATOM   3594  C CG2   . VAL A  1  466 ? 74.016  -22.235 -31.686 1.00 10.07 ? 466  VAL A CG2   1 
ATOM   3595  N N     . GLY A  1  467 ? 73.067  -25.770 -34.545 1.00 10.45 ? 467  GLY A N     1 
ATOM   3596  C CA    . GLY A  1  467 ? 72.397  -26.987 -34.966 1.00 10.75 ? 467  GLY A CA    1 
ATOM   3597  C C     . GLY A  1  467 ? 72.115  -27.018 -36.458 1.00 11.81 ? 467  GLY A C     1 
ATOM   3598  O O     . GLY A  1  467 ? 71.709  -28.048 -36.994 1.00 12.25 ? 467  GLY A O     1 
ATOM   3599  N N     . LYS A  1  468 ? 72.318  -25.884 -37.127 1.00 11.99 ? 468  LYS A N     1 
ATOM   3600  C CA    . LYS A  1  468 ? 72.096  -25.785 -38.569 1.00 11.84 ? 468  LYS A CA    1 
ATOM   3601  C C     . LYS A  1  468 ? 73.385  -25.337 -39.249 1.00 12.04 ? 468  LYS A C     1 
ATOM   3602  O O     . LYS A  1  468 ? 73.837  -25.956 -40.214 1.00 13.85 ? 468  LYS A O     1 
ATOM   3603  C CB    . LYS A  1  468 ? 70.975  -24.785 -38.879 1.00 12.92 ? 468  LYS A CB    1 
ATOM   3604  C CG    . LYS A  1  468 ? 69.616  -25.163 -38.308 1.00 14.22 ? 468  LYS A CG    1 
ATOM   3605  C CD    . LYS A  1  468 ? 69.075  -26.435 -38.945 1.00 18.21 ? 468  LYS A CD    1 
ATOM   3606  C CE    . LYS A  1  468 ? 67.718  -26.803 -38.360 1.00 21.01 ? 468  LYS A CE    1 
ATOM   3607  N NZ    . LYS A  1  468 ? 67.132  -27.995 -39.032 1.00 25.68 ? 468  LYS A NZ    1 
ATOM   3608  N N     . VAL A  1  469 ? 73.971  -24.252 -38.747 1.00 10.22 ? 469  VAL A N     1 
ATOM   3609  C CA    . VAL A  1  469 ? 75.220  -23.736 -39.296 1.00 9.20  ? 469  VAL A CA    1 
ATOM   3610  C C     . VAL A  1  469 ? 76.339  -23.877 -38.265 1.00 8.05  ? 469  VAL A C     1 
ATOM   3611  O O     . VAL A  1  469 ? 77.480  -24.177 -38.610 1.00 9.90  ? 469  VAL A O     1 
ATOM   3612  C CB    . VAL A  1  469 ? 75.101  -22.232 -39.673 1.00 6.39  ? 469  VAL A CB    1 
ATOM   3613  C CG1   . VAL A  1  469 ? 76.413  -21.743 -40.270 1.00 8.77  ? 469  VAL A CG1   1 
ATOM   3614  C CG2   . VAL A  1  469 ? 73.961  -22.023 -40.661 1.00 8.53  ? 469  VAL A CG2   1 
ATOM   3615  N N     . LEU A  1  470 ? 75.999  -23.663 -36.999 1.00 8.42  ? 470  LEU A N     1 
ATOM   3616  C CA    . LEU A  1  470 ? 76.973  -23.730 -35.909 1.00 7.84  ? 470  LEU A CA    1 
ATOM   3617  C C     . LEU A  1  470 ? 76.806  -24.956 -35.021 1.00 9.32  ? 470  LEU A C     1 
ATOM   3618  O O     . LEU A  1  470 ? 75.743  -25.578 -34.995 1.00 9.80  ? 470  LEU A O     1 
ATOM   3619  C CB    . LEU A  1  470 ? 76.834  -22.495 -35.015 1.00 8.80  ? 470  LEU A CB    1 
ATOM   3620  C CG    . LEU A  1  470 ? 76.740  -21.121 -35.674 1.00 8.12  ? 470  LEU A CG    1 
ATOM   3621  C CD1   . LEU A  1  470 ? 76.505  -20.066 -34.593 1.00 8.40  ? 470  LEU A CD1   1 
ATOM   3622  C CD2   . LEU A  1  470 ? 78.006  -20.830 -36.452 1.00 7.36  ? 470  LEU A CD2   1 
ATOM   3623  N N     . ASP A  1  471 ? 77.859  -25.295 -34.283 1.00 10.66 ? 471  ASP A N     1 
ATOM   3624  C CA    . ASP A  1  471 ? 77.776  -26.412 -33.353 1.00 11.03 ? 471  ASP A CA    1 
ATOM   3625  C C     . ASP A  1  471 ? 77.540  -25.840 -31.954 1.00 11.49 ? 471  ASP A C     1 
ATOM   3626  O O     . ASP A  1  471 ? 77.341  -24.629 -31.806 1.00 10.86 ? 471  ASP A O     1 
ATOM   3627  C CB    . ASP A  1  471 ? 79.043  -27.291 -33.413 1.00 12.47 ? 471  ASP A CB    1 
ATOM   3628  C CG    . ASP A  1  471 ? 80.297  -26.592 -32.912 1.00 12.53 ? 471  ASP A CG    1 
ATOM   3629  O OD1   . ASP A  1  471 ? 81.386  -27.185 -33.083 1.00 15.54 ? 471  ASP A OD1   1 
ATOM   3630  O OD2   . ASP A  1  471 ? 80.220  -25.479 -32.349 1.00 12.26 ? 471  ASP A OD2   1 
ATOM   3631  N N     . GLY A  1  472 ? 77.557  -26.697 -30.938 1.00 9.75  ? 472  GLY A N     1 
ATOM   3632  C CA    . GLY A  1  472 ? 77.305  -26.255 -29.574 1.00 10.70 ? 472  GLY A CA    1 
ATOM   3633  C C     . GLY A  1  472 ? 78.300  -25.289 -28.961 1.00 10.15 ? 472  GLY A C     1 
ATOM   3634  O O     . GLY A  1  472 ? 78.045  -24.732 -27.886 1.00 11.06 ? 472  GLY A O     1 
ATOM   3635  N N     . ASP A  1  473 ? 79.430  -25.094 -29.631 1.00 10.91 ? 473  ASP A N     1 
ATOM   3636  C CA    . ASP A  1  473 ? 80.467  -24.186 -29.152 1.00 11.70 ? 473  ASP A CA    1 
ATOM   3637  C C     . ASP A  1  473 ? 80.508  -22.933 -30.027 1.00 10.94 ? 473  ASP A C     1 
ATOM   3638  O O     . ASP A  1  473 ? 81.451  -22.150 -29.962 1.00 10.21 ? 473  ASP A O     1 
ATOM   3639  C CB    . ASP A  1  473 ? 81.830  -24.884 -29.177 1.00 13.67 ? 473  ASP A CB    1 
ATOM   3640  C CG    . ASP A  1  473 ? 81.866  -26.125 -28.299 1.00 16.92 ? 473  ASP A CG    1 
ATOM   3641  O OD1   . ASP A  1  473 ? 81.599  -26.002 -27.087 1.00 19.77 ? 473  ASP A OD1   1 
ATOM   3642  O OD2   . ASP A  1  473 ? 82.160  -27.223 -28.818 1.00 20.36 ? 473  ASP A OD2   1 
ATOM   3643  N N     . PHE A  1  474 ? 79.469  -22.770 -30.841 1.00 10.02 ? 474  PHE A N     1 
ATOM   3644  C CA    . PHE A  1  474 ? 79.314  -21.640 -31.755 1.00 9.44  ? 474  PHE A CA    1 
ATOM   3645  C C     . PHE A  1  474 ? 80.309  -21.598 -32.906 1.00 9.23  ? 474  PHE A C     1 
ATOM   3646  O O     . PHE A  1  474 ? 80.514  -20.554 -33.532 1.00 9.69  ? 474  PHE A O     1 
ATOM   3647  C CB    . PHE A  1  474 ? 79.333  -20.316 -30.983 1.00 8.20  ? 474  PHE A CB    1 
ATOM   3648  C CG    . PHE A  1  474 ? 78.224  -20.197 -29.974 1.00 8.20  ? 474  PHE A CG    1 
ATOM   3649  C CD1   . PHE A  1  474 ? 78.361  -20.747 -28.703 1.00 7.63  ? 474  PHE A CD1   1 
ATOM   3650  C CD2   . PHE A  1  474 ? 77.025  -19.579 -30.314 1.00 9.29  ? 474  PHE A CD2   1 
ATOM   3651  C CE1   . PHE A  1  474 ? 77.317  -20.686 -27.780 1.00 8.75  ? 474  PHE A CE1   1 
ATOM   3652  C CE2   . PHE A  1  474 ? 75.975  -19.513 -29.402 1.00 9.20  ? 474  PHE A CE2   1 
ATOM   3653  C CZ    . PHE A  1  474 ? 76.121  -20.068 -28.133 1.00 10.67 ? 474  PHE A CZ    1 
ATOM   3654  N N     . ARG A  1  475 ? 80.926  -22.738 -33.192 1.00 7.95  ? 475  ARG A N     1 
ATOM   3655  C CA    . ARG A  1  475 ? 81.863  -22.822 -34.301 1.00 8.07  ? 475  ARG A CA    1 
ATOM   3656  C C     . ARG A  1  475 ? 81.069  -23.080 -35.577 1.00 8.07  ? 475  ARG A C     1 
ATOM   3657  O O     . ARG A  1  475 ? 80.059  -23.786 -35.552 1.00 8.73  ? 475  ARG A O     1 
ATOM   3658  C CB    . ARG A  1  475 ? 82.833  -23.996 -34.121 1.00 8.33  ? 475  ARG A CB    1 
ATOM   3659  C CG    . ARG A  1  475 ? 83.789  -23.920 -32.949 1.00 9.89  ? 475  ARG A CG    1 
ATOM   3660  C CD    . ARG A  1  475 ? 84.856  -24.994 -33.129 1.00 12.61 ? 475  ARG A CD    1 
ATOM   3661  N NE    . ARG A  1  475 ? 85.777  -25.110 -32.003 1.00 13.22 ? 475  ARG A NE    1 
ATOM   3662  C CZ    A ARG A  1  475 ? 85.429  -25.542 -30.797 0.50 14.38 ? 475  ARG A CZ    1 
ATOM   3663  C CZ    B ARG A  1  475 ? 87.018  -24.640 -32.004 0.50 15.02 ? 475  ARG A CZ    1 
ATOM   3664  N NH1   A ARG A  1  475 ? 84.178  -25.897 -30.554 0.50 17.31 ? 475  ARG A NH1   1 
ATOM   3665  N NH1   B ARG A  1  475 ? 87.494  -24.024 -33.074 0.50 17.94 ? 475  ARG A NH1   1 
ATOM   3666  N NH2   A ARG A  1  475 ? 86.334  -25.631 -29.837 0.50 17.22 ? 475  ARG A NH2   1 
ATOM   3667  N NH2   B ARG A  1  475 ? 87.780  -24.775 -30.932 0.50 17.71 ? 475  ARG A NH2   1 
ATOM   3668  N N     . VAL A  1  476 ? 81.516  -22.502 -36.687 1.00 8.63  ? 476  VAL A N     1 
ATOM   3669  C CA    . VAL A  1  476 ? 80.867  -22.748 -37.969 1.00 8.04  ? 476  VAL A CA    1 
ATOM   3670  C C     . VAL A  1  476 ? 81.350  -24.152 -38.347 1.00 8.98  ? 476  VAL A C     1 
ATOM   3671  O O     . VAL A  1  476 ? 82.549  -24.381 -38.503 1.00 9.75  ? 476  VAL A O     1 
ATOM   3672  C CB    . VAL A  1  476 ? 81.321  -21.732 -39.040 1.00 8.70  ? 476  VAL A CB    1 
ATOM   3673  C CG1   . VAL A  1  476 ? 80.835  -22.164 -40.415 1.00 9.48  ? 476  VAL A CG1   1 
ATOM   3674  C CG2   . VAL A  1  476 ? 80.765  -20.350 -38.706 1.00 10.83 ? 476  VAL A CG2   1 
ATOM   3675  N N     . THR A  1  477 ? 80.425  -25.095 -38.482 1.00 9.77  ? 477  THR A N     1 
ATOM   3676  C CA    . THR A  1  477 ? 80.817  -26.463 -38.801 1.00 10.61 ? 477  THR A CA    1 
ATOM   3677  C C     . THR A  1  477 ? 81.609  -26.581 -40.100 1.00 11.02 ? 477  THR A C     1 
ATOM   3678  O O     . THR A  1  477 ? 81.317  -25.907 -41.090 1.00 10.93 ? 477  THR A O     1 
ATOM   3679  C CB    . THR A  1  477 ? 79.587  -27.402 -38.868 1.00 10.80 ? 477  THR A CB    1 
ATOM   3680  O OG1   . THR A  1  477 ? 78.739  -27.019 -39.959 1.00 13.17 ? 477  THR A OG1   1 
ATOM   3681  C CG2   . THR A  1  477 ? 78.796  -27.332 -37.565 1.00 10.12 ? 477  THR A CG2   1 
ATOM   3682  N N     . GLY A  1  478 ? 82.634  -27.430 -40.077 1.00 10.40 ? 478  GLY A N     1 
ATOM   3683  C CA    . GLY A  1  478 ? 83.445  -27.648 -41.260 1.00 10.93 ? 478  GLY A CA    1 
ATOM   3684  C C     . GLY A  1  478 ? 84.557  -26.649 -41.500 1.00 11.41 ? 478  GLY A C     1 
ATOM   3685  O O     . GLY A  1  478 ? 85.357  -26.828 -42.416 1.00 12.08 ? 478  GLY A O     1 
ATOM   3686  N N     . ILE A  1  479 ? 84.615  -25.603 -40.682 1.00 10.50 ? 479  ILE A N     1 
ATOM   3687  C CA    . ILE A  1  479 ? 85.643  -24.576 -40.823 1.00 10.75 ? 479  ILE A CA    1 
ATOM   3688  C C     . ILE A  1  479 ? 86.329  -24.330 -39.483 1.00 10.79 ? 479  ILE A C     1 
ATOM   3689  O O     . ILE A  1  479 ? 85.662  -24.133 -38.471 1.00 11.45 ? 479  ILE A O     1 
ATOM   3690  C CB    . ILE A  1  479 ? 85.034  -23.240 -41.312 1.00 9.93  ? 479  ILE A CB    1 
ATOM   3691  C CG1   . ILE A  1  479 ? 84.300  -23.457 -42.636 1.00 10.72 ? 479  ILE A CG1   1 
ATOM   3692  C CG2   . ILE A  1  479 ? 86.130  -22.197 -41.479 1.00 9.17  ? 479  ILE A CG2   1 
ATOM   3693  C CD1   . ILE A  1  479 ? 83.641  -22.209 -43.177 1.00 11.84 ? 479  ILE A CD1   1 
ATOM   3694  N N     . ASN A  1  480 ? 87.659  -24.351 -39.476 1.00 11.26 ? 480  ASN A N     1 
ATOM   3695  C CA    . ASN A  1  480 ? 88.410  -24.116 -38.246 1.00 11.06 ? 480  ASN A CA    1 
ATOM   3696  C C     . ASN A  1  480 ? 88.635  -22.625 -38.025 1.00 10.70 ? 480  ASN A C     1 
ATOM   3697  O O     . ASN A  1  480 ? 88.616  -21.838 -38.974 1.00 9.54  ? 480  ASN A O     1 
ATOM   3698  C CB    . ASN A  1  480 ? 89.773  -24.815 -38.292 1.00 12.88 ? 480  ASN A CB    1 
ATOM   3699  C CG    . ASN A  1  480 ? 89.655  -26.313 -38.483 1.00 13.91 ? 480  ASN A CG    1 
ATOM   3700  O OD1   . ASN A  1  480 ? 88.818  -26.962 -37.863 1.00 15.27 ? 480  ASN A OD1   1 
ATOM   3701  N ND2   . ASN A  1  480 ? 90.506  -26.872 -39.339 1.00 17.19 ? 480  ASN A ND2   1 
ATOM   3702  N N     . ALA A  1  481 ? 88.836  -22.256 -36.761 1.00 9.82  ? 481  ALA A N     1 
ATOM   3703  C CA    . ALA A  1  481 ? 89.105  -20.874 -36.363 1.00 8.57  ? 481  ALA A CA    1 
ATOM   3704  C C     . ALA A  1  481 ? 88.042  -19.858 -36.770 1.00 8.01  ? 481  ALA A C     1 
ATOM   3705  O O     . ALA A  1  481 ? 88.363  -18.700 -37.042 1.00 8.48  ? 481  ALA A O     1 
ATOM   3706  C CB    . ALA A  1  481 ? 90.463  -20.440 -36.905 1.00 11.83 ? 481  ALA A CB    1 
ATOM   3707  N N     . LEU A  1  482 ? 86.784  -20.285 -36.803 1.00 8.10  ? 482  LEU A N     1 
ATOM   3708  C CA    . LEU A  1  482 ? 85.692  -19.389 -37.171 1.00 7.58  ? 482  LEU A CA    1 
ATOM   3709  C C     . LEU A  1  482 ? 84.449  -19.633 -36.322 1.00 7.82  ? 482  LEU A C     1 
ATOM   3710  O O     . LEU A  1  482 ? 83.922  -20.743 -36.282 1.00 7.89  ? 482  LEU A O     1 
ATOM   3711  C CB    . LEU A  1  482 ? 85.329  -19.569 -38.649 1.00 8.71  ? 482  LEU A CB    1 
ATOM   3712  C CG    . LEU A  1  482 ? 84.202  -18.669 -39.169 1.00 7.65  ? 482  LEU A CG    1 
ATOM   3713  C CD1   . LEU A  1  482 ? 84.651  -17.213 -39.142 1.00 9.69  ? 482  LEU A CD1   1 
ATOM   3714  C CD2   . LEU A  1  482 ? 83.822  -19.081 -40.583 1.00 8.39  ? 482  LEU A CD2   1 
ATOM   3715  N N     . ARG A  1  483 ? 83.983  -18.596 -35.636 1.00 7.07  ? 483  ARG A N     1 
ATOM   3716  C CA    . ARG A  1  483 ? 82.781  -18.729 -34.820 1.00 7.98  ? 483  ARG A CA    1 
ATOM   3717  C C     . ARG A  1  483 ? 81.827  -17.580 -35.108 1.00 8.23  ? 483  ARG A C     1 
ATOM   3718  O O     . ARG A  1  483 ? 82.182  -16.621 -35.788 1.00 8.97  ? 483  ARG A O     1 
ATOM   3719  C CB    . ARG A  1  483 ? 83.122  -18.736 -33.326 1.00 9.42  ? 483  ARG A CB    1 
ATOM   3720  C CG    . ARG A  1  483 ? 84.206  -19.727 -32.944 1.00 8.97  ? 483  ARG A CG    1 
ATOM   3721  C CD    . ARG A  1  483 ? 84.093  -20.145 -31.485 1.00 11.14 ? 483  ARG A CD    1 
ATOM   3722  N NE    . ARG A  1  483 ? 85.324  -20.778 -31.021 1.00 11.52 ? 483  ARG A NE    1 
ATOM   3723  C CZ    . ARG A  1  483 ? 85.409  -21.589 -29.972 1.00 12.00 ? 483  ARG A CZ    1 
ATOM   3724  N NH1   . ARG A  1  483 ? 84.328  -21.889 -29.263 1.00 14.03 ? 483  ARG A NH1   1 
ATOM   3725  N NH2   . ARG A  1  483 ? 86.586  -22.087 -29.621 1.00 12.83 ? 483  ARG A NH2   1 
ATOM   3726  N N     . VAL A  1  484 ? 80.611  -17.704 -34.595 1.00 7.24  ? 484  VAL A N     1 
ATOM   3727  C CA    . VAL A  1  484 ? 79.592  -16.678 -34.748 1.00 7.25  ? 484  VAL A CA    1 
ATOM   3728  C C     . VAL A  1  484 ? 78.973  -16.477 -33.371 1.00 7.15  ? 484  VAL A C     1 
ATOM   3729  O O     . VAL A  1  484 ? 78.530  -17.435 -32.739 1.00 8.80  ? 484  VAL A O     1 
ATOM   3730  C CB    . VAL A  1  484 ? 78.484  -17.101 -35.740 1.00 5.72  ? 484  VAL A CB    1 
ATOM   3731  C CG1   . VAL A  1  484 ? 77.320  -16.119 -35.662 1.00 7.79  ? 484  VAL A CG1   1 
ATOM   3732  C CG2   . VAL A  1  484 ? 79.039  -17.141 -37.162 1.00 5.07  ? 484  VAL A CG2   1 
ATOM   3733  N N     . VAL A  1  485 ? 78.961  -15.232 -32.900 1.00 7.15  ? 485  VAL A N     1 
ATOM   3734  C CA    . VAL A  1  485 ? 78.397  -14.917 -31.591 1.00 7.06  ? 485  VAL A CA    1 
ATOM   3735  C C     . VAL A  1  485 ? 77.624  -13.598 -31.646 1.00 7.19  ? 485  VAL A C     1 
ATOM   3736  O O     . VAL A  1  485 ? 78.218  -12.523 -31.648 1.00 8.16  ? 485  VAL A O     1 
ATOM   3737  C CB    . VAL A  1  485 ? 79.509  -14.802 -30.510 1.00 7.44  ? 485  VAL A CB    1 
ATOM   3738  C CG1   . VAL A  1  485 ? 78.881  -14.622 -29.129 1.00 8.97  ? 485  VAL A CG1   1 
ATOM   3739  C CG2   . VAL A  1  485 ? 80.404  -16.042 -30.540 1.00 8.21  ? 485  VAL A CG2   1 
ATOM   3740  N N     . ASP A  1  486 ? 76.298  -13.701 -31.703 1.00 6.60  ? 486  ASP A N     1 
ATOM   3741  C CA    . ASP A  1  486 ? 75.399  -12.546 -31.749 1.00 7.78  ? 486  ASP A CA    1 
ATOM   3742  C C     . ASP A  1  486 ? 73.955  -13.047 -31.817 1.00 7.30  ? 486  ASP A C     1 
ATOM   3743  O O     . ASP A  1  486 ? 73.691  -14.217 -31.550 1.00 6.88  ? 486  ASP A O     1 
ATOM   3744  C CB    . ASP A  1  486 ? 75.705  -11.644 -32.957 1.00 7.93  ? 486  ASP A CB    1 
ATOM   3745  C CG    . ASP A  1  486 ? 75.652  -12.386 -34.281 1.00 6.66  ? 486  ASP A CG    1 
ATOM   3746  O OD1   . ASP A  1  486 ? 74.966  -13.427 -34.356 1.00 8.61  ? 486  ASP A OD1   1 
ATOM   3747  O OD2   . ASP A  1  486 ? 76.290  -11.916 -35.251 1.00 7.75  ? 486  ASP A OD2   1 
ATOM   3748  N N     . GLY A  1  487 ? 73.024  -12.174 -32.193 1.00 6.79  ? 487  GLY A N     1 
ATOM   3749  C CA    . GLY A  1  487 ? 71.627  -12.578 -32.253 1.00 7.48  ? 487  GLY A CA    1 
ATOM   3750  C C     . GLY A  1  487 ? 71.203  -13.528 -33.360 1.00 6.43  ? 487  GLY A C     1 
ATOM   3751  O O     . GLY A  1  487 ? 70.043  -13.928 -33.411 1.00 7.89  ? 487  GLY A O     1 
ATOM   3752  N N     . SER A  1  488 ? 72.128  -13.910 -34.234 1.00 6.78  ? 488  SER A N     1 
ATOM   3753  C CA    . SER A  1  488 ? 71.800  -14.798 -35.347 1.00 6.34  ? 488  SER A CA    1 
ATOM   3754  C C     . SER A  1  488 ? 71.792  -16.289 -35.019 1.00 7.09  ? 488  SER A C     1 
ATOM   3755  O O     . SER A  1  488 ? 71.386  -17.099 -35.854 1.00 7.99  ? 488  SER A O     1 
ATOM   3756  C CB    . SER A  1  488 ? 72.794  -14.582 -36.494 1.00 6.29  ? 488  SER A CB    1 
ATOM   3757  O OG    . SER A  1  488 ? 74.067  -15.125 -36.163 1.00 8.22  ? 488  SER A OG    1 
ATOM   3758  N N     . THR A  1  489 ? 72.196  -16.659 -33.807 1.00 8.44  ? 489  THR A N     1 
ATOM   3759  C CA    . THR A  1  489 ? 72.322  -18.078 -33.482 1.00 7.40  ? 489  THR A CA    1 
ATOM   3760  C C     . THR A  1  489 ? 71.153  -18.913 -32.961 1.00 9.24  ? 489  THR A C     1 
ATOM   3761  O O     . THR A  1  489 ? 71.278  -20.137 -32.872 1.00 9.86  ? 489  THR A O     1 
ATOM   3762  C CB    . THR A  1  489 ? 73.515  -18.295 -32.531 1.00 9.34  ? 489  THR A CB    1 
ATOM   3763  O OG1   . THR A  1  489 ? 73.142  -17.943 -31.197 1.00 11.88 ? 489  THR A OG1   1 
ATOM   3764  C CG2   . THR A  1  489 ? 74.694  -17.433 -32.964 1.00 7.14  ? 489  THR A CG2   1 
ATOM   3765  N N     . PHE A  1  490 ? 70.029  -18.290 -32.623 1.00 8.23  ? 490  PHE A N     1 
ATOM   3766  C CA    . PHE A  1  490 ? 68.882  -19.051 -32.128 1.00 7.01  ? 490  PHE A CA    1 
ATOM   3767  C C     . PHE A  1  490 ? 67.582  -18.639 -32.808 1.00 8.17  ? 490  PHE A C     1 
ATOM   3768  O O     . PHE A  1  490 ? 67.405  -17.483 -33.177 1.00 9.16  ? 490  PHE A O     1 
ATOM   3769  C CB    . PHE A  1  490 ? 68.752  -18.894 -30.615 1.00 8.40  ? 490  PHE A CB    1 
ATOM   3770  C CG    . PHE A  1  490 ? 69.925  -19.441 -29.849 1.00 8.56  ? 490  PHE A CG    1 
ATOM   3771  C CD1   . PHE A  1  490 ? 70.815  -18.585 -29.210 1.00 7.83  ? 490  PHE A CD1   1 
ATOM   3772  C CD2   . PHE A  1  490 ? 70.142  -20.815 -29.773 1.00 8.20  ? 490  PHE A CD2   1 
ATOM   3773  C CE1   . PHE A  1  490 ? 71.906  -19.085 -28.502 1.00 8.51  ? 490  PHE A CE1   1 
ATOM   3774  C CE2   . PHE A  1  490 ? 71.232  -21.329 -29.066 1.00 8.94  ? 490  PHE A CE2   1 
ATOM   3775  C CZ    . PHE A  1  490 ? 72.115  -20.464 -28.430 1.00 7.99  ? 490  PHE A CZ    1 
ATOM   3776  N N     . PRO A  1  491 ? 66.648  -19.588 -32.970 1.00 8.41  ? 491  PRO A N     1 
ATOM   3777  C CA    . PRO A  1  491 ? 65.358  -19.329 -33.618 1.00 8.45  ? 491  PRO A CA    1 
ATOM   3778  C C     . PRO A  1  491 ? 64.315  -18.557 -32.821 1.00 9.20  ? 491  PRO A C     1 
ATOM   3779  O O     . PRO A  1  491 ? 63.477  -17.864 -33.400 1.00 9.49  ? 491  PRO A O     1 
ATOM   3780  C CB    . PRO A  1  491 ? 64.870  -20.730 -33.968 1.00 8.20  ? 491  PRO A CB    1 
ATOM   3781  C CG    . PRO A  1  491 ? 65.389  -21.543 -32.819 1.00 9.70  ? 491  PRO A CG    1 
ATOM   3782  C CD    . PRO A  1  491 ? 66.801  -21.024 -32.665 1.00 8.64  ? 491  PRO A CD    1 
ATOM   3783  N N     . TYR A  1  492 ? 64.361  -18.670 -31.500 1.00 8.77  ? 492  TYR A N     1 
ATOM   3784  C CA    . TYR A  1  492 ? 63.371  -18.001 -30.671 1.00 9.41  ? 492  TYR A CA    1 
ATOM   3785  C C     . TYR A  1  492 ? 63.973  -16.938 -29.767 1.00 9.16  ? 492  TYR A C     1 
ATOM   3786  O O     . TYR A  1  492 ? 65.137  -17.019 -29.385 1.00 9.09  ? 492  TYR A O     1 
ATOM   3787  C CB    . TYR A  1  492 ? 62.613  -19.060 -29.867 1.00 11.10 ? 492  TYR A CB    1 
ATOM   3788  C CG    . TYR A  1  492 ? 62.009  -20.123 -30.764 1.00 12.28 ? 492  TYR A CG    1 
ATOM   3789  C CD1   . TYR A  1  492 ? 62.229  -21.481 -30.526 1.00 14.41 ? 492  TYR A CD1   1 
ATOM   3790  C CD2   . TYR A  1  492 ? 61.251  -19.765 -31.883 1.00 10.80 ? 492  TYR A CD2   1 
ATOM   3791  C CE1   . TYR A  1  492 ? 61.710  -22.457 -31.387 1.00 14.82 ? 492  TYR A CE1   1 
ATOM   3792  C CE2   . TYR A  1  492 ? 60.732  -20.729 -32.745 1.00 13.67 ? 492  TYR A CE2   1 
ATOM   3793  C CZ    . TYR A  1  492 ? 60.967  -22.070 -32.493 1.00 15.65 ? 492  TYR A CZ    1 
ATOM   3794  O OH    . TYR A  1  492 ? 60.473  -23.016 -33.362 1.00 16.89 ? 492  TYR A OH    1 
ATOM   3795  N N     . THR A  1  493 ? 63.178  -15.924 -29.443 1.00 8.62  ? 493  THR A N     1 
ATOM   3796  C CA    . THR A  1  493 ? 63.660  -14.849 -28.594 1.00 8.70  ? 493  THR A CA    1 
ATOM   3797  C C     . THR A  1  493 ? 63.785  -15.355 -27.152 1.00 8.86  ? 493  THR A C     1 
ATOM   3798  O O     . THR A  1  493 ? 62.909  -16.053 -26.643 1.00 9.53  ? 493  THR A O     1 
ATOM   3799  C CB    . THR A  1  493 ? 62.724  -13.609 -28.698 1.00 10.06 ? 493  THR A CB    1 
ATOM   3800  O OG1   . THR A  1  493 ? 63.393  -12.462 -28.161 1.00 11.42 ? 493  THR A OG1   1 
ATOM   3801  C CG2   . THR A  1  493 ? 61.422  -13.837 -27.955 1.00 10.79 ? 493  THR A CG2   1 
ATOM   3802  N N     . PRO A  1  494 ? 64.892  -15.009 -26.479 1.00 8.04  ? 494  PRO A N     1 
ATOM   3803  C CA    . PRO A  1  494 ? 65.199  -15.406 -25.099 1.00 9.42  ? 494  PRO A CA    1 
ATOM   3804  C C     . PRO A  1  494 ? 64.336  -14.795 -23.999 1.00 8.36  ? 494  PRO A C     1 
ATOM   3805  O O     . PRO A  1  494 ? 64.247  -15.340 -22.899 1.00 9.94  ? 494  PRO A O     1 
ATOM   3806  C CB    . PRO A  1  494 ? 66.667  -15.021 -24.957 1.00 9.99  ? 494  PRO A CB    1 
ATOM   3807  C CG    . PRO A  1  494 ? 66.751  -13.781 -25.785 1.00 8.91  ? 494  PRO A CG    1 
ATOM   3808  C CD    . PRO A  1  494 ? 65.966  -14.160 -27.030 1.00 8.70  ? 494  PRO A CD    1 
ATOM   3809  N N     . ALA A  1  495 ? 63.707  -13.665 -24.292 1.00 7.98  ? 495  ALA A N     1 
ATOM   3810  C CA    . ALA A  1  495 ? 62.859  -12.991 -23.319 1.00 7.65  ? 495  ALA A CA    1 
ATOM   3811  C C     . ALA A  1  495 ? 62.063  -11.930 -24.060 1.00 7.94  ? 495  ALA A C     1 
ATOM   3812  O O     . ALA A  1  495 ? 62.118  -11.854 -25.288 1.00 8.77  ? 495  ALA A O     1 
ATOM   3813  C CB    . ALA A  1  495 ? 63.719  -12.342 -22.236 1.00 7.82  ? 495  ALA A CB    1 
ATOM   3814  N N     . SER A  1  496 ? 61.327  -11.110 -23.317 1.00 8.02  ? 496  SER A N     1 
ATOM   3815  C CA    . SER A  1  496 ? 60.540  -10.044 -23.929 1.00 7.25  ? 496  SER A CA    1 
ATOM   3816  C C     . SER A  1  496 ? 61.481  -9.061  -24.622 1.00 9.56  ? 496  SER A C     1 
ATOM   3817  O O     . SER A  1  496 ? 61.140  -8.461  -25.644 1.00 8.73  ? 496  SER A O     1 
ATOM   3818  C CB    . SER A  1  496 ? 59.723  -9.312  -22.861 1.00 6.98  ? 496  SER A CB    1 
ATOM   3819  O OG    . SER A  1  496 ? 60.568  -8.741  -21.877 1.00 8.30  ? 496  SER A OG    1 
ATOM   3820  N N     . HIS A  1  497 ? 62.671  -8.910  -24.050 1.00 8.24  ? 497  HIS A N     1 
ATOM   3821  C CA    . HIS A  1  497 ? 63.693  -8.014  -24.569 1.00 7.37  ? 497  HIS A CA    1 
ATOM   3822  C C     . HIS A  1  497 ? 64.983  -8.820  -24.509 1.00 7.03  ? 497  HIS A C     1 
ATOM   3823  O O     . HIS A  1  497 ? 65.437  -9.214  -23.435 1.00 7.49  ? 497  HIS A O     1 
ATOM   3824  C CB    . HIS A  1  497 ? 63.731  -6.751  -23.713 1.00 7.48  ? 497  HIS A CB    1 
ATOM   3825  C CG    . HIS A  1  497 ? 62.461  -5.957  -23.786 1.00 8.63  ? 497  HIS A CG    1 
ATOM   3826  N ND1   . HIS A  1  497 ? 61.308  -6.329  -23.125 1.00 8.75  ? 497  HIS A ND1   1 
ATOM   3827  C CD2   . HIS A  1  497 ? 62.142  -4.857  -24.508 1.00 9.39  ? 497  HIS A CD2   1 
ATOM   3828  C CE1   . HIS A  1  497 ? 60.335  -5.492  -23.439 1.00 10.71 ? 497  HIS A CE1   1 
ATOM   3829  N NE2   . HIS A  1  497 ? 60.814  -4.590  -24.278 1.00 9.29  ? 497  HIS A NE2   1 
ATOM   3830  N N     . PRO A  1  498 ? 65.591  -9.071  -25.678 1.00 7.86  ? 498  PRO A N     1 
ATOM   3831  C CA    . PRO A  1  498 ? 66.816  -9.855  -25.831 1.00 6.88  ? 498  PRO A CA    1 
ATOM   3832  C C     . PRO A  1  498 ? 68.209  -9.293  -25.596 1.00 7.14  ? 498  PRO A C     1 
ATOM   3833  O O     . PRO A  1  498 ? 69.158  -10.072 -25.563 1.00 7.09  ? 498  PRO A O     1 
ATOM   3834  C CB    . PRO A  1  498 ? 66.679  -10.373 -27.251 1.00 7.68  ? 498  PRO A CB    1 
ATOM   3835  C CG    . PRO A  1  498 ? 66.191  -9.130  -27.955 1.00 8.04  ? 498  PRO A CG    1 
ATOM   3836  C CD    . PRO A  1  498 ? 65.119  -8.600  -26.997 1.00 7.44  ? 498  PRO A CD    1 
ATOM   3837  N N     . GLN A  1  499 ? 68.371  -7.985  -25.431 1.00 5.58  ? 499  GLN A N     1 
ATOM   3838  C CA    . GLN A  1  499 ? 69.733  -7.479  -25.267 1.00 5.86  ? 499  GLN A CA    1 
ATOM   3839  C C     . GLN A  1  499 ? 70.486  -8.092  -24.087 1.00 6.94  ? 499  GLN A C     1 
ATOM   3840  O O     . GLN A  1  499 ? 71.681  -8.366  -24.193 1.00 8.11  ? 499  GLN A O     1 
ATOM   3841  C CB    . GLN A  1  499 ? 69.757  -5.940  -25.191 1.00 7.09  ? 499  GLN A CB    1 
ATOM   3842  C CG    . GLN A  1  499 ? 69.477  -5.308  -23.833 1.00 6.38  ? 499  GLN A CG    1 
ATOM   3843  C CD    . GLN A  1  499 ? 69.799  -3.818  -23.844 1.00 7.50  ? 499  GLN A CD    1 
ATOM   3844  O OE1   . GLN A  1  499 ? 70.753  -3.389  -24.497 1.00 9.08  ? 499  GLN A OE1   1 
ATOM   3845  N NE2   . GLN A  1  499 ? 69.018  -3.028  -23.113 1.00 9.16  ? 499  GLN A NE2   1 
ATOM   3846  N N     . GLY A  1  500 ? 69.799  -8.329  -22.976 1.00 6.46  ? 500  GLY A N     1 
ATOM   3847  C CA    . GLY A  1  500 ? 70.474  -8.918  -21.828 1.00 7.08  ? 500  GLY A CA    1 
ATOM   3848  C C     . GLY A  1  500 ? 71.123  -10.248 -22.174 1.00 7.51  ? 500  GLY A C     1 
ATOM   3849  O O     . GLY A  1  500 ? 72.266  -10.523 -21.792 1.00 6.53  ? 500  GLY A O     1 
ATOM   3850  N N     . PHE A  1  501 ? 70.394  -11.083 -22.906 1.00 7.52  ? 501  PHE A N     1 
ATOM   3851  C CA    . PHE A  1  501 ? 70.907  -12.388 -23.303 1.00 7.43  ? 501  PHE A CA    1 
ATOM   3852  C C     . PHE A  1  501 ? 72.079  -12.261 -24.283 1.00 7.10  ? 501  PHE A C     1 
ATOM   3853  O O     . PHE A  1  501 ? 73.085  -12.960 -24.151 1.00 8.73  ? 501  PHE A O     1 
ATOM   3854  C CB    . PHE A  1  501 ? 69.789  -13.220 -23.940 1.00 8.95  ? 501  PHE A CB    1 
ATOM   3855  C CG    . PHE A  1  501 ? 70.236  -14.577 -24.409 1.00 8.54  ? 501  PHE A CG    1 
ATOM   3856  C CD1   . PHE A  1  501 ? 70.472  -15.602 -23.498 1.00 9.29  ? 501  PHE A CD1   1 
ATOM   3857  C CD2   . PHE A  1  501 ? 70.446  -14.820 -25.763 1.00 8.03  ? 501  PHE A CD2   1 
ATOM   3858  C CE1   . PHE A  1  501 ? 70.913  -16.852 -23.932 1.00 9.36  ? 501  PHE A CE1   1 
ATOM   3859  C CE2   . PHE A  1  501 ? 70.887  -16.064 -26.208 1.00 8.82  ? 501  PHE A CE2   1 
ATOM   3860  C CZ    . PHE A  1  501 ? 71.120  -17.082 -25.292 1.00 10.21 ? 501  PHE A CZ    1 
ATOM   3861  N N     . TYR A  1  502 ? 71.959  -11.369 -25.262 1.00 7.73  ? 502  TYR A N     1 
ATOM   3862  C CA    . TYR A  1  502 ? 73.030  -11.201 -26.242 1.00 7.60  ? 502  TYR A CA    1 
ATOM   3863  C C     . TYR A  1  502 ? 74.282  -10.571 -25.624 1.00 8.45  ? 502  TYR A C     1 
ATOM   3864  O O     . TYR A  1  502 ? 75.399  -10.876 -26.044 1.00 8.94  ? 502  TYR A O     1 
ATOM   3865  C CB    . TYR A  1  502 ? 72.538  -10.373 -27.436 1.00 7.43  ? 502  TYR A CB    1 
ATOM   3866  C CG    . TYR A  1  502 ? 71.368  -10.994 -28.184 1.00 7.99  ? 502  TYR A CG    1 
ATOM   3867  C CD1   . TYR A  1  502 ? 70.419  -10.191 -28.814 1.00 9.03  ? 502  TYR A CD1   1 
ATOM   3868  C CD2   . TYR A  1  502 ? 71.187  -12.379 -28.227 1.00 8.95  ? 502  TYR A CD2   1 
ATOM   3869  C CE1   . TYR A  1  502 ? 69.312  -10.746 -29.459 1.00 8.77  ? 502  TYR A CE1   1 
ATOM   3870  C CE2   . TYR A  1  502 ? 70.077  -12.946 -28.876 1.00 7.77  ? 502  TYR A CE2   1 
ATOM   3871  C CZ    . TYR A  1  502 ? 69.146  -12.120 -29.483 1.00 9.78  ? 502  TYR A CZ    1 
ATOM   3872  O OH    . TYR A  1  502 ? 68.029  -12.654 -30.087 1.00 9.63  ? 502  TYR A OH    1 
ATOM   3873  N N     . LEU A  1  503 ? 74.102  -9.693  -24.637 1.00 8.13  ? 503  LEU A N     1 
ATOM   3874  C CA    . LEU A  1  503 ? 75.248  -9.072  -23.962 1.00 7.52  ? 503  LEU A CA    1 
ATOM   3875  C C     . LEU A  1  503 ? 75.985  -10.176 -23.206 1.00 8.02  ? 503  LEU A C     1 
ATOM   3876  O O     . LEU A  1  503 ? 77.209  -10.282 -23.266 1.00 7.57  ? 503  LEU A O     1 
ATOM   3877  C CB    . LEU A  1  503 ? 74.781  -7.998  -22.970 1.00 7.69  ? 503  LEU A CB    1 
ATOM   3878  C CG    . LEU A  1  503 ? 74.233  -6.694  -23.561 1.00 8.47  ? 503  LEU A CG    1 
ATOM   3879  C CD1   . LEU A  1  503 ? 73.357  -5.993  -22.536 1.00 9.37  ? 503  LEU A CD1   1 
ATOM   3880  C CD2   . LEU A  1  503 ? 75.387  -5.800  -24.002 1.00 8.15  ? 503  LEU A CD2   1 
ATOM   3881  N N     . MET A  1  504 ? 75.216  -10.998 -22.500 1.00 8.64  ? 504  MET A N     1 
ATOM   3882  C CA    . MET A  1  504 ? 75.760  -12.108 -21.727 1.00 8.32  ? 504  MET A CA    1 
ATOM   3883  C C     . MET A  1  504 ? 76.466  -13.098 -22.650 1.00 8.86  ? 504  MET A C     1 
ATOM   3884  O O     . MET A  1  504 ? 77.573  -13.548 -22.363 1.00 7.82  ? 504  MET A O     1 
ATOM   3885  C CB    . MET A  1  504 ? 74.617  -12.800 -20.970 1.00 8.14  ? 504  MET A CB    1 
ATOM   3886  C CG    . MET A  1  504 ? 75.006  -14.013 -20.127 1.00 10.12 ? 504  MET A CG    1 
ATOM   3887  S SD    . MET A  1  504 ? 75.213  -15.554 -21.047 1.00 9.85  ? 504  MET A SD    1 
ATOM   3888  C CE    . MET A  1  504 ? 73.531  -15.868 -21.608 1.00 11.36 ? 504  MET A CE    1 
ATOM   3889  N N     . LEU A  1  505 ? 75.831  -13.414 -23.775 1.00 7.92  ? 505  LEU A N     1 
ATOM   3890  C CA    . LEU A  1  505 ? 76.391  -14.364 -24.732 1.00 6.99  ? 505  LEU A CA    1 
ATOM   3891  C C     . LEU A  1  505 ? 77.807  -14.007 -25.174 1.00 8.42  ? 505  LEU A C     1 
ATOM   3892  O O     . LEU A  1  505 ? 78.667  -14.883 -25.296 1.00 7.68  ? 505  LEU A O     1 
ATOM   3893  C CB    . LEU A  1  505 ? 75.483  -14.464 -25.965 1.00 7.72  ? 505  LEU A CB    1 
ATOM   3894  C CG    . LEU A  1  505 ? 75.879  -15.511 -27.007 1.00 9.19  ? 505  LEU A CG    1 
ATOM   3895  C CD1   . LEU A  1  505 ? 75.694  -16.901 -26.408 1.00 10.55 ? 505  LEU A CD1   1 
ATOM   3896  C CD2   . LEU A  1  505 ? 75.020  -15.357 -28.263 1.00 11.68 ? 505  LEU A CD2   1 
ATOM   3897  N N     . GLY A  1  506 ? 78.046  -12.721 -25.412 1.00 6.94  ? 506  GLY A N     1 
ATOM   3898  C CA    . GLY A  1  506 ? 79.355  -12.280 -25.854 1.00 6.81  ? 506  GLY A CA    1 
ATOM   3899  C C     . GLY A  1  506 ? 80.458  -12.707 -24.906 1.00 8.30  ? 506  GLY A C     1 
ATOM   3900  O O     . GLY A  1  506 ? 81.420  -13.365 -25.312 1.00 7.85  ? 506  GLY A O     1 
ATOM   3901  N N     . ARG A  1  507 ? 80.327  -12.337 -23.638 1.00 8.09  ? 507  ARG A N     1 
ATOM   3902  C CA    . ARG A  1  507 ? 81.343  -12.706 -22.662 1.00 8.73  ? 507  ARG A CA    1 
ATOM   3903  C C     . ARG A  1  507 ? 81.339  -14.202 -22.371 1.00 10.20 ? 507  ARG A C     1 
ATOM   3904  O O     . ARG A  1  507 ? 82.400  -14.794 -22.184 1.00 9.38  ? 507  ARG A O     1 
ATOM   3905  C CB    . ARG A  1  507 ? 81.159  -11.936 -21.355 1.00 10.12 ? 507  ARG A CB    1 
ATOM   3906  C CG    . ARG A  1  507 ? 82.118  -12.404 -20.260 1.00 10.65 ? 507  ARG A CG    1 
ATOM   3907  C CD    . ARG A  1  507 ? 82.066  -11.492 -19.063 1.00 11.60 ? 507  ARG A CD    1 
ATOM   3908  N NE    . ARG A  1  507 ? 82.842  -11.992 -17.929 1.00 9.79  ? 507  ARG A NE    1 
ATOM   3909  C CZ    . ARG A  1  507 ? 84.165  -11.918 -17.815 1.00 10.65 ? 507  ARG A CZ    1 
ATOM   3910  N NH1   . ARG A  1  507 ? 84.899  -11.362 -18.773 1.00 9.78  ? 507  ARG A NH1   1 
ATOM   3911  N NH2   . ARG A  1  507 ? 84.753  -12.387 -16.720 1.00 10.56 ? 507  ARG A NH2   1 
ATOM   3912  N N     . TYR A  1  508 ? 80.153  -14.805 -22.326 1.00 10.42 ? 508  TYR A N     1 
ATOM   3913  C CA    . TYR A  1  508 ? 80.040  -16.238 -22.063 1.00 9.43  ? 508  TYR A CA    1 
ATOM   3914  C C     . TYR A  1  508 ? 80.929  -17.042 -23.013 1.00 10.46 ? 508  TYR A C     1 
ATOM   3915  O O     . TYR A  1  508 ? 81.733  -17.874 -22.581 1.00 9.62  ? 508  TYR A O     1 
ATOM   3916  C CB    . TYR A  1  508 ? 78.592  -16.705 -22.234 1.00 10.55 ? 508  TYR A CB    1 
ATOM   3917  C CG    . TYR A  1  508 ? 78.411  -18.182 -21.965 1.00 9.36  ? 508  TYR A CG    1 
ATOM   3918  C CD1   . TYR A  1  508 ? 78.171  -18.651 -20.672 1.00 11.26 ? 508  TYR A CD1   1 
ATOM   3919  C CD2   . TYR A  1  508 ? 78.521  -19.115 -22.995 1.00 9.74  ? 508  TYR A CD2   1 
ATOM   3920  C CE1   . TYR A  1  508 ? 78.048  -20.015 -20.412 1.00 13.02 ? 508  TYR A CE1   1 
ATOM   3921  C CE2   . TYR A  1  508 ? 78.399  -20.480 -22.746 1.00 11.22 ? 508  TYR A CE2   1 
ATOM   3922  C CZ    . TYR A  1  508 ? 78.165  -20.922 -21.454 1.00 11.02 ? 508  TYR A CZ    1 
ATOM   3923  O OH    . TYR A  1  508 ? 78.058  -22.273 -21.205 1.00 12.34 ? 508  TYR A OH    1 
ATOM   3924  N N     . VAL A  1  509 ? 80.773  -16.805 -24.312 1.00 8.56  ? 509  VAL A N     1 
ATOM   3925  C CA    . VAL A  1  509 ? 81.576  -17.526 -25.289 1.00 8.61  ? 509  VAL A CA    1 
ATOM   3926  C C     . VAL A  1  509 ? 83.039  -17.131 -25.153 1.00 8.82  ? 509  VAL A C     1 
ATOM   3927  O O     . VAL A  1  509 ? 83.934  -17.949 -25.371 1.00 9.88  ? 509  VAL A O     1 
ATOM   3928  C CB    . VAL A  1  509 ? 81.091  -17.258 -26.726 1.00 8.29  ? 509  VAL A CB    1 
ATOM   3929  C CG1   . VAL A  1  509 ? 81.964  -18.013 -27.718 1.00 8.88  ? 509  VAL A CG1   1 
ATOM   3930  C CG2   . VAL A  1  509 ? 79.639  -17.701 -26.865 1.00 8.28  ? 509  VAL A CG2   1 
ATOM   3931  N N     . GLY A  1  510 ? 83.282  -15.876 -24.789 1.00 8.19  ? 510  GLY A N     1 
ATOM   3932  C CA    . GLY A  1  510 ? 84.647  -15.422 -24.606 1.00 9.68  ? 510  GLY A CA    1 
ATOM   3933  C C     . GLY A  1  510 ? 85.326  -16.248 -23.529 1.00 9.58  ? 510  GLY A C     1 
ATOM   3934  O O     . GLY A  1  510 ? 86.469  -16.675 -23.693 1.00 10.95 ? 510  GLY A O     1 
ATOM   3935  N N     . ILE A  1  511 ? 84.616  -16.477 -22.426 1.00 9.50  ? 511  ILE A N     1 
ATOM   3936  C CA    . ILE A  1  511 ? 85.153  -17.262 -21.319 1.00 8.90  ? 511  ILE A CA    1 
ATOM   3937  C C     . ILE A  1  511 ? 85.356  -18.718 -21.736 1.00 10.57 ? 511  ILE A C     1 
ATOM   3938  O O     . ILE A  1  511 ? 86.330  -19.351 -21.333 1.00 11.53 ? 511  ILE A O     1 
ATOM   3939  C CB    . ILE A  1  511 ? 84.219  -17.218 -20.087 1.00 8.96  ? 511  ILE A CB    1 
ATOM   3940  C CG1   . ILE A  1  511 ? 84.221  -15.813 -19.478 1.00 10.22 ? 511  ILE A CG1   1 
ATOM   3941  C CG2   . ILE A  1  511 ? 84.674  -18.238 -19.050 1.00 11.29 ? 511  ILE A CG2   1 
ATOM   3942  C CD1   . ILE A  1  511 ? 85.585  -15.357 -18.976 1.00 10.86 ? 511  ILE A CD1   1 
ATOM   3943  N N     . LYS A  1  512 ? 84.438  -19.253 -22.537 1.00 10.12 ? 512  LYS A N     1 
ATOM   3944  C CA    . LYS A  1  512 ? 84.573  -20.634 -22.993 1.00 10.16 ? 512  LYS A CA    1 
ATOM   3945  C C     . LYS A  1  512 ? 85.838  -20.773 -23.834 1.00 11.38 ? 512  LYS A C     1 
ATOM   3946  O O     . LYS A  1  512 ? 86.549  -21.776 -23.742 1.00 12.61 ? 512  LYS A O     1 
ATOM   3947  C CB    . LYS A  1  512 ? 83.352  -21.059 -23.816 1.00 12.31 ? 512  LYS A CB    1 
ATOM   3948  C CG    . LYS A  1  512 ? 82.051  -21.086 -23.026 1.00 13.81 ? 512  LYS A CG    1 
ATOM   3949  C CD    . LYS A  1  512 ? 82.094  -22.097 -21.884 1.00 17.85 ? 512  LYS A CD    1 
ATOM   3950  C CE    . LYS A  1  512 ? 82.194  -23.520 -22.402 1.00 19.63 ? 512  LYS A CE    1 
ATOM   3951  N NZ    . LYS A  1  512 ? 82.027  -24.514 -21.302 1.00 22.84 ? 512  LYS A NZ    1 
ATOM   3952  N N     . ILE A  1  513 ? 86.120  -19.763 -24.652 1.00 11.35 ? 513  ILE A N     1 
ATOM   3953  C CA    . ILE A  1  513 ? 87.313  -19.791 -25.493 1.00 10.79 ? 513  ILE A CA    1 
ATOM   3954  C C     . ILE A  1  513 ? 88.571  -19.729 -24.624 1.00 11.82 ? 513  ILE A C     1 
ATOM   3955  O O     . ILE A  1  513 ? 89.538  -20.448 -24.874 1.00 12.13 ? 513  ILE A O     1 
ATOM   3956  C CB    . ILE A  1  513 ? 87.314  -18.618 -26.505 1.00 9.93  ? 513  ILE A CB    1 
ATOM   3957  C CG1   . ILE A  1  513 ? 86.205  -18.827 -27.540 1.00 10.95 ? 513  ILE A CG1   1 
ATOM   3958  C CG2   . ILE A  1  513 ? 88.663  -18.535 -27.212 1.00 9.38  ? 513  ILE A CG2   1 
ATOM   3959  C CD1   . ILE A  1  513 ? 86.004  -17.649 -28.471 1.00 11.14 ? 513  ILE A CD1   1 
ATOM   3960  N N     . LEU A  1  514 ? 88.558  -18.878 -23.602 1.00 11.82 ? 514  LEU A N     1 
ATOM   3961  C CA    . LEU A  1  514 ? 89.709  -18.766 -22.712 1.00 13.37 ? 514  LEU A CA    1 
ATOM   3962  C C     . LEU A  1  514 ? 89.943  -20.068 -21.955 1.00 14.54 ? 514  LEU A C     1 
ATOM   3963  O O     . LEU A  1  514 ? 91.086  -20.480 -21.762 1.00 15.78 ? 514  LEU A O     1 
ATOM   3964  C CB    . LEU A  1  514 ? 89.521  -17.620 -21.712 1.00 13.27 ? 514  LEU A CB    1 
ATOM   3965  C CG    . LEU A  1  514 ? 89.582  -16.208 -22.299 1.00 13.61 ? 514  LEU A CG    1 
ATOM   3966  C CD1   . LEU A  1  514 ? 89.505  -15.184 -21.175 1.00 14.46 ? 514  LEU A CD1   1 
ATOM   3967  C CD2   . LEU A  1  514 ? 90.876  -16.035 -23.088 1.00 13.19 ? 514  LEU A CD2   1 
ATOM   3968  N N     . GLN A  1  515 ? 88.864  -20.719 -21.528 1.00 14.82 ? 515  GLN A N     1 
ATOM   3969  C CA    . GLN A  1  515 ? 89.001  -21.977 -20.800 1.00 16.86 ? 515  GLN A CA    1 
ATOM   3970  C C     . GLN A  1  515 ? 89.580  -23.039 -21.728 1.00 17.39 ? 515  GLN A C     1 
ATOM   3971  O O     . GLN A  1  515 ? 90.367  -23.887 -21.303 1.00 18.03 ? 515  GLN A O     1 
ATOM   3972  C CB    . GLN A  1  515 ? 87.645  -22.431 -20.249 1.00 16.98 ? 515  GLN A CB    1 
ATOM   3973  C CG    . GLN A  1  515 ? 86.991  -21.404 -19.336 1.00 18.03 ? 515  GLN A CG    1 
ATOM   3974  C CD    . GLN A  1  515 ? 85.758  -21.934 -18.624 1.00 19.49 ? 515  GLN A CD    1 
ATOM   3975  O OE1   . GLN A  1  515 ? 85.003  -22.735 -19.173 1.00 20.12 ? 515  GLN A OE1   1 
ATOM   3976  N NE2   . GLN A  1  515 ? 85.540  -21.471 -17.399 1.00 20.86 ? 515  GLN A NE2   1 
ATOM   3977  N N     . GLU A  1  516 ? 89.197  -22.977 -22.998 1.00 16.92 ? 516  GLU A N     1 
ATOM   3978  C CA    . GLU A  1  516 ? 89.685  -23.920 -23.991 1.00 19.13 ? 516  GLU A CA    1 
ATOM   3979  C C     . GLU A  1  516 ? 91.177  -23.696 -24.239 1.00 18.99 ? 516  GLU A C     1 
ATOM   3980  O O     . GLU A  1  516 ? 91.938  -24.657 -24.361 1.00 19.11 ? 516  GLU A O     1 
ATOM   3981  C CB    . GLU A  1  516 ? 88.897  -23.760 -25.295 1.00 20.34 ? 516  GLU A CB    1 
ATOM   3982  C CG    . GLU A  1  516 ? 89.145  -24.858 -26.305 1.00 24.64 ? 516  GLU A CG    1 
ATOM   3983  C CD    . GLU A  1  516 ? 88.189  -24.785 -27.474 1.00 27.34 ? 516  GLU A CD    1 
ATOM   3984  O OE1   . GLU A  1  516 ? 88.292  -23.832 -28.274 1.00 28.48 ? 516  GLU A OE1   1 
ATOM   3985  O OE2   . GLU A  1  516 ? 87.327  -25.679 -27.583 1.00 29.98 ? 516  GLU A OE2   1 
ATOM   3986  N N     . ARG A  1  517 ? 91.593  -22.431 -24.308 1.00 18.00 ? 517  ARG A N     1 
ATOM   3987  C CA    . ARG A  1  517 ? 93.000  -22.098 -24.528 1.00 19.71 ? 517  ARG A CA    1 
ATOM   3988  C C     . ARG A  1  517 ? 93.829  -22.515 -23.314 1.00 21.09 ? 517  ARG A C     1 
ATOM   3989  O O     . ARG A  1  517 ? 94.988  -22.909 -23.450 1.00 22.28 ? 517  ARG A O     1 
ATOM   3990  C CB    . ARG A  1  517 ? 93.175  -20.591 -24.785 1.00 18.30 ? 517  ARG A CB    1 
ATOM   3991  C CG    . ARG A  1  517 ? 92.660  -20.102 -26.145 1.00 17.76 ? 517  ARG A CG    1 
ATOM   3992  C CD    . ARG A  1  517 ? 93.420  -20.721 -27.320 1.00 17.92 ? 517  ARG A CD    1 
ATOM   3993  N NE    . ARG A  1  517 ? 94.845  -20.386 -27.338 1.00 18.09 ? 517  ARG A NE    1 
ATOM   3994  C CZ    . ARG A  1  517 ? 95.371  -19.305 -27.911 1.00 18.59 ? 517  ARG A CZ    1 
ATOM   3995  N NH1   . ARG A  1  517 ? 94.595  -18.422 -28.531 1.00 17.26 ? 517  ARG A NH1   1 
ATOM   3996  N NH2   . ARG A  1  517 ? 96.685  -19.113 -27.875 1.00 16.96 ? 517  ARG A NH2   1 
ATOM   3997  N N     . SER A  1  518 ? 93.230  -22.436 -22.129 1.00 22.06 ? 518  SER A N     1 
ATOM   3998  C CA    . SER A  1  518 ? 93.926  -22.817 -20.903 1.00 24.62 ? 518  SER A CA    1 
ATOM   3999  C C     . SER A  1  518 ? 94.256  -24.300 -20.906 1.00 25.80 ? 518  SER A C     1 
ATOM   4000  O O     . SER A  1  518 ? 95.352  -24.710 -20.512 1.00 26.47 ? 518  SER A O     1 
ATOM   4001  C CB    . SER A  1  518 ? 93.070  -22.499 -19.675 1.00 25.69 ? 518  SER A CB    1 
ATOM   4002  O OG    . SER A  1  518 ? 93.224  -21.147 -19.285 1.00 29.08 ? 518  SER A OG    1 
ATOM   4003  N N     . ALA A  1  519 ? 93.298  -25.098 -21.359 1.00 26.54 ? 519  ALA A N     1 
ATOM   4004  C CA    . ALA A  1  519 ? 93.462  -26.541 -21.402 1.00 28.15 ? 519  ALA A CA    1 
ATOM   4005  C C     . ALA A  1  519 ? 94.471  -27.000 -22.442 1.00 29.92 ? 519  ALA A C     1 
ATOM   4006  O O     . ALA A  1  519 ? 95.097  -28.044 -22.275 1.00 30.11 ? 519  ALA A O     1 
ATOM   4007  C CB    . ALA A  1  519 ? 92.112  -27.209 -21.659 1.00 28.49 ? 519  ALA A CB    1 
ATOM   4008  N N     . SER A  1  520 ? 94.635  -26.220 -23.507 1.00 31.08 ? 520  SER A N     1 
ATOM   4009  C CA    . SER A  1  520 ? 95.558  -26.587 -24.574 1.00 32.79 ? 520  SER A CA    1 
ATOM   4010  C C     . SER A  1  520 ? 96.933  -25.944 -24.469 1.00 33.34 ? 520  SER A C     1 
ATOM   4011  O O     . SER A  1  520 ? 97.767  -26.137 -25.349 1.00 33.99 ? 520  SER A O     1 
ATOM   4012  C CB    . SER A  1  520 ? 94.945  -26.259 -25.944 1.00 32.24 ? 520  SER A CB    1 
ATOM   4013  O OG    . SER A  1  520 ? 94.846  -24.858 -26.138 1.00 32.51 ? 520  SER A OG    1 
ATOM   4014  N N     . ASP A  1  521 ? 97.174  -25.172 -23.412 1.00 34.61 ? 521  ASP A N     1 
ATOM   4015  C CA    . ASP A  1  521 ? 98.481  -24.538 -23.239 1.00 35.80 ? 521  ASP A CA    1 
ATOM   4016  C C     . ASP A  1  521 ? 99.562  -25.593 -23.022 1.00 36.53 ? 521  ASP A C     1 
ATOM   4017  O O     . ASP A  1  521 ? 100.757 -25.226 -22.989 1.00 37.38 ? 521  ASP A O     1 
ATOM   4018  C CB    . ASP A  1  521 ? 98.482  -23.572 -22.047 1.00 35.47 ? 521  ASP A CB    1 
ATOM   4019  C CG    . ASP A  1  521 ? 97.888  -22.224 -22.386 1.00 36.76 ? 521  ASP A CG    1 
ATOM   4020  O OD1   . ASP A  1  521 ? 98.333  -21.619 -23.386 1.00 35.50 ? 521  ASP A OD1   1 
ATOM   4021  O OD2   . ASP A  1  521 ? 96.986  -21.769 -21.651 1.00 36.83 ? 521  ASP A OD2   1 
ATOM   4022  O OXT   . ASP A  1  521 ? 99.201  -26.779 -22.881 1.00 37.08 ? 521  ASP A OXT   1 
ATOM   4023  N N     . LEU B  1  1   ? 49.242  42.137  8.648   1.00 15.05 ? 1    LEU B N     1 
ATOM   4024  C CA    . LEU B  1  1   ? 48.783  43.385  7.974   1.00 14.77 ? 1    LEU B CA    1 
ATOM   4025  C C     . LEU B  1  1   ? 49.818  44.492  8.129   1.00 15.00 ? 1    LEU B C     1 
ATOM   4026  O O     . LEU B  1  1   ? 50.619  44.485  9.068   1.00 16.82 ? 1    LEU B O     1 
ATOM   4027  C CB    . LEU B  1  1   ? 47.444  43.840  8.561   1.00 16.06 ? 1    LEU B CB    1 
ATOM   4028  C CG    . LEU B  1  1   ? 46.311  42.814  8.477   1.00 16.73 ? 1    LEU B CG    1 
ATOM   4029  C CD1   . LEU B  1  1   ? 45.096  43.324  9.234   1.00 19.61 ? 1    LEU B CD1   1 
ATOM   4030  C CD2   . LEU B  1  1   ? 45.967  42.552  7.021   1.00 19.16 ? 1    LEU B CD2   1 
ATOM   4031  N N     . ALA B  1  2   ? 49.793  45.443  7.203   1.00 13.16 ? 2    ALA B N     1 
ATOM   4032  C CA    . ALA B  1  2   ? 50.733  46.554  7.209   1.00 13.57 ? 2    ALA B CA    1 
ATOM   4033  C C     . ALA B  1  2   ? 50.164  47.793  7.883   1.00 13.39 ? 2    ALA B C     1 
ATOM   4034  O O     . ALA B  1  2   ? 48.986  47.842  8.238   1.00 14.20 ? 2    ALA B O     1 
ATOM   4035  C CB    . ALA B  1  2   ? 51.142  46.887  5.779   1.00 13.98 ? 2    ALA B CB    1 
ATOM   4036  N N     . THR B  1  3   ? 51.023  48.793  8.053   1.00 13.48 ? 3    THR B N     1 
ATOM   4037  C CA    . THR B  1  3   ? 50.642  50.055  8.668   1.00 16.32 ? 3    THR B CA    1 
ATOM   4038  C C     . THR B  1  3   ? 50.776  51.158  7.626   1.00 15.58 ? 3    THR B C     1 
ATOM   4039  O O     . THR B  1  3   ? 51.775  51.226  6.910   1.00 15.94 ? 3    THR B O     1 
ATOM   4040  C CB    . THR B  1  3   ? 51.553  50.385  9.865   1.00 18.29 ? 3    THR B CB    1 
ATOM   4041  O OG1   . THR B  1  3   ? 51.472  49.332  10.832  1.00 20.80 ? 3    THR B OG1   1 
ATOM   4042  C CG2   . THR B  1  3   ? 51.129  51.694  10.511  1.00 20.51 ? 3    THR B CG2   1 
ATOM   4043  N N     . THR B  1  4   ? 49.762  52.013  7.542   1.00 16.35 ? 4    THR B N     1 
ATOM   4044  C CA    . THR B  1  4   ? 49.746  53.118  6.588   1.00 15.87 ? 4    THR B CA    1 
ATOM   4045  C C     . THR B  1  4   ? 51.096  53.820  6.445   1.00 15.94 ? 4    THR B C     1 
ATOM   4046  O O     . THR B  1  4   ? 51.734  54.172  7.438   1.00 16.90 ? 4    THR B O     1 
ATOM   4047  C CB    . THR B  1  4   ? 48.680  54.161  6.988   1.00 16.53 ? 4    THR B CB    1 
ATOM   4048  O OG1   . THR B  1  4   ? 47.388  53.544  6.969   1.00 18.72 ? 4    THR B OG1   1 
ATOM   4049  C CG2   . THR B  1  4   ? 48.688  55.340  6.027   1.00 17.81 ? 4    THR B CG2   1 
ATOM   4050  N N     . SER B  1  5   ? 51.518  54.025  5.200   1.00 16.05 ? 5    SER B N     1 
ATOM   4051  C CA    . SER B  1  5   ? 52.787  54.687  4.898   1.00 16.69 ? 5    SER B CA    1 
ATOM   4052  C C     . SER B  1  5   ? 52.812  55.075  3.425   1.00 16.47 ? 5    SER B C     1 
ATOM   4053  O O     . SER B  1  5   ? 51.923  54.694  2.669   1.00 14.21 ? 5    SER B O     1 
ATOM   4054  C CB    . SER B  1  5   ? 53.957  53.743  5.178   1.00 17.48 ? 5    SER B CB    1 
ATOM   4055  O OG    . SER B  1  5   ? 53.969  52.670  4.247   1.00 20.13 ? 5    SER B OG    1 
ATOM   4056  N N     . ASP B  1  6   ? 53.828  55.828  3.015   1.00 16.29 ? 6    ASP B N     1 
ATOM   4057  C CA    . ASP B  1  6   ? 53.931  56.216  1.619   1.00 16.31 ? 6    ASP B CA    1 
ATOM   4058  C C     . ASP B  1  6   ? 54.257  54.986  0.788   1.00 15.19 ? 6    ASP B C     1 
ATOM   4059  O O     . ASP B  1  6   ? 54.773  53.995  1.305   1.00 14.69 ? 6    ASP B O     1 
ATOM   4060  C CB    . ASP B  1  6   ? 55.047  57.247  1.405   1.00 18.80 ? 6    ASP B CB    1 
ATOM   4061  C CG    . ASP B  1  6   ? 54.841  58.519  2.192   1.00 21.63 ? 6    ASP B CG    1 
ATOM   4062  O OD1   . ASP B  1  6   ? 53.686  58.836  2.543   1.00 21.77 ? 6    ASP B OD1   1 
ATOM   4063  O OD2   . ASP B  1  6   ? 55.851  59.216  2.429   1.00 23.84 ? 6    ASP B OD2   1 
ATOM   4064  N N     . HIS B  1  7   ? 53.948  55.051  -0.500  1.00 14.98 ? 7    HIS B N     1 
ATOM   4065  C CA    . HIS B  1  7   ? 54.256  53.950  -1.398  1.00 15.14 ? 7    HIS B CA    1 
ATOM   4066  C C     . HIS B  1  7   ? 55.784  53.850  -1.365  1.00 15.05 ? 7    HIS B C     1 
ATOM   4067  O O     . HIS B  1  7   ? 56.477  54.845  -1.582  1.00 15.30 ? 7    HIS B O     1 
ATOM   4068  C CB    . HIS B  1  7   ? 53.779  54.275  -2.812  1.00 13.89 ? 7    HIS B CB    1 
ATOM   4069  C CG    . HIS B  1  7   ? 53.842  53.110  -3.750  1.00 14.32 ? 7    HIS B CG    1 
ATOM   4070  N ND1   . HIS B  1  7   ? 52.783  52.249  -3.940  1.00 14.07 ? 7    HIS B ND1   1 
ATOM   4071  C CD2   . HIS B  1  7   ? 54.835  52.669  -4.558  1.00 14.33 ? 7    HIS B CD2   1 
ATOM   4072  C CE1   . HIS B  1  7   ? 53.118  51.331  -4.829  1.00 14.16 ? 7    HIS B CE1   1 
ATOM   4073  N NE2   . HIS B  1  7   ? 54.358  51.564  -5.220  1.00 14.99 ? 7    HIS B NE2   1 
ATOM   4074  N N     . ASP B  1  8   ? 56.302  52.656  -1.091  1.00 14.90 ? 8    ASP B N     1 
ATOM   4075  C CA    . ASP B  1  8   ? 57.746  52.435  -0.989  1.00 15.66 ? 8    ASP B CA    1 
ATOM   4076  C C     . ASP B  1  8   ? 58.448  52.241  -2.333  1.00 15.37 ? 8    ASP B C     1 
ATOM   4077  O O     . ASP B  1  8   ? 58.375  51.167  -2.929  1.00 14.88 ? 8    ASP B O     1 
ATOM   4078  C CB    . ASP B  1  8   ? 58.012  51.218  -0.099  1.00 15.93 ? 8    ASP B CB    1 
ATOM   4079  C CG    . ASP B  1  8   ? 59.469  51.095  0.314   1.00 16.15 ? 8    ASP B CG    1 
ATOM   4080  O OD1   . ASP B  1  8   ? 60.329  51.765  -0.298  1.00 16.97 ? 8    ASP B OD1   1 
ATOM   4081  O OD2   . ASP B  1  8   ? 59.751  50.316  1.250   1.00 15.31 ? 8    ASP B OD2   1 
ATOM   4082  N N     . PHE B  1  9   ? 59.145  53.277  -2.797  1.00 13.85 ? 9    PHE B N     1 
ATOM   4083  C CA    . PHE B  1  9   ? 59.867  53.209  -4.066  1.00 13.93 ? 9    PHE B CA    1 
ATOM   4084  C C     . PHE B  1  9   ? 61.371  52.995  -3.874  1.00 13.59 ? 9    PHE B C     1 
ATOM   4085  O O     . PHE B  1  9   ? 62.173  53.411  -4.714  1.00 13.30 ? 9    PHE B O     1 
ATOM   4086  C CB    . PHE B  1  9   ? 59.647  54.489  -4.882  1.00 14.03 ? 9    PHE B CB    1 
ATOM   4087  C CG    . PHE B  1  9   ? 58.291  54.584  -5.527  1.00 15.01 ? 9    PHE B CG    1 
ATOM   4088  C CD1   . PHE B  1  9   ? 57.378  55.555  -5.124  1.00 15.62 ? 9    PHE B CD1   1 
ATOM   4089  C CD2   . PHE B  1  9   ? 57.937  53.722  -6.563  1.00 14.97 ? 9    PHE B CD2   1 
ATOM   4090  C CE1   . PHE B  1  9   ? 56.133  55.669  -5.748  1.00 15.44 ? 9    PHE B CE1   1 
ATOM   4091  C CE2   . PHE B  1  9   ? 56.696  53.827  -7.191  1.00 13.45 ? 9    PHE B CE2   1 
ATOM   4092  C CZ    . PHE B  1  9   ? 55.793  54.804  -6.782  1.00 16.10 ? 9    PHE B CZ    1 
ATOM   4093  N N     . SER B  1  10  ? 61.756  52.347  -2.780  1.00 14.14 ? 10   SER B N     1 
ATOM   4094  C CA    . SER B  1  10  ? 63.173  52.099  -2.520  1.00 14.76 ? 10   SER B CA    1 
ATOM   4095  C C     . SER B  1  10  ? 63.806  51.284  -3.646  1.00 15.33 ? 10   SER B C     1 
ATOM   4096  O O     . SER B  1  10  ? 64.988  51.444  -3.953  1.00 15.10 ? 10   SER B O     1 
ATOM   4097  C CB    . SER B  1  10  ? 63.354  51.357  -1.191  1.00 14.76 ? 10   SER B CB    1 
ATOM   4098  O OG    . SER B  1  10  ? 62.924  52.147  -0.096  1.00 15.97 ? 10   SER B OG    1 
ATOM   4099  N N     . TYR B  1  11  ? 63.008  50.423  -4.271  1.00 13.74 ? 11   TYR B N     1 
ATOM   4100  C CA    . TYR B  1  11  ? 63.491  49.569  -5.351  1.00 13.94 ? 11   TYR B CA    1 
ATOM   4101  C C     . TYR B  1  11  ? 63.957  50.320  -6.597  1.00 13.03 ? 11   TYR B C     1 
ATOM   4102  O O     . TYR B  1  11  ? 64.570  49.730  -7.488  1.00 14.55 ? 11   TYR B O     1 
ATOM   4103  C CB    . TYR B  1  11  ? 62.405  48.556  -5.738  1.00 12.16 ? 11   TYR B CB    1 
ATOM   4104  C CG    . TYR B  1  11  ? 61.188  49.162  -6.404  1.00 11.76 ? 11   TYR B CG    1 
ATOM   4105  C CD1   . TYR B  1  11  ? 61.217  49.535  -7.747  1.00 11.32 ? 11   TYR B CD1   1 
ATOM   4106  C CD2   . TYR B  1  11  ? 60.006  49.360  -5.690  1.00 12.11 ? 11   TYR B CD2   1 
ATOM   4107  C CE1   . TYR B  1  11  ? 60.095  50.088  -8.369  1.00 13.05 ? 11   TYR B CE1   1 
ATOM   4108  C CE2   . TYR B  1  11  ? 58.878  49.914  -6.300  1.00 11.94 ? 11   TYR B CE2   1 
ATOM   4109  C CZ    . TYR B  1  11  ? 58.931  50.274  -7.638  1.00 11.93 ? 11   TYR B CZ    1 
ATOM   4110  O OH    . TYR B  1  11  ? 57.823  50.812  -8.247  1.00 13.19 ? 11   TYR B OH    1 
ATOM   4111  N N     . LEU B  1  12  ? 63.664  51.614  -6.674  1.00 13.64 ? 12   LEU B N     1 
ATOM   4112  C CA    . LEU B  1  12  ? 64.079  52.391  -7.834  1.00 14.71 ? 12   LEU B CA    1 
ATOM   4113  C C     . LEU B  1  12  ? 65.598  52.380  -7.981  1.00 14.51 ? 12   LEU B C     1 
ATOM   4114  O O     . LEU B  1  12  ? 66.125  52.652  -9.062  1.00 15.12 ? 12   LEU B O     1 
ATOM   4115  C CB    . LEU B  1  12  ? 63.575  53.833  -7.725  1.00 16.19 ? 12   LEU B CB    1 
ATOM   4116  C CG    . LEU B  1  12  ? 62.058  54.006  -7.859  1.00 16.12 ? 12   LEU B CG    1 
ATOM   4117  C CD1   . LEU B  1  12  ? 61.688  55.478  -7.757  1.00 15.82 ? 12   LEU B CD1   1 
ATOM   4118  C CD2   . LEU B  1  12  ? 61.601  53.434  -9.195  1.00 17.01 ? 12   LEU B CD2   1 
ATOM   4119  N N     . SER B  1  13  ? 66.295  52.057  -6.895  1.00 13.94 ? 13   SER B N     1 
ATOM   4120  C CA    . SER B  1  13  ? 67.754  52.010  -6.908  1.00 16.20 ? 13   SER B CA    1 
ATOM   4121  C C     . SER B  1  13  ? 68.267  50.962  -7.890  1.00 15.88 ? 13   SER B C     1 
ATOM   4122  O O     . SER B  1  13  ? 69.385  51.073  -8.401  1.00 15.52 ? 13   SER B O     1 
ATOM   4123  C CB    . SER B  1  13  ? 68.293  51.713  -5.504  1.00 14.65 ? 13   SER B CB    1 
ATOM   4124  O OG    . SER B  1  13  ? 67.931  50.412  -5.075  1.00 17.23 ? 13   SER B OG    1 
ATOM   4125  N N     . PHE B  1  14  ? 67.460  49.937  -8.151  1.00 15.34 ? 14   PHE B N     1 
ATOM   4126  C CA    . PHE B  1  14  ? 67.866  48.901  -9.089  1.00 15.07 ? 14   PHE B CA    1 
ATOM   4127  C C     . PHE B  1  14  ? 66.910  48.745  -10.268 1.00 15.00 ? 14   PHE B C     1 
ATOM   4128  O O     . PHE B  1  14  ? 66.828  47.682  -10.880 1.00 15.47 ? 14   PHE B O     1 
ATOM   4129  C CB    . PHE B  1  14  ? 68.080  47.556  -8.368  1.00 15.08 ? 14   PHE B CB    1 
ATOM   4130  C CG    . PHE B  1  14  ? 66.919  47.103  -7.516  1.00 15.20 ? 14   PHE B CG    1 
ATOM   4131  C CD1   . PHE B  1  14  ? 65.766  46.584  -8.096  1.00 15.32 ? 14   PHE B CD1   1 
ATOM   4132  C CD2   . PHE B  1  14  ? 67.004  47.147  -6.126  1.00 15.24 ? 14   PHE B CD2   1 
ATOM   4133  C CE1   . PHE B  1  14  ? 64.714  46.112  -7.303  1.00 15.55 ? 14   PHE B CE1   1 
ATOM   4134  C CE2   . PHE B  1  14  ? 65.959  46.678  -5.321  1.00 16.16 ? 14   PHE B CE2   1 
ATOM   4135  C CZ    . PHE B  1  14  ? 64.813  46.158  -5.912  1.00 15.63 ? 14   PHE B CZ    1 
ATOM   4136  N N     . ALA B  1  15  ? 66.194  49.818  -10.588 1.00 15.68 ? 15   ALA B N     1 
ATOM   4137  C CA    . ALA B  1  15  ? 65.268  49.813  -11.717 1.00 17.84 ? 15   ALA B CA    1 
ATOM   4138  C C     . ALA B  1  15  ? 65.922  50.591  -12.856 1.00 19.54 ? 15   ALA B C     1 
ATOM   4139  O O     . ALA B  1  15  ? 66.455  51.680  -12.644 1.00 20.61 ? 15   ALA B O     1 
ATOM   4140  C CB    . ALA B  1  15  ? 63.950  50.466  -11.325 1.00 16.52 ? 15   ALA B CB    1 
ATOM   4141  N N     . TYR B  1  16  ? 65.884  50.031  -14.061 1.00 19.84 ? 16   TYR B N     1 
ATOM   4142  C CA    . TYR B  1  16  ? 66.493  50.684  -15.214 1.00 20.87 ? 16   TYR B CA    1 
ATOM   4143  C C     . TYR B  1  16  ? 65.586  50.650  -16.429 1.00 20.94 ? 16   TYR B C     1 
ATOM   4144  O O     . TYR B  1  16  ? 64.751  49.756  -16.571 1.00 20.27 ? 16   TYR B O     1 
ATOM   4145  C CB    . TYR B  1  16  ? 67.803  49.992  -15.595 1.00 21.96 ? 16   TYR B CB    1 
ATOM   4146  C CG    . TYR B  1  16  ? 68.790  49.815  -14.468 1.00 24.47 ? 16   TYR B CG    1 
ATOM   4147  C CD1   . TYR B  1  16  ? 68.603  48.832  -13.496 1.00 23.80 ? 16   TYR B CD1   1 
ATOM   4148  C CD2   . TYR B  1  16  ? 69.920  50.629  -14.375 1.00 25.65 ? 16   TYR B CD2   1 
ATOM   4149  C CE1   . TYR B  1  16  ? 69.518  48.661  -12.460 1.00 25.59 ? 16   TYR B CE1   1 
ATOM   4150  C CE2   . TYR B  1  16  ? 70.840  50.468  -13.344 1.00 26.53 ? 16   TYR B CE2   1 
ATOM   4151  C CZ    . TYR B  1  16  ? 70.633  49.484  -12.390 1.00 27.69 ? 16   TYR B CZ    1 
ATOM   4152  O OH    . TYR B  1  16  ? 71.537  49.328  -11.365 1.00 28.80 ? 16   TYR B OH    1 
ATOM   4153  N N     . ASP B  1  17  ? 65.752  51.629  -17.310 1.00 21.25 ? 17   ASP B N     1 
ATOM   4154  C CA    . ASP B  1  17  ? 64.973  51.653  -18.537 1.00 21.54 ? 17   ASP B CA    1 
ATOM   4155  C C     . ASP B  1  17  ? 65.716  50.669  -19.427 1.00 21.95 ? 17   ASP B C     1 
ATOM   4156  O O     . ASP B  1  17  ? 66.942  50.586  -19.374 1.00 22.42 ? 17   ASP B O     1 
ATOM   4157  C CB    . ASP B  1  17  ? 64.972  53.048  -19.167 1.00 21.89 ? 17   ASP B CB    1 
ATOM   4158  C CG    . ASP B  1  17  ? 64.104  53.122  -20.413 1.00 20.80 ? 17   ASP B CG    1 
ATOM   4159  O OD1   . ASP B  1  17  ? 64.491  52.545  -21.452 1.00 21.32 ? 17   ASP B OD1   1 
ATOM   4160  O OD2   . ASP B  1  17  ? 63.029  53.751  -20.351 1.00 21.39 ? 17   ASP B OD2   1 
ATOM   4161  N N     . ALA B  1  18  ? 64.984  49.911  -20.232 1.00 21.40 ? 18   ALA B N     1 
ATOM   4162  C CA    . ALA B  1  18  ? 65.607  48.919  -21.096 1.00 22.06 ? 18   ALA B CA    1 
ATOM   4163  C C     . ALA B  1  18  ? 66.736  49.482  -21.958 1.00 22.33 ? 18   ALA B C     1 
ATOM   4164  O O     . ALA B  1  18  ? 67.669  48.761  -22.311 1.00 22.59 ? 18   ALA B O     1 
ATOM   4165  C CB    . ALA B  1  18  ? 64.546  48.257  -21.972 1.00 20.95 ? 18   ALA B CB    1 
ATOM   4166  N N     . THR B  1  19  ? 66.661  50.766  -22.296 1.00 23.37 ? 19   THR B N     1 
ATOM   4167  C CA    . THR B  1  19  ? 67.700  51.380  -23.119 1.00 24.26 ? 19   THR B CA    1 
ATOM   4168  C C     . THR B  1  19  ? 69.023  51.475  -22.368 1.00 25.16 ? 19   THR B C     1 
ATOM   4169  O O     . THR B  1  19  ? 70.081  51.591  -22.979 1.00 26.19 ? 19   THR B O     1 
ATOM   4170  C CB    . THR B  1  19  ? 67.311  52.797  -23.578 1.00 24.05 ? 19   THR B CB    1 
ATOM   4171  O OG1   . THR B  1  19  ? 67.088  53.626  -22.433 1.00 24.80 ? 19   THR B OG1   1 
ATOM   4172  C CG2   . THR B  1  19  ? 66.061  52.764  -24.437 1.00 22.38 ? 19   THR B CG2   1 
ATOM   4173  N N     . ASP B  1  20  ? 68.958  51.424  -21.041 1.00 25.56 ? 20   ASP B N     1 
ATOM   4174  C CA    . ASP B  1  20  ? 70.159  51.503  -20.219 1.00 26.16 ? 20   ASP B CA    1 
ATOM   4175  C C     . ASP B  1  20  ? 70.654  50.143  -19.746 1.00 26.01 ? 20   ASP B C     1 
ATOM   4176  O O     . ASP B  1  20  ? 71.630  50.054  -19.006 1.00 26.92 ? 20   ASP B O     1 
ATOM   4177  C CB    . ASP B  1  20  ? 69.937  52.432  -19.016 1.00 27.28 ? 20   ASP B CB    1 
ATOM   4178  C CG    . ASP B  1  20  ? 69.674  53.868  -19.434 1.00 29.31 ? 20   ASP B CG    1 
ATOM   4179  O OD1   . ASP B  1  20  ? 70.447  54.387  -20.267 1.00 30.40 ? 20   ASP B OD1   1 
ATOM   4180  O OD2   . ASP B  1  20  ? 68.704  54.476  -18.935 1.00 29.21 ? 20   ASP B OD2   1 
ATOM   4181  N N     . LEU B  1  21  ? 69.977  49.086  -20.181 1.00 25.13 ? 21   LEU B N     1 
ATOM   4182  C CA    . LEU B  1  21  ? 70.375  47.732  -19.825 1.00 24.33 ? 21   LEU B CA    1 
ATOM   4183  C C     . LEU B  1  21  ? 71.369  47.242  -20.859 1.00 24.35 ? 21   LEU B C     1 
ATOM   4184  O O     . LEU B  1  21  ? 71.381  47.723  -21.990 1.00 25.13 ? 21   LEU B O     1 
ATOM   4185  C CB    . LEU B  1  21  ? 69.159  46.797  -19.787 1.00 24.13 ? 21   LEU B CB    1 
ATOM   4186  C CG    . LEU B  1  21  ? 68.220  46.916  -18.583 1.00 24.27 ? 21   LEU B CG    1 
ATOM   4187  C CD1   . LEU B  1  21  ? 67.098  45.902  -18.719 1.00 23.74 ? 21   LEU B CD1   1 
ATOM   4188  C CD2   . LEU B  1  21  ? 68.996  46.668  -17.296 1.00 23.55 ? 21   LEU B CD2   1 
ATOM   4189  N N     . GLU B  1  22  ? 72.199  46.281  -20.472 1.00 25.17 ? 22   GLU B N     1 
ATOM   4190  C CA    . GLU B  1  22  ? 73.193  45.736  -21.385 1.00 25.44 ? 22   GLU B CA    1 
ATOM   4191  C C     . GLU B  1  22  ? 72.509  45.041  -22.571 1.00 25.96 ? 22   GLU B C     1 
ATOM   4192  O O     . GLU B  1  22  ? 71.385  44.548  -22.445 1.00 25.60 ? 22   GLU B O     1 
ATOM   4193  C CB    . GLU B  1  22  ? 74.110  44.750  -20.644 1.00 25.72 ? 22   GLU B CB    1 
ATOM   4194  C CG    . GLU B  1  22  ? 73.451  43.454  -20.169 1.00 25.19 ? 22   GLU B CG    1 
ATOM   4195  C CD    . GLU B  1  22  ? 72.459  43.650  -19.029 1.00 25.37 ? 22   GLU B CD    1 
ATOM   4196  O OE1   . GLU B  1  22  ? 72.645  44.582  -18.219 1.00 23.28 ? 22   GLU B OE1   1 
ATOM   4197  O OE2   . GLU B  1  22  ? 71.496  42.856  -18.932 1.00 22.33 ? 22   GLU B OE2   1 
ATOM   4198  N N     . LEU B  1  23  ? 73.174  45.023  -23.726 1.00 25.82 ? 23   LEU B N     1 
ATOM   4199  C CA    . LEU B  1  23  ? 72.617  44.380  -24.919 1.00 26.87 ? 23   LEU B CA    1 
ATOM   4200  C C     . LEU B  1  23  ? 72.583  42.869  -24.758 1.00 26.83 ? 23   LEU B C     1 
ATOM   4201  O O     . LEU B  1  23  ? 71.739  42.190  -25.345 1.00 27.59 ? 23   LEU B O     1 
ATOM   4202  C CB    . LEU B  1  23  ? 73.438  44.719  -26.169 1.00 28.43 ? 23   LEU B CB    1 
ATOM   4203  C CG    . LEU B  1  23  ? 73.539  46.167  -26.664 1.00 29.68 ? 23   LEU B CG    1 
ATOM   4204  C CD1   . LEU B  1  23  ? 74.250  46.156  -28.016 1.00 30.38 ? 23   LEU B CD1   1 
ATOM   4205  C CD2   . LEU B  1  23  ? 72.153  46.807  -26.787 1.00 28.17 ? 23   LEU B CD2   1 
ATOM   4206  N N     . GLU B  1  24  ? 73.523  42.339  -23.983 1.00 26.63 ? 24   GLU B N     1 
ATOM   4207  C CA    . GLU B  1  24  ? 73.588  40.901  -23.737 1.00 26.88 ? 24   GLU B CA    1 
ATOM   4208  C C     . GLU B  1  24  ? 73.951  40.655  -22.278 1.00 25.71 ? 24   GLU B C     1 
ATOM   4209  O O     . GLU B  1  24  ? 75.047  40.981  -21.835 1.00 25.28 ? 24   GLU B O     1 
ATOM   4210  C CB    . GLU B  1  24  ? 74.632  40.233  -24.637 1.00 29.31 ? 24   GLU B CB    1 
ATOM   4211  C CG    . GLU B  1  24  ? 74.611  38.713  -24.542 1.00 34.09 ? 24   GLU B CG    1 
ATOM   4212  C CD    . GLU B  1  24  ? 75.455  38.039  -25.605 1.00 36.68 ? 24   GLU B CD    1 
ATOM   4213  O OE1   . GLU B  1  24  ? 75.476  38.542  -26.750 1.00 39.07 ? 24   GLU B OE1   1 
ATOM   4214  O OE2   . GLU B  1  24  ? 76.081  36.998  -25.295 1.00 38.20 ? 24   GLU B OE2   1 
ATOM   4215  N N     . GLY B  1  25  ? 73.024  40.067  -21.534 1.00 24.16 ? 25   GLY B N     1 
ATOM   4216  C CA    . GLY B  1  25  ? 73.260  39.816  -20.125 1.00 22.52 ? 25   GLY B CA    1 
ATOM   4217  C C     . GLY B  1  25  ? 73.063  38.384  -19.703 1.00 19.94 ? 25   GLY B C     1 
ATOM   4218  O O     . GLY B  1  25  ? 72.409  37.612  -20.394 1.00 19.65 ? 25   GLY B O     1 
ATOM   4219  N N     . SER B  1  26  ? 73.631  38.041  -18.553 1.00 18.33 ? 26   SER B N     1 
ATOM   4220  C CA    . SER B  1  26  ? 73.554  36.695  -18.002 1.00 16.07 ? 26   SER B CA    1 
ATOM   4221  C C     . SER B  1  26  ? 73.032  36.766  -16.570 1.00 15.73 ? 26   SER B C     1 
ATOM   4222  O O     . SER B  1  26  ? 73.519  37.561  -15.771 1.00 16.24 ? 26   SER B O     1 
ATOM   4223  C CB    . SER B  1  26  ? 74.949  36.067  -18.004 1.00 17.65 ? 26   SER B CB    1 
ATOM   4224  O OG    . SER B  1  26  ? 74.933  34.768  -17.451 1.00 16.62 ? 26   SER B OG    1 
ATOM   4225  N N     . TYR B  1  27  ? 72.042  35.938  -16.248 1.00 14.30 ? 27   TYR B N     1 
ATOM   4226  C CA    . TYR B  1  27  ? 71.451  35.910  -14.908 1.00 12.98 ? 27   TYR B CA    1 
ATOM   4227  C C     . TYR B  1  27  ? 71.091  34.483  -14.522 1.00 12.55 ? 27   TYR B C     1 
ATOM   4228  O O     . TYR B  1  27  ? 71.177  33.577  -15.342 1.00 12.92 ? 27   TYR B O     1 
ATOM   4229  C CB    . TYR B  1  27  ? 70.168  36.755  -14.863 1.00 12.35 ? 27   TYR B CB    1 
ATOM   4230  C CG    . TYR B  1  27  ? 70.340  38.194  -15.286 1.00 14.02 ? 27   TYR B CG    1 
ATOM   4231  C CD1   . TYR B  1  27  ? 70.404  38.545  -16.636 1.00 12.64 ? 27   TYR B CD1   1 
ATOM   4232  C CD2   . TYR B  1  27  ? 70.472  39.203  -14.336 1.00 12.15 ? 27   TYR B CD2   1 
ATOM   4233  C CE1   . TYR B  1  27  ? 70.599  39.868  -17.024 1.00 12.74 ? 27   TYR B CE1   1 
ATOM   4234  C CE2   . TYR B  1  27  ? 70.668  40.525  -14.712 1.00 13.64 ? 27   TYR B CE2   1 
ATOM   4235  C CZ    . TYR B  1  27  ? 70.732  40.851  -16.058 1.00 13.36 ? 27   TYR B CZ    1 
ATOM   4236  O OH    . TYR B  1  27  ? 70.939  42.159  -16.431 1.00 16.33 ? 27   TYR B OH    1 
ATOM   4237  N N     . ASP B  1  28  ? 70.685  34.285  -13.271 1.00 11.94 ? 28   ASP B N     1 
ATOM   4238  C CA    . ASP B  1  28  ? 70.268  32.962  -12.822 1.00 11.49 ? 28   ASP B CA    1 
ATOM   4239  C C     . ASP B  1  28  ? 68.805  32.764  -13.227 1.00 11.41 ? 28   ASP B C     1 
ATOM   4240  O O     . ASP B  1  28  ? 68.412  31.683  -13.670 1.00 11.25 ? 28   ASP B O     1 
ATOM   4241  C CB    . ASP B  1  28  ? 70.405  32.829  -11.306 1.00 13.27 ? 28   ASP B CB    1 
ATOM   4242  C CG    . ASP B  1  28  ? 71.849  32.709  -10.861 1.00 14.05 ? 28   ASP B CG    1 
ATOM   4243  O OD1   . ASP B  1  28  ? 72.527  31.761  -11.311 1.00 14.36 ? 28   ASP B OD1   1 
ATOM   4244  O OD2   . ASP B  1  28  ? 72.307  33.556  -10.065 1.00 14.08 ? 28   ASP B OD2   1 
ATOM   4245  N N     . TYR B  1  29  ? 68.003  33.814  -13.068 1.00 10.25 ? 29   TYR B N     1 
ATOM   4246  C CA    . TYR B  1  29  ? 66.590  33.755  -13.433 1.00 9.69  ? 29   TYR B CA    1 
ATOM   4247  C C     . TYR B  1  29  ? 66.155  35.016  -14.159 1.00 9.97  ? 29   TYR B C     1 
ATOM   4248  O O     . TYR B  1  29  ? 66.570  36.123  -13.816 1.00 10.80 ? 29   TYR B O     1 
ATOM   4249  C CB    . TYR B  1  29  ? 65.698  33.573  -12.195 1.00 10.83 ? 29   TYR B CB    1 
ATOM   4250  C CG    . TYR B  1  29  ? 65.937  32.283  -11.455 1.00 10.49 ? 29   TYR B CG    1 
ATOM   4251  C CD1   . TYR B  1  29  ? 66.910  32.201  -10.460 1.00 10.30 ? 29   TYR B CD1   1 
ATOM   4252  C CD2   . TYR B  1  29  ? 65.240  31.126  -11.794 1.00 11.33 ? 29   TYR B CD2   1 
ATOM   4253  C CE1   . TYR B  1  29  ? 67.188  30.998  -9.828  1.00 11.69 ? 29   TYR B CE1   1 
ATOM   4254  C CE2   . TYR B  1  29  ? 65.510  29.912  -11.165 1.00 11.02 ? 29   TYR B CE2   1 
ATOM   4255  C CZ    . TYR B  1  29  ? 66.490  29.857  -10.184 1.00 11.01 ? 29   TYR B CZ    1 
ATOM   4256  O OH    . TYR B  1  29  ? 66.786  28.661  -9.575  1.00 14.07 ? 29   TYR B OH    1 
ATOM   4257  N N     . VAL B  1  30  ? 65.330  34.833  -15.182 1.00 9.91  ? 30   VAL B N     1 
ATOM   4258  C CA    . VAL B  1  30  ? 64.793  35.947  -15.948 1.00 10.66 ? 30   VAL B CA    1 
ATOM   4259  C C     . VAL B  1  30  ? 63.282  35.814  -15.845 1.00 10.78 ? 30   VAL B C     1 
ATOM   4260  O O     . VAL B  1  30  ? 62.719  34.775  -16.197 1.00 11.57 ? 30   VAL B O     1 
ATOM   4261  C CB    . VAL B  1  30  ? 65.218  35.888  -17.433 1.00 10.55 ? 30   VAL B CB    1 
ATOM   4262  C CG1   . VAL B  1  30  ? 64.496  36.975  -18.224 1.00 12.36 ? 30   VAL B CG1   1 
ATOM   4263  C CG2   . VAL B  1  30  ? 66.727  36.074  -17.547 1.00 12.13 ? 30   VAL B CG2   1 
ATOM   4264  N N     . ILE B  1  31  ? 62.633  36.850  -15.326 1.00 10.83 ? 31   ILE B N     1 
ATOM   4265  C CA    . ILE B  1  31  ? 61.184  36.837  -15.166 1.00 11.00 ? 31   ILE B CA    1 
ATOM   4266  C C     . ILE B  1  31  ? 60.546  37.798  -16.160 1.00 10.44 ? 31   ILE B C     1 
ATOM   4267  O O     . ILE B  1  31  ? 60.882  38.983  -16.198 1.00 11.13 ? 31   ILE B O     1 
ATOM   4268  C CB    . ILE B  1  31  ? 60.772  37.246  -13.723 1.00 12.93 ? 31   ILE B CB    1 
ATOM   4269  C CG1   . ILE B  1  31  ? 61.269  36.205  -12.712 1.00 15.43 ? 31   ILE B CG1   1 
ATOM   4270  C CG2   . ILE B  1  31  ? 59.258  37.359  -13.620 1.00 12.68 ? 31   ILE B CG2   1 
ATOM   4271  C CD1   . ILE B  1  31  ? 62.767  36.136  -12.566 1.00 21.29 ? 31   ILE B CD1   1 
ATOM   4272  N N     . VAL B  1  32  ? 59.632  37.278  -16.973 1.00 9.06  ? 32   VAL B N     1 
ATOM   4273  C CA    . VAL B  1  32  ? 58.945  38.094  -17.967 1.00 9.01  ? 32   VAL B CA    1 
ATOM   4274  C C     . VAL B  1  32  ? 57.643  38.625  -17.391 1.00 8.60  ? 32   VAL B C     1 
ATOM   4275  O O     . VAL B  1  32  ? 56.717  37.858  -17.117 1.00 9.73  ? 32   VAL B O     1 
ATOM   4276  C CB    . VAL B  1  32  ? 58.631  37.282  -19.243 1.00 8.07  ? 32   VAL B CB    1 
ATOM   4277  C CG1   . VAL B  1  32  ? 57.881  38.149  -20.244 1.00 11.09 ? 32   VAL B CG1   1 
ATOM   4278  C CG2   . VAL B  1  32  ? 59.923  36.768  -19.859 1.00 11.05 ? 32   VAL B CG2   1 
ATOM   4279  N N     . GLY B  1  33  ? 57.584  39.943  -17.214 1.00 8.75  ? 33   GLY B N     1 
ATOM   4280  C CA    . GLY B  1  33  ? 56.398  40.572  -16.663 1.00 9.80  ? 33   GLY B CA    1 
ATOM   4281  C C     . GLY B  1  33  ? 56.552  40.893  -15.187 1.00 8.69  ? 33   GLY B C     1 
ATOM   4282  O O     . GLY B  1  33  ? 56.538  39.992  -14.351 1.00 8.69  ? 33   GLY B O     1 
ATOM   4283  N N     . GLY B  1  34  ? 56.707  42.174  -14.865 1.00 7.67  ? 34   GLY B N     1 
ATOM   4284  C CA    . GLY B  1  34  ? 56.852  42.578  -13.477 1.00 7.78  ? 34   GLY B CA    1 
ATOM   4285  C C     . GLY B  1  34  ? 55.483  42.899  -12.913 1.00 9.11  ? 34   GLY B C     1 
ATOM   4286  O O     . GLY B  1  34  ? 55.211  44.028  -12.494 1.00 9.42  ? 34   GLY B O     1 
ATOM   4287  N N     . GLY B  1  35  ? 54.617  41.892  -12.904 1.00 8.16  ? 35   GLY B N     1 
ATOM   4288  C CA    . GLY B  1  35  ? 53.264  42.089  -12.425 1.00 8.25  ? 35   GLY B CA    1 
ATOM   4289  C C     . GLY B  1  35  ? 52.959  41.589  -11.030 1.00 9.05  ? 35   GLY B C     1 
ATOM   4290  O O     . GLY B  1  35  ? 53.838  41.494  -10.169 1.00 8.79  ? 35   GLY B O     1 
ATOM   4291  N N     . THR B  1  36  ? 51.689  41.263  -10.820 1.00 7.27  ? 36   THR B N     1 
ATOM   4292  C CA    . THR B  1  36  ? 51.195  40.787  -9.536  1.00 7.62  ? 36   THR B CA    1 
ATOM   4293  C C     . THR B  1  36  ? 51.971  39.579  -9.016  1.00 7.83  ? 36   THR B C     1 
ATOM   4294  O O     . THR B  1  36  ? 52.443  39.593  -7.879  1.00 8.56  ? 36   THR B O     1 
ATOM   4295  C CB    . THR B  1  36  ? 49.699  40.466  -9.644  1.00 6.21  ? 36   THR B CB    1 
ATOM   4296  O OG1   . THR B  1  36  ? 49.027  41.600  -10.210 1.00 7.92  ? 36   THR B OG1   1 
ATOM   4297  C CG2   . THR B  1  36  ? 49.100  40.181  -8.269  1.00 8.34  ? 36   THR B CG2   1 
ATOM   4298  N N     . SER B  1  37  ? 52.110  38.543  -9.840  1.00 8.17  ? 37   SER B N     1 
ATOM   4299  C CA    . SER B  1  37  ? 52.866  37.357  -9.434  1.00 8.05  ? 37   SER B CA    1 
ATOM   4300  C C     . SER B  1  37  ? 54.361  37.557  -9.682  1.00 8.18  ? 37   SER B C     1 
ATOM   4301  O O     . SER B  1  37  ? 55.198  37.127  -8.887  1.00 8.82  ? 37   SER B O     1 
ATOM   4302  C CB    . SER B  1  37  ? 52.403  36.116  -10.209 1.00 8.24  ? 37   SER B CB    1 
ATOM   4303  O OG    . SER B  1  37  ? 51.103  35.703  -9.824  1.00 7.97  ? 37   SER B OG    1 
ATOM   4304  N N     . GLY B  1  38  ? 54.684  38.213  -10.791 1.00 8.14  ? 38   GLY B N     1 
ATOM   4305  C CA    . GLY B  1  38  ? 56.072  38.441  -11.159 1.00 7.61  ? 38   GLY B CA    1 
ATOM   4306  C C     . GLY B  1  38  ? 56.963  39.138  -10.147 1.00 8.22  ? 38   GLY B C     1 
ATOM   4307  O O     . GLY B  1  38  ? 58.094  38.714  -9.927  1.00 8.64  ? 38   GLY B O     1 
ATOM   4308  N N     . CYS B  1  39  ? 56.471  40.204  -9.529  1.00 8.63  ? 39   CYS B N     1 
ATOM   4309  C CA    . CYS B  1  39  ? 57.284  40.935  -8.564  1.00 9.40  ? 39   CYS B CA    1 
ATOM   4310  C C     . CYS B  1  39  ? 57.661  40.119  -7.326  1.00 9.62  ? 39   CYS B C     1 
ATOM   4311  O O     . CYS B  1  39  ? 58.838  40.033  -6.978  1.00 8.47  ? 39   CYS B O     1 
ATOM   4312  C CB    . CYS B  1  39  ? 56.586  42.241  -8.176  1.00 10.48 ? 39   CYS B CB    1 
ATOM   4313  S SG    . CYS B  1  39  ? 56.575  43.459  -9.523  1.00 10.20 ? 39   CYS B SG    1 
ATOM   4314  N N     . PRO B  1  40  ? 56.680  39.509  -6.641  1.00 8.95  ? 40   PRO B N     1 
ATOM   4315  C CA    . PRO B  1  40  ? 57.063  38.724  -5.461  1.00 8.76  ? 40   PRO B CA    1 
ATOM   4316  C C     . PRO B  1  40  ? 57.932  37.517  -5.820  1.00 8.77  ? 40   PRO B C     1 
ATOM   4317  O O     . PRO B  1  40  ? 58.780  37.098  -5.030  1.00 9.13  ? 40   PRO B O     1 
ATOM   4318  C CB    . PRO B  1  40  ? 55.718  38.331  -4.842  1.00 10.04 ? 40   PRO B CB    1 
ATOM   4319  C CG    . PRO B  1  40  ? 54.761  38.382  -6.015  1.00 9.87  ? 40   PRO B CG    1 
ATOM   4320  C CD    . PRO B  1  40  ? 55.215  39.606  -6.762  1.00 9.55  ? 40   PRO B CD    1 
ATOM   4321  N N     . LEU B  1  41  ? 57.722  36.962  -7.012  1.00 9.36  ? 41   LEU B N     1 
ATOM   4322  C CA    . LEU B  1  41  ? 58.521  35.824  -7.463  1.00 8.58  ? 41   LEU B CA    1 
ATOM   4323  C C     . LEU B  1  41  ? 59.968  36.287  -7.615  1.00 9.49  ? 41   LEU B C     1 
ATOM   4324  O O     . LEU B  1  41  ? 60.899  35.665  -7.088  1.00 9.02  ? 41   LEU B O     1 
ATOM   4325  C CB    . LEU B  1  41  ? 58.006  35.304  -8.811  1.00 9.72  ? 41   LEU B CB    1 
ATOM   4326  C CG    . LEU B  1  41  ? 58.896  34.277  -9.525  1.00 10.52 ? 41   LEU B CG    1 
ATOM   4327  C CD1   . LEU B  1  41  ? 59.074  33.035  -8.659  1.00 10.76 ? 41   LEU B CD1   1 
ATOM   4328  C CD2   . LEU B  1  41  ? 58.272  33.912  -10.866 1.00 11.60 ? 41   LEU B CD2   1 
ATOM   4329  N N     . ALA B  1  42  ? 60.146  37.390  -8.332  1.00 9.14  ? 42   ALA B N     1 
ATOM   4330  C CA    . ALA B  1  42  ? 61.472  37.952  -8.560  1.00 9.19  ? 42   ALA B CA    1 
ATOM   4331  C C     . ALA B  1  42  ? 62.189  38.274  -7.250  1.00 9.32  ? 42   ALA B C     1 
ATOM   4332  O O     . ALA B  1  42  ? 63.361  37.933  -7.075  1.00 9.97  ? 42   ALA B O     1 
ATOM   4333  C CB    . ALA B  1  42  ? 61.356  39.203  -9.409  1.00 10.12 ? 42   ALA B CB    1 
ATOM   4334  N N     . ALA B  1  43  ? 61.489  38.939  -6.335  1.00 8.97  ? 43   ALA B N     1 
ATOM   4335  C CA    . ALA B  1  43  ? 62.073  39.309  -5.046  1.00 9.07  ? 43   ALA B CA    1 
ATOM   4336  C C     . ALA B  1  43  ? 62.538  38.085  -4.261  1.00 9.22  ? 43   ALA B C     1 
ATOM   4337  O O     . ALA B  1  43  ? 63.630  38.078  -3.684  1.00 11.06 ? 43   ALA B O     1 
ATOM   4338  C CB    . ALA B  1  43  ? 61.059  40.100  -4.227  1.00 8.86  ? 43   ALA B CB    1 
ATOM   4339  N N     . THR B  1  44  ? 61.708  37.049  -4.243  1.00 8.37  ? 44   THR B N     1 
ATOM   4340  C CA    . THR B  1  44  ? 62.028  35.826  -3.526  1.00 8.67  ? 44   THR B CA    1 
ATOM   4341  C C     . THR B  1  44  ? 63.280  35.156  -4.079  1.00 10.57 ? 44   THR B C     1 
ATOM   4342  O O     . THR B  1  44  ? 64.201  34.823  -3.332  1.00 11.12 ? 44   THR B O     1 
ATOM   4343  C CB    . THR B  1  44  ? 60.847  34.850  -3.590  1.00 9.81  ? 44   THR B CB    1 
ATOM   4344  O OG1   . THR B  1  44  ? 59.728  35.437  -2.916  1.00 9.50  ? 44   THR B OG1   1 
ATOM   4345  C CG2   . THR B  1  44  ? 61.196  33.521  -2.929  1.00 10.65 ? 44   THR B CG2   1 
ATOM   4346  N N     . LEU B  1  45  ? 63.316  34.962  -5.391  1.00 10.69 ? 45   LEU B N     1 
ATOM   4347  C CA    . LEU B  1  45  ? 64.469  34.333  -6.016  1.00 11.03 ? 45   LEU B CA    1 
ATOM   4348  C C     . LEU B  1  45  ? 65.739  35.153  -5.800  1.00 12.55 ? 45   LEU B C     1 
ATOM   4349  O O     . LEU B  1  45  ? 66.820  34.584  -5.647  1.00 11.93 ? 45   LEU B O     1 
ATOM   4350  C CB    . LEU B  1  45  ? 64.216  34.140  -7.515  1.00 10.84 ? 45   LEU B CB    1 
ATOM   4351  C CG    . LEU B  1  45  ? 63.131  33.117  -7.870  1.00 9.08  ? 45   LEU B CG    1 
ATOM   4352  C CD1   . LEU B  1  45  ? 62.825  33.177  -9.358  1.00 11.17 ? 45   LEU B CD1   1 
ATOM   4353  C CD2   . LEU B  1  45  ? 63.591  31.723  -7.472  1.00 10.99 ? 45   LEU B CD2   1 
ATOM   4354  N N     . SER B  1  46  ? 65.604  36.479  -5.769  1.00 12.04 ? 46   SER B N     1 
ATOM   4355  C CA    . SER B  1  46  ? 66.757  37.361  -5.588  1.00 12.10 ? 46   SER B CA    1 
ATOM   4356  C C     . SER B  1  46  ? 67.400  37.222  -4.212  1.00 12.52 ? 46   SER B C     1 
ATOM   4357  O O     . SER B  1  46  ? 68.477  37.764  -3.972  1.00 13.79 ? 46   SER B O     1 
ATOM   4358  C CB    . SER B  1  46  ? 66.365  38.826  -5.826  1.00 10.85 ? 46   SER B CB    1 
ATOM   4359  O OG    . SER B  1  46  ? 65.683  39.376  -4.711  1.00 11.43 ? 46   SER B OG    1 
ATOM   4360  N N     . GLU B  1  47  ? 66.742  36.504  -3.308  1.00 12.88 ? 47   GLU B N     1 
ATOM   4361  C CA    . GLU B  1  47  ? 67.295  36.305  -1.973  1.00 13.53 ? 47   GLU B CA    1 
ATOM   4362  C C     . GLU B  1  47  ? 68.608  35.530  -2.054  1.00 14.28 ? 47   GLU B C     1 
ATOM   4363  O O     . GLU B  1  47  ? 69.489  35.689  -1.205  1.00 13.61 ? 47   GLU B O     1 
ATOM   4364  C CB    . GLU B  1  47  ? 66.292  35.559  -1.087  1.00 14.92 ? 47   GLU B CB    1 
ATOM   4365  C CG    . GLU B  1  47  ? 65.177  36.451  -0.552  1.00 17.42 ? 47   GLU B CG    1 
ATOM   4366  C CD    . GLU B  1  47  ? 64.114  35.681  0.210   1.00 18.81 ? 47   GLU B CD    1 
ATOM   4367  O OE1   . GLU B  1  47  ? 64.461  34.691  0.886   1.00 22.05 ? 47   GLU B OE1   1 
ATOM   4368  O OE2   . GLU B  1  47  ? 62.930  36.077  0.145   1.00 18.28 ? 47   GLU B OE2   1 
ATOM   4369  N N     . LYS B  1  48  ? 68.745  34.704  -3.086  1.00 14.05 ? 48   LYS B N     1 
ATOM   4370  C CA    . LYS B  1  48  ? 69.953  33.906  -3.257  1.00 15.06 ? 48   LYS B CA    1 
ATOM   4371  C C     . LYS B  1  48  ? 70.575  33.999  -4.644  1.00 15.54 ? 48   LYS B C     1 
ATOM   4372  O O     . LYS B  1  48  ? 71.781  33.786  -4.801  1.00 15.88 ? 48   LYS B O     1 
ATOM   4373  C CB    . LYS B  1  48  ? 69.658  32.434  -2.955  1.00 16.37 ? 48   LYS B CB    1 
ATOM   4374  C CG    . LYS B  1  48  ? 69.287  32.146  -1.510  1.00 21.29 ? 48   LYS B CG    1 
ATOM   4375  C CD    . LYS B  1  48  ? 69.146  30.651  -1.277  1.00 23.62 ? 48   LYS B CD    1 
ATOM   4376  C CE    . LYS B  1  48  ? 68.843  30.337  0.181   1.00 25.74 ? 48   LYS B CE    1 
ATOM   4377  N NZ    . LYS B  1  48  ? 68.756  28.866  0.415   1.00 26.70 ? 48   LYS B NZ    1 
ATOM   4378  N N     . TYR B  1  49  ? 69.769  34.328  -5.647  1.00 14.87 ? 49   TYR B N     1 
ATOM   4379  C CA    . TYR B  1  49  ? 70.283  34.382  -7.008  1.00 13.26 ? 49   TYR B CA    1 
ATOM   4380  C C     . TYR B  1  49  ? 70.144  35.705  -7.747  1.00 13.21 ? 49   TYR B C     1 
ATOM   4381  O O     . TYR B  1  49  ? 69.432  36.610  -7.312  1.00 11.71 ? 49   TYR B O     1 
ATOM   4382  C CB    . TYR B  1  49  ? 69.643  33.259  -7.829  1.00 14.11 ? 49   TYR B CB    1 
ATOM   4383  C CG    . TYR B  1  49  ? 69.959  31.880  -7.296  1.00 15.77 ? 49   TYR B CG    1 
ATOM   4384  C CD1   . TYR B  1  49  ? 69.034  31.173  -6.525  1.00 15.27 ? 49   TYR B CD1   1 
ATOM   4385  C CD2   . TYR B  1  49  ? 71.202  31.295  -7.532  1.00 16.59 ? 49   TYR B CD2   1 
ATOM   4386  C CE1   . TYR B  1  49  ? 69.344  29.917  -6.002  1.00 18.94 ? 49   TYR B CE1   1 
ATOM   4387  C CE2   . TYR B  1  49  ? 71.521  30.045  -7.014  1.00 18.69 ? 49   TYR B CE2   1 
ATOM   4388  C CZ    . TYR B  1  49  ? 70.592  29.362  -6.250  1.00 19.27 ? 49   TYR B CZ    1 
ATOM   4389  O OH    . TYR B  1  49  ? 70.920  28.130  -5.728  1.00 22.14 ? 49   TYR B OH    1 
ATOM   4390  N N     . LYS B  1  50  ? 70.852  35.807  -8.869  1.00 12.32 ? 50   LYS B N     1 
ATOM   4391  C CA    . LYS B  1  50  ? 70.827  37.003  -9.700  1.00 12.47 ? 50   LYS B CA    1 
ATOM   4392  C C     . LYS B  1  50  ? 69.586  36.938  -10.577 1.00 12.81 ? 50   LYS B C     1 
ATOM   4393  O O     . LYS B  1  50  ? 69.438  36.034  -11.401 1.00 13.52 ? 50   LYS B O     1 
ATOM   4394  C CB    . LYS B  1  50  ? 72.092  37.070  -10.555 1.00 11.43 ? 50   LYS B CB    1 
ATOM   4395  C CG    . LYS B  1  50  ? 73.372  37.151  -9.731  1.00 11.89 ? 50   LYS B CG    1 
ATOM   4396  C CD    . LYS B  1  50  ? 73.434  38.456  -8.951  1.00 13.46 ? 50   LYS B CD    1 
ATOM   4397  C CE    . LYS B  1  50  ? 74.688  38.539  -8.094  1.00 14.27 ? 50   LYS B CE    1 
ATOM   4398  N NZ    . LYS B  1  50  ? 74.787  39.858  -7.412  1.00 15.44 ? 50   LYS B NZ    1 
ATOM   4399  N N     . VAL B  1  51  ? 68.703  37.912  -10.392 1.00 10.80 ? 51   VAL B N     1 
ATOM   4400  C CA    . VAL B  1  51  ? 67.438  37.961  -11.112 1.00 11.61 ? 51   VAL B CA    1 
ATOM   4401  C C     . VAL B  1  51  ? 67.235  39.222  -11.938 1.00 11.96 ? 51   VAL B C     1 
ATOM   4402  O O     . VAL B  1  51  ? 67.617  40.318  -11.526 1.00 11.36 ? 51   VAL B O     1 
ATOM   4403  C CB    . VAL B  1  51  ? 66.259  37.859  -10.107 1.00 11.17 ? 51   VAL B CB    1 
ATOM   4404  C CG1   . VAL B  1  51  ? 64.928  37.887  -10.842 1.00 9.31  ? 51   VAL B CG1   1 
ATOM   4405  C CG2   . VAL B  1  51  ? 66.395  36.596  -9.272  1.00 10.77 ? 51   VAL B CG2   1 
ATOM   4406  N N     . LEU B  1  52  ? 66.629  39.049  -13.109 1.00 12.26 ? 52   LEU B N     1 
ATOM   4407  C CA    . LEU B  1  52  ? 66.304  40.160  -13.990 1.00 12.93 ? 52   LEU B CA    1 
ATOM   4408  C C     . LEU B  1  52  ? 64.808  40.090  -14.273 1.00 12.20 ? 52   LEU B C     1 
ATOM   4409  O O     . LEU B  1  52  ? 64.295  39.049  -14.688 1.00 12.06 ? 52   LEU B O     1 
ATOM   4410  C CB    . LEU B  1  52  ? 67.066  40.076  -15.318 1.00 11.99 ? 52   LEU B CB    1 
ATOM   4411  C CG    . LEU B  1  52  ? 66.604  41.106  -16.359 1.00 13.56 ? 52   LEU B CG    1 
ATOM   4412  C CD1   . LEU B  1  52  ? 66.900  42.516  -15.862 1.00 14.79 ? 52   LEU B CD1   1 
ATOM   4413  C CD2   . LEU B  1  52  ? 67.302  40.857  -17.684 1.00 14.50 ? 52   LEU B CD2   1 
ATOM   4414  N N     . VAL B  1  53  ? 64.111  41.191  -14.021 1.00 12.57 ? 53   VAL B N     1 
ATOM   4415  C CA    . VAL B  1  53  ? 62.679  41.274  -14.274 1.00 12.60 ? 53   VAL B CA    1 
ATOM   4416  C C     . VAL B  1  53  ? 62.502  42.227  -15.441 1.00 13.50 ? 53   VAL B C     1 
ATOM   4417  O O     . VAL B  1  53  ? 63.041  43.331  -15.426 1.00 15.05 ? 53   VAL B O     1 
ATOM   4418  C CB    . VAL B  1  53  ? 61.917  41.846  -13.068 1.00 16.15 ? 53   VAL B CB    1 
ATOM   4419  C CG1   . VAL B  1  53  ? 60.429  41.895  -13.372 1.00 16.15 ? 53   VAL B CG1   1 
ATOM   4420  C CG2   . VAL B  1  53  ? 62.184  41.007  -11.849 1.00 17.76 ? 53   VAL B CG2   1 
ATOM   4421  N N     . LEU B  1  54  ? 61.752  41.798  -16.449 1.00 10.77 ? 54   LEU B N     1 
ATOM   4422  C CA    . LEU B  1  54  ? 61.516  42.618  -17.634 1.00 10.98 ? 54   LEU B CA    1 
ATOM   4423  C C     . LEU B  1  54  ? 60.043  42.989  -17.743 1.00 10.81 ? 54   LEU B C     1 
ATOM   4424  O O     . LEU B  1  54  ? 59.187  42.122  -17.917 1.00 11.34 ? 54   LEU B O     1 
ATOM   4425  C CB    . LEU B  1  54  ? 61.968  41.859  -18.882 1.00 11.54 ? 54   LEU B CB    1 
ATOM   4426  C CG    . LEU B  1  54  ? 63.468  41.552  -18.898 1.00 12.45 ? 54   LEU B CG    1 
ATOM   4427  C CD1   . LEU B  1  54  ? 63.793  40.556  -20.001 1.00 12.28 ? 54   LEU B CD1   1 
ATOM   4428  C CD2   . LEU B  1  54  ? 64.242  42.850  -19.086 1.00 13.94 ? 54   LEU B CD2   1 
ATOM   4429  N N     . GLU B  1  55  ? 59.761  44.286  -17.647 1.00 9.74  ? 55   GLU B N     1 
ATOM   4430  C CA    . GLU B  1  55  ? 58.394  44.799  -17.714 1.00 10.55 ? 55   GLU B CA    1 
ATOM   4431  C C     . GLU B  1  55  ? 58.213  45.755  -18.889 1.00 10.58 ? 55   GLU B C     1 
ATOM   4432  O O     . GLU B  1  55  ? 58.988  46.690  -19.062 1.00 11.30 ? 55   GLU B O     1 
ATOM   4433  C CB    . GLU B  1  55  ? 58.057  45.512  -16.400 1.00 10.82 ? 55   GLU B CB    1 
ATOM   4434  C CG    . GLU B  1  55  ? 56.772  46.319  -16.413 1.00 11.12 ? 55   GLU B CG    1 
ATOM   4435  C CD    . GLU B  1  55  ? 55.565  45.486  -16.769 1.00 9.94  ? 55   GLU B CD    1 
ATOM   4436  O OE1   . GLU B  1  55  ? 55.448  44.357  -16.247 1.00 10.79 ? 55   GLU B OE1   1 
ATOM   4437  O OE2   . GLU B  1  55  ? 54.730  45.965  -17.563 1.00 10.90 ? 55   GLU B OE2   1 
ATOM   4438  N N     . ARG B  1  56  ? 57.174  45.527  -19.685 1.00 8.78  ? 56   ARG B N     1 
ATOM   4439  C CA    . ARG B  1  56  ? 56.914  46.361  -20.854 1.00 10.63 ? 56   ARG B CA    1 
ATOM   4440  C C     . ARG B  1  56  ? 56.453  47.778  -20.521 1.00 10.43 ? 56   ARG B C     1 
ATOM   4441  O O     . ARG B  1  56  ? 56.709  48.709  -21.284 1.00 11.44 ? 56   ARG B O     1 
ATOM   4442  C CB    . ARG B  1  56  ? 55.868  45.691  -21.747 1.00 9.74  ? 56   ARG B CB    1 
ATOM   4443  C CG    . ARG B  1  56  ? 54.523  45.519  -21.060 1.00 8.09  ? 56   ARG B CG    1 
ATOM   4444  C CD    . ARG B  1  56  ? 53.468  44.917  -21.977 1.00 9.19  ? 56   ARG B CD    1 
ATOM   4445  N NE    . ARG B  1  56  ? 52.181  44.866  -21.291 1.00 8.17  ? 56   ARG B NE    1 
ATOM   4446  C CZ    . ARG B  1  56  ? 51.001  44.817  -21.898 1.00 6.68  ? 56   ARG B CZ    1 
ATOM   4447  N NH1   . ARG B  1  56  ? 50.927  44.802  -23.224 1.00 8.32  ? 56   ARG B NH1   1 
ATOM   4448  N NH2   . ARG B  1  56  ? 49.890  44.813  -21.175 1.00 8.61  ? 56   ARG B NH2   1 
ATOM   4449  N N     . GLY B  1  57  ? 55.774  47.938  -19.387 1.00 10.43 ? 57   GLY B N     1 
ATOM   4450  C CA    . GLY B  1  57  ? 55.267  49.244  -18.997 1.00 10.70 ? 57   GLY B CA    1 
ATOM   4451  C C     . GLY B  1  57  ? 56.239  50.155  -18.266 1.00 11.41 ? 57   GLY B C     1 
ATOM   4452  O O     . GLY B  1  57  ? 57.406  49.820  -18.086 1.00 11.93 ? 57   GLY B O     1 
ATOM   4453  N N     . SER B  1  58  ? 55.742  51.313  -17.840 1.00 11.76 ? 58   SER B N     1 
ATOM   4454  C CA    . SER B  1  58  ? 56.553  52.300  -17.130 1.00 11.81 ? 58   SER B CA    1 
ATOM   4455  C C     . SER B  1  58  ? 56.560  52.078  -15.621 1.00 13.15 ? 58   SER B C     1 
ATOM   4456  O O     . SER B  1  58  ? 55.901  51.174  -15.106 1.00 12.97 ? 58   SER B O     1 
ATOM   4457  C CB    . SER B  1  58  ? 56.015  53.710  -17.397 1.00 13.04 ? 58   SER B CB    1 
ATOM   4458  O OG    . SER B  1  58  ? 55.955  54.000  -18.779 1.00 13.18 ? 58   SER B OG    1 
ATOM   4459  N N     . LEU B  1  59  ? 57.323  52.912  -14.919 1.00 12.37 ? 59   LEU B N     1 
ATOM   4460  C CA    . LEU B  1  59  ? 57.376  52.859  -13.465 1.00 13.15 ? 59   LEU B CA    1 
ATOM   4461  C C     . LEU B  1  59  ? 56.076  53.525  -13.020 1.00 13.10 ? 59   LEU B C     1 
ATOM   4462  O O     . LEU B  1  59  ? 55.528  54.361  -13.739 1.00 13.73 ? 59   LEU B O     1 
ATOM   4463  C CB    . LEU B  1  59  ? 58.569  53.666  -12.936 1.00 13.93 ? 59   LEU B CB    1 
ATOM   4464  C CG    . LEU B  1  59  ? 59.975  53.143  -13.239 1.00 15.58 ? 59   LEU B CG    1 
ATOM   4465  C CD1   . LEU B  1  59  ? 61.007  54.210  -12.888 1.00 17.96 ? 59   LEU B CD1   1 
ATOM   4466  C CD2   . LEU B  1  59  ? 60.229  51.869  -12.449 1.00 16.36 ? 59   LEU B CD2   1 
ATOM   4467  N N     . PRO B  1  60  ? 55.557  53.157  -11.839 1.00 13.19 ? 60   PRO B N     1 
ATOM   4468  C CA    . PRO B  1  60  ? 54.313  53.763  -11.360 1.00 13.98 ? 60   PRO B CA    1 
ATOM   4469  C C     . PRO B  1  60  ? 54.395  55.289  -11.276 1.00 13.92 ? 60   PRO B C     1 
ATOM   4470  O O     . PRO B  1  60  ? 53.405  55.986  -11.486 1.00 14.44 ? 60   PRO B O     1 
ATOM   4471  C CB    . PRO B  1  60  ? 54.123  53.118  -9.990  1.00 14.01 ? 60   PRO B CB    1 
ATOM   4472  C CG    . PRO B  1  60  ? 54.719  51.756  -10.185 1.00 13.30 ? 60   PRO B CG    1 
ATOM   4473  C CD    . PRO B  1  60  ? 55.985  52.060  -10.953 1.00 12.67 ? 60   PRO B CD    1 
ATOM   4474  N N     . THR B  1  61  ? 55.585  55.798  -10.976 1.00 14.90 ? 61   THR B N     1 
ATOM   4475  C CA    . THR B  1  61  ? 55.792  57.236  -10.854 1.00 15.99 ? 61   THR B CA    1 
ATOM   4476  C C     . THR B  1  61  ? 55.488  58.013  -12.135 1.00 15.28 ? 61   THR B C     1 
ATOM   4477  O O     . THR B  1  61  ? 55.258  59.224  -12.089 1.00 17.11 ? 61   THR B O     1 
ATOM   4478  C CB    . THR B  1  61  ? 57.237  57.546  -10.414 1.00 16.28 ? 61   THR B CB    1 
ATOM   4479  O OG1   . THR B  1  61  ? 58.158  56.939  -11.328 1.00 17.87 ? 61   THR B OG1   1 
ATOM   4480  C CG2   . THR B  1  61  ? 57.491  57.006  -9.015  1.00 16.77 ? 61   THR B CG2   1 
ATOM   4481  N N     . ALA B  1  62  ? 55.480  57.325  -13.273 1.00 14.70 ? 62   ALA B N     1 
ATOM   4482  C CA    . ALA B  1  62  ? 55.202  57.978  -14.550 1.00 14.78 ? 62   ALA B CA    1 
ATOM   4483  C C     . ALA B  1  62  ? 53.734  58.371  -14.679 1.00 14.91 ? 62   ALA B C     1 
ATOM   4484  O O     . ALA B  1  62  ? 53.382  59.227  -15.493 1.00 15.37 ? 62   ALA B O     1 
ATOM   4485  C CB    . ALA B  1  62  ? 55.598  57.066  -15.704 1.00 13.82 ? 62   ALA B CB    1 
ATOM   4486  N N     . TYR B  1  63  ? 52.881  57.736  -13.879 1.00 14.91 ? 63   TYR B N     1 
ATOM   4487  C CA    . TYR B  1  63  ? 51.449  58.016  -13.889 1.00 14.44 ? 63   TYR B CA    1 
ATOM   4488  C C     . TYR B  1  63  ? 50.945  58.100  -12.449 1.00 15.55 ? 63   TYR B C     1 
ATOM   4489  O O     . TYR B  1  63  ? 50.436  57.126  -11.897 1.00 14.01 ? 63   TYR B O     1 
ATOM   4490  C CB    . TYR B  1  63  ? 50.703  56.921  -14.660 1.00 13.84 ? 63   TYR B CB    1 
ATOM   4491  C CG    . TYR B  1  63  ? 51.161  56.793  -16.095 1.00 14.64 ? 63   TYR B CG    1 
ATOM   4492  C CD1   . TYR B  1  63  ? 52.239  55.975  -16.437 1.00 13.75 ? 63   TYR B CD1   1 
ATOM   4493  C CD2   . TYR B  1  63  ? 50.553  57.536  -17.106 1.00 15.19 ? 63   TYR B CD2   1 
ATOM   4494  C CE1   . TYR B  1  63  ? 52.700  55.903  -17.751 1.00 12.58 ? 63   TYR B CE1   1 
ATOM   4495  C CE2   . TYR B  1  63  ? 51.008  57.472  -18.419 1.00 14.46 ? 63   TYR B CE2   1 
ATOM   4496  C CZ    . TYR B  1  63  ? 52.081  56.656  -18.733 1.00 13.48 ? 63   TYR B CZ    1 
ATOM   4497  O OH    . TYR B  1  63  ? 52.543  56.613  -20.029 1.00 15.85 ? 63   TYR B OH    1 
ATOM   4498  N N     . PRO B  1  64  ? 51.072  59.284  -11.828 1.00 15.91 ? 64   PRO B N     1 
ATOM   4499  C CA    . PRO B  1  64  ? 50.669  59.587  -10.450 1.00 16.14 ? 64   PRO B CA    1 
ATOM   4500  C C     . PRO B  1  64  ? 49.293  59.111  -9.990  1.00 15.27 ? 64   PRO B C     1 
ATOM   4501  O O     . PRO B  1  64  ? 49.116  58.773  -8.820  1.00 15.39 ? 64   PRO B O     1 
ATOM   4502  C CB    . PRO B  1  64  ? 50.795  61.108  -10.385 1.00 18.18 ? 64   PRO B CB    1 
ATOM   4503  C CG    . PRO B  1  64  ? 51.932  61.380  -11.314 1.00 17.80 ? 64   PRO B CG    1 
ATOM   4504  C CD    . PRO B  1  64  ? 51.584  60.499  -12.490 1.00 17.17 ? 64   PRO B CD    1 
ATOM   4505  N N     . ASN B  1  65  ? 48.323  59.084  -10.897 1.00 15.63 ? 65   ASN B N     1 
ATOM   4506  C CA    . ASN B  1  65  ? 46.974  58.668  -10.532 1.00 16.01 ? 65   ASN B CA    1 
ATOM   4507  C C     . ASN B  1  65  ? 46.792  57.184  -10.225 1.00 16.20 ? 65   ASN B C     1 
ATOM   4508  O O     . ASN B  1  65  ? 45.711  56.763  -9.817  1.00 14.09 ? 65   ASN B O     1 
ATOM   4509  C CB    . ASN B  1  65  ? 45.986  59.119  -11.608 1.00 18.89 ? 65   ASN B CB    1 
ATOM   4510  C CG    . ASN B  1  65  ? 45.801  60.627  -11.621 1.00 21.02 ? 65   ASN B CG    1 
ATOM   4511  O OD1   . ASN B  1  65  ? 45.278  61.204  -10.670 1.00 26.11 ? 65   ASN B OD1   1 
ATOM   4512  N ND2   . ASN B  1  65  ? 46.244  61.272  -12.690 1.00 22.68 ? 65   ASN B ND2   1 
ATOM   4513  N N     . VAL B  1  66  ? 47.838  56.388  -10.417 1.00 15.80 ? 66   VAL B N     1 
ATOM   4514  C CA    . VAL B  1  66  ? 47.741  54.969  -10.093 1.00 13.75 ? 66   VAL B CA    1 
ATOM   4515  C C     . VAL B  1  66  ? 48.171  54.785  -8.638  1.00 14.02 ? 66   VAL B C     1 
ATOM   4516  O O     . VAL B  1  66  ? 48.126  53.679  -8.103  1.00 14.00 ? 66   VAL B O     1 
ATOM   4517  C CB    . VAL B  1  66  ? 48.659  54.091  -10.989 1.00 13.17 ? 66   VAL B CB    1 
ATOM   4518  C CG1   . VAL B  1  66  ? 48.308  54.288  -12.453 1.00 12.73 ? 66   VAL B CG1   1 
ATOM   4519  C CG2   . VAL B  1  66  ? 50.124  54.421  -10.731 1.00 14.56 ? 66   VAL B CG2   1 
ATOM   4520  N N     . LEU B  1  67  ? 48.571  55.879  -7.993  1.00 12.73 ? 67   LEU B N     1 
ATOM   4521  C CA    . LEU B  1  67  ? 49.043  55.809  -6.613  1.00 12.87 ? 67   LEU B CA    1 
ATOM   4522  C C     . LEU B  1  67  ? 48.043  56.193  -5.521  1.00 12.16 ? 67   LEU B C     1 
ATOM   4523  O O     . LEU B  1  67  ? 48.399  56.230  -4.340  1.00 12.20 ? 67   LEU B O     1 
ATOM   4524  C CB    . LEU B  1  67  ? 50.315  56.652  -6.472  1.00 13.33 ? 67   LEU B CB    1 
ATOM   4525  C CG    . LEU B  1  67  ? 51.481  56.232  -7.376  1.00 12.47 ? 67   LEU B CG    1 
ATOM   4526  C CD1   . LEU B  1  67  ? 52.635  57.210  -7.225  1.00 15.07 ? 67   LEU B CD1   1 
ATOM   4527  C CD2   . LEU B  1  67  ? 51.927  54.819  -7.021  1.00 14.60 ? 67   LEU B CD2   1 
ATOM   4528  N N     . THR B  1  68  ? 46.797  56.465  -5.900  1.00 12.52 ? 68   THR B N     1 
ATOM   4529  C CA    . THR B  1  68  ? 45.774  56.828  -4.922  1.00 13.55 ? 68   THR B CA    1 
ATOM   4530  C C     . THR B  1  68  ? 44.439  56.169  -5.248  1.00 13.52 ? 68   THR B C     1 
ATOM   4531  O O     . THR B  1  68  ? 44.176  55.811  -6.398  1.00 14.14 ? 68   THR B O     1 
ATOM   4532  C CB    . THR B  1  68  ? 45.537  58.357  -4.881  1.00 15.95 ? 68   THR B CB    1 
ATOM   4533  O OG1   . THR B  1  68  ? 45.035  58.792  -6.149  1.00 15.89 ? 68   THR B OG1   1 
ATOM   4534  C CG2   . THR B  1  68  ? 46.831  59.102  -4.562  1.00 15.07 ? 68   THR B CG2   1 
ATOM   4535  N N     . ALA B  1  69  ? 43.600  56.012  -4.229  1.00 13.25 ? 69   ALA B N     1 
ATOM   4536  C CA    . ALA B  1  69  ? 42.288  55.423  -4.423  1.00 13.91 ? 69   ALA B CA    1 
ATOM   4537  C C     . ALA B  1  69  ? 41.393  56.295  -5.293  1.00 14.64 ? 69   ALA B C     1 
ATOM   4538  O O     . ALA B  1  69  ? 40.657  55.783  -6.125  1.00 14.69 ? 69   ALA B O     1 
ATOM   4539  C CB    . ALA B  1  69  ? 41.621  55.160  -3.070  1.00 12.54 ? 69   ALA B CB    1 
ATOM   4540  N N     . ASP B  1  70  ? 41.441  57.613  -5.132  1.00 15.74 ? 70   ASP B N     1 
ATOM   4541  C CA    . ASP B  1  70  ? 40.574  58.431  -5.972  1.00 17.05 ? 70   ASP B CA    1 
ATOM   4542  C C     . ASP B  1  70  ? 41.056  58.550  -7.411  1.00 16.56 ? 70   ASP B C     1 
ATOM   4543  O O     . ASP B  1  70  ? 40.411  59.185  -8.241  1.00 17.67 ? 70   ASP B O     1 
ATOM   4544  C CB    . ASP B  1  70  ? 40.329  59.825  -5.373  1.00 20.44 ? 70   ASP B CB    1 
ATOM   4545  C CG    A ASP B  1  70  ? 41.578  60.474  -4.833  0.50 19.37 ? 70   ASP B CG    1 
ATOM   4546  C CG    B ASP B  1  70  ? 40.038  59.800  -3.894  0.50 20.16 ? 70   ASP B CG    1 
ATOM   4547  O OD1   A ASP B  1  70  ? 42.636  60.415  -5.493  0.50 21.81 ? 70   ASP B OD1   1 
ATOM   4548  O OD1   B ASP B  1  70  ? 39.739  58.719  -3.344  0.50 23.76 ? 70   ASP B OD1   1 
ATOM   4549  O OD2   A ASP B  1  70  ? 41.490  61.066  -3.737  0.50 21.22 ? 70   ASP B OD2   1 
ATOM   4550  O OD2   B ASP B  1  70  ? 40.128  60.879  -3.272  0.50 24.08 ? 70   ASP B OD2   1 
ATOM   4551  N N     . GLY B  1  71  ? 42.176  57.903  -7.712  1.00 15.49 ? 71   GLY B N     1 
ATOM   4552  C CA    . GLY B  1  71  ? 42.697  57.920  -9.068  1.00 13.90 ? 71   GLY B CA    1 
ATOM   4553  C C     . GLY B  1  71  ? 42.266  56.695  -9.861  1.00 12.70 ? 71   GLY B C     1 
ATOM   4554  O O     . GLY B  1  71  ? 42.547  56.584  -11.053 1.00 12.33 ? 71   GLY B O     1 
ATOM   4555  N N     . PHE B  1  72  ? 41.575  55.775  -9.196  1.00 12.97 ? 72   PHE B N     1 
ATOM   4556  C CA    . PHE B  1  72  ? 41.101  54.539  -9.822  1.00 11.59 ? 72   PHE B CA    1 
ATOM   4557  C C     . PHE B  1  72  ? 40.335  54.763  -11.123 1.00 11.16 ? 72   PHE B C     1 
ATOM   4558  O O     . PHE B  1  72  ? 40.694  54.225  -12.170 1.00 11.48 ? 72   PHE B O     1 
ATOM   4559  C CB    . PHE B  1  72  ? 40.217  53.757  -8.840  1.00 11.45 ? 72   PHE B CB    1 
ATOM   4560  C CG    . PHE B  1  72  ? 39.568  52.541  -9.444  1.00 11.10 ? 72   PHE B CG    1 
ATOM   4561  C CD1   . PHE B  1  72  ? 40.343  51.506  -9.953  1.00 11.04 ? 72   PHE B CD1   1 
ATOM   4562  C CD2   . PHE B  1  72  ? 38.181  52.438  -9.511  1.00 10.73 ? 72   PHE B CD2   1 
ATOM   4563  C CE1   . PHE B  1  72  ? 39.749  50.384  -10.522 1.00 10.74 ? 72   PHE B CE1   1 
ATOM   4564  C CE2   . PHE B  1  72  ? 37.573  51.318  -10.078 1.00 11.05 ? 72   PHE B CE2   1 
ATOM   4565  C CZ    . PHE B  1  72  ? 38.362  50.289  -10.585 1.00 11.02 ? 72   PHE B CZ    1 
ATOM   4566  N N     . VAL B  1  73  ? 39.275  55.558  -11.059 1.00 11.35 ? 73   VAL B N     1 
ATOM   4567  C CA    . VAL B  1  73  ? 38.477  55.826  -12.247 1.00 12.16 ? 73   VAL B CA    1 
ATOM   4568  C C     . VAL B  1  73  ? 39.281  56.582  -13.303 1.00 12.19 ? 73   VAL B C     1 
ATOM   4569  O O     . VAL B  1  73  ? 39.172  56.296  -14.495 1.00 11.94 ? 73   VAL B O     1 
ATOM   4570  C CB    . VAL B  1  73  ? 37.206  56.624  -11.885 1.00 12.30 ? 73   VAL B CB    1 
ATOM   4571  C CG1   . VAL B  1  73  ? 36.469  57.051  -13.147 1.00 14.46 ? 73   VAL B CG1   1 
ATOM   4572  C CG2   . VAL B  1  73  ? 36.303  55.766  -11.013 1.00 15.09 ? 73   VAL B CG2   1 
ATOM   4573  N N     . TYR B  1  74  ? 40.098  57.535  -12.865 1.00 13.09 ? 74   TYR B N     1 
ATOM   4574  C CA    . TYR B  1  74  ? 40.913  58.322  -13.784 1.00 12.69 ? 74   TYR B CA    1 
ATOM   4575  C C     . TYR B  1  74  ? 41.724  57.452  -14.743 1.00 13.40 ? 74   TYR B C     1 
ATOM   4576  O O     . TYR B  1  74  ? 41.724  57.681  -15.951 1.00 12.69 ? 74   TYR B O     1 
ATOM   4577  C CB    . TYR B  1  74  ? 41.873  59.225  -13.004 1.00 15.70 ? 74   TYR B CB    1 
ATOM   4578  C CG    . TYR B  1  74  ? 42.763  60.073  -13.888 1.00 18.56 ? 74   TYR B CG    1 
ATOM   4579  C CD1   . TYR B  1  74  ? 42.340  61.321  -14.348 1.00 21.02 ? 74   TYR B CD1   1 
ATOM   4580  C CD2   . TYR B  1  74  ? 44.024  59.620  -14.281 1.00 19.52 ? 74   TYR B CD2   1 
ATOM   4581  C CE1   . TYR B  1  74  ? 43.153  62.099  -15.177 1.00 22.23 ? 74   TYR B CE1   1 
ATOM   4582  C CE2   . TYR B  1  74  ? 44.843  60.387  -15.109 1.00 22.11 ? 74   TYR B CE2   1 
ATOM   4583  C CZ    . TYR B  1  74  ? 44.402  61.625  -15.552 1.00 22.41 ? 74   TYR B CZ    1 
ATOM   4584  O OH    . TYR B  1  74  ? 45.210  62.385  -16.369 1.00 23.34 ? 74   TYR B OH    1 
ATOM   4585  N N     . ASN B  1  75  ? 42.419  56.455  -14.203 1.00 12.31 ? 75   ASN B N     1 
ATOM   4586  C CA    . ASN B  1  75  ? 43.241  55.578  -15.031 1.00 12.30 ? 75   ASN B CA    1 
ATOM   4587  C C     . ASN B  1  75  ? 42.422  54.888  -16.117 1.00 11.08 ? 75   ASN B C     1 
ATOM   4588  O O     . ASN B  1  75  ? 42.880  54.745  -17.250 1.00 10.85 ? 75   ASN B O     1 
ATOM   4589  C CB    . ASN B  1  75  ? 43.925  54.531  -14.154 1.00 12.34 ? 75   ASN B CB    1 
ATOM   4590  C CG    . ASN B  1  75  ? 44.718  55.151  -13.023 1.00 13.09 ? 75   ASN B CG    1 
ATOM   4591  O OD1   . ASN B  1  75  ? 44.752  54.619  -11.911 1.00 14.93 ? 75   ASN B OD1   1 
ATOM   4592  N ND2   . ASN B  1  75  ? 45.365  56.279  -13.299 1.00 10.59 ? 75   ASN B ND2   1 
ATOM   4593  N N     . LEU B  1  76  ? 41.213  54.458  -15.769 1.00 10.55 ? 76   LEU B N     1 
ATOM   4594  C CA    . LEU B  1  76  ? 40.343  53.789  -16.731 1.00 10.28 ? 76   LEU B CA    1 
ATOM   4595  C C     . LEU B  1  76  ? 39.830  54.759  -17.796 1.00 11.25 ? 76   LEU B C     1 
ATOM   4596  O O     . LEU B  1  76  ? 39.586  54.367  -18.934 1.00 10.25 ? 76   LEU B O     1 
ATOM   4597  C CB    . LEU B  1  76  ? 39.152  53.143  -16.019 1.00 9.94  ? 76   LEU B CB    1 
ATOM   4598  C CG    . LEU B  1  76  ? 39.444  52.027  -15.013 1.00 10.49 ? 76   LEU B CG    1 
ATOM   4599  C CD1   . LEU B  1  76  ? 38.140  51.560  -14.386 1.00 10.41 ? 76   LEU B CD1   1 
ATOM   4600  C CD2   . LEU B  1  76  ? 40.143  50.868  -15.710 1.00 10.48 ? 76   LEU B CD2   1 
ATOM   4601  N N     . GLN B  1  77  ? 39.674  56.027  -17.426 1.00 12.43 ? 77   GLN B N     1 
ATOM   4602  C CA    . GLN B  1  77  ? 39.183  57.036  -18.367 1.00 13.10 ? 77   GLN B CA    1 
ATOM   4603  C C     . GLN B  1  77  ? 40.235  57.526  -19.360 1.00 13.70 ? 77   GLN B C     1 
ATOM   4604  O O     . GLN B  1  77  ? 39.896  57.993  -20.447 1.00 14.56 ? 77   GLN B O     1 
ATOM   4605  C CB    . GLN B  1  77  ? 38.640  58.252  -17.612 1.00 14.11 ? 77   GLN B CB    1 
ATOM   4606  C CG    . GLN B  1  77  ? 37.442  57.977  -16.729 1.00 12.66 ? 77   GLN B CG    1 
ATOM   4607  C CD    . GLN B  1  77  ? 37.120  59.162  -15.838 1.00 13.65 ? 77   GLN B CD    1 
ATOM   4608  O OE1   . GLN B  1  77  ? 38.000  59.696  -15.163 1.00 14.09 ? 77   GLN B OE1   1 
ATOM   4609  N NE2   . GLN B  1  77  ? 35.858  59.574  -15.826 1.00 13.62 ? 77   GLN B NE2   1 
ATOM   4610  N N     . GLN B  1  78  ? 41.507  57.432  -18.988 1.00 15.35 ? 78   GLN B N     1 
ATOM   4611  C CA    . GLN B  1  78  ? 42.579  57.911  -19.855 1.00 15.77 ? 78   GLN B CA    1 
ATOM   4612  C C     . GLN B  1  78  ? 42.714  57.184  -21.185 1.00 16.87 ? 78   GLN B C     1 
ATOM   4613  O O     . GLN B  1  78  ? 42.685  55.956  -21.250 1.00 16.60 ? 78   GLN B O     1 
ATOM   4614  C CB    . GLN B  1  78  ? 43.911  57.883  -19.103 1.00 16.92 ? 78   GLN B CB    1 
ATOM   4615  C CG    A GLN B  1  78  ? 43.887  58.747  -17.855 0.50 15.71 ? 78   GLN B CG    1 
ATOM   4616  C CG    B GLN B  1  78  ? 45.093  58.444  -19.886 0.50 16.14 ? 78   GLN B CG    1 
ATOM   4617  C CD    A GLN B  1  78  ? 43.163  60.068  -18.078 0.50 16.18 ? 78   GLN B CD    1 
ATOM   4618  C CD    B GLN B  1  78  ? 46.362  58.499  -19.060 0.50 16.71 ? 78   GLN B CD    1 
ATOM   4619  O OE1   A GLN B  1  78  ? 43.601  60.909  -18.867 0.50 16.32 ? 78   GLN B OE1   1 
ATOM   4620  O OE1   B GLN B  1  78  ? 46.673  57.565  -18.319 0.50 17.00 ? 78   GLN B OE1   1 
ATOM   4621  N NE2   A GLN B  1  78  ? 42.040  60.249  -17.388 0.50 11.64 ? 78   GLN B NE2   1 
ATOM   4622  N NE2   B GLN B  1  78  ? 47.242  59.494  -19.031 0.50 12.38 ? 78   GLN B NE2   1 
ATOM   4623  N N     . GLU B  1  79  ? 42.864  57.963  -22.251 1.00 17.08 ? 79   GLU B N     1 
ATOM   4624  C CA    . GLU B  1  79  ? 42.999  57.406  -23.585 1.00 18.09 ? 79   GLU B CA    1 
ATOM   4625  C C     . GLU B  1  79  ? 44.216  56.490  -23.646 1.00 15.73 ? 79   GLU B C     1 
ATOM   4626  O O     . GLU B  1  79  ? 45.249  56.765  -23.034 1.00 14.51 ? 79   GLU B O     1 
ATOM   4627  C CB    . GLU B  1  79  ? 43.135  58.529  -24.617 1.00 21.61 ? 79   GLU B CB    1 
ATOM   4628  C CG    . GLU B  1  79  ? 42.390  58.244  -25.907 1.00 28.11 ? 79   GLU B CG    1 
ATOM   4629  C CD    . GLU B  1  79  ? 40.884  58.230  -25.710 1.00 30.75 ? 79   GLU B CD    1 
ATOM   4630  O OE1   . GLU B  1  79  ? 40.201  57.435  -26.388 1.00 33.48 ? 79   GLU B OE1   1 
ATOM   4631  O OE2   . GLU B  1  79  ? 40.382  59.022  -24.883 1.00 34.09 ? 79   GLU B OE2   1 
ATOM   4632  N N     . ASP B  1  80  ? 44.079  55.398  -24.388 1.00 15.04 ? 80   ASP B N     1 
ATOM   4633  C CA    . ASP B  1  80  ? 45.146  54.420  -24.535 1.00 15.11 ? 80   ASP B CA    1 
ATOM   4634  C C     . ASP B  1  80  ? 46.086  54.833  -25.662 1.00 15.24 ? 80   ASP B C     1 
ATOM   4635  O O     . ASP B  1  80  ? 45.753  54.681  -26.839 1.00 15.89 ? 80   ASP B O     1 
ATOM   4636  C CB    . ASP B  1  80  ? 44.545  53.047  -24.844 1.00 15.25 ? 80   ASP B CB    1 
ATOM   4637  C CG    . ASP B  1  80  ? 45.576  51.938  -24.821 1.00 16.19 ? 80   ASP B CG    1 
ATOM   4638  O OD1   . ASP B  1  80  ? 46.787  52.238  -24.908 1.00 15.09 ? 80   ASP B OD1   1 
ATOM   4639  O OD2   . ASP B  1  80  ? 45.169  50.761  -24.731 1.00 16.38 ? 80   ASP B OD2   1 
ATOM   4640  N N     . ASP B  1  81  ? 47.257  55.353  -25.301 1.00 15.34 ? 81   ASP B N     1 
ATOM   4641  C CA    . ASP B  1  81  ? 48.232  55.780  -26.300 1.00 15.76 ? 81   ASP B CA    1 
ATOM   4642  C C     . ASP B  1  81  ? 49.332  54.747  -26.504 1.00 15.18 ? 81   ASP B C     1 
ATOM   4643  O O     . ASP B  1  81  ? 50.353  55.037  -27.125 1.00 14.92 ? 81   ASP B O     1 
ATOM   4644  C CB    . ASP B  1  81  ? 48.862  57.122  -25.909 1.00 16.89 ? 81   ASP B CB    1 
ATOM   4645  C CG    . ASP B  1  81  ? 49.642  57.053  -24.611 1.00 19.72 ? 81   ASP B CG    1 
ATOM   4646  O OD1   . ASP B  1  81  ? 49.893  55.937  -24.111 1.00 17.63 ? 81   ASP B OD1   1 
ATOM   4647  O OD2   . ASP B  1  81  ? 50.015  58.126  -24.094 1.00 20.81 ? 81   ASP B OD2   1 
ATOM   4648  N N     . GLY B  1  82  ? 49.119  53.544  -25.976 1.00 15.20 ? 82   GLY B N     1 
ATOM   4649  C CA    . GLY B  1  82  ? 50.101  52.483  -26.118 1.00 14.12 ? 82   GLY B CA    1 
ATOM   4650  C C     . GLY B  1  82  ? 51.152  52.464  -25.025 1.00 14.49 ? 82   GLY B C     1 
ATOM   4651  O O     . GLY B  1  82  ? 51.950  51.531  -24.941 1.00 14.75 ? 82   GLY B O     1 
ATOM   4652  N N     . LYS B  1  83  ? 51.152  53.489  -24.180 1.00 14.42 ? 83   LYS B N     1 
ATOM   4653  C CA    . LYS B  1  83  ? 52.127  53.578  -23.098 1.00 14.48 ? 83   LYS B CA    1 
ATOM   4654  C C     . LYS B  1  83  ? 51.482  53.690  -21.718 1.00 12.53 ? 83   LYS B C     1 
ATOM   4655  O O     . LYS B  1  83  ? 52.119  53.410  -20.706 1.00 14.61 ? 83   LYS B O     1 
ATOM   4656  C CB    . LYS B  1  83  ? 53.048  54.779  -23.339 1.00 17.97 ? 83   LYS B CB    1 
ATOM   4657  C CG    . LYS B  1  83  ? 53.840  54.706  -24.641 1.00 22.79 ? 83   LYS B CG    1 
ATOM   4658  C CD    . LYS B  1  83  ? 54.833  53.547  -24.620 1.00 25.93 ? 83   LYS B CD    1 
ATOM   4659  C CE    . LYS B  1  83  ? 55.688  53.479  -25.887 1.00 28.17 ? 83   LYS B CE    1 
ATOM   4660  N NZ    . LYS B  1  83  ? 54.955  52.973  -27.084 1.00 30.57 ? 83   LYS B NZ    1 
ATOM   4661  N N     . THR B  1  84  ? 50.220  54.100  -21.682 1.00 11.48 ? 84   THR B N     1 
ATOM   4662  C CA    . THR B  1  84  ? 49.488  54.261  -20.427 1.00 11.31 ? 84   THR B CA    1 
ATOM   4663  C C     . THR B  1  84  ? 49.358  52.955  -19.639 1.00 11.72 ? 84   THR B C     1 
ATOM   4664  O O     . THR B  1  84  ? 49.359  51.868  -20.216 1.00 12.04 ? 84   THR B O     1 
ATOM   4665  C CB    . THR B  1  84  ? 48.088  54.841  -20.693 1.00 11.16 ? 84   THR B CB    1 
ATOM   4666  O OG1   . THR B  1  84  ? 47.493  54.154  -21.798 1.00 12.88 ? 84   THR B OG1   1 
ATOM   4667  C CG2   . THR B  1  84  ? 48.176  56.331  -21.014 1.00 12.67 ? 84   THR B CG2   1 
ATOM   4668  N N     . PRO B  1  85  ? 49.228  53.049  -18.301 1.00 12.23 ? 85   PRO B N     1 
ATOM   4669  C CA    . PRO B  1  85  ? 49.105  51.876  -17.423 1.00 11.37 ? 85   PRO B CA    1 
ATOM   4670  C C     . PRO B  1  85  ? 47.870  51.005  -17.634 1.00 11.68 ? 85   PRO B C     1 
ATOM   4671  O O     . PRO B  1  85  ? 47.830  49.862  -17.183 1.00 10.55 ? 85   PRO B O     1 
ATOM   4672  C CB    . PRO B  1  85  ? 49.160  52.485  -16.021 1.00 10.24 ? 85   PRO B CB    1 
ATOM   4673  C CG    . PRO B  1  85  ? 48.542  53.840  -16.217 1.00 11.86 ? 85   PRO B CG    1 
ATOM   4674  C CD    . PRO B  1  85  ? 49.167  54.297  -17.516 1.00 10.98 ? 85   PRO B CD    1 
ATOM   4675  N N     . VAL B  1  86  ? 46.867  51.545  -18.315 1.00 10.26 ? 86   VAL B N     1 
ATOM   4676  C CA    . VAL B  1  86  ? 45.649  50.795  -18.587 1.00 9.57  ? 86   VAL B CA    1 
ATOM   4677  C C     . VAL B  1  86  ? 45.535  50.500  -20.078 1.00 11.03 ? 86   VAL B C     1 
ATOM   4678  O O     . VAL B  1  86  ? 45.303  51.403  -20.884 1.00 11.78 ? 86   VAL B O     1 
ATOM   4679  C CB    . VAL B  1  86  ? 44.395  51.574  -18.135 1.00 9.28  ? 86   VAL B CB    1 
ATOM   4680  C CG1   . VAL B  1  86  ? 43.131  50.789  -18.490 1.00 9.51  ? 86   VAL B CG1   1 
ATOM   4681  C CG2   . VAL B  1  86  ? 44.457  51.826  -16.639 1.00 9.78  ? 86   VAL B CG2   1 
ATOM   4682  N N     . GLU B  1  87  ? 45.721  49.235  -20.445 1.00 8.79  ? 87   GLU B N     1 
ATOM   4683  C CA    . GLU B  1  87  ? 45.611  48.834  -21.838 1.00 9.28  ? 87   GLU B CA    1 
ATOM   4684  C C     . GLU B  1  87  ? 44.193  48.346  -22.096 1.00 9.40  ? 87   GLU B C     1 
ATOM   4685  O O     . GLU B  1  87  ? 43.703  47.431  -21.425 1.00 9.78  ? 87   GLU B O     1 
ATOM   4686  C CB    . GLU B  1  87  ? 46.606  47.719  -22.180 1.00 10.63 ? 87   GLU B CB    1 
ATOM   4687  C CG    . GLU B  1  87  ? 46.294  47.044  -23.517 1.00 12.35 ? 87   GLU B CG    1 
ATOM   4688  C CD    . GLU B  1  87  ? 47.417  46.169  -24.031 1.00 12.58 ? 87   GLU B CD    1 
ATOM   4689  O OE1   . GLU B  1  87  ? 48.258  45.728  -23.224 1.00 12.58 ? 87   GLU B OE1   1 
ATOM   4690  O OE2   . GLU B  1  87  ? 47.451  45.911  -25.253 1.00 14.33 ? 87   GLU B OE2   1 
ATOM   4691  N N     . ARG B  1  88  ? 43.541  48.963  -23.072 1.00 8.70  ? 88   ARG B N     1 
ATOM   4692  C CA    . ARG B  1  88  ? 42.178  48.609  -23.428 1.00 8.96  ? 88   ARG B CA    1 
ATOM   4693  C C     . ARG B  1  88  ? 42.104  47.492  -24.456 1.00 8.91  ? 88   ARG B C     1 
ATOM   4694  O O     . ARG B  1  88  ? 42.944  47.396  -25.351 1.00 10.29 ? 88   ARG B O     1 
ATOM   4695  C CB    . ARG B  1  88  ? 41.451  49.824  -24.014 1.00 10.51 ? 88   ARG B CB    1 
ATOM   4696  C CG    . ARG B  1  88  ? 41.425  51.057  -23.139 1.00 8.76  ? 88   ARG B CG    1 
ATOM   4697  C CD    . ARG B  1  88  ? 40.660  52.176  -23.841 1.00 10.97 ? 88   ARG B CD    1 
ATOM   4698  N NE    . ARG B  1  88  ? 40.542  53.364  -23.007 1.00 12.46 ? 88   ARG B NE    1 
ATOM   4699  C CZ    . ARG B  1  88  ? 39.760  54.400  -23.289 1.00 13.99 ? 88   ARG B CZ    1 
ATOM   4700  N NH1   . ARG B  1  88  ? 39.018  54.398  -24.391 1.00 14.09 ? 88   ARG B NH1   1 
ATOM   4701  N NH2   . ARG B  1  88  ? 39.715  55.439  -22.464 1.00 15.50 ? 88   ARG B NH2   1 
ATOM   4702  N N     . PHE B  1  89  ? 41.092  46.643  -24.319 1.00 8.41  ? 89   PHE B N     1 
ATOM   4703  C CA    . PHE B  1  89  ? 40.857  45.586  -25.288 1.00 8.84  ? 89   PHE B CA    1 
ATOM   4704  C C     . PHE B  1  89  ? 39.385  45.215  -25.245 1.00 7.82  ? 89   PHE B C     1 
ATOM   4705  O O     . PHE B  1  89  ? 38.686  45.530  -24.284 1.00 9.72  ? 89   PHE B O     1 
ATOM   4706  C CB    . PHE B  1  89  ? 41.784  44.370  -25.059 1.00 10.02 ? 89   PHE B CB    1 
ATOM   4707  C CG    . PHE B  1  89  ? 41.447  43.522  -23.862 1.00 10.42 ? 89   PHE B CG    1 
ATOM   4708  C CD1   . PHE B  1  89  ? 40.596  42.426  -23.984 1.00 8.90  ? 89   PHE B CD1   1 
ATOM   4709  C CD2   . PHE B  1  89  ? 42.051  43.763  -22.632 1.00 11.18 ? 89   PHE B CD2   1 
ATOM   4710  C CE1   . PHE B  1  89  ? 40.358  41.577  -22.904 1.00 10.00 ? 89   PHE B CE1   1 
ATOM   4711  C CE2   . PHE B  1  89  ? 41.820  42.920  -21.543 1.00 10.98 ? 89   PHE B CE2   1 
ATOM   4712  C CZ    . PHE B  1  89  ? 40.975  41.826  -21.680 1.00 10.49 ? 89   PHE B CZ    1 
ATOM   4713  N N     . VAL B  1  90  ? 38.901  44.608  -26.321 1.00 8.20  ? 90   VAL B N     1 
ATOM   4714  C CA    . VAL B  1  90  ? 37.506  44.202  -26.398 1.00 8.58  ? 90   VAL B CA    1 
ATOM   4715  C C     . VAL B  1  90  ? 37.488  42.726  -26.756 1.00 8.45  ? 90   VAL B C     1 
ATOM   4716  O O     . VAL B  1  90  ? 38.108  42.321  -27.739 1.00 9.65  ? 90   VAL B O     1 
ATOM   4717  C CB    . VAL B  1  90  ? 36.756  44.993  -27.494 1.00 9.99  ? 90   VAL B CB    1 
ATOM   4718  C CG1   . VAL B  1  90  ? 35.279  44.633  -27.480 1.00 10.61 ? 90   VAL B CG1   1 
ATOM   4719  C CG2   . VAL B  1  90  ? 36.941  46.483  -27.276 1.00 10.89 ? 90   VAL B CG2   1 
ATOM   4720  N N     . SER B  1  91  ? 36.795  41.916  -25.962 1.00 8.30  ? 91   SER B N     1 
ATOM   4721  C CA    . SER B  1  91  ? 36.735  40.487  -26.256 1.00 7.90  ? 91   SER B CA    1 
ATOM   4722  C C     . SER B  1  91  ? 35.906  40.271  -27.519 1.00 8.36  ? 91   SER B C     1 
ATOM   4723  O O     . SER B  1  91  ? 35.166  41.159  -27.951 1.00 8.27  ? 91   SER B O     1 
ATOM   4724  C CB    . SER B  1  91  ? 36.112  39.708  -25.091 1.00 8.09  ? 91   SER B CB    1 
ATOM   4725  O OG    . SER B  1  91  ? 34.698  39.823  -25.075 1.00 8.11  ? 91   SER B OG    1 
ATOM   4726  N N     . GLU B  1  92  ? 36.036  39.089  -28.110 1.00 7.11  ? 92   GLU B N     1 
ATOM   4727  C CA    . GLU B  1  92  ? 35.295  38.757  -29.319 1.00 8.92  ? 92   GLU B CA    1 
ATOM   4728  C C     . GLU B  1  92  ? 33.795  38.694  -29.025 1.00 10.19 ? 92   GLU B C     1 
ATOM   4729  O O     . GLU B  1  92  ? 32.972  38.719  -29.944 1.00 10.79 ? 92   GLU B O     1 
ATOM   4730  C CB    . GLU B  1  92  ? 35.795  37.425  -29.888 1.00 8.93  ? 92   GLU B CB    1 
ATOM   4731  C CG    A GLU B  1  92  ? 37.161  37.521  -30.557 0.50 11.14 ? 92   GLU B CG    1 
ATOM   4732  C CG    B GLU B  1  92  ? 35.217  37.121  -31.282 0.50 11.31 ? 92   GLU B CG    1 
ATOM   4733  C CD    A GLU B  1  92  ? 37.780  36.163  -30.834 0.50 12.96 ? 92   GLU B CD    1 
ATOM   4734  C CD    B GLU B  1  92  ? 35.713  35.797  -31.829 0.50 13.31 ? 92   GLU B CD    1 
ATOM   4735  O OE1   A GLU B  1  92  ? 37.024  35.213  -31.125 0.50 14.23 ? 92   GLU B OE1   1 
ATOM   4736  O OE1   B GLU B  1  92  ? 36.893  35.463  -31.594 0.50 14.37 ? 92   GLU B OE1   1 
ATOM   4737  O OE2   A GLU B  1  92  ? 39.024  36.050  -30.771 0.50 16.96 ? 92   GLU B OE2   1 
ATOM   4738  O OE2   B GLU B  1  92  ? 34.922  35.095  -32.493 0.50 17.47 ? 92   GLU B OE2   1 
ATOM   4739  N N     . ASP B  1  93  ? 33.446  38.628  -27.740 1.00 8.48  ? 93   ASP B N     1 
ATOM   4740  C CA    . ASP B  1  93  ? 32.045  38.589  -27.328 1.00 9.37  ? 93   ASP B CA    1 
ATOM   4741  C C     . ASP B  1  93  ? 31.455  39.994  -27.430 1.00 10.02 ? 93   ASP B C     1 
ATOM   4742  O O     . ASP B  1  93  ? 30.235  40.165  -27.398 1.00 12.13 ? 93   ASP B O     1 
ATOM   4743  C CB    . ASP B  1  93  ? 31.902  38.119  -25.876 1.00 9.29  ? 93   ASP B CB    1 
ATOM   4744  C CG    . ASP B  1  93  ? 32.781  36.935  -25.549 1.00 9.32  ? 93   ASP B CG    1 
ATOM   4745  O OD1   . ASP B  1  93  ? 33.960  37.154  -25.187 1.00 9.65  ? 93   ASP B OD1   1 
ATOM   4746  O OD2   . ASP B  1  93  ? 32.294  35.787  -25.659 1.00 10.22 ? 93   ASP B OD2   1 
ATOM   4747  N N     . GLY B  1  94  ? 32.334  40.990  -27.528 1.00 10.29 ? 94   GLY B N     1 
ATOM   4748  C CA    . GLY B  1  94  ? 31.906  42.377  -27.617 1.00 11.07 ? 94   GLY B CA    1 
ATOM   4749  C C     . GLY B  1  94  ? 31.917  43.114  -26.285 1.00 11.86 ? 94   GLY B C     1 
ATOM   4750  O O     . GLY B  1  94  ? 31.309  44.176  -26.155 1.00 12.38 ? 94   GLY B O     1 
ATOM   4751  N N     . ILE B  1  95  ? 32.622  42.568  -25.299 1.00 10.34 ? 95   ILE B N     1 
ATOM   4752  C CA    . ILE B  1  95  ? 32.685  43.176  -23.968 1.00 9.20  ? 95   ILE B CA    1 
ATOM   4753  C C     . ILE B  1  95  ? 34.006  43.909  -23.718 1.00 9.56  ? 95   ILE B C     1 
ATOM   4754  O O     . ILE B  1  95  ? 35.081  43.314  -23.794 1.00 10.32 ? 95   ILE B O     1 
ATOM   4755  C CB    . ILE B  1  95  ? 32.483  42.093  -22.878 1.00 8.52  ? 95   ILE B CB    1 
ATOM   4756  C CG1   . ILE B  1  95  ? 31.122  41.410  -23.073 1.00 7.97  ? 95   ILE B CG1   1 
ATOM   4757  C CG2   . ILE B  1  95  ? 32.579  42.707  -21.488 1.00 7.87  ? 95   ILE B CG2   1 
ATOM   4758  C CD1   . ILE B  1  95  ? 29.925  42.365  -23.045 1.00 8.79  ? 95   ILE B CD1   1 
ATOM   4759  N N     . ASP B  1  96  ? 33.916  45.205  -23.421 1.00 9.01  ? 96   ASP B N     1 
ATOM   4760  C CA    . ASP B  1  96  ? 35.100  46.023  -23.160 1.00 9.07  ? 96   ASP B CA    1 
ATOM   4761  C C     . ASP B  1  96  ? 35.841  45.534  -21.922 1.00 8.80  ? 96   ASP B C     1 
ATOM   4762  O O     . ASP B  1  96  ? 35.225  45.093  -20.951 1.00 8.35  ? 96   ASP B O     1 
ATOM   4763  C CB    . ASP B  1  96  ? 34.711  47.494  -22.981 1.00 8.76  ? 96   ASP B CB    1 
ATOM   4764  C CG    . ASP B  1  96  ? 34.202  48.126  -24.263 1.00 12.18 ? 96   ASP B CG    1 
ATOM   4765  O OD1   . ASP B  1  96  ? 34.432  47.550  -25.348 1.00 11.77 ? 96   ASP B OD1   1 
ATOM   4766  O OD2   . ASP B  1  96  ? 33.585  49.211  -24.184 1.00 12.57 ? 96   ASP B OD2   1 
ATOM   4767  N N     . ASN B  1  97  ? 37.166  45.633  -21.951 1.00 8.55  ? 97   ASN B N     1 
ATOM   4768  C CA    . ASN B  1  97  ? 37.985  45.153  -20.846 1.00 7.43  ? 97   ASN B CA    1 
ATOM   4769  C C     . ASN B  1  97  ? 39.326  45.885  -20.803 1.00 8.39  ? 97   ASN B C     1 
ATOM   4770  O O     . ASN B  1  97  ? 39.652  46.664  -21.703 1.00 6.92  ? 97   ASN B O     1 
ATOM   4771  C CB    . ASN B  1  97  ? 38.235  43.655  -21.033 1.00 6.84  ? 97   ASN B CB    1 
ATOM   4772  C CG    . ASN B  1  97  ? 38.220  42.893  -19.728 1.00 5.75  ? 97   ASN B CG    1 
ATOM   4773  O OD1   . ASN B  1  97  ? 38.692  43.383  -18.705 1.00 8.39  ? 97   ASN B OD1   1 
ATOM   4774  N ND2   . ASN B  1  97  ? 37.685  41.674  -19.762 1.00 8.22  ? 97   ASN B ND2   1 
ATOM   4775  N N     . VAL B  1  98  ? 40.103  45.638  -19.752 1.00 7.05  ? 98   VAL B N     1 
ATOM   4776  C CA    . VAL B  1  98  ? 41.410  46.268  -19.620 1.00 7.12  ? 98   VAL B CA    1 
ATOM   4777  C C     . VAL B  1  98  ? 42.387  45.361  -18.881 1.00 7.04  ? 98   VAL B C     1 
ATOM   4778  O O     . VAL B  1  98  ? 41.980  44.442  -18.169 1.00 9.14  ? 98   VAL B O     1 
ATOM   4779  C CB    . VAL B  1  98  ? 41.341  47.609  -18.830 1.00 7.28  ? 98   VAL B CB    1 
ATOM   4780  C CG1   . VAL B  1  98  ? 40.338  48.556  -19.471 1.00 8.00  ? 98   VAL B CG1   1 
ATOM   4781  C CG2   . VAL B  1  98  ? 40.973  47.342  -17.373 1.00 8.71  ? 98   VAL B CG2   1 
ATOM   4782  N N     . ARG B  1  99  ? 43.678  45.612  -19.080 1.00 7.17  ? 99   ARG B N     1 
ATOM   4783  C CA    . ARG B  1  99  ? 44.725  44.875  -18.386 1.00 7.78  ? 99   ARG B CA    1 
ATOM   4784  C C     . ARG B  1  99  ? 45.844  45.859  -18.071 1.00 7.83  ? 99   ARG B C     1 
ATOM   4785  O O     . ARG B  1  99  ? 46.007  46.870  -18.754 1.00 8.33  ? 99   ARG B O     1 
ATOM   4786  C CB    . ARG B  1  99  ? 45.265  43.700  -19.221 1.00 9.37  ? 99   ARG B CB    1 
ATOM   4787  C CG    . ARG B  1  99  ? 45.885  44.058  -20.562 1.00 8.25  ? 99   ARG B CG    1 
ATOM   4788  C CD    . ARG B  1  99  ? 46.735  42.891  -21.075 1.00 10.41 ? 99   ARG B CD    1 
ATOM   4789  N NE    . ARG B  1  99  ? 47.018  42.996  -22.503 1.00 8.63  ? 99   ARG B NE    1 
ATOM   4790  C CZ    . ARG B  1  99  ? 48.071  42.451  -23.102 1.00 9.97  ? 99   ARG B CZ    1 
ATOM   4791  N NH1   . ARG B  1  99  ? 48.961  41.754  -22.401 1.00 8.58  ? 99   ARG B NH1   1 
ATOM   4792  N NH2   . ARG B  1  99  ? 48.240  42.609  -24.408 1.00 12.21 ? 99   ARG B NH2   1 
ATOM   4793  N N     . GLY B  1  100 ? 46.603  45.574  -17.022 1.00 7.99  ? 100  GLY B N     1 
ATOM   4794  C CA    . GLY B  1  100 ? 47.684  46.464  -16.647 1.00 7.06  ? 100  GLY B CA    1 
ATOM   4795  C C     . GLY B  1  100 ? 48.878  46.447  -17.582 1.00 7.93  ? 100  GLY B C     1 
ATOM   4796  O O     . GLY B  1  100 ? 49.154  45.449  -18.244 1.00 8.39  ? 100  GLY B O     1 
ATOM   4797  N N     . ARG B  1  101 ? 49.589  47.569  -17.624 1.00 7.98  ? 101  ARG B N     1 
ATOM   4798  C CA    . ARG B  1  101 ? 50.780  47.728  -18.455 1.00 7.34  ? 101  ARG B CA    1 
ATOM   4799  C C     . ARG B  1  101 ? 51.650  48.735  -17.711 1.00 9.21  ? 101  ARG B C     1 
ATOM   4800  O O     . ARG B  1  101 ? 51.778  49.893  -18.108 1.00 10.37 ? 101  ARG B O     1 
ATOM   4801  C CB    . ARG B  1  101 ? 50.388  48.262  -19.837 1.00 8.94  ? 101  ARG B CB    1 
ATOM   4802  C CG    . ARG B  1  101 ? 51.552  48.439  -20.805 1.00 7.80  ? 101  ARG B CG    1 
ATOM   4803  C CD    . ARG B  1  101 ? 51.040  48.748  -22.201 1.00 10.94 ? 101  ARG B CD    1 
ATOM   4804  N NE    . ARG B  1  101 ? 50.138  49.895  -22.192 1.00 12.61 ? 101  ARG B NE    1 
ATOM   4805  C CZ    . ARG B  1  101 ? 49.313  50.213  -23.183 1.00 13.12 ? 101  ARG B CZ    1 
ATOM   4806  N NH1   . ARG B  1  101 ? 49.267  49.469  -24.284 1.00 12.80 ? 101  ARG B NH1   1 
ATOM   4807  N NH2   . ARG B  1  101 ? 48.523  51.272  -23.067 1.00 13.80 ? 101  ARG B NH2   1 
ATOM   4808  N N     . VAL B  1  102 ? 52.240  48.270  -16.617 1.00 8.77  ? 102  VAL B N     1 
ATOM   4809  C CA    . VAL B  1  102 ? 53.058  49.110  -15.755 1.00 9.77  ? 102  VAL B CA    1 
ATOM   4810  C C     . VAL B  1  102 ? 53.753  48.191  -14.752 1.00 9.63  ? 102  VAL B C     1 
ATOM   4811  O O     . VAL B  1  102 ? 53.321  47.057  -14.551 1.00 9.01  ? 102  VAL B O     1 
ATOM   4812  C CB    . VAL B  1  102 ? 52.144  50.121  -15.007 1.00 9.47  ? 102  VAL B CB    1 
ATOM   4813  C CG1   . VAL B  1  102 ? 51.068  49.370  -14.221 1.00 11.37 ? 102  VAL B CG1   1 
ATOM   4814  C CG2   . VAL B  1  102 ? 52.964  51.007  -14.085 1.00 11.57 ? 102  VAL B CG2   1 
ATOM   4815  N N     . LEU B  1  103 ? 54.842  48.657  -14.144 1.00 8.98  ? 103  LEU B N     1 
ATOM   4816  C CA    . LEU B  1  103 ? 55.535  47.840  -13.153 1.00 9.71  ? 103  LEU B CA    1 
ATOM   4817  C C     . LEU B  1  103 ? 54.576  47.689  -11.975 1.00 9.66  ? 103  LEU B C     1 
ATOM   4818  O O     . LEU B  1  103 ? 54.032  48.673  -11.474 1.00 10.99 ? 103  LEU B O     1 
ATOM   4819  C CB    . LEU B  1  103 ? 56.833  48.514  -12.705 1.00 9.55  ? 103  LEU B CB    1 
ATOM   4820  C CG    . LEU B  1  103 ? 57.669  47.705  -11.710 1.00 9.55  ? 103  LEU B CG    1 
ATOM   4821  C CD1   . LEU B  1  103 ? 58.103  46.390  -12.347 1.00 10.38 ? 103  LEU B CD1   1 
ATOM   4822  C CD2   . LEU B  1  103 ? 58.883  48.518  -11.284 1.00 10.12 ? 103  LEU B CD2   1 
ATOM   4823  N N     . GLY B  1  104 ? 54.372  46.452  -11.540 1.00 8.62  ? 104  GLY B N     1 
ATOM   4824  C CA    . GLY B  1  104 ? 53.435  46.187  -10.466 1.00 8.29  ? 104  GLY B CA    1 
ATOM   4825  C C     . GLY B  1  104 ? 52.242  45.492  -11.103 1.00 7.14  ? 104  GLY B C     1 
ATOM   4826  O O     . GLY B  1  104 ? 51.391  44.920  -10.428 1.00 9.03  ? 104  GLY B O     1 
ATOM   4827  N N     . GLY B  1  105 ? 52.191  45.549  -12.428 1.00 7.10  ? 105  GLY B N     1 
ATOM   4828  C CA    . GLY B  1  105 ? 51.116  44.911  -13.161 1.00 7.85  ? 105  GLY B CA    1 
ATOM   4829  C C     . GLY B  1  105 ? 49.732  45.465  -12.896 1.00 7.68  ? 105  GLY B C     1 
ATOM   4830  O O     . GLY B  1  105 ? 49.548  46.647  -12.600 1.00 7.71  ? 105  GLY B O     1 
ATOM   4831  N N     . THR B  1  106 ? 48.743  44.589  -12.988 1.00 7.85  ? 106  THR B N     1 
ATOM   4832  C CA    . THR B  1  106 ? 47.364  44.993  -12.790 1.00 8.45  ? 106  THR B CA    1 
ATOM   4833  C C     . THR B  1  106 ? 47.034  45.327  -11.332 1.00 8.34  ? 106  THR B C     1 
ATOM   4834  O O     . THR B  1  106 ? 45.998  45.929  -11.047 1.00 8.36  ? 106  THR B O     1 
ATOM   4835  C CB    . THR B  1  106 ? 46.431  43.905  -13.368 1.00 9.25  ? 106  THR B CB    1 
ATOM   4836  O OG1   . THR B  1  106 ? 46.761  43.708  -14.750 1.00 7.79  ? 106  THR B OG1   1 
ATOM   4837  C CG2   . THR B  1  106 ? 44.973  44.322  -13.281 1.00 7.82  ? 106  THR B CG2   1 
ATOM   4838  N N     . SER B  1  107 ? 47.921  44.965  -10.407 1.00 8.57  ? 107  SER B N     1 
ATOM   4839  C CA    . SER B  1  107 ? 47.682  45.282  -9.000  1.00 7.88  ? 107  SER B CA    1 
ATOM   4840  C C     . SER B  1  107 ? 47.863  46.790  -8.801  1.00 9.38  ? 107  SER B C     1 
ATOM   4841  O O     . SER B  1  107 ? 47.490  47.336  -7.761  1.00 9.71  ? 107  SER B O     1 
ATOM   4842  C CB    . SER B  1  107 ? 48.651  44.517  -8.083  1.00 8.44  ? 107  SER B CB    1 
ATOM   4843  O OG    . SER B  1  107 ? 49.967  45.045  -8.150  1.00 8.16  ? 107  SER B OG    1 
ATOM   4844  N N     . ILE B  1  108 ? 48.427  47.455  -9.808  1.00 9.43  ? 108  ILE B N     1 
ATOM   4845  C CA    . ILE B  1  108 ? 48.659  48.901  -9.762  1.00 10.44 ? 108  ILE B CA    1 
ATOM   4846  C C     . ILE B  1  108 ? 47.457  49.712  -10.259 1.00 10.71 ? 108  ILE B C     1 
ATOM   4847  O O     . ILE B  1  108 ? 47.387  50.925  -10.044 1.00 11.73 ? 108  ILE B O     1 
ATOM   4848  C CB    . ILE B  1  108 ? 49.939  49.282  -10.590 1.00 11.56 ? 108  ILE B CB    1 
ATOM   4849  C CG1   . ILE B  1  108 ? 51.187  49.111  -9.721  1.00 14.99 ? 108  ILE B CG1   1 
ATOM   4850  C CG2   . ILE B  1  108 ? 49.866  50.722  -11.096 1.00 13.40 ? 108  ILE B CG2   1 
ATOM   4851  C CD1   . ILE B  1  108 ? 51.337  50.186  -8.644  1.00 15.72 ? 108  ILE B CD1   1 
ATOM   4852  N N     . ILE B  1  109 ? 46.502  49.049  -10.906 1.00 9.81  ? 109  ILE B N     1 
ATOM   4853  C CA    . ILE B  1  109 ? 45.328  49.748  -11.425 1.00 9.36  ? 109  ILE B CA    1 
ATOM   4854  C C     . ILE B  1  109 ? 44.003  49.153  -10.971 1.00 9.39  ? 109  ILE B C     1 
ATOM   4855  O O     . ILE B  1  109 ? 42.943  49.600  -11.417 1.00 8.90  ? 109  ILE B O     1 
ATOM   4856  C CB    . ILE B  1  109 ? 45.308  49.765  -12.975 1.00 9.78  ? 109  ILE B CB    1 
ATOM   4857  C CG1   . ILE B  1  109 ? 45.199  48.332  -13.515 1.00 10.34 ? 109  ILE B CG1   1 
ATOM   4858  C CG2   . ILE B  1  109 ? 46.557  50.455  -13.509 1.00 9.83  ? 109  ILE B CG2   1 
ATOM   4859  C CD1   . ILE B  1  109 ? 44.792  48.261  -14.978 1.00 9.36  ? 109  ILE B CD1   1 
ATOM   4860  N N     . ASN B  1  110 ? 44.048  48.165  -10.080 1.00 7.20  ? 110  ASN B N     1 
ATOM   4861  C CA    . ASN B  1  110 ? 42.814  47.519  -9.644  1.00 8.32  ? 110  ASN B CA    1 
ATOM   4862  C C     . ASN B  1  110 ? 42.015  48.235  -8.558  1.00 8.27  ? 110  ASN B C     1 
ATOM   4863  O O     . ASN B  1  110 ? 42.344  49.359  -8.169  1.00 8.24  ? 110  ASN B O     1 
ATOM   4864  C CB    . ASN B  1  110 ? 43.085  46.055  -9.247  1.00 8.00  ? 110  ASN B CB    1 
ATOM   4865  C CG    . ASN B  1  110 ? 43.945  45.912  -8.010  1.00 7.20  ? 110  ASN B CG    1 
ATOM   4866  O OD1   . ASN B  1  110 ? 44.045  46.819  -7.193  1.00 8.16  ? 110  ASN B OD1   1 
ATOM   4867  N ND2   . ASN B  1  110 ? 44.552  44.737  -7.856  1.00 8.22  ? 110  ASN B ND2   1 
ATOM   4868  N N     . ALA B  1  111 ? 40.947  47.589  -8.096  1.00 6.73  ? 111  ALA B N     1 
ATOM   4869  C CA    . ALA B  1  111 ? 40.070  48.168  -7.079  1.00 7.72  ? 111  ALA B CA    1 
ATOM   4870  C C     . ALA B  1  111 ? 40.534  47.961  -5.635  1.00 7.54  ? 111  ALA B C     1 
ATOM   4871  O O     . ALA B  1  111 ? 39.800  48.270  -4.691  1.00 9.45  ? 111  ALA B O     1 
ATOM   4872  C CB    . ALA B  1  111 ? 38.646  47.639  -7.260  1.00 7.31  ? 111  ALA B CB    1 
ATOM   4873  N N     . GLY B  1  112 ? 41.738  47.421  -5.472  1.00 7.91  ? 112  GLY B N     1 
ATOM   4874  C CA    . GLY B  1  112 ? 42.313  47.227  -4.148  1.00 7.21  ? 112  GLY B CA    1 
ATOM   4875  C C     . GLY B  1  112 ? 41.791  46.157  -3.205  1.00 7.49  ? 112  GLY B C     1 
ATOM   4876  O O     . GLY B  1  112 ? 42.401  45.924  -2.163  1.00 8.18  ? 112  GLY B O     1 
ATOM   4877  N N     . VAL B  1  113 ? 40.690  45.496  -3.548  1.00 8.16  ? 113  VAL B N     1 
ATOM   4878  C CA    . VAL B  1  113 ? 40.132  44.473  -2.664  1.00 7.28  ? 113  VAL B CA    1 
ATOM   4879  C C     . VAL B  1  113 ? 41.087  43.296  -2.479  1.00 7.36  ? 113  VAL B C     1 
ATOM   4880  O O     . VAL B  1  113 ? 41.569  42.718  -3.455  1.00 7.97  ? 113  VAL B O     1 
ATOM   4881  C CB    . VAL B  1  113 ? 38.779  43.954  -3.199  1.00 7.63  ? 113  VAL B CB    1 
ATOM   4882  C CG1   . VAL B  1  113 ? 38.163  42.976  -2.205  1.00 8.37  ? 113  VAL B CG1   1 
ATOM   4883  C CG2   . VAL B  1  113 ? 37.831  45.127  -3.432  1.00 6.31  ? 113  VAL B CG2   1 
ATOM   4884  N N     . TYR B  1  114 ? 41.362  42.949  -1.222  1.00 7.08  ? 114  TYR B N     1 
ATOM   4885  C CA    . TYR B  1  114 ? 42.264  41.838  -0.917  1.00 8.11  ? 114  TYR B CA    1 
ATOM   4886  C C     . TYR B  1  114 ? 41.582  40.714  -0.151  1.00 7.98  ? 114  TYR B C     1 
ATOM   4887  O O     . TYR B  1  114 ? 40.952  40.948  0.882   1.00 8.25  ? 114  TYR B O     1 
ATOM   4888  C CB    . TYR B  1  114 ? 43.458  42.318  -0.086  1.00 6.92  ? 114  TYR B CB    1 
ATOM   4889  C CG    . TYR B  1  114 ? 44.440  41.211  0.252   1.00 7.24  ? 114  TYR B CG    1 
ATOM   4890  C CD1   . TYR B  1  114 ? 45.545  40.956  -0.562  1.00 7.71  ? 114  TYR B CD1   1 
ATOM   4891  C CD2   . TYR B  1  114 ? 44.252  40.404  1.377   1.00 7.61  ? 114  TYR B CD2   1 
ATOM   4892  C CE1   . TYR B  1  114 ? 46.443  39.922  -0.262  1.00 7.75  ? 114  TYR B CE1   1 
ATOM   4893  C CE2   . TYR B  1  114 ? 45.137  39.372  1.682   1.00 8.86  ? 114  TYR B CE2   1 
ATOM   4894  C CZ    . TYR B  1  114 ? 46.230  39.136  0.861   1.00 7.00  ? 114  TYR B CZ    1 
ATOM   4895  O OH    . TYR B  1  114 ? 47.112  38.124  1.168   1.00 9.03  ? 114  TYR B OH    1 
ATOM   4896  N N     . ALA B  1  115 ? 41.739  39.491  -0.649  1.00 7.66  ? 115  ALA B N     1 
ATOM   4897  C CA    . ALA B  1  115 ? 41.163  38.320  -0.006  1.00 7.62  ? 115  ALA B CA    1 
ATOM   4898  C C     . ALA B  1  115 ? 42.087  37.121  -0.170  1.00 7.79  ? 115  ALA B C     1 
ATOM   4899  O O     . ALA B  1  115 ? 42.808  37.018  -1.162  1.00 6.86  ? 115  ALA B O     1 
ATOM   4900  C CB    . ALA B  1  115 ? 39.799  38.005  -0.620  1.00 8.78  ? 115  ALA B CB    1 
ATOM   4901  N N     . ARG B  1  116 ? 42.095  36.236  0.822   1.00 7.47  ? 116  ARG B N     1 
ATOM   4902  C CA    . ARG B  1  116 ? 42.886  35.017  0.725   1.00 8.45  ? 116  ARG B CA    1 
ATOM   4903  C C     . ARG B  1  116 ? 41.987  34.050  -0.032  1.00 9.39  ? 116  ARG B C     1 
ATOM   4904  O O     . ARG B  1  116 ? 40.765  34.182  -0.001  1.00 9.11  ? 116  ARG B O     1 
ATOM   4905  C CB    . ARG B  1  116 ? 43.199  34.438  2.108   1.00 8.91  ? 116  ARG B CB    1 
ATOM   4906  C CG    . ARG B  1  116 ? 44.266  35.189  2.867   1.00 8.90  ? 116  ARG B CG    1 
ATOM   4907  C CD    . ARG B  1  116 ? 44.631  34.446  4.137   1.00 9.26  ? 116  ARG B CD    1 
ATOM   4908  N NE    . ARG B  1  116 ? 45.697  35.120  4.870   1.00 10.09 ? 116  ARG B NE    1 
ATOM   4909  C CZ    . ARG B  1  116 ? 46.311  34.605  5.929   1.00 11.73 ? 116  ARG B CZ    1 
ATOM   4910  N NH1   . ARG B  1  116 ? 45.965  33.405  6.379   1.00 10.87 ? 116  ARG B NH1   1 
ATOM   4911  N NH2   . ARG B  1  116 ? 47.274  35.289  6.535   1.00 12.61 ? 116  ARG B NH2   1 
ATOM   4912  N N     . ALA B  1  117 ? 42.586  33.078  -0.707  1.00 8.05  ? 117  ALA B N     1 
ATOM   4913  C CA    . ALA B  1  117 ? 41.805  32.116  -1.467  1.00 9.55  ? 117  ALA B CA    1 
ATOM   4914  C C     . ALA B  1  117 ? 40.954  31.190  -0.601  1.00 10.84 ? 117  ALA B C     1 
ATOM   4915  O O     . ALA B  1  117 ? 41.266  30.931  0.564   1.00 10.67 ? 117  ALA B O     1 
ATOM   4916  C CB    . ALA B  1  117 ? 42.727  31.289  -2.349  1.00 9.00  ? 117  ALA B CB    1 
ATOM   4917  N N     . ASN B  1  118 ? 39.866  30.710  -1.197  1.00 11.10 ? 118  ASN B N     1 
ATOM   4918  C CA    . ASN B  1  118 ? 38.948  29.764  -0.570  1.00 12.07 ? 118  ASN B CA    1 
ATOM   4919  C C     . ASN B  1  118 ? 39.833  28.604  -0.091  1.00 13.64 ? 118  ASN B C     1 
ATOM   4920  O O     . ASN B  1  118 ? 40.499  27.961  -0.900  1.00 13.76 ? 118  ASN B O     1 
ATOM   4921  C CB    . ASN B  1  118 ? 37.961  29.279  -1.638  1.00 11.12 ? 118  ASN B CB    1 
ATOM   4922  C CG    . ASN B  1  118 ? 36.954  28.277  -1.112  1.00 12.89 ? 118  ASN B CG    1 
ATOM   4923  O OD1   . ASN B  1  118 ? 37.238  27.517  -0.187  1.00 14.84 ? 118  ASN B OD1   1 
ATOM   4924  N ND2   . ASN B  1  118 ? 35.774  28.262  -1.727  1.00 14.59 ? 118  ASN B ND2   1 
ATOM   4925  N N     . THR B  1  119 ? 39.852  28.334  1.211   1.00 14.45 ? 119  THR B N     1 
ATOM   4926  C CA    . THR B  1  119 ? 40.709  27.268  1.731   1.00 15.82 ? 119  THR B CA    1 
ATOM   4927  C C     . THR B  1  119 ? 40.386  25.863  1.221   1.00 16.74 ? 119  THR B C     1 
ATOM   4928  O O     . THR B  1  119 ? 41.150  24.929  1.459   1.00 17.89 ? 119  THR B O     1 
ATOM   4929  C CB    . THR B  1  119 ? 40.705  27.241  3.283   1.00 16.82 ? 119  THR B CB    1 
ATOM   4930  O OG1   . THR B  1  119 ? 39.375  27.011  3.761   1.00 18.92 ? 119  THR B OG1   1 
ATOM   4931  C CG2   . THR B  1  119 ? 41.222  28.559  3.842   1.00 17.72 ? 119  THR B CG2   1 
ATOM   4932  N N     . SER B  1  120 ? 39.275  25.713  0.508   1.00 16.62 ? 120  SER B N     1 
ATOM   4933  C CA    . SER B  1  120 ? 38.880  24.404  -0.010  1.00 19.01 ? 120  SER B CA    1 
ATOM   4934  C C     . SER B  1  120 ? 39.271  24.149  -1.468  1.00 19.71 ? 120  SER B C     1 
ATOM   4935  O O     . SER B  1  120 ? 39.049  23.055  -1.987  1.00 21.58 ? 120  SER B O     1 
ATOM   4936  C CB    . SER B  1  120 ? 37.366  24.222  0.134   1.00 19.35 ? 120  SER B CB    1 
ATOM   4937  O OG    . SER B  1  120 ? 36.958  24.386  1.480   1.00 21.70 ? 120  SER B OG    1 
ATOM   4938  N N     . ILE B  1  121 ? 39.865  25.139  -2.127  1.00 19.47 ? 121  ILE B N     1 
ATOM   4939  C CA    . ILE B  1  121 ? 40.231  24.977  -3.533  1.00 20.03 ? 121  ILE B CA    1 
ATOM   4940  C C     . ILE B  1  121 ? 41.615  24.398  -3.811  1.00 19.39 ? 121  ILE B C     1 
ATOM   4941  O O     . ILE B  1  121 ? 41.926  24.059  -4.952  1.00 19.70 ? 121  ILE B O     1 
ATOM   4942  C CB    . ILE B  1  121 ? 40.096  26.319  -4.308  1.00 20.65 ? 121  ILE B CB    1 
ATOM   4943  C CG1   . ILE B  1  121 ? 40.980  27.404  -3.684  1.00 22.12 ? 121  ILE B CG1   1 
ATOM   4944  C CG2   . ILE B  1  121 ? 38.647  26.770  -4.305  1.00 20.83 ? 121  ILE B CG2   1 
ATOM   4945  C CD1   . ILE B  1  121 ? 42.470  27.236  -3.919  1.00 21.51 ? 121  ILE B CD1   1 
ATOM   4946  N N     . TYR B  1  122 ? 42.442  24.275  -2.778  1.00 18.57 ? 122  TYR B N     1 
ATOM   4947  C CA    . TYR B  1  122 ? 43.791  23.755  -2.960  1.00 18.07 ? 122  TYR B CA    1 
ATOM   4948  C C     . TYR B  1  122 ? 43.859  22.272  -3.323  1.00 20.04 ? 122  TYR B C     1 
ATOM   4949  O O     . TYR B  1  122 ? 44.691  21.862  -4.129  1.00 19.06 ? 122  TYR B O     1 
ATOM   4950  C CB    . TYR B  1  122 ? 44.634  24.018  -1.706  1.00 16.30 ? 122  TYR B CB    1 
ATOM   4951  C CG    . TYR B  1  122 ? 44.795  25.487  -1.367  1.00 13.97 ? 122  TYR B CG    1 
ATOM   4952  C CD1   . TYR B  1  122 ? 43.917  26.124  -0.488  1.00 13.26 ? 122  TYR B CD1   1 
ATOM   4953  C CD2   . TYR B  1  122 ? 45.824  26.243  -1.932  1.00 11.97 ? 122  TYR B CD2   1 
ATOM   4954  C CE1   . TYR B  1  122 ? 44.062  27.481  -0.177  1.00 13.21 ? 122  TYR B CE1   1 
ATOM   4955  C CE2   . TYR B  1  122 ? 45.975  27.600  -1.629  1.00 12.66 ? 122  TYR B CE2   1 
ATOM   4956  C CZ    . TYR B  1  122 ? 45.095  28.208  -0.752  1.00 11.56 ? 122  TYR B CZ    1 
ATOM   4957  O OH    . TYR B  1  122 ? 45.263  29.538  -0.436  1.00 10.86 ? 122  TYR B OH    1 
ATOM   4958  N N     . SER B  1  123 ? 42.979  21.471  -2.739  1.00 20.96 ? 123  SER B N     1 
ATOM   4959  C CA    . SER B  1  123 ? 42.975  20.036  -3.004  1.00 23.79 ? 123  SER B CA    1 
ATOM   4960  C C     . SER B  1  123 ? 42.669  19.598  -4.437  1.00 24.05 ? 123  SER B C     1 
ATOM   4961  O O     . SER B  1  123 ? 43.260  18.640  -4.927  1.00 25.41 ? 123  SER B O     1 
ATOM   4962  C CB    . SER B  1  123 ? 42.014  19.332  -2.043  1.00 24.78 ? 123  SER B CB    1 
ATOM   4963  O OG    . SER B  1  123 ? 42.530  19.332  -0.721  1.00 28.34 ? 123  SER B OG    1 
ATOM   4964  N N     . ALA B  1  124 ? 41.760  20.288  -5.114  1.00 24.69 ? 124  ALA B N     1 
ATOM   4965  C CA    . ALA B  1  124 ? 41.402  19.914  -6.482  1.00 25.07 ? 124  ALA B CA    1 
ATOM   4966  C C     . ALA B  1  124 ? 42.126  20.726  -7.548  1.00 24.95 ? 124  ALA B C     1 
ATOM   4967  O O     . ALA B  1  124 ? 41.749  20.703  -8.714  1.00 26.18 ? 124  ALA B O     1 
ATOM   4968  C CB    . ALA B  1  124 ? 39.890  20.042  -6.669  1.00 25.72 ? 124  ALA B CB    1 
ATOM   4969  N N     . SER B  1  125 ? 43.173  21.434  -7.148  1.00 22.95 ? 125  SER B N     1 
ATOM   4970  C CA    . SER B  1  125 ? 43.925  22.282  -8.070  1.00 20.52 ? 125  SER B CA    1 
ATOM   4971  C C     . SER B  1  125 ? 44.912  21.610  -9.026  1.00 19.30 ? 125  SER B C     1 
ATOM   4972  O O     . SER B  1  125 ? 45.224  22.164  -10.075 1.00 19.62 ? 125  SER B O     1 
ATOM   4973  C CB    . SER B  1  125 ? 44.672  23.358  -7.274  1.00 19.72 ? 125  SER B CB    1 
ATOM   4974  O OG    . SER B  1  125 ? 45.657  22.761  -6.455  1.00 19.49 ? 125  SER B OG    1 
ATOM   4975  N N     . GLY B  1  126 ? 45.414  20.434  -8.668  1.00 18.15 ? 126  GLY B N     1 
ATOM   4976  C CA    . GLY B  1  126 ? 46.381  19.763  -9.520  1.00 15.60 ? 126  GLY B CA    1 
ATOM   4977  C C     . GLY B  1  126 ? 47.779  20.049  -9.014  1.00 15.37 ? 126  GLY B C     1 
ATOM   4978  O O     . GLY B  1  126 ? 48.781  19.693  -9.634  1.00 14.69 ? 126  GLY B O     1 
ATOM   4979  N N     . VAL B  1  127 ? 47.827  20.717  -7.868  1.00 14.19 ? 127  VAL B N     1 
ATOM   4980  C CA    . VAL B  1  127 ? 49.071  21.077  -7.204  1.00 13.75 ? 127  VAL B CA    1 
ATOM   4981  C C     . VAL B  1  127 ? 48.977  20.599  -5.758  1.00 14.31 ? 127  VAL B C     1 
ATOM   4982  O O     . VAL B  1  127 ? 47.938  20.748  -5.118  1.00 15.17 ? 127  VAL B O     1 
ATOM   4983  C CB    . VAL B  1  127 ? 49.286  22.619  -7.200  1.00 12.75 ? 127  VAL B CB    1 
ATOM   4984  C CG1   . VAL B  1  127 ? 50.469  22.990  -6.306  1.00 12.42 ? 127  VAL B CG1   1 
ATOM   4985  C CG2   . VAL B  1  127 ? 49.523  23.113  -8.622  1.00 11.50 ? 127  VAL B CG2   1 
ATOM   4986  N N     . ASP B  1  128 ? 50.052  20.006  -5.252  1.00 14.69 ? 128  ASP B N     1 
ATOM   4987  C CA    . ASP B  1  128 ? 50.075  19.541  -3.869  1.00 16.35 ? 128  ASP B CA    1 
ATOM   4988  C C     . ASP B  1  128 ? 50.664  20.699  -3.072  1.00 14.04 ? 128  ASP B C     1 
ATOM   4989  O O     . ASP B  1  128 ? 51.873  20.914  -3.074  1.00 14.82 ? 128  ASP B O     1 
ATOM   4990  C CB    . ASP B  1  128 ? 50.952  18.294  -3.749  1.00 18.24 ? 128  ASP B CB    1 
ATOM   4991  C CG    . ASP B  1  128 ? 50.274  17.053  -4.301  1.00 21.14 ? 128  ASP B CG    1 
ATOM   4992  O OD1   . ASP B  1  128 ? 50.988  16.129  -4.739  1.00 24.94 ? 128  ASP B OD1   1 
ATOM   4993  O OD2   . ASP B  1  128 ? 49.025  16.994  -4.283  1.00 22.68 ? 128  ASP B OD2   1 
ATOM   4994  N N     . TRP B  1  129 ? 49.796  21.448  -2.400  1.00 15.15 ? 129  TRP B N     1 
ATOM   4995  C CA    . TRP B  1  129 ? 50.224  22.619  -1.643  1.00 13.87 ? 129  TRP B CA    1 
ATOM   4996  C C     . TRP B  1  129 ? 50.791  22.396  -0.251  1.00 14.49 ? 129  TRP B C     1 
ATOM   4997  O O     . TRP B  1  129 ? 50.294  21.575  0.518   1.00 13.81 ? 129  TRP B O     1 
ATOM   4998  C CB    . TRP B  1  129 ? 49.067  23.617  -1.518  1.00 14.57 ? 129  TRP B CB    1 
ATOM   4999  C CG    . TRP B  1  129 ? 48.499  24.075  -2.823  1.00 13.72 ? 129  TRP B CG    1 
ATOM   5000  C CD1   . TRP B  1  129 ? 47.546  23.446  -3.569  1.00 13.32 ? 129  TRP B CD1   1 
ATOM   5001  C CD2   . TRP B  1  129 ? 48.863  25.257  -3.546  1.00 13.05 ? 129  TRP B CD2   1 
ATOM   5002  N NE1   . TRP B  1  129 ? 47.292  24.165  -4.714  1.00 13.53 ? 129  TRP B NE1   1 
ATOM   5003  C CE2   . TRP B  1  129 ? 48.087  25.281  -4.724  1.00 12.98 ? 129  TRP B CE2   1 
ATOM   5004  C CE3   . TRP B  1  129 ? 49.770  26.299  -3.312  1.00 13.43 ? 129  TRP B CE3   1 
ATOM   5005  C CZ2   . TRP B  1  129 ? 48.189  26.308  -5.670  1.00 13.23 ? 129  TRP B CZ2   1 
ATOM   5006  C CZ3   . TRP B  1  129 ? 49.873  27.323  -4.254  1.00 12.74 ? 129  TRP B CZ3   1 
ATOM   5007  C CH2   . TRP B  1  129 ? 49.085  27.317  -5.417  1.00 11.89 ? 129  TRP B CH2   1 
ATOM   5008  N N     . ASP B  1  130 ? 51.843  23.150  0.053   1.00 13.61 ? 130  ASP B N     1 
ATOM   5009  C CA    . ASP B  1  130 ? 52.480  23.142  1.365   1.00 13.06 ? 130  ASP B CA    1 
ATOM   5010  C C     . ASP B  1  130 ? 51.707  24.274  2.038   1.00 13.71 ? 130  ASP B C     1 
ATOM   5011  O O     . ASP B  1  130 ? 52.055  25.445  1.885   1.00 13.87 ? 130  ASP B O     1 
ATOM   5012  C CB    . ASP B  1  130 ? 53.959  23.523  1.240   1.00 14.21 ? 130  ASP B CB    1 
ATOM   5013  C CG    . ASP B  1  130 ? 54.665  23.595  2.583   1.00 16.50 ? 130  ASP B CG    1 
ATOM   5014  O OD1   . ASP B  1  130 ? 54.011  23.954  3.584   1.00 17.57 ? 130  ASP B OD1   1 
ATOM   5015  O OD2   . ASP B  1  130 ? 55.881  23.307  2.633   1.00 18.55 ? 130  ASP B OD2   1 
ATOM   5016  N N     . MET B  1  131 ? 50.644  23.931  2.758   1.00 13.72 ? 131  MET B N     1 
ATOM   5017  C CA    . MET B  1  131 ? 49.814  24.942  3.404   1.00 14.21 ? 131  MET B CA    1 
ATOM   5018  C C     . MET B  1  131 ? 50.508  25.819  4.433   1.00 13.38 ? 131  MET B C     1 
ATOM   5019  O O     . MET B  1  131 ? 50.116  26.969  4.633   1.00 12.76 ? 131  MET B O     1 
ATOM   5020  C CB    . MET B  1  131 ? 48.574  24.291  4.019   1.00 15.93 ? 131  MET B CB    1 
ATOM   5021  C CG    . MET B  1  131 ? 47.609  23.721  2.981   1.00 19.00 ? 131  MET B CG    1 
ATOM   5022  S SD    . MET B  1  131 ? 47.243  24.836  1.591   1.00 23.51 ? 131  MET B SD    1 
ATOM   5023  C CE    . MET B  1  131 ? 46.255  26.049  2.409   1.00 20.96 ? 131  MET B CE    1 
ATOM   5024  N N     . ASP B  1  132 ? 51.525  25.292  5.102   1.00 12.51 ? 132  ASP B N     1 
ATOM   5025  C CA    . ASP B  1  132 ? 52.237  26.116  6.061   1.00 13.82 ? 132  ASP B CA    1 
ATOM   5026  C C     . ASP B  1  132 ? 52.945  27.211  5.273   1.00 12.26 ? 132  ASP B C     1 
ATOM   5027  O O     . ASP B  1  132 ? 52.961  28.372  5.687   1.00 12.50 ? 132  ASP B O     1 
ATOM   5028  C CB    . ASP B  1  132 ? 53.251  25.289  6.856   1.00 16.45 ? 132  ASP B CB    1 
ATOM   5029  C CG    . ASP B  1  132 ? 52.587  24.300  7.789   1.00 19.48 ? 132  ASP B CG    1 
ATOM   5030  O OD1   . ASP B  1  132 ? 51.625  24.687  8.480   1.00 20.26 ? 132  ASP B OD1   1 
ATOM   5031  O OD2   . ASP B  1  132 ? 53.033  23.136  7.838   1.00 25.99 ? 132  ASP B OD2   1 
ATOM   5032  N N     . LEU B  1  133 ? 53.512  26.843  4.125   1.00 12.37 ? 133  LEU B N     1 
ATOM   5033  C CA    . LEU B  1  133 ? 54.207  27.809  3.281   1.00 11.90 ? 133  LEU B CA    1 
ATOM   5034  C C     . LEU B  1  133 ? 53.209  28.808  2.700   1.00 11.20 ? 133  LEU B C     1 
ATOM   5035  O O     . LEU B  1  133 ? 53.482  30.005  2.640   1.00 11.06 ? 133  LEU B O     1 
ATOM   5036  C CB    . LEU B  1  133 ? 54.956  27.097  2.146   1.00 12.73 ? 133  LEU B CB    1 
ATOM   5037  C CG    . LEU B  1  133 ? 55.689  27.995  1.141   1.00 12.25 ? 133  LEU B CG    1 
ATOM   5038  C CD1   . LEU B  1  133 ? 56.667  28.912  1.862   1.00 13.37 ? 133  LEU B CD1   1 
ATOM   5039  C CD2   . LEU B  1  133 ? 56.415  27.130  0.119   1.00 13.86 ? 133  LEU B CD2   1 
ATOM   5040  N N     . VAL B  1  134 ? 52.050  28.310  2.276   1.00 10.50 ? 134  VAL B N     1 
ATOM   5041  C CA    . VAL B  1  134 ? 51.017  29.174  1.718   1.00 10.36 ? 134  VAL B CA    1 
ATOM   5042  C C     . VAL B  1  134 ? 50.673  30.299  2.687   1.00 10.74 ? 134  VAL B C     1 
ATOM   5043  O O     . VAL B  1  134 ? 50.701  31.471  2.317   1.00 9.71  ? 134  VAL B O     1 
ATOM   5044  C CB    . VAL B  1  134 ? 49.725  28.385  1.403   1.00 10.50 ? 134  VAL B CB    1 
ATOM   5045  C CG1   . VAL B  1  134 ? 48.565  29.348  1.170   1.00 10.28 ? 134  VAL B CG1   1 
ATOM   5046  C CG2   . VAL B  1  134 ? 49.937  27.516  0.171   1.00 10.68 ? 134  VAL B CG2   1 
ATOM   5047  N N     . ASN B  1  135 ? 50.362  29.948  3.932   1.00 10.43 ? 135  ASN B N     1 
ATOM   5048  C CA    . ASN B  1  135 ? 50.015  30.964  4.919   1.00 9.85  ? 135  ASN B CA    1 
ATOM   5049  C C     . ASN B  1  135 ? 51.186  31.875  5.275   1.00 9.30  ? 135  ASN B C     1 
ATOM   5050  O O     . ASN B  1  135 ? 51.001  33.075  5.482   1.00 9.61  ? 135  ASN B O     1 
ATOM   5051  C CB    . ASN B  1  135 ? 49.445  30.310  6.175   1.00 9.21  ? 135  ASN B CB    1 
ATOM   5052  C CG    . ASN B  1  135 ? 48.037  29.789  5.964   1.00 10.73 ? 135  ASN B CG    1 
ATOM   5053  O OD1   . ASN B  1  135 ? 47.446  29.960  4.892   1.00 10.86 ? 135  ASN B OD1   1 
ATOM   5054  N ND2   . ASN B  1  135 ? 47.499  29.154  6.998   1.00 11.62 ? 135  ASN B ND2   1 
ATOM   5055  N N     . GLN B  1  136 ? 52.388  31.313  5.350   1.00 10.29 ? 136  GLN B N     1 
ATOM   5056  C CA    . GLN B  1  136 ? 53.565  32.121  5.649   1.00 10.22 ? 136  GLN B CA    1 
ATOM   5057  C C     . GLN B  1  136 ? 53.698  33.168  4.556   1.00 9.88  ? 136  GLN B C     1 
ATOM   5058  O O     . GLN B  1  136 ? 54.039  34.321  4.817   1.00 9.15  ? 136  GLN B O     1 
ATOM   5059  C CB    . GLN B  1  136 ? 54.824  31.251  5.671   1.00 12.47 ? 136  GLN B CB    1 
ATOM   5060  C CG    . GLN B  1  136 ? 55.022  30.465  6.952   1.00 12.95 ? 136  GLN B CG    1 
ATOM   5061  C CD    . GLN B  1  136 ? 56.002  29.326  6.769   1.00 16.35 ? 136  GLN B CD    1 
ATOM   5062  O OE1   . GLN B  1  136 ? 56.894  29.394  5.922   1.00 18.40 ? 136  GLN B OE1   1 
ATOM   5063  N NE2   . GLN B  1  136 ? 55.848  28.274  7.566   1.00 17.80 ? 136  GLN B NE2   1 
ATOM   5064  N N     . THR B  1  137 ? 53.405  32.757  3.325   1.00 9.84  ? 137  THR B N     1 
ATOM   5065  C CA    . THR B  1  137 ? 53.509  33.653  2.184   1.00 9.12  ? 137  THR B CA    1 
ATOM   5066  C C     . THR B  1  137 ? 52.427  34.730  2.223   1.00 9.52  ? 137  THR B C     1 
ATOM   5067  O O     . THR B  1  137 ? 52.708  35.894  1.956   1.00 9.57  ? 137  THR B O     1 
ATOM   5068  C CB    . THR B  1  137 ? 53.449  32.858  0.865   1.00 8.74  ? 137  THR B CB    1 
ATOM   5069  O OG1   . THR B  1  137 ? 54.508  31.890  0.857   1.00 9.89  ? 137  THR B OG1   1 
ATOM   5070  C CG2   . THR B  1  137 ? 53.633  33.787  -0.330  1.00 9.32  ? 137  THR B CG2   1 
ATOM   5071  N N     . TYR B  1  138 ? 51.197  34.354  2.561   1.00 9.26  ? 138  TYR B N     1 
ATOM   5072  C CA    . TYR B  1  138 ? 50.128  35.345  2.663   1.00 9.19  ? 138  TYR B CA    1 
ATOM   5073  C C     . TYR B  1  138 ? 50.560  36.407  3.676   1.00 9.45  ? 138  TYR B C     1 
ATOM   5074  O O     . TYR B  1  138 ? 50.408  37.605  3.434   1.00 9.63  ? 138  TYR B O     1 
ATOM   5075  C CB    . TYR B  1  138 ? 48.821  34.700  3.137   1.00 8.30  ? 138  TYR B CB    1 
ATOM   5076  C CG    . TYR B  1  138 ? 47.982  34.051  2.053   1.00 8.78  ? 138  TYR B CG    1 
ATOM   5077  C CD1   . TYR B  1  138 ? 47.425  32.785  2.245   1.00 10.25 ? 138  TYR B CD1   1 
ATOM   5078  C CD2   . TYR B  1  138 ? 47.703  34.718  0.859   1.00 9.06  ? 138  TYR B CD2   1 
ATOM   5079  C CE1   . TYR B  1  138 ? 46.607  32.199  1.275   1.00 10.12 ? 138  TYR B CE1   1 
ATOM   5080  C CE2   . TYR B  1  138 ? 46.885  34.144  -0.114  1.00 9.70  ? 138  TYR B CE2   1 
ATOM   5081  C CZ    . TYR B  1  138 ? 46.341  32.884  0.099   1.00 9.04  ? 138  TYR B CZ    1 
ATOM   5082  O OH    . TYR B  1  138 ? 45.527  32.312  -0.857  1.00 10.44 ? 138  TYR B OH    1 
ATOM   5083  N N     . GLU B  1  139 ? 51.102  35.966  4.810   1.00 9.81  ? 139  GLU B N     1 
ATOM   5084  C CA    . GLU B  1  139 ? 51.557  36.886  5.854   1.00 10.67 ? 139  GLU B CA    1 
ATOM   5085  C C     . GLU B  1  139 ? 52.650  37.827  5.348   1.00 8.27  ? 139  GLU B C     1 
ATOM   5086  O O     . GLU B  1  139 ? 52.644  39.020  5.636   1.00 9.73  ? 139  GLU B O     1 
ATOM   5087  C CB    . GLU B  1  139 ? 52.055  36.084  7.066   1.00 12.44 ? 139  GLU B CB    1 
ATOM   5088  C CG    . GLU B  1  139 ? 50.938  35.375  7.819   1.00 16.47 ? 139  GLU B CG    1 
ATOM   5089  C CD    . GLU B  1  139 ? 51.411  34.200  8.653   1.00 20.56 ? 139  GLU B CD    1 
ATOM   5090  O OE1   . GLU B  1  139 ? 50.557  33.589  9.328   1.00 23.83 ? 139  GLU B OE1   1 
ATOM   5091  O OE2   . GLU B  1  139 ? 52.623  33.889  8.642   1.00 24.70 ? 139  GLU B OE2   1 
ATOM   5092  N N     . TRP B  1  140 ? 53.585  37.276  4.587   1.00 8.89  ? 140  TRP B N     1 
ATOM   5093  C CA    . TRP B  1  140 ? 54.691  38.036  4.015   1.00 8.83  ? 140  TRP B CA    1 
ATOM   5094  C C     . TRP B  1  140 ? 54.141  39.173  3.145   1.00 8.42  ? 140  TRP B C     1 
ATOM   5095  O O     . TRP B  1  140 ? 54.609  40.318  3.215   1.00 9.95  ? 140  TRP B O     1 
ATOM   5096  C CB    . TRP B  1  140 ? 55.546  37.071  3.189   1.00 9.61  ? 140  TRP B CB    1 
ATOM   5097  C CG    . TRP B  1  140 ? 56.793  37.603  2.575   1.00 10.88 ? 140  TRP B CG    1 
ATOM   5098  C CD1   . TRP B  1  140 ? 58.054  37.569  3.108   1.00 11.69 ? 140  TRP B CD1   1 
ATOM   5099  C CD2   . TRP B  1  140 ? 56.936  38.092  1.239   1.00 10.88 ? 140  TRP B CD2   1 
ATOM   5100  N NE1   . TRP B  1  140 ? 58.973  37.989  2.175   1.00 12.41 ? 140  TRP B NE1   1 
ATOM   5101  C CE2   . TRP B  1  140 ? 58.313  38.317  1.019   1.00 12.19 ? 140  TRP B CE2   1 
ATOM   5102  C CE3   . TRP B  1  140 ? 56.033  38.353  0.200   1.00 9.92  ? 140  TRP B CE3   1 
ATOM   5103  C CZ2   . TRP B  1  140 ? 58.810  38.789  -0.201  1.00 12.55 ? 140  TRP B CZ2   1 
ATOM   5104  C CZ3   . TRP B  1  140 ? 56.528  38.825  -1.016  1.00 12.30 ? 140  TRP B CZ3   1 
ATOM   5105  C CH2   . TRP B  1  140 ? 57.906  39.036  -1.203  1.00 11.57 ? 140  TRP B CH2   1 
ATOM   5106  N N     . VAL B  1  141 ? 53.139  38.860  2.327   1.00 8.80  ? 141  VAL B N     1 
ATOM   5107  C CA    . VAL B  1  141 ? 52.523  39.857  1.458   1.00 9.31  ? 141  VAL B CA    1 
ATOM   5108  C C     . VAL B  1  141 ? 51.707  40.867  2.260   1.00 8.90  ? 141  VAL B C     1 
ATOM   5109  O O     . VAL B  1  141 ? 51.853  42.079  2.091   1.00 9.61  ? 141  VAL B O     1 
ATOM   5110  C CB    . VAL B  1  141 ? 51.584  39.192  0.415   1.00 8.98  ? 141  VAL B CB    1 
ATOM   5111  C CG1   . VAL B  1  141 ? 50.822  40.257  -0.364  1.00 9.01  ? 141  VAL B CG1   1 
ATOM   5112  C CG2   . VAL B  1  141 ? 52.394  38.326  -0.536  1.00 9.12  ? 141  VAL B CG2   1 
ATOM   5113  N N     . GLU B  1  142 ? 50.853  40.356  3.139   1.00 8.52  ? 142  GLU B N     1 
ATOM   5114  C CA    . GLU B  1  142 ? 49.987  41.196  3.957   1.00 8.81  ? 142  GLU B CA    1 
ATOM   5115  C C     . GLU B  1  142 ? 50.729  42.181  4.853   1.00 9.58  ? 142  GLU B C     1 
ATOM   5116  O O     . GLU B  1  142 ? 50.299  43.324  5.004   1.00 10.19 ? 142  GLU B O     1 
ATOM   5117  C CB    . GLU B  1  142 ? 49.051  40.308  4.781   1.00 9.47  ? 142  GLU B CB    1 
ATOM   5118  C CG    . GLU B  1  142 ? 48.053  39.562  3.900   1.00 10.09 ? 142  GLU B CG    1 
ATOM   5119  C CD    . GLU B  1  142 ? 47.504  38.300  4.537   1.00 11.45 ? 142  GLU B CD    1 
ATOM   5120  O OE1   . GLU B  1  142 ? 46.832  37.526  3.817   1.00 9.97  ? 142  GLU B OE1   1 
ATOM   5121  O OE2   . GLU B  1  142 ? 47.743  38.077  5.745   1.00 11.05 ? 142  GLU B OE2   1 
ATOM   5122  N N     . ASP B  1  143 ? 51.843  41.753  5.436   1.00 10.07 ? 143  ASP B N     1 
ATOM   5123  C CA    . ASP B  1  143 ? 52.611  42.643  6.305   1.00 11.94 ? 143  ASP B CA    1 
ATOM   5124  C C     . ASP B  1  143 ? 53.258  43.781  5.521   1.00 11.80 ? 143  ASP B C     1 
ATOM   5125  O O     . ASP B  1  143 ? 53.765  44.742  6.114   1.00 13.19 ? 143  ASP B O     1 
ATOM   5126  C CB    . ASP B  1  143 ? 53.704  41.869  7.049   1.00 13.88 ? 143  ASP B CB    1 
ATOM   5127  C CG    . ASP B  1  143 ? 53.147  40.948  8.118   1.00 15.29 ? 143  ASP B CG    1 
ATOM   5128  O OD1   . ASP B  1  143 ? 52.011  41.182  8.582   1.00 20.15 ? 143  ASP B OD1   1 
ATOM   5129  O OD2   . ASP B  1  143 ? 53.854  39.996  8.506   1.00 19.58 ? 143  ASP B OD2   1 
ATOM   5130  N N     . THR B  1  144 ? 53.223  43.685  4.194   1.00 9.94  ? 144  THR B N     1 
ATOM   5131  C CA    . THR B  1  144 ? 53.839  44.697  3.347   1.00 10.73 ? 144  THR B CA    1 
ATOM   5132  C C     . THR B  1  144 ? 52.881  45.639  2.624   1.00 10.04 ? 144  THR B C     1 
ATOM   5133  O O     . THR B  1  144 ? 53.134  46.844  2.557   1.00 10.57 ? 144  THR B O     1 
ATOM   5134  C CB    . THR B  1  144 ? 54.743  44.042  2.280   1.00 11.76 ? 144  THR B CB    1 
ATOM   5135  O OG1   . THR B  1  144 ? 55.629  43.109  2.911   1.00 14.32 ? 144  THR B OG1   1 
ATOM   5136  C CG2   . THR B  1  144 ? 55.571  45.100  1.554   1.00 12.19 ? 144  THR B CG2   1 
ATOM   5137  N N     . ILE B  1  145 ? 51.787  45.101  2.085   1.00 8.62  ? 145  ILE B N     1 
ATOM   5138  C CA    . ILE B  1  145 ? 50.847  45.928  1.327   1.00 8.96  ? 145  ILE B CA    1 
ATOM   5139  C C     . ILE B  1  145 ? 49.346  45.761  1.587   1.00 8.92  ? 145  ILE B C     1 
ATOM   5140  O O     . ILE B  1  145 ? 48.535  46.237  0.792   1.00 9.22  ? 145  ILE B O     1 
ATOM   5141  C CB    . ILE B  1  145 ? 51.067  45.748  -0.201  1.00 7.67  ? 145  ILE B CB    1 
ATOM   5142  C CG1   . ILE B  1  145 ? 50.805  44.293  -0.604  1.00 8.33  ? 145  ILE B CG1   1 
ATOM   5143  C CG2   . ILE B  1  145 ? 52.490  46.150  -0.574  1.00 11.11 ? 145  ILE B CG2   1 
ATOM   5144  C CD1   . ILE B  1  145 ? 50.791  44.066  -2.108  1.00 7.68  ? 145  ILE B CD1   1 
ATOM   5145  N N     . VAL B  1  146 ? 48.961  45.106  2.677   1.00 8.85  ? 146  VAL B N     1 
ATOM   5146  C CA    . VAL B  1  146 ? 47.535  44.930  2.954   1.00 8.41  ? 146  VAL B CA    1 
ATOM   5147  C C     . VAL B  1  146 ? 47.131  45.633  4.249   1.00 10.71 ? 146  VAL B C     1 
ATOM   5148  O O     . VAL B  1  146 ? 47.819  45.528  5.270   1.00 11.48 ? 146  VAL B O     1 
ATOM   5149  C CB    . VAL B  1  146 ? 47.157  43.435  3.017   1.00 9.01  ? 146  VAL B CB    1 
ATOM   5150  C CG1   . VAL B  1  146 ? 45.650  43.281  3.225   1.00 8.88  ? 146  VAL B CG1   1 
ATOM   5151  C CG2   . VAL B  1  146 ? 47.575  42.749  1.724   1.00 9.49  ? 146  VAL B CG2   1 
ATOM   5152  N N     . TYR B  1  147 ? 46.007  46.345  4.201   1.00 9.81  ? 147  TYR B N     1 
ATOM   5153  C CA    . TYR B  1  147 ? 45.542  47.111  5.350   1.00 10.66 ? 147  TYR B CA    1 
ATOM   5154  C C     . TYR B  1  147 ? 44.103  46.871  5.770   1.00 11.44 ? 147  TYR B C     1 
ATOM   5155  O O     . TYR B  1  147 ? 43.249  46.564  4.947   1.00 11.73 ? 147  TYR B O     1 
ATOM   5156  C CB    . TYR B  1  147 ? 45.698  48.611  5.056   1.00 11.20 ? 147  TYR B CB    1 
ATOM   5157  C CG    . TYR B  1  147 ? 47.037  48.957  4.470   1.00 10.44 ? 147  TYR B CG    1 
ATOM   5158  C CD1   . TYR B  1  147 ? 47.316  48.707  3.127   1.00 10.62 ? 147  TYR B CD1   1 
ATOM   5159  C CD2   . TYR B  1  147 ? 48.066  49.431  5.280   1.00 9.60  ? 147  TYR B CD2   1 
ATOM   5160  C CE1   . TYR B  1  147 ? 48.587  48.909  2.611   1.00 10.60 ? 147  TYR B CE1   1 
ATOM   5161  C CE2   . TYR B  1  147 ? 49.338  49.637  4.775   1.00 10.13 ? 147  TYR B CE2   1 
ATOM   5162  C CZ    . TYR B  1  147 ? 49.595  49.371  3.442   1.00 11.30 ? 147  TYR B CZ    1 
ATOM   5163  O OH    . TYR B  1  147 ? 50.864  49.546  2.948   1.00 12.05 ? 147  TYR B OH    1 
ATOM   5164  N N     . LYS B  1  148 ? 43.852  47.023  7.067   1.00 11.40 ? 148  LYS B N     1 
ATOM   5165  C CA    . LYS B  1  148 ? 42.511  46.910  7.622   1.00 12.32 ? 148  LYS B CA    1 
ATOM   5166  C C     . LYS B  1  148 ? 41.956  48.289  7.303   1.00 12.90 ? 148  LYS B C     1 
ATOM   5167  O O     . LYS B  1  148 ? 42.491  49.296  7.762   1.00 13.66 ? 148  LYS B O     1 
ATOM   5168  C CB    . LYS B  1  148 ? 42.580  46.687  9.131   1.00 12.97 ? 148  LYS B CB    1 
ATOM   5169  C CG    . LYS B  1  148 ? 41.229  46.656  9.833   1.00 13.85 ? 148  LYS B CG    1 
ATOM   5170  C CD    . LYS B  1  148 ? 41.409  46.262  11.297  1.00 16.40 ? 148  LYS B CD    1 
ATOM   5171  C CE    . LYS B  1  148 ? 40.156  46.531  12.118  1.00 21.20 ? 148  LYS B CE    1 
ATOM   5172  N NZ    . LYS B  1  148 ? 38.967  45.782  11.646  1.00 25.00 ? 148  LYS B NZ    1 
ATOM   5173  N N     . PRO B  1  149 ? 40.873  48.355  6.517   1.00 12.84 ? 149  PRO B N     1 
ATOM   5174  C CA    . PRO B  1  149 ? 40.263  49.630  6.124   1.00 12.78 ? 149  PRO B CA    1 
ATOM   5175  C C     . PRO B  1  149 ? 39.573  50.489  7.174   1.00 12.49 ? 149  PRO B C     1 
ATOM   5176  O O     . PRO B  1  149 ? 39.188  50.015  8.244   1.00 12.80 ? 149  PRO B O     1 
ATOM   5177  C CB    . PRO B  1  149 ? 39.296  49.210  5.021   1.00 12.70 ? 149  PRO B CB    1 
ATOM   5178  C CG    . PRO B  1  149 ? 38.797  47.900  5.524   1.00 13.54 ? 149  PRO B CG    1 
ATOM   5179  C CD    . PRO B  1  149 ? 40.079  47.219  6.008   1.00 13.08 ? 149  PRO B CD    1 
ATOM   5180  N N     . ASN B  1  150 ? 39.425  51.769  6.837   1.00 14.96 ? 150  ASN B N     1 
ATOM   5181  C CA    . ASN B  1  150 ? 38.736  52.729  7.695   1.00 15.52 ? 150  ASN B CA    1 
ATOM   5182  C C     . ASN B  1  150 ? 37.268  52.361  7.563   1.00 16.09 ? 150  ASN B C     1 
ATOM   5183  O O     . ASN B  1  150 ? 36.875  51.722  6.585   1.00 15.10 ? 150  ASN B O     1 
ATOM   5184  C CB    . ASN B  1  150 ? 38.892  54.155  7.159   1.00 17.78 ? 150  ASN B CB    1 
ATOM   5185  C CG    . ASN B  1  150 ? 40.305  54.686  7.266   1.00 18.76 ? 150  ASN B CG    1 
ATOM   5186  O OD1   . ASN B  1  150 ? 40.725  55.507  6.451   1.00 23.77 ? 150  ASN B OD1   1 
ATOM   5187  N ND2   . ASN B  1  150 ? 41.035  54.246  8.281   1.00 19.05 ? 150  ASN B ND2   1 
ATOM   5188  N N     . SER B  1  151 ? 36.452  52.750  8.532   1.00 16.36 ? 151  SER B N     1 
ATOM   5189  C CA    . SER B  1  151 ? 35.029  52.479  8.418   1.00 16.08 ? 151  SER B CA    1 
ATOM   5190  C C     . SER B  1  151 ? 34.552  53.508  7.395   1.00 14.76 ? 151  SER B C     1 
ATOM   5191  O O     . SER B  1  151 ? 35.048  54.639  7.369   1.00 14.07 ? 151  SER B O     1 
ATOM   5192  C CB    . SER B  1  151 ? 34.321  52.693  9.757   1.00 17.90 ? 151  SER B CB    1 
ATOM   5193  O OG    . SER B  1  151 ? 34.400  54.044  10.166  1.00 22.16 ? 151  SER B OG    1 
ATOM   5194  N N     . GLN B  1  152 ? 33.617  53.111  6.538   1.00 12.84 ? 152  GLN B N     1 
ATOM   5195  C CA    . GLN B  1  152 ? 33.078  54.003  5.514   1.00 12.57 ? 152  GLN B CA    1 
ATOM   5196  C C     . GLN B  1  152 ? 31.563  53.870  5.512   1.00 12.28 ? 152  GLN B C     1 
ATOM   5197  O O     . GLN B  1  152 ? 31.030  52.762  5.445   1.00 11.19 ? 152  GLN B O     1 
ATOM   5198  C CB    . GLN B  1  152 ? 33.616  53.630  4.133   1.00 13.03 ? 152  GLN B CB    1 
ATOM   5199  C CG    . GLN B  1  152 ? 35.126  53.550  4.039   1.00 12.47 ? 152  GLN B CG    1 
ATOM   5200  C CD    . GLN B  1  152 ? 35.579  53.077  2.675   1.00 12.54 ? 152  GLN B CD    1 
ATOM   5201  O OE1   . GLN B  1  152 ? 35.838  53.878  1.777   1.00 10.28 ? 152  GLN B OE1   1 
ATOM   5202  N NE2   . GLN B  1  152 ? 35.655  51.764  2.506   1.00 13.18 ? 152  GLN B NE2   1 
ATOM   5203  N N     . SER B  1  153 ? 30.873  55.004  5.572   1.00 12.46 ? 153  SER B N     1 
ATOM   5204  C CA    . SER B  1  153 ? 29.417  55.011  5.607   1.00 12.12 ? 153  SER B CA    1 
ATOM   5205  C C     . SER B  1  153 ? 28.732  54.139  4.562   1.00 11.29 ? 153  SER B C     1 
ATOM   5206  O O     . SER B  1  153 ? 27.930  53.275  4.913   1.00 12.60 ? 153  SER B O     1 
ATOM   5207  C CB    . SER B  1  153 ? 28.892  56.442  5.487   1.00 13.02 ? 153  SER B CB    1 
ATOM   5208  O OG    . SER B  1  153 ? 27.476  56.455  5.554   1.00 13.08 ? 153  SER B OG    1 
ATOM   5209  N N     . TRP B  1  154 ? 29.032  54.346  3.282   1.00 11.34 ? 154  TRP B N     1 
ATOM   5210  C CA    . TRP B  1  154 ? 28.365  53.539  2.269   1.00 9.24  ? 154  TRP B CA    1 
ATOM   5211  C C     . TRP B  1  154 ? 28.660  52.048  2.384   1.00 9.84  ? 154  TRP B C     1 
ATOM   5212  O O     . TRP B  1  154 ? 27.776  51.222  2.149   1.00 9.15  ? 154  TRP B O     1 
ATOM   5213  C CB    . TRP B  1  154 ? 28.696  54.013  0.853   1.00 10.03 ? 154  TRP B CB    1 
ATOM   5214  C CG    . TRP B  1  154 ? 27.876  53.276  -0.153  1.00 10.09 ? 154  TRP B CG    1 
ATOM   5215  C CD1   . TRP B  1  154 ? 28.306  52.311  -1.022  1.00 10.66 ? 154  TRP B CD1   1 
ATOM   5216  C CD2   . TRP B  1  154 ? 26.455  53.357  -0.316  1.00 10.14 ? 154  TRP B CD2   1 
ATOM   5217  N NE1   . TRP B  1  154 ? 27.240  51.785  -1.709  1.00 10.88 ? 154  TRP B NE1   1 
ATOM   5218  C CE2   . TRP B  1  154 ? 26.091  52.408  -1.296  1.00 9.65  ? 154  TRP B CE2   1 
ATOM   5219  C CE3   . TRP B  1  154 ? 25.452  54.139  0.274   1.00 12.71 ? 154  TRP B CE3   1 
ATOM   5220  C CZ2   . TRP B  1  154 ? 24.765  52.218  -1.700  1.00 10.43 ? 154  TRP B CZ2   1 
ATOM   5221  C CZ3   . TRP B  1  154 ? 24.132  53.950  -0.129  1.00 11.26 ? 154  TRP B CZ3   1 
ATOM   5222  C CH2   . TRP B  1  154 ? 23.802  52.997  -1.107  1.00 12.02 ? 154  TRP B CH2   1 
ATOM   5223  N N     . GLN B  1  155 ? 29.892  51.692  2.731   1.00 9.83  ? 155  GLN B N     1 
ATOM   5224  C CA    . GLN B  1  155 ? 30.210  50.277  2.879   1.00 9.99  ? 155  GLN B CA    1 
ATOM   5225  C C     . GLN B  1  155 ? 29.415  49.713  4.059   1.00 10.27 ? 155  GLN B C     1 
ATOM   5226  O O     . GLN B  1  155 ? 28.948  48.574  4.011   1.00 9.72  ? 155  GLN B O     1 
ATOM   5227  C CB    . GLN B  1  155 ? 31.714  50.076  3.093   1.00 9.34  ? 155  GLN B CB    1 
ATOM   5228  C CG    . GLN B  1  155 ? 32.560  50.436  1.873   1.00 9.87  ? 155  GLN B CG    1 
ATOM   5229  C CD    . GLN B  1  155 ? 32.188  49.618  0.644   1.00 9.05  ? 155  GLN B CD    1 
ATOM   5230  O OE1   . GLN B  1  155 ? 32.260  48.391  0.658   1.00 9.38  ? 155  GLN B OE1   1 
ATOM   5231  N NE2   . GLN B  1  155 ? 31.787  50.296  -0.422  1.00 8.03  ? 155  GLN B NE2   1 
ATOM   5232  N N     . SER B  1  156 ? 29.244  50.512  5.111   1.00 10.37 ? 156  SER B N     1 
ATOM   5233  C CA    . SER B  1  156 ? 28.480  50.068  6.275   1.00 11.04 ? 156  SER B CA    1 
ATOM   5234  C C     . SER B  1  156 ? 27.014  49.882  5.900   1.00 10.86 ? 156  SER B C     1 
ATOM   5235  O O     . SER B  1  156 ? 26.354  48.953  6.371   1.00 10.47 ? 156  SER B O     1 
ATOM   5236  C CB    . SER B  1  156 ? 28.600  51.078  7.421   1.00 10.11 ? 156  SER B CB    1 
ATOM   5237  O OG    . SER B  1  156 ? 29.902  51.061  7.979   1.00 12.30 ? 156  SER B OG    1 
ATOM   5238  N N     . VAL B  1  157 ? 26.501  50.766  5.050   1.00 10.69 ? 157  VAL B N     1 
ATOM   5239  C CA    . VAL B  1  157 ? 25.120  50.660  4.604   1.00 10.74 ? 157  VAL B CA    1 
ATOM   5240  C C     . VAL B  1  157 ? 24.976  49.356  3.826   1.00 11.12 ? 157  VAL B C     1 
ATOM   5241  O O     . VAL B  1  157 ? 24.009  48.613  3.994   1.00 11.08 ? 157  VAL B O     1 
ATOM   5242  C CB    . VAL B  1  157 ? 24.738  51.842  3.691   1.00 11.88 ? 157  VAL B CB    1 
ATOM   5243  C CG1   . VAL B  1  157 ? 23.381  51.597  3.052   1.00 13.04 ? 157  VAL B CG1   1 
ATOM   5244  C CG2   . VAL B  1  157 ? 24.716  53.128  4.503   1.00 14.37 ? 157  VAL B CG2   1 
ATOM   5245  N N     . THR B  1  158 ? 25.960  49.078  2.978   1.00 9.43  ? 158  THR B N     1 
ATOM   5246  C CA    . THR B  1  158 ? 25.956  47.864  2.179   1.00 8.57  ? 158  THR B CA    1 
ATOM   5247  C C     . THR B  1  158 ? 25.997  46.637  3.092   1.00 8.53  ? 158  THR B C     1 
ATOM   5248  O O     . THR B  1  158 ? 25.309  45.648  2.847   1.00 8.74  ? 158  THR B O     1 
ATOM   5249  C CB    . THR B  1  158 ? 27.159  47.858  1.216   1.00 8.72  ? 158  THR B CB    1 
ATOM   5250  O OG1   . THR B  1  158 ? 27.053  48.983  0.332   1.00 9.54  ? 158  THR B OG1   1 
ATOM   5251  C CG2   . THR B  1  158 ? 27.189  46.588  0.389   1.00 9.49  ? 158  THR B CG2   1 
ATOM   5252  N N     . LYS B  1  159 ? 26.802  46.700  4.147   1.00 8.37  ? 159  LYS B N     1 
ATOM   5253  C CA    . LYS B  1  159 ? 26.894  45.585  5.085   1.00 8.08  ? 159  LYS B CA    1 
ATOM   5254  C C     . LYS B  1  159 ? 25.529  45.318  5.725   1.00 8.83  ? 159  LYS B C     1 
ATOM   5255  O O     . LYS B  1  159 ? 25.119  44.165  5.864   1.00 7.80  ? 159  LYS B O     1 
ATOM   5256  C CB    . LYS B  1  159 ? 27.943  45.887  6.159   1.00 8.60  ? 159  LYS B CB    1 
ATOM   5257  C CG    . LYS B  1  159 ? 28.008  44.889  7.313   1.00 8.66  ? 159  LYS B CG    1 
ATOM   5258  C CD    . LYS B  1  159 ? 29.245  45.163  8.172   1.00 8.58  ? 159  LYS B CD    1 
ATOM   5259  C CE    . LYS B  1  159 ? 29.239  44.360  9.469   1.00 8.32  ? 159  LYS B CE    1 
ATOM   5260  N NZ    . LYS B  1  159 ? 30.519  44.566  10.213  1.00 9.22  ? 159  LYS B NZ    1 
ATOM   5261  N N     . THR B  1  160 ? 24.817  46.377  6.104   1.00 8.54  ? 160  THR B N     1 
ATOM   5262  C CA    . THR B  1  160 ? 23.504  46.184  6.711   1.00 9.03  ? 160  THR B CA    1 
ATOM   5263  C C     . THR B  1  160 ? 22.547  45.557  5.699   1.00 8.45  ? 160  THR B C     1 
ATOM   5264  O O     . THR B  1  160 ? 21.730  44.707  6.051   1.00 9.27  ? 160  THR B O     1 
ATOM   5265  C CB    . THR B  1  160 ? 22.899  47.515  7.243   1.00 10.77 ? 160  THR B CB    1 
ATOM   5266  O OG1   . THR B  1  160 ? 22.611  48.400  6.154   1.00 14.96 ? 160  THR B OG1   1 
ATOM   5267  C CG2   . THR B  1  160 ? 23.874  48.193  8.194   1.00 9.16  ? 160  THR B CG2   1 
ATOM   5268  N N     . ALA B  1  161 ? 22.664  45.962  4.436   1.00 7.86  ? 161  ALA B N     1 
ATOM   5269  C CA    . ALA B  1  161 ? 21.805  45.428  3.380   1.00 8.91  ? 161  ALA B CA    1 
ATOM   5270  C C     . ALA B  1  161 ? 22.051  43.933  3.180   1.00 9.56  ? 161  ALA B C     1 
ATOM   5271  O O     . ALA B  1  161 ? 21.108  43.147  3.093   1.00 9.26  ? 161  ALA B O     1 
ATOM   5272  C CB    . ALA B  1  161 ? 22.054  46.181  2.084   1.00 9.95  ? 161  ALA B CB    1 
ATOM   5273  N N     . PHE B  1  162 ? 23.322  43.546  3.102   1.00 9.47  ? 162  PHE B N     1 
ATOM   5274  C CA    . PHE B  1  162 ? 23.687  42.142  2.933   1.00 9.09  ? 162  PHE B CA    1 
ATOM   5275  C C     . PHE B  1  162 ? 23.158  41.291  4.090   1.00 9.60  ? 162  PHE B C     1 
ATOM   5276  O O     . PHE B  1  162 ? 22.593  40.221  3.873   1.00 8.59  ? 162  PHE B O     1 
ATOM   5277  C CB    . PHE B  1  162 ? 25.214  41.991  2.852   1.00 8.43  ? 162  PHE B CB    1 
ATOM   5278  C CG    . PHE B  1  162 ? 25.783  42.180  1.469   1.00 8.87  ? 162  PHE B CG    1 
ATOM   5279  C CD1   . PHE B  1  162 ? 26.917  42.963  1.275   1.00 10.18 ? 162  PHE B CD1   1 
ATOM   5280  C CD2   . PHE B  1  162 ? 25.206  41.555  0.365   1.00 11.39 ? 162  PHE B CD2   1 
ATOM   5281  C CE1   . PHE B  1  162 ? 27.473  43.123  0.004   1.00 9.98  ? 162  PHE B CE1   1 
ATOM   5282  C CE2   . PHE B  1  162 ? 25.756  41.708  -0.913  1.00 9.61  ? 162  PHE B CE2   1 
ATOM   5283  C CZ    . PHE B  1  162 ? 26.891  42.495  -1.091  1.00 11.04 ? 162  PHE B CZ    1 
ATOM   5284  N N     . LEU B  1  163 ? 23.342  41.763  5.321   1.00 8.54  ? 163  LEU B N     1 
ATOM   5285  C CA    . LEU B  1  163 ? 22.871  41.009  6.481   1.00 8.92  ? 163  LEU B CA    1 
ATOM   5286  C C     . LEU B  1  163 ? 21.346  40.937  6.521   1.00 9.59  ? 163  LEU B C     1 
ATOM   5287  O O     . LEU B  1  163 ? 20.770  39.924  6.924   1.00 9.31  ? 163  LEU B O     1 
ATOM   5288  C CB    . LEU B  1  163 ? 23.425  41.629  7.771   1.00 8.07  ? 163  LEU B CB    1 
ATOM   5289  C CG    . LEU B  1  163 ? 24.951  41.511  7.891   1.00 9.16  ? 163  LEU B CG    1 
ATOM   5290  C CD1   . LEU B  1  163 ? 25.438  42.258  9.125   1.00 12.50 ? 163  LEU B CD1   1 
ATOM   5291  C CD2   . LEU B  1  163 ? 25.349  40.038  7.960   1.00 10.76 ? 163  LEU B CD2   1 
ATOM   5292  N N     . GLU B  1  164 ? 20.690  42.006  6.088   1.00 9.84  ? 164  GLU B N     1 
ATOM   5293  C CA    . GLU B  1  164 ? 19.238  42.019  6.070   1.00 10.59 ? 164  GLU B CA    1 
ATOM   5294  C C     . GLU B  1  164 ? 18.747  41.036  5.007   1.00 10.35 ? 164  GLU B C     1 
ATOM   5295  O O     . GLU B  1  164 ? 17.708  40.398  5.172   1.00 11.52 ? 164  GLU B O     1 
ATOM   5296  C CB    . GLU B  1  164 ? 18.721  43.427  5.765   1.00 10.99 ? 164  GLU B CB    1 
ATOM   5297  C CG    . GLU B  1  164 ? 17.389  43.740  6.421   1.00 13.21 ? 164  GLU B CG    1 
ATOM   5298  C CD    . GLU B  1  164 ? 16.828  45.084  6.000   1.00 11.24 ? 164  GLU B CD    1 
ATOM   5299  O OE1   . GLU B  1  164 ? 17.541  46.102  6.142   1.00 12.97 ? 164  GLU B OE1   1 
ATOM   5300  O OE2   . GLU B  1  164 ? 15.672  45.118  5.529   1.00 14.06 ? 164  GLU B OE2   1 
ATOM   5301  N N     . ALA B  1  165 ? 19.513  40.903  3.924   1.00 10.65 ? 165  ALA B N     1 
ATOM   5302  C CA    . ALA B  1  165 ? 19.155  40.007  2.823   1.00 9.77  ? 165  ALA B CA    1 
ATOM   5303  C C     . ALA B  1  165 ? 19.608  38.554  2.981   1.00 11.21 ? 165  ALA B C     1 
ATOM   5304  O O     . ALA B  1  165 ? 19.658  37.806  2.005   1.00 11.42 ? 165  ALA B O     1 
ATOM   5305  C CB    . ALA B  1  165 ? 19.679  40.574  1.504   1.00 8.75  ? 165  ALA B CB    1 
ATOM   5306  N N     . GLY B  1  166 ? 19.961  38.159  4.200   1.00 9.77  ? 166  GLY B N     1 
ATOM   5307  C CA    . GLY B  1  166 ? 20.353  36.781  4.441   1.00 8.90  ? 166  GLY B CA    1 
ATOM   5308  C C     . GLY B  1  166 ? 21.723  36.292  4.004   1.00 8.58  ? 166  GLY B C     1 
ATOM   5309  O O     . GLY B  1  166 ? 21.937  35.079  3.919   1.00 9.53  ? 166  GLY B O     1 
ATOM   5310  N N     . VAL B  1  167 ? 22.651  37.197  3.715   1.00 8.61  ? 167  VAL B N     1 
ATOM   5311  C CA    . VAL B  1  167 ? 23.993  36.769  3.326   1.00 8.88  ? 167  VAL B CA    1 
ATOM   5312  C C     . VAL B  1  167 ? 24.709  36.545  4.658   1.00 9.27  ? 167  VAL B C     1 
ATOM   5313  O O     . VAL B  1  167 ? 25.403  37.422  5.173   1.00 9.97  ? 167  VAL B O     1 
ATOM   5314  C CB    . VAL B  1  167 ? 24.710  37.846  2.486   1.00 10.50 ? 167  VAL B CB    1 
ATOM   5315  C CG1   . VAL B  1  167 ? 26.063  37.319  2.009   1.00 9.63  ? 167  VAL B CG1   1 
ATOM   5316  C CG2   . VAL B  1  167 ? 23.849  38.218  1.292   1.00 11.94 ? 167  VAL B CG2   1 
ATOM   5317  N N     . HIS B  1  168 ? 24.515  35.347  5.200   1.00 9.35  ? 168  HIS B N     1 
ATOM   5318  C CA    . HIS B  1  168 ? 25.049  34.965  6.502   1.00 9.56  ? 168  HIS B CA    1 
ATOM   5319  C C     . HIS B  1  168 ? 26.099  33.860  6.453   1.00 9.88  ? 168  HIS B C     1 
ATOM   5320  O O     . HIS B  1  168 ? 26.180  33.102  5.482   1.00 11.23 ? 168  HIS B O     1 
ATOM   5321  C CB    . HIS B  1  168 ? 23.883  34.530  7.390   1.00 8.90  ? 168  HIS B CB    1 
ATOM   5322  C CG    . HIS B  1  168 ? 22.824  35.576  7.544   1.00 8.10  ? 168  HIS B CG    1 
ATOM   5323  N ND1   . HIS B  1  168 ? 21.544  35.284  7.965   1.00 9.75  ? 168  HIS B ND1   1 
ATOM   5324  C CD2   . HIS B  1  168 ? 22.861  36.917  7.357   1.00 9.34  ? 168  HIS B CD2   1 
ATOM   5325  C CE1   . HIS B  1  168 ? 20.840  36.399  8.031   1.00 10.30 ? 168  HIS B CE1   1 
ATOM   5326  N NE2   . HIS B  1  168 ? 21.616  37.405  7.667   1.00 9.12  ? 168  HIS B NE2   1 
ATOM   5327  N N     . PRO B  1  169 ? 26.907  33.741  7.519   1.00 10.09 ? 169  PRO B N     1 
ATOM   5328  C CA    . PRO B  1  169 ? 26.881  34.585  8.721   1.00 8.86  ? 169  PRO B CA    1 
ATOM   5329  C C     . PRO B  1  169 ? 27.693  35.865  8.543   1.00 10.45 ? 169  PRO B C     1 
ATOM   5330  O O     . PRO B  1  169 ? 28.154  36.173  7.444   1.00 9.81  ? 169  PRO B O     1 
ATOM   5331  C CB    . PRO B  1  169 ? 27.504  33.677  9.771   1.00 10.66 ? 169  PRO B CB    1 
ATOM   5332  C CG    . PRO B  1  169 ? 28.582  32.998  8.975   1.00 8.46  ? 169  PRO B CG    1 
ATOM   5333  C CD    . PRO B  1  169 ? 27.854  32.624  7.691   1.00 10.23 ? 169  PRO B CD    1 
ATOM   5334  N N     . ASN B  1  170 ? 27.858  36.606  9.634   1.00 9.21  ? 170  ASN B N     1 
ATOM   5335  C CA    . ASN B  1  170 ? 28.664  37.825  9.622   1.00 10.24 ? 170  ASN B CA    1 
ATOM   5336  C C     . ASN B  1  170 ? 30.035  37.405  10.142  1.00 11.62 ? 170  ASN B C     1 
ATOM   5337  O O     . ASN B  1  170 ? 30.127  36.707  11.151  1.00 13.40 ? 170  ASN B O     1 
ATOM   5338  C CB    . ASN B  1  170 ? 28.056  38.891  10.540  1.00 9.91  ? 170  ASN B CB    1 
ATOM   5339  C CG    . ASN B  1  170 ? 28.978  40.081  10.741  1.00 10.20 ? 170  ASN B CG    1 
ATOM   5340  O OD1   . ASN B  1  170 ? 29.819  40.379  9.894   1.00 9.77  ? 170  ASN B OD1   1 
ATOM   5341  N ND2   . ASN B  1  170 ? 28.816  40.772  11.860  1.00 10.22 ? 170  ASN B ND2   1 
ATOM   5342  N N     . HIS B  1  171 ? 31.096  37.815  9.450   1.00 10.27 ? 171  HIS B N     1 
ATOM   5343  C CA    . HIS B  1  171 ? 32.457  37.452  9.846   1.00 11.28 ? 171  HIS B CA    1 
ATOM   5344  C C     . HIS B  1  171 ? 33.246  38.618  10.431  1.00 12.11 ? 171  HIS B C     1 
ATOM   5345  O O     . HIS B  1  171 ? 34.428  38.466  10.746  1.00 12.55 ? 171  HIS B O     1 
ATOM   5346  C CB    . HIS B  1  171 ? 33.221  36.904  8.637   1.00 11.73 ? 171  HIS B CB    1 
ATOM   5347  C CG    . HIS B  1  171 ? 32.639  35.648  8.073   1.00 10.60 ? 171  HIS B CG    1 
ATOM   5348  N ND1   . HIS B  1  171 ? 32.843  34.411  8.646   1.00 11.58 ? 171  HIS B ND1   1 
ATOM   5349  C CD2   . HIS B  1  171 ? 31.839  35.439  7.001   1.00 11.43 ? 171  HIS B CD2   1 
ATOM   5350  C CE1   . HIS B  1  171 ? 32.193  33.495  7.952   1.00 12.71 ? 171  HIS B CE1   1 
ATOM   5351  N NE2   . HIS B  1  171 ? 31.575  34.093  6.949   1.00 10.53 ? 171  HIS B NE2   1 
ATOM   5352  N N     . GLY B  1  172 ? 32.598  39.770  10.584  1.00 10.35 ? 172  GLY B N     1 
ATOM   5353  C CA    . GLY B  1  172 ? 33.289  40.937  11.106  1.00 10.84 ? 172  GLY B CA    1 
ATOM   5354  C C     . GLY B  1  172 ? 34.394  41.281  10.128  1.00 9.71  ? 172  GLY B C     1 
ATOM   5355  O O     . GLY B  1  172 ? 34.153  41.312  8.923   1.00 10.21 ? 172  GLY B O     1 
ATOM   5356  N N     . PHE B  1  173 ? 35.595  41.557  10.626  1.00 9.02  ? 173  PHE B N     1 
ATOM   5357  C CA    . PHE B  1  173 ? 36.715  41.840  9.736   1.00 8.33  ? 173  PHE B CA    1 
ATOM   5358  C C     . PHE B  1  173 ? 37.486  40.543  9.550   1.00 9.48  ? 173  PHE B C     1 
ATOM   5359  O O     . PHE B  1  173 ? 37.951  39.943  10.523  1.00 10.16 ? 173  PHE B O     1 
ATOM   5360  C CB    . PHE B  1  173 ? 37.664  42.886  10.320  1.00 8.82  ? 173  PHE B CB    1 
ATOM   5361  C CG    . PHE B  1  173 ? 38.919  43.067  9.504   1.00 8.08  ? 173  PHE B CG    1 
ATOM   5362  C CD1   . PHE B  1  173 ? 38.857  43.608  8.223   1.00 8.97  ? 173  PHE B CD1   1 
ATOM   5363  C CD2   . PHE B  1  173 ? 40.151  42.648  9.993   1.00 10.06 ? 173  PHE B CD2   1 
ATOM   5364  C CE1   . PHE B  1  173 ? 40.007  43.726  7.436   1.00 9.40  ? 173  PHE B CE1   1 
ATOM   5365  C CE2   . PHE B  1  173 ? 41.306  42.760  9.218   1.00 10.93 ? 173  PHE B CE2   1 
ATOM   5366  C CZ    . PHE B  1  173 ? 41.235  43.299  7.936   1.00 10.10 ? 173  PHE B CZ    1 
ATOM   5367  N N     . SER B  1  174 ? 37.632  40.119  8.300   1.00 8.15  ? 174  SER B N     1 
ATOM   5368  C CA    . SER B  1  174 ? 38.337  38.878  7.999   1.00 7.80  ? 174  SER B CA    1 
ATOM   5369  C C     . SER B  1  174 ? 38.834  38.880  6.563   1.00 8.91  ? 174  SER B C     1 
ATOM   5370  O O     . SER B  1  174 ? 38.150  39.366  5.667   1.00 9.66  ? 174  SER B O     1 
ATOM   5371  C CB    . SER B  1  174 ? 37.406  37.684  8.214   1.00 9.39  ? 174  SER B CB    1 
ATOM   5372  O OG    . SER B  1  174 ? 38.047  36.472  7.860   1.00 12.41 ? 174  SER B OG    1 
ATOM   5373  N N     . LEU B  1  175 ? 40.024  38.325  6.353   1.00 9.10  ? 175  LEU B N     1 
ATOM   5374  C CA    . LEU B  1  175 ? 40.621  38.266  5.024   1.00 8.40  ? 175  LEU B CA    1 
ATOM   5375  C C     . LEU B  1  175 ? 40.187  37.036  4.232   1.00 9.09  ? 175  LEU B C     1 
ATOM   5376  O O     . LEU B  1  175 ? 40.367  36.978  3.016   1.00 9.90  ? 175  LEU B O     1 
ATOM   5377  C CB    . LEU B  1  175 ? 42.146  38.244  5.140   1.00 8.86  ? 175  LEU B CB    1 
ATOM   5378  C CG    . LEU B  1  175 ? 42.843  39.383  5.884   1.00 9.94  ? 175  LEU B CG    1 
ATOM   5379  C CD1   . LEU B  1  175 ? 44.342  39.134  5.881   1.00 11.16 ? 175  LEU B CD1   1 
ATOM   5380  C CD2   . LEU B  1  175 ? 42.520  40.708  5.222   1.00 10.15 ? 175  LEU B CD2   1 
ATOM   5381  N N     . ASP B  1  176 ? 39.614  36.059  4.922   1.00 8.14  ? 176  ASP B N     1 
ATOM   5382  C CA    . ASP B  1  176 ? 39.216  34.810  4.286   1.00 8.28  ? 176  ASP B CA    1 
ATOM   5383  C C     . ASP B  1  176 ? 37.936  34.783  3.472   1.00 7.97  ? 176  ASP B C     1 
ATOM   5384  O O     . ASP B  1  176 ? 36.899  35.309  3.882   1.00 9.37  ? 176  ASP B O     1 
ATOM   5385  C CB    . ASP B  1  176 ? 39.161  33.705  5.336   1.00 8.98  ? 176  ASP B CB    1 
ATOM   5386  C CG    . ASP B  1  176 ? 40.527  33.354  5.868   1.00 11.22 ? 176  ASP B CG    1 
ATOM   5387  O OD1   . ASP B  1  176 ? 41.374  32.914  5.063   1.00 12.51 ? 176  ASP B OD1   1 
ATOM   5388  O OD2   . ASP B  1  176 ? 40.755  33.519  7.083   1.00 13.50 ? 176  ASP B OD2   1 
ATOM   5389  N N     . HIS B  1  177 ? 38.028  34.139  2.313   1.00 8.77  ? 177  HIS B N     1 
ATOM   5390  C CA    . HIS B  1  177 ? 36.892  33.987  1.416   1.00 9.43  ? 177  HIS B CA    1 
ATOM   5391  C C     . HIS B  1  177 ? 35.973  32.916  1.999   1.00 9.08  ? 177  HIS B C     1 
ATOM   5392  O O     . HIS B  1  177 ? 36.231  31.718  1.855   1.00 11.88 ? 177  HIS B O     1 
ATOM   5393  C CB    . HIS B  1  177 ? 37.366  33.545  0.029   1.00 8.49  ? 177  HIS B CB    1 
ATOM   5394  C CG    . HIS B  1  177 ? 36.247  33.274  -0.929  1.00 9.01  ? 177  HIS B CG    1 
ATOM   5395  N ND1   . HIS B  1  177 ? 35.708  34.247  -1.740  1.00 8.88  ? 177  HIS B ND1   1 
ATOM   5396  C CD2   . HIS B  1  177 ? 35.532  32.147  -1.164  1.00 9.81  ? 177  HIS B CD2   1 
ATOM   5397  C CE1   . HIS B  1  177 ? 34.706  33.733  -2.435  1.00 7.53  ? 177  HIS B CE1   1 
ATOM   5398  N NE2   . HIS B  1  177 ? 34.579  32.462  -2.104  1.00 8.70  ? 177  HIS B NE2   1 
ATOM   5399  N N     . GLU B  1  178 ? 34.908  33.350  2.664   1.00 9.34  ? 178  GLU B N     1 
ATOM   5400  C CA    . GLU B  1  178 ? 33.946  32.434  3.260   1.00 9.25  ? 178  GLU B CA    1 
ATOM   5401  C C     . GLU B  1  178 ? 32.534  32.925  2.980   1.00 8.58  ? 178  GLU B C     1 
ATOM   5402  O O     . GLU B  1  178 ? 32.295  34.128  2.865   1.00 9.70  ? 178  GLU B O     1 
ATOM   5403  C CB    . GLU B  1  178 ? 34.123  32.357  4.780   1.00 11.13 ? 178  GLU B CB    1 
ATOM   5404  C CG    . GLU B  1  178 ? 35.489  31.919  5.257   1.00 13.02 ? 178  GLU B CG    1 
ATOM   5405  C CD    . GLU B  1  178 ? 35.533  31.782  6.769   1.00 13.20 ? 178  GLU B CD    1 
ATOM   5406  O OE1   . GLU B  1  178 ? 35.081  30.741  7.289   1.00 16.61 ? 178  GLU B OE1   1 
ATOM   5407  O OE2   . GLU B  1  178 ? 36.000  32.725  7.440   1.00 14.12 ? 178  GLU B OE2   1 
ATOM   5408  N N     . GLU B  1  179 ? 31.602  31.987  2.887   1.00 8.50  ? 179  GLU B N     1 
ATOM   5409  C CA    . GLU B  1  179 ? 30.206  32.332  2.658   1.00 8.50  ? 179  GLU B CA    1 
ATOM   5410  C C     . GLU B  1  179 ? 29.736  33.251  3.780   1.00 9.50  ? 179  GLU B C     1 
ATOM   5411  O O     . GLU B  1  179 ? 29.995  32.992  4.958   1.00 9.20  ? 179  GLU B O     1 
ATOM   5412  C CB    . GLU B  1  179 ? 29.352  31.060  2.620   1.00 9.59  ? 179  GLU B CB    1 
ATOM   5413  C CG    . GLU B  1  179 ? 27.855  31.313  2.586   1.00 15.99 ? 179  GLU B CG    1 
ATOM   5414  C CD    . GLU B  1  179 ? 27.052  30.033  2.517   1.00 19.18 ? 179  GLU B CD    1 
ATOM   5415  O OE1   . GLU B  1  179 ? 27.616  28.960  2.824   1.00 23.10 ? 179  GLU B OE1   1 
ATOM   5416  O OE2   . GLU B  1  179 ? 25.854  30.104  2.174   1.00 20.77 ? 179  GLU B OE2   1 
ATOM   5417  N N     . GLY B  1  180 ? 29.050  34.326  3.409   1.00 8.24  ? 180  GLY B N     1 
ATOM   5418  C CA    . GLY B  1  180 ? 28.562  35.268  4.397   1.00 9.10  ? 180  GLY B CA    1 
ATOM   5419  C C     . GLY B  1  180 ? 29.027  36.679  4.097   1.00 7.34  ? 180  GLY B C     1 
ATOM   5420  O O     . GLY B  1  180 ? 29.578  36.949  3.029   1.00 7.86  ? 180  GLY B O     1 
ATOM   5421  N N     . THR B  1  181 ? 28.810  37.581  5.048   1.00 7.99  ? 181  THR B N     1 
ATOM   5422  C CA    . THR B  1  181 ? 29.195  38.975  4.886   1.00 7.89  ? 181  THR B CA    1 
ATOM   5423  C C     . THR B  1  181 ? 30.383  39.315  5.765   1.00 8.18  ? 181  THR B C     1 
ATOM   5424  O O     . THR B  1  181 ? 30.486  38.836  6.896   1.00 8.04  ? 181  THR B O     1 
ATOM   5425  C CB    . THR B  1  181 ? 28.031  39.904  5.260   1.00 8.56  ? 181  THR B CB    1 
ATOM   5426  O OG1   . THR B  1  181 ? 26.900  39.608  4.429   1.00 8.48  ? 181  THR B OG1   1 
ATOM   5427  C CG2   . THR B  1  181 ? 28.432  41.365  5.080   1.00 10.07 ? 181  THR B CG2   1 
ATOM   5428  N N     . ARG B  1  182 ? 31.278  40.149  5.245   1.00 8.80  ? 182  ARG B N     1 
ATOM   5429  C CA    . ARG B  1  182 ? 32.454  40.549  6.003   1.00 7.22  ? 182  ARG B CA    1 
ATOM   5430  C C     . ARG B  1  182 ? 33.092  41.804  5.432   1.00 8.47  ? 182  ARG B C     1 
ATOM   5431  O O     . ARG B  1  182 ? 32.758  42.245  4.332   1.00 8.73  ? 182  ARG B O     1 
ATOM   5432  C CB    . ARG B  1  182 ? 33.502  39.427  5.987   1.00 8.01  ? 182  ARG B CB    1 
ATOM   5433  C CG    . ARG B  1  182 ? 34.334  39.343  4.693   1.00 8.80  ? 182  ARG B CG    1 
ATOM   5434  C CD    . ARG B  1  182 ? 35.332  38.192  4.760   1.00 6.69  ? 182  ARG B CD    1 
ATOM   5435  N NE    . ARG B  1  182 ? 36.384  38.259  3.745   1.00 6.36  ? 182  ARG B NE    1 
ATOM   5436  C CZ    . ARG B  1  182 ? 36.249  37.887  2.475   1.00 6.75  ? 182  ARG B CZ    1 
ATOM   5437  N NH1   . ARG B  1  182 ? 35.095  37.415  2.030   1.00 7.14  ? 182  ARG B NH1   1 
ATOM   5438  N NH2   . ARG B  1  182 ? 37.287  37.968  1.649   1.00 7.07  ? 182  ARG B NH2   1 
ATOM   5439  N N     . ILE B  1  183 ? 33.995  42.387  6.212   1.00 7.70  ? 183  ILE B N     1 
ATOM   5440  C CA    . ILE B  1  183 ? 34.772  43.536  5.776   1.00 7.28  ? 183  ILE B CA    1 
ATOM   5441  C C     . ILE B  1  183 ? 36.128  42.874  5.555   1.00 7.61  ? 183  ILE B C     1 
ATOM   5442  O O     . ILE B  1  183 ? 36.655  42.231  6.464   1.00 7.10  ? 183  ILE B O     1 
ATOM   5443  C CB    . ILE B  1  183 ? 34.912  44.605  6.880   1.00 8.15  ? 183  ILE B CB    1 
ATOM   5444  C CG1   . ILE B  1  183 ? 33.554  45.255  7.153   1.00 9.32  ? 183  ILE B CG1   1 
ATOM   5445  C CG2   . ILE B  1  183 ? 35.936  45.659  6.457   1.00 8.18  ? 183  ILE B CG2   1 
ATOM   5446  C CD1   . ILE B  1  183 ? 33.570  46.258  8.295   1.00 12.05 ? 183  ILE B CD1   1 
ATOM   5447  N N     . THR B  1  184 ? 36.679  42.998  4.352   1.00 5.69  ? 184  THR B N     1 
ATOM   5448  C CA    . THR B  1  184 ? 37.964  42.377  4.054   1.00 8.06  ? 184  THR B CA    1 
ATOM   5449  C C     . THR B  1  184 ? 39.086  43.413  3.967   1.00 7.44  ? 184  THR B C     1 
ATOM   5450  O O     . THR B  1  184 ? 38.856  44.604  4.169   1.00 9.89  ? 184  THR B O     1 
ATOM   5451  C CB    . THR B  1  184 ? 37.879  41.551  2.739   1.00 7.20  ? 184  THR B CB    1 
ATOM   5452  O OG1   . THR B  1  184 ? 39.006  40.674  2.658   1.00 9.49  ? 184  THR B OG1   1 
ATOM   5453  C CG2   . THR B  1  184 ? 37.866  42.462  1.514   1.00 7.91  ? 184  THR B CG2   1 
ATOM   5454  N N     . GLY B  1  185 ? 40.303  42.957  3.688   1.00 9.11  ? 185  GLY B N     1 
ATOM   5455  C CA    . GLY B  1  185 ? 41.426  43.875  3.595   1.00 8.72  ? 185  GLY B CA    1 
ATOM   5456  C C     . GLY B  1  185 ? 41.499  44.599  2.263   1.00 8.63  ? 185  GLY B C     1 
ATOM   5457  O O     . GLY B  1  185 ? 40.775  44.266  1.325   1.00 8.80  ? 185  GLY B O     1 
ATOM   5458  N N     . SER B  1  186 ? 42.370  45.599  2.183   1.00 8.89  ? 186  SER B N     1 
ATOM   5459  C CA    . SER B  1  186 ? 42.545  46.371  0.957   1.00 8.42  ? 186  SER B CA    1 
ATOM   5460  C C     . SER B  1  186 ? 44.012  46.735  0.746   1.00 8.22  ? 186  SER B C     1 
ATOM   5461  O O     . SER B  1  186 ? 44.775  46.840  1.710   1.00 8.28  ? 186  SER B O     1 
ATOM   5462  C CB    . SER B  1  186 ? 41.702  47.651  1.028   1.00 9.08  ? 186  SER B CB    1 
ATOM   5463  O OG    . SER B  1  186 ? 41.908  48.474  -0.108  1.00 9.89  ? 186  SER B OG    1 
ATOM   5464  N N     . THR B  1  187 ? 44.412  46.907  -0.510  1.00 8.34  ? 187  THR B N     1 
ATOM   5465  C CA    . THR B  1  187 ? 45.782  47.293  -0.805  1.00 8.71  ? 187  THR B CA    1 
ATOM   5466  C C     . THR B  1  187 ? 45.892  48.818  -0.834  1.00 9.71  ? 187  THR B C     1 
ATOM   5467  O O     . THR B  1  187 ? 46.944  49.379  -1.141  1.00 9.24  ? 187  THR B O     1 
ATOM   5468  C CB    . THR B  1  187 ? 46.301  46.659  -2.121  1.00 8.06  ? 187  THR B CB    1 
ATOM   5469  O OG1   . THR B  1  187 ? 45.300  46.740  -3.142  1.00 8.99  ? 187  THR B OG1   1 
ATOM   5470  C CG2   . THR B  1  187 ? 46.666  45.200  -1.884  1.00 8.92  ? 187  THR B CG2   1 
ATOM   5471  N N     . PHE B  1  188 ? 44.779  49.479  -0.524  1.00 10.65 ? 188  PHE B N     1 
ATOM   5472  C CA    . PHE B  1  188 ? 44.751  50.939  -0.410  1.00 10.80 ? 188  PHE B CA    1 
ATOM   5473  C C     . PHE B  1  188 ? 44.862  51.141  1.098   1.00 10.17 ? 188  PHE B C     1 
ATOM   5474  O O     . PHE B  1  188 ? 44.127  50.496  1.850   1.00 11.41 ? 188  PHE B O     1 
ATOM   5475  C CB    . PHE B  1  188 ? 43.409  51.527  -0.857  1.00 10.97 ? 188  PHE B CB    1 
ATOM   5476  C CG    . PHE B  1  188 ? 43.203  51.537  -2.338  1.00 9.91  ? 188  PHE B CG    1 
ATOM   5477  C CD1   . PHE B  1  188 ? 42.116  50.876  -2.901  1.00 10.27 ? 188  PHE B CD1   1 
ATOM   5478  C CD2   . PHE B  1  188 ? 44.078  52.224  -3.176  1.00 9.86  ? 188  PHE B CD2   1 
ATOM   5479  C CE1   . PHE B  1  188 ? 41.901  50.898  -4.275  1.00 10.11 ? 188  PHE B CE1   1 
ATOM   5480  C CE2   . PHE B  1  188 ? 43.869  52.251  -4.553  1.00 11.19 ? 188  PHE B CE2   1 
ATOM   5481  C CZ    . PHE B  1  188 ? 42.777  51.585  -5.101  1.00 10.78 ? 188  PHE B CZ    1 
ATOM   5482  N N     . ASP B  1  189 ? 45.766  52.004  1.561   1.00 10.93 ? 189  ASP B N     1 
ATOM   5483  C CA    . ASP B  1  189 ? 45.860  52.206  2.999   1.00 10.67 ? 189  ASP B CA    1 
ATOM   5484  C C     . ASP B  1  189 ? 44.840  53.228  3.497   1.00 11.58 ? 189  ASP B C     1 
ATOM   5485  O O     . ASP B  1  189 ? 44.047  53.765  2.727   1.00 11.00 ? 189  ASP B O     1 
ATOM   5486  C CB    . ASP B  1  189 ? 47.292  52.574  3.448   1.00 11.87 ? 189  ASP B CB    1 
ATOM   5487  C CG    . ASP B  1  189 ? 47.756  53.939  2.962   1.00 12.45 ? 189  ASP B CG    1 
ATOM   5488  O OD1   . ASP B  1  189 ? 46.918  54.829  2.720   1.00 11.92 ? 189  ASP B OD1   1 
ATOM   5489  O OD2   . ASP B  1  189 ? 48.990  54.123  2.853   1.00 13.89 ? 189  ASP B OD2   1 
ATOM   5490  N N     . ASN B  1  190 ? 44.866  53.492  4.794   1.00 12.08 ? 190  ASN B N     1 
ATOM   5491  C CA    . ASN B  1  190 ? 43.903  54.390  5.409   1.00 12.98 ? 190  ASN B CA    1 
ATOM   5492  C C     . ASN B  1  190 ? 43.962  55.865  5.019   1.00 13.14 ? 190  ASN B C     1 
ATOM   5493  O O     . ASN B  1  190 ? 43.100  56.651  5.419   1.00 15.01 ? 190  ASN B O     1 
ATOM   5494  C CB    . ASN B  1  190 ? 43.989  54.200  6.917   1.00 13.81 ? 190  ASN B CB    1 
ATOM   5495  C CG    . ASN B  1  190 ? 43.827  52.745  7.310   1.00 15.35 ? 190  ASN B CG    1 
ATOM   5496  O OD1   . ASN B  1  190 ? 42.734  52.299  7.645   1.00 17.57 ? 190  ASN B OD1   1 
ATOM   5497  N ND2   . ASN B  1  190 ? 44.914  51.989  7.237   1.00 19.10 ? 190  ASN B ND2   1 
ATOM   5498  N N     . LYS B  1  191 ? 44.966  56.247  4.239   1.00 12.90 ? 191  LYS B N     1 
ATOM   5499  C CA    . LYS B  1  191 ? 45.075  57.625  3.770   1.00 14.56 ? 191  LYS B CA    1 
ATOM   5500  C C     . LYS B  1  191 ? 44.748  57.650  2.280   1.00 14.89 ? 191  LYS B C     1 
ATOM   5501  O O     . LYS B  1  191 ? 44.785  58.699  1.639   1.00 16.13 ? 191  LYS B O     1 
ATOM   5502  C CB    . LYS B  1  191 ? 46.479  58.185  4.019   1.00 15.10 ? 191  LYS B CB    1 
ATOM   5503  C CG    . LYS B  1  191 ? 46.798  58.360  5.495   1.00 20.25 ? 191  LYS B CG    1 
ATOM   5504  C CD    . LYS B  1  191 ? 48.162  58.989  5.709   1.00 22.72 ? 191  LYS B CD    1 
ATOM   5505  C CE    . LYS B  1  191 ? 48.477  59.118  7.194   1.00 26.85 ? 191  LYS B CE    1 
ATOM   5506  N NZ    . LYS B  1  191 ? 49.794  59.774  7.440   1.00 29.98 ? 191  LYS B NZ    1 
ATOM   5507  N N     . GLY B  1  192 ? 44.426  56.480  1.738   1.00 14.04 ? 192  GLY B N     1 
ATOM   5508  C CA    . GLY B  1  192 ? 44.075  56.384  0.333   1.00 14.10 ? 192  GLY B CA    1 
ATOM   5509  C C     . GLY B  1  192 ? 45.241  56.070  -0.582  1.00 13.84 ? 192  GLY B C     1 
ATOM   5510  O O     . GLY B  1  192 ? 45.067  55.980  -1.794  1.00 14.84 ? 192  GLY B O     1 
ATOM   5511  N N     . THR B  1  193 ? 46.431  55.906  -0.015  1.00 12.95 ? 193  THR B N     1 
ATOM   5512  C CA    . THR B  1  193 ? 47.603  55.598  -0.820  1.00 12.77 ? 193  THR B CA    1 
ATOM   5513  C C     . THR B  1  193 ? 47.535  54.161  -1.317  1.00 12.29 ? 193  THR B C     1 
ATOM   5514  O O     . THR B  1  193 ? 47.266  53.247  -0.540  1.00 11.57 ? 193  THR B O     1 
ATOM   5515  C CB    . THR B  1  193 ? 48.895  55.764  -0.004  1.00 13.38 ? 193  THR B CB    1 
ATOM   5516  O OG1   . THR B  1  193 ? 48.989  57.113  0.472   1.00 15.96 ? 193  THR B OG1   1 
ATOM   5517  C CG2   . THR B  1  193 ? 50.108  55.447  -0.868  1.00 15.24 ? 193  THR B CG2   1 
ATOM   5518  N N     . ARG B  1  194 ? 47.771  53.963  -2.610  1.00 10.41 ? 194  ARG B N     1 
ATOM   5519  C CA    . ARG B  1  194 ? 47.760  52.617  -3.159  1.00 10.43 ? 194  ARG B CA    1 
ATOM   5520  C C     . ARG B  1  194 ? 49.095  51.937  -2.956  1.00 10.18 ? 194  ARG B C     1 
ATOM   5521  O O     . ARG B  1  194 ? 50.152  52.531  -3.181  1.00 10.42 ? 194  ARG B O     1 
ATOM   5522  C CB    . ARG B  1  194 ? 47.462  52.615  -4.661  1.00 9.48  ? 194  ARG B CB    1 
ATOM   5523  C CG    . ARG B  1  194 ? 47.334  51.194  -5.219  1.00 10.41 ? 194  ARG B CG    1 
ATOM   5524  C CD    . ARG B  1  194 ? 47.465  51.169  -6.731  1.00 10.57 ? 194  ARG B CD    1 
ATOM   5525  N NE    . ARG B  1  194 ? 46.287  51.668  -7.434  1.00 9.84  ? 194  ARG B NE    1 
ATOM   5526  C CZ    . ARG B  1  194 ? 45.168  50.977  -7.613  1.00 9.31  ? 194  ARG B CZ    1 
ATOM   5527  N NH1   . ARG B  1  194 ? 45.070  49.751  -7.129  1.00 9.89  ? 194  ARG B NH1   1 
ATOM   5528  N NH2   . ARG B  1  194 ? 44.166  51.497  -8.307  1.00 8.98  ? 194  ARG B NH2   1 
ATOM   5529  N N     . HIS B  1  195 ? 49.031  50.684  -2.533  1.00 9.30  ? 195  HIS B N     1 
ATOM   5530  C CA    . HIS B  1  195 ? 50.211  49.867  -2.347  1.00 9.22  ? 195  HIS B CA    1 
ATOM   5531  C C     . HIS B  1  195 ? 50.001  48.708  -3.313  1.00 10.37 ? 195  HIS B C     1 
ATOM   5532  O O     . HIS B  1  195 ? 48.862  48.304  -3.555  1.00 9.75  ? 195  HIS B O     1 
ATOM   5533  C CB    . HIS B  1  195 ? 50.310  49.419  -0.893  1.00 9.98  ? 195  HIS B CB    1 
ATOM   5534  C CG    . HIS B  1  195 ? 50.603  50.549  0.047   1.00 10.80 ? 195  HIS B CG    1 
ATOM   5535  N ND1   . HIS B  1  195 ? 51.879  51.012  0.274   1.00 11.86 ? 195  HIS B ND1   1 
ATOM   5536  C CD2   . HIS B  1  195 ? 49.775  51.350  0.759   1.00 11.63 ? 195  HIS B CD2   1 
ATOM   5537  C CE1   . HIS B  1  195 ? 51.827  52.053  1.090   1.00 13.57 ? 195  HIS B CE1   1 
ATOM   5538  N NE2   . HIS B  1  195 ? 50.564  52.277  1.398   1.00 12.18 ? 195  HIS B NE2   1 
ATOM   5539  N N     . ALA B  1  196 ? 51.078  48.192  -3.892  1.00 10.04 ? 196  ALA B N     1 
ATOM   5540  C CA    . ALA B  1  196 ? 50.932  47.123  -4.868  1.00 9.90  ? 196  ALA B CA    1 
ATOM   5541  C C     . ALA B  1  196 ? 52.112  46.165  -4.949  1.00 10.02 ? 196  ALA B C     1 
ATOM   5542  O O     . ALA B  1  196 ? 53.055  46.246  -4.164  1.00 9.19  ? 196  ALA B O     1 
ATOM   5543  C CB    . ALA B  1  196 ? 50.662  47.730  -6.238  1.00 9.99  ? 196  ALA B CB    1 
ATOM   5544  N N     . ALA B  1  197 ? 52.049  45.264  -5.926  1.00 9.23  ? 197  ALA B N     1 
ATOM   5545  C CA    . ALA B  1  197 ? 53.083  44.256  -6.125  1.00 9.00  ? 197  ALA B CA    1 
ATOM   5546  C C     . ALA B  1  197 ? 54.483  44.820  -6.319  1.00 7.82  ? 197  ALA B C     1 
ATOM   5547  O O     . ALA B  1  197 ? 55.464  44.181  -5.940  1.00 8.25  ? 197  ALA B O     1 
ATOM   5548  C CB    . ALA B  1  197 ? 52.715  43.363  -7.311  1.00 7.63  ? 197  ALA B CB    1 
ATOM   5549  N N     . ASP B  1  198 ? 54.588  46.009  -6.902  1.00 9.55  ? 198  ASP B N     1 
ATOM   5550  C CA    . ASP B  1  198 ? 55.905  46.591  -7.123  1.00 9.72  ? 198  ASP B CA    1 
ATOM   5551  C C     . ASP B  1  198 ? 56.650  46.770  -5.800  1.00 9.44  ? 198  ASP B C     1 
ATOM   5552  O O     . ASP B  1  198 ? 57.869  46.641  -5.747  1.00 9.58  ? 198  ASP B O     1 
ATOM   5553  C CB    . ASP B  1  198 ? 55.785  47.929  -7.870  1.00 11.70 ? 198  ASP B CB    1 
ATOM   5554  C CG    . ASP B  1  198 ? 55.047  48.985  -7.074  1.00 11.83 ? 198  ASP B CG    1 
ATOM   5555  O OD1   . ASP B  1  198 ? 53.945  48.696  -6.567  1.00 12.89 ? 198  ASP B OD1   1 
ATOM   5556  O OD2   . ASP B  1  198 ? 55.568  50.117  -6.968  1.00 11.71 ? 198  ASP B OD2   1 
ATOM   5557  N N     . GLU B  1  199 ? 55.916  47.037  -4.726  1.00 10.40 ? 199  GLU B N     1 
ATOM   5558  C CA    . GLU B  1  199 ? 56.550  47.219  -3.426  1.00 9.25  ? 199  GLU B CA    1 
ATOM   5559  C C     . GLU B  1  199 ? 57.129  45.926  -2.864  1.00 10.60 ? 199  GLU B C     1 
ATOM   5560  O O     . GLU B  1  199 ? 57.996  45.955  -1.989  1.00 11.28 ? 199  GLU B O     1 
ATOM   5561  C CB    . GLU B  1  199 ? 55.558  47.820  -2.439  1.00 9.03  ? 199  GLU B CB    1 
ATOM   5562  C CG    . GLU B  1  199 ? 55.334  49.299  -2.645  1.00 9.14  ? 199  GLU B CG    1 
ATOM   5563  C CD    . GLU B  1  199 ? 54.196  49.811  -1.808  1.00 11.22 ? 199  GLU B CD    1 
ATOM   5564  O OE1   . GLU B  1  199 ? 53.040  49.522  -2.169  1.00 11.34 ? 199  GLU B OE1   1 
ATOM   5565  O OE2   . GLU B  1  199 ? 54.455  50.480  -0.784  1.00 11.53 ? 199  GLU B OE2   1 
ATOM   5566  N N     . LEU B  1  200 ? 56.660  44.786  -3.361  1.00 8.45  ? 200  LEU B N     1 
ATOM   5567  C CA    . LEU B  1  200 ? 57.187  43.517  -2.885  1.00 9.29  ? 200  LEU B CA    1 
ATOM   5568  C C     . LEU B  1  200 ? 58.624  43.333  -3.386  1.00 9.30  ? 200  LEU B C     1 
ATOM   5569  O O     . LEU B  1  200 ? 59.359  42.478  -2.893  1.00 11.00 ? 200  LEU B O     1 
ATOM   5570  C CB    . LEU B  1  200 ? 56.284  42.363  -3.336  1.00 8.34  ? 200  LEU B CB    1 
ATOM   5571  C CG    . LEU B  1  200 ? 54.869  42.466  -2.745  1.00 9.40  ? 200  LEU B CG    1 
ATOM   5572  C CD1   . LEU B  1  200 ? 54.018  41.283  -3.193  1.00 10.33 ? 200  LEU B CD1   1 
ATOM   5573  C CD2   . LEU B  1  200 ? 54.961  42.502  -1.223  1.00 10.63 ? 200  LEU B CD2   1 
ATOM   5574  N N     . LEU B  1  201 ? 59.021  44.153  -4.357  1.00 9.51  ? 201  LEU B N     1 
ATOM   5575  C CA    . LEU B  1  201 ? 60.382  44.105  -4.897  1.00 9.25  ? 201  LEU B CA    1 
ATOM   5576  C C     . LEU B  1  201 ? 61.359  44.551  -3.807  1.00 11.34 ? 201  LEU B C     1 
ATOM   5577  O O     . LEU B  1  201 ? 62.532  44.178  -3.819  1.00 11.85 ? 201  LEU B O     1 
ATOM   5578  C CB    . LEU B  1  201 ? 60.510  45.031  -6.110  1.00 9.36  ? 201  LEU B CB    1 
ATOM   5579  C CG    . LEU B  1  201 ? 59.707  44.666  -7.364  1.00 8.93  ? 201  LEU B CG    1 
ATOM   5580  C CD1   . LEU B  1  201 ? 59.755  45.816  -8.361  1.00 8.85  ? 201  LEU B CD1   1 
ATOM   5581  C CD2   . LEU B  1  201 ? 60.269  43.397  -7.986  1.00 9.28  ? 201  LEU B CD2   1 
ATOM   5582  N N     . ASN B  1  202 ? 60.863  45.353  -2.868  1.00 12.08 ? 202  ASN B N     1 
ATOM   5583  C CA    . ASN B  1  202 ? 61.680  45.852  -1.765  1.00 12.70 ? 202  ASN B CA    1 
ATOM   5584  C C     . ASN B  1  202 ? 62.073  44.737  -0.804  1.00 13.61 ? 202  ASN B C     1 
ATOM   5585  O O     . ASN B  1  202 ? 62.976  44.908  0.018   1.00 14.34 ? 202  ASN B O     1 
ATOM   5586  C CB    . ASN B  1  202 ? 60.929  46.937  -0.988  1.00 13.04 ? 202  ASN B CB    1 
ATOM   5587  C CG    . ASN B  1  202 ? 60.659  48.169  -1.821  1.00 13.86 ? 202  ASN B CG    1 
ATOM   5588  O OD1   . ASN B  1  202 ? 61.567  48.720  -2.444  1.00 13.06 ? 202  ASN B OD1   1 
ATOM   5589  N ND2   . ASN B  1  202 ? 59.408  48.616  -1.832  1.00 14.87 ? 202  ASN B ND2   1 
ATOM   5590  N N     . LYS B  1  203 ? 61.391  43.600  -0.907  1.00 13.68 ? 203  LYS B N     1 
ATOM   5591  C CA    . LYS B  1  203 ? 61.666  42.455  -0.047  1.00 15.15 ? 203  LYS B CA    1 
ATOM   5592  C C     . LYS B  1  203 ? 62.816  41.626  -0.614  1.00 14.12 ? 203  LYS B C     1 
ATOM   5593  O O     . LYS B  1  203 ? 63.340  40.736  0.055   1.00 15.51 ? 203  LYS B O     1 
ATOM   5594  C CB    . LYS B  1  203 ? 60.417  41.578  0.080   1.00 15.90 ? 203  LYS B CB    1 
ATOM   5595  C CG    . LYS B  1  203 ? 59.191  42.288  0.643   1.00 19.03 ? 203  LYS B CG    1 
ATOM   5596  C CD    . LYS B  1  203 ? 59.305  42.542  2.141   1.00 21.08 ? 203  LYS B CD    1 
ATOM   5597  C CE    . LYS B  1  203 ? 59.234  41.249  2.936   1.00 22.64 ? 203  LYS B CE    1 
ATOM   5598  N NZ    . LYS B  1  203 ? 59.262  41.503  4.406   1.00 23.38 ? 203  LYS B NZ    1 
ATOM   5599  N N     . GLY B  1  204 ? 63.197  41.920  -1.853  1.00 15.03 ? 204  GLY B N     1 
ATOM   5600  C CA    . GLY B  1  204 ? 64.285  41.196  -2.485  1.00 14.54 ? 204  GLY B CA    1 
ATOM   5601  C C     . GLY B  1  204 ? 65.629  41.772  -2.088  1.00 16.00 ? 204  GLY B C     1 
ATOM   5602  O O     . GLY B  1  204 ? 65.697  42.715  -1.300  1.00 15.78 ? 204  GLY B O     1 
ATOM   5603  N N     . ASN B  1  205 ? 66.701  41.205  -2.633  1.00 15.33 ? 205  ASN B N     1 
ATOM   5604  C CA    . ASN B  1  205 ? 68.048  41.676  -2.333  1.00 15.75 ? 205  ASN B CA    1 
ATOM   5605  C C     . ASN B  1  205 ? 68.430  42.714  -3.384  1.00 16.57 ? 205  ASN B C     1 
ATOM   5606  O O     . ASN B  1  205 ? 68.514  42.404  -4.573  1.00 16.33 ? 205  ASN B O     1 
ATOM   5607  C CB    . ASN B  1  205 ? 69.031  40.503  -2.365  1.00 16.11 ? 205  ASN B CB    1 
ATOM   5608  C CG    . ASN B  1  205 ? 70.421  40.897  -1.911  1.00 15.66 ? 205  ASN B CG    1 
ATOM   5609  O OD1   . ASN B  1  205 ? 70.999  41.859  -2.414  1.00 17.70 ? 205  ASN B OD1   1 
ATOM   5610  N ND2   . ASN B  1  205 ? 70.968  40.150  -0.957  1.00 18.20 ? 205  ASN B ND2   1 
ATOM   5611  N N     . SER B  1  206 ? 68.656  43.947  -2.942  1.00 15.67 ? 206  SER B N     1 
ATOM   5612  C CA    . SER B  1  206 ? 68.998  45.035  -3.848  1.00 18.07 ? 206  SER B CA    1 
ATOM   5613  C C     . SER B  1  206 ? 70.303  44.848  -4.617  1.00 17.83 ? 206  SER B C     1 
ATOM   5614  O O     . SER B  1  206 ? 70.580  45.592  -5.558  1.00 19.40 ? 206  SER B O     1 
ATOM   5615  C CB    . SER B  1  206 ? 69.036  46.361  -3.083  1.00 18.96 ? 206  SER B CB    1 
ATOM   5616  O OG    . SER B  1  206 ? 69.982  46.320  -2.029  1.00 21.35 ? 206  SER B OG    1 
ATOM   5617  N N     . ASN B  1  207 ? 71.105  43.862  -4.227  1.00 17.16 ? 207  ASN B N     1 
ATOM   5618  C CA    . ASN B  1  207 ? 72.367  43.617  -4.917  1.00 16.79 ? 207  ASN B CA    1 
ATOM   5619  C C     . ASN B  1  207 ? 72.254  42.452  -5.900  1.00 15.52 ? 207  ASN B C     1 
ATOM   5620  O O     . ASN B  1  207 ? 73.169  42.212  -6.692  1.00 14.13 ? 207  ASN B O     1 
ATOM   5621  C CB    . ASN B  1  207 ? 73.482  43.328  -3.907  1.00 18.89 ? 207  ASN B CB    1 
ATOM   5622  C CG    . ASN B  1  207 ? 74.861  43.326  -4.544  1.00 21.02 ? 207  ASN B CG    1 
ATOM   5623  O OD1   . ASN B  1  207 ? 75.588  42.331  -4.480  1.00 22.62 ? 207  ASN B OD1   1 
ATOM   5624  N ND2   . ASN B  1  207 ? 75.231  44.446  -5.158  1.00 20.27 ? 207  ASN B ND2   1 
ATOM   5625  N N     . ASN B  1  208 ? 71.132  41.735  -5.857  1.00 14.12 ? 208  ASN B N     1 
ATOM   5626  C CA    . ASN B  1  208 ? 70.918  40.596  -6.750  1.00 13.81 ? 208  ASN B CA    1 
ATOM   5627  C C     . ASN B  1  208 ? 69.758  40.800  -7.717  1.00 13.38 ? 208  ASN B C     1 
ATOM   5628  O O     . ASN B  1  208 ? 69.655  40.103  -8.725  1.00 14.02 ? 208  ASN B O     1 
ATOM   5629  C CB    . ASN B  1  208 ? 70.647  39.316  -5.952  1.00 13.35 ? 208  ASN B CB    1 
ATOM   5630  C CG    . ASN B  1  208 ? 71.793  38.936  -5.042  1.00 14.17 ? 208  ASN B CG    1 
ATOM   5631  O OD1   . ASN B  1  208 ? 72.954  39.229  -5.329  1.00 16.63 ? 208  ASN B OD1   1 
ATOM   5632  N ND2   . ASN B  1  208 ? 71.475  38.260  -3.942  1.00 12.70 ? 208  ASN B ND2   1 
ATOM   5633  N N     . LEU B  1  209 ? 68.889  41.756  -7.412  1.00 12.69 ? 209  LEU B N     1 
ATOM   5634  C CA    . LEU B  1  209 ? 67.721  42.014  -8.247  1.00 12.86 ? 209  LEU B CA    1 
ATOM   5635  C C     . LEU B  1  209 ? 67.852  43.251  -9.128  1.00 14.52 ? 209  LEU B C     1 
ATOM   5636  O O     . LEU B  1  209 ? 68.252  44.313  -8.660  1.00 14.79 ? 209  LEU B O     1 
ATOM   5637  C CB    . LEU B  1  209 ? 66.484  42.160  -7.352  1.00 13.03 ? 209  LEU B CB    1 
ATOM   5638  C CG    . LEU B  1  209 ? 65.106  42.420  -7.972  1.00 13.16 ? 209  LEU B CG    1 
ATOM   5639  C CD1   . LEU B  1  209 ? 64.705  41.264  -8.883  1.00 14.65 ? 209  LEU B CD1   1 
ATOM   5640  C CD2   . LEU B  1  209 ? 64.088  42.586  -6.851  1.00 13.99 ? 209  LEU B CD2   1 
ATOM   5641  N N     . ARG B  1  210 ? 67.517  43.092  -10.407 1.00 14.11 ? 210  ARG B N     1 
ATOM   5642  C CA    . ARG B  1  210 ? 67.537  44.186  -11.374 1.00 14.06 ? 210  ARG B CA    1 
ATOM   5643  C C     . ARG B  1  210 ? 66.194  44.175  -12.086 1.00 13.83 ? 210  ARG B C     1 
ATOM   5644  O O     . ARG B  1  210 ? 65.701  43.119  -12.487 1.00 13.18 ? 210  ARG B O     1 
ATOM   5645  C CB    . ARG B  1  210 ? 68.682  44.025  -12.388 1.00 15.59 ? 210  ARG B CB    1 
ATOM   5646  C CG    . ARG B  1  210 ? 70.057  44.381  -11.822 1.00 18.50 ? 210  ARG B CG    1 
ATOM   5647  C CD    . ARG B  1  210 ? 71.209  44.053  -12.778 1.00 20.88 ? 210  ARG B CD    1 
ATOM   5648  N NE    . ARG B  1  210 ? 71.400  45.037  -13.843 0.50 23.48 ? 210  ARG B NE    1 
ATOM   5649  C CZ    . ARG B  1  210 ? 71.916  46.252  -13.669 0.50 24.15 ? 210  ARG B CZ    1 
ATOM   5650  N NH1   . ARG B  1  210 ? 72.302  46.655  -12.466 0.50 24.52 ? 210  ARG B NH1   1 
ATOM   5651  N NH2   . ARG B  1  210 ? 72.052  47.065  -14.707 0.50 25.07 ? 210  ARG B NH2   1 
ATOM   5652  N N     . VAL B  1  211 ? 65.602  45.354  -12.219 1.00 12.19 ? 211  VAL B N     1 
ATOM   5653  C CA    . VAL B  1  211 ? 64.309  45.505  -12.872 1.00 12.95 ? 211  VAL B CA    1 
ATOM   5654  C C     . VAL B  1  211 ? 64.426  46.382  -14.110 1.00 13.96 ? 211  VAL B C     1 
ATOM   5655  O O     . VAL B  1  211 ? 64.966  47.486  -14.052 1.00 13.92 ? 211  VAL B O     1 
ATOM   5656  C CB    . VAL B  1  211 ? 63.275  46.153  -11.926 1.00 12.74 ? 211  VAL B CB    1 
ATOM   5657  C CG1   . VAL B  1  211 ? 61.958  46.356  -12.657 1.00 14.11 ? 211  VAL B CG1   1 
ATOM   5658  C CG2   . VAL B  1  211 ? 63.075  45.290  -10.689 1.00 12.40 ? 211  VAL B CG2   1 
ATOM   5659  N N     . GLY B  1  212 ? 63.913  45.886  -15.230 1.00 13.32 ? 212  GLY B N     1 
ATOM   5660  C CA    . GLY B  1  212 ? 63.955  46.658  -16.453 1.00 14.37 ? 212  GLY B CA    1 
ATOM   5661  C C     . GLY B  1  212 ? 62.552  47.055  -16.866 1.00 13.76 ? 212  GLY B C     1 
ATOM   5662  O O     . GLY B  1  212 ? 61.670  46.201  -16.955 1.00 14.69 ? 212  GLY B O     1 
ATOM   5663  N N     . VAL B  1  213 ? 62.330  48.348  -17.088 1.00 12.45 ? 213  VAL B N     1 
ATOM   5664  C CA    . VAL B  1  213 ? 61.016  48.820  -17.518 1.00 12.27 ? 213  VAL B CA    1 
ATOM   5665  C C     . VAL B  1  213 ? 61.103  49.230  -18.983 1.00 12.35 ? 213  VAL B C     1 
ATOM   5666  O O     . VAL B  1  213 ? 62.199  49.410  -19.515 1.00 13.36 ? 213  VAL B O     1 
ATOM   5667  C CB    . VAL B  1  213 ? 60.515  50.012  -16.667 1.00 12.55 ? 213  VAL B CB    1 
ATOM   5668  C CG1   . VAL B  1  213 ? 60.350  49.574  -15.217 1.00 12.77 ? 213  VAL B CG1   1 
ATOM   5669  C CG2   . VAL B  1  213 ? 61.484  51.184  -16.770 1.00 13.90 ? 213  VAL B CG2   1 
ATOM   5670  N N     . HIS B  1  214 ? 59.954  49.369  -19.636 1.00 13.03 ? 214  HIS B N     1 
ATOM   5671  C CA    . HIS B  1  214 ? 59.929  49.724  -21.051 1.00 12.74 ? 214  HIS B CA    1 
ATOM   5672  C C     . HIS B  1  214 ? 60.687  48.647  -21.818 1.00 13.15 ? 214  HIS B C     1 
ATOM   5673  O O     . HIS B  1  214 ? 61.379  48.926  -22.801 1.00 12.54 ? 214  HIS B O     1 
ATOM   5674  C CB    . HIS B  1  214 ? 60.575  51.094  -21.267 1.00 14.93 ? 214  HIS B CB    1 
ATOM   5675  C CG    . HIS B  1  214 ? 59.817  52.220  -20.637 1.00 16.86 ? 214  HIS B CG    1 
ATOM   5676  N ND1   . HIS B  1  214 ? 60.432  53.363  -20.169 1.00 20.13 ? 214  HIS B ND1   1 
ATOM   5677  C CD2   . HIS B  1  214 ? 58.494  52.388  -20.409 1.00 17.97 ? 214  HIS B CD2   1 
ATOM   5678  C CE1   . HIS B  1  214 ? 59.521  54.182  -19.680 1.00 19.45 ? 214  HIS B CE1   1 
ATOM   5679  N NE2   . HIS B  1  214 ? 58.335  53.615  -19.813 1.00 18.05 ? 214  HIS B NE2   1 
ATOM   5680  N N     . ALA B  1  215 ? 60.548  47.409  -21.347 1.00 12.40 ? 215  ALA B N     1 
ATOM   5681  C CA    . ALA B  1  215 ? 61.195  46.248  -21.950 1.00 12.56 ? 215  ALA B CA    1 
ATOM   5682  C C     . ALA B  1  215 ? 60.130  45.296  -22.485 1.00 11.78 ? 215  ALA B C     1 
ATOM   5683  O O     . ALA B  1  215 ? 59.441  44.624  -21.718 1.00 12.17 ? 215  ALA B O     1 
ATOM   5684  C CB    . ALA B  1  215 ? 62.057  45.535  -20.912 1.00 11.47 ? 215  ALA B CB    1 
ATOM   5685  N N     . SER B  1  216 ? 60.002  45.244  -23.806 1.00 11.93 ? 216  SER B N     1 
ATOM   5686  C CA    . SER B  1  216 ? 59.018  44.387  -24.455 1.00 11.47 ? 216  SER B CA    1 
ATOM   5687  C C     . SER B  1  216 ? 59.626  43.035  -24.813 1.00 11.32 ? 216  SER B C     1 
ATOM   5688  O O     . SER B  1  216 ? 60.416  42.936  -25.750 1.00 11.65 ? 216  SER B O     1 
ATOM   5689  C CB    . SER B  1  216 ? 58.501  45.075  -25.721 1.00 12.07 ? 216  SER B CB    1 
ATOM   5690  O OG    . SER B  1  216 ? 57.551  44.277  -26.403 1.00 11.75 ? 216  SER B OG    1 
ATOM   5691  N N     . VAL B  1  217 ? 59.265  41.998  -24.062 1.00 10.58 ? 217  VAL B N     1 
ATOM   5692  C CA    . VAL B  1  217 ? 59.788  40.661  -24.328 1.00 11.14 ? 217  VAL B CA    1 
ATOM   5693  C C     . VAL B  1  217 ? 59.028  40.081  -25.513 1.00 11.47 ? 217  VAL B C     1 
ATOM   5694  O O     . VAL B  1  217 ? 57.807  39.910  -25.463 1.00 10.92 ? 217  VAL B O     1 
ATOM   5695  C CB    . VAL B  1  217 ? 59.639  39.744  -23.101 1.00 9.49  ? 217  VAL B CB    1 
ATOM   5696  C CG1   . VAL B  1  217 ? 60.236  38.369  -23.400 1.00 9.91  ? 217  VAL B CG1   1 
ATOM   5697  C CG2   . VAL B  1  217 ? 60.340  40.378  -21.906 1.00 11.13 ? 217  VAL B CG2   1 
ATOM   5698  N N     . GLU B  1  218 ? 59.764  39.784  -26.580 1.00 11.37 ? 218  GLU B N     1 
ATOM   5699  C CA    . GLU B  1  218 ? 59.163  39.274  -27.810 1.00 12.72 ? 218  GLU B CA    1 
ATOM   5700  C C     . GLU B  1  218 ? 59.297  37.780  -28.075 1.00 13.59 ? 218  GLU B C     1 
ATOM   5701  O O     . GLU B  1  218 ? 58.482  37.212  -28.798 1.00 13.24 ? 218  GLU B O     1 
ATOM   5702  C CB    . GLU B  1  218 ? 59.750  40.006  -29.021 1.00 14.79 ? 218  GLU B CB    1 
ATOM   5703  C CG    . GLU B  1  218 ? 59.806  41.512  -28.894 1.00 17.21 ? 218  GLU B CG    1 
ATOM   5704  C CD    . GLU B  1  218 ? 60.374  42.165  -30.134 1.00 18.06 ? 218  GLU B CD    1 
ATOM   5705  O OE1   . GLU B  1  218 ? 61.257  41.551  -30.772 1.00 18.69 ? 218  GLU B OE1   1 
ATOM   5706  O OE2   . GLU B  1  218 ? 59.942  43.288  -30.469 1.00 18.72 ? 218  GLU B OE2   1 
ATOM   5707  N N     . LYS B  1  219 ? 60.311  37.140  -27.506 1.00 12.51 ? 219  LYS B N     1 
ATOM   5708  C CA    . LYS B  1  219 ? 60.516  35.728  -27.769 1.00 13.78 ? 219  LYS B CA    1 
ATOM   5709  C C     . LYS B  1  219 ? 61.355  35.027  -26.718 1.00 12.27 ? 219  LYS B C     1 
ATOM   5710  O O     . LYS B  1  219 ? 62.291  35.599  -26.161 1.00 13.63 ? 219  LYS B O     1 
ATOM   5711  C CB    . LYS B  1  219 ? 61.188  35.579  -29.147 1.00 16.49 ? 219  LYS B CB    1 
ATOM   5712  C CG    . LYS B  1  219 ? 61.309  34.154  -29.665 1.00 21.64 ? 219  LYS B CG    1 
ATOM   5713  C CD    . LYS B  1  219 ? 61.960  34.138  -31.053 1.00 23.98 ? 219  LYS B CD    1 
ATOM   5714  C CE    . LYS B  1  219 ? 61.957  32.734  -31.661 1.00 26.30 ? 219  LYS B CE    1 
ATOM   5715  N NZ    . LYS B  1  219 ? 62.526  32.708  -33.043 1.00 29.87 ? 219  LYS B NZ    1 
ATOM   5716  N N     . ILE B  1  220 ? 60.995  33.780  -26.447 1.00 11.90 ? 220  ILE B N     1 
ATOM   5717  C CA    . ILE B  1  220 ? 61.746  32.947  -25.522 1.00 13.08 ? 220  ILE B CA    1 
ATOM   5718  C C     . ILE B  1  220 ? 62.686  32.168  -26.439 1.00 13.76 ? 220  ILE B C     1 
ATOM   5719  O O     . ILE B  1  220 ? 62.255  31.648  -27.468 1.00 15.80 ? 220  ILE B O     1 
ATOM   5720  C CB    . ILE B  1  220 ? 60.843  31.953  -24.771 1.00 13.04 ? 220  ILE B CB    1 
ATOM   5721  C CG1   . ILE B  1  220 ? 59.803  32.713  -23.943 1.00 13.54 ? 220  ILE B CG1   1 
ATOM   5722  C CG2   . ILE B  1  220 ? 61.699  31.068  -23.871 1.00 13.73 ? 220  ILE B CG2   1 
ATOM   5723  C CD1   . ILE B  1  220 ? 58.794  31.812  -23.271 1.00 17.35 ? 220  ILE B CD1   1 
ATOM   5724  N N     . ILE B  1  221 ? 63.963  32.096  -26.075 1.00 13.66 ? 221  ILE B N     1 
ATOM   5725  C CA    . ILE B  1  221 ? 64.951  31.385  -26.888 1.00 14.54 ? 221  ILE B CA    1 
ATOM   5726  C C     . ILE B  1  221 ? 65.128  29.958  -26.380 1.00 13.43 ? 221  ILE B C     1 
ATOM   5727  O O     . ILE B  1  221 ? 65.195  29.738  -25.171 1.00 12.66 ? 221  ILE B O     1 
ATOM   5728  C CB    . ILE B  1  221 ? 66.322  32.089  -26.837 1.00 15.96 ? 221  ILE B CB    1 
ATOM   5729  C CG1   . ILE B  1  221 ? 66.160  33.569  -27.172 1.00 17.86 ? 221  ILE B CG1   1 
ATOM   5730  C CG2   . ILE B  1  221 ? 67.284  31.433  -27.824 1.00 16.07 ? 221  ILE B CG2   1 
ATOM   5731  C CD1   . ILE B  1  221 ? 67.412  34.392  -26.941 1.00 21.58 ? 221  ILE B CD1   1 
ATOM   5732  N N     . PHE B  1  222 ? 65.217  28.996  -27.297 1.00 14.04 ? 222  PHE B N     1 
ATOM   5733  C CA    . PHE B  1  222 ? 65.389  27.594  -26.913 1.00 14.54 ? 222  PHE B CA    1 
ATOM   5734  C C     . PHE B  1  222 ? 66.594  26.913  -27.539 1.00 16.19 ? 222  PHE B C     1 
ATOM   5735  O O     . PHE B  1  222 ? 67.113  27.359  -28.554 1.00 17.13 ? 222  PHE B O     1 
ATOM   5736  C CB    . PHE B  1  222 ? 64.154  26.775  -27.292 1.00 14.77 ? 222  PHE B CB    1 
ATOM   5737  C CG    . PHE B  1  222 ? 62.891  27.251  -26.651 1.00 15.62 ? 222  PHE B CG    1 
ATOM   5738  C CD1   . PHE B  1  222 ? 62.030  28.102  -27.334 1.00 16.52 ? 222  PHE B CD1   1 
ATOM   5739  C CD2   . PHE B  1  222 ? 62.562  26.853  -25.355 1.00 15.70 ? 222  PHE B CD2   1 
ATOM   5740  C CE1   . PHE B  1  222 ? 60.843  28.553  -26.740 1.00 16.23 ? 222  PHE B CE1   1 
ATOM   5741  C CE2   . PHE B  1  222 ? 61.381  27.293  -24.742 1.00 15.92 ? 222  PHE B CE2   1 
ATOM   5742  C CZ    . PHE B  1  222 ? 60.515  28.149  -25.437 1.00 14.28 ? 222  PHE B CZ    1 
ATOM   5743  N N     . SER B  1  223 ? 67.015  25.814  -26.922 1.00 17.42 ? 223  SER B N     1 
ATOM   5744  C CA    . SER B  1  223 ? 68.133  25.014  -27.408 1.00 19.35 ? 223  SER B CA    1 
ATOM   5745  C C     . SER B  1  223 ? 67.580  24.094  -28.484 1.00 20.75 ? 223  SER B C     1 
ATOM   5746  O O     . SER B  1  223 ? 66.369  24.001  -28.654 1.00 21.01 ? 223  SER B O     1 
ATOM   5747  C CB    . SER B  1  223 ? 68.724  24.174  -26.266 1.00 19.05 ? 223  SER B CB    1 
ATOM   5748  O OG    . SER B  1  223 ? 67.754  23.292  -25.748 1.00 18.29 ? 223  SER B OG    1 
ATOM   5749  N N     . ASN B  1  224 ? 68.467  23.411  -29.198 1.00 21.23 ? 224  ASN B N     1 
ATOM   5750  C CA    . ASN B  1  224 ? 68.056  22.485  -30.243 1.00 22.30 ? 224  ASN B CA    1 
ATOM   5751  C C     . ASN B  1  224 ? 67.377  21.270  -29.625 1.00 22.39 ? 224  ASN B C     1 
ATOM   5752  O O     . ASN B  1  224 ? 67.623  20.924  -28.469 1.00 22.91 ? 224  ASN B O     1 
ATOM   5753  C CB    . ASN B  1  224 ? 69.273  22.006  -31.046 1.00 23.44 ? 224  ASN B CB    1 
ATOM   5754  C CG    . ASN B  1  224 ? 70.010  23.138  -31.745 1.00 25.59 ? 224  ASN B CG    1 
ATOM   5755  O OD1   . ASN B  1  224 ? 71.171  22.984  -32.131 1.00 27.32 ? 224  ASN B OD1   1 
ATOM   5756  N ND2   . ASN B  1  224 ? 69.335  24.267  -31.936 1.00 25.83 ? 224  ASN B ND2   1 
ATOM   5757  N N     . ALA B  1  225 ? 66.512  20.622  -30.396 1.00 22.10 ? 225  ALA B N     1 
ATOM   5758  C CA    . ALA B  1  225 ? 65.843  19.420  -29.913 1.00 22.77 ? 225  ALA B CA    1 
ATOM   5759  C C     . ALA B  1  225 ? 66.844  18.283  -30.114 1.00 22.85 ? 225  ALA B C     1 
ATOM   5760  O O     . ALA B  1  225 ? 67.746  18.388  -30.948 1.00 22.28 ? 225  ALA B O     1 
ATOM   5761  C CB    . ALA B  1  225 ? 64.580  19.149  -30.708 1.00 24.46 ? 225  ALA B CB    1 
ATOM   5762  N N     . PRO B  1  226 ? 66.717  17.190  -29.335 1.00 23.50 ? 226  PRO B N     1 
ATOM   5763  C CA    . PRO B  1  226 ? 65.724  16.929  -28.286 1.00 24.06 ? 226  PRO B CA    1 
ATOM   5764  C C     . PRO B  1  226 ? 66.172  17.532  -26.951 1.00 24.38 ? 226  PRO B C     1 
ATOM   5765  O O     . PRO B  1  226 ? 67.207  18.191  -26.876 1.00 25.68 ? 226  PRO B O     1 
ATOM   5766  C CB    . PRO B  1  226 ? 65.677  15.403  -28.251 1.00 24.06 ? 226  PRO B CB    1 
ATOM   5767  C CG    . PRO B  1  226 ? 67.136  15.062  -28.404 1.00 23.53 ? 226  PRO B CG    1 
ATOM   5768  C CD    . PRO B  1  226 ? 67.560  15.996  -29.549 1.00 24.52 ? 226  PRO B CD    1 
ATOM   5769  N N     . GLY B  1  227 ? 65.407  17.293  -25.893 1.00 24.69 ? 227  GLY B N     1 
ATOM   5770  C CA    . GLY B  1  227 ? 65.778  17.838  -24.601 1.00 24.34 ? 227  GLY B CA    1 
ATOM   5771  C C     . GLY B  1  227 ? 65.725  19.354  -24.644 1.00 23.61 ? 227  GLY B C     1 
ATOM   5772  O O     . GLY B  1  227 ? 66.658  20.043  -24.230 1.00 25.44 ? 227  GLY B O     1 
ATOM   5773  N N     . LEU B  1  228 ? 64.625  19.876  -25.170 1.00 21.27 ? 228  LEU B N     1 
ATOM   5774  C CA    . LEU B  1  228 ? 64.415  21.315  -25.266 1.00 18.88 ? 228  LEU B CA    1 
ATOM   5775  C C     . LEU B  1  228 ? 64.603  22.033  -23.928 1.00 17.06 ? 228  LEU B C     1 
ATOM   5776  O O     . LEU B  1  228 ? 64.119  21.581  -22.885 1.00 16.64 ? 228  LEU B O     1 
ATOM   5777  C CB    . LEU B  1  228 ? 63.004  21.584  -25.787 1.00 20.00 ? 228  LEU B CB    1 
ATOM   5778  C CG    . LEU B  1  228 ? 62.716  20.988  -27.165 1.00 20.96 ? 228  LEU B CG    1 
ATOM   5779  C CD1   . LEU B  1  228 ? 61.222  20.964  -27.426 1.00 21.91 ? 228  LEU B CD1   1 
ATOM   5780  C CD2   . LEU B  1  228 ? 63.447  21.796  -28.222 1.00 21.91 ? 228  LEU B CD2   1 
ATOM   5781  N N     . THR B  1  229 ? 65.295  23.167  -23.972 1.00 16.06 ? 229  THR B N     1 
ATOM   5782  C CA    . THR B  1  229 ? 65.541  23.971  -22.781 1.00 15.70 ? 229  THR B CA    1 
ATOM   5783  C C     . THR B  1  229 ? 65.523  25.463  -23.105 1.00 14.81 ? 229  THR B C     1 
ATOM   5784  O O     . THR B  1  229 ? 66.103  25.894  -24.100 1.00 14.12 ? 229  THR B O     1 
ATOM   5785  C CB    . THR B  1  229 ? 66.906  23.628  -22.152 1.00 16.64 ? 229  THR B CB    1 
ATOM   5786  O OG1   . THR B  1  229 ? 66.976  22.218  -21.915 1.00 19.09 ? 229  THR B OG1   1 
ATOM   5787  C CG2   . THR B  1  229 ? 67.089  24.363  -20.829 1.00 17.08 ? 229  THR B CG2   1 
ATOM   5788  N N     . ALA B  1  230 ? 64.848  26.249  -22.269 1.00 12.16 ? 230  ALA B N     1 
ATOM   5789  C CA    . ALA B  1  230 ? 64.793  27.695  -22.465 1.00 13.04 ? 230  ALA B CA    1 
ATOM   5790  C C     . ALA B  1  230 ? 66.151  28.254  -22.046 1.00 13.60 ? 230  ALA B C     1 
ATOM   5791  O O     . ALA B  1  230 ? 66.638  27.964  -20.953 1.00 15.32 ? 230  ALA B O     1 
ATOM   5792  C CB    . ALA B  1  230 ? 63.686  28.298  -21.611 1.00 11.29 ? 230  ALA B CB    1 
ATOM   5793  N N     . THR B  1  231 ? 66.764  29.052  -22.914 1.00 13.83 ? 231  THR B N     1 
ATOM   5794  C CA    . THR B  1  231 ? 68.078  29.612  -22.621 1.00 13.79 ? 231  THR B CA    1 
ATOM   5795  C C     . THR B  1  231 ? 68.074  31.106  -22.317 1.00 13.75 ? 231  THR B C     1 
ATOM   5796  O O     . THR B  1  231 ? 69.068  31.646  -21.829 1.00 14.14 ? 231  THR B O     1 
ATOM   5797  C CB    . THR B  1  231 ? 69.049  29.349  -23.789 1.00 14.15 ? 231  THR B CB    1 
ATOM   5798  O OG1   . THR B  1  231 ? 68.534  29.946  -24.985 1.00 16.51 ? 231  THR B OG1   1 
ATOM   5799  C CG2   . THR B  1  231 ? 69.216  27.852  -24.009 1.00 14.83 ? 231  THR B CG2   1 
ATOM   5800  N N     . GLY B  1  232 ? 66.958  31.770  -22.596 1.00 11.90 ? 232  GLY B N     1 
ATOM   5801  C CA    . GLY B  1  232 ? 66.868  33.196  -22.344 1.00 11.98 ? 232  GLY B CA    1 
ATOM   5802  C C     . GLY B  1  232 ? 65.723  33.811  -23.121 1.00 11.50 ? 232  GLY B C     1 
ATOM   5803  O O     . GLY B  1  232 ? 64.851  33.097  -23.613 1.00 12.16 ? 232  GLY B O     1 
ATOM   5804  N N     . VAL B  1  233 ? 65.719  35.135  -23.233 1.00 12.31 ? 233  VAL B N     1 
ATOM   5805  C CA    . VAL B  1  233 ? 64.664  35.824  -23.963 1.00 13.11 ? 233  VAL B CA    1 
ATOM   5806  C C     . VAL B  1  233 ? 65.215  37.012  -24.741 1.00 13.03 ? 233  VAL B C     1 
ATOM   5807  O O     . VAL B  1  233 ? 66.324  37.483  -24.481 1.00 13.61 ? 233  VAL B O     1 
ATOM   5808  C CB    . VAL B  1  233 ? 63.563  36.358  -23.009 1.00 13.41 ? 233  VAL B CB    1 
ATOM   5809  C CG1   . VAL B  1  233 ? 63.004  35.225  -22.161 1.00 12.48 ? 233  VAL B CG1   1 
ATOM   5810  C CG2   . VAL B  1  233 ? 64.127  37.462  -22.126 1.00 13.79 ? 233  VAL B CG2   1 
ATOM   5811  N N     . ILE B  1  234 ? 64.429  37.483  -25.701 1.00 12.58 ? 234  ILE B N     1 
ATOM   5812  C CA    . ILE B  1  234 ? 64.791  38.642  -26.502 1.00 13.31 ? 234  ILE B CA    1 
ATOM   5813  C C     . ILE B  1  234 ? 63.796  39.742  -26.151 1.00 13.40 ? 234  ILE B C     1 
ATOM   5814  O O     . ILE B  1  234 ? 62.585  39.513  -26.176 1.00 14.18 ? 234  ILE B O     1 
ATOM   5815  C CB    . ILE B  1  234 ? 64.665  38.362  -28.012 1.00 14.22 ? 234  ILE B CB    1 
ATOM   5816  C CG1   . ILE B  1  234 ? 65.582  37.207  -28.412 1.00 15.19 ? 234  ILE B CG1   1 
ATOM   5817  C CG2   . ILE B  1  234 ? 64.991  39.627  -28.799 1.00 14.77 ? 234  ILE B CG2   1 
ATOM   5818  C CD1   . ILE B  1  234 ? 65.437  36.784  -29.863 1.00 17.08 ? 234  ILE B CD1   1 
ATOM   5819  N N     . TYR B  1  235 ? 64.293  40.924  -25.804 1.00 13.13 ? 235  TYR B N     1 
ATOM   5820  C CA    . TYR B  1  235 ? 63.403  42.032  -25.482 1.00 13.50 ? 235  TYR B CA    1 
ATOM   5821  C C     . TYR B  1  235 ? 63.843  43.281  -26.234 1.00 15.10 ? 235  TYR B C     1 
ATOM   5822  O O     . TYR B  1  235 ? 65.014  43.425  -26.584 1.00 14.86 ? 235  TYR B O     1 
ATOM   5823  C CB    . TYR B  1  235 ? 63.350  42.269  -23.961 1.00 12.66 ? 235  TYR B CB    1 
ATOM   5824  C CG    . TYR B  1  235 ? 64.644  42.680  -23.297 1.00 13.59 ? 235  TYR B CG    1 
ATOM   5825  C CD1   . TYR B  1  235 ? 64.955  44.026  -23.106 1.00 13.69 ? 235  TYR B CD1   1 
ATOM   5826  C CD2   . TYR B  1  235 ? 65.543  41.724  -22.825 1.00 12.80 ? 235  TYR B CD2   1 
ATOM   5827  C CE1   . TYR B  1  235 ? 66.122  44.411  -22.455 1.00 14.30 ? 235  TYR B CE1   1 
ATOM   5828  C CE2   . TYR B  1  235 ? 66.717  42.099  -22.174 1.00 13.41 ? 235  TYR B CE2   1 
ATOM   5829  C CZ    . TYR B  1  235 ? 66.998  43.444  -21.992 1.00 15.16 ? 235  TYR B CZ    1 
ATOM   5830  O OH    . TYR B  1  235 ? 68.154  43.824  -21.350 1.00 18.24 ? 235  TYR B OH    1 
ATOM   5831  N N     . ARG B  1  236 ? 62.899  44.177  -26.501 1.00 15.26 ? 236  ARG B N     1 
ATOM   5832  C CA    . ARG B  1  236 ? 63.208  45.389  -27.251 1.00 16.85 ? 236  ARG B CA    1 
ATOM   5833  C C     . ARG B  1  236 ? 62.933  46.643  -26.425 1.00 18.02 ? 236  ARG B C     1 
ATOM   5834  O O     . ARG B  1  236 ? 61.949  46.700  -25.685 1.00 16.86 ? 236  ARG B O     1 
ATOM   5835  C CB    . ARG B  1  236 ? 62.372  45.411  -28.536 1.00 18.03 ? 236  ARG B CB    1 
ATOM   5836  C CG    . ARG B  1  236 ? 62.929  46.284  -29.653 1.00 19.73 ? 236  ARG B CG    1 
ATOM   5837  C CD    . ARG B  1  236 ? 62.045  46.192  -30.895 1.00 20.63 ? 236  ARG B CD    1 
ATOM   5838  N NE    . ARG B  1  236 ? 61.945  44.825  -31.404 1.00 21.30 ? 236  ARG B NE    1 
ATOM   5839  C CZ    . ARG B  1  236 ? 62.867  44.230  -32.155 1.00 22.70 ? 236  ARG B CZ    1 
ATOM   5840  N NH1   . ARG B  1  236 ? 63.971  44.881  -32.501 1.00 23.51 ? 236  ARG B NH1   1 
ATOM   5841  N NH2   . ARG B  1  236 ? 62.690  42.978  -32.559 1.00 23.36 ? 236  ARG B NH2   1 
ATOM   5842  N N     . ASP B  1  237 ? 63.804  47.645  -26.547 1.00 18.43 ? 237  ASP B N     1 
ATOM   5843  C CA    . ASP B  1  237 ? 63.627  48.890  -25.804 1.00 19.58 ? 237  ASP B CA    1 
ATOM   5844  C C     . ASP B  1  237 ? 62.899  49.951  -26.627 1.00 20.46 ? 237  ASP B C     1 
ATOM   5845  O O     . ASP B  1  237 ? 62.523  49.710  -27.777 1.00 20.03 ? 237  ASP B O     1 
ATOM   5846  C CB    . ASP B  1  237 ? 64.977  49.443  -25.313 1.00 19.86 ? 237  ASP B CB    1 
ATOM   5847  C CG    . ASP B  1  237 ? 65.921  49.814  -26.447 1.00 21.55 ? 237  ASP B CG    1 
ATOM   5848  O OD1   . ASP B  1  237 ? 65.452  50.290  -27.500 1.00 21.88 ? 237  ASP B OD1   1 
ATOM   5849  O OD2   . ASP B  1  237 ? 67.145  49.647  -26.270 1.00 21.56 ? 237  ASP B OD2   1 
ATOM   5850  N N     . SER B  1  238 ? 62.706  51.124  -26.031 1.00 20.44 ? 238  SER B N     1 
ATOM   5851  C CA    . SER B  1  238 ? 62.000  52.221  -26.687 1.00 21.96 ? 238  SER B CA    1 
ATOM   5852  C C     . SER B  1  238 ? 62.655  52.743  -27.963 1.00 22.85 ? 238  SER B C     1 
ATOM   5853  O O     . SER B  1  238 ? 62.007  53.428  -28.750 1.00 24.30 ? 238  SER B O     1 
ATOM   5854  C CB    . SER B  1  238 ? 61.789  53.377  -25.699 1.00 20.85 ? 238  SER B CB    1 
ATOM   5855  O OG    . SER B  1  238 ? 63.020  53.857  -25.193 1.00 23.08 ? 238  SER B OG    1 
ATOM   5856  N N     . ASN B  1  239 ? 63.931  52.431  -28.166 1.00 23.65 ? 239  ASN B N     1 
ATOM   5857  C CA    . ASN B  1  239 ? 64.626  52.878  -29.370 1.00 24.60 ? 239  ASN B CA    1 
ATOM   5858  C C     . ASN B  1  239 ? 64.488  51.858  -30.488 1.00 25.41 ? 239  ASN B C     1 
ATOM   5859  O O     . ASN B  1  239 ? 64.910  52.099  -31.615 1.00 25.71 ? 239  ASN B O     1 
ATOM   5860  C CB    . ASN B  1  239 ? 66.116  53.112  -29.092 1.00 25.53 ? 239  ASN B CB    1 
ATOM   5861  C CG    . ASN B  1  239 ? 66.363  54.315  -28.214 1.00 26.31 ? 239  ASN B CG    1 
ATOM   5862  O OD1   . ASN B  1  239 ? 65.667  55.326  -28.320 1.00 27.88 ? 239  ASN B OD1   1 
ATOM   5863  N ND2   . ASN B  1  239 ? 67.374  54.225  -27.358 1.00 25.76 ? 239  ASN B ND2   1 
ATOM   5864  N N     . GLY B  1  240 ? 63.897  50.714  -30.164 1.00 24.96 ? 240  GLY B N     1 
ATOM   5865  C CA    . GLY B  1  240 ? 63.730  49.665  -31.153 1.00 25.32 ? 240  GLY B CA    1 
ATOM   5866  C C     . GLY B  1  240 ? 64.905  48.712  -31.188 1.00 23.84 ? 240  GLY B C     1 
ATOM   5867  O O     . GLY B  1  240 ? 64.986  47.834  -32.045 1.00 25.48 ? 240  GLY B O     1 
ATOM   5868  N N     . THR B  1  241 ? 65.824  48.892  -30.249 1.00 23.66 ? 241  THR B N     1 
ATOM   5869  C CA    . THR B  1  241 ? 67.006  48.044  -30.161 1.00 23.85 ? 241  THR B CA    1 
ATOM   5870  C C     . THR B  1  241 ? 66.735  46.778  -29.352 1.00 22.82 ? 241  THR B C     1 
ATOM   5871  O O     . THR B  1  241 ? 66.207  46.840  -28.237 1.00 21.70 ? 241  THR B O     1 
ATOM   5872  C CB    . THR B  1  241 ? 68.172  48.794  -29.506 1.00 25.99 ? 241  THR B CB    1 
ATOM   5873  O OG1   . THR B  1  241 ? 68.354  50.049  -30.170 1.00 28.08 ? 241  THR B OG1   1 
ATOM   5874  C CG2   . THR B  1  241 ? 69.456  47.980  -29.607 1.00 27.18 ? 241  THR B CG2   1 
ATOM   5875  N N     . PRO B  1  242 ? 67.072  45.602  -29.917 1.00 21.86 ? 242  PRO B N     1 
ATOM   5876  C CA    . PRO B  1  242 ? 66.852  44.335  -29.214 1.00 21.55 ? 242  PRO B CA    1 
ATOM   5877  C C     . PRO B  1  242 ? 67.984  43.979  -28.262 1.00 21.84 ? 242  PRO B C     1 
ATOM   5878  O O     . PRO B  1  242 ? 69.153  44.230  -28.551 1.00 21.03 ? 242  PRO B O     1 
ATOM   5879  C CB    . PRO B  1  242 ? 66.728  43.331  -30.356 1.00 21.74 ? 242  PRO B CB    1 
ATOM   5880  C CG    . PRO B  1  242 ? 67.739  43.850  -31.337 1.00 21.33 ? 242  PRO B CG    1 
ATOM   5881  C CD    . PRO B  1  242 ? 67.472  45.354  -31.317 1.00 21.88 ? 242  PRO B CD    1 
ATOM   5882  N N     . HIS B  1  243 ? 67.623  43.392  -27.127 1.00 19.76 ? 243  HIS B N     1 
ATOM   5883  C CA    . HIS B  1  243 ? 68.588  42.965  -26.124 1.00 19.18 ? 243  HIS B CA    1 
ATOM   5884  C C     . HIS B  1  243 ? 68.328  41.491  -25.878 1.00 18.60 ? 243  HIS B C     1 
ATOM   5885  O O     . HIS B  1  243 ? 67.276  40.967  -26.246 1.00 17.28 ? 243  HIS B O     1 
ATOM   5886  C CB    . HIS B  1  243 ? 68.379  43.697  -24.799 1.00 19.37 ? 243  HIS B CB    1 
ATOM   5887  C CG    . HIS B  1  243 ? 68.486  45.184  -24.891 1.00 20.54 ? 243  HIS B CG    1 
ATOM   5888  N ND1   . HIS B  1  243 ? 67.785  45.925  -25.818 1.00 21.96 ? 243  HIS B ND1   1 
ATOM   5889  C CD2   . HIS B  1  243 ? 69.167  46.075  -24.134 1.00 21.80 ? 243  HIS B CD2   1 
ATOM   5890  C CE1   . HIS B  1  243 ? 68.029  47.207  -25.625 1.00 22.38 ? 243  HIS B CE1   1 
ATOM   5891  N NE2   . HIS B  1  243 ? 68.864  47.327  -24.609 1.00 22.53 ? 243  HIS B NE2   1 
ATOM   5892  N N     . GLN B  1  244 ? 69.283  40.830  -25.243 1.00 17.82 ? 244  GLN B N     1 
ATOM   5893  C CA    . GLN B  1  244 ? 69.135  39.425  -24.917 1.00 18.24 ? 244  GLN B CA    1 
ATOM   5894  C C     . GLN B  1  244 ? 69.571  39.199  -23.478 1.00 18.00 ? 244  GLN B C     1 
ATOM   5895  O O     . GLN B  1  244 ? 70.580  39.746  -23.030 1.00 17.28 ? 244  GLN B O     1 
ATOM   5896  C CB    . GLN B  1  244 ? 69.976  38.560  -25.858 1.00 20.18 ? 244  GLN B CB    1 
ATOM   5897  C CG    . GLN B  1  244 ? 69.446  38.488  -27.281 1.00 22.38 ? 244  GLN B CG    1 
ATOM   5898  C CD    . GLN B  1  244 ? 70.289  37.589  -28.167 1.00 24.01 ? 244  GLN B CD    1 
ATOM   5899  O OE1   . GLN B  1  244 ? 71.451  37.886  -28.447 1.00 26.04 ? 244  GLN B OE1   1 
ATOM   5900  N NE2   . GLN B  1  244 ? 69.709  36.478  -28.606 1.00 26.59 ? 244  GLN B NE2   1 
ATOM   5901  N N     . ALA B  1  245 ? 68.788  38.410  -22.752 1.00 16.57 ? 245  ALA B N     1 
ATOM   5902  C CA    . ALA B  1  245 ? 69.099  38.080  -21.368 1.00 14.61 ? 245  ALA B CA    1 
ATOM   5903  C C     . ALA B  1  245 ? 69.090  36.562  -21.297 1.00 16.01 ? 245  ALA B C     1 
ATOM   5904  O O     . ALA B  1  245 ? 68.079  35.929  -21.596 1.00 17.70 ? 245  ALA B O     1 
ATOM   5905  C CB    . ALA B  1  245 ? 68.048  38.662  -20.430 1.00 14.26 ? 245  ALA B CB    1 
ATOM   5906  N N     . PHE B  1  246 ? 70.219  35.977  -20.917 1.00 15.49 ? 246  PHE B N     1 
ATOM   5907  C CA    . PHE B  1  246 ? 70.318  34.528  -20.833 1.00 16.74 ? 246  PHE B CA    1 
ATOM   5908  C C     . PHE B  1  246 ? 70.369  34.046  -19.393 1.00 15.86 ? 246  PHE B C     1 
ATOM   5909  O O     . PHE B  1  246 ? 70.735  34.799  -18.490 1.00 16.30 ? 246  PHE B O     1 
ATOM   5910  C CB    . PHE B  1  246 ? 71.564  34.038  -21.579 1.00 17.69 ? 246  PHE B CB    1 
ATOM   5911  C CG    . PHE B  1  246 ? 71.601  34.435  -23.031 1.00 19.48 ? 246  PHE B CG    1 
ATOM   5912  C CD1   . PHE B  1  246 ? 72.009  35.710  -23.410 1.00 20.78 ? 246  PHE B CD1   1 
ATOM   5913  C CD2   . PHE B  1  246 ? 71.223  33.531  -24.018 1.00 21.39 ? 246  PHE B CD2   1 
ATOM   5914  C CE1   . PHE B  1  246 ? 72.041  36.079  -24.755 1.00 22.35 ? 246  PHE B CE1   1 
ATOM   5915  C CE2   . PHE B  1  246 ? 71.249  33.889  -25.365 1.00 21.55 ? 246  PHE B CE2   1 
ATOM   5916  C CZ    . PHE B  1  246 ? 71.660  35.165  -25.734 1.00 21.14 ? 246  PHE B CZ    1 
ATOM   5917  N N     . VAL B  1  247 ? 69.989  32.790  -19.183 1.00 16.06 ? 247  VAL B N     1 
ATOM   5918  C CA    . VAL B  1  247 ? 70.017  32.200  -17.850 1.00 17.18 ? 247  VAL B CA    1 
ATOM   5919  C C     . VAL B  1  247 ? 71.179  31.218  -17.774 1.00 16.22 ? 247  VAL B C     1 
ATOM   5920  O O     . VAL B  1  247 ? 71.504  30.550  -18.755 1.00 18.24 ? 247  VAL B O     1 
ATOM   5921  C CB    . VAL B  1  247 ? 68.695  31.463  -17.520 1.00 17.15 ? 247  VAL B CB    1 
ATOM   5922  C CG1   . VAL B  1  247 ? 67.558  32.468  -17.401 1.00 18.77 ? 247  VAL B CG1   1 
ATOM   5923  C CG2   . VAL B  1  247 ? 68.382  30.432  -18.592 1.00 17.24 ? 247  VAL B CG2   1 
ATOM   5924  N N     . ARG B  1  248 ? 71.811  31.138  -16.609 1.00 17.04 ? 248  ARG B N     1 
ATOM   5925  C CA    . ARG B  1  248 ? 72.946  30.245  -16.428 1.00 17.21 ? 248  ARG B CA    1 
ATOM   5926  C C     . ARG B  1  248 ? 72.524  28.853  -15.969 1.00 17.51 ? 248  ARG B C     1 
ATOM   5927  O O     . ARG B  1  248 ? 71.339  28.584  -15.773 1.00 17.53 ? 248  ARG B O     1 
ATOM   5928  C CB    . ARG B  1  248 ? 73.946  30.866  -15.441 1.00 18.05 ? 248  ARG B CB    1 
ATOM   5929  C CG    . ARG B  1  248 ? 74.551  32.177  -15.950 1.00 20.24 ? 248  ARG B CG    1 
ATOM   5930  C CD    . ARG B  1  248 ? 75.855  32.535  -15.242 1.00 21.66 ? 248  ARG B CD    1 
ATOM   5931  N NE    . ARG B  1  248 ? 75.657  33.088  -13.904 1.00 22.02 ? 248  ARG B NE    1 
ATOM   5932  C CZ    . ARG B  1  248 ? 75.430  34.373  -13.647 1.00 21.21 ? 248  ARG B CZ    1 
ATOM   5933  N NH1   . ARG B  1  248 ? 75.369  35.254  -14.637 1.00 21.78 ? 248  ARG B NH1   1 
ATOM   5934  N NH2   . ARG B  1  248 ? 75.274  34.779  -12.395 1.00 21.31 ? 248  ARG B NH2   1 
ATOM   5935  N N     . SER B  1  249 ? 73.501  27.964  -15.815 1.00 18.30 ? 249  SER B N     1 
ATOM   5936  C CA    . SER B  1  249 ? 73.243  26.590  -15.392 1.00 19.45 ? 249  SER B CA    1 
ATOM   5937  C C     . SER B  1  249 ? 72.259  26.508  -14.231 1.00 19.14 ? 249  SER B C     1 
ATOM   5938  O O     . SER B  1  249 ? 72.378  27.244  -13.251 1.00 20.61 ? 249  SER B O     1 
ATOM   5939  C CB    . SER B  1  249 ? 74.553  25.907  -14.993 1.00 20.17 ? 249  SER B CB    1 
ATOM   5940  O OG    . SER B  1  249 ? 74.333  24.546  -14.667 1.00 23.28 ? 249  SER B OG    1 
ATOM   5941  N N     . LYS B  1  250 ? 71.296  25.598  -14.354 1.00 17.98 ? 250  LYS B N     1 
ATOM   5942  C CA    . LYS B  1  250 ? 70.263  25.388  -13.341 1.00 18.52 ? 250  LYS B CA    1 
ATOM   5943  C C     . LYS B  1  250 ? 69.266  26.539  -13.236 1.00 17.24 ? 250  LYS B C     1 
ATOM   5944  O O     . LYS B  1  250 ? 68.287  26.457  -12.492 1.00 19.01 ? 250  LYS B O     1 
ATOM   5945  C CB    . LYS B  1  250 ? 70.903  25.144  -11.970 1.00 20.05 ? 250  LYS B CB    1 
ATOM   5946  C CG    . LYS B  1  250 ? 71.558  23.785  -11.809 1.00 23.39 ? 250  LYS B CG    1 
ATOM   5947  C CD    . LYS B  1  250 ? 72.010  23.587  -10.373 1.00 25.35 ? 250  LYS B CD    1 
ATOM   5948  C CE    . LYS B  1  250 ? 72.349  22.137  -10.088 1.00 28.43 ? 250  LYS B CE    1 
ATOM   5949  N NZ    . LYS B  1  250 ? 72.602  21.930  -8.637  1.00 28.61 ? 250  LYS B NZ    1 
ATOM   5950  N N     . GLY B  1  251 ? 69.521  27.612  -13.975 1.00 16.13 ? 251  GLY B N     1 
ATOM   5951  C CA    . GLY B  1  251 ? 68.633  28.761  -13.948 1.00 14.31 ? 251  GLY B CA    1 
ATOM   5952  C C     . GLY B  1  251 ? 67.403  28.538  -14.805 1.00 13.26 ? 251  GLY B C     1 
ATOM   5953  O O     . GLY B  1  251 ? 67.332  27.561  -15.551 1.00 13.00 ? 251  GLY B O     1 
ATOM   5954  N N     . GLU B  1  252 ? 66.438  29.448  -14.723 1.00 12.16 ? 252  GLU B N     1 
ATOM   5955  C CA    . GLU B  1  252 ? 65.213  29.290  -15.492 1.00 10.85 ? 252  GLU B CA    1 
ATOM   5956  C C     . GLU B  1  252 ? 64.598  30.604  -15.942 1.00 12.39 ? 252  GLU B C     1 
ATOM   5957  O O     . GLU B  1  252 ? 64.861  31.669  -15.375 1.00 10.28 ? 252  GLU B O     1 
ATOM   5958  C CB    . GLU B  1  252 ? 64.169  28.540  -14.657 1.00 13.52 ? 252  GLU B CB    1 
ATOM   5959  C CG    . GLU B  1  252 ? 64.653  27.234  -14.042 1.00 14.45 ? 252  GLU B CG    1 
ATOM   5960  C CD    . GLU B  1  252 ? 63.557  26.511  -13.279 1.00 16.83 ? 252  GLU B CD    1 
ATOM   5961  O OE1   . GLU B  1  252 ? 62.494  26.246  -13.876 1.00 17.16 ? 252  GLU B OE1   1 
ATOM   5962  O OE2   . GLU B  1  252 ? 63.758  26.200  -12.086 1.00 16.79 ? 252  GLU B OE2   1 
ATOM   5963  N N     . VAL B  1  253 ? 63.778  30.505  -16.980 1.00 11.73 ? 253  VAL B N     1 
ATOM   5964  C CA    . VAL B  1  253 ? 63.038  31.640  -17.504 1.00 11.00 ? 253  VAL B CA    1 
ATOM   5965  C C     . VAL B  1  253 ? 61.637  31.383  -16.961 1.00 11.29 ? 253  VAL B C     1 
ATOM   5966  O O     . VAL B  1  253 ? 61.123  30.270  -17.077 1.00 9.34  ? 253  VAL B O     1 
ATOM   5967  C CB    . VAL B  1  253 ? 62.978  31.630  -19.051 1.00 11.46 ? 253  VAL B CB    1 
ATOM   5968  C CG1   . VAL B  1  253 ? 61.966  32.666  -19.542 1.00 9.24  ? 253  VAL B CG1   1 
ATOM   5969  C CG2   . VAL B  1  253 ? 64.358  31.926  -19.634 1.00 10.22 ? 253  VAL B CG2   1 
ATOM   5970  N N     . ILE B  1  254 ? 61.036  32.386  -16.336 1.00 8.20  ? 254  ILE B N     1 
ATOM   5971  C CA    . ILE B  1  254 ? 59.689  32.227  -15.809 1.00 10.24 ? 254  ILE B CA    1 
ATOM   5972  C C     . ILE B  1  254 ? 58.820  33.308  -16.418 1.00 8.09  ? 254  ILE B C     1 
ATOM   5973  O O     . ILE B  1  254 ? 59.150  34.493  -16.354 1.00 9.75  ? 254  ILE B O     1 
ATOM   5974  C CB    . ILE B  1  254 ? 59.651  32.346  -14.274 1.00 10.71 ? 254  ILE B CB    1 
ATOM   5975  C CG1   . ILE B  1  254 ? 60.554  31.275  -13.656 1.00 12.52 ? 254  ILE B CG1   1 
ATOM   5976  C CG2   . ILE B  1  254 ? 58.211  32.164  -13.776 1.00 11.14 ? 254  ILE B CG2   1 
ATOM   5977  C CD1   . ILE B  1  254 ? 60.814  31.461  -12.184 1.00 14.96 ? 254  ILE B CD1   1 
ATOM   5978  N N     . VAL B  1  255 ? 57.719  32.886  -17.027 1.00 8.55  ? 255  VAL B N     1 
ATOM   5979  C CA    . VAL B  1  255 ? 56.802  33.814  -17.663 1.00 8.50  ? 255  VAL B CA    1 
ATOM   5980  C C     . VAL B  1  255 ? 55.665  34.142  -16.699 1.00 7.77  ? 255  VAL B C     1 
ATOM   5981  O O     . VAL B  1  255 ? 54.955  33.251  -16.233 1.00 7.69  ? 255  VAL B O     1 
ATOM   5982  C CB    . VAL B  1  255 ? 56.236  33.205  -18.965 1.00 8.09  ? 255  VAL B CB    1 
ATOM   5983  C CG1   . VAL B  1  255 ? 55.368  34.225  -19.687 1.00 10.68 ? 255  VAL B CG1   1 
ATOM   5984  C CG2   . VAL B  1  255 ? 57.385  32.754  -19.867 1.00 10.54 ? 255  VAL B CG2   1 
ATOM   5985  N N     . SER B  1  256 ? 55.517  35.431  -16.400 1.00 6.46  ? 256  SER B N     1 
ATOM   5986  C CA    . SER B  1  256 ? 54.489  35.936  -15.490 1.00 7.63  ? 256  SER B CA    1 
ATOM   5987  C C     . SER B  1  256 ? 53.847  37.128  -16.188 1.00 7.65  ? 256  SER B C     1 
ATOM   5988  O O     . SER B  1  256 ? 53.527  38.140  -15.559 1.00 7.14  ? 256  SER B O     1 
ATOM   5989  C CB    . SER B  1  256 ? 55.134  36.395  -14.176 1.00 7.21  ? 256  SER B CB    1 
ATOM   5990  O OG    . SER B  1  256 ? 55.856  35.341  -13.552 1.00 9.33  ? 256  SER B OG    1 
ATOM   5991  N N     . ALA B  1  257 ? 53.655  36.991  -17.497 1.00 7.25  ? 257  ALA B N     1 
ATOM   5992  C CA    . ALA B  1  257 ? 53.097  38.059  -18.324 1.00 6.48  ? 257  ALA B CA    1 
ATOM   5993  C C     . ALA B  1  257 ? 51.578  38.187  -18.289 1.00 7.57  ? 257  ALA B C     1 
ATOM   5994  O O     . ALA B  1  257 ? 51.002  38.977  -19.030 1.00 7.75  ? 257  ALA B O     1 
ATOM   5995  C CB    . ALA B  1  257 ? 53.581  37.886  -19.766 1.00 7.58  ? 257  ALA B CB    1 
ATOM   5996  N N     . GLY B  1  258 ? 50.936  37.404  -17.428 1.00 6.30  ? 258  GLY B N     1 
ATOM   5997  C CA    . GLY B  1  258 ? 49.488  37.453  -17.286 1.00 7.48  ? 258  GLY B CA    1 
ATOM   5998  C C     . GLY B  1  258 ? 48.669  36.539  -18.179 1.00 8.31  ? 258  GLY B C     1 
ATOM   5999  O O     . GLY B  1  258 ? 49.180  35.915  -19.114 1.00 8.84  ? 258  GLY B O     1 
ATOM   6000  N N     . THR B  1  259 ? 47.378  36.467  -17.878 1.00 6.97  ? 259  THR B N     1 
ATOM   6001  C CA    . THR B  1  259 ? 46.433  35.643  -18.622 1.00 7.95  ? 259  THR B CA    1 
ATOM   6002  C C     . THR B  1  259 ? 46.500  35.914  -20.121 1.00 8.38  ? 259  THR B C     1 
ATOM   6003  O O     . THR B  1  259 ? 46.399  34.997  -20.937 1.00 9.02  ? 259  THR B O     1 
ATOM   6004  C CB    . THR B  1  259 ? 45.000  35.903  -18.112 1.00 8.52  ? 259  THR B CB    1 
ATOM   6005  O OG1   . THR B  1  259 ? 44.909  35.488  -16.740 1.00 10.24 ? 259  THR B OG1   1 
ATOM   6006  C CG2   . THR B  1  259 ? 43.972  35.153  -18.952 1.00 8.10  ? 259  THR B CG2   1 
ATOM   6007  N N     . ILE B  1  260 ? 46.684  37.176  -20.486 1.00 8.60  ? 260  ILE B N     1 
ATOM   6008  C CA    . ILE B  1  260 ? 46.760  37.549  -21.888 1.00 8.17  ? 260  ILE B CA    1 
ATOM   6009  C C     . ILE B  1  260 ? 48.186  37.476  -22.421 1.00 8.09  ? 260  ILE B C     1 
ATOM   6010  O O     . ILE B  1  260 ? 48.429  36.912  -23.486 1.00 8.70  ? 260  ILE B O     1 
ATOM   6011  C CB    . ILE B  1  260 ? 46.218  38.985  -22.112 1.00 9.30  ? 260  ILE B CB    1 
ATOM   6012  C CG1   . ILE B  1  260 ? 44.789  39.101  -21.568 1.00 11.99 ? 260  ILE B CG1   1 
ATOM   6013  C CG2   . ILE B  1  260 ? 46.247  39.324  -23.592 1.00 7.89  ? 260  ILE B CG2   1 
ATOM   6014  C CD1   . ILE B  1  260 ? 43.804  38.126  -22.184 1.00 13.49 ? 260  ILE B CD1   1 
ATOM   6015  N N     . GLY B  1  261 ? 49.131  38.028  -21.668 1.00 8.37  ? 261  GLY B N     1 
ATOM   6016  C CA    . GLY B  1  261 ? 50.516  38.048  -22.110 1.00 8.21  ? 261  GLY B CA    1 
ATOM   6017  C C     . GLY B  1  261 ? 51.287  36.742  -22.181 1.00 8.06  ? 261  GLY B C     1 
ATOM   6018  O O     . GLY B  1  261 ? 52.091  36.552  -23.091 1.00 7.62  ? 261  GLY B O     1 
ATOM   6019  N N     . THR B  1  262 ? 51.062  35.845  -21.231 1.00 7.96  ? 262  THR B N     1 
ATOM   6020  C CA    . THR B  1  262 ? 51.786  34.577  -21.221 1.00 6.82  ? 262  THR B CA    1 
ATOM   6021  C C     . THR B  1  262 ? 51.477  33.670  -22.416 1.00 8.55  ? 262  THR B C     1 
ATOM   6022  O O     . THR B  1  262 ? 52.395  33.238  -23.117 1.00 7.65  ? 262  THR B O     1 
ATOM   6023  C CB    . THR B  1  262 ? 51.552  33.838  -19.891 1.00 6.50  ? 262  THR B CB    1 
ATOM   6024  O OG1   . THR B  1  262 ? 52.221  34.556  -18.844 1.00 7.26  ? 262  THR B OG1   1 
ATOM   6025  C CG2   . THR B  1  262 ? 52.094  32.418  -19.951 1.00 7.97  ? 262  THR B CG2   1 
ATOM   6026  N N     . PRO B  1  263 ? 50.192  33.376  -22.679 1.00 7.65  ? 263  PRO B N     1 
ATOM   6027  C CA    . PRO B  1  263 ? 49.902  32.510  -23.829 1.00 8.05  ? 263  PRO B CA    1 
ATOM   6028  C C     . PRO B  1  263 ? 50.409  33.149  -25.124 1.00 8.13  ? 263  PRO B C     1 
ATOM   6029  O O     . PRO B  1  263 ? 50.902  32.463  -26.015 1.00 8.90  ? 263  PRO B O     1 
ATOM   6030  C CB    . PRO B  1  263 ? 48.379  32.392  -23.806 1.00 8.74  ? 263  PRO B CB    1 
ATOM   6031  C CG    . PRO B  1  263 ? 48.035  32.590  -22.355 1.00 8.64  ? 263  PRO B CG    1 
ATOM   6032  C CD    . PRO B  1  263 ? 48.957  33.715  -21.949 1.00 7.88  ? 263  PRO B CD    1 
ATOM   6033  N N     . GLN B  1  264 ? 50.279  34.469  -25.222 1.00 7.98  ? 264  GLN B N     1 
ATOM   6034  C CA    . GLN B  1  264 ? 50.743  35.181  -26.407 1.00 8.76  ? 264  GLN B CA    1 
ATOM   6035  C C     . GLN B  1  264 ? 52.235  34.963  -26.639 1.00 7.26  ? 264  GLN B C     1 
ATOM   6036  O O     . GLN B  1  264 ? 52.648  34.632  -27.750 1.00 8.52  ? 264  GLN B O     1 
ATOM   6037  C CB    . GLN B  1  264 ? 50.476  36.684  -26.281 1.00 7.49  ? 264  GLN B CB    1 
ATOM   6038  C CG    . GLN B  1  264 ? 51.134  37.509  -27.382 1.00 8.62  ? 264  GLN B CG    1 
ATOM   6039  C CD    . GLN B  1  264 ? 50.972  39.002  -27.173 1.00 9.70  ? 264  GLN B CD    1 
ATOM   6040  O OE1   . GLN B  1  264 ? 51.139  39.504  -26.063 1.00 9.44  ? 264  GLN B OE1   1 
ATOM   6041  N NE2   . GLN B  1  264 ? 50.657  39.721  -28.245 1.00 9.29  ? 264  GLN B NE2   1 
ATOM   6042  N N     . LEU B  1  265 ? 53.043  35.159  -25.597 1.00 7.76  ? 265  LEU B N     1 
ATOM   6043  C CA    . LEU B  1  265 ? 54.490  34.989  -25.727 1.00 7.75  ? 265  LEU B CA    1 
ATOM   6044  C C     . LEU B  1  265 ? 54.867  33.546  -26.067 1.00 8.45  ? 265  LEU B C     1 
ATOM   6045  O O     . LEU B  1  265 ? 55.784  33.313  -26.860 1.00 10.01 ? 265  LEU B O     1 
ATOM   6046  C CB    . LEU B  1  265 ? 55.208  35.425  -24.443 1.00 9.34  ? 265  LEU B CB    1 
ATOM   6047  C CG    . LEU B  1  265 ? 56.734  35.263  -24.459 1.00 9.50  ? 265  LEU B CG    1 
ATOM   6048  C CD1   . LEU B  1  265 ? 57.336  36.089  -25.598 1.00 11.32 ? 265  LEU B CD1   1 
ATOM   6049  C CD2   . LEU B  1  265 ? 57.311  35.696  -23.117 1.00 10.50 ? 265  LEU B CD2   1 
ATOM   6050  N N     . LEU B  1  266 ? 54.170  32.580  -25.474 1.00 7.86  ? 266  LEU B N     1 
ATOM   6051  C CA    . LEU B  1  266 ? 54.459  31.175  -25.754 1.00 7.86  ? 266  LEU B CA    1 
ATOM   6052  C C     . LEU B  1  266 ? 54.188  30.859  -27.222 1.00 7.71  ? 266  LEU B C     1 
ATOM   6053  O O     . LEU B  1  266 ? 55.004  30.215  -27.881 1.00 7.97  ? 266  LEU B O     1 
ATOM   6054  C CB    . LEU B  1  266 ? 53.624  30.259  -24.853 1.00 7.59  ? 266  LEU B CB    1 
ATOM   6055  C CG    . LEU B  1  266 ? 54.050  30.234  -23.380 1.00 7.67  ? 266  LEU B CG    1 
ATOM   6056  C CD1   . LEU B  1  266 ? 53.017  29.484  -22.553 1.00 9.18  ? 266  LEU B CD1   1 
ATOM   6057  C CD2   . LEU B  1  266 ? 55.425  29.577  -23.253 1.00 8.90  ? 266  LEU B CD2   1 
ATOM   6058  N N     . LEU B  1  267 ? 53.049  31.316  -27.734 1.00 8.16  ? 267  LEU B N     1 
ATOM   6059  C CA    . LEU B  1  267 ? 52.709  31.078  -29.131 1.00 8.46  ? 267  LEU B CA    1 
ATOM   6060  C C     . LEU B  1  267 ? 53.755  31.707  -30.047 1.00 9.95  ? 267  LEU B C     1 
ATOM   6061  O O     . LEU B  1  267 ? 54.257  31.061  -30.967 1.00 10.03 ? 267  LEU B O     1 
ATOM   6062  C CB    . LEU B  1  267 ? 51.327  31.656  -29.450 1.00 9.29  ? 267  LEU B CB    1 
ATOM   6063  C CG    . LEU B  1  267 ? 50.142  30.970  -28.768 1.00 7.71  ? 267  LEU B CG    1 
ATOM   6064  C CD1   . LEU B  1  267 ? 48.881  31.793  -28.986 1.00 9.33  ? 267  LEU B CD1   1 
ATOM   6065  C CD2   . LEU B  1  267 ? 49.974  29.552  -29.313 1.00 8.71  ? 267  LEU B CD2   1 
ATOM   6066  N N     . LEU B  1  268 ? 54.087  32.968  -29.788 1.00 8.50  ? 268  LEU B N     1 
ATOM   6067  C CA    . LEU B  1  268 ? 55.075  33.674  -30.597 1.00 9.63  ? 268  LEU B CA    1 
ATOM   6068  C C     . LEU B  1  268 ? 56.444  33.001  -30.546 1.00 9.66  ? 268  LEU B C     1 
ATOM   6069  O O     . LEU B  1  268 ? 57.269  33.189  -31.443 1.00 11.63 ? 268  LEU B O     1 
ATOM   6070  C CB    . LEU B  1  268 ? 55.202  35.129  -30.129 1.00 8.60  ? 268  LEU B CB    1 
ATOM   6071  C CG    . LEU B  1  268 ? 54.045  36.077  -30.453 1.00 10.01 ? 268  LEU B CG    1 
ATOM   6072  C CD1   . LEU B  1  268 ? 54.264  37.409  -29.747 1.00 10.30 ? 268  LEU B CD1   1 
ATOM   6073  C CD2   . LEU B  1  268 ? 53.949  36.278  -31.960 1.00 10.39 ? 268  LEU B CD2   1 
ATOM   6074  N N     . SER B  1  269 ? 56.674  32.206  -29.505 1.00 8.86  ? 269  SER B N     1 
ATOM   6075  C CA    . SER B  1  269 ? 57.950  31.519  -29.330 1.00 9.05  ? 269  SER B CA    1 
ATOM   6076  C C     . SER B  1  269 ? 57.958  30.092  -29.867 1.00 10.37 ? 269  SER B C     1 
ATOM   6077  O O     . SER B  1  269 ? 58.931  29.363  -29.686 1.00 11.82 ? 269  SER B O     1 
ATOM   6078  C CB    . SER B  1  269 ? 58.337  31.514  -27.847 1.00 9.96  ? 269  SER B CB    1 
ATOM   6079  O OG    . SER B  1  269 ? 58.436  32.841  -27.357 1.00 9.80  ? 269  SER B OG    1 
ATOM   6080  N N     . GLY B  1  270 ? 56.871  29.686  -30.513 1.00 9.51  ? 270  GLY B N     1 
ATOM   6081  C CA    . GLY B  1  270 ? 56.819  28.345  -31.070 1.00 10.12 ? 270  GLY B CA    1 
ATOM   6082  C C     . GLY B  1  270 ? 56.285  27.261  -30.156 1.00 9.05  ? 270  GLY B C     1 
ATOM   6083  O O     . GLY B  1  270 ? 56.438  26.073  -30.448 1.00 10.77 ? 270  GLY B O     1 
ATOM   6084  N N     . VAL B  1  271 ? 55.666  27.649  -29.045 1.00 8.59  ? 271  VAL B N     1 
ATOM   6085  C CA    . VAL B  1  271 ? 55.099  26.665  -28.128 1.00 9.20  ? 271  VAL B CA    1 
ATOM   6086  C C     . VAL B  1  271 ? 53.578  26.787  -28.168 1.00 9.78  ? 271  VAL B C     1 
ATOM   6087  O O     . VAL B  1  271 ? 52.999  27.696  -27.571 1.00 9.05  ? 271  VAL B O     1 
ATOM   6088  C CB    . VAL B  1  271 ? 55.602  26.881  -26.683 1.00 9.95  ? 271  VAL B CB    1 
ATOM   6089  C CG1   . VAL B  1  271 ? 55.043  25.802  -25.770 1.00 9.80  ? 271  VAL B CG1   1 
ATOM   6090  C CG2   . VAL B  1  271 ? 57.122  26.861  -26.655 1.00 11.33 ? 271  VAL B CG2   1 
ATOM   6091  N N     . GLY B  1  272 ? 52.942  25.868  -28.889 1.00 8.29  ? 272  GLY B N     1 
ATOM   6092  C CA    . GLY B  1  272 ? 51.495  25.885  -29.019 1.00 8.06  ? 272  GLY B CA    1 
ATOM   6093  C C     . GLY B  1  272 ? 51.029  24.838  -30.014 1.00 9.35  ? 272  GLY B C     1 
ATOM   6094  O O     . GLY B  1  272 ? 51.841  24.036  -30.466 1.00 8.68  ? 272  GLY B O     1 
ATOM   6095  N N     . PRO B  1  273 ? 49.737  24.824  -30.387 1.00 9.35  ? 273  PRO B N     1 
ATOM   6096  C CA    . PRO B  1  273 ? 49.201  23.844  -31.342 1.00 10.19 ? 273  PRO B CA    1 
ATOM   6097  C C     . PRO B  1  273 ? 49.989  23.839  -32.647 1.00 10.55 ? 273  PRO B C     1 
ATOM   6098  O O     . PRO B  1  273 ? 50.138  24.872  -33.290 1.00 8.96  ? 273  PRO B O     1 
ATOM   6099  C CB    . PRO B  1  273 ? 47.762  24.309  -31.542 1.00 11.19 ? 273  PRO B CB    1 
ATOM   6100  C CG    . PRO B  1  273 ? 47.435  24.973  -30.231 1.00 10.94 ? 273  PRO B CG    1 
ATOM   6101  C CD    . PRO B  1  273 ? 48.685  25.758  -29.952 1.00 11.16 ? 273  PRO B CD    1 
ATOM   6102  N N     . GLU B  1  274 ? 50.485  22.668  -33.030 1.00 9.52  ? 274  GLU B N     1 
ATOM   6103  C CA    . GLU B  1  274 ? 51.283  22.518  -34.243 1.00 10.96 ? 274  GLU B CA    1 
ATOM   6104  C C     . GLU B  1  274 ? 50.626  23.093  -35.493 1.00 10.24 ? 274  GLU B C     1 
ATOM   6105  O O     . GLU B  1  274 ? 51.225  23.887  -36.209 1.00 11.19 ? 274  GLU B O     1 
ATOM   6106  C CB    . GLU B  1  274 ? 51.602  21.032  -34.462 1.00 13.50 ? 274  GLU B CB    1 
ATOM   6107  C CG    . GLU B  1  274 ? 52.677  20.736  -35.509 1.00 18.49 ? 274  GLU B CG    1 
ATOM   6108  C CD    . GLU B  1  274 ? 52.254  21.070  -36.925 1.00 21.09 ? 274  GLU B CD    1 
ATOM   6109  O OE1   . GLU B  1  274 ? 51.096  20.771  -37.290 1.00 23.35 ? 274  GLU B OE1   1 
ATOM   6110  O OE2   . GLU B  1  274 ? 53.088  21.611  -37.685 1.00 21.91 ? 274  GLU B OE2   1 
ATOM   6111  N N     . SER B  1  275 ? 49.391  22.697  -35.763 1.00 10.81 ? 275  SER B N     1 
ATOM   6112  C CA    . SER B  1  275 ? 48.729  23.188  -36.963 1.00 11.21 ? 275  SER B CA    1 
ATOM   6113  C C     . SER B  1  275 ? 48.437  24.686  -36.925 1.00 10.41 ? 275  SER B C     1 
ATOM   6114  O O     . SER B  1  275 ? 48.418  25.344  -37.964 1.00 10.91 ? 275  SER B O     1 
ATOM   6115  C CB    . SER B  1  275 ? 47.444  22.405  -37.222 1.00 13.53 ? 275  SER B CB    1 
ATOM   6116  O OG    . SER B  1  275 ? 46.508  22.599  -36.198 1.00 20.10 ? 275  SER B OG    1 
ATOM   6117  N N     . TYR B  1  276 ? 48.193  25.228  -35.736 1.00 10.18 ? 276  TYR B N     1 
ATOM   6118  C CA    . TYR B  1  276 ? 47.925  26.658  -35.609 1.00 9.13  ? 276  TYR B CA    1 
ATOM   6119  C C     . TYR B  1  276 ? 49.197  27.434  -35.917 1.00 9.46  ? 276  TYR B C     1 
ATOM   6120  O O     . TYR B  1  276 ? 49.202  28.338  -36.746 1.00 8.21  ? 276  TYR B O     1 
ATOM   6121  C CB    . TYR B  1  276 ? 47.439  27.009  -34.193 1.00 9.17  ? 276  TYR B CB    1 
ATOM   6122  C CG    . TYR B  1  276 ? 47.303  28.501  -33.958 1.00 9.92  ? 276  TYR B CG    1 
ATOM   6123  C CD1   . TYR B  1  276 ? 46.254  29.226  -34.522 1.00 11.66 ? 276  TYR B CD1   1 
ATOM   6124  C CD2   . TYR B  1  276 ? 48.251  29.195  -33.208 1.00 11.26 ? 276  TYR B CD2   1 
ATOM   6125  C CE1   . TYR B  1  276 ? 46.153  30.604  -34.347 1.00 11.23 ? 276  TYR B CE1   1 
ATOM   6126  C CE2   . TYR B  1  276 ? 48.161  30.573  -33.029 1.00 11.45 ? 276  TYR B CE2   1 
ATOM   6127  C CZ    . TYR B  1  276 ? 47.112  31.270  -33.602 1.00 12.94 ? 276  TYR B CZ    1 
ATOM   6128  O OH    . TYR B  1  276 ? 47.033  32.634  -33.440 1.00 13.29 ? 276  TYR B OH    1 
ATOM   6129  N N     . LEU B  1  277 ? 50.285  27.077  -35.246 1.00 7.57  ? 277  LEU B N     1 
ATOM   6130  C CA    . LEU B  1  277 ? 51.557  27.754  -35.461 1.00 8.12  ? 277  LEU B CA    1 
ATOM   6131  C C     . LEU B  1  277 ? 52.033  27.663  -36.904 1.00 8.93  ? 277  LEU B C     1 
ATOM   6132  O O     . LEU B  1  277 ? 52.448  28.654  -37.496 1.00 8.57  ? 277  LEU B O     1 
ATOM   6133  C CB    . LEU B  1  277 ? 52.624  27.195  -34.508 1.00 8.76  ? 277  LEU B CB    1 
ATOM   6134  C CG    . LEU B  1  277 ? 52.393  27.445  -33.009 1.00 8.87  ? 277  LEU B CG    1 
ATOM   6135  C CD1   . LEU B  1  277 ? 53.515  26.808  -32.210 1.00 12.52 ? 277  LEU B CD1   1 
ATOM   6136  C CD2   . LEU B  1  277 ? 52.339  28.939  -32.742 1.00 9.28  ? 277  LEU B CD2   1 
ATOM   6137  N N     . SER B  1  278 ? 51.977  26.474  -37.482 1.00 9.94  ? 278  SER B N     1 
ATOM   6138  C CA    . SER B  1  278 ? 52.414  26.329  -38.862 1.00 10.00 ? 278  SER B CA    1 
ATOM   6139  C C     . SER B  1  278 ? 51.533  27.110  -39.843 1.00 9.60  ? 278  SER B C     1 
ATOM   6140  O O     . SER B  1  278 ? 52.011  27.555  -40.881 1.00 11.45 ? 278  SER B O     1 
ATOM   6141  C CB    . SER B  1  278 ? 52.472  24.851  -39.264 1.00 13.32 ? 278  SER B CB    1 
ATOM   6142  O OG    A SER B  1  278 ? 51.192  24.266  -39.296 0.50 12.70 ? 278  SER B OG    1 
ATOM   6143  O OG    B SER B  1  278 ? 53.167  23.984  -38.466 0.50 13.64 ? 278  SER B OG    1 
ATOM   6144  N N     . SER B  1  279 ? 50.254  27.289  -39.524 1.00 10.38 ? 279  SER B N     1 
ATOM   6145  C CA    . SER B  1  279 ? 49.361  28.031  -40.417 1.00 10.33 ? 279  SER B CA    1 
ATOM   6146  C C     . SER B  1  279 ? 49.839  29.469  -40.518 1.00 11.27 ? 279  SER B C     1 
ATOM   6147  O O     . SER B  1  279 ? 49.579  30.153  -41.506 1.00 10.98 ? 279  SER B O     1 
ATOM   6148  C CB    . SER B  1  279 ? 47.911  28.010  -39.906 1.00 11.56 ? 279  SER B CB    1 
ATOM   6149  O OG    . SER B  1  279 ? 47.736  28.898  -38.819 1.00 12.89 ? 279  SER B OG    1 
ATOM   6150  N N     . LEU B  1  280 ? 50.549  29.923  -39.493 1.00 8.85  ? 280  LEU B N     1 
ATOM   6151  C CA    . LEU B  1  280 ? 51.061  31.290  -39.458 1.00 9.80  ? 280  LEU B CA    1 
ATOM   6152  C C     . LEU B  1  280 ? 52.555  31.360  -39.756 1.00 10.83 ? 280  LEU B C     1 
ATOM   6153  O O     . LEU B  1  280 ? 53.163  32.431  -39.686 1.00 10.71 ? 280  LEU B O     1 
ATOM   6154  C CB    . LEU B  1  280 ? 50.784  31.915  -38.088 1.00 10.08 ? 280  LEU B CB    1 
ATOM   6155  C CG    . LEU B  1  280 ? 49.313  32.019  -37.686 1.00 10.27 ? 280  LEU B CG    1 
ATOM   6156  C CD1   . LEU B  1  280 ? 49.208  32.618  -36.292 1.00 12.48 ? 280  LEU B CD1   1 
ATOM   6157  C CD2   . LEU B  1  280 ? 48.565  32.874  -38.702 1.00 11.29 ? 280  LEU B CD2   1 
ATOM   6158  N N     . ASN B  1  281 ? 53.138  30.209  -40.079 1.00 10.36 ? 281  ASN B N     1 
ATOM   6159  C CA    . ASN B  1  281 ? 54.559  30.104  -40.392 1.00 11.20 ? 281  ASN B CA    1 
ATOM   6160  C C     . ASN B  1  281 ? 55.466  30.368  -39.193 1.00 10.19 ? 281  ASN B C     1 
ATOM   6161  O O     . ASN B  1  281 ? 56.610  30.792  -39.354 1.00 12.78 ? 281  ASN B O     1 
ATOM   6162  C CB    . ASN B  1  281 ? 54.923  31.049  -41.539 1.00 11.97 ? 281  ASN B CB    1 
ATOM   6163  C CG    . ASN B  1  281 ? 54.287  30.637  -42.848 1.00 13.34 ? 281  ASN B CG    1 
ATOM   6164  O OD1   . ASN B  1  281 ? 54.016  31.473  -43.709 1.00 16.28 ? 281  ASN B OD1   1 
ATOM   6165  N ND2   . ASN B  1  281 ? 54.057  29.340  -43.012 1.00 11.86 ? 281  ASN B ND2   1 
ATOM   6166  N N     . ILE B  1  282 ? 54.945  30.134  -37.993 1.00 9.61  ? 282  ILE B N     1 
ATOM   6167  C CA    . ILE B  1  282 ? 55.737  30.306  -36.781 1.00 9.69  ? 282  ILE B CA    1 
ATOM   6168  C C     . ILE B  1  282 ? 56.395  28.949  -36.535 1.00 10.54 ? 282  ILE B C     1 
ATOM   6169  O O     . ILE B  1  282 ? 55.709  27.938  -36.408 1.00 10.29 ? 282  ILE B O     1 
ATOM   6170  C CB    . ILE B  1  282 ? 54.850  30.667  -35.570 1.00 9.25  ? 282  ILE B CB    1 
ATOM   6171  C CG1   . ILE B  1  282 ? 54.204  32.039  -35.791 1.00 9.49  ? 282  ILE B CG1   1 
ATOM   6172  C CG2   . ILE B  1  282 ? 55.691  30.665  -34.290 1.00 10.07 ? 282  ILE B CG2   1 
ATOM   6173  C CD1   . ILE B  1  282 ? 53.118  32.382  -34.780 1.00 10.83 ? 282  ILE B CD1   1 
ATOM   6174  N N     . PRO B  1  283 ? 57.736  28.902  -36.498 1.00 12.03 ? 283  PRO B N     1 
ATOM   6175  C CA    . PRO B  1  283 ? 58.413  27.622  -36.267 1.00 12.80 ? 283  PRO B CA    1 
ATOM   6176  C C     . PRO B  1  283 ? 57.935  26.951  -34.986 1.00 12.66 ? 283  PRO B C     1 
ATOM   6177  O O     . PRO B  1  283 ? 57.827  27.595  -33.942 1.00 14.61 ? 283  PRO B O     1 
ATOM   6178  C CB    . PRO B  1  283 ? 59.883  28.020  -36.199 1.00 12.78 ? 283  PRO B CB    1 
ATOM   6179  C CG    . PRO B  1  283 ? 59.944  29.189  -37.139 1.00 14.94 ? 283  PRO B CG    1 
ATOM   6180  C CD    . PRO B  1  283 ? 58.713  29.974  -36.751 1.00 11.95 ? 283  PRO B CD    1 
ATOM   6181  N N     . VAL B  1  284 ? 57.646  25.658  -35.071 1.00 13.45 ? 284  VAL B N     1 
ATOM   6182  C CA    . VAL B  1  284 ? 57.173  24.907  -33.916 1.00 12.99 ? 284  VAL B CA    1 
ATOM   6183  C C     . VAL B  1  284 ? 58.324  24.336  -33.095 1.00 14.22 ? 284  VAL B C     1 
ATOM   6184  O O     . VAL B  1  284 ? 59.112  23.533  -33.595 1.00 15.28 ? 284  VAL B O     1 
ATOM   6185  C CB    . VAL B  1  284 ? 56.258  23.739  -34.348 1.00 13.12 ? 284  VAL B CB    1 
ATOM   6186  C CG1   . VAL B  1  284 ? 55.839  22.921  -33.133 1.00 15.11 ? 284  VAL B CG1   1 
ATOM   6187  C CG2   . VAL B  1  284 ? 55.031  24.282  -35.064 1.00 12.89 ? 284  VAL B CG2   1 
ATOM   6188  N N     . VAL B  1  285 ? 58.417  24.761  -31.839 1.00 12.26 ? 285  VAL B N     1 
ATOM   6189  C CA    . VAL B  1  285 ? 59.452  24.274  -30.933 1.00 12.24 ? 285  VAL B CA    1 
ATOM   6190  C C     . VAL B  1  285 ? 58.927  22.983  -30.309 1.00 11.93 ? 285  VAL B C     1 
ATOM   6191  O O     . VAL B  1  285 ? 59.630  21.977  -30.248 1.00 13.44 ? 285  VAL B O     1 
ATOM   6192  C CB    . VAL B  1  285 ? 59.760  25.311  -29.833 1.00 12.66 ? 285  VAL B CB    1 
ATOM   6193  C CG1   . VAL B  1  285 ? 60.645  24.695  -28.758 1.00 11.80 ? 285  VAL B CG1   1 
ATOM   6194  C CG2   . VAL B  1  285 ? 60.457  26.515  -30.451 1.00 13.50 ? 285  VAL B CG2   1 
ATOM   6195  N N     . LEU B  1  286 ? 57.680  23.020  -29.855 1.00 10.64 ? 286  LEU B N     1 
ATOM   6196  C CA    . LEU B  1  286 ? 57.037  21.850  -29.276 1.00 11.04 ? 286  LEU B CA    1 
ATOM   6197  C C     . LEU B  1  286 ? 55.530  22.013  -29.409 1.00 12.28 ? 286  LEU B C     1 
ATOM   6198  O O     . LEU B  1  286 ? 54.970  23.035  -29.003 1.00 12.32 ? 286  LEU B O     1 
ATOM   6199  C CB    . LEU B  1  286 ? 57.413  21.684  -27.799 1.00 12.59 ? 286  LEU B CB    1 
ATOM   6200  C CG    . LEU B  1  286 ? 56.760  20.505  -27.068 1.00 13.02 ? 286  LEU B CG    1 
ATOM   6201  C CD1   . LEU B  1  286 ? 57.118  19.191  -27.754 1.00 15.28 ? 286  LEU B CD1   1 
ATOM   6202  C CD2   . LEU B  1  286 ? 57.219  20.491  -25.616 1.00 15.03 ? 286  LEU B CD2   1 
ATOM   6203  N N     . SER B  1  287 ? 54.877  21.015  -29.994 1.00 11.69 ? 287  SER B N     1 
ATOM   6204  C CA    . SER B  1  287 ? 53.434  21.070  -30.158 1.00 11.11 ? 287  SER B CA    1 
ATOM   6205  C C     . SER B  1  287 ? 52.804  20.973  -28.772 1.00 11.95 ? 287  SER B C     1 
ATOM   6206  O O     . SER B  1  287 ? 52.961  19.970  -28.072 1.00 12.54 ? 287  SER B O     1 
ATOM   6207  C CB    . SER B  1  287 ? 52.942  19.925  -31.047 1.00 11.02 ? 287  SER B CB    1 
ATOM   6208  O OG    . SER B  1  287 ? 51.566  20.082  -31.343 1.00 12.67 ? 287  SER B OG    1 
ATOM   6209  N N     . HIS B  1  288 ? 52.105  22.034  -28.386 1.00 10.83 ? 288  HIS B N     1 
ATOM   6210  C CA    . HIS B  1  288 ? 51.451  22.137  -27.084 1.00 10.46 ? 288  HIS B CA    1 
ATOM   6211  C C     . HIS B  1  288 ? 50.006  22.557  -27.353 1.00 10.97 ? 288  HIS B C     1 
ATOM   6212  O O     . HIS B  1  288 ? 49.693  23.744  -27.429 1.00 10.72 ? 288  HIS B O     1 
ATOM   6213  C CB    . HIS B  1  288 ? 52.168  23.195  -26.243 1.00 12.08 ? 288  HIS B CB    1 
ATOM   6214  C CG    . HIS B  1  288 ? 52.752  22.663  -24.972 1.00 14.01 ? 288  HIS B CG    1 
ATOM   6215  N ND1   . HIS B  1  288 ? 51.978  22.135  -23.963 1.00 14.90 ? 288  HIS B ND1   1 
ATOM   6216  C CD2   . HIS B  1  288 ? 54.035  22.584  -24.545 1.00 14.61 ? 288  HIS B CD2   1 
ATOM   6217  C CE1   . HIS B  1  288 ? 52.757  21.756  -22.965 1.00 14.31 ? 288  HIS B CE1   1 
ATOM   6218  N NE2   . HIS B  1  288 ? 54.009  22.019  -23.292 1.00 14.09 ? 288  HIS B NE2   1 
ATOM   6219  N N     . PRO B  1  289 ? 49.106  21.576  -27.490 1.00 10.38 ? 289  PRO B N     1 
ATOM   6220  C CA    . PRO B  1  289 ? 47.681  21.779  -27.768 1.00 10.63 ? 289  PRO B CA    1 
ATOM   6221  C C     . PRO B  1  289 ? 46.900  22.794  -26.945 1.00 10.40 ? 289  PRO B C     1 
ATOM   6222  O O     . PRO B  1  289 ? 46.022  23.469  -27.480 1.00 10.82 ? 289  PRO B O     1 
ATOM   6223  C CB    . PRO B  1  289 ? 47.094  20.376  -27.610 1.00 12.34 ? 289  PRO B CB    1 
ATOM   6224  C CG    . PRO B  1  289 ? 48.231  19.489  -27.980 1.00 13.93 ? 289  PRO B CG    1 
ATOM   6225  C CD    . PRO B  1  289 ? 49.391  20.145  -27.282 1.00 11.36 ? 289  PRO B CD    1 
ATOM   6226  N N     . TYR B  1  290 ? 47.215  22.918  -25.661 1.00 9.07  ? 290  TYR B N     1 
ATOM   6227  C CA    . TYR B  1  290 ? 46.438  23.805  -24.808 1.00 8.00  ? 290  TYR B CA    1 
ATOM   6228  C C     . TYR B  1  290 ? 46.925  25.212  -24.501 1.00 8.89  ? 290  TYR B C     1 
ATOM   6229  O O     . TYR B  1  290 ? 46.329  25.901  -23.675 1.00 8.20  ? 290  TYR B O     1 
ATOM   6230  C CB    . TYR B  1  290 ? 46.107  23.063  -23.515 1.00 9.84  ? 290  TYR B CB    1 
ATOM   6231  C CG    . TYR B  1  290 ? 45.376  21.766  -23.792 1.00 11.68 ? 290  TYR B CG    1 
ATOM   6232  C CD1   . TYR B  1  290 ? 45.945  20.536  -23.471 1.00 13.11 ? 290  TYR B CD1   1 
ATOM   6233  C CD2   . TYR B  1  290 ? 44.132  21.772  -24.418 1.00 12.29 ? 290  TYR B CD2   1 
ATOM   6234  C CE1   . TYR B  1  290 ? 45.289  19.339  -23.772 1.00 13.85 ? 290  TYR B CE1   1 
ATOM   6235  C CE2   . TYR B  1  290 ? 43.469  20.586  -24.722 1.00 14.63 ? 290  TYR B CE2   1 
ATOM   6236  C CZ    . TYR B  1  290 ? 44.052  19.375  -24.397 1.00 15.20 ? 290  TYR B CZ    1 
ATOM   6237  O OH    . TYR B  1  290 ? 43.394  18.204  -24.697 1.00 18.26 ? 290  TYR B OH    1 
ATOM   6238  N N     . VAL B  1  291 ? 47.990  25.653  -25.158 1.00 7.82  ? 291  VAL B N     1 
ATOM   6239  C CA    . VAL B  1  291 ? 48.469  27.010  -24.936 1.00 7.59  ? 291  VAL B CA    1 
ATOM   6240  C C     . VAL B  1  291 ? 47.412  27.942  -25.534 1.00 8.20  ? 291  VAL B C     1 
ATOM   6241  O O     . VAL B  1  291 ? 47.070  27.828  -26.712 1.00 9.61  ? 291  VAL B O     1 
ATOM   6242  C CB    . VAL B  1  291 ? 49.831  27.248  -25.624 1.00 6.69  ? 291  VAL B CB    1 
ATOM   6243  C CG1   . VAL B  1  291 ? 50.185  28.730  -25.594 1.00 6.96  ? 291  VAL B CG1   1 
ATOM   6244  C CG2   . VAL B  1  291 ? 50.913  26.443  -24.907 1.00 8.71  ? 291  VAL B CG2   1 
ATOM   6245  N N     . GLY B  1  292 ? 46.877  28.840  -24.710 1.00 7.43  ? 292  GLY B N     1 
ATOM   6246  C CA    . GLY B  1  292 ? 45.856  29.763  -25.177 1.00 7.99  ? 292  GLY B CA    1 
ATOM   6247  C C     . GLY B  1  292 ? 44.447  29.204  -25.081 1.00 9.81  ? 292  GLY B C     1 
ATOM   6248  O O     . GLY B  1  292 ? 43.485  29.845  -25.505 1.00 9.08  ? 292  GLY B O     1 
ATOM   6249  N N     . GLN B  1  293 ? 44.316  28.001  -24.531 1.00 9.20  ? 293  GLN B N     1 
ATOM   6250  C CA    . GLN B  1  293 ? 43.005  27.383  -24.383 1.00 7.30  ? 293  GLN B CA    1 
ATOM   6251  C C     . GLN B  1  293 ? 42.528  27.524  -22.942 1.00 7.78  ? 293  GLN B C     1 
ATOM   6252  O O     . GLN B  1  293 ? 43.332  27.718  -22.029 1.00 8.41  ? 293  GLN B O     1 
ATOM   6253  C CB    . GLN B  1  293 ? 43.067  25.900  -24.772 1.00 8.89  ? 293  GLN B CB    1 
ATOM   6254  C CG    . GLN B  1  293 ? 43.505  25.652  -26.207 1.00 12.32 ? 293  GLN B CG    1 
ATOM   6255  C CD    . GLN B  1  293 ? 42.565  26.278  -27.221 1.00 13.49 ? 293  GLN B CD    1 
ATOM   6256  O OE1   . GLN B  1  293 ? 41.371  25.977  -27.245 1.00 17.62 ? 293  GLN B OE1   1 
ATOM   6257  N NE2   . GLN B  1  293 ? 43.100  27.152  -28.064 1.00 16.69 ? 293  GLN B NE2   1 
ATOM   6258  N N     . PHE B  1  294 ? 41.216  27.435  -22.755 1.00 8.92  ? 294  PHE B N     1 
ATOM   6259  C CA    . PHE B  1  294 ? 40.592  27.539  -21.444 1.00 9.81  ? 294  PHE B CA    1 
ATOM   6260  C C     . PHE B  1  294 ? 40.776  28.912  -20.807 1.00 10.02 ? 294  PHE B C     1 
ATOM   6261  O O     . PHE B  1  294 ? 41.305  29.034  -19.700 1.00 11.10 ? 294  PHE B O     1 
ATOM   6262  C CB    . PHE B  1  294 ? 41.130  26.447  -20.516 1.00 11.83 ? 294  PHE B CB    1 
ATOM   6263  C CG    . PHE B  1  294 ? 41.069  25.069  -21.110 1.00 14.12 ? 294  PHE B CG    1 
ATOM   6264  C CD1   . PHE B  1  294 ? 42.236  24.380  -21.419 1.00 13.94 ? 294  PHE B CD1   1 
ATOM   6265  C CD2   . PHE B  1  294 ? 39.844  24.465  -21.374 1.00 15.00 ? 294  PHE B CD2   1 
ATOM   6266  C CE1   . PHE B  1  294 ? 42.188  23.109  -21.983 1.00 16.66 ? 294  PHE B CE1   1 
ATOM   6267  C CE2   . PHE B  1  294 ? 39.783  23.191  -21.940 1.00 16.96 ? 294  PHE B CE2   1 
ATOM   6268  C CZ    . PHE B  1  294 ? 40.960  22.512  -22.245 1.00 17.61 ? 294  PHE B CZ    1 
ATOM   6269  N N     . LEU B  1  295 ? 40.350  29.943  -21.530 1.00 9.07  ? 295  LEU B N     1 
ATOM   6270  C CA    . LEU B  1  295 ? 40.400  31.326  -21.046 1.00 9.21  ? 295  LEU B CA    1 
ATOM   6271  C C     . LEU B  1  295 ? 39.055  31.565  -20.381 1.00 8.35  ? 295  LEU B C     1 
ATOM   6272  O O     . LEU B  1  295 ? 38.021  31.450  -21.033 1.00 9.73  ? 295  LEU B O     1 
ATOM   6273  C CB    . LEU B  1  295 ? 40.555  32.316  -22.204 1.00 11.60 ? 295  LEU B CB    1 
ATOM   6274  C CG    . LEU B  1  295 ? 41.935  32.756  -22.701 1.00 15.83 ? 295  LEU B CG    1 
ATOM   6275  C CD1   . LEU B  1  295 ? 42.591  33.623  -21.657 1.00 15.09 ? 295  LEU B CD1   1 
ATOM   6276  C CD2   . LEU B  1  295 ? 42.790  31.551  -23.033 1.00 15.94 ? 295  LEU B CD2   1 
ATOM   6277  N N     . HIS B  1  296 ? 39.062  31.910  -19.096 1.00 7.46  ? 296  HIS B N     1 
ATOM   6278  C CA    . HIS B  1  296 ? 37.823  32.143  -18.351 1.00 8.21  ? 296  HIS B CA    1 
ATOM   6279  C C     . HIS B  1  296 ? 37.675  33.580  -17.849 1.00 9.77  ? 296  HIS B C     1 
ATOM   6280  O O     . HIS B  1  296 ? 38.636  34.170  -17.362 1.00 12.19 ? 296  HIS B O     1 
ATOM   6281  C CB    . HIS B  1  296 ? 37.754  31.235  -17.113 1.00 8.70  ? 296  HIS B CB    1 
ATOM   6282  C CG    . HIS B  1  296 ? 37.810  29.768  -17.407 1.00 8.88  ? 296  HIS B CG    1 
ATOM   6283  N ND1   . HIS B  1  296 ? 36.770  28.916  -17.106 1.00 9.05  ? 296  HIS B ND1   1 
ATOM   6284  C CD2   . HIS B  1  296 ? 38.803  28.992  -17.900 1.00 7.49  ? 296  HIS B CD2   1 
ATOM   6285  C CE1   . HIS B  1  296 ? 37.122  27.675  -17.395 1.00 8.50  ? 296  HIS B CE1   1 
ATOM   6286  N NE2   . HIS B  1  296 ? 38.351  27.694  -17.879 1.00 8.59  ? 296  HIS B NE2   1 
ATOM   6287  N N     . ASP B  1  297 ? 36.474  34.144  -17.965 1.00 8.04  ? 297  ASP B N     1 
ATOM   6288  C CA    . ASP B  1  297 ? 36.234  35.486  -17.439 1.00 7.01  ? 297  ASP B CA    1 
ATOM   6289  C C     . ASP B  1  297 ? 34.901  35.516  -16.704 1.00 6.48  ? 297  ASP B C     1 
ATOM   6290  O O     . ASP B  1  297 ? 33.835  35.420  -17.321 1.00 7.14  ? 297  ASP B O     1 
ATOM   6291  C CB    . ASP B  1  297 ? 36.233  36.549  -18.538 1.00 6.78  ? 297  ASP B CB    1 
ATOM   6292  C CG    . ASP B  1  297 ? 36.208  37.958  -17.967 1.00 8.36  ? 297  ASP B CG    1 
ATOM   6293  O OD1   . ASP B  1  297 ? 36.911  38.196  -16.959 1.00 7.12  ? 297  ASP B OD1   1 
ATOM   6294  O OD2   . ASP B  1  297 ? 35.499  38.824  -18.524 1.00 8.41  ? 297  ASP B OD2   1 
ATOM   6295  N N     . ASN B  1  298 ? 34.960  35.646  -15.382 1.00 5.41  ? 298  ASN B N     1 
ATOM   6296  C CA    . ASN B  1  298 ? 33.745  35.682  -14.581 1.00 6.38  ? 298  ASN B CA    1 
ATOM   6297  C C     . ASN B  1  298 ? 32.892  36.863  -14.991 1.00 6.51  ? 298  ASN B C     1 
ATOM   6298  O O     . ASN B  1  298 ? 33.367  37.995  -15.038 1.00 8.22  ? 298  ASN B O     1 
ATOM   6299  C CB    . ASN B  1  298 ? 34.072  35.805  -13.094 1.00 5.50  ? 298  ASN B CB    1 
ATOM   6300  C CG    . ASN B  1  298 ? 35.034  34.736  -12.621 1.00 7.76  ? 298  ASN B CG    1 
ATOM   6301  O OD1   . ASN B  1  298 ? 36.210  34.743  -12.983 1.00 8.59  ? 298  ASN B OD1   1 
ATOM   6302  N ND2   . ASN B  1  298 ? 34.538  33.809  -11.809 1.00 8.56  ? 298  ASN B ND2   1 
ATOM   6303  N N     . PRO B  1  299 ? 31.620  36.614  -15.309 1.00 7.07  ? 299  PRO B N     1 
ATOM   6304  C CA    . PRO B  1  299 ? 30.756  37.726  -15.707 1.00 7.26  ? 299  PRO B CA    1 
ATOM   6305  C C     . PRO B  1  299 ? 30.332  38.611  -14.541 1.00 8.11  ? 299  PRO B C     1 
ATOM   6306  O O     . PRO B  1  299 ? 30.151  38.142  -13.413 1.00 9.71  ? 299  PRO B O     1 
ATOM   6307  C CB    . PRO B  1  299 ? 29.569  37.021  -16.361 1.00 8.30  ? 299  PRO B CB    1 
ATOM   6308  C CG    . PRO B  1  299 ? 29.490  35.722  -15.605 1.00 10.13 ? 299  PRO B CG    1 
ATOM   6309  C CD    . PRO B  1  299 ? 30.940  35.317  -15.485 1.00 6.98  ? 299  PRO B CD    1 
ATOM   6310  N N     . ARG B  1  300 ? 30.197  39.902  -14.820 1.00 8.08  ? 300  ARG B N     1 
ATOM   6311  C CA    . ARG B  1  300 ? 29.747  40.857  -13.819 1.00 7.94  ? 300  ARG B CA    1 
ATOM   6312  C C     . ARG B  1  300 ? 28.400  41.405  -14.265 1.00 8.35  ? 300  ARG B C     1 
ATOM   6313  O O     . ARG B  1  300 ? 28.242  41.826  -15.410 1.00 9.33  ? 300  ARG B O     1 
ATOM   6314  C CB    . ARG B  1  300 ? 30.735  42.024  -13.674 1.00 9.36  ? 300  ARG B CB    1 
ATOM   6315  C CG    . ARG B  1  300 ? 30.197  43.204  -12.842 1.00 8.22  ? 300  ARG B CG    1 
ATOM   6316  C CD    . ARG B  1  300 ? 31.313  44.181  -12.461 1.00 9.91  ? 300  ARG B CD    1 
ATOM   6317  N NE    . ARG B  1  300 ? 32.068  44.620  -13.629 1.00 11.35 ? 300  ARG B NE    1 
ATOM   6318  C CZ    . ARG B  1  300 ? 31.927  45.801  -14.226 1.00 9.78  ? 300  ARG B CZ    1 
ATOM   6319  N NH1   . ARG B  1  300 ? 31.060  46.691  -13.765 1.00 10.45 ? 300  ARG B NH1   1 
ATOM   6320  N NH2   . ARG B  1  300 ? 32.643  46.077  -15.307 1.00 10.75 ? 300  ARG B NH2   1 
ATOM   6321  N N     . ASN B  1  301 ? 27.417  41.357  -13.376 1.00 7.82  ? 301  ASN B N     1 
ATOM   6322  C CA    . ASN B  1  301 ? 26.113  41.924  -13.681 1.00 8.60  ? 301  ASN B CA    1 
ATOM   6323  C C     . ASN B  1  301 ? 25.867  42.887  -12.537 1.00 9.78  ? 301  ASN B C     1 
ATOM   6324  O O     . ASN B  1  301 ? 26.355  42.674  -11.422 1.00 9.55  ? 301  ASN B O     1 
ATOM   6325  C CB    . ASN B  1  301 ? 25.043  40.840  -13.821 1.00 9.64  ? 301  ASN B CB    1 
ATOM   6326  C CG    . ASN B  1  301 ? 25.221  40.031  -15.099 1.00 9.54  ? 301  ASN B CG    1 
ATOM   6327  O OD1   . ASN B  1  301 ? 25.973  39.058  -15.131 1.00 10.69 ? 301  ASN B OD1   1 
ATOM   6328  N ND2   . ASN B  1  301 ? 24.548  40.451  -16.168 1.00 10.46 ? 301  ASN B ND2   1 
ATOM   6329  N N     . PHE B  1  302 ? 25.116  43.947  -12.800 1.00 9.75  ? 302  PHE B N     1 
ATOM   6330  C CA    . PHE B  1  302 ? 24.972  44.982  -11.793 1.00 9.94  ? 302  PHE B CA    1 
ATOM   6331  C C     . PHE B  1  302 ? 23.733  45.850  -11.895 1.00 9.00  ? 302  PHE B C     1 
ATOM   6332  O O     . PHE B  1  302 ? 22.969  45.773  -12.855 1.00 9.92  ? 302  PHE B O     1 
ATOM   6333  C CB    . PHE B  1  302 ? 26.183  45.894  -11.938 1.00 9.08  ? 302  PHE B CB    1 
ATOM   6334  C CG    . PHE B  1  302 ? 26.343  46.435  -13.340 1.00 10.29 ? 302  PHE B CG    1 
ATOM   6335  C CD1   . PHE B  1  302 ? 25.618  47.548  -13.759 1.00 10.40 ? 302  PHE B CD1   1 
ATOM   6336  C CD2   . PHE B  1  302 ? 27.152  45.780  -14.266 1.00 11.20 ? 302  PHE B CD2   1 
ATOM   6337  C CE1   . PHE B  1  302 ? 25.692  47.999  -15.079 1.00 9.66  ? 302  PHE B CE1   1 
ATOM   6338  C CE2   . PHE B  1  302 ? 27.232  46.221  -15.586 1.00 10.84 ? 302  PHE B CE2   1 
ATOM   6339  C CZ    . PHE B  1  302 ? 26.499  47.333  -15.994 1.00 12.26 ? 302  PHE B CZ    1 
ATOM   6340  N N     . ILE B  1  303 ? 23.576  46.699  -10.882 1.00 9.26  ? 303  ILE B N     1 
ATOM   6341  C CA    . ILE B  1  303 ? 22.501  47.677  -10.819 1.00 7.39  ? 303  ILE B CA    1 
ATOM   6342  C C     . ILE B  1  303 ? 23.113  48.965  -10.269 1.00 8.33  ? 303  ILE B C     1 
ATOM   6343  O O     . ILE B  1  303 ? 23.781  48.957  -9.224  1.00 8.18  ? 303  ILE B O     1 
ATOM   6344  C CB    . ILE B  1  303 ? 21.342  47.237  -9.889  1.00 9.09  ? 303  ILE B CB    1 
ATOM   6345  C CG1   . ILE B  1  303 ? 20.591  46.052  -10.503 1.00 7.20  ? 303  ILE B CG1   1 
ATOM   6346  C CG2   . ILE B  1  303 ? 20.382  48.405  -9.673  1.00 8.80  ? 303  ILE B CG2   1 
ATOM   6347  C CD1   . ILE B  1  303 ? 19.910  46.364  -11.834 1.00 9.65  ? 303  ILE B CD1   1 
ATOM   6348  N N     . ASN B  1  304 ? 22.904  50.061  -10.994 1.00 8.82  ? 304  ASN B N     1 
ATOM   6349  C CA    . ASN B  1  304 ? 23.404  51.374  -10.600 1.00 10.26 ? 304  ASN B CA    1 
ATOM   6350  C C     . ASN B  1  304 ? 22.245  52.195  -10.056 1.00 11.11 ? 304  ASN B C     1 
ATOM   6351  O O     . ASN B  1  304 ? 21.228  52.342  -10.732 1.00 11.58 ? 304  ASN B O     1 
ATOM   6352  C CB    . ASN B  1  304 ? 23.964  52.136  -11.803 1.00 10.85 ? 304  ASN B CB    1 
ATOM   6353  C CG    . ASN B  1  304 ? 25.042  51.380  -12.530 1.00 10.48 ? 304  ASN B CG    1 
ATOM   6354  O OD1   . ASN B  1  304 ? 26.046  50.993  -11.941 1.00 9.76  ? 304  ASN B OD1   1 
ATOM   6355  N ND2   . ASN B  1  304 ? 24.845  51.174  -13.827 1.00 10.69 ? 304  ASN B ND2   1 
ATOM   6356  N N     . ILE B  1  305 ? 22.393  52.733  -8.851  1.00 11.02 ? 305  ILE B N     1 
ATOM   6357  C CA    . ILE B  1  305 ? 21.342  53.571  -8.285  1.00 10.79 ? 305  ILE B CA    1 
ATOM   6358  C C     . ILE B  1  305 ? 21.887  54.976  -8.057  1.00 11.64 ? 305  ILE B C     1 
ATOM   6359  O O     . ILE B  1  305 ? 23.056  55.155  -7.697  1.00 10.69 ? 305  ILE B O     1 
ATOM   6360  C CB    . ILE B  1  305 ? 20.791  53.018  -6.941  1.00 10.42 ? 305  ILE B CB    1 
ATOM   6361  C CG1   . ILE B  1  305 ? 21.864  53.080  -5.852  1.00 10.80 ? 305  ILE B CG1   1 
ATOM   6362  C CG2   . ILE B  1  305 ? 20.285  51.593  -7.137  1.00 9.22  ? 305  ILE B CG2   1 
ATOM   6363  C CD1   . ILE B  1  305 ? 21.328  52.835  -4.458  1.00 13.21 ? 305  ILE B CD1   1 
ATOM   6364  N N     . LEU B  1  306 ? 21.034  55.966  -8.299  1.00 12.03 ? 306  LEU B N     1 
ATOM   6365  C CA    . LEU B  1  306 ? 21.375  57.372  -8.114  1.00 13.31 ? 306  LEU B CA    1 
ATOM   6366  C C     . LEU B  1  306 ? 20.531  57.895  -6.953  1.00 14.36 ? 306  LEU B C     1 
ATOM   6367  O O     . LEU B  1  306 ? 19.368  58.250  -7.134  1.00 15.33 ? 306  LEU B O     1 
ATOM   6368  C CB    . LEU B  1  306 ? 21.054  58.159  -9.387  1.00 14.17 ? 306  LEU B CB    1 
ATOM   6369  C CG    . LEU B  1  306 ? 21.882  57.805  -10.627 1.00 14.34 ? 306  LEU B CG    1 
ATOM   6370  C CD1   . LEU B  1  306 ? 21.098  58.125  -11.889 1.00 15.26 ? 306  LEU B CD1   1 
ATOM   6371  C CD2   . LEU B  1  306 ? 23.197  58.562  -10.593 1.00 16.78 ? 306  LEU B CD2   1 
ATOM   6372  N N     . PRO B  1  307 ? 21.106  57.935  -5.742  1.00 13.56 ? 307  PRO B N     1 
ATOM   6373  C CA    . PRO B  1  307 ? 20.403  58.412  -4.544  1.00 15.28 ? 307  PRO B CA    1 
ATOM   6374  C C     . PRO B  1  307 ? 19.960  59.869  -4.660  1.00 16.23 ? 307  PRO B C     1 
ATOM   6375  O O     . PRO B  1  307 ? 20.596  60.668  -5.351  1.00 15.88 ? 307  PRO B O     1 
ATOM   6376  C CB    . PRO B  1  307 ? 21.438  58.227  -3.430  1.00 16.43 ? 307  PRO B CB    1 
ATOM   6377  C CG    . PRO B  1  307 ? 22.318  57.119  -3.945  1.00 17.80 ? 307  PRO B CG    1 
ATOM   6378  C CD    . PRO B  1  307 ? 22.465  57.480  -5.402  1.00 15.99 ? 307  PRO B CD    1 
ATOM   6379  N N     . PRO B  1  308 ? 18.857  60.232  -3.981  1.00 17.79 ? 308  PRO B N     1 
ATOM   6380  C CA    . PRO B  1  308 ? 18.339  61.604  -4.009  1.00 18.21 ? 308  PRO B CA    1 
ATOM   6381  C C     . PRO B  1  308 ? 19.270  62.556  -3.258  1.00 18.99 ? 308  PRO B C     1 
ATOM   6382  O O     . PRO B  1  308 ? 19.292  63.758  -3.520  1.00 18.55 ? 308  PRO B O     1 
ATOM   6383  C CB    . PRO B  1  308 ? 16.970  61.466  -3.348  1.00 19.17 ? 308  PRO B CB    1 
ATOM   6384  C CG    . PRO B  1  308 ? 17.176  60.357  -2.367  1.00 18.44 ? 308  PRO B CG    1 
ATOM   6385  C CD    . PRO B  1  308 ? 17.979  59.357  -3.184  1.00 18.00 ? 308  PRO B CD    1 
ATOM   6386  N N     . ASN B  1  309 ? 20.032  61.999  -2.321  1.00 18.90 ? 309  ASN B N     1 
ATOM   6387  C CA    . ASN B  1  309 ? 20.984  62.768  -1.535  1.00 19.11 ? 309  ASN B CA    1 
ATOM   6388  C C     . ASN B  1  309 ? 22.366  62.217  -1.826  1.00 19.56 ? 309  ASN B C     1 
ATOM   6389  O O     . ASN B  1  309 ? 22.534  61.015  -2.040  1.00 19.79 ? 309  ASN B O     1 
ATOM   6390  C CB    . ASN B  1  309 ? 20.655  62.660  -0.040  1.00 19.50 ? 309  ASN B CB    1 
ATOM   6391  C CG    . ASN B  1  309 ? 19.292  63.233  0.291   1.00 19.67 ? 309  ASN B CG    1 
ATOM   6392  O OD1   . ASN B  1  309 ? 19.056  64.430  0.135   1.00 19.60 ? 309  ASN B OD1   1 
ATOM   6393  N ND2   . ASN B  1  309 ? 18.384  62.377  0.744   1.00 20.69 ? 309  ASN B ND2   1 
ATOM   6394  N N     . PRO B  1  310 ? 23.382  63.092  -1.837  1.00 19.96 ? 310  PRO B N     1 
ATOM   6395  C CA    . PRO B  1  310 ? 24.756  62.661  -2.114  1.00 19.55 ? 310  PRO B CA    1 
ATOM   6396  C C     . PRO B  1  310 ? 25.288  61.568  -1.183  1.00 18.99 ? 310  PRO B C     1 
ATOM   6397  O O     . PRO B  1  310 ? 24.999  61.562  0.007   1.00 18.44 ? 310  PRO B O     1 
ATOM   6398  C CB    . PRO B  1  310 ? 25.568  63.956  -1.954  1.00 20.44 ? 310  PRO B CB    1 
ATOM   6399  C CG    . PRO B  1  310 ? 24.573  65.052  -2.178  1.00 20.25 ? 310  PRO B CG    1 
ATOM   6400  C CD    . PRO B  1  310 ? 23.344  64.525  -1.485  1.00 21.57 ? 310  PRO B CD    1 
ATOM   6401  N N     . ILE B  1  311 ? 26.051  60.636  -1.743  1.00 17.44 ? 311  ILE B N     1 
ATOM   6402  C CA    . ILE B  1  311 ? 26.699  59.600  -0.957  1.00 15.86 ? 311  ILE B CA    1 
ATOM   6403  C C     . ILE B  1  311 ? 28.172  59.809  -1.247  1.00 15.56 ? 311  ILE B C     1 
ATOM   6404  O O     . ILE B  1  311 ? 28.526  60.294  -2.318  1.00 16.68 ? 311  ILE B O     1 
ATOM   6405  C CB    . ILE B  1  311 ? 26.251  58.153  -1.341  1.00 14.78 ? 311  ILE B CB    1 
ATOM   6406  C CG1   . ILE B  1  311 ? 26.452  57.883  -2.826  1.00 15.70 ? 311  ILE B CG1   1 
ATOM   6407  C CG2   . ILE B  1  311 ? 24.811  57.932  -0.937  1.00 14.93 ? 311  ILE B CG2   1 
ATOM   6408  C CD1   . ILE B  1  311 ? 26.161  56.435  -3.213  1.00 14.17 ? 311  ILE B CD1   1 
ATOM   6409  N N     . GLU B  1  312 ? 29.026  59.461  -0.298  1.00 15.60 ? 312  GLU B N     1 
ATOM   6410  C CA    . GLU B  1  312 ? 30.448  59.662  -0.489  1.00 15.66 ? 312  GLU B CA    1 
ATOM   6411  C C     . GLU B  1  312 ? 31.130  58.507  -1.215  1.00 15.64 ? 312  GLU B C     1 
ATOM   6412  O O     . GLU B  1  312 ? 30.734  57.345  -1.075  1.00 15.55 ? 312  GLU B O     1 
ATOM   6413  C CB    . GLU B  1  312 ? 31.125  59.893  0.865   1.00 17.41 ? 312  GLU B CB    1 
ATOM   6414  C CG    . GLU B  1  312 ? 31.431  58.638  1.674   1.00 20.64 ? 312  GLU B CG    1 
ATOM   6415  C CD    . GLU B  1  312 ? 30.212  57.787  2.009   1.00 22.04 ? 312  GLU B CD    1 
ATOM   6416  O OE1   . GLU B  1  312 ? 29.063  58.268  1.898   1.00 23.94 ? 312  GLU B OE1   1 
ATOM   6417  O OE2   . GLU B  1  312 ? 30.415  56.622  2.413   1.00 20.88 ? 312  GLU B OE2   1 
ATOM   6418  N N     . PRO B  1  313 ? 32.164  58.815  -2.018  1.00 15.75 ? 313  PRO B N     1 
ATOM   6419  C CA    . PRO B  1  313 ? 32.883  57.765  -2.747  1.00 15.61 ? 313  PRO B CA    1 
ATOM   6420  C C     . PRO B  1  313 ? 33.585  56.885  -1.715  1.00 14.16 ? 313  PRO B C     1 
ATOM   6421  O O     . PRO B  1  313 ? 34.014  57.366  -0.670  1.00 15.12 ? 313  PRO B O     1 
ATOM   6422  C CB    . PRO B  1  313 ? 33.890  58.550  -3.600  1.00 16.84 ? 313  PRO B CB    1 
ATOM   6423  C CG    . PRO B  1  313 ? 33.288  59.938  -3.696  1.00 18.08 ? 313  PRO B CG    1 
ATOM   6424  C CD    . PRO B  1  313 ? 32.734  60.140  -2.319  1.00 16.55 ? 313  PRO B CD    1 
ATOM   6425  N N     . THR B  1  314 ? 33.699  55.597  -1.999  1.00 13.76 ? 314  THR B N     1 
ATOM   6426  C CA    . THR B  1  314 ? 34.355  54.687  -1.071  1.00 13.09 ? 314  THR B CA    1 
ATOM   6427  C C     . THR B  1  314 ? 35.156  53.633  -1.810  1.00 12.66 ? 314  THR B C     1 
ATOM   6428  O O     . THR B  1  314 ? 34.990  53.445  -3.016  1.00 14.74 ? 314  THR B O     1 
ATOM   6429  C CB    . THR B  1  314 ? 33.326  53.941  -0.195  1.00 14.07 ? 314  THR B CB    1 
ATOM   6430  O OG1   . THR B  1  314 ? 32.395  53.255  -1.042  1.00 12.60 ? 314  THR B OG1   1 
ATOM   6431  C CG2   . THR B  1  314 ? 32.570  54.904  0.712   1.00 14.41 ? 314  THR B CG2   1 
ATOM   6432  N N     . ILE B  1  315 ? 36.052  52.968  -1.090  1.00 11.78 ? 315  ILE B N     1 
ATOM   6433  C CA    . ILE B  1  315 ? 36.802  51.876  -1.690  1.00 11.05 ? 315  ILE B CA    1 
ATOM   6434  C C     . ILE B  1  315 ? 36.013  50.649  -1.231  1.00 10.53 ? 315  ILE B C     1 
ATOM   6435  O O     . ILE B  1  315 ? 35.475  50.634  -0.123  1.00 9.92  ? 315  ILE B O     1 
ATOM   6436  C CB    . ILE B  1  315 ? 38.270  51.794  -1.179  1.00 12.09 ? 315  ILE B CB    1 
ATOM   6437  C CG1   . ILE B  1  315 ? 38.313  51.650  0.342   1.00 14.10 ? 315  ILE B CG1   1 
ATOM   6438  C CG2   . ILE B  1  315 ? 39.037  53.036  -1.614  1.00 13.75 ? 315  ILE B CG2   1 
ATOM   6439  C CD1   . ILE B  1  315 ? 39.720  51.411  0.884   1.00 13.27 ? 315  ILE B CD1   1 
ATOM   6440  N N     . VAL B  1  316 ? 35.912  49.639  -2.085  1.00 8.95  ? 316  VAL B N     1 
ATOM   6441  C CA    . VAL B  1  316 ? 35.167  48.436  -1.733  1.00 8.92  ? 316  VAL B CA    1 
ATOM   6442  C C     . VAL B  1  316 ? 35.857  47.660  -0.619  1.00 7.43  ? 316  VAL B C     1 
ATOM   6443  O O     . VAL B  1  316 ? 37.047  47.350  -0.715  1.00 8.99  ? 316  VAL B O     1 
ATOM   6444  C CB    . VAL B  1  316 ? 34.998  47.512  -2.955  1.00 9.47  ? 316  VAL B CB    1 
ATOM   6445  C CG1   . VAL B  1  316 ? 34.382  46.187  -2.527  1.00 9.53  ? 316  VAL B CG1   1 
ATOM   6446  C CG2   . VAL B  1  316 ? 34.114  48.186  -3.992  1.00 12.60 ? 316  VAL B CG2   1 
ATOM   6447  N N     . THR B  1  317 ? 35.109  47.359  0.442   1.00 7.75  ? 317  THR B N     1 
ATOM   6448  C CA    . THR B  1  317 ? 35.652  46.603  1.566   1.00 8.00  ? 317  THR B CA    1 
ATOM   6449  C C     . THR B  1  317 ? 34.668  45.549  2.071   1.00 8.04  ? 317  THR B C     1 
ATOM   6450  O O     . THR B  1  317 ? 35.076  44.526  2.627   1.00 7.76  ? 317  THR B O     1 
ATOM   6451  C CB    . THR B  1  317 ? 36.011  47.518  2.757   1.00 8.97  ? 317  THR B CB    1 
ATOM   6452  O OG1   . THR B  1  317 ? 34.824  48.155  3.245   1.00 9.28  ? 317  THR B OG1   1 
ATOM   6453  C CG2   . THR B  1  317 ? 37.025  48.574  2.342   1.00 8.77  ? 317  THR B CG2   1 
ATOM   6454  N N     . VAL B  1  318 ? 33.377  45.803  1.878   1.00 6.13  ? 318  VAL B N     1 
ATOM   6455  C CA    . VAL B  1  318 ? 32.343  44.878  2.329   1.00 6.62  ? 318  VAL B CA    1 
ATOM   6456  C C     . VAL B  1  318 ? 31.967  43.891  1.232   1.00 6.93  ? 318  VAL B C     1 
ATOM   6457  O O     . VAL B  1  318 ? 31.562  44.281  0.135   1.00 7.56  ? 318  VAL B O     1 
ATOM   6458  C CB    . VAL B  1  318 ? 31.083  45.646  2.798   1.00 7.02  ? 318  VAL B CB    1 
ATOM   6459  C CG1   . VAL B  1  318 ? 29.916  44.686  2.989   1.00 8.02  ? 318  VAL B CG1   1 
ATOM   6460  C CG2   . VAL B  1  318 ? 31.383  46.360  4.108   1.00 7.87  ? 318  VAL B CG2   1 
ATOM   6461  N N     . LEU B  1  319 ? 32.116  42.605  1.538   1.00 6.62  ? 319  LEU B N     1 
ATOM   6462  C CA    . LEU B  1  319 ? 31.804  41.556  0.578   1.00 5.92  ? 319  LEU B CA    1 
ATOM   6463  C C     . LEU B  1  319 ? 30.669  40.657  1.056   1.00 6.41  ? 319  LEU B C     1 
ATOM   6464  O O     . LEU B  1  319 ? 30.609  40.273  2.227   1.00 7.74  ? 319  LEU B O     1 
ATOM   6465  C CB    . LEU B  1  319 ? 33.054  40.711  0.302   1.00 6.78  ? 319  LEU B CB    1 
ATOM   6466  C CG    . LEU B  1  319 ? 34.309  41.475  -0.139  1.00 7.65  ? 319  LEU B CG    1 
ATOM   6467  C CD1   . LEU B  1  319 ? 35.421  40.486  -0.474  1.00 6.45  ? 319  LEU B CD1   1 
ATOM   6468  C CD2   . LEU B  1  319 ? 33.988  42.335  -1.353  1.00 9.50  ? 319  LEU B CD2   1 
ATOM   6469  N N     . GLY B  1  320 ? 29.762  40.346  0.134   1.00 5.98  ? 320  GLY B N     1 
ATOM   6470  C CA    . GLY B  1  320 ? 28.632  39.478  0.422   1.00 7.55  ? 320  GLY B CA    1 
ATOM   6471  C C     . GLY B  1  320 ? 28.880  38.231  -0.403  1.00 8.41  ? 320  GLY B C     1 
ATOM   6472  O O     . GLY B  1  320 ? 28.624  38.204  -1.612  1.00 8.13  ? 320  GLY B O     1 
ATOM   6473  N N     . ILE B  1  321 ? 29.377  37.190  0.254   1.00 8.31  ? 321  ILE B N     1 
ATOM   6474  C CA    . ILE B  1  321 ? 29.737  35.958  -0.428  1.00 8.29  ? 321  ILE B CA    1 
ATOM   6475  C C     . ILE B  1  321 ? 28.740  34.807  -0.349  1.00 9.02  ? 321  ILE B C     1 
ATOM   6476  O O     . ILE B  1  321 ? 28.344  34.382  0.730   1.00 8.81  ? 321  ILE B O     1 
ATOM   6477  C CB    . ILE B  1  321 ? 31.100  35.437  0.105   1.00 8.05  ? 321  ILE B CB    1 
ATOM   6478  C CG1   . ILE B  1  321 ? 32.172  36.521  -0.043  1.00 9.07  ? 321  ILE B CG1   1 
ATOM   6479  C CG2   . ILE B  1  321 ? 31.506  34.165  -0.629  1.00 9.15  ? 321  ILE B CG2   1 
ATOM   6480  C CD1   . ILE B  1  321 ? 32.442  36.959  -1.477  1.00 8.56  ? 321  ILE B CD1   1 
ATOM   6481  N N     . SER B  1  322 ? 28.335  34.318  -1.517  1.00 9.35  ? 322  SER B N     1 
ATOM   6482  C CA    . SER B  1  322 ? 27.445  33.167  -1.610  1.00 11.32 ? 322  SER B CA    1 
ATOM   6483  C C     . SER B  1  322 ? 28.274  32.098  -2.317  1.00 12.09 ? 322  SER B C     1 
ATOM   6484  O O     . SER B  1  322 ? 29.344  32.396  -2.849  1.00 12.46 ? 322  SER B O     1 
ATOM   6485  C CB    . SER B  1  322 ? 26.185  33.519  -2.412  1.00 12.17 ? 322  SER B CB    1 
ATOM   6486  O OG    . SER B  1  322 ? 25.391  34.477  -1.715  1.00 17.67 ? 322  SER B OG    1 
ATOM   6487  N N     . ASN B  1  323 ? 27.810  30.855  -2.316  1.00 13.18 ? 323  ASN B N     1 
ATOM   6488  C CA    . ASN B  1  323 ? 28.569  29.786  -2.954  1.00 14.35 ? 323  ASN B CA    1 
ATOM   6489  C C     . ASN B  1  323 ? 28.695  29.939  -4.461  1.00 13.41 ? 323  ASN B C     1 
ATOM   6490  O O     . ASN B  1  323 ? 29.734  29.621  -5.039  1.00 14.65 ? 323  ASN B O     1 
ATOM   6491  C CB    . ASN B  1  323 ? 27.940  28.421  -2.655  1.00 17.87 ? 323  ASN B CB    1 
ATOM   6492  C CG    . ASN B  1  323 ? 28.228  27.940  -1.250  1.00 22.14 ? 323  ASN B CG    1 
ATOM   6493  O OD1   . ASN B  1  323 ? 27.311  27.694  -0.468  1.00 25.94 ? 323  ASN B OD1   1 
ATOM   6494  N ND2   . ASN B  1  323 ? 29.507  27.795  -0.922  1.00 20.81 ? 323  ASN B ND2   1 
ATOM   6495  N N     . ASP B  1  324 ? 27.644  30.440  -5.098  1.00 11.63 ? 324  ASP B N     1 
ATOM   6496  C CA    . ASP B  1  324 ? 27.645  30.572  -6.548  1.00 11.16 ? 324  ASP B CA    1 
ATOM   6497  C C     . ASP B  1  324 ? 27.892  31.960  -7.125  1.00 8.65  ? 324  ASP B C     1 
ATOM   6498  O O     . ASP B  1  324 ? 28.033  32.104  -8.339  1.00 7.91  ? 324  ASP B O     1 
ATOM   6499  C CB    . ASP B  1  324 ? 26.331  30.015  -7.100  1.00 13.43 ? 324  ASP B CB    1 
ATOM   6500  C CG    . ASP B  1  324 ? 26.024  28.629  -6.568  1.00 14.81 ? 324  ASP B CG    1 
ATOM   6501  O OD1   . ASP B  1  324 ? 26.933  27.775  -6.580  1.00 15.22 ? 324  ASP B OD1   1 
ATOM   6502  O OD2   . ASP B  1  324 ? 24.874  28.396  -6.141  1.00 17.49 ? 324  ASP B OD2   1 
ATOM   6503  N N     . PHE B  1  325 ? 27.945  32.975  -6.270  1.00 7.58  ? 325  PHE B N     1 
ATOM   6504  C CA    . PHE B  1  325 ? 28.177  34.338  -6.729  1.00 6.58  ? 325  PHE B CA    1 
ATOM   6505  C C     . PHE B  1  325 ? 28.706  35.206  -5.590  1.00 6.74  ? 325  PHE B C     1 
ATOM   6506  O O     . PHE B  1  325 ? 28.411  34.959  -4.420  1.00 7.75  ? 325  PHE B O     1 
ATOM   6507  C CB    . PHE B  1  325 ? 26.885  34.917  -7.328  1.00 6.43  ? 325  PHE B CB    1 
ATOM   6508  C CG    . PHE B  1  325 ? 25.690  34.805  -6.424  1.00 6.84  ? 325  PHE B CG    1 
ATOM   6509  C CD1   . PHE B  1  325 ? 25.476  35.736  -5.410  1.00 7.94  ? 325  PHE B CD1   1 
ATOM   6510  C CD2   . PHE B  1  325 ? 24.786  33.753  -6.573  1.00 9.45  ? 325  PHE B CD2   1 
ATOM   6511  C CE1   . PHE B  1  325 ? 24.380  35.622  -4.556  1.00 7.82  ? 325  PHE B CE1   1 
ATOM   6512  C CE2   . PHE B  1  325 ? 23.685  33.630  -5.720  1.00 10.16 ? 325  PHE B CE2   1 
ATOM   6513  C CZ    . PHE B  1  325 ? 23.483  34.564  -4.713  1.00 7.50  ? 325  PHE B CZ    1 
ATOM   6514  N N     . TYR B  1  326 ? 29.497  36.214  -5.945  1.00 6.98  ? 326  TYR B N     1 
ATOM   6515  C CA    . TYR B  1  326 ? 30.112  37.111  -4.970  1.00 7.95  ? 326  TYR B CA    1 
ATOM   6516  C C     . TYR B  1  326 ? 29.657  38.539  -5.251  1.00 7.62  ? 326  TYR B C     1 
ATOM   6517  O O     . TYR B  1  326 ? 29.636  38.974  -6.405  1.00 8.43  ? 326  TYR B O     1 
ATOM   6518  C CB    . TYR B  1  326 ? 31.628  37.000  -5.086  1.00 8.41  ? 326  TYR B CB    1 
ATOM   6519  C CG    . TYR B  1  326 ? 32.106  35.586  -5.363  1.00 8.17  ? 326  TYR B CG    1 
ATOM   6520  C CD1   . TYR B  1  326 ? 32.941  35.319  -6.445  1.00 7.72  ? 326  TYR B CD1   1 
ATOM   6521  C CD2   . TYR B  1  326 ? 31.725  34.521  -4.547  1.00 8.53  ? 326  TYR B CD2   1 
ATOM   6522  C CE1   . TYR B  1  326 ? 33.388  34.023  -6.711  1.00 11.48 ? 326  TYR B CE1   1 
ATOM   6523  C CE2   . TYR B  1  326 ? 32.166  33.220  -4.805  1.00 10.60 ? 326  TYR B CE2   1 
ATOM   6524  C CZ    . TYR B  1  326 ? 32.998  32.984  -5.889  1.00 9.95  ? 326  TYR B CZ    1 
ATOM   6525  O OH    . TYR B  1  326 ? 33.446  31.711  -6.156  1.00 14.30 ? 326  TYR B OH    1 
ATOM   6526  N N     . GLN B  1  327 ? 29.320  39.281  -4.201  1.00 6.57  ? 327  GLN B N     1 
ATOM   6527  C CA    . GLN B  1  327 ? 28.803  40.630  -4.399  1.00 6.62  ? 327  GLN B CA    1 
ATOM   6528  C C     . GLN B  1  327 ? 29.413  41.730  -3.543  1.00 7.18  ? 327  GLN B C     1 
ATOM   6529  O O     . GLN B  1  327 ? 30.016  41.472  -2.503  1.00 7.90  ? 327  GLN B O     1 
ATOM   6530  C CB    . GLN B  1  327 ? 27.288  40.595  -4.193  1.00 7.19  ? 327  GLN B CB    1 
ATOM   6531  C CG    . GLN B  1  327 ? 26.641  39.388  -4.866  1.00 8.82  ? 327  GLN B CG    1 
ATOM   6532  C CD    . GLN B  1  327 ? 25.142  39.352  -4.714  1.00 8.56  ? 327  GLN B CD    1 
ATOM   6533  O OE1   . GLN B  1  327 ? 24.617  39.433  -3.606  1.00 10.22 ? 327  GLN B OE1   1 
ATOM   6534  N NE2   . GLN B  1  327 ? 24.438  39.217  -5.832  1.00 9.61  ? 327  GLN B NE2   1 
ATOM   6535  N N     . CYS B  1  328 ? 29.243  42.967  -3.999  1.00 8.32  ? 328  CYS B N     1 
ATOM   6536  C CA    . CYS B  1  328 ? 29.757  44.132  -3.293  1.00 9.50  ? 328  CYS B CA    1 
ATOM   6537  C C     . CYS B  1  328 ? 29.114  45.388  -3.863  1.00 9.25  ? 328  CYS B C     1 
ATOM   6538  O O     . CYS B  1  328 ? 28.317  45.321  -4.806  1.00 9.58  ? 328  CYS B O     1 
ATOM   6539  C CB    . CYS B  1  328 ? 31.279  44.227  -3.448  1.00 11.27 ? 328  CYS B CB    1 
ATOM   6540  S SG    . CYS B  1  328 ? 31.841  44.504  -5.148  1.00 16.22 ? 328  CYS B SG    1 
ATOM   6541  N N     . SER B  1  329 ? 29.462  46.533  -3.292  1.00 8.51  ? 329  SER B N     1 
ATOM   6542  C CA    . SER B  1  329 ? 28.919  47.795  -3.766  1.00 9.32  ? 329  SER B CA    1 
ATOM   6543  C C     . SER B  1  329 ? 29.993  48.868  -3.763  1.00 10.61 ? 329  SER B C     1 
ATOM   6544  O O     . SER B  1  329 ? 30.692  49.068  -2.770  1.00 13.08 ? 329  SER B O     1 
ATOM   6545  C CB    . SER B  1  329 ? 27.735  48.234  -2.903  1.00 11.79 ? 329  SER B CB    1 
ATOM   6546  O OG    . SER B  1  329 ? 27.109  49.374  -3.465  1.00 12.24 ? 329  SER B OG    1 
ATOM   6547  N N     . PHE B  1  330 ? 30.117  49.547  -4.895  1.00 10.95 ? 330  PHE B N     1 
ATOM   6548  C CA    . PHE B  1  330 ? 31.095  50.608  -5.085  1.00 12.36 ? 330  PHE B CA    1 
ATOM   6549  C C     . PHE B  1  330 ? 30.354  51.942  -5.222  1.00 11.30 ? 330  PHE B C     1 
ATOM   6550  O O     . PHE B  1  330 ? 29.450  52.060  -6.043  1.00 12.44 ? 330  PHE B O     1 
ATOM   6551  C CB    . PHE B  1  330 ? 31.891  50.305  -6.364  1.00 10.93 ? 330  PHE B CB    1 
ATOM   6552  C CG    . PHE B  1  330 ? 32.779  51.424  -6.828  1.00 14.64 ? 330  PHE B CG    1 
ATOM   6553  C CD1   . PHE B  1  330 ? 33.826  51.882  -6.037  1.00 16.88 ? 330  PHE B CD1   1 
ATOM   6554  C CD2   . PHE B  1  330 ? 32.593  51.990  -8.089  1.00 14.77 ? 330  PHE B CD2   1 
ATOM   6555  C CE1   . PHE B  1  330 ? 34.682  52.888  -6.497  1.00 18.66 ? 330  PHE B CE1   1 
ATOM   6556  C CE2   . PHE B  1  330 ? 33.440  52.993  -8.559  1.00 15.84 ? 330  PHE B CE2   1 
ATOM   6557  C CZ    . PHE B  1  330 ? 34.487  53.443  -7.762  1.00 16.90 ? 330  PHE B CZ    1 
ATOM   6558  N N     . SER B  1  331 ? 30.713  52.932  -4.409  1.00 10.41 ? 331  SER B N     1 
ATOM   6559  C CA    . SER B  1  331 ? 30.080  54.250  -4.507  1.00 11.94 ? 331  SER B CA    1 
ATOM   6560  C C     . SER B  1  331 ? 31.115  55.184  -5.126  1.00 11.32 ? 331  SER B C     1 
ATOM   6561  O O     . SER B  1  331 ? 32.300  55.118  -4.796  1.00 12.03 ? 331  SER B O     1 
ATOM   6562  C CB    . SER B  1  331 ? 29.626  54.758  -3.132  1.00 11.05 ? 331  SER B CB    1 
ATOM   6563  O OG    . SER B  1  331 ? 30.710  54.895  -2.234  1.00 10.62 ? 331  SER B OG    1 
ATOM   6564  N N     . SER B  1  332 ? 30.672  56.055  -6.021  1.00 11.70 ? 332  SER B N     1 
ATOM   6565  C CA    . SER B  1  332 ? 31.593  56.944  -6.709  1.00 13.88 ? 332  SER B CA    1 
ATOM   6566  C C     . SER B  1  332 ? 31.020  58.286  -7.114  1.00 14.38 ? 332  SER B C     1 
ATOM   6567  O O     . SER B  1  332 ? 29.811  58.489  -7.120  1.00 14.21 ? 332  SER B O     1 
ATOM   6568  C CB    . SER B  1  332 ? 32.117  56.221  -7.966  1.00 15.92 ? 332  SER B CB    1 
ATOM   6569  O OG    . SER B  1  332 ? 32.806  57.099  -8.835  1.00 17.43 ? 332  SER B OG    1 
ATOM   6570  N N     . LEU B  1  333 ? 31.914  59.201  -7.460  1.00 15.22 ? 333  LEU B N     1 
ATOM   6571  C CA    . LEU B  1  333 ? 31.520  60.515  -7.935  1.00 15.86 ? 333  LEU B CA    1 
ATOM   6572  C C     . LEU B  1  333 ? 31.047  60.276  -9.358  1.00 16.52 ? 333  LEU B C     1 
ATOM   6573  O O     . LEU B  1  333 ? 31.380  59.254  -9.960  1.00 16.66 ? 333  LEU B O     1 
ATOM   6574  C CB    . LEU B  1  333 ? 32.723  61.465  -7.946  1.00 16.09 ? 333  LEU B CB    1 
ATOM   6575  C CG    . LEU B  1  333 ? 33.348  61.860  -6.607  1.00 16.61 ? 333  LEU B CG    1 
ATOM   6576  C CD1   . LEU B  1  333 ? 34.662  62.581  -6.851  1.00 18.72 ? 333  LEU B CD1   1 
ATOM   6577  C CD2   . LEU B  1  333 ? 32.382  62.735  -5.841  1.00 18.03 ? 333  LEU B CD2   1 
ATOM   6578  N N     . PRO B  1  334 ? 30.269  61.215  -9.925  1.00 16.89 ? 334  PRO B N     1 
ATOM   6579  C CA    . PRO B  1  334 ? 29.793  61.017  -11.300 1.00 17.77 ? 334  PRO B CA    1 
ATOM   6580  C C     . PRO B  1  334 ? 30.946  60.889  -12.292 1.00 18.07 ? 334  PRO B C     1 
ATOM   6581  O O     . PRO B  1  334 ? 32.062  61.336  -12.022 1.00 18.81 ? 334  PRO B O     1 
ATOM   6582  C CB    . PRO B  1  334 ? 28.930  62.256  -11.559 1.00 18.37 ? 334  PRO B CB    1 
ATOM   6583  C CG    . PRO B  1  334 ? 29.547  63.319  -10.647 1.00 17.96 ? 334  PRO B CG    1 
ATOM   6584  C CD    . PRO B  1  334 ? 29.826  62.515  -9.383  1.00 18.02 ? 334  PRO B CD    1 
ATOM   6585  N N     . PHE B  1  335 ? 30.672  60.270  -13.436 1.00 18.56 ? 335  PHE B N     1 
ATOM   6586  C CA    . PHE B  1  335 ? 31.666  60.088  -14.490 1.00 19.29 ? 335  PHE B CA    1 
ATOM   6587  C C     . PHE B  1  335 ? 31.534  61.193  -15.535 1.00 19.85 ? 335  PHE B C     1 
ATOM   6588  O O     . PHE B  1  335 ? 30.476  61.352  -16.145 1.00 19.86 ? 335  PHE B O     1 
ATOM   6589  C CB    . PHE B  1  335 ? 31.464  58.739  -15.191 1.00 17.72 ? 335  PHE B CB    1 
ATOM   6590  C CG    . PHE B  1  335 ? 31.727  57.535  -14.320 1.00 15.66 ? 335  PHE B CG    1 
ATOM   6591  C CD1   . PHE B  1  335 ? 31.287  56.276  -14.730 1.00 15.01 ? 335  PHE B CD1   1 
ATOM   6592  C CD2   . PHE B  1  335 ? 32.435  57.639  -13.122 1.00 16.37 ? 335  PHE B CD2   1 
ATOM   6593  C CE1   . PHE B  1  335 ? 31.543  55.122  -13.962 1.00 14.56 ? 335  PHE B CE1   1 
ATOM   6594  C CE2   . PHE B  1  335 ? 32.701  56.497  -12.338 1.00 14.55 ? 335  PHE B CE2   1 
ATOM   6595  C CZ    . PHE B  1  335 ? 32.255  55.232  -12.761 1.00 14.76 ? 335  PHE B CZ    1 
ATOM   6596  N N     . THR B  1  336 ? 32.607  61.944  -15.759 1.00 21.88 ? 336  THR B N     1 
ATOM   6597  C CA    . THR B  1  336 ? 32.586  63.011  -16.757 1.00 21.85 ? 336  THR B CA    1 
ATOM   6598  C C     . THR B  1  336 ? 32.802  62.404  -18.138 1.00 20.73 ? 336  THR B C     1 
ATOM   6599  O O     . THR B  1  336 ? 32.193  62.824  -19.122 1.00 21.55 ? 336  THR B O     1 
ATOM   6600  C CB    . THR B  1  336 ? 33.677  64.063  -16.489 1.00 23.86 ? 336  THR B CB    1 
ATOM   6601  O OG1   . THR B  1  336 ? 34.958  63.426  -16.386 1.00 26.11 ? 336  THR B OG1   1 
ATOM   6602  C CG2   . THR B  1  336 ? 33.378  64.812  -15.207 1.00 25.56 ? 336  THR B CG2   1 
ATOM   6603  N N     . THR B  1  337 ? 33.685  61.415  -18.192 1.00 18.24 ? 337  THR B N     1 
ATOM   6604  C CA    . THR B  1  337 ? 33.987  60.681  -19.415 1.00 16.83 ? 337  THR B CA    1 
ATOM   6605  C C     . THR B  1  337 ? 33.908  59.209  -19.006 1.00 16.29 ? 337  THR B C     1 
ATOM   6606  O O     . THR B  1  337 ? 34.023  58.889  -17.826 1.00 14.80 ? 337  THR B O     1 
ATOM   6607  C CB    . THR B  1  337 ? 35.389  61.009  -19.949 1.00 17.68 ? 337  THR B CB    1 
ATOM   6608  O OG1   . THR B  1  337 ? 36.369  60.641  -18.977 1.00 18.69 ? 337  THR B OG1   1 
ATOM   6609  C CG2   . THR B  1  337 ? 35.503  62.502  -20.251 1.00 18.18 ? 337  THR B CG2   1 
ATOM   6610  N N     . PRO B  1  338 ? 33.729  58.296  -19.972 1.00 15.98 ? 338  PRO B N     1 
ATOM   6611  C CA    . PRO B  1  338 ? 33.628  56.872  -19.629 1.00 15.59 ? 338  PRO B CA    1 
ATOM   6612  C C     . PRO B  1  338 ? 34.891  56.168  -19.158 1.00 13.65 ? 338  PRO B C     1 
ATOM   6613  O O     . PRO B  1  338 ? 35.943  56.270  -19.790 1.00 12.97 ? 338  PRO B O     1 
ATOM   6614  C CB    . PRO B  1  338 ? 33.116  56.228  -20.921 1.00 15.67 ? 338  PRO B CB    1 
ATOM   6615  C CG    . PRO B  1  338 ? 32.675  57.415  -21.811 1.00 18.92 ? 338  PRO B CG    1 
ATOM   6616  C CD    . PRO B  1  338 ? 33.659  58.483  -21.429 1.00 16.91 ? 338  PRO B CD    1 
ATOM   6617  N N     . PRO B  1  339 ? 34.812  55.463  -18.020 1.00 13.52 ? 339  PRO B N     1 
ATOM   6618  C CA    . PRO B  1  339 ? 35.997  54.745  -17.542 1.00 12.61 ? 339  PRO B CA    1 
ATOM   6619  C C     . PRO B  1  339 ? 35.920  53.446  -18.344 1.00 12.33 ? 339  PRO B C     1 
ATOM   6620  O O     . PRO B  1  339 ? 35.038  52.621  -18.104 1.00 12.36 ? 339  PRO B O     1 
ATOM   6621  C CB    . PRO B  1  339 ? 35.696  54.516  -16.060 1.00 13.96 ? 339  PRO B CB    1 
ATOM   6622  C CG    . PRO B  1  339 ? 34.710  55.601  -15.722 1.00 14.38 ? 339  PRO B CG    1 
ATOM   6623  C CD    . PRO B  1  339 ? 33.825  55.606  -16.940 1.00 13.82 ? 339  PRO B CD    1 
ATOM   6624  N N     . PHE B  1  340 ? 36.821  53.269  -19.303 1.00 11.61 ? 340  PHE B N     1 
ATOM   6625  C CA    . PHE B  1  340 ? 36.779  52.078  -20.143 1.00 11.38 ? 340  PHE B CA    1 
ATOM   6626  C C     . PHE B  1  340 ? 36.767  50.768  -19.365 1.00 10.47 ? 340  PHE B C     1 
ATOM   6627  O O     . PHE B  1  340 ? 37.602  50.542  -18.490 1.00 11.34 ? 340  PHE B O     1 
ATOM   6628  C CB    . PHE B  1  340 ? 37.948  52.071  -21.128 1.00 11.62 ? 340  PHE B CB    1 
ATOM   6629  C CG    . PHE B  1  340 ? 37.734  51.161  -22.301 1.00 11.31 ? 340  PHE B CG    1 
ATOM   6630  C CD1   . PHE B  1  340 ? 36.944  51.565  -23.374 1.00 12.15 ? 340  PHE B CD1   1 
ATOM   6631  C CD2   . PHE B  1  340 ? 38.296  49.889  -22.324 1.00 10.57 ? 340  PHE B CD2   1 
ATOM   6632  C CE1   . PHE B  1  340 ? 36.716  50.715  -24.454 1.00 11.49 ? 340  PHE B CE1   1 
ATOM   6633  C CE2   . PHE B  1  340 ? 38.075  49.031  -23.397 1.00 10.78 ? 340  PHE B CE2   1 
ATOM   6634  C CZ    . PHE B  1  340 ? 37.282  49.444  -24.467 1.00 10.64 ? 340  PHE B CZ    1 
ATOM   6635  N N     . GLY B  1  341 ? 35.813  49.905  -19.702 1.00 10.67 ? 341  GLY B N     1 
ATOM   6636  C CA    . GLY B  1  341 ? 35.708  48.622  -19.034 1.00 10.18 ? 341  GLY B CA    1 
ATOM   6637  C C     . GLY B  1  341 ? 34.728  48.603  -17.876 1.00 10.61 ? 341  GLY B C     1 
ATOM   6638  O O     . GLY B  1  341 ? 34.245  47.537  -17.498 1.00 10.38 ? 341  GLY B O     1 
ATOM   6639  N N     . PHE B  1  342 ? 34.425  49.767  -17.305 1.00 11.04 ? 342  PHE B N     1 
ATOM   6640  C CA    . PHE B  1  342 ? 33.491  49.810  -16.183 1.00 10.36 ? 342  PHE B CA    1 
ATOM   6641  C C     . PHE B  1  342 ? 32.128  49.345  -16.683 1.00 10.75 ? 342  PHE B C     1 
ATOM   6642  O O     . PHE B  1  342 ? 31.495  48.469  -16.094 1.00 11.01 ? 342  PHE B O     1 
ATOM   6643  C CB    . PHE B  1  342 ? 33.385  51.220  -15.603 1.00 11.53 ? 342  PHE B CB    1 
ATOM   6644  C CG    . PHE B  1  342 ? 32.782  51.249  -14.228 1.00 11.93 ? 342  PHE B CG    1 
ATOM   6645  C CD1   . PHE B  1  342 ? 33.573  51.032  -13.102 1.00 13.21 ? 342  PHE B CD1   1 
ATOM   6646  C CD2   . PHE B  1  342 ? 31.412  51.414  -14.063 1.00 12.10 ? 342  PHE B CD2   1 
ATOM   6647  C CE1   . PHE B  1  342 ? 33.004  50.974  -11.831 1.00 13.47 ? 342  PHE B CE1   1 
ATOM   6648  C CE2   . PHE B  1  342 ? 30.832  51.356  -12.798 1.00 12.96 ? 342  PHE B CE2   1 
ATOM   6649  C CZ    . PHE B  1  342 ? 31.631  51.134  -11.679 1.00 13.79 ? 342  PHE B CZ    1 
ATOM   6650  N N     . PHE B  1  343 ? 31.673  49.954  -17.769 1.00 10.97 ? 343  PHE B N     1 
ATOM   6651  C CA    . PHE B  1  343 ? 30.423  49.561  -18.393 1.00 11.12 ? 343  PHE B CA    1 
ATOM   6652  C C     . PHE B  1  343 ? 30.897  48.764  -19.614 1.00 11.65 ? 343  PHE B C     1 
ATOM   6653  O O     . PHE B  1  343 ? 31.976  49.029  -20.150 1.00 9.95  ? 343  PHE B O     1 
ATOM   6654  C CB    . PHE B  1  343 ? 29.606  50.809  -18.736 1.00 11.75 ? 343  PHE B CB    1 
ATOM   6655  C CG    . PHE B  1  343 ? 29.105  51.542  -17.512 1.00 13.44 ? 343  PHE B CG    1 
ATOM   6656  C CD1   . PHE B  1  343 ? 29.267  52.918  -17.382 1.00 14.34 ? 343  PHE B CD1   1 
ATOM   6657  C CD2   . PHE B  1  343 ? 28.492  50.841  -16.473 1.00 14.26 ? 343  PHE B CD2   1 
ATOM   6658  C CE1   . PHE B  1  343 ? 28.827  53.585  -16.231 1.00 16.07 ? 343  PHE B CE1   1 
ATOM   6659  C CE2   . PHE B  1  343 ? 28.050  51.495  -15.322 1.00 14.41 ? 343  PHE B CE2   1 
ATOM   6660  C CZ    . PHE B  1  343 ? 28.219  52.871  -15.202 1.00 14.86 ? 343  PHE B CZ    1 
ATOM   6661  N N     . PRO B  1  344 ? 30.114  47.767  -20.058 1.00 12.32 ? 344  PRO B N     1 
ATOM   6662  C CA    . PRO B  1  344 ? 30.480  46.920  -21.201 1.00 11.98 ? 344  PRO B CA    1 
ATOM   6663  C C     . PRO B  1  344 ? 30.675  47.528  -22.590 1.00 13.30 ? 344  PRO B C     1 
ATOM   6664  O O     . PRO B  1  344 ? 31.369  46.938  -23.425 1.00 10.54 ? 344  PRO B O     1 
ATOM   6665  C CB    . PRO B  1  344 ? 29.402  45.839  -21.176 1.00 12.95 ? 344  PRO B CB    1 
ATOM   6666  C CG    . PRO B  1  344 ? 28.209  46.586  -20.692 1.00 11.94 ? 344  PRO B CG    1 
ATOM   6667  C CD    . PRO B  1  344 ? 28.775  47.412  -19.555 1.00 12.39 ? 344  PRO B CD    1 
ATOM   6668  N N     . SER B  1  345 ? 30.074  48.692  -22.827 1.00 13.85 ? 345  SER B N     1 
ATOM   6669  C CA    . SER B  1  345 ? 30.180  49.385  -24.110 1.00 18.02 ? 345  SER B CA    1 
ATOM   6670  C C     . SER B  1  345 ? 30.420  50.870  -23.885 1.00 18.43 ? 345  SER B C     1 
ATOM   6671  O O     . SER B  1  345 ? 30.105  51.409  -22.831 1.00 18.56 ? 345  SER B O     1 
ATOM   6672  C CB    . SER B  1  345 ? 28.898  49.205  -24.923 1.00 18.97 ? 345  SER B CB    1 
ATOM   6673  O OG    . SER B  1  345 ? 28.536  47.838  -24.986 1.00 23.62 ? 345  SER B OG    1 
ATOM   6674  N N     . SER B  1  346 ? 30.967  51.539  -24.888 1.00 21.46 ? 346  SER B N     1 
ATOM   6675  C CA    . SER B  1  346 ? 31.248  52.963  -24.776 1.00 23.64 ? 346  SER B CA    1 
ATOM   6676  C C     . SER B  1  346 ? 30.011  53.860  -24.915 1.00 25.39 ? 346  SER B C     1 
ATOM   6677  O O     . SER B  1  346 ? 30.074  55.055  -24.619 1.00 25.75 ? 346  SER B O     1 
ATOM   6678  C CB    . SER B  1  346 ? 32.291  53.367  -25.820 1.00 24.50 ? 346  SER B CB    1 
ATOM   6679  O OG    . SER B  1  346 ? 31.825  53.127  -27.136 1.00 26.45 ? 346  SER B OG    1 
ATOM   6680  N N     . SER B  1  347 ? 28.887  53.294  -25.348 1.00 25.52 ? 347  SER B N     1 
ATOM   6681  C CA    . SER B  1  347 ? 27.672  54.083  -25.533 1.00 26.45 ? 347  SER B CA    1 
ATOM   6682  C C     . SER B  1  347 ? 26.768  54.088  -24.309 1.00 25.43 ? 347  SER B C     1 
ATOM   6683  O O     . SER B  1  347 ? 25.631  54.534  -24.378 1.00 27.08 ? 347  SER B O     1 
ATOM   6684  C CB    . SER B  1  347 ? 26.886  53.565  -26.742 1.00 27.09 ? 347  SER B CB    1 
ATOM   6685  O OG    . SER B  1  347 ? 26.328  52.292  -26.486 1.00 29.55 ? 347  SER B OG    1 
ATOM   6686  N N     . TYR B  1  348 ? 27.278  53.592  -23.188 1.00 23.35 ? 348  TYR B N     1 
ATOM   6687  C CA    . TYR B  1  348 ? 26.512  53.522  -21.941 1.00 20.61 ? 348  TYR B CA    1 
ATOM   6688  C C     . TYR B  1  348 ? 26.254  54.920  -21.361 1.00 19.99 ? 348  TYR B C     1 
ATOM   6689  O O     . TYR B  1  348 ? 27.116  55.791  -21.427 1.00 18.65 ? 348  TYR B O     1 
ATOM   6690  C CB    . TYR B  1  348 ? 27.288  52.690  -20.916 1.00 18.98 ? 348  TYR B CB    1 
ATOM   6691  C CG    . TYR B  1  348 ? 26.444  52.101  -19.817 1.00 17.37 ? 348  TYR B CG    1 
ATOM   6692  C CD1   . TYR B  1  348 ? 25.904  50.821  -19.941 1.00 17.20 ? 348  TYR B CD1   1 
ATOM   6693  C CD2   . TYR B  1  348 ? 26.203  52.811  -18.646 1.00 17.62 ? 348  TYR B CD2   1 
ATOM   6694  C CE1   . TYR B  1  348 ? 25.145  50.258  -18.916 1.00 14.77 ? 348  TYR B CE1   1 
ATOM   6695  C CE2   . TYR B  1  348 ? 25.447  52.262  -17.618 1.00 15.93 ? 348  TYR B CE2   1 
ATOM   6696  C CZ    . TYR B  1  348 ? 24.923  50.986  -17.761 1.00 14.77 ? 348  TYR B CZ    1 
ATOM   6697  O OH    . TYR B  1  348 ? 24.174  50.444  -16.751 1.00 12.44 ? 348  TYR B OH    1 
ATOM   6698  N N     . PRO B  1  349 ? 25.059  55.154  -20.788 1.00 19.95 ? 349  PRO B N     1 
ATOM   6699  C CA    . PRO B  1  349 ? 24.752  56.470  -20.210 1.00 20.01 ? 349  PRO B CA    1 
ATOM   6700  C C     . PRO B  1  349 ? 25.585  56.702  -18.948 1.00 19.49 ? 349  PRO B C     1 
ATOM   6701  O O     . PRO B  1  349 ? 25.662  55.829  -18.088 1.00 20.41 ? 349  PRO B O     1 
ATOM   6702  C CB    . PRO B  1  349 ? 23.258  56.372  -19.917 1.00 20.59 ? 349  PRO B CB    1 
ATOM   6703  C CG    . PRO B  1  349 ? 23.083  54.915  -19.591 1.00 20.59 ? 349  PRO B CG    1 
ATOM   6704  C CD    . PRO B  1  349 ? 23.903  54.248  -20.671 1.00 20.14 ? 349  PRO B CD    1 
ATOM   6705  N N     . LEU B  1  350 ? 26.207  57.872  -18.841 1.00 18.10 ? 350  LEU B N     1 
ATOM   6706  C CA    . LEU B  1  350 ? 27.049  58.174  -17.686 1.00 18.18 ? 350  LEU B CA    1 
ATOM   6707  C C     . LEU B  1  350 ? 26.297  58.805  -16.521 1.00 18.43 ? 350  LEU B C     1 
ATOM   6708  O O     . LEU B  1  350 ? 25.340  59.549  -16.714 1.00 17.72 ? 350  LEU B O     1 
ATOM   6709  C CB    . LEU B  1  350 ? 28.197  59.100  -18.095 1.00 18.27 ? 350  LEU B CB    1 
ATOM   6710  C CG    . LEU B  1  350 ? 29.151  58.584  -19.174 1.00 18.99 ? 350  LEU B CG    1 
ATOM   6711  C CD1   . LEU B  1  350 ? 30.220  59.629  -19.435 1.00 19.43 ? 350  LEU B CD1   1 
ATOM   6712  C CD2   . LEU B  1  350 ? 29.787  57.273  -18.727 1.00 18.91 ? 350  LEU B CD2   1 
ATOM   6713  N N     . PRO B  1  351 ? 26.725  58.509  -15.286 1.00 18.74 ? 351  PRO B N     1 
ATOM   6714  C CA    . PRO B  1  351 ? 26.073  59.070  -14.100 1.00 19.21 ? 351  PRO B CA    1 
ATOM   6715  C C     . PRO B  1  351 ? 26.463  60.538  -13.916 1.00 20.51 ? 351  PRO B C     1 
ATOM   6716  O O     . PRO B  1  351 ? 27.650  60.861  -13.869 1.00 20.13 ? 351  PRO B O     1 
ATOM   6717  C CB    . PRO B  1  351 ? 26.597  58.183  -12.976 1.00 18.84 ? 351  PRO B CB    1 
ATOM   6718  C CG    . PRO B  1  351 ? 27.983  57.868  -13.433 1.00 19.06 ? 351  PRO B CG    1 
ATOM   6719  C CD    . PRO B  1  351 ? 27.787  57.560  -14.904 1.00 19.36 ? 351  PRO B CD    1 
ATOM   6720  N N     . ASN B  1  352 ? 25.472  61.421  -13.812 1.00 21.43 ? 352  ASN B N     1 
ATOM   6721  C CA    . ASN B  1  352 ? 25.752  62.846  -13.647 1.00 24.04 ? 352  ASN B CA    1 
ATOM   6722  C C     . ASN B  1  352 ? 25.771  63.286  -12.177 1.00 22.88 ? 352  ASN B C     1 
ATOM   6723  O O     . ASN B  1  352 ? 25.925  64.466  -11.876 1.00 23.80 ? 352  ASN B O     1 
ATOM   6724  C CB    . ASN B  1  352 ? 24.746  63.690  -14.470 1.00 27.13 ? 352  ASN B CB    1 
ATOM   6725  C CG    . ASN B  1  352 ? 23.310  63.581  -13.961 1.00 31.81 ? 352  ASN B CG    1 
ATOM   6726  O OD1   . ASN B  1  352 ? 23.093  63.170  -12.816 1.00 31.66 ? 352  ASN B OD1   1 
ATOM   6727  N ND2   . ASN B  1  352 ? 22.326  63.990  -14.774 1.00 36.27 ? 352  ASN B ND2   1 
ATOM   6728  N N     . SER B  1  353 ? 25.625  62.328  -11.268 1.00 21.22 ? 353  SER B N     1 
ATOM   6729  C CA    . SER B  1  353 ? 25.651  62.603  -9.830  1.00 20.11 ? 353  SER B CA    1 
ATOM   6730  C C     . SER B  1  353 ? 26.280  61.406  -9.118  1.00 19.08 ? 353  SER B C     1 
ATOM   6731  O O     . SER B  1  353 ? 26.607  60.413  -9.767  1.00 17.36 ? 353  SER B O     1 
ATOM   6732  C CB    . SER B  1  353 ? 24.233  62.846  -9.304  1.00 22.37 ? 353  SER B CB    1 
ATOM   6733  O OG    . SER B  1  353 ? 23.408  61.711  -9.506  1.00 25.74 ? 353  SER B OG    1 
ATOM   6734  N N     . THR B  1  354 ? 26.457  61.488  -7.799  1.00 17.01 ? 354  THR B N     1 
ATOM   6735  C CA    . THR B  1  354 ? 27.056  60.369  -7.067  1.00 16.64 ? 354  THR B CA    1 
ATOM   6736  C C     . THR B  1  354 ? 26.157  59.153  -7.240  1.00 15.72 ? 354  THR B C     1 
ATOM   6737  O O     . THR B  1  354 ? 24.938  59.287  -7.333  1.00 17.13 ? 354  THR B O     1 
ATOM   6738  C CB    . THR B  1  354 ? 27.225  60.669  -5.553  1.00 16.96 ? 354  THR B CB    1 
ATOM   6739  O OG1   . THR B  1  354 ? 25.946  60.945  -4.965  1.00 17.25 ? 354  THR B OG1   1 
ATOM   6740  C CG2   . THR B  1  354 ? 28.152  61.862  -5.345  1.00 17.67 ? 354  THR B CG2   1 
ATOM   6741  N N     . PHE B  1  355 ? 26.752  57.966  -7.294  1.00 14.48 ? 355  PHE B N     1 
ATOM   6742  C CA    . PHE B  1  355 ? 25.961  56.759  -7.486  1.00 13.41 ? 355  PHE B CA    1 
ATOM   6743  C C     . PHE B  1  355 ? 26.584  55.537  -6.827  1.00 11.53 ? 355  PHE B C     1 
ATOM   6744  O O     . PHE B  1  355 ? 27.746  55.559  -6.424  1.00 11.09 ? 355  PHE B O     1 
ATOM   6745  C CB    . PHE B  1  355 ? 25.772  56.498  -8.989  1.00 14.15 ? 355  PHE B CB    1 
ATOM   6746  C CG    . PHE B  1  355 ? 26.991  55.932  -9.678  1.00 13.27 ? 355  PHE B CG    1 
ATOM   6747  C CD1   . PHE B  1  355 ? 27.033  54.588  -10.046 1.00 15.60 ? 355  PHE B CD1   1 
ATOM   6748  C CD2   . PHE B  1  355 ? 28.089  56.739  -9.966  1.00 14.47 ? 355  PHE B CD2   1 
ATOM   6749  C CE1   . PHE B  1  355 ? 28.153  54.056  -10.695 1.00 16.45 ? 355  PHE B CE1   1 
ATOM   6750  C CE2   . PHE B  1  355 ? 29.213  56.218  -10.614 1.00 16.55 ? 355  PHE B CE2   1 
ATOM   6751  C CZ    . PHE B  1  355 ? 29.243  54.873  -10.979 1.00 16.90 ? 355  PHE B CZ    1 
ATOM   6752  N N     . ALA B  1  356 ? 25.789  54.479  -6.712  1.00 10.67 ? 356  ALA B N     1 
ATOM   6753  C CA    . ALA B  1  356 ? 26.247  53.223  -6.128  1.00 10.41 ? 356  ALA B CA    1 
ATOM   6754  C C     . ALA B  1  356 ? 26.101  52.127  -7.174  1.00 10.98 ? 356  ALA B C     1 
ATOM   6755  O O     . ALA B  1  356 ? 25.064  52.011  -7.826  1.00 10.71 ? 356  ALA B O     1 
ATOM   6756  C CB    . ALA B  1  356 ? 25.429  52.881  -4.890  1.00 11.54 ? 356  ALA B CB    1 
ATOM   6757  N N     . HIS B  1  357 ? 27.155  51.333  -7.320  1.00 10.09 ? 357  HIS B N     1 
ATOM   6758  C CA    . HIS B  1  357 ? 27.217  50.239  -8.283  1.00 9.88  ? 357  HIS B CA    1 
ATOM   6759  C C     . HIS B  1  357 ? 27.173  48.910  -7.527  1.00 10.93 ? 357  HIS B C     1 
ATOM   6760  O O     . HIS B  1  357 ? 28.167  48.507  -6.925  1.00 12.28 ? 357  HIS B O     1 
ATOM   6761  C CB    . HIS B  1  357 ? 28.532  50.363  -9.066  1.00 9.67  ? 357  HIS B CB    1 
ATOM   6762  C CG    . HIS B  1  357 ? 28.748  49.312  -10.115 1.00 9.81  ? 357  HIS B CG    1 
ATOM   6763  N ND1   . HIS B  1  357 ? 28.105  49.328  -11.334 1.00 9.89  ? 357  HIS B ND1   1 
ATOM   6764  C CD2   . HIS B  1  357 ? 29.603  48.262  -10.155 1.00 10.14 ? 357  HIS B CD2   1 
ATOM   6765  C CE1   . HIS B  1  357 ? 28.558  48.337  -12.082 1.00 11.16 ? 357  HIS B CE1   1 
ATOM   6766  N NE2   . HIS B  1  357 ? 29.469  47.676  -11.391 1.00 10.70 ? 357  HIS B NE2   1 
ATOM   6767  N N     . PHE B  1  358 ? 26.020  48.247  -7.534  1.00 8.98  ? 358  PHE B N     1 
ATOM   6768  C CA    . PHE B  1  358 ? 25.895  46.953  -6.873  1.00 10.13 ? 358  PHE B CA    1 
ATOM   6769  C C     . PHE B  1  358 ? 26.275  45.907  -7.911  1.00 9.97  ? 358  PHE B C     1 
ATOM   6770  O O     . PHE B  1  358 ? 25.579  45.737  -8.915  1.00 10.56 ? 358  PHE B O     1 
ATOM   6771  C CB    . PHE B  1  358 ? 24.464  46.715  -6.377  1.00 9.49  ? 358  PHE B CB    1 
ATOM   6772  C CG    . PHE B  1  358 ? 24.099  47.534  -5.174  1.00 9.91  ? 358  PHE B CG    1 
ATOM   6773  C CD1   . PHE B  1  358 ? 23.599  48.823  -5.317  1.00 11.98 ? 358  PHE B CD1   1 
ATOM   6774  C CD2   . PHE B  1  358 ? 24.288  47.026  -3.891  1.00 12.36 ? 358  PHE B CD2   1 
ATOM   6775  C CE1   . PHE B  1  358 ? 23.291  49.598  -4.197  1.00 12.44 ? 358  PHE B CE1   1 
ATOM   6776  C CE2   . PHE B  1  358 ? 23.984  47.792  -2.765  1.00 12.60 ? 358  PHE B CE2   1 
ATOM   6777  C CZ    . PHE B  1  358 ? 23.485  49.081  -2.920  1.00 12.32 ? 358  PHE B CZ    1 
ATOM   6778  N N     . ALA B  1  359 ? 27.385  45.214  -7.667  1.00 9.42  ? 359  ALA B N     1 
ATOM   6779  C CA    . ALA B  1  359 ? 27.888  44.219  -8.605  1.00 9.13  ? 359  ALA B CA    1 
ATOM   6780  C C     . ALA B  1  359 ? 27.833  42.784  -8.093  1.00 9.46  ? 359  ALA B C     1 
ATOM   6781  O O     . ALA B  1  359 ? 27.981  42.522  -6.896  1.00 9.21  ? 359  ALA B O     1 
ATOM   6782  C CB    . ALA B  1  359 ? 29.315  44.573  -9.003  1.00 10.01 ? 359  ALA B CB    1 
ATOM   6783  N N     . SER B  1  360 ? 27.625  41.860  -9.026  1.00 8.22  ? 360  SER B N     1 
ATOM   6784  C CA    . SER B  1  360 ? 27.541  40.437  -8.715  1.00 8.43  ? 360  SER B CA    1 
ATOM   6785  C C     . SER B  1  360 ? 28.439  39.654  -9.677  1.00 8.86  ? 360  SER B C     1 
ATOM   6786  O O     . SER B  1  360 ? 28.326  39.787  -10.900 1.00 8.60  ? 360  SER B O     1 
ATOM   6787  C CB    . SER B  1  360 ? 26.084  39.972  -8.837  1.00 8.93  ? 360  SER B CB    1 
ATOM   6788  O OG    . SER B  1  360 ? 25.925  38.611  -8.464  1.00 8.70  ? 360  SER B OG    1 
ATOM   6789  N N     . LYS B  1  361 ? 29.336  38.850  -9.111  1.00 8.23  ? 361  LYS B N     1 
ATOM   6790  C CA    . LYS B  1  361 ? 30.281  38.044  -9.887  1.00 8.08  ? 361  LYS B CA    1 
ATOM   6791  C C     . LYS B  1  361 ? 29.931  36.561  -9.790  1.00 7.78  ? 361  LYS B C     1 
ATOM   6792  O O     . LYS B  1  361 ? 29.824  36.018  -8.695  1.00 8.82  ? 361  LYS B O     1 
ATOM   6793  C CB    . LYS B  1  361 ? 31.708  38.259  -9.357  1.00 10.45 ? 361  LYS B CB    1 
ATOM   6794  C CG    . LYS B  1  361 ? 32.782  37.377  -10.008 1.00 9.35  ? 361  LYS B CG    1 
ATOM   6795  C CD    . LYS B  1  361 ? 34.142  37.575  -9.333  1.00 10.90 ? 361  LYS B CD    1 
ATOM   6796  C CE    . LYS B  1  361 ? 35.179  36.591  -9.855  1.00 10.66 ? 361  LYS B CE    1 
ATOM   6797  N NZ    . LYS B  1  361 ? 36.481  36.682  -9.117  1.00 9.66  ? 361  LYS B NZ    1 
ATOM   6798  N N     . VAL B  1  362 ? 29.745  35.910  -10.935 1.00 7.43  ? 362  VAL B N     1 
ATOM   6799  C CA    . VAL B  1  362 ? 29.432  34.486  -10.947 1.00 6.58  ? 362  VAL B CA    1 
ATOM   6800  C C     . VAL B  1  362 ? 30.704  33.686  -10.660 1.00 7.94  ? 362  VAL B C     1 
ATOM   6801  O O     . VAL B  1  362 ? 31.770  33.977  -11.208 1.00 7.35  ? 362  VAL B O     1 
ATOM   6802  C CB    . VAL B  1  362 ? 28.841  34.052  -12.313 1.00 6.73  ? 362  VAL B CB    1 
ATOM   6803  C CG1   . VAL B  1  362 ? 28.700  32.532  -12.373 1.00 7.27  ? 362  VAL B CG1   1 
ATOM   6804  C CG2   . VAL B  1  362 ? 27.482  34.704  -12.513 1.00 7.97  ? 362  VAL B CG2   1 
ATOM   6805  N N     . ALA B  1  363 ? 30.589  32.694  -9.782  1.00 7.82  ? 363  ALA B N     1 
ATOM   6806  C CA    . ALA B  1  363 ? 31.722  31.848  -9.413  1.00 8.64  ? 363  ALA B CA    1 
ATOM   6807  C C     . ALA B  1  363 ? 32.219  31.033  -10.608 1.00 7.86  ? 363  ALA B C     1 
ATOM   6808  O O     . ALA B  1  363 ? 31.479  30.801  -11.561 1.00 7.53  ? 363  ALA B O     1 
ATOM   6809  C CB    . ALA B  1  363 ? 31.316  30.914  -8.277  1.00 9.00  ? 363  ALA B CB    1 
ATOM   6810  N N     . GLY B  1  364 ? 33.473  30.595  -10.549 1.00 8.18  ? 364  GLY B N     1 
ATOM   6811  C CA    . GLY B  1  364 ? 34.036  29.809  -11.637 1.00 7.56  ? 364  GLY B CA    1 
ATOM   6812  C C     . GLY B  1  364 ? 34.867  30.664  -12.576 1.00 7.82  ? 364  GLY B C     1 
ATOM   6813  O O     . GLY B  1  364 ? 35.982  31.063  -12.229 1.00 7.67  ? 364  GLY B O     1 
ATOM   6814  N N     . PRO B  1  365 ? 34.368  30.943  -13.788 1.00 7.14  ? 365  PRO B N     1 
ATOM   6815  C CA    . PRO B  1  365 ? 33.080  30.498  -14.329 1.00 7.93  ? 365  PRO B CA    1 
ATOM   6816  C C     . PRO B  1  365 ? 33.288  29.174  -15.054 1.00 7.87  ? 365  PRO B C     1 
ATOM   6817  O O     . PRO B  1  365 ? 34.423  28.805  -15.358 1.00 8.79  ? 365  PRO B O     1 
ATOM   6818  C CB    . PRO B  1  365 ? 32.726  31.614  -15.295 1.00 8.36  ? 365  PRO B CB    1 
ATOM   6819  C CG    . PRO B  1  365 ? 34.067  31.914  -15.905 1.00 8.07  ? 365  PRO B CG    1 
ATOM   6820  C CD    . PRO B  1  365 ? 35.002  31.917  -14.698 1.00 7.54  ? 365  PRO B CD    1 
ATOM   6821  N N     . LEU B  1  366 ? 32.200  28.467  -15.342 1.00 8.72  ? 366  LEU B N     1 
ATOM   6822  C CA    . LEU B  1  366 ? 32.298  27.194  -16.049 1.00 10.01 ? 366  LEU B CA    1 
ATOM   6823  C C     . LEU B  1  366 ? 32.535  27.419  -17.540 1.00 9.65  ? 366  LEU B C     1 
ATOM   6824  O O     . LEU B  1  366 ? 33.149  26.589  -18.215 1.00 11.00 ? 366  LEU B O     1 
ATOM   6825  C CB    . LEU B  1  366 ? 31.023  26.375  -15.834 1.00 9.94  ? 366  LEU B CB    1 
ATOM   6826  C CG    . LEU B  1  366 ? 30.808  25.892  -14.398 1.00 11.41 ? 366  LEU B CG    1 
ATOM   6827  C CD1   . LEU B  1  366 ? 29.411  25.312  -14.253 1.00 11.50 ? 366  LEU B CD1   1 
ATOM   6828  C CD2   . LEU B  1  366 ? 31.867  24.856  -14.042 1.00 12.40 ? 366  LEU B CD2   1 
ATOM   6829  N N     . SER B  1  367 ? 32.046  28.547  -18.048 1.00 9.64  ? 367  SER B N     1 
ATOM   6830  C CA    . SER B  1  367 ? 32.202  28.893  -19.458 1.00 8.23  ? 367  SER B CA    1 
ATOM   6831  C C     . SER B  1  367 ? 33.632  29.334  -19.735 1.00 9.16  ? 367  SER B C     1 
ATOM   6832  O O     . SER B  1  367 ? 34.287  29.911  -18.869 1.00 8.98  ? 367  SER B O     1 
ATOM   6833  C CB    . SER B  1  367 ? 31.258  30.039  -19.830 1.00 9.08  ? 367  SER B CB    1 
ATOM   6834  O OG    . SER B  1  367 ? 29.910  29.705  -19.557 1.00 8.96  ? 367  SER B OG    1 
ATOM   6835  N N     . TYR B  1  368 ? 34.112  29.068  -20.944 1.00 8.93  ? 368  TYR B N     1 
ATOM   6836  C CA    . TYR B  1  368 ? 35.462  29.464  -21.312 1.00 9.05  ? 368  TYR B CA    1 
ATOM   6837  C C     . TYR B  1  368 ? 35.607  29.623  -22.816 1.00 9.47  ? 368  TYR B C     1 
ATOM   6838  O O     . TYR B  1  368 ? 34.759  29.170  -23.595 1.00 8.61  ? 368  TYR B O     1 
ATOM   6839  C CB    . TYR B  1  368 ? 36.482  28.442  -20.797 1.00 9.99  ? 368  TYR B CB    1 
ATOM   6840  C CG    . TYR B  1  368 ? 36.354  27.072  -21.421 1.00 11.90 ? 368  TYR B CG    1 
ATOM   6841  C CD1   . TYR B  1  368 ? 36.896  26.800  -22.680 1.00 12.05 ? 368  TYR B CD1   1 
ATOM   6842  C CD2   . TYR B  1  368 ? 35.672  26.050  -20.763 1.00 14.52 ? 368  TYR B CD2   1 
ATOM   6843  C CE1   . TYR B  1  368 ? 36.758  25.540  -23.267 1.00 15.11 ? 368  TYR B CE1   1 
ATOM   6844  C CE2   . TYR B  1  368 ? 35.527  24.788  -21.341 1.00 15.83 ? 368  TYR B CE2   1 
ATOM   6845  C CZ    . TYR B  1  368 ? 36.071  24.542  -22.590 1.00 14.82 ? 368  TYR B CZ    1 
ATOM   6846  O OH    . TYR B  1  368 ? 35.922  23.297  -23.160 1.00 17.37 ? 368  TYR B OH    1 
ATOM   6847  N N     . GLY B  1  369 ? 36.689  30.285  -23.205 1.00 8.23  ? 369  GLY B N     1 
ATOM   6848  C CA    . GLY B  1  369 ? 36.985  30.510  -24.605 1.00 8.77  ? 369  GLY B CA    1 
ATOM   6849  C C     . GLY B  1  369 ? 38.464  30.292  -24.852 1.00 9.62  ? 369  GLY B C     1 
ATOM   6850  O O     . GLY B  1  369 ? 39.105  29.502  -24.156 1.00 10.48 ? 369  GLY B O     1 
ATOM   6851  N N     . SER B  1  370 ? 39.018  30.996  -25.831 1.00 8.42  ? 370  SER B N     1 
ATOM   6852  C CA    . SER B  1  370 ? 40.431  30.840  -26.147 1.00 9.09  ? 370  SER B CA    1 
ATOM   6853  C C     . SER B  1  370 ? 41.086  32.139  -26.592 1.00 9.17  ? 370  SER B C     1 
ATOM   6854  O O     . SER B  1  370 ? 40.416  33.137  -26.864 1.00 8.22  ? 370  SER B O     1 
ATOM   6855  C CB    . SER B  1  370 ? 40.611  29.790  -27.245 1.00 10.72 ? 370  SER B CB    1 
ATOM   6856  O OG    . SER B  1  370 ? 40.082  30.253  -28.474 1.00 13.69 ? 370  SER B OG    1 
ATOM   6857  N N     . LEU B  1  371 ? 42.411  32.104  -26.654 1.00 9.10  ? 371  LEU B N     1 
ATOM   6858  C CA    . LEU B  1  371 ? 43.200  33.248  -27.075 1.00 9.93  ? 371  LEU B CA    1 
ATOM   6859  C C     . LEU B  1  371 ? 43.951  32.895  -28.355 1.00 10.49 ? 371  LEU B C     1 
ATOM   6860  O O     . LEU B  1  371 ? 44.506  31.803  -28.475 1.00 10.66 ? 371  LEU B O     1 
ATOM   6861  C CB    . LEU B  1  371 ? 44.188  33.635  -25.967 1.00 10.06 ? 371  LEU B CB    1 
ATOM   6862  C CG    . LEU B  1  371 ? 45.188  34.773  -26.217 1.00 8.97  ? 371  LEU B CG    1 
ATOM   6863  C CD1   . LEU B  1  371 ? 45.561  35.413  -24.888 1.00 10.29 ? 371  LEU B CD1   1 
ATOM   6864  C CD2   . LEU B  1  371 ? 46.426  34.249  -26.940 1.00 8.74  ? 371  LEU B CD2   1 
ATOM   6865  N N     . THR B  1  372 ? 43.943  33.817  -29.313 1.00 9.56  ? 372  THR B N     1 
ATOM   6866  C CA    . THR B  1  372 ? 44.643  33.633  -30.583 1.00 10.36 ? 372  THR B CA    1 
ATOM   6867  C C     . THR B  1  372 ? 45.399  34.921  -30.901 1.00 8.90  ? 372  THR B C     1 
ATOM   6868  O O     . THR B  1  372 ? 45.032  35.998  -30.428 1.00 9.83  ? 372  THR B O     1 
ATOM   6869  C CB    . THR B  1  372 ? 43.664  33.337  -31.744 1.00 12.25 ? 372  THR B CB    1 
ATOM   6870  O OG1   . THR B  1  372 ? 42.684  34.380  -31.824 1.00 15.50 ? 372  THR B OG1   1 
ATOM   6871  C CG2   . THR B  1  372 ? 42.965  32.001  -31.533 1.00 14.22 ? 372  THR B CG2   1 
ATOM   6872  N N     . LEU B  1  373 ? 46.456  34.813  -31.695 1.00 8.42  ? 373  LEU B N     1 
ATOM   6873  C CA    . LEU B  1  373 ? 47.246  35.987  -32.057 1.00 9.17  ? 373  LEU B CA    1 
ATOM   6874  C C     . LEU B  1  373 ? 46.541  36.863  -33.090 1.00 11.18 ? 373  LEU B C     1 
ATOM   6875  O O     . LEU B  1  373 ? 45.815  36.362  -33.949 1.00 11.64 ? 373  LEU B O     1 
ATOM   6876  C CB    . LEU B  1  373 ? 48.602  35.552  -32.620 1.00 8.55  ? 373  LEU B CB    1 
ATOM   6877  C CG    . LEU B  1  373 ? 49.485  34.710  -31.698 1.00 8.17  ? 373  LEU B CG    1 
ATOM   6878  C CD1   . LEU B  1  373 ? 50.711  34.234  -32.466 1.00 8.43  ? 373  LEU B CD1   1 
ATOM   6879  C CD2   . LEU B  1  373 ? 49.888  35.531  -30.482 1.00 9.69  ? 373  LEU B CD2   1 
ATOM   6880  N N     . LYS B  1  374 ? 46.754  38.175  -32.993 1.00 13.00 ? 374  LYS B N     1 
ATOM   6881  C CA    . LYS B  1  374 ? 46.183  39.129  -33.942 1.00 14.15 ? 374  LYS B CA    1 
ATOM   6882  C C     . LYS B  1  374 ? 47.326  39.523  -34.876 1.00 14.25 ? 374  LYS B C     1 
ATOM   6883  O O     . LYS B  1  374 ? 47.111  40.054  -35.966 1.00 17.17 ? 374  LYS B O     1 
ATOM   6884  C CB    . LYS B  1  374 ? 45.649  40.366  -33.218 1.00 16.95 ? 374  LYS B CB    1 
ATOM   6885  C CG    . LYS B  1  374 ? 44.919  41.363  -34.117 1.00 23.92 ? 374  LYS B CG    1 
ATOM   6886  C CD    . LYS B  1  374 ? 43.647  40.761  -34.707 1.00 28.19 ? 374  LYS B CD    1 
ATOM   6887  C CE    . LYS B  1  374 ? 42.766  41.824  -35.359 1.00 30.66 ? 374  LYS B CE    1 
ATOM   6888  N NZ    . LYS B  1  374 ? 43.431  42.516  -36.498 1.00 33.06 ? 374  LYS B NZ    1 
ATOM   6889  N N     . SER B  1  375 ? 48.546  39.265  -34.416 1.00 12.76 ? 375  SER B N     1 
ATOM   6890  C CA    . SER B  1  375 ? 49.763  39.526  -35.176 1.00 11.62 ? 375  SER B CA    1 
ATOM   6891  C C     . SER B  1  375 ? 50.671  38.329  -34.941 1.00 11.84 ? 375  SER B C     1 
ATOM   6892  O O     . SER B  1  375 ? 50.878  37.912  -33.802 1.00 12.62 ? 375  SER B O     1 
ATOM   6893  C CB    . SER B  1  375 ? 50.463  40.795  -34.691 1.00 12.25 ? 375  SER B CB    1 
ATOM   6894  O OG    . SER B  1  375 ? 51.721  40.940  -35.331 1.00 11.84 ? 375  SER B OG    1 
ATOM   6895  N N     . SER B  1  376 ? 51.215  37.774  -36.013 1.00 13.29 ? 376  SER B N     1 
ATOM   6896  C CA    . SER B  1  376 ? 52.082  36.612  -35.880 1.00 14.27 ? 376  SER B CA    1 
ATOM   6897  C C     . SER B  1  376 ? 53.507  36.982  -35.493 1.00 13.17 ? 376  SER B C     1 
ATOM   6898  O O     . SER B  1  376 ? 54.333  36.099  -35.270 1.00 14.31 ? 376  SER B O     1 
ATOM   6899  C CB    . SER B  1  376 ? 52.101  35.824  -37.192 1.00 16.12 ? 376  SER B CB    1 
ATOM   6900  O OG    . SER B  1  376 ? 52.638  36.607  -38.244 1.00 17.85 ? 376  SER B OG    1 
ATOM   6901  N N     . SER B  1  377 ? 53.796  38.276  -35.389 1.00 14.09 ? 377  SER B N     1 
ATOM   6902  C CA    . SER B  1  377 ? 55.156  38.701  -35.067 1.00 14.56 ? 377  SER B CA    1 
ATOM   6903  C C     . SER B  1  377 ? 55.312  39.850  -34.076 1.00 15.47 ? 377  SER B C     1 
ATOM   6904  O O     . SER B  1  377 ? 56.373  40.000  -33.473 1.00 18.26 ? 377  SER B O     1 
ATOM   6905  C CB    . SER B  1  377 ? 55.884  39.085  -36.356 1.00 16.25 ? 377  SER B CB    1 
ATOM   6906  O OG    . SER B  1  377 ? 55.278  40.223  -36.951 1.00 16.65 ? 377  SER B OG    1 
ATOM   6907  N N     . ASN B  1  378 ? 54.271  40.657  -33.906 1.00 13.23 ? 378  ASN B N     1 
ATOM   6908  C CA    . ASN B  1  378 ? 54.347  41.808  -33.011 1.00 12.55 ? 378  ASN B CA    1 
ATOM   6909  C C     . ASN B  1  378 ? 53.677  41.556  -31.660 1.00 10.94 ? 378  ASN B C     1 
ATOM   6910  O O     . ASN B  1  378 ? 52.453  41.498  -31.567 1.00 11.38 ? 378  ASN B O     1 
ATOM   6911  C CB    . ASN B  1  378 ? 53.699  43.018  -33.688 1.00 13.20 ? 378  ASN B CB    1 
ATOM   6912  C CG    . ASN B  1  378 ? 54.069  44.329  -33.027 1.00 15.34 ? 378  ASN B CG    1 
ATOM   6913  O OD1   . ASN B  1  378 ? 54.454  44.364  -31.858 1.00 15.68 ? 378  ASN B OD1   1 
ATOM   6914  N ND2   . ASN B  1  378 ? 53.940  45.424  -33.774 1.00 17.25 ? 378  ASN B ND2   1 
ATOM   6915  N N     . VAL B  1  379 ? 54.490  41.432  -30.613 1.00 9.86  ? 379  VAL B N     1 
ATOM   6916  C CA    . VAL B  1  379 ? 53.983  41.181  -29.269 1.00 9.38  ? 379  VAL B CA    1 
ATOM   6917  C C     . VAL B  1  379 ? 53.228  42.389  -28.696 1.00 10.35 ? 379  VAL B C     1 
ATOM   6918  O O     . VAL B  1  379 ? 52.515  42.267  -27.700 1.00 10.04 ? 379  VAL B O     1 
ATOM   6919  C CB    . VAL B  1  379 ? 55.144  40.782  -28.308 1.00 8.91  ? 379  VAL B CB    1 
ATOM   6920  C CG1   . VAL B  1  379 ? 56.002  42.002  -27.978 1.00 9.27  ? 379  VAL B CG1   1 
ATOM   6921  C CG2   . VAL B  1  379 ? 54.586  40.142  -27.040 1.00 8.30  ? 379  VAL B CG2   1 
ATOM   6922  N N     . ARG B  1  380 ? 53.384  43.553  -29.323 1.00 11.42 ? 380  ARG B N     1 
ATOM   6923  C CA    . ARG B  1  380 ? 52.704  44.761  -28.859 1.00 13.27 ? 380  ARG B CA    1 
ATOM   6924  C C     . ARG B  1  380 ? 51.276  44.868  -29.384 1.00 12.16 ? 380  ARG B C     1 
ATOM   6925  O O     . ARG B  1  380 ? 50.543  45.790  -29.026 1.00 13.71 ? 380  ARG B O     1 
ATOM   6926  C CB    . ARG B  1  380 ? 53.478  46.011  -29.269 1.00 15.65 ? 380  ARG B CB    1 
ATOM   6927  C CG    . ARG B  1  380 ? 54.831  46.182  -28.608 1.00 21.00 ? 380  ARG B CG    1 
ATOM   6928  C CD    . ARG B  1  380 ? 55.478  47.454  -29.128 1.00 25.39 ? 380  ARG B CD    1 
ATOM   6929  N NE    . ARG B  1  380 ? 56.812  47.687  -28.588 1.00 30.13 ? 380  ARG B NE    1 
ATOM   6930  C CZ    . ARG B  1  380 ? 57.064  48.179  -27.380 1.00 32.33 ? 380  ARG B CZ    1 
ATOM   6931  N NH1   . ARG B  1  380 ? 56.071  48.499  -26.567 1.00 33.18 ? 380  ARG B NH1   1 
ATOM   6932  N NH2   . ARG B  1  380 ? 58.318  48.365  -26.997 1.00 33.55 ? 380  ARG B NH2   1 
ATOM   6933  N N     . VAL B  1  381 ? 50.889  43.940  -30.252 1.00 11.30 ? 381  VAL B N     1 
ATOM   6934  C CA    . VAL B  1  381 ? 49.534  43.931  -30.791 1.00 12.10 ? 381  VAL B CA    1 
ATOM   6935  C C     . VAL B  1  381 ? 48.731  42.971  -29.923 1.00 12.35 ? 381  VAL B C     1 
ATOM   6936  O O     . VAL B  1  381 ? 49.044  41.783  -29.845 1.00 13.10 ? 381  VAL B O     1 
ATOM   6937  C CB    . VAL B  1  381 ? 49.504  43.450  -32.260 1.00 11.69 ? 381  VAL B CB    1 
ATOM   6938  C CG1   . VAL B  1  381 ? 48.068  43.364  -32.753 1.00 13.41 ? 381  VAL B CG1   1 
ATOM   6939  C CG2   . VAL B  1  381 ? 50.290  44.415  -33.134 1.00 12.27 ? 381  VAL B CG2   1 
ATOM   6940  N N     . SER B  1  382 ? 47.705  43.496  -29.261 1.00 12.40 ? 382  SER B N     1 
ATOM   6941  C CA    . SER B  1  382 ? 46.867  42.698  -28.372 1.00 13.73 ? 382  SER B CA    1 
ATOM   6942  C C     . SER B  1  382 ? 46.305  41.453  -29.041 1.00 12.99 ? 382  SER B C     1 
ATOM   6943  O O     . SER B  1  382 ? 45.884  41.489  -30.192 1.00 13.23 ? 382  SER B O     1 
ATOM   6944  C CB    . SER B  1  382 ? 45.708  43.544  -27.839 1.00 15.29 ? 382  SER B CB    1 
ATOM   6945  O OG    A SER B  1  382 ? 46.182  44.660  -27.111 0.50 16.97 ? 382  SER B OG    1 
ATOM   6946  O OG    B SER B  1  382 ? 44.892  42.832  -26.947 0.50 16.98 ? 382  SER B OG    1 
ATOM   6947  N N     . PRO B  1  383 ? 46.297  40.324  -28.320 1.00 12.75 ? 383  PRO B N     1 
ATOM   6948  C CA    . PRO B  1  383 ? 45.767  39.082  -28.891 1.00 12.19 ? 383  PRO B CA    1 
ATOM   6949  C C     . PRO B  1  383 ? 44.254  39.157  -28.920 1.00 12.27 ? 383  PRO B C     1 
ATOM   6950  O O     . PRO B  1  383 ? 43.658  40.014  -28.269 1.00 13.88 ? 383  PRO B O     1 
ATOM   6951  C CB    . PRO B  1  383 ? 46.222  38.010  -27.898 1.00 11.41 ? 383  PRO B CB    1 
ATOM   6952  C CG    . PRO B  1  383 ? 47.388  38.653  -27.164 1.00 14.04 ? 383  PRO B CG    1 
ATOM   6953  C CD    . PRO B  1  383 ? 46.928  40.078  -27.012 1.00 12.81 ? 383  PRO B CD    1 
ATOM   6954  N N     . ASN B  1  384 ? 43.629  38.265  -29.673 1.00 10.61 ? 384  ASN B N     1 
ATOM   6955  C CA    . ASN B  1  384 ? 42.182  38.228  -29.689 1.00 12.52 ? 384  ASN B CA    1 
ATOM   6956  C C     . ASN B  1  384 ? 41.813  37.243  -28.597 1.00 11.31 ? 384  ASN B C     1 
ATOM   6957  O O     . ASN B  1  384 ? 42.498  36.249  -28.409 1.00 11.88 ? 384  ASN B O     1 
ATOM   6958  C CB    . ASN B  1  384 ? 41.652  37.724  -31.035 1.00 12.87 ? 384  ASN B CB    1 
ATOM   6959  C CG    . ASN B  1  384 ? 41.662  38.798  -32.110 0.50 15.88 ? 384  ASN B CG    1 
ATOM   6960  O OD1   . ASN B  1  384 ? 41.191  39.914  -31.891 0.50 18.40 ? 384  ASN B OD1   1 
ATOM   6961  N ND2   . ASN B  1  384 ? 42.182  38.458  -33.283 0.50 17.82 ? 384  ASN B ND2   1 
ATOM   6962  N N     . VAL B  1  385 ? 40.738  37.522  -27.876 1.00 10.34 ? 385  VAL B N     1 
ATOM   6963  C CA    . VAL B  1  385 ? 40.288  36.636  -26.824 1.00 9.25  ? 385  VAL B CA    1 
ATOM   6964  C C     . VAL B  1  385 ? 38.772  36.576  -26.807 1.00 9.87  ? 385  VAL B C     1 
ATOM   6965  O O     . VAL B  1  385 ? 38.103  37.583  -27.025 1.00 8.92  ? 385  VAL B O     1 
ATOM   6966  C CB    . VAL B  1  385 ? 40.780  37.110  -25.430 1.00 11.09 ? 385  VAL B CB    1 
ATOM   6967  C CG1   . VAL B  1  385 ? 42.292  37.076  -25.359 0.50 7.89  ? 385  VAL B CG1   1 
ATOM   6968  C CG2   . VAL B  1  385 ? 40.280  38.519  -25.147 0.50 7.36  ? 385  VAL B CG2   1 
ATOM   6969  N N     . LYS B  1  386 ? 38.234  35.384  -26.585 1.00 7.97  ? 386  LYS B N     1 
ATOM   6970  C CA    . LYS B  1  386 ? 36.791  35.208  -26.488 1.00 8.96  ? 386  LYS B CA    1 
ATOM   6971  C C     . LYS B  1  386 ? 36.516  34.426  -25.212 1.00 9.05  ? 386  LYS B C     1 
ATOM   6972  O O     . LYS B  1  386 ? 37.196  33.441  -24.930 1.00 9.80  ? 386  LYS B O     1 
ATOM   6973  C CB    . LYS B  1  386 ? 36.234  34.465  -27.705 1.00 10.45 ? 386  LYS B CB    1 
ATOM   6974  C CG    . LYS B  1  386 ? 34.711  34.468  -27.728 1.00 11.71 ? 386  LYS B CG    1 
ATOM   6975  C CD    . LYS B  1  386 ? 34.142  33.899  -29.009 1.00 12.02 ? 386  LYS B CD    1 
ATOM   6976  C CE    . LYS B  1  386 ? 32.639  34.139  -29.066 1.00 13.95 ? 386  LYS B CE    1 
ATOM   6977  N NZ    . LYS B  1  386 ? 32.035  33.624  -30.327 1.00 15.16 ? 386  LYS B NZ    1 
ATOM   6978  N N     . PHE B  1  387 ? 35.526  34.860  -24.437 1.00 7.55  ? 387  PHE B N     1 
ATOM   6979  C CA    . PHE B  1  387 ? 35.220  34.187  -23.178 1.00 7.25  ? 387  PHE B CA    1 
ATOM   6980  C C     . PHE B  1  387 ? 33.937  33.350  -23.183 1.00 7.17  ? 387  PHE B C     1 
ATOM   6981  O O     . PHE B  1  387 ? 33.728  32.523  -22.298 1.00 7.63  ? 387  PHE B O     1 
ATOM   6982  C CB    . PHE B  1  387 ? 35.172  35.222  -22.050 1.00 8.44  ? 387  PHE B CB    1 
ATOM   6983  C CG    . PHE B  1  387 ? 36.472  35.962  -21.845 1.00 6.75  ? 387  PHE B CG    1 
ATOM   6984  C CD1   . PHE B  1  387 ? 36.543  37.339  -22.034 1.00 6.46  ? 387  PHE B CD1   1 
ATOM   6985  C CD2   . PHE B  1  387 ? 37.617  35.285  -21.430 1.00 7.18  ? 387  PHE B CD2   1 
ATOM   6986  C CE1   . PHE B  1  387 ? 37.735  38.035  -21.805 1.00 7.94  ? 387  PHE B CE1   1 
ATOM   6987  C CE2   . PHE B  1  387 ? 38.814  35.969  -21.198 1.00 7.33  ? 387  PHE B CE2   1 
ATOM   6988  C CZ    . PHE B  1  387 ? 38.872  37.348  -21.385 1.00 7.57  ? 387  PHE B CZ    1 
ATOM   6989  N N     . ASN B  1  388 ? 33.089  33.559  -24.185 1.00 6.43  ? 388  ASN B N     1 
ATOM   6990  C CA    . ASN B  1  388 ? 31.835  32.815  -24.312 1.00 7.22  ? 388  ASN B CA    1 
ATOM   6991  C C     . ASN B  1  388 ? 30.942  32.889  -23.076 1.00 7.26  ? 388  ASN B C     1 
ATOM   6992  O O     . ASN B  1  388 ? 30.475  31.867  -22.565 1.00 6.84  ? 388  ASN B O     1 
ATOM   6993  C CB    . ASN B  1  388 ? 32.128  31.350  -24.655 1.00 7.87  ? 388  ASN B CB    1 
ATOM   6994  C CG    . ASN B  1  388 ? 32.764  31.193  -26.020 1.00 10.15 ? 388  ASN B CG    1 
ATOM   6995  O OD1   . ASN B  1  388 ? 32.283  31.754  -27.005 1.00 10.71 ? 388  ASN B OD1   1 
ATOM   6996  N ND2   . ASN B  1  388 ? 33.847  30.426  -26.089 1.00 10.32 ? 388  ASN B ND2   1 
ATOM   6997  N N     . TYR B  1  389 ? 30.696  34.107  -22.609 1.00 6.95  ? 389  TYR B N     1 
ATOM   6998  C CA    . TYR B  1  389 ? 29.860  34.321  -21.438 1.00 7.32  ? 389  TYR B CA    1 
ATOM   6999  C C     . TYR B  1  389 ? 28.548  33.560  -21.543 1.00 8.14  ? 389  TYR B C     1 
ATOM   7000  O O     . TYR B  1  389 ? 27.871  33.592  -22.577 1.00 8.39  ? 389  TYR B O     1 
ATOM   7001  C CB    . TYR B  1  389 ? 29.550  35.810  -21.254 1.00 7.77  ? 389  TYR B CB    1 
ATOM   7002  C CG    . TYR B  1  389 ? 30.763  36.695  -21.105 1.00 7.43  ? 389  TYR B CG    1 
ATOM   7003  C CD1   . TYR B  1  389 ? 31.287  37.385  -22.199 1.00 7.62  ? 389  TYR B CD1   1 
ATOM   7004  C CD2   . TYR B  1  389 ? 31.387  36.848  -19.866 1.00 7.38  ? 389  TYR B CD2   1 
ATOM   7005  C CE1   . TYR B  1  389 ? 32.404  38.207  -22.066 1.00 6.75  ? 389  TYR B CE1   1 
ATOM   7006  C CE2   . TYR B  1  389 ? 32.507  37.666  -19.718 1.00 7.35  ? 389  TYR B CE2   1 
ATOM   7007  C CZ    . TYR B  1  389 ? 33.008  38.343  -20.822 1.00 7.01  ? 389  TYR B CZ    1 
ATOM   7008  O OH    . TYR B  1  389 ? 34.106  39.157  -20.683 1.00 8.51  ? 389  TYR B OH    1 
ATOM   7009  N N     . TYR B  1  390 ? 28.209  32.866  -20.462 1.00 7.67  ? 390  TYR B N     1 
ATOM   7010  C CA    . TYR B  1  390 ? 26.971  32.104  -20.356 1.00 8.14  ? 390  TYR B CA    1 
ATOM   7011  C C     . TYR B  1  390 ? 26.759  30.961  -21.345 1.00 9.61  ? 390  TYR B C     1 
ATOM   7012  O O     . TYR B  1  390 ? 25.633  30.495  -21.530 1.00 11.26 ? 390  TYR B O     1 
ATOM   7013  C CB    . TYR B  1  390 ? 25.781  33.077  -20.373 1.00 8.16  ? 390  TYR B CB    1 
ATOM   7014  C CG    . TYR B  1  390 ? 25.809  34.012  -19.179 1.00 10.45 ? 390  TYR B CG    1 
ATOM   7015  C CD1   . TYR B  1  390 ? 25.707  35.398  -19.336 1.00 11.50 ? 390  TYR B CD1   1 
ATOM   7016  C CD2   . TYR B  1  390 ? 26.007  33.510  -17.893 1.00 10.65 ? 390  TYR B CD2   1 
ATOM   7017  C CE1   . TYR B  1  390 ? 25.815  36.257  -18.232 1.00 13.24 ? 390  TYR B CE1   1 
ATOM   7018  C CE2   . TYR B  1  390 ? 26.116  34.358  -16.792 1.00 11.35 ? 390  TYR B CE2   1 
ATOM   7019  C CZ    . TYR B  1  390 ? 26.024  35.723  -16.966 1.00 11.78 ? 390  TYR B CZ    1 
ATOM   7020  O OH    . TYR B  1  390 ? 26.186  36.549  -15.873 1.00 11.93 ? 390  TYR B OH    1 
ATOM   7021  N N     . SER B  1  391 ? 27.836  30.494  -21.971 1.00 8.98  ? 391  SER B N     1 
ATOM   7022  C CA    . SER B  1  391 ? 27.722  29.368  -22.893 1.00 10.13 ? 391  SER B CA    1 
ATOM   7023  C C     . SER B  1  391 ? 27.367  28.150  -22.042 1.00 10.86 ? 391  SER B C     1 
ATOM   7024  O O     . SER B  1  391 ? 26.699  27.221  -22.501 1.00 12.80 ? 391  SER B O     1 
ATOM   7025  C CB    . SER B  1  391 ? 29.036  29.150  -23.649 1.00 9.78  ? 391  SER B CB    1 
ATOM   7026  O OG    . SER B  1  391 ? 30.131  29.020  -22.761 1.00 12.89 ? 391  SER B OG    1 
ATOM   7027  N N     . ASN B  1  392 ? 27.822  28.158  -20.792 1.00 11.14 ? 392  ASN B N     1 
ATOM   7028  C CA    . ASN B  1  392 ? 27.492  27.086  -19.868 1.00 11.16 ? 392  ASN B CA    1 
ATOM   7029  C C     . ASN B  1  392 ? 26.289  27.610  -19.092 1.00 11.66 ? 392  ASN B C     1 
ATOM   7030  O O     . ASN B  1  392 ? 26.382  28.619  -18.388 1.00 10.60 ? 392  ASN B O     1 
ATOM   7031  C CB    . ASN B  1  392 ? 28.643  26.800  -18.910 1.00 11.80 ? 392  ASN B CB    1 
ATOM   7032  C CG    . ASN B  1  392 ? 28.374  25.592  -18.048 1.00 12.50 ? 392  ASN B CG    1 
ATOM   7033  O OD1   . ASN B  1  392 ? 27.496  25.617  -17.188 1.00 13.27 ? 392  ASN B OD1   1 
ATOM   7034  N ND2   . ASN B  1  392 ? 29.116  24.519  -18.293 1.00 15.37 ? 392  ASN B ND2   1 
ATOM   7035  N N     . LEU B  1  393 ? 25.157  26.928  -19.226 1.00 10.90 ? 393  LEU B N     1 
ATOM   7036  C CA    . LEU B  1  393 ? 23.931  27.367  -18.574 1.00 9.80  ? 393  LEU B CA    1 
ATOM   7037  C C     . LEU B  1  393 ? 23.954  27.407  -17.053 1.00 8.87  ? 393  LEU B C     1 
ATOM   7038  O O     . LEU B  1  393 ? 23.141  28.103  -16.443 1.00 9.69  ? 393  LEU B O     1 
ATOM   7039  C CB    . LEU B  1  393 ? 22.753  26.520  -19.063 1.00 11.76 ? 393  LEU B CB    1 
ATOM   7040  C CG    . LEU B  1  393 ? 22.497  26.641  -20.570 1.00 14.30 ? 393  LEU B CG    1 
ATOM   7041  C CD1   . LEU B  1  393 ? 21.344  25.735  -20.959 1.00 15.29 ? 393  LEU B CD1   1 
ATOM   7042  C CD2   . LEU B  1  393 ? 22.186  28.088  -20.936 1.00 15.34 ? 393  LEU B CD2   1 
ATOM   7043  N N     . THR B  1  394 ? 24.870  26.674  -16.429 1.00 8.13  ? 394  THR B N     1 
ATOM   7044  C CA    . THR B  1  394 ? 24.946  26.707  -14.973 1.00 8.68  ? 394  THR B CA    1 
ATOM   7045  C C     . THR B  1  394 ? 25.446  28.094  -14.555 1.00 9.08  ? 394  THR B C     1 
ATOM   7046  O O     . THR B  1  394 ? 25.035  28.618  -13.520 1.00 9.50  ? 394  THR B O     1 
ATOM   7047  C CB    . THR B  1  394 ? 25.859  25.587  -14.423 1.00 9.74  ? 394  THR B CB    1 
ATOM   7048  O OG1   . THR B  1  394 ? 25.254  24.313  -14.692 1.00 12.27 ? 394  THR B OG1   1 
ATOM   7049  C CG2   . THR B  1  394 ? 26.042  25.732  -12.918 1.00 10.55 ? 394  THR B CG2   1 
ATOM   7050  N N     . ASP B  1  395 ? 26.314  28.701  -15.363 1.00 7.77  ? 395  ASP B N     1 
ATOM   7051  C CA    . ASP B  1  395 ? 26.785  30.051  -15.049 1.00 8.28  ? 395  ASP B CA    1 
ATOM   7052  C C     . ASP B  1  395 ? 25.572  30.989  -15.077 1.00 7.74  ? 395  ASP B C     1 
ATOM   7053  O O     . ASP B  1  395 ? 25.438  31.873  -14.228 1.00 7.48  ? 395  ASP B O     1 
ATOM   7054  C CB    . ASP B  1  395 ? 27.806  30.562  -16.079 1.00 7.46  ? 395  ASP B CB    1 
ATOM   7055  C CG    . ASP B  1  395 ? 29.195  29.956  -15.911 1.00 8.19  ? 395  ASP B CG    1 
ATOM   7056  O OD1   . ASP B  1  395 ? 29.492  29.370  -14.847 1.00 7.49  ? 395  ASP B OD1   1 
ATOM   7057  O OD2   . ASP B  1  395 ? 30.002  30.091  -16.855 1.00 8.74  ? 395  ASP B OD2   1 
ATOM   7058  N N     . LEU B  1  396 ? 24.696  30.801  -16.066 1.00 7.99  ? 396  LEU B N     1 
ATOM   7059  C CA    . LEU B  1  396 ? 23.504  31.638  -16.207 1.00 7.41  ? 396  LEU B CA    1 
ATOM   7060  C C     . LEU B  1  396 ? 22.569  31.494  -15.008 1.00 7.99  ? 396  LEU B C     1 
ATOM   7061  O O     . LEU B  1  396 ? 22.067  32.486  -14.488 1.00 7.37  ? 396  LEU B O     1 
ATOM   7062  C CB    . LEU B  1  396 ? 22.753  31.291  -17.504 1.00 8.28  ? 396  LEU B CB    1 
ATOM   7063  C CG    . LEU B  1  396 ? 21.536  32.163  -17.845 1.00 7.26  ? 396  LEU B CG    1 
ATOM   7064  C CD1   . LEU B  1  396 ? 21.947  33.625  -17.951 1.00 8.99  ? 396  LEU B CD1   1 
ATOM   7065  C CD2   . LEU B  1  396 ? 20.920  31.688  -19.157 1.00 9.26  ? 396  LEU B CD2   1 
ATOM   7066  N N     . SER B  1  397 ? 22.337  30.262  -14.568 1.00 8.81  ? 397  SER B N     1 
ATOM   7067  C CA    . SER B  1  397 ? 21.470  30.036  -13.416 1.00 8.29  ? 397  SER B CA    1 
ATOM   7068  C C     . SER B  1  397 ? 22.040  30.771  -12.208 1.00 9.30  ? 397  SER B C     1 
ATOM   7069  O O     . SER B  1  397 ? 21.301  31.345  -11.406 1.00 9.17  ? 397  SER B O     1 
ATOM   7070  C CB    . SER B  1  397 ? 21.365  28.538  -13.110 1.00 9.92  ? 397  SER B CB    1 
ATOM   7071  O OG    A SER B  1  397 ? 22.617  28.001  -12.734 0.50 13.48 ? 397  SER B OG    1 
ATOM   7072  O OG    B SER B  1  397 ? 20.500  28.337  -11.996 0.50 13.31 ? 397  SER B OG    1 
ATOM   7073  N N     . HIS B  1  398 ? 23.362  30.753  -12.085 1.00 8.78  ? 398  HIS B N     1 
ATOM   7074  C CA    . HIS B  1  398 ? 24.023  31.429  -10.979 1.00 8.50  ? 398  HIS B CA    1 
ATOM   7075  C C     . HIS B  1  398 ? 23.872  32.942  -11.087 1.00 9.84  ? 398  HIS B C     1 
ATOM   7076  O O     . HIS B  1  398 ? 23.746  33.618  -10.068 1.00 9.78  ? 398  HIS B O     1 
ATOM   7077  C CB    . HIS B  1  398 ? 25.495  31.018  -10.918 1.00 9.76  ? 398  HIS B CB    1 
ATOM   7078  C CG    . HIS B  1  398 ? 25.694  29.595  -10.498 1.00 11.18 ? 398  HIS B CG    1 
ATOM   7079  N ND1   . HIS B  1  398 ? 26.900  28.939  -10.623 1.00 10.87 ? 398  HIS B ND1   1 
ATOM   7080  C CD2   . HIS B  1  398 ? 24.836  28.701  -9.951  1.00 11.09 ? 398  HIS B CD2   1 
ATOM   7081  C CE1   . HIS B  1  398 ? 26.775  27.704  -10.172 1.00 11.42 ? 398  HIS B CE1   1 
ATOM   7082  N NE2   . HIS B  1  398 ? 25.532  27.533  -9.759  1.00 12.09 ? 398  HIS B NE2   1 
ATOM   7083  N N     . CYS B  1  399 ? 23.871  33.475  -12.310 1.00 9.33  ? 399  CYS B N     1 
ATOM   7084  C CA    . CYS B  1  399 ? 23.692  34.917  -12.496 1.00 8.79  ? 399  CYS B CA    1 
ATOM   7085  C C     . CYS B  1  399 ? 22.298  35.289  -12.029 1.00 8.55  ? 399  CYS B C     1 
ATOM   7086  O O     . CYS B  1  399 ? 22.099  36.297  -11.355 1.00 8.75  ? 399  CYS B O     1 
ATOM   7087  C CB    . CYS B  1  399 ? 23.823  35.337  -13.968 1.00 10.46 ? 399  CYS B CB    1 
ATOM   7088  S SG    . CYS B  1  399 ? 23.429  37.112  -14.202 1.00 14.49 ? 399  CYS B SG    1 
ATOM   7089  N N     . VAL B  1  400 ? 21.328  34.473  -12.413 1.00 9.25  ? 400  VAL B N     1 
ATOM   7090  C CA    . VAL B  1  400 ? 19.941  34.708  -12.040 1.00 9.12  ? 400  VAL B CA    1 
ATOM   7091  C C     . VAL B  1  400 ? 19.789  34.763  -10.525 1.00 9.60  ? 400  VAL B C     1 
ATOM   7092  O O     . VAL B  1  400 ? 19.196  35.697  -9.988  1.00 8.48  ? 400  VAL B O     1 
ATOM   7093  C CB    . VAL B  1  400 ? 19.011  33.611  -12.614 1.00 8.96  ? 400  VAL B CB    1 
ATOM   7094  C CG1   . VAL B  1  400 ? 17.594  33.802  -12.093 1.00 9.83  ? 400  VAL B CG1   1 
ATOM   7095  C CG2   . VAL B  1  400 ? 19.018  33.682  -14.138 1.00 10.21 ? 400  VAL B CG2   1 
ATOM   7096  N N     . SER B  1  401 ? 20.331  33.765  -9.834  1.00 9.66  ? 401  SER B N     1 
ATOM   7097  C CA    . SER B  1  401 ? 20.250  33.733  -8.379  1.00 9.17  ? 401  SER B CA    1 
ATOM   7098  C C     . SER B  1  401 ? 20.942  34.959  -7.797  1.00 8.88  ? 401  SER B C     1 
ATOM   7099  O O     . SER B  1  401 ? 20.443  35.585  -6.861  1.00 8.31  ? 401  SER B O     1 
ATOM   7100  C CB    . SER B  1  401 ? 20.905  32.460  -7.840  1.00 11.03 ? 401  SER B CB    1 
ATOM   7101  O OG    . SER B  1  401 ? 20.225  31.308  -8.308  1.00 15.51 ? 401  SER B OG    1 
ATOM   7102  N N     . GLY B  1  402 ? 22.093  35.301  -8.366  1.00 7.78  ? 402  GLY B N     1 
ATOM   7103  C CA    . GLY B  1  402 ? 22.834  36.456  -7.897  1.00 7.08  ? 402  GLY B CA    1 
ATOM   7104  C C     . GLY B  1  402 ? 22.072  37.758  -8.055  1.00 7.19  ? 402  GLY B C     1 
ATOM   7105  O O     . GLY B  1  402 ? 22.047  38.571  -7.136  1.00 7.19  ? 402  GLY B O     1 
ATOM   7106  N N     . MET B  1  403 ? 21.443  37.969  -9.208  1.00 6.69  ? 403  MET B N     1 
ATOM   7107  C CA    . MET B  1  403 ? 20.700  39.208  -9.409  1.00 7.09  ? 403  MET B CA    1 
ATOM   7108  C C     . MET B  1  403 ? 19.424  39.268  -8.576  1.00 7.90  ? 403  MET B C     1 
ATOM   7109  O O     . MET B  1  403 ? 18.955  40.349  -8.231  1.00 7.54  ? 403  MET B O     1 
ATOM   7110  C CB    . MET B  1  403 ? 20.406  39.429  -10.895 1.00 7.99  ? 403  MET B CB    1 
ATOM   7111  C CG    . MET B  1  403 ? 21.663  39.705  -11.724 1.00 7.48  ? 403  MET B CG    1 
ATOM   7112  S SD    . MET B  1  403 ? 22.884  40.805  -10.922 1.00 10.30 ? 403  MET B SD    1 
ATOM   7113  C CE    . MET B  1  403 ? 21.993  42.387  -10.883 1.00 10.53 ? 403  MET B CE    1 
ATOM   7114  N N     . LYS B  1  404 ? 18.860  38.111  -8.252  1.00 8.38  ? 404  LYS B N     1 
ATOM   7115  C CA    . LYS B  1  404 ? 17.681  38.088  -7.402  1.00 9.26  ? 404  LYS B CA    1 
ATOM   7116  C C     . LYS B  1  404 ? 18.120  38.542  -6.018  1.00 9.42  ? 404  LYS B C     1 
ATOM   7117  O O     . LYS B  1  404 ? 17.376  39.225  -5.317  1.00 9.08  ? 404  LYS B O     1 
ATOM   7118  C CB    . LYS B  1  404 ? 17.081  36.678  -7.324  1.00 9.96  ? 404  LYS B CB    1 
ATOM   7119  C CG    . LYS B  1  404 ? 16.274  36.257  -8.542  1.00 9.93  ? 404  LYS B CG    1 
ATOM   7120  C CD    . LYS B  1  404 ? 15.763  34.836  -8.368  1.00 9.22  ? 404  LYS B CD    1 
ATOM   7121  C CE    . LYS B  1  404 ? 14.857  34.418  -9.509  1.00 9.94  ? 404  LYS B CE    1 
ATOM   7122  N NZ    . LYS B  1  404 ? 14.438  32.995  -9.375  1.00 11.21 ? 404  LYS B NZ    1 
ATOM   7123  N N     . LYS B  1  405 ? 19.337  38.172  -5.623  1.00 8.87  ? 405  LYS B N     1 
ATOM   7124  C CA    . LYS B  1  405 ? 19.838  38.580  -4.314  1.00 7.96  ? 405  LYS B CA    1 
ATOM   7125  C C     . LYS B  1  405 ? 20.038  40.095  -4.308  1.00 8.33  ? 405  LYS B C     1 
ATOM   7126  O O     . LYS B  1  405 ? 19.777  40.761  -3.307  1.00 8.01  ? 405  LYS B O     1 
ATOM   7127  C CB    . LYS B  1  405 ? 21.146  37.853  -3.970  1.00 8.31  ? 405  LYS B CB    1 
ATOM   7128  C CG    . LYS B  1  405 ? 21.712  38.214  -2.585  1.00 6.86  ? 405  LYS B CG    1 
ATOM   7129  C CD    . LYS B  1  405 ? 20.745  37.873  -1.445  1.00 8.42  ? 405  LYS B CD    1 
ATOM   7130  C CE    . LYS B  1  405 ? 20.568  36.370  -1.278  1.00 8.98  ? 405  LYS B CE    1 
ATOM   7131  N NZ    . LYS B  1  405 ? 19.628  36.031  -0.159  1.00 11.21 ? 405  LYS B NZ    1 
ATOM   7132  N N     . ILE B  1  406 ? 20.492  40.645  -5.431  1.00 8.07  ? 406  ILE B N     1 
ATOM   7133  C CA    . ILE B  1  406 ? 20.656  42.091  -5.528  1.00 8.99  ? 406  ILE B CA    1 
ATOM   7134  C C     . ILE B  1  406 ? 19.252  42.676  -5.368  1.00 8.75  ? 406  ILE B C     1 
ATOM   7135  O O     . ILE B  1  406 ? 19.062  43.698  -4.706  1.00 8.72  ? 406  ILE B O     1 
ATOM   7136  C CB    . ILE B  1  406 ? 21.248  42.524  -6.898  1.00 8.41  ? 406  ILE B CB    1 
ATOM   7137  C CG1   . ILE B  1  406 ? 22.694  42.029  -7.026  1.00 8.78  ? 406  ILE B CG1   1 
ATOM   7138  C CG2   . ILE B  1  406 ? 21.190  44.040  -7.035  1.00 9.40  ? 406  ILE B CG2   1 
ATOM   7139  C CD1   . ILE B  1  406 ? 23.627  42.519  -5.925  1.00 11.75 ? 406  ILE B CD1   1 
ATOM   7140  N N     . GLY B  1  407 ? 18.264  42.009  -5.963  1.00 9.81  ? 407  GLY B N     1 
ATOM   7141  C CA    . GLY B  1  407 ? 16.888  42.463  -5.844  1.00 8.93  ? 407  GLY B CA    1 
ATOM   7142  C C     . GLY B  1  407 ? 16.484  42.521  -4.382  1.00 9.54  ? 407  GLY B C     1 
ATOM   7143  O O     . GLY B  1  407 ? 15.779  43.437  -3.954  1.00 10.37 ? 407  GLY B O     1 
ATOM   7144  N N     . GLU B  1  408 ? 16.927  41.537  -3.606  1.00 9.09  ? 408  GLU B N     1 
ATOM   7145  C CA    . GLU B  1  408 ? 16.621  41.509  -2.180  1.00 9.03  ? 408  GLU B CA    1 
ATOM   7146  C C     . GLU B  1  408 ? 17.269  42.710  -1.497  1.00 9.42  ? 408  GLU B C     1 
ATOM   7147  O O     . GLU B  1  408 ? 16.643  43.368  -0.666  1.00 10.41 ? 408  GLU B O     1 
ATOM   7148  C CB    . GLU B  1  408 ? 17.134  40.219  -1.535  1.00 8.61  ? 408  GLU B CB    1 
ATOM   7149  C CG    . GLU B  1  408 ? 16.276  38.992  -1.802  1.00 11.19 ? 408  GLU B CG    1 
ATOM   7150  C CD    . GLU B  1  408 ? 16.707  37.801  -0.961  1.00 12.85 ? 408  GLU B CD    1 
ATOM   7151  O OE1   . GLU B  1  408 ? 17.434  36.925  -1.475  1.00 14.08 ? 408  GLU B OE1   1 
ATOM   7152  O OE2   . GLU B  1  408 ? 16.327  37.754  0.228   1.00 16.94 ? 408  GLU B OE2   1 
ATOM   7153  N N     . LEU B  1  409 ? 18.526  42.988  -1.845  1.00 9.17  ? 409  LEU B N     1 
ATOM   7154  C CA    . LEU B  1  409 ? 19.229  44.124  -1.260  1.00 9.12  ? 409  LEU B CA    1 
ATOM   7155  C C     . LEU B  1  409 ? 18.475  45.421  -1.514  1.00 9.71  ? 409  LEU B C     1 
ATOM   7156  O O     . LEU B  1  409 ? 18.344  46.253  -0.620  1.00 9.87  ? 409  LEU B O     1 
ATOM   7157  C CB    . LEU B  1  409 ? 20.645  44.248  -1.826  1.00 9.79  ? 409  LEU B CB    1 
ATOM   7158  C CG    A LEU B  1  409 ? 21.757  43.573  -1.019  0.50 8.45  ? 409  LEU B CG    1 
ATOM   7159  C CG    B LEU B  1  409 ? 21.574  43.039  -1.564  0.50 8.53  ? 409  LEU B CG    1 
ATOM   7160  C CD1   A LEU B  1  409 ? 21.650  42.069  -1.144  0.50 9.46  ? 409  LEU B CD1   1 
ATOM   7161  C CD1   B LEU B  1  409 ? 22.946  43.283  -2.174  0.50 9.56  ? 409  LEU B CD1   1 
ATOM   7162  C CD2   A LEU B  1  409 ? 23.111  44.049  -1.525  0.50 9.87  ? 409  LEU B CD2   1 
ATOM   7163  C CD2   B LEU B  1  409 ? 21.695  42.757  -0.074  0.50 10.04 ? 409  LEU B CD2   1 
ATOM   7164  N N     . LEU B  1  410 ? 17.986  45.589  -2.739  1.00 10.66 ? 410  LEU B N     1 
ATOM   7165  C CA    . LEU B  1  410 ? 17.248  46.790  -3.110  1.00 10.76 ? 410  LEU B CA    1 
ATOM   7166  C C     . LEU B  1  410 ? 15.925  46.915  -2.362  1.00 11.82 ? 410  LEU B C     1 
ATOM   7167  O O     . LEU B  1  410 ? 15.359  48.006  -2.269  1.00 13.75 ? 410  LEU B O     1 
ATOM   7168  C CB    . LEU B  1  410 ? 16.976  46.797  -4.615  1.00 10.83 ? 410  LEU B CB    1 
ATOM   7169  C CG    . LEU B  1  410 ? 18.208  46.942  -5.506  1.00 9.93  ? 410  LEU B CG    1 
ATOM   7170  C CD1   . LEU B  1  410 ? 17.790  46.867  -6.970  1.00 13.06 ? 410  LEU B CD1   1 
ATOM   7171  C CD2   . LEU B  1  410 ? 18.903  48.261  -5.212  1.00 12.63 ? 410  LEU B CD2   1 
ATOM   7172  N N     . SER B  1  411 ? 15.442  45.798  -1.828  1.00 10.31 ? 411  SER B N     1 
ATOM   7173  C CA    . SER B  1  411 ? 14.173  45.773  -1.104  1.00 10.54 ? 411  SER B CA    1 
ATOM   7174  C C     . SER B  1  411 ? 14.318  45.867  0.414   1.00 11.34 ? 411  SER B C     1 
ATOM   7175  O O     . SER B  1  411 ? 13.319  45.845  1.137   1.00 12.21 ? 411  SER B O     1 
ATOM   7176  C CB    . SER B  1  411 ? 13.411  44.494  -1.452  1.00 11.32 ? 411  SER B CB    1 
ATOM   7177  O OG    . SER B  1  411 ? 13.300  44.334  -2.858  1.00 13.16 ? 411  SER B OG    1 
ATOM   7178  N N     . THR B  1  412 ? 15.553  45.976  0.895   1.00 11.09 ? 412  THR B N     1 
ATOM   7179  C CA    . THR B  1  412 ? 15.812  46.051  2.331   1.00 10.38 ? 412  THR B CA    1 
ATOM   7180  C C     . THR B  1  412 ? 15.478  47.405  2.946   1.00 11.07 ? 412  THR B C     1 
ATOM   7181  O O     . THR B  1  412 ? 15.427  48.419  2.252   1.00 11.92 ? 412  THR B O     1 
ATOM   7182  C CB    . THR B  1  412 ? 17.300  45.778  2.662   1.00 8.78  ? 412  THR B CB    1 
ATOM   7183  O OG1   . THR B  1  412 ? 18.120  46.763  2.019   1.00 9.94  ? 412  THR B OG1   1 
ATOM   7184  C CG2   . THR B  1  412 ? 17.714  44.387  2.206   1.00 8.88  ? 412  THR B CG2   1 
ATOM   7185  N N     . ASP B  1  413 ? 15.255  47.411  4.258   1.00 12.28 ? 413  ASP B N     1 
ATOM   7186  C CA    . ASP B  1  413 ? 14.978  48.657  4.967   1.00 12.48 ? 413  ASP B CA    1 
ATOM   7187  C C     . ASP B  1  413 ? 16.223  49.520  4.791   1.00 12.38 ? 413  ASP B C     1 
ATOM   7188  O O     . ASP B  1  413 ? 16.142  50.741  4.651   1.00 12.69 ? 413  ASP B O     1 
ATOM   7189  C CB    . ASP B  1  413 ? 14.782  48.415  6.471   1.00 12.56 ? 413  ASP B CB    1 
ATOM   7190  C CG    . ASP B  1  413 ? 13.517  47.641  6.797   1.00 14.34 ? 413  ASP B CG    1 
ATOM   7191  O OD1   . ASP B  1  413 ? 12.687  47.409  5.894   1.00 14.89 ? 413  ASP B OD1   1 
ATOM   7192  O OD2   . ASP B  1  413 ? 13.352  47.272  7.984   1.00 14.49 ? 413  ASP B OD2   1 
ATOM   7193  N N     . ALA B  1  414 ? 17.378  48.860  4.807   1.00 11.51 ? 414  ALA B N     1 
ATOM   7194  C CA    . ALA B  1  414 ? 18.668  49.527  4.678   1.00 11.34 ? 414  ALA B CA    1 
ATOM   7195  C C     . ALA B  1  414 ? 18.803  50.440  3.464   1.00 11.91 ? 414  ALA B C     1 
ATOM   7196  O O     . ALA B  1  414 ? 19.390  51.510  3.557   1.00 12.70 ? 414  ALA B O     1 
ATOM   7197  C CB    . ALA B  1  414 ? 19.789  48.488  4.669   1.00 10.95 ? 414  ALA B CB    1 
ATOM   7198  N N     . LEU B  1  415 ? 18.260  50.039  2.322   1.00 12.07 ? 415  LEU B N     1 
ATOM   7199  C CA    . LEU B  1  415 ? 18.394  50.878  1.137   1.00 13.54 ? 415  LEU B CA    1 
ATOM   7200  C C     . LEU B  1  415 ? 17.173  51.755  0.852   1.00 14.81 ? 415  LEU B C     1 
ATOM   7201  O O     . LEU B  1  415 ? 17.174  52.552  -0.082  1.00 13.33 ? 415  LEU B O     1 
ATOM   7202  C CB    . LEU B  1  415 ? 18.712  50.007  -0.081  1.00 14.83 ? 415  LEU B CB    1 
ATOM   7203  C CG    . LEU B  1  415 ? 19.957  49.113  0.004   1.00 16.84 ? 415  LEU B CG    1 
ATOM   7204  C CD1   . LEU B  1  415 ? 20.286  48.579  -1.376  1.00 17.69 ? 415  LEU B CD1   1 
ATOM   7205  C CD2   . LEU B  1  415 ? 21.134  49.896  0.548   1.00 18.04 ? 415  LEU B CD2   1 
ATOM   7206  N N     . LYS B  1  416 ? 16.129  51.620  1.660   1.00 15.07 ? 416  LYS B N     1 
ATOM   7207  C CA    . LYS B  1  416 ? 14.919  52.418  1.463   1.00 16.89 ? 416  LYS B CA    1 
ATOM   7208  C C     . LYS B  1  416 ? 15.204  53.926  1.363   1.00 16.72 ? 416  LYS B C     1 
ATOM   7209  O O     . LYS B  1  416 ? 14.630  54.619  0.517   1.00 15.77 ? 416  LYS B O     1 
ATOM   7210  C CB    . LYS B  1  416 ? 13.922  52.135  2.602   1.00 18.94 ? 416  LYS B CB    1 
ATOM   7211  C CG    . LYS B  1  416 ? 12.472  52.465  2.277   1.00 23.75 ? 416  LYS B CG    1 
ATOM   7212  C CD    . LYS B  1  416 ? 11.547  52.102  3.441   1.00 26.51 ? 416  LYS B CD    1 
ATOM   7213  C CE    . LYS B  1  416 ? 11.426  50.591  3.636   1.00 28.05 ? 416  LYS B CE    1 
ATOM   7214  N NZ    . LYS B  1  416 ? 10.476  49.949  2.677   1.00 31.05 ? 416  LYS B NZ    1 
ATOM   7215  N N     . PRO B  1  417 ? 16.090  54.458  2.225   1.00 16.38 ? 417  PRO B N     1 
ATOM   7216  C CA    . PRO B  1  417 ? 16.416  55.889  2.194   1.00 16.64 ? 417  PRO B CA    1 
ATOM   7217  C C     . PRO B  1  417 ? 17.074  56.364  0.901   1.00 16.15 ? 417  PRO B C     1 
ATOM   7218  O O     . PRO B  1  417 ? 17.156  57.565  0.645   1.00 16.02 ? 417  PRO B O     1 
ATOM   7219  C CB    . PRO B  1  417 ? 17.354  56.059  3.389   1.00 17.24 ? 417  PRO B CB    1 
ATOM   7220  C CG    . PRO B  1  417 ? 16.920  54.986  4.325   1.00 17.89 ? 417  PRO B CG    1 
ATOM   7221  C CD    . PRO B  1  417 ? 16.704  53.812  3.398   1.00 16.58 ? 417  PRO B CD    1 
ATOM   7222  N N     . TYR B  1  418 ? 17.545  55.429  0.085   1.00 15.03 ? 418  TYR B N     1 
ATOM   7223  C CA    . TYR B  1  418 ? 18.213  55.811  -1.148  1.00 14.58 ? 418  TYR B CA    1 
ATOM   7224  C C     . TYR B  1  418 ? 17.341  55.751  -2.391  1.00 16.31 ? 418  TYR B C     1 
ATOM   7225  O O     . TYR B  1  418 ? 17.824  55.922  -3.510  1.00 15.89 ? 418  TYR B O     1 
ATOM   7226  C CB    . TYR B  1  418 ? 19.489  54.984  -1.305  1.00 15.22 ? 418  TYR B CB    1 
ATOM   7227  C CG    . TYR B  1  418 ? 20.383  55.167  -0.101  1.00 13.59 ? 418  TYR B CG    1 
ATOM   7228  C CD1   . TYR B  1  418 ? 20.340  54.273  0.970   1.00 14.42 ? 418  TYR B CD1   1 
ATOM   7229  C CD2   . TYR B  1  418 ? 21.185  56.302  0.023   1.00 12.95 ? 418  TYR B CD2   1 
ATOM   7230  C CE1   . TYR B  1  418 ? 21.066  54.512  2.138   1.00 14.96 ? 418  TYR B CE1   1 
ATOM   7231  C CE2   . TYR B  1  418 ? 21.910  56.550  1.183   1.00 15.92 ? 418  TYR B CE2   1 
ATOM   7232  C CZ    . TYR B  1  418 ? 21.845  55.655  2.236   1.00 15.61 ? 418  TYR B CZ    1 
ATOM   7233  O OH    . TYR B  1  418 ? 22.541  55.918  3.394   1.00 17.22 ? 418  TYR B OH    1 
ATOM   7234  N N     . LYS B  1  419 ? 16.050  55.514  -2.185  1.00 16.78 ? 419  LYS B N     1 
ATOM   7235  C CA    . LYS B  1  419 ? 15.091  55.494  -3.281  1.00 18.31 ? 419  LYS B CA    1 
ATOM   7236  C C     . LYS B  1  419 ? 14.662  56.947  -3.481  1.00 19.43 ? 419  LYS B C     1 
ATOM   7237  O O     . LYS B  1  419 ? 14.788  57.763  -2.566  1.00 20.45 ? 419  LYS B O     1 
ATOM   7238  C CB    . LYS B  1  419 ? 13.858  54.660  -2.918  1.00 18.78 ? 419  LYS B CB    1 
ATOM   7239  C CG    . LYS B  1  419 ? 14.081  53.162  -2.875  1.00 19.29 ? 419  LYS B CG    1 
ATOM   7240  C CD    . LYS B  1  419 ? 12.752  52.427  -2.774  1.00 19.23 ? 419  LYS B CD    1 
ATOM   7241  C CE    . LYS B  1  419 ? 12.941  50.920  -2.826  1.00 20.96 ? 419  LYS B CE    1 
ATOM   7242  N NZ    . LYS B  1  419 ? 11.643  50.194  -2.803  1.00 18.81 ? 419  LYS B NZ    1 
ATOM   7243  N N     . VAL B  1  420 ? 14.166  57.273  -4.669  1.00 19.99 ? 420  VAL B N     1 
ATOM   7244  C CA    . VAL B  1  420 ? 13.707  58.630  -4.940  1.00 22.83 ? 420  VAL B CA    1 
ATOM   7245  C C     . VAL B  1  420 ? 12.197  58.675  -4.751  1.00 25.66 ? 420  VAL B C     1 
ATOM   7246  O O     . VAL B  1  420 ? 11.598  59.745  -4.713  1.00 26.48 ? 420  VAL B O     1 
ATOM   7247  C CB    . VAL B  1  420 ? 14.043  59.068  -6.381  1.00 21.70 ? 420  VAL B CB    1 
ATOM   7248  C CG1   . VAL B  1  420 ? 15.544  59.121  -6.560  1.00 21.41 ? 420  VAL B CG1   1 
ATOM   7249  C CG2   . VAL B  1  420 ? 13.412  58.109  -7.384  1.00 21.92 ? 420  VAL B CG2   1 
ATOM   7250  N N     . GLU B  1  421 ? 11.596  57.498  -4.621  1.00 28.42 ? 421  GLU B N     1 
ATOM   7251  C CA    . GLU B  1  421 ? 10.157  57.388  -4.438  1.00 32.66 ? 421  GLU B CA    1 
ATOM   7252  C C     . GLU B  1  421 ? 9.747   56.128  -3.693  1.00 34.47 ? 421  GLU B C     1 
ATOM   7253  O O     . GLU B  1  421 ? 10.361  55.080  -3.842  1.00 33.84 ? 421  GLU B O     1 
ATOM   7254  C CB    . GLU B  1  421 ? 9.454   57.432  -5.807  1.00 33.69 ? 421  GLU B CB    1 
ATOM   7255  C CG    . GLU B  1  421 ? 8.000   56.959  -5.793  1.00 37.65 ? 421  GLU B CG    1 
ATOM   7256  C CD    . GLU B  1  421 ? 7.245   57.334  -7.062  1.00 39.47 ? 421  GLU B CD    1 
ATOM   7257  O OE1   . GLU B  1  421 ? 7.839   57.270  -8.163  1.00 40.94 ? 421  GLU B OE1   1 
ATOM   7258  O OE2   . GLU B  1  421 ? 6.050   57.692  -6.956  1.00 39.69 ? 421  GLU B OE2   1 
ATOM   7259  N N     . ASP B  1  422 ? 8.688   56.250  -2.899  1.00 37.05 ? 422  ASP B N     1 
ATOM   7260  C CA    . ASP B  1  422 ? 8.147   55.144  -2.118  1.00 38.52 ? 422  ASP B CA    1 
ATOM   7261  C C     . ASP B  1  422 ? 7.432   54.240  -3.103  1.00 38.91 ? 422  ASP B C     1 
ATOM   7262  O O     . ASP B  1  422 ? 6.443   54.655  -3.676  1.00 39.48 ? 422  ASP B O     1 
ATOM   7263  C CB    . ASP B  1  422 ? 7.123   55.674  -1.113  1.00 40.30 ? 422  ASP B CB    1 
ATOM   7264  C CG    . ASP B  1  422 ? 7.501   55.388  0.328   1.00 41.72 ? 422  ASP B CG    1 
ATOM   7265  O OD1   . ASP B  1  422 ? 7.829   54.224  0.660   1.00 41.78 ? 422  ASP B OD1   1 
ATOM   7266  O OD2   . ASP B  1  422 ? 7.440   56.343  1.133   1.00 42.68 ? 422  ASP B OD2   1 
ATOM   7267  N N     . LEU B  1  423 ? 7.933   53.028  -3.314  1.00 38.14 ? 423  LEU B N     1 
ATOM   7268  C CA    . LEU B  1  423 ? 7.303   52.080  -4.235  1.00 37.36 ? 423  LEU B CA    1 
ATOM   7269  C C     . LEU B  1  423 ? 7.644   50.686  -3.743  1.00 36.66 ? 423  LEU B C     1 
ATOM   7270  O O     . LEU B  1  423 ? 8.679   50.495  -3.105  1.00 37.28 ? 423  LEU B O     1 
ATOM   7271  C CB    . LEU B  1  423 ? 7.776   52.313  -5.681  1.00 37.71 ? 423  LEU B CB    1 
ATOM   7272  C CG    . LEU B  1  423 ? 7.227   53.622  -6.299  1.00 38.15 ? 423  LEU B CG    1 
ATOM   7273  C CD1   . LEU B  1  423 ? 7.508   53.663  -7.788  1.00 38.00 ? 423  LEU B CD1   1 
ATOM   7274  C CD2   . LEU B  1  423 ? 5.711   53.738  -6.082  1.00 38.10 ? 423  LEU B CD2   1 
ATOM   7275  N N     . PRO B  1  424 ? 6.789   49.690  -4.036  1.00 36.00 ? 424  PRO B N     1 
ATOM   7276  C CA    . PRO B  1  424 ? 7.105   48.343  -3.545  1.00 35.06 ? 424  PRO B CA    1 
ATOM   7277  C C     . PRO B  1  424 ? 8.317   47.621  -4.106  1.00 34.24 ? 424  PRO B C     1 
ATOM   7278  O O     . PRO B  1  424 ? 8.568   47.600  -5.315  1.00 33.89 ? 424  PRO B O     1 
ATOM   7279  C CB    . PRO B  1  424 ? 5.827   47.539  -3.814  1.00 34.90 ? 424  PRO B CB    1 
ATOM   7280  C CG    . PRO B  1  424 ? 4.860   48.501  -4.533  1.00 35.49 ? 424  PRO B CG    1 
ATOM   7281  C CD    . PRO B  1  424 ? 5.697   49.655  -5.024  1.00 35.60 ? 424  PRO B CD    1 
ATOM   7282  N N     . GLY B  1  425 ? 9.042   46.980  -3.197  1.00 32.88 ? 425  GLY B N     1 
ATOM   7283  C CA    . GLY B  1  425 ? 10.223  46.214  -3.570  1.00 29.58 ? 425  GLY B CA    1 
ATOM   7284  C C     . GLY B  1  425 ? 11.444  46.874  -4.212  1.00 27.14 ? 425  GLY B C     1 
ATOM   7285  O O     . GLY B  1  425 ? 12.105  47.745  -3.631  1.00 27.67 ? 425  GLY B O     1 
ATOM   7286  N N     . VAL B  1  426 ? 11.771  46.413  -5.417  1.00 23.94 ? 426  VAL B N     1 
ATOM   7287  C CA    . VAL B  1  426 ? 12.922  46.924  -6.156  1.00 21.59 ? 426  VAL B CA    1 
ATOM   7288  C C     . VAL B  1  426 ? 12.571  48.202  -6.904  1.00 21.01 ? 426  VAL B C     1 
ATOM   7289  O O     . VAL B  1  426 ? 13.416  48.794  -7.567  1.00 21.60 ? 426  VAL B O     1 
ATOM   7290  C CB    . VAL B  1  426 ? 13.445  45.874  -7.174  1.00 19.52 ? 426  VAL B CB    1 
ATOM   7291  C CG1   . VAL B  1  426 ? 13.670  44.546  -6.479  1.00 17.84 ? 426  VAL B CG1   1 
ATOM   7292  C CG2   . VAL B  1  426 ? 12.453  45.711  -8.340  1.00 18.67 ? 426  VAL B CG2   1 
ATOM   7293  N N     . GLU B  1  427 ? 11.317  48.624  -6.798  1.00 21.70 ? 427  GLU B N     1 
ATOM   7294  C CA    . GLU B  1  427 ? 10.869  49.841  -7.471  1.00 22.53 ? 427  GLU B CA    1 
ATOM   7295  C C     . GLU B  1  427 ? 11.067  51.088  -6.609  1.00 21.44 ? 427  GLU B C     1 
ATOM   7296  O O     . GLU B  1  427 ? 11.061  51.012  -5.387  1.00 20.73 ? 427  GLU B O     1 
ATOM   7297  C CB    . GLU B  1  427 ? 9.388   49.722  -7.884  1.00 24.92 ? 427  GLU B CB    1 
ATOM   7298  C CG    . GLU B  1  427 ? 9.103   48.634  -8.912  1.00 30.28 ? 427  GLU B CG    1 
ATOM   7299  C CD    . GLU B  1  427 ? 7.669   48.644  -9.399  1.00 33.70 ? 427  GLU B CD    1 
ATOM   7300  O OE1   . GLU B  1  427 ? 7.225   49.695  -9.917  1.00 36.21 ? 427  GLU B OE1   1 
ATOM   7301  O OE2   . GLU B  1  427 ? 6.995   47.598  -9.267  1.00 35.19 ? 427  GLU B OE2   1 
ATOM   7302  N N     . GLY B  1  428 ? 11.249  52.238  -7.251  1.00 19.72 ? 428  GLY B N     1 
ATOM   7303  C CA    . GLY B  1  428 ? 11.442  53.471  -6.505  1.00 18.92 ? 428  GLY B CA    1 
ATOM   7304  C C     . GLY B  1  428 ? 12.813  54.113  -6.612  1.00 17.42 ? 428  GLY B C     1 
ATOM   7305  O O     . GLY B  1  428 ? 13.004  55.239  -6.163  1.00 16.88 ? 428  GLY B O     1 
ATOM   7306  N N     . PHE B  1  429 ? 13.770  53.414  -7.213  1.00 16.91 ? 429  PHE B N     1 
ATOM   7307  C CA    . PHE B  1  429 ? 15.113  53.965  -7.371  1.00 16.65 ? 429  PHE B CA    1 
ATOM   7308  C C     . PHE B  1  429 ? 15.281  54.696  -8.687  1.00 16.39 ? 429  PHE B C     1 
ATOM   7309  O O     . PHE B  1  429 ? 14.524  54.477  -9.628  1.00 17.29 ? 429  PHE B O     1 
ATOM   7310  C CB    . PHE B  1  429 ? 16.185  52.864  -7.332  1.00 15.16 ? 429  PHE B CB    1 
ATOM   7311  C CG    . PHE B  1  429 ? 16.309  52.171  -6.002  1.00 15.50 ? 429  PHE B CG    1 
ATOM   7312  C CD1   . PHE B  1  429 ? 15.611  50.993  -5.748  1.00 14.99 ? 429  PHE B CD1   1 
ATOM   7313  C CD2   . PHE B  1  429 ? 17.158  52.678  -5.019  1.00 14.62 ? 429  PHE B CD2   1 
ATOM   7314  C CE1   . PHE B  1  429 ? 15.749  50.327  -4.525  1.00 13.35 ? 429  PHE B CE1   1 
ATOM   7315  C CE2   . PHE B  1  429 ? 17.312  52.031  -3.791  1.00 14.22 ? 429  PHE B CE2   1 
ATOM   7316  C CZ    . PHE B  1  429 ? 16.606  50.839  -3.543  1.00 12.51 ? 429  PHE B CZ    1 
ATOM   7317  N N     . ASN B  1  430 ? 16.280  55.570  -8.735  1.00 15.95 ? 430  ASN B N     1 
ATOM   7318  C CA    . ASN B  1  430 ? 16.624  56.293  -9.951  1.00 16.82 ? 430  ASN B CA    1 
ATOM   7319  C C     . ASN B  1  430 ? 17.723  55.393  -10.496 1.00 15.91 ? 430  ASN B C     1 
ATOM   7320  O O     . ASN B  1  430 ? 18.873  55.470  -10.059 1.00 15.96 ? 430  ASN B O     1 
ATOM   7321  C CB    . ASN B  1  430 ? 17.181  57.684  -9.621  1.00 17.26 ? 430  ASN B CB    1 
ATOM   7322  C CG    . ASN B  1  430 ? 17.603  58.460  -10.860 1.00 18.71 ? 430  ASN B CG    1 
ATOM   7323  O OD1   . ASN B  1  430 ? 18.026  59.615  -10.766 1.00 20.42 ? 430  ASN B OD1   1 
ATOM   7324  N ND2   . ASN B  1  430 ? 17.494  57.831  -12.025 1.00 18.05 ? 430  ASN B ND2   1 
ATOM   7325  N N     . ILE B  1  431 ? 17.352  54.516  -11.424 1.00 14.82 ? 431  ILE B N     1 
ATOM   7326  C CA    . ILE B  1  431 ? 18.291  53.564  -12.006 1.00 14.09 ? 431  ILE B CA    1 
ATOM   7327  C C     . ILE B  1  431 ? 19.011  54.088  -13.240 1.00 14.75 ? 431  ILE B C     1 
ATOM   7328  O O     . ILE B  1  431 ? 18.393  54.673  -14.131 1.00 15.57 ? 431  ILE B O     1 
ATOM   7329  C CB    . ILE B  1  431 ? 17.566  52.247  -12.407 1.00 14.65 ? 431  ILE B CB    1 
ATOM   7330  C CG1   . ILE B  1  431 ? 16.855  51.642  -11.193 1.00 15.66 ? 431  ILE B CG1   1 
ATOM   7331  C CG2   . ILE B  1  431 ? 18.564  51.251  -13.001 1.00 15.75 ? 431  ILE B CG2   1 
ATOM   7332  C CD1   . ILE B  1  431 ? 17.783  51.203  -10.083 1.00 15.18 ? 431  ILE B CD1   1 
ATOM   7333  N N     . LEU B  1  432 ? 20.322  53.878  -13.277 1.00 13.40 ? 432  LEU B N     1 
ATOM   7334  C CA    . LEU B  1  432 ? 21.137  54.272  -14.420 1.00 13.59 ? 432  LEU B CA    1 
ATOM   7335  C C     . LEU B  1  432 ? 21.425  52.983  -15.182 1.00 14.61 ? 432  LEU B C     1 
ATOM   7336  O O     . LEU B  1  432 ? 22.056  52.074  -14.646 1.00 14.79 ? 432  LEU B O     1 
ATOM   7337  C CB    . LEU B  1  432 ? 22.460  54.890  -13.965 1.00 15.41 ? 432  LEU B CB    1 
ATOM   7338  C CG    . LEU B  1  432 ? 23.431  55.216  -15.102 1.00 16.13 ? 432  LEU B CG    1 
ATOM   7339  C CD1   . LEU B  1  432 ? 22.892  56.399  -15.896 1.00 17.81 ? 432  LEU B CD1   1 
ATOM   7340  C CD2   . LEU B  1  432 ? 24.808  55.540  -14.540 1.00 18.49 ? 432  LEU B CD2   1 
ATOM   7341  N N     . GLY B  1  433 ? 20.965  52.899  -16.424 1.00 14.38 ? 433  GLY B N     1 
ATOM   7342  C CA    . GLY B  1  433 ? 21.195  51.695  -17.202 1.00 13.81 ? 433  GLY B CA    1 
ATOM   7343  C C     . GLY B  1  433 ? 20.011  50.745  -17.164 1.00 13.95 ? 433  GLY B C     1 
ATOM   7344  O O     . GLY B  1  433 ? 18.886  51.155  -16.882 1.00 13.97 ? 433  GLY B O     1 
ATOM   7345  N N     . ILE B  1  434 ? 20.269  49.468  -17.435 1.00 12.85 ? 434  ILE B N     1 
ATOM   7346  C CA    . ILE B  1  434 ? 19.221  48.449  -17.458 1.00 12.82 ? 434  ILE B CA    1 
ATOM   7347  C C     . ILE B  1  434 ? 18.754  48.042  -16.061 1.00 12.11 ? 434  ILE B C     1 
ATOM   7348  O O     . ILE B  1  434 ? 19.545  47.568  -15.248 1.00 11.79 ? 434  ILE B O     1 
ATOM   7349  C CB    . ILE B  1  434 ? 19.705  47.184  -18.200 1.00 13.51 ? 434  ILE B CB    1 
ATOM   7350  C CG1   . ILE B  1  434 ? 20.201  47.565  -19.599 1.00 13.34 ? 434  ILE B CG1   1 
ATOM   7351  C CG2   . ILE B  1  434 ? 18.572  46.160  -18.282 1.00 12.60 ? 434  ILE B CG2   1 
ATOM   7352  C CD1   . ILE B  1  434 ? 20.831  46.423  -20.365 1.00 14.39 ? 434  ILE B CD1   1 
ATOM   7353  N N     . PRO B  1  435 ? 17.453  48.212  -15.770 1.00 11.40 ? 435  PRO B N     1 
ATOM   7354  C CA    . PRO B  1  435 ? 16.918  47.849  -14.456 1.00 11.44 ? 435  PRO B CA    1 
ATOM   7355  C C     . PRO B  1  435 ? 16.589  46.364  -14.351 1.00 10.99 ? 435  PRO B C     1 
ATOM   7356  O O     . PRO B  1  435 ? 16.517  45.664  -15.361 1.00 10.87 ? 435  PRO B O     1 
ATOM   7357  C CB    . PRO B  1  435 ? 15.667  48.709  -14.355 1.00 12.25 ? 435  PRO B CB    1 
ATOM   7358  C CG    . PRO B  1  435 ? 15.158  48.669  -15.761 1.00 12.49 ? 435  PRO B CG    1 
ATOM   7359  C CD    . PRO B  1  435 ? 16.420  48.878  -16.587 1.00 12.36 ? 435  PRO B CD    1 
ATOM   7360  N N     . LEU B  1  436 ? 16.393  45.889  -13.124 1.00 10.68 ? 436  LEU B N     1 
ATOM   7361  C CA    . LEU B  1  436 ? 16.042  44.491  -12.900 1.00 11.06 ? 436  LEU B CA    1 
ATOM   7362  C C     . LEU B  1  436 ? 14.601  44.277  -13.307 1.00 12.04 ? 436  LEU B C     1 
ATOM   7363  O O     . LEU B  1  436 ? 13.813  45.223  -13.361 1.00 13.21 ? 436  LEU B O     1 
ATOM   7364  C CB    . LEU B  1  436 ? 16.131  44.120  -11.417 1.00 11.80 ? 436  LEU B CB    1 
ATOM   7365  C CG    . LEU B  1  436 ? 17.453  43.997  -10.674 1.00 12.81 ? 436  LEU B CG    1 
ATOM   7366  C CD1   . LEU B  1  436 ? 17.152  43.603  -9.229  1.00 13.44 ? 436  LEU B CD1   1 
ATOM   7367  C CD2   . LEU B  1  436 ? 18.340  42.958  -11.341 1.00 12.68 ? 436  LEU B CD2   1 
ATOM   7368  N N     . PRO B  1  437 ? 14.236  43.027  -13.618 1.00 12.36 ? 437  PRO B N     1 
ATOM   7369  C CA    . PRO B  1  437 ? 12.843  42.783  -13.992 1.00 12.63 ? 437  PRO B CA    1 
ATOM   7370  C C     . PRO B  1  437 ? 12.042  43.099  -12.726 1.00 13.59 ? 437  PRO B C     1 
ATOM   7371  O O     . PRO B  1  437 ? 12.543  42.898  -11.621 1.00 14.06 ? 437  PRO B O     1 
ATOM   7372  C CB    . PRO B  1  437 ? 12.834  41.292  -14.310 1.00 12.90 ? 437  PRO B CB    1 
ATOM   7373  C CG    . PRO B  1  437 ? 14.214  41.060  -14.857 1.00 12.63 ? 437  PRO B CG    1 
ATOM   7374  C CD    . PRO B  1  437 ? 15.078  41.848  -13.898 1.00 10.51 ? 437  PRO B CD    1 
ATOM   7375  N N     . LYS B  1  438 ? 10.819  43.596  -12.871 1.00 14.40 ? 438  LYS B N     1 
ATOM   7376  C CA    . LYS B  1  438 ? 10.002  43.922  -11.703 1.00 15.52 ? 438  LYS B CA    1 
ATOM   7377  C C     . LYS B  1  438 ? 9.620   42.677  -10.907 1.00 14.77 ? 438  LYS B C     1 
ATOM   7378  O O     . LYS B  1  438 ? 9.699   42.661  -9.675  1.00 15.42 ? 438  LYS B O     1 
ATOM   7379  C CB    . LYS B  1  438 ? 8.748   44.680  -12.147 1.00 18.59 ? 438  LYS B CB    1 
ATOM   7380  C CG    . LYS B  1  438 ? 9.046   46.070  -12.686 1.00 22.70 ? 438  LYS B CG    1 
ATOM   7381  C CD    . LYS B  1  438 ? 7.858   46.654  -13.437 1.00 26.42 ? 438  LYS B CD    1 
ATOM   7382  C CE    . LYS B  1  438 ? 7.592   45.885  -14.728 1.00 28.52 ? 438  LYS B CE    1 
ATOM   7383  N NZ    . LYS B  1  438 ? 6.490   46.478  -15.536 1.00 31.11 ? 438  LYS B NZ    1 
ATOM   7384  N N     . ASP B  1  439 ? 9.220   41.631  -11.622 1.00 13.82 ? 439  ASP B N     1 
ATOM   7385  C CA    . ASP B  1  439 ? 8.815   40.364  -11.017 1.00 13.88 ? 439  ASP B CA    1 
ATOM   7386  C C     . ASP B  1  439 ? 10.044  39.555  -10.604 1.00 13.54 ? 439  ASP B C     1 
ATOM   7387  O O     . ASP B  1  439 ? 10.760  39.025  -11.453 1.00 13.53 ? 439  ASP B O     1 
ATOM   7388  C CB    . ASP B  1  439 ? 7.976   39.570  -12.026 1.00 13.01 ? 439  ASP B CB    1 
ATOM   7389  C CG    . ASP B  1  439 ? 7.481   38.242  -11.476 1.00 13.97 ? 439  ASP B CG    1 
ATOM   7390  O OD1   . ASP B  1  439 ? 7.913   37.826  -10.378 1.00 11.71 ? 439  ASP B OD1   1 
ATOM   7391  O OD2   . ASP B  1  439 ? 6.651   37.605  -12.162 1.00 13.55 ? 439  ASP B OD2   1 
ATOM   7392  N N     . GLN B  1  440 ? 10.276  39.449  -9.298  1.00 12.68 ? 440  GLN B N     1 
ATOM   7393  C CA    . GLN B  1  440 ? 11.436  38.726  -8.791  1.00 12.17 ? 440  GLN B CA    1 
ATOM   7394  C C     . GLN B  1  440 ? 11.379  37.209  -8.953  1.00 11.68 ? 440  GLN B C     1 
ATOM   7395  O O     . GLN B  1  440 ? 12.339  36.512  -8.615  1.00 13.14 ? 440  GLN B O     1 
ATOM   7396  C CB    . GLN B  1  440 ? 11.679  39.094  -7.324  1.00 12.02 ? 440  GLN B CB    1 
ATOM   7397  C CG    . GLN B  1  440 ? 11.910  40.586  -7.105  1.00 11.96 ? 440  GLN B CG    1 
ATOM   7398  C CD    . GLN B  1  440 ? 13.054  41.136  -7.947  1.00 12.58 ? 440  GLN B CD    1 
ATOM   7399  O OE1   . GLN B  1  440 ? 14.227  40.860  -7.685  1.00 12.40 ? 440  GLN B OE1   1 
ATOM   7400  N NE2   . GLN B  1  440 ? 12.713  41.913  -8.970  1.00 12.84 ? 440  GLN B NE2   1 
ATOM   7401  N N     . THR B  1  441 ? 10.267  36.699  -9.478  1.00 12.28 ? 441  THR B N     1 
ATOM   7402  C CA    . THR B  1  441 ? 10.112  35.261  -9.699  1.00 12.37 ? 441  THR B CA    1 
ATOM   7403  C C     . THR B  1  441 ? 10.133  34.904  -11.188 1.00 12.43 ? 441  THR B C     1 
ATOM   7404  O O     . THR B  1  441 ? 9.981   33.738  -11.548 1.00 14.32 ? 441  THR B O     1 
ATOM   7405  C CB    . THR B  1  441 ? 8.784   34.724  -9.114  1.00 13.27 ? 441  THR B CB    1 
ATOM   7406  O OG1   . THR B  1  441 ? 7.677   35.299  -9.823  1.00 12.41 ? 441  THR B OG1   1 
ATOM   7407  C CG2   . THR B  1  441 ? 8.674   35.059  -7.636  1.00 13.66 ? 441  THR B CG2   1 
ATOM   7408  N N     . ASP B  1  442 ? 10.320  35.904  -12.045 1.00 11.81 ? 442  ASP B N     1 
ATOM   7409  C CA    . ASP B  1  442 ? 10.347  35.688  -13.495 1.00 12.97 ? 442  ASP B CA    1 
ATOM   7410  C C     . ASP B  1  442 ? 11.756  35.318  -13.964 1.00 11.57 ? 442  ASP B C     1 
ATOM   7411  O O     . ASP B  1  442 ? 12.515  36.173  -14.427 1.00 11.38 ? 442  ASP B O     1 
ATOM   7412  C CB    . ASP B  1  442 ? 9.882   36.952  -14.220 1.00 12.83 ? 442  ASP B CB    1 
ATOM   7413  C CG    . ASP B  1  442 ? 9.569   36.706  -15.686 1.00 15.07 ? 442  ASP B CG    1 
ATOM   7414  O OD1   . ASP B  1  442 ? 10.040  35.690  -16.238 1.00 14.88 ? 442  ASP B OD1   1 
ATOM   7415  O OD2   . ASP B  1  442 ? 8.861   37.538  -16.288 1.00 17.28 ? 442  ASP B OD2   1 
ATOM   7416  N N     . ASP B  1  443 ? 12.093  34.038  -13.853 1.00 12.15 ? 443  ASP B N     1 
ATOM   7417  C CA    . ASP B  1  443 ? 13.410  33.548  -14.245 1.00 12.16 ? 443  ASP B CA    1 
ATOM   7418  C C     . ASP B  1  443 ? 13.784  33.871  -15.687 1.00 10.61 ? 443  ASP B C     1 
ATOM   7419  O O     . ASP B  1  443 ? 14.919  34.256  -15.967 1.00 10.70 ? 443  ASP B O     1 
ATOM   7420  C CB    . ASP B  1  443 ? 13.490  32.035  -14.013 1.00 13.73 ? 443  ASP B CB    1 
ATOM   7421  C CG    . ASP B  1  443 ? 13.472  31.670  -12.535 1.00 16.50 ? 443  ASP B CG    1 
ATOM   7422  O OD1   . ASP B  1  443 ? 13.166  32.551  -11.706 1.00 17.03 ? 443  ASP B OD1   1 
ATOM   7423  O OD2   . ASP B  1  443 ? 13.757  30.502  -12.203 1.00 19.85 ? 443  ASP B OD2   1 
ATOM   7424  N N     . ALA B  1  444 ? 12.841  33.715  -16.609 1.00 11.16 ? 444  ALA B N     1 
ATOM   7425  C CA    . ALA B  1  444 ? 13.127  34.006  -18.009 1.00 10.43 ? 444  ALA B CA    1 
ATOM   7426  C C     . ALA B  1  444 ? 13.545  35.460  -18.195 1.00 10.95 ? 444  ALA B C     1 
ATOM   7427  O O     . ALA B  1  444 ? 14.434  35.759  -18.991 1.00 11.02 ? 444  ALA B O     1 
ATOM   7428  C CB    . ALA B  1  444 ? 11.908  33.696  -18.871 1.00 12.06 ? 444  ALA B CB    1 
ATOM   7429  N N     . ALA B  1  445 ? 12.900  36.364  -17.465 1.00 10.29 ? 445  ALA B N     1 
ATOM   7430  C CA    . ALA B  1  445 ? 13.223  37.783  -17.562 1.00 10.32 ? 445  ALA B CA    1 
ATOM   7431  C C     . ALA B  1  445 ? 14.614  38.057  -16.995 1.00 11.15 ? 445  ALA B C     1 
ATOM   7432  O O     . ALA B  1  445 ? 15.356  38.882  -17.532 1.00 10.22 ? 445  ALA B O     1 
ATOM   7433  C CB    . ALA B  1  445 ? 12.181  38.613  -16.825 1.00 11.54 ? 445  ALA B CB    1 
ATOM   7434  N N     . PHE B  1  446 ? 14.963  37.370  -15.909 1.00 10.12 ? 446  PHE B N     1 
ATOM   7435  C CA    . PHE B  1  446 ? 16.282  37.544  -15.306 1.00 9.46  ? 446  PHE B CA    1 
ATOM   7436  C C     . PHE B  1  446 ? 17.372  36.981  -16.217 1.00 9.49  ? 446  PHE B C     1 
ATOM   7437  O O     . PHE B  1  446 ? 18.489  37.491  -16.245 1.00 8.53  ? 446  PHE B O     1 
ATOM   7438  C CB    . PHE B  1  446 ? 16.353  36.874  -13.927 1.00 10.56 ? 446  PHE B CB    1 
ATOM   7439  C CG    . PHE B  1  446 ? 15.885  37.754  -12.799 1.00 9.73  ? 446  PHE B CG    1 
ATOM   7440  C CD1   . PHE B  1  446 ? 14.530  37.978  -12.584 1.00 11.90 ? 446  PHE B CD1   1 
ATOM   7441  C CD2   . PHE B  1  446 ? 16.807  38.378  -11.962 1.00 9.77  ? 446  PHE B CD2   1 
ATOM   7442  C CE1   . PHE B  1  446 ? 14.100  38.813  -11.550 1.00 11.88 ? 446  PHE B CE1   1 
ATOM   7443  C CE2   . PHE B  1  446 ? 16.389  39.213  -10.929 1.00 9.80  ? 446  PHE B CE2   1 
ATOM   7444  C CZ    . PHE B  1  446 ? 15.035  39.432  -10.722 1.00 11.43 ? 446  PHE B CZ    1 
ATOM   7445  N N     . GLU B  1  447 ? 17.057  35.926  -16.961 1.00 9.03  ? 447  GLU B N     1 
ATOM   7446  C CA    . GLU B  1  447 ? 18.042  35.361  -17.873 1.00 9.53  ? 447  GLU B CA    1 
ATOM   7447  C C     . GLU B  1  447 ? 18.352  36.366  -18.967 1.00 10.76 ? 447  GLU B C     1 
ATOM   7448  O O     . GLU B  1  447 ? 19.508  36.556  -19.340 1.00 9.27  ? 447  GLU B O     1 
ATOM   7449  C CB    . GLU B  1  447 ? 17.522  34.052  -18.476 1.00 11.03 ? 447  GLU B CB    1 
ATOM   7450  C CG    . GLU B  1  447 ? 17.667  32.865  -17.544 1.00 13.60 ? 447  GLU B CG    1 
ATOM   7451  C CD    . GLU B  1  447 ? 17.185  31.565  -18.153 1.00 17.22 ? 447  GLU B CD    1 
ATOM   7452  O OE1   . GLU B  1  447 ? 17.131  31.467  -19.396 1.00 19.06 ? 447  GLU B OE1   1 
ATOM   7453  O OE2   . GLU B  1  447 ? 16.877  30.627  -17.387 1.00 17.26 ? 447  GLU B OE2   1 
ATOM   7454  N N     . THR B  1  448 ? 17.315  37.015  -19.485 1.00 11.46 ? 448  THR B N     1 
ATOM   7455  C CA    . THR B  1  448 ? 17.504  38.015  -20.525 1.00 11.50 ? 448  THR B CA    1 
ATOM   7456  C C     . THR B  1  448 ? 18.315  39.181  -19.971 1.00 11.59 ? 448  THR B C     1 
ATOM   7457  O O     . THR B  1  448 ? 19.194  39.716  -20.650 1.00 11.55 ? 448  THR B O     1 
ATOM   7458  C CB    . THR B  1  448 ? 16.151  38.529  -21.054 1.00 13.86 ? 448  THR B CB    1 
ATOM   7459  O OG1   . THR B  1  448 ? 15.468  37.455  -21.710 1.00 15.36 ? 448  THR B OG1   1 
ATOM   7460  C CG2   . THR B  1  448 ? 16.357  39.676  -22.036 1.00 14.55 ? 448  THR B CG2   1 
ATOM   7461  N N     . PHE B  1  449 ? 18.018  39.569  -18.733 1.00 10.79 ? 449  PHE B N     1 
ATOM   7462  C CA    . PHE B  1  449 ? 18.740  40.656  -18.074 1.00 10.02 ? 449  PHE B CA    1 
ATOM   7463  C C     . PHE B  1  449 ? 20.217  40.295  -17.985 1.00 11.25 ? 449  PHE B C     1 
ATOM   7464  O O     . PHE B  1  449 ? 21.089  41.084  -18.349 1.00 9.23  ? 449  PHE B O     1 
ATOM   7465  C CB    . PHE B  1  449 ? 18.204  40.877  -16.655 1.00 11.60 ? 449  PHE B CB    1 
ATOM   7466  C CG    . PHE B  1  449 ? 19.034  41.832  -15.839 1.00 10.94 ? 449  PHE B CG    1 
ATOM   7467  C CD1   . PHE B  1  449 ? 18.808  43.204  -15.902 1.00 11.86 ? 449  PHE B CD1   1 
ATOM   7468  C CD2   . PHE B  1  449 ? 20.076  41.361  -15.042 1.00 9.43  ? 449  PHE B CD2   1 
ATOM   7469  C CE1   . PHE B  1  449 ? 19.610  44.095  -15.184 1.00 11.70 ? 449  PHE B CE1   1 
ATOM   7470  C CE2   . PHE B  1  449 ? 20.884  42.242  -14.323 1.00 9.64  ? 449  PHE B CE2   1 
ATOM   7471  C CZ    . PHE B  1  449 ? 20.653  43.612  -14.393 1.00 9.33  ? 449  PHE B CZ    1 
ATOM   7472  N N     . CYS B  1  450 ? 20.489  39.092  -17.491 1.00 9.93  ? 450  CYS B N     1 
ATOM   7473  C CA    . CYS B  1  450 ? 21.857  38.618  -17.350 1.00 10.11 ? 450  CYS B CA    1 
ATOM   7474  C C     . CYS B  1  450 ? 22.637  38.651  -18.658 1.00 10.92 ? 450  CYS B C     1 
ATOM   7475  O O     . CYS B  1  450 ? 23.748  39.177  -18.720 1.00 11.98 ? 450  CYS B O     1 
ATOM   7476  C CB    . CYS B  1  450 ? 21.853  37.197  -16.776 1.00 9.10  ? 450  CYS B CB    1 
ATOM   7477  S SG    . CYS B  1  450 ? 21.554  37.161  -14.975 1.00 11.15 ? 450  CYS B SG    1 
ATOM   7478  N N     . ARG B  1  451 ? 22.046  38.092  -19.705 1.00 10.54 ? 451  ARG B N     1 
ATOM   7479  C CA    . ARG B  1  451 ? 22.695  38.044  -21.006 1.00 9.73  ? 451  ARG B CA    1 
ATOM   7480  C C     . ARG B  1  451 ? 22.916  39.402  -21.652 1.00 10.55 ? 451  ARG B C     1 
ATOM   7481  O O     . ARG B  1  451 ? 23.990  39.675  -22.181 1.00 11.24 ? 451  ARG B O     1 
ATOM   7482  C CB    . ARG B  1  451 ? 21.886  37.174  -21.977 1.00 9.37  ? 451  ARG B CB    1 
ATOM   7483  C CG    . ARG B  1  451 ? 21.906  35.678  -21.686 1.00 10.54 ? 451  ARG B CG    1 
ATOM   7484  C CD    . ARG B  1  451 ? 21.068  34.938  -22.730 1.00 9.92  ? 451  ARG B CD    1 
ATOM   7485  N NE    . ARG B  1  451 ? 21.052  33.489  -22.546 1.00 10.08 ? 451  ARG B NE    1 
ATOM   7486  C CZ    . ARG B  1  451 ? 22.072  32.681  -22.823 1.00 9.39  ? 451  ARG B CZ    1 
ATOM   7487  N NH1   . ARG B  1  451 ? 23.211  33.174  -23.300 1.00 10.66 ? 451  ARG B NH1   1 
ATOM   7488  N NH2   . ARG B  1  451 ? 21.944  31.372  -22.642 1.00 8.80  ? 451  ARG B NH2   1 
ATOM   7489  N N     . GLU B  1  452 ? 21.909  40.263  -21.598 1.00 10.06 ? 452  GLU B N     1 
ATOM   7490  C CA    . GLU B  1  452 ? 22.000  41.571  -22.238 1.00 11.34 ? 452  GLU B CA    1 
ATOM   7491  C C     . GLU B  1  452 ? 22.708  42.696  -21.499 1.00 11.59 ? 452  GLU B C     1 
ATOM   7492  O O     . GLU B  1  452 ? 23.058  43.709  -22.106 1.00 11.68 ? 452  GLU B O     1 
ATOM   7493  C CB    . GLU B  1  452 ? 20.604  42.059  -22.603 1.00 11.62 ? 452  GLU B CB    1 
ATOM   7494  C CG    . GLU B  1  452 ? 19.807  41.093  -23.434 1.00 17.90 ? 452  GLU B CG    1 
ATOM   7495  C CD    . GLU B  1  452 ? 18.744  41.798  -24.244 1.00 21.81 ? 452  GLU B CD    1 
ATOM   7496  O OE1   . GLU B  1  452 ? 17.944  42.564  -23.657 1.00 20.39 ? 452  GLU B OE1   1 
ATOM   7497  O OE2   . GLU B  1  452 ? 18.716  41.587  -25.476 1.00 22.50 ? 452  GLU B OE2   1 
ATOM   7498  N N     . SER B  1  453 ? 22.928  42.531  -20.200 1.00 9.48  ? 453  SER B N     1 
ATOM   7499  C CA    . SER B  1  453 ? 23.567  43.578  -19.414 1.00 9.13  ? 453  SER B CA    1 
ATOM   7500  C C     . SER B  1  453 ? 24.944  43.207  -18.891 1.00 9.29  ? 453  SER B C     1 
ATOM   7501  O O     . SER B  1  453 ? 25.553  43.984  -18.159 1.00 9.15  ? 453  SER B O     1 
ATOM   7502  C CB    . SER B  1  453 ? 22.679  43.940  -18.220 1.00 9.51  ? 453  SER B CB    1 
ATOM   7503  O OG    . SER B  1  453 ? 22.639  42.875  -17.281 1.00 11.42 ? 453  SER B OG    1 
ATOM   7504  N N     . VAL B  1  454 ? 25.434  42.033  -19.278 1.00 8.16  ? 454  VAL B N     1 
ATOM   7505  C CA    . VAL B  1  454 ? 26.724  41.537  -18.804 1.00 8.34  ? 454  VAL B CA    1 
ATOM   7506  C C     . VAL B  1  454 ? 27.948  42.402  -19.105 1.00 9.16  ? 454  VAL B C     1 
ATOM   7507  O O     . VAL B  1  454 ? 28.023  43.077  -20.131 1.00 9.51  ? 454  VAL B O     1 
ATOM   7508  C CB    . VAL B  1  454 ? 26.981  40.094  -19.332 1.00 8.37  ? 454  VAL B CB    1 
ATOM   7509  C CG1   . VAL B  1  454 ? 27.308  40.123  -20.825 1.00 9.10  ? 454  VAL B CG1   1 
ATOM   7510  C CG2   . VAL B  1  454 ? 28.101  39.435  -18.537 1.00 9.66  ? 454  VAL B CG2   1 
ATOM   7511  N N     . ALA B  1  455 ? 28.898  42.377  -18.176 1.00 8.62  ? 455  ALA B N     1 
ATOM   7512  C CA    . ALA B  1  455 ? 30.154  43.104  -18.296 1.00 7.82  ? 455  ALA B CA    1 
ATOM   7513  C C     . ALA B  1  455 ? 31.223  42.177  -17.729 1.00 8.44  ? 455  ALA B C     1 
ATOM   7514  O O     . ALA B  1  455 ? 30.910  41.087  -17.263 1.00 8.44  ? 455  ALA B O     1 
ATOM   7515  C CB    . ALA B  1  455 ? 30.101  44.398  -17.490 1.00 9.94  ? 455  ALA B CB    1 
ATOM   7516  N N     . SER B  1  456 ? 32.480  42.593  -17.782 1.00 6.98  ? 456  SER B N     1 
ATOM   7517  C CA    . SER B  1  456 ? 33.546  41.769  -17.230 1.00 7.53  ? 456  SER B CA    1 
ATOM   7518  C C     . SER B  1  456 ? 33.851  42.217  -15.807 1.00 8.09  ? 456  SER B C     1 
ATOM   7519  O O     . SER B  1  456 ? 33.730  43.396  -15.486 1.00 9.82  ? 456  SER B O     1 
ATOM   7520  C CB    . SER B  1  456 ? 34.814  41.888  -18.076 1.00 8.45  ? 456  SER B CB    1 
ATOM   7521  O OG    . SER B  1  456 ? 35.905  41.251  -17.431 1.00 8.81  ? 456  SER B OG    1 
ATOM   7522  N N     . TYR B  1  457 ? 34.239  41.275  -14.953 1.00 9.20  ? 457  TYR B N     1 
ATOM   7523  C CA    . TYR B  1  457 ? 34.588  41.619  -13.581 1.00 9.97  ? 457  TYR B CA    1 
ATOM   7524  C C     . TYR B  1  457 ? 36.090  41.912  -13.543 1.00 9.89  ? 457  TYR B C     1 
ATOM   7525  O O     . TYR B  1  457 ? 36.636  42.277  -12.502 1.00 9.80  ? 457  TYR B O     1 
ATOM   7526  C CB    . TYR B  1  457 ? 34.256  40.470  -12.619 1.00 11.26 ? 457  TYR B CB    1 
ATOM   7527  C CG    . TYR B  1  457 ? 33.797  40.965  -11.268 1.00 14.62 ? 457  TYR B CG    1 
ATOM   7528  C CD1   . TYR B  1  457 ? 32.441  41.151  -10.995 1.00 13.73 ? 457  TYR B CD1   1 
ATOM   7529  C CD2   . TYR B  1  457 ? 34.720  41.337  -10.292 1.00 15.87 ? 457  TYR B CD2   1 
ATOM   7530  C CE1   . TYR B  1  457 ? 32.015  41.704  -9.787  1.00 16.71 ? 457  TYR B CE1   1 
ATOM   7531  C CE2   . TYR B  1  457 ? 34.306  41.889  -9.083  1.00 18.14 ? 457  TYR B CE2   1 
ATOM   7532  C CZ    . TYR B  1  457 ? 32.954  42.072  -8.840  1.00 17.72 ? 457  TYR B CZ    1 
ATOM   7533  O OH    . TYR B  1  457 ? 32.546  42.644  -7.659  1.00 22.26 ? 457  TYR B OH    1 
ATOM   7534  N N     . TRP B  1  458 ? 36.736  41.749  -14.698 1.00 8.67  ? 458  TRP B N     1 
ATOM   7535  C CA    . TRP B  1  458 ? 38.170  41.986  -14.881 1.00 9.09  ? 458  TRP B CA    1 
ATOM   7536  C C     . TRP B  1  458 ? 39.043  40.940  -14.194 1.00 8.46  ? 458  TRP B C     1 
ATOM   7537  O O     . TRP B  1  458 ? 40.252  41.130  -14.050 1.00 8.22  ? 458  TRP B O     1 
ATOM   7538  C CB    . TRP B  1  458 ? 38.567  43.369  -14.359 1.00 10.75 ? 458  TRP B CB    1 
ATOM   7539  C CG    . TRP B  1  458 ? 37.663  44.494  -14.775 1.00 12.91 ? 458  TRP B CG    1 
ATOM   7540  C CD1   . TRP B  1  458 ? 37.313  44.846  -16.048 1.00 14.36 ? 458  TRP B CD1   1 
ATOM   7541  C CD2   . TRP B  1  458 ? 37.020  45.435  -13.906 1.00 14.35 ? 458  TRP B CD2   1 
ATOM   7542  N NE1   . TRP B  1  458 ? 36.492  45.952  -16.024 1.00 14.88 ? 458  TRP B NE1   1 
ATOM   7543  C CE2   . TRP B  1  458 ? 36.298  46.333  -14.722 1.00 15.77 ? 458  TRP B CE2   1 
ATOM   7544  C CE3   . TRP B  1  458 ? 36.985  45.609  -12.515 1.00 14.53 ? 458  TRP B CE3   1 
ATOM   7545  C CZ2   . TRP B  1  458 ? 35.549  47.391  -14.193 1.00 15.59 ? 458  TRP B CZ2   1 
ATOM   7546  C CZ3   . TRP B  1  458 ? 36.239  46.662  -11.989 1.00 17.32 ? 458  TRP B CZ3   1 
ATOM   7547  C CH2   . TRP B  1  458 ? 35.532  47.538  -12.830 1.00 16.85 ? 458  TRP B CH2   1 
ATOM   7548  N N     . HIS B  1  459 ? 38.434  39.838  -13.776 1.00 7.56  ? 459  HIS B N     1 
ATOM   7549  C CA    . HIS B  1  459 ? 39.169  38.784  -13.092 1.00 6.89  ? 459  HIS B CA    1 
ATOM   7550  C C     . HIS B  1  459 ? 39.439  37.590  -14.000 1.00 8.40  ? 459  HIS B C     1 
ATOM   7551  O O     . HIS B  1  459 ? 39.542  36.455  -13.528 1.00 9.31  ? 459  HIS B O     1 
ATOM   7552  C CB    . HIS B  1  459 ? 38.400  38.339  -11.840 1.00 7.44  ? 459  HIS B CB    1 
ATOM   7553  C CG    . HIS B  1  459 ? 38.246  39.417  -10.807 1.00 6.11  ? 459  HIS B CG    1 
ATOM   7554  N ND1   . HIS B  1  459 ? 37.616  39.207  -9.601  1.00 7.24  ? 459  HIS B ND1   1 
ATOM   7555  C CD2   . HIS B  1  459 ? 38.637  40.714  -10.808 1.00 7.04  ? 459  HIS B CD2   1 
ATOM   7556  C CE1   . HIS B  1  459 ? 37.623  40.329  -8.901  1.00 6.61  ? 459  HIS B CE1   1 
ATOM   7557  N NE2   . HIS B  1  459 ? 38.236  41.258  -9.610  1.00 6.26  ? 459  HIS B NE2   1 
ATOM   7558  N N     . TYR B  1  460 ? 39.556  37.851  -15.301 1.00 7.60  ? 460  TYR B N     1 
ATOM   7559  C CA    . TYR B  1  460 ? 39.834  36.793  -16.270 1.00 7.42  ? 460  TYR B CA    1 
ATOM   7560  C C     . TYR B  1  460 ? 41.107  36.059  -15.863 1.00 7.51  ? 460  TYR B C     1 
ATOM   7561  O O     . TYR B  1  460 ? 41.994  36.628  -15.220 1.00 8.01  ? 460  TYR B O     1 
ATOM   7562  C CB    . TYR B  1  460 ? 39.961  37.379  -17.682 1.00 6.94  ? 460  TYR B CB    1 
ATOM   7563  C CG    . TYR B  1  460 ? 40.788  38.641  -17.744 1.00 6.46  ? 460  TYR B CG    1 
ATOM   7564  C CD1   . TYR B  1  460 ? 42.180  38.580  -17.774 1.00 6.89  ? 460  TYR B CD1   1 
ATOM   7565  C CD2   . TYR B  1  460 ? 40.180  39.900  -17.705 1.00 7.87  ? 460  TYR B CD2   1 
ATOM   7566  C CE1   . TYR B  1  460 ? 42.953  39.741  -17.759 1.00 8.32  ? 460  TYR B CE1   1 
ATOM   7567  C CE2   . TYR B  1  460 ? 40.943  41.067  -17.688 1.00 7.96  ? 460  TYR B CE2   1 
ATOM   7568  C CZ    . TYR B  1  460 ? 42.328  40.978  -17.710 1.00 9.47  ? 460  TYR B CZ    1 
ATOM   7569  O OH    . TYR B  1  460 ? 43.095  42.119  -17.633 1.00 10.31 ? 460  TYR B OH    1 
ATOM   7570  N N     . HIS B  1  461 ? 41.182  34.787  -16.238 1.00 7.14  ? 461  HIS B N     1 
ATOM   7571  C CA    . HIS B  1  461 ? 42.308  33.934  -15.885 1.00 8.08  ? 461  HIS B CA    1 
ATOM   7572  C C     . HIS B  1  461 ? 42.329  32.728  -16.815 1.00 8.23  ? 461  HIS B C     1 
ATOM   7573  O O     . HIS B  1  461 ? 41.441  32.569  -17.653 1.00 7.72  ? 461  HIS B O     1 
ATOM   7574  C CB    . HIS B  1  461 ? 42.148  33.452  -14.441 1.00 7.12  ? 461  HIS B CB    1 
ATOM   7575  C CG    . HIS B  1  461 ? 40.800  32.862  -14.158 1.00 8.06  ? 461  HIS B CG    1 
ATOM   7576  N ND1   . HIS B  1  461 ? 39.679  33.634  -13.940 1.00 8.30  ? 461  HIS B ND1   1 
ATOM   7577  C CD2   . HIS B  1  461 ? 40.382  31.574  -14.120 1.00 8.54  ? 461  HIS B CD2   1 
ATOM   7578  C CE1   . HIS B  1  461 ? 38.628  32.847  -13.782 1.00 8.29  ? 461  HIS B CE1   1 
ATOM   7579  N NE2   . HIS B  1  461 ? 39.028  31.593  -13.886 1.00 7.67  ? 461  HIS B NE2   1 
ATOM   7580  N N     . GLY B  1  462 ? 43.336  31.874  -16.650 1.00 8.19  ? 462  GLY B N     1 
ATOM   7581  C CA    . GLY B  1  462 ? 43.452  30.691  -17.488 1.00 8.68  ? 462  GLY B CA    1 
ATOM   7582  C C     . GLY B  1  462 ? 44.293  30.935  -18.728 1.00 8.36  ? 462  GLY B C     1 
ATOM   7583  O O     . GLY B  1  462 ? 44.909  31.991  -18.869 1.00 9.00  ? 462  GLY B O     1 
ATOM   7584  N N     . GLY B  1  463 ? 44.328  29.955  -19.626 1.00 8.33  ? 463  GLY B N     1 
ATOM   7585  C CA    . GLY B  1  463 ? 45.104  30.097  -20.848 1.00 7.60  ? 463  GLY B CA    1 
ATOM   7586  C C     . GLY B  1  463 ? 46.402  29.310  -20.875 1.00 9.38  ? 463  GLY B C     1 
ATOM   7587  O O     . GLY B  1  463 ? 47.006  29.129  -21.934 1.00 10.50 ? 463  GLY B O     1 
ATOM   7588  N N     . CYS B  1  464 ? 46.842  28.846  -19.710 1.00 8.44  ? 464  CYS B N     1 
ATOM   7589  C CA    . CYS B  1  464 ? 48.076  28.069  -19.600 1.00 9.28  ? 464  CYS B CA    1 
ATOM   7590  C C     . CYS B  1  464 ? 47.929  27.257  -18.318 1.00 8.84  ? 464  CYS B C     1 
ATOM   7591  O O     . CYS B  1  464 ? 48.715  27.389  -17.378 1.00 9.26  ? 464  CYS B O     1 
ATOM   7592  C CB    . CYS B  1  464 ? 49.272  29.014  -19.499 1.00 9.73  ? 464  CYS B CB    1 
ATOM   7593  S SG    . CYS B  1  464 ? 50.855  28.205  -19.719 1.00 11.31 ? 464  CYS B SG    1 
ATOM   7594  N N     . LEU B  1  465 ? 46.913  26.402  -18.313 1.00 10.46 ? 465  LEU B N     1 
ATOM   7595  C CA    . LEU B  1  465 ? 46.552  25.599  -17.150 1.00 10.11 ? 465  LEU B CA    1 
ATOM   7596  C C     . LEU B  1  465 ? 47.470  24.494  -16.655 1.00 10.73 ? 465  LEU B C     1 
ATOM   7597  O O     . LEU B  1  465 ? 48.113  23.789  -17.432 1.00 9.36  ? 465  LEU B O     1 
ATOM   7598  C CB    . LEU B  1  465 ? 45.171  24.971  -17.369 1.00 9.92  ? 465  LEU B CB    1 
ATOM   7599  C CG    . LEU B  1  465 ? 43.986  25.846  -17.781 1.00 11.58 ? 465  LEU B CG    1 
ATOM   7600  C CD1   . LEU B  1  465 ? 42.724  24.999  -17.729 1.00 11.10 ? 465  LEU B CD1   1 
ATOM   7601  C CD2   . LEU B  1  465 ? 43.858  27.046  -16.860 1.00 12.38 ? 465  LEU B CD2   1 
ATOM   7602  N N     . VAL B  1  466 ? 47.506  24.355  -15.335 1.00 10.05 ? 466  VAL B N     1 
ATOM   7603  C CA    . VAL B  1  466 ? 48.259  23.288  -14.706 1.00 9.50  ? 466  VAL B CA    1 
ATOM   7604  C C     . VAL B  1  466 ? 47.464  22.055  -15.137 1.00 9.74  ? 466  VAL B C     1 
ATOM   7605  O O     . VAL B  1  466 ? 46.234  22.040  -15.043 1.00 11.64 ? 466  VAL B O     1 
ATOM   7606  C CB    . VAL B  1  466 ? 48.227  23.408  -13.162 1.00 10.33 ? 466  VAL B CB    1 
ATOM   7607  C CG1   . VAL B  1  466 ? 48.661  22.097  -12.523 1.00 10.34 ? 466  VAL B CG1   1 
ATOM   7608  C CG2   . VAL B  1  466 ? 49.147  24.531  -12.715 1.00 8.68  ? 466  VAL B CG2   1 
ATOM   7609  N N     . GLY B  1  467 ? 48.156  21.039  -15.635 1.00 10.81 ? 467  GLY B N     1 
ATOM   7610  C CA    . GLY B  1  467 ? 47.470  19.839  -16.077 1.00 11.19 ? 467  GLY B CA    1 
ATOM   7611  C C     . GLY B  1  467 ? 47.143  19.837  -17.560 1.00 11.41 ? 467  GLY B C     1 
ATOM   7612  O O     . GLY B  1  467 ? 46.751  18.806  -18.112 1.00 12.44 ? 467  GLY B O     1 
ATOM   7613  N N     . LYS B  1  468 ? 47.290  20.992  -18.204 1.00 12.39 ? 468  LYS B N     1 
ATOM   7614  C CA    . LYS B  1  468 ? 47.026  21.127  -19.637 1.00 11.41 ? 468  LYS B CA    1 
ATOM   7615  C C     . LYS B  1  468 ? 48.309  21.549  -20.350 1.00 11.58 ? 468  LYS B C     1 
ATOM   7616  O O     . LYS B  1  468 ? 48.653  21.010  -21.404 1.00 12.05 ? 468  LYS B O     1 
ATOM   7617  C CB    . LYS B  1  468 ? 45.936  22.172  -19.890 1.00 12.83 ? 468  LYS B CB    1 
ATOM   7618  C CG    . LYS B  1  468 ? 44.585  21.841  -19.279 1.00 14.17 ? 468  LYS B CG    1 
ATOM   7619  C CD    . LYS B  1  468 ? 43.932  20.655  -19.960 1.00 18.42 ? 468  LYS B CD    1 
ATOM   7620  C CE    . LYS B  1  468 ? 42.592  20.341  -19.312 1.00 20.71 ? 468  LYS B CE    1 
ATOM   7621  N NZ    . LYS B  1  468 ? 41.888  19.223  -19.992 1.00 24.08 ? 468  LYS B NZ    1 
ATOM   7622  N N     . VAL B  1  469 ? 49.007  22.525  -19.774 1.00 11.45 ? 469  VAL B N     1 
ATOM   7623  C CA    . VAL B  1  469 ? 50.259  23.016  -20.336 1.00 10.35 ? 469  VAL B CA    1 
ATOM   7624  C C     . VAL B  1  469 ? 51.391  22.874  -19.318 1.00 9.52  ? 469  VAL B C     1 
ATOM   7625  O O     . VAL B  1  469 ? 52.535  22.603  -19.684 1.00 11.12 ? 469  VAL B O     1 
ATOM   7626  C CB    . VAL B  1  469 ? 50.157  24.514  -20.734 1.00 10.40 ? 469  VAL B CB    1 
ATOM   7627  C CG1   . VAL B  1  469 ? 51.460  24.972  -21.383 1.00 10.88 ? 469  VAL B CG1   1 
ATOM   7628  C CG2   . VAL B  1  469 ? 48.988  24.728  -21.687 1.00 11.08 ? 469  VAL B CG2   1 
ATOM   7629  N N     . LEU B  1  470 ? 51.062  23.056  -18.043 1.00 9.68  ? 470  LEU B N     1 
ATOM   7630  C CA    . LEU B  1  470 ? 52.049  22.983  -16.965 1.00 9.20  ? 470  LEU B CA    1 
ATOM   7631  C C     . LEU B  1  470 ? 51.872  21.762  -16.072 1.00 9.98  ? 470  LEU B C     1 
ATOM   7632  O O     . LEU B  1  470 ? 50.813  21.139  -16.063 1.00 10.67 ? 470  LEU B O     1 
ATOM   7633  C CB    . LEU B  1  470 ? 51.940  24.227  -16.075 1.00 9.84  ? 470  LEU B CB    1 
ATOM   7634  C CG    . LEU B  1  470 ? 51.853  25.604  -16.734 1.00 8.90  ? 470  LEU B CG    1 
ATOM   7635  C CD1   . LEU B  1  470 ? 51.565  26.656  -15.666 1.00 9.08  ? 470  LEU B CD1   1 
ATOM   7636  C CD2   . LEU B  1  470 ? 53.149  25.908  -17.461 1.00 8.19  ? 470  LEU B CD2   1 
ATOM   7637  N N     . ASP B  1  471 ? 52.914  21.430  -15.314 1.00 11.14 ? 471  ASP B N     1 
ATOM   7638  C CA    . ASP B  1  471 ? 52.835  20.315  -14.385 1.00 11.77 ? 471  ASP B CA    1 
ATOM   7639  C C     . ASP B  1  471 ? 52.576  20.903  -12.999 1.00 12.77 ? 471  ASP B C     1 
ATOM   7640  O O     . ASP B  1  471 ? 52.385  22.114  -12.865 1.00 11.15 ? 471  ASP B O     1 
ATOM   7641  C CB    . ASP B  1  471 ? 54.125  19.464  -14.424 1.00 12.89 ? 471  ASP B CB    1 
ATOM   7642  C CG    . ASP B  1  471 ? 55.351  20.184  -13.877 1.00 15.15 ? 471  ASP B CG    1 
ATOM   7643  O OD1   . ASP B  1  471 ? 56.462  19.611  -13.983 1.00 16.14 ? 471  ASP B OD1   1 
ATOM   7644  O OD2   . ASP B  1  471 ? 55.226  21.305  -13.342 1.00 15.41 ? 471  ASP B OD2   1 
ATOM   7645  N N     . GLY B  1  472 ? 52.552  20.052  -11.979 1.00 11.56 ? 472  GLY B N     1 
ATOM   7646  C CA    . GLY B  1  472 ? 52.299  20.508  -10.620 1.00 12.93 ? 472  GLY B CA    1 
ATOM   7647  C C     . GLY B  1  472 ? 53.324  21.434  -9.988  1.00 11.91 ? 472  GLY B C     1 
ATOM   7648  O O     . GLY B  1  472 ? 53.095  21.960  -8.896  1.00 13.23 ? 472  GLY B O     1 
ATOM   7649  N N     . ASP B  1  473 ? 54.448  21.645  -10.663 1.00 12.27 ? 473  ASP B N     1 
ATOM   7650  C CA    . ASP B  1  473 ? 55.501  22.525  -10.166 1.00 12.47 ? 473  ASP B CA    1 
ATOM   7651  C C     . ASP B  1  473 ? 55.573  23.761  -11.060 1.00 11.53 ? 473  ASP B C     1 
ATOM   7652  O O     . ASP B  1  473 ? 56.529  24.532  -11.015 1.00 11.10 ? 473  ASP B O     1 
ATOM   7653  C CB    . ASP B  1  473 ? 56.842  21.782  -10.161 1.00 17.13 ? 473  ASP B CB    1 
ATOM   7654  C CG    . ASP B  1  473 ? 56.818  20.548  -9.281  1.00 18.88 ? 473  ASP B CG    1 
ATOM   7655  O OD1   . ASP B  1  473 ? 56.527  20.677  -8.073  1.00 22.41 ? 473  ASP B OD1   1 
ATOM   7656  O OD2   . ASP B  1  473 ? 57.107  19.451  -9.802  1.00 22.40 ? 473  ASP B OD2   1 
ATOM   7657  N N     . PHE B  1  474 ? 54.539  23.919  -11.881 1.00 10.62 ? 474  PHE B N     1 
ATOM   7658  C CA    . PHE B  1  474 ? 54.388  25.033  -12.813 1.00 9.49  ? 474  PHE B CA    1 
ATOM   7659  C C     . PHE B  1  474 ? 55.367  25.058  -13.989 1.00 8.97  ? 474  PHE B C     1 
ATOM   7660  O O     . PHE B  1  474 ? 55.535  26.086  -14.652 1.00 8.74  ? 474  PHE B O     1 
ATOM   7661  C CB    . PHE B  1  474 ? 54.428  26.371  -12.059 1.00 9.99  ? 474  PHE B CB    1 
ATOM   7662  C CG    . PHE B  1  474 ? 53.306  26.538  -11.067 1.00 8.92  ? 474  PHE B CG    1 
ATOM   7663  C CD1   . PHE B  1  474 ? 53.414  26.019  -9.777  1.00 8.78  ? 474  PHE B CD1   1 
ATOM   7664  C CD2   . PHE B  1  474 ? 52.108  27.149  -11.443 1.00 8.57  ? 474  PHE B CD2   1 
ATOM   7665  C CE1   . PHE B  1  474 ? 52.343  26.099  -8.876  1.00 8.22  ? 474  PHE B CE1   1 
ATOM   7666  C CE2   . PHE B  1  474 ? 51.034  27.233  -10.550 1.00 9.37  ? 474  PHE B CE2   1 
ATOM   7667  C CZ    . PHE B  1  474 ? 51.153  26.705  -9.266  1.00 8.62  ? 474  PHE B CZ    1 
ATOM   7668  N N     . ARG B  1  475 ? 56.002  23.924  -14.261 1.00 9.04  ? 475  ARG B N     1 
ATOM   7669  C CA    . ARG B  1  475 ? 56.928  23.851  -15.382 1.00 9.51  ? 475  ARG B CA    1 
ATOM   7670  C C     . ARG B  1  475 ? 56.129  23.591  -16.653 1.00 9.10  ? 475  ARG B C     1 
ATOM   7671  O O     . ARG B  1  475 ? 55.113  22.895  -16.618 1.00 9.56  ? 475  ARG B O     1 
ATOM   7672  C CB    . ARG B  1  475 ? 57.920  22.691  -15.210 1.00 10.30 ? 475  ARG B CB    1 
ATOM   7673  C CG    . ARG B  1  475 ? 58.762  22.704  -13.949 1.00 12.76 ? 475  ARG B CG    1 
ATOM   7674  C CD    . ARG B  1  475 ? 59.858  21.638  -14.038 1.00 13.85 ? 475  ARG B CD    1 
ATOM   7675  N NE    A ARG B  1  475 ? 60.478  21.364  -12.743 0.50 12.93 ? 475  ARG B NE    1 
ATOM   7676  N NE    B ARG B  1  475 ? 61.153  22.180  -13.581 0.50 13.59 ? 475  ARG B NE    1 
ATOM   7677  C CZ    A ARG B  1  475 ? 59.938  20.592  -11.805 0.50 13.15 ? 475  ARG B CZ    1 
ATOM   7678  C CZ    B ARG B  1  475 ? 61.757  21.799  -12.460 0.50 14.09 ? 475  ARG B CZ    1 
ATOM   7679  N NH1   A ARG B  1  475 ? 58.764  20.008  -12.013 0.50 11.13 ? 475  ARG B NH1   1 
ATOM   7680  N NH1   B ARG B  1  475 ? 61.192  20.891  -11.671 0.50 12.10 ? 475  ARG B NH1   1 
ATOM   7681  N NH2   A ARG B  1  475 ? 60.569  20.405  -10.656 0.50 14.21 ? 475  ARG B NH2   1 
ATOM   7682  N NH2   B ARG B  1  475 ? 62.926  22.326  -12.124 0.50 15.08 ? 475  ARG B NH2   1 
ATOM   7683  N N     . VAL B  1  476 ? 56.577  24.159  -17.768 1.00 9.90  ? 476  VAL B N     1 
ATOM   7684  C CA    . VAL B  1  476 ? 55.921  23.911  -19.048 1.00 9.97  ? 476  VAL B CA    1 
ATOM   7685  C C     . VAL B  1  476 ? 56.405  22.504  -19.408 1.00 11.11 ? 476  VAL B C     1 
ATOM   7686  O O     . VAL B  1  476 ? 57.610  22.264  -19.497 1.00 12.36 ? 476  VAL B O     1 
ATOM   7687  C CB    . VAL B  1  476 ? 56.381  24.916  -20.129 1.00 10.51 ? 476  VAL B CB    1 
ATOM   7688  C CG1   . VAL B  1  476 ? 55.879  24.483  -21.500 1.00 10.74 ? 476  VAL B CG1   1 
ATOM   7689  C CG2   . VAL B  1  476 ? 55.854  26.310  -19.794 1.00 9.15  ? 476  VAL B CG2   1 
ATOM   7690  N N     . THR B  1  477 ? 55.476  21.574  -19.595 1.00 11.29 ? 477  THR B N     1 
ATOM   7691  C CA    . THR B  1  477 ? 55.855  20.198  -19.910 1.00 13.92 ? 477  THR B CA    1 
ATOM   7692  C C     . THR B  1  477 ? 56.633  20.088  -21.219 1.00 14.24 ? 477  THR B C     1 
ATOM   7693  O O     . THR B  1  477 ? 56.399  20.847  -22.157 1.00 15.35 ? 477  THR B O     1 
ATOM   7694  C CB    . THR B  1  477 ? 54.621  19.288  -19.998 1.00 14.78 ? 477  THR B CB    1 
ATOM   7695  O OG1   . THR B  1  477 ? 53.781  19.730  -21.067 1.00 17.75 ? 477  THR B OG1   1 
ATOM   7696  C CG2   . THR B  1  477 ? 53.836  19.320  -18.691 1.00 14.02 ? 477  THR B CG2   1 
ATOM   7697  N N     . GLY B  1  478 ? 57.569  19.143  -21.264 1.00 14.58 ? 478  GLY B N     1 
ATOM   7698  C CA    . GLY B  1  478 ? 58.366  18.931  -22.460 1.00 13.64 ? 478  GLY B CA    1 
ATOM   7699  C C     . GLY B  1  478 ? 59.523  19.892  -22.655 1.00 15.34 ? 478  GLY B C     1 
ATOM   7700  O O     . GLY B  1  478 ? 60.322  19.725  -23.578 1.00 15.31 ? 478  GLY B O     1 
ATOM   7701  N N     . ILE B  1  479 ? 59.628  20.893  -21.786 1.00 14.19 ? 479  ILE B N     1 
ATOM   7702  C CA    . ILE B  1  479 ? 60.693  21.883  -21.891 1.00 14.68 ? 479  ILE B CA    1 
ATOM   7703  C C     . ILE B  1  479 ? 61.344  22.133  -20.533 1.00 14.32 ? 479  ILE B C     1 
ATOM   7704  O O     . ILE B  1  479 ? 60.651  22.246  -19.527 1.00 14.72 ? 479  ILE B O     1 
ATOM   7705  C CB    . ILE B  1  479 ? 60.134  23.222  -22.424 1.00 14.47 ? 479  ILE B CB    1 
ATOM   7706  C CG1   . ILE B  1  479 ? 59.433  22.989  -23.764 1.00 14.97 ? 479  ILE B CG1   1 
ATOM   7707  C CG2   . ILE B  1  479 ? 61.256  24.237  -22.573 1.00 15.27 ? 479  ILE B CG2   1 
ATOM   7708  C CD1   . ILE B  1  479 ? 58.730  24.209  -24.313 1.00 15.54 ? 479  ILE B CD1   1 
ATOM   7709  N N     . ASN B  1  480 ? 62.672  22.215  -20.507 1.00 14.70 ? 480  ASN B N     1 
ATOM   7710  C CA    . ASN B  1  480 ? 63.395  22.471  -19.262 1.00 13.60 ? 480  ASN B CA    1 
ATOM   7711  C C     . ASN B  1  480 ? 63.641  23.958  -19.058 1.00 13.15 ? 480  ASN B C     1 
ATOM   7712  O O     . ASN B  1  480 ? 63.631  24.731  -20.012 1.00 12.89 ? 480  ASN B O     1 
ATOM   7713  C CB    . ASN B  1  480 ? 64.754  21.763  -19.254 1.00 17.22 ? 480  ASN B CB    1 
ATOM   7714  C CG    . ASN B  1  480 ? 64.640  20.276  -19.454 1.00 17.74 ? 480  ASN B CG    1 
ATOM   7715  O OD1   . ASN B  1  480 ? 63.726  19.637  -18.940 1.00 20.89 ? 480  ASN B OD1   1 
ATOM   7716  N ND2   . ASN B  1  480 ? 65.589  19.706  -20.187 1.00 22.17 ? 480  ASN B ND2   1 
ATOM   7717  N N     . ALA B  1  481 ? 63.875  24.341  -17.806 1.00 11.62 ? 481  ALA B N     1 
ATOM   7718  C CA    . ALA B  1  481 ? 64.165  25.725  -17.437 1.00 11.65 ? 481  ALA B CA    1 
ATOM   7719  C C     . ALA B  1  481 ? 63.114  26.741  -17.873 1.00 10.65 ? 481  ALA B C     1 
ATOM   7720  O O     . ALA B  1  481 ? 63.442  27.895  -18.161 1.00 10.73 ? 481  ALA B O     1 
ATOM   7721  C CB    . ALA B  1  481 ? 65.532  26.130  -17.982 1.00 14.26 ? 481  ALA B CB    1 
ATOM   7722  N N     . LEU B  1  482 ? 61.855  26.316  -17.904 1.00 10.67 ? 482  LEU B N     1 
ATOM   7723  C CA    . LEU B  1  482 ? 60.765  27.204  -18.295 1.00 11.12 ? 482  LEU B CA    1 
ATOM   7724  C C     . LEU B  1  482 ? 59.526  26.962  -17.441 1.00 9.92  ? 482  LEU B C     1 
ATOM   7725  O O     . LEU B  1  482 ? 59.005  25.848  -17.389 1.00 11.39 ? 482  LEU B O     1 
ATOM   7726  C CB    . LEU B  1  482 ? 60.405  26.997  -19.768 1.00 10.87 ? 482  LEU B CB    1 
ATOM   7727  C CG    . LEU B  1  482 ? 59.276  27.889  -20.295 1.00 10.64 ? 482  LEU B CG    1 
ATOM   7728  C CD1   . LEU B  1  482 ? 59.719  29.344  -20.252 1.00 11.25 ? 482  LEU B CD1   1 
ATOM   7729  C CD2   . LEU B  1  482 ? 58.914  27.488  -21.720 1.00 11.02 ? 482  LEU B CD2   1 
ATOM   7730  N N     . ARG B  1  483 ? 59.058  28.009  -16.771 1.00 9.45  ? 483  ARG B N     1 
ATOM   7731  C CA    . ARG B  1  483 ? 57.867  27.903  -15.943 1.00 9.11  ? 483  ARG B CA    1 
ATOM   7732  C C     . ARG B  1  483 ? 56.944  29.077  -16.222 1.00 8.43  ? 483  ARG B C     1 
ATOM   7733  O O     . ARG B  1  483 ? 57.327  30.042  -16.887 1.00 9.32  ? 483  ARG B O     1 
ATOM   7734  C CB    . ARG B  1  483 ? 58.225  27.893  -14.452 1.00 10.04 ? 483  ARG B CB    1 
ATOM   7735  C CG    . ARG B  1  483 ? 59.277  26.865  -14.070 1.00 10.31 ? 483  ARG B CG    1 
ATOM   7736  C CD    . ARG B  1  483 ? 59.173  26.467  -12.599 1.00 11.02 ? 483  ARG B CD    1 
ATOM   7737  N NE    . ARG B  1  483 ? 60.400  25.812  -12.148 1.00 11.78 ? 483  ARG B NE    1 
ATOM   7738  C CZ    . ARG B  1  483 ? 60.487  25.029  -11.078 1.00 13.66 ? 483  ARG B CZ    1 
ATOM   7739  N NH1   . ARG B  1  483 ? 59.415  24.783  -10.335 1.00 14.86 ? 483  ARG B NH1   1 
ATOM   7740  N NH2   . ARG B  1  483 ? 61.656  24.500  -10.742 1.00 15.02 ? 483  ARG B NH2   1 
ATOM   7741  N N     . VAL B  1  484 ? 55.725  28.973  -15.710 1.00 8.18  ? 484  VAL B N     1 
ATOM   7742  C CA    . VAL B  1  484 ? 54.720  30.016  -15.854 1.00 5.96  ? 484  VAL B CA    1 
ATOM   7743  C C     . VAL B  1  484 ? 54.111  30.231  -14.473 1.00 7.11  ? 484  VAL B C     1 
ATOM   7744  O O     . VAL B  1  484 ? 53.683  29.280  -13.822 1.00 7.50  ? 484  VAL B O     1 
ATOM   7745  C CB    . VAL B  1  484 ? 53.608  29.604  -16.843 1.00 6.23  ? 484  VAL B CB    1 
ATOM   7746  C CG1   . VAL B  1  484 ? 52.460  30.609  -16.787 1.00 6.39  ? 484  VAL B CG1   1 
ATOM   7747  C CG2   . VAL B  1  484 ? 54.174  29.532  -18.259 1.00 6.89  ? 484  VAL B CG2   1 
ATOM   7748  N N     . VAL B  1  485 ? 54.098  31.480  -14.017 1.00 7.14  ? 485  VAL B N     1 
ATOM   7749  C CA    . VAL B  1  485 ? 53.541  31.796  -12.707 1.00 7.41  ? 485  VAL B CA    1 
ATOM   7750  C C     . VAL B  1  485 ? 52.812  33.135  -12.751 1.00 7.69  ? 485  VAL B C     1 
ATOM   7751  O O     . VAL B  1  485 ? 53.429  34.196  -12.725 1.00 7.59  ? 485  VAL B O     1 
ATOM   7752  C CB    . VAL B  1  485 ? 54.649  31.849  -11.619 1.00 8.11  ? 485  VAL B CB    1 
ATOM   7753  C CG1   . VAL B  1  485 ? 54.023  32.073  -10.251 1.00 8.60  ? 485  VAL B CG1   1 
ATOM   7754  C CG2   . VAL B  1  485 ? 55.446  30.550  -11.618 1.00 8.66  ? 485  VAL B CG2   1 
ATOM   7755  N N     . ASP B  1  486 ? 51.488  33.062  -12.843 1.00 7.76  ? 486  ASP B N     1 
ATOM   7756  C CA    . ASP B  1  486 ? 50.613  34.231  -12.885 1.00 7.70  ? 486  ASP B CA    1 
ATOM   7757  C C     . ASP B  1  486 ? 49.180  33.718  -12.932 1.00 7.60  ? 486  ASP B C     1 
ATOM   7758  O O     . ASP B  1  486 ? 48.934  32.541  -12.660 1.00 7.42  ? 486  ASP B O     1 
ATOM   7759  C CB    . ASP B  1  486 ? 50.909  35.114  -14.107 1.00 8.49  ? 486  ASP B CB    1 
ATOM   7760  C CG    . ASP B  1  486 ? 50.851  34.349  -15.421 1.00 7.91  ? 486  ASP B CG    1 
ATOM   7761  O OD1   . ASP B  1  486 ? 50.139  33.326  -15.492 1.00 10.54 ? 486  ASP B OD1   1 
ATOM   7762  O OD2   . ASP B  1  486 ? 51.516  34.785  -16.385 1.00 8.86  ? 486  ASP B OD2   1 
ATOM   7763  N N     . GLY B  1  487 ? 48.234  34.583  -13.286 1.00 7.07  ? 487  GLY B N     1 
ATOM   7764  C CA    . GLY B  1  487 ? 46.842  34.162  -13.328 1.00 7.04  ? 487  GLY B CA    1 
ATOM   7765  C C     . GLY B  1  487 ? 46.403  33.249  -14.464 1.00 6.16  ? 487  GLY B C     1 
ATOM   7766  O O     . GLY B  1  487 ? 45.234  32.886  -14.539 1.00 6.09  ? 487  GLY B O     1 
ATOM   7767  N N     . SER B  1  488 ? 47.323  32.863  -15.341 1.00 6.99  ? 488  SER B N     1 
ATOM   7768  C CA    . SER B  1  488 ? 46.970  32.003  -16.469 1.00 6.78  ? 488  SER B CA    1 
ATOM   7769  C C     . SER B  1  488 ? 46.939  30.514  -16.136 1.00 8.88  ? 488  SER B C     1 
ATOM   7770  O O     . SER B  1  488 ? 46.513  29.707  -16.964 1.00 7.61  ? 488  SER B O     1 
ATOM   7771  C CB    . SER B  1  488 ? 47.972  32.204  -17.612 1.00 6.78  ? 488  SER B CB    1 
ATOM   7772  O OG    . SER B  1  488 ? 49.231  31.617  -17.287 1.00 9.58  ? 488  SER B OG    1 
ATOM   7773  N N     . THR B  1  489 ? 47.347  30.150  -14.923 1.00 8.70  ? 489  THR B N     1 
ATOM   7774  C CA    . THR B  1  489 ? 47.459  28.734  -14.571 1.00 8.81  ? 489  THR B CA    1 
ATOM   7775  C C     . THR B  1  489 ? 46.282  27.912  -14.040 1.00 9.50  ? 489  THR B C     1 
ATOM   7776  O O     . THR B  1  489 ? 46.391  26.687  -13.960 1.00 9.61  ? 489  THR B O     1 
ATOM   7777  C CB    . THR B  1  489 ? 48.648  28.523  -13.607 1.00 10.03 ? 489  THR B CB    1 
ATOM   7778  O OG1   . THR B  1  489 ? 48.264  28.892  -12.280 1.00 11.46 ? 489  THR B OG1   1 
ATOM   7779  C CG2   . THR B  1  489 ? 49.832  29.375  -14.029 1.00 8.88  ? 489  THR B CG2   1 
ATOM   7780  N N     . PHE B  1  490 ? 45.170  28.542  -13.679 1.00 8.50  ? 490  PHE B N     1 
ATOM   7781  C CA    . PHE B  1  490 ? 44.024  27.779  -13.177 1.00 8.82  ? 490  PHE B CA    1 
ATOM   7782  C C     . PHE B  1  490 ? 42.731  28.190  -13.872 1.00 8.54  ? 490  PHE B C     1 
ATOM   7783  O O     . PHE B  1  490 ? 42.576  29.339  -14.275 1.00 8.55  ? 490  PHE B O     1 
ATOM   7784  C CB    . PHE B  1  490 ? 43.890  27.943  -11.661 1.00 8.37  ? 490  PHE B CB    1 
ATOM   7785  C CG    . PHE B  1  490 ? 45.052  27.383  -10.890 1.00 8.85  ? 490  PHE B CG    1 
ATOM   7786  C CD1   . PHE B  1  490 ? 45.961  28.226  -10.265 1.00 9.02  ? 490  PHE B CD1   1 
ATOM   7787  C CD2   . PHE B  1  490 ? 45.254  26.007  -10.815 1.00 10.02 ? 490  PHE B CD2   1 
ATOM   7788  C CE1   . PHE B  1  490 ? 47.058  27.710  -9.575  1.00 10.19 ? 490  PHE B CE1   1 
ATOM   7789  C CE2   . PHE B  1  490 ? 46.347  25.479  -10.127 1.00 9.69  ? 490  PHE B CE2   1 
ATOM   7790  C CZ    . PHE B  1  490 ? 47.252  26.333  -9.506  1.00 9.50  ? 490  PHE B CZ    1 
ATOM   7791  N N     . PRO B  1  491 ? 41.784  27.250  -14.023 1.00 9.29  ? 491  PRO B N     1 
ATOM   7792  C CA    . PRO B  1  491 ? 40.506  27.530  -14.686 1.00 9.18  ? 491  PRO B CA    1 
ATOM   7793  C C     . PRO B  1  491 ? 39.461  28.308  -13.897 1.00 8.76  ? 491  PRO B C     1 
ATOM   7794  O O     . PRO B  1  491 ? 38.626  28.999  -14.483 1.00 9.41  ? 491  PRO B O     1 
ATOM   7795  C CB    . PRO B  1  491 ? 40.008  26.138  -15.062 1.00 9.59  ? 491  PRO B CB    1 
ATOM   7796  C CG    . PRO B  1  491 ? 40.492  25.306  -13.915 1.00 10.15 ? 491  PRO B CG    1 
ATOM   7797  C CD    . PRO B  1  491 ? 41.910  25.812  -13.714 1.00 9.60  ? 491  PRO B CD    1 
ATOM   7798  N N     . TYR B  1  492 ? 39.495  28.195  -12.576 1.00 9.10  ? 492  TYR B N     1 
ATOM   7799  C CA    . TYR B  1  492 ? 38.511  28.881  -11.753 1.00 9.79  ? 492  TYR B CA    1 
ATOM   7800  C C     . TYR B  1  492 ? 39.138  29.934  -10.853 1.00 9.83  ? 492  TYR B C     1 
ATOM   7801  O O     . TYR B  1  492 ? 40.315  29.852  -10.502 1.00 11.19 ? 492  TYR B O     1 
ATOM   7802  C CB    . TYR B  1  492 ? 37.734  27.846  -10.939 1.00 12.04 ? 492  TYR B CB    1 
ATOM   7803  C CG    . TYR B  1  492 ? 37.099  26.787  -11.818 1.00 9.70  ? 492  TYR B CG    1 
ATOM   7804  C CD1   . TYR B  1  492 ? 37.257  25.431  -11.535 1.00 13.88 ? 492  TYR B CD1   1 
ATOM   7805  C CD2   . TYR B  1  492 ? 36.367  27.142  -12.954 1.00 10.06 ? 492  TYR B CD2   1 
ATOM   7806  C CE1   . TYR B  1  492 ? 36.706  24.454  -12.365 1.00 12.33 ? 492  TYR B CE1   1 
ATOM   7807  C CE2   . TYR B  1  492 ? 35.812  26.173  -13.789 1.00 10.18 ? 492  TYR B CE2   1 
ATOM   7808  C CZ    . TYR B  1  492 ? 35.988  24.833  -13.488 1.00 12.71 ? 492  TYR B CZ    1 
ATOM   7809  O OH    . TYR B  1  492 ? 35.456  23.873  -14.320 1.00 15.33 ? 492  TYR B OH    1 
ATOM   7810  N N     . THR B  1  493 ? 38.346  30.939  -10.498 1.00 9.49  ? 493  THR B N     1 
ATOM   7811  C CA    . THR B  1  493 ? 38.831  32.017  -9.654  1.00 10.00 ? 493  THR B CA    1 
ATOM   7812  C C     . THR B  1  493 ? 38.973  31.507  -8.213  1.00 8.92  ? 493  THR B C     1 
ATOM   7813  O O     . THR B  1  493 ? 38.099  30.811  -7.696  1.00 9.47  ? 493  THR B O     1 
ATOM   7814  C CB    . THR B  1  493 ? 37.874  33.237  -9.751  1.00 9.73  ? 493  THR B CB    1 
ATOM   7815  O OG1   . THR B  1  493 ? 38.556  34.415  -9.308  1.00 10.86 ? 493  THR B OG1   1 
ATOM   7816  C CG2   . THR B  1  493 ? 36.612  33.017  -8.919  1.00 9.92  ? 493  THR B CG2   1 
ATOM   7817  N N     . PRO B  1  494 ? 40.092  31.840  -7.552  1.00 9.68  ? 494  PRO B N     1 
ATOM   7818  C CA    . PRO B  1  494 ? 40.380  31.420  -6.176  1.00 10.20 ? 494  PRO B CA    1 
ATOM   7819  C C     . PRO B  1  494 ? 39.517  32.045  -5.082  1.00 9.51  ? 494  PRO B C     1 
ATOM   7820  O O     . PRO B  1  494 ? 39.417  31.507  -3.982  1.00 9.87  ? 494  PRO B O     1 
ATOM   7821  C CB    . PRO B  1  494 ? 41.850  31.785  -6.014  1.00 9.97  ? 494  PRO B CB    1 
ATOM   7822  C CG    . PRO B  1  494 ? 41.949  33.048  -6.810  1.00 10.04 ? 494  PRO B CG    1 
ATOM   7823  C CD    . PRO B  1  494 ? 41.181  32.687  -8.073  1.00 8.70  ? 494  PRO B CD    1 
ATOM   7824  N N     . ALA B  1  495 ? 38.910  33.185  -5.384  1.00 7.60  ? 495  ALA B N     1 
ATOM   7825  C CA    . ALA B  1  495 ? 38.066  33.879  -4.420  1.00 8.05  ? 495  ALA B CA    1 
ATOM   7826  C C     . ALA B  1  495 ? 37.292  34.944  -5.176  1.00 7.10  ? 495  ALA B C     1 
ATOM   7827  O O     . ALA B  1  495 ? 37.367  35.014  -6.402  1.00 7.95  ? 495  ALA B O     1 
ATOM   7828  C CB    . ALA B  1  495 ? 38.926  34.523  -3.336  1.00 8.14  ? 495  ALA B CB    1 
ATOM   7829  N N     . SER B  1  496 ? 36.552  35.773  -4.447  1.00 7.20  ? 496  SER B N     1 
ATOM   7830  C CA    . SER B  1  496 ? 35.774  36.839  -5.070  1.00 8.10  ? 496  SER B CA    1 
ATOM   7831  C C     . SER B  1  496 ? 36.713  37.825  -5.758  1.00 9.04  ? 496  SER B C     1 
ATOM   7832  O O     . SER B  1  496 ? 36.362  38.439  -6.765  1.00 7.89  ? 496  SER B O     1 
ATOM   7833  C CB    . SER B  1  496 ? 34.950  37.572  -4.011  1.00 8.52  ? 496  SER B CB    1 
ATOM   7834  O OG    . SER B  1  496 ? 35.794  38.125  -3.015  1.00 9.58  ? 496  SER B OG    1 
ATOM   7835  N N     . HIS B  1  497 ? 37.911  37.958  -5.197  1.00 8.00  ? 497  HIS B N     1 
ATOM   7836  C CA    . HIS B  1  497 ? 38.946  38.853  -5.707  1.00 6.90  ? 497  HIS B CA    1 
ATOM   7837  C C     . HIS B  1  497 ? 40.244  38.048  -5.627  1.00 7.83  ? 497  HIS B C     1 
ATOM   7838  O O     . HIS B  1  497 ? 40.699  37.684  -4.542  1.00 7.54  ? 497  HIS B O     1 
ATOM   7839  C CB    . HIS B  1  497 ? 38.979  40.121  -4.852  1.00 7.55  ? 497  HIS B CB    1 
ATOM   7840  C CG    . HIS B  1  497 ? 37.706  40.909  -4.917  1.00 7.56  ? 497  HIS B CG    1 
ATOM   7841  N ND1   . HIS B  1  497 ? 36.556  40.532  -4.251  1.00 9.92  ? 497  HIS B ND1   1 
ATOM   7842  C CD2   . HIS B  1  497 ? 37.385  42.027  -5.611  1.00 8.10  ? 497  HIS B CD2   1 
ATOM   7843  C CE1   . HIS B  1  497 ? 35.586  41.382  -4.534  1.00 9.00  ? 497  HIS B CE1   1 
ATOM   7844  N NE2   . HIS B  1  497 ? 36.063  42.299  -5.360  1.00 8.74  ? 497  HIS B NE2   1 
ATOM   7845  N N     . PRO B  1  498 ? 40.858  37.774  -6.789  1.00 7.21  ? 498  PRO B N     1 
ATOM   7846  C CA    . PRO B  1  498 ? 42.085  36.996  -6.968  1.00 6.24  ? 498  PRO B CA    1 
ATOM   7847  C C     . PRO B  1  498 ? 43.483  37.552  -6.732  1.00 7.35  ? 498  PRO B C     1 
ATOM   7848  O O     . PRO B  1  498 ? 44.434  36.769  -6.712  1.00 7.42  ? 498  PRO B O     1 
ATOM   7849  C CB    . PRO B  1  498 ? 41.943  36.514  -8.400  1.00 6.94  ? 498  PRO B CB    1 
ATOM   7850  C CG    . PRO B  1  498 ? 41.468  37.779  -9.067  1.00 6.75  ? 498  PRO B CG    1 
ATOM   7851  C CD    . PRO B  1  498 ? 40.398  38.296  -8.093  1.00 6.69  ? 498  PRO B CD    1 
ATOM   7852  N N     . GLN B  1  499 ? 43.645  38.858  -6.559  1.00 6.72  ? 499  GLN B N     1 
ATOM   7853  C CA    . GLN B  1  499 ? 45.004  39.364  -6.395  1.00 5.70  ? 499  GLN B CA    1 
ATOM   7854  C C     . GLN B  1  499 ? 45.735  38.741  -5.205  1.00 6.34  ? 499  GLN B C     1 
ATOM   7855  O O     . GLN B  1  499 ? 46.921  38.439  -5.300  1.00 6.33  ? 499  GLN B O     1 
ATOM   7856  C CB    . GLN B  1  499 ? 45.027  40.905  -6.321  1.00 6.99  ? 499  GLN B CB    1 
ATOM   7857  C CG    . GLN B  1  499 ? 44.852  41.537  -4.945  1.00 7.31  ? 499  GLN B CG    1 
ATOM   7858  C CD    . GLN B  1  499 ? 45.147  43.036  -4.970  1.00 6.92  ? 499  GLN B CD    1 
ATOM   7859  O OE1   . GLN B  1  499 ? 46.090  43.479  -5.625  1.00 8.81  ? 499  GLN B OE1   1 
ATOM   7860  N NE2   . GLN B  1  499 ? 44.351  43.815  -4.241  1.00 8.35  ? 499  GLN B NE2   1 
ATOM   7861  N N     . GLY B  1  500 ? 45.033  38.527  -4.096  1.00 5.77  ? 500  GLY B N     1 
ATOM   7862  C CA    . GLY B  1  500 ? 45.682  37.922  -2.943  1.00 6.95  ? 500  GLY B CA    1 
ATOM   7863  C C     . GLY B  1  500 ? 46.327  36.585  -3.288  1.00 7.10  ? 500  GLY B C     1 
ATOM   7864  O O     . GLY B  1  500 ? 47.474  36.314  -2.916  1.00 6.85  ? 500  GLY B O     1 
ATOM   7865  N N     . PHE B  1  501 ? 45.595  35.747  -4.013  1.00 7.18  ? 501  PHE B N     1 
ATOM   7866  C CA    . PHE B  1  501 ? 46.102  34.436  -4.405  1.00 6.91  ? 501  PHE B CA    1 
ATOM   7867  C C     . PHE B  1  501 ? 47.275  34.539  -5.384  1.00 6.04  ? 501  PHE B C     1 
ATOM   7868  O O     . PHE B  1  501 ? 48.262  33.818  -5.250  1.00 7.68  ? 501  PHE B O     1 
ATOM   7869  C CB    . PHE B  1  501 ? 44.978  33.606  -5.034  1.00 7.38  ? 501  PHE B CB    1 
ATOM   7870  C CG    . PHE B  1  501 ? 45.422  32.251  -5.522  1.00 8.35  ? 501  PHE B CG    1 
ATOM   7871  C CD1   . PHE B  1  501 ? 45.666  31.216  -4.627  1.00 8.46  ? 501  PHE B CD1   1 
ATOM   7872  C CD2   . PHE B  1  501 ? 45.613  32.020  -6.881  1.00 7.93  ? 501  PHE B CD2   1 
ATOM   7873  C CE1   . PHE B  1  501 ? 46.094  29.969  -5.078  1.00 10.13 ? 501  PHE B CE1   1 
ATOM   7874  C CE2   . PHE B  1  501 ? 46.042  30.778  -7.345  1.00 7.97  ? 501  PHE B CE2   1 
ATOM   7875  C CZ    . PHE B  1  501 ? 46.284  29.750  -6.440  1.00 9.17  ? 501  PHE B CZ    1 
ATOM   7876  N N     . TYR B  1  502 ? 47.174  35.438  -6.360  1.00 7.66  ? 502  TYR B N     1 
ATOM   7877  C CA    . TYR B  1  502 ? 48.241  35.594  -7.349  1.00 6.74  ? 502  TYR B CA    1 
ATOM   7878  C C     . TYR B  1  502 ? 49.502  36.208  -6.740  1.00 8.11  ? 502  TYR B C     1 
ATOM   7879  O O     . TYR B  1  502 ? 50.615  35.871  -7.147  1.00 8.82  ? 502  TYR B O     1 
ATOM   7880  C CB    . TYR B  1  502 ? 47.752  36.433  -8.539  1.00 7.65  ? 502  TYR B CB    1 
ATOM   7881  C CG    . TYR B  1  502 ? 46.577  35.820  -9.286  1.00 7.71  ? 502  TYR B CG    1 
ATOM   7882  C CD1   . TYR B  1  502 ? 45.664  36.624  -9.967  1.00 7.42  ? 502  TYR B CD1   1 
ATOM   7883  C CD2   . TYR B  1  502 ? 46.360  34.440  -9.285  1.00 6.96  ? 502  TYR B CD2   1 
ATOM   7884  C CE1   . TYR B  1  502 ? 44.559  36.072  -10.622 1.00 8.11  ? 502  TYR B CE1   1 
ATOM   7885  C CE2   . TYR B  1  502 ? 45.258  33.878  -9.937  1.00 6.63  ? 502  TYR B CE2   1 
ATOM   7886  C CZ    . TYR B  1  502 ? 44.361  34.700  -10.598 1.00 7.44  ? 502  TYR B CZ    1 
ATOM   7887  O OH    . TYR B  1  502 ? 43.247  34.159  -11.200 1.00 11.52 ? 502  TYR B OH    1 
ATOM   7888  N N     . LEU B  1  503 ? 49.331  37.102  -5.767  1.00 7.05  ? 503  LEU B N     1 
ATOM   7889  C CA    . LEU B  1  503 ? 50.477  37.719  -5.097  1.00 7.38  ? 503  LEU B CA    1 
ATOM   7890  C C     . LEU B  1  503 ? 51.213  36.612  -4.344  1.00 7.47  ? 503  LEU B C     1 
ATOM   7891  O O     . LEU B  1  503 ? 52.436  36.495  -4.422  1.00 8.08  ? 503  LEU B O     1 
ATOM   7892  C CB    . LEU B  1  503 ? 50.011  38.799  -4.112  1.00 7.66  ? 503  LEU B CB    1 
ATOM   7893  C CG    . LEU B  1  503 ? 49.463  40.105  -4.703  1.00 7.19  ? 503  LEU B CG    1 
ATOM   7894  C CD1   . LEU B  1  503 ? 48.637  40.847  -3.662  1.00 8.69  ? 503  LEU B CD1   1 
ATOM   7895  C CD2   . LEU B  1  503 ? 50.617  40.970  -5.199  1.00 8.09  ? 503  LEU B CD2   1 
ATOM   7896  N N     . MET B  1  504 ? 50.446  35.801  -3.621  1.00 7.55  ? 504  MET B N     1 
ATOM   7897  C CA    . MET B  1  504 ? 50.987  34.685  -2.853  1.00 7.52  ? 504  MET B CA    1 
ATOM   7898  C C     . MET B  1  504 ? 51.669  33.668  -3.771  1.00 8.62  ? 504  MET B C     1 
ATOM   7899  O O     . MET B  1  504 ? 52.764  33.188  -3.478  1.00 8.03  ? 504  MET B O     1 
ATOM   7900  C CB    . MET B  1  504 ? 49.850  34.016  -2.060  1.00 7.75  ? 504  MET B CB    1 
ATOM   7901  C CG    . MET B  1  504 ? 50.246  32.801  -1.224  1.00 7.02  ? 504  MET B CG    1 
ATOM   7902  S SD    . MET B  1  504 ? 50.434  31.259  -2.153  1.00 10.26 ? 504  MET B SD    1 
ATOM   7903  C CE    . MET B  1  504 ? 48.740  30.972  -2.683  1.00 10.56 ? 504  MET B CE    1 
ATOM   7904  N N     . LEU B  1  505 ? 51.029  33.356  -4.892  1.00 6.93  ? 505  LEU B N     1 
ATOM   7905  C CA    . LEU B  1  505 ? 51.568  32.385  -5.836  1.00 8.59  ? 505  LEU B CA    1 
ATOM   7906  C C     . LEU B  1  505 ? 52.991  32.707  -6.288  1.00 8.08  ? 505  LEU B C     1 
ATOM   7907  O O     . LEU B  1  505 ? 53.837  31.815  -6.391  1.00 7.70  ? 505  LEU B O     1 
ATOM   7908  C CB    . LEU B  1  505 ? 50.657  32.293  -7.063  1.00 8.25  ? 505  LEU B CB    1 
ATOM   7909  C CG    . LEU B  1  505 ? 51.049  31.244  -8.101  1.00 10.02 ? 505  LEU B CG    1 
ATOM   7910  C CD1   . LEU B  1  505 ? 50.927  29.856  -7.486  1.00 10.98 ? 505  LEU B CD1   1 
ATOM   7911  C CD2   . LEU B  1  505 ? 50.153  31.372  -9.319  1.00 12.73 ? 505  LEU B CD2   1 
ATOM   7912  N N     . GLY B  1  506 ? 53.247  33.983  -6.557  1.00 7.82  ? 506  GLY B N     1 
ATOM   7913  C CA    . GLY B  1  506 ? 54.564  34.393  -7.009  1.00 7.08  ? 506  GLY B CA    1 
ATOM   7914  C C     . GLY B  1  506 ? 55.654  33.989  -6.039  1.00 8.20  ? 506  GLY B C     1 
ATOM   7915  O O     . GLY B  1  506 ? 56.644  33.363  -6.429  1.00 8.10  ? 506  GLY B O     1 
ATOM   7916  N N     . ARG B  1  507 ? 55.489  34.349  -4.770  1.00 8.40  ? 507  ARG B N     1 
ATOM   7917  C CA    . ARG B  1  507 ? 56.500  33.986  -3.782  1.00 8.84  ? 507  ARG B CA    1 
ATOM   7918  C C     . ARG B  1  507 ? 56.476  32.489  -3.498  1.00 9.76  ? 507  ARG B C     1 
ATOM   7919  O O     . ARG B  1  507 ? 57.528  31.873  -3.317  1.00 10.25 ? 507  ARG B O     1 
ATOM   7920  C CB    . ARG B  1  507 ? 56.304  34.757  -2.473  1.00 10.11 ? 507  ARG B CB    1 
ATOM   7921  C CG    . ARG B  1  507 ? 57.222  34.261  -1.349  1.00 10.63 ? 507  ARG B CG    1 
ATOM   7922  C CD    . ARG B  1  507 ? 57.227  35.221  -0.177  1.00 12.19 ? 507  ARG B CD    1 
ATOM   7923  N NE    . ARG B  1  507 ? 58.016  34.746  0.962   1.00 9.57  ? 507  ARG B NE    1 
ATOM   7924  C CZ    . ARG B  1  507 ? 59.340  34.826  1.065   1.00 10.81 ? 507  ARG B CZ    1 
ATOM   7925  N NH1   . ARG B  1  507 ? 60.066  35.363  0.093   1.00 10.57 ? 507  ARG B NH1   1 
ATOM   7926  N NH2   . ARG B  1  507 ? 59.940  34.386  2.166   1.00 11.43 ? 507  ARG B NH2   1 
ATOM   7927  N N     . TYR B  1  508 ? 55.282  31.903  -3.459  1.00 9.75  ? 508  TYR B N     1 
ATOM   7928  C CA    . TYR B  1  508 ? 55.163  30.471  -3.193  1.00 9.38  ? 508  TYR B CA    1 
ATOM   7929  C C     . TYR B  1  508 ? 56.065  29.672  -4.133  1.00 9.87  ? 508  TYR B C     1 
ATOM   7930  O O     . TYR B  1  508 ? 56.887  28.868  -3.688  1.00 9.35  ? 508  TYR B O     1 
ATOM   7931  C CB    . TYR B  1  508 ? 53.712  30.005  -3.364  1.00 8.57  ? 508  TYR B CB    1 
ATOM   7932  C CG    . TYR B  1  508 ? 53.515  28.535  -3.057  1.00 8.82  ? 508  TYR B CG    1 
ATOM   7933  C CD1   . TYR B  1  508 ? 53.301  28.097  -1.750  1.00 9.07  ? 508  TYR B CD1   1 
ATOM   7934  C CD2   . TYR B  1  508 ? 53.590  27.580  -4.069  1.00 8.21  ? 508  TYR B CD2   1 
ATOM   7935  C CE1   . TYR B  1  508 ? 53.169  26.739  -1.459  1.00 9.70  ? 508  TYR B CE1   1 
ATOM   7936  C CE2   . TYR B  1  508 ? 53.460  26.223  -3.789  1.00 8.79  ? 508  TYR B CE2   1 
ATOM   7937  C CZ    . TYR B  1  508 ? 53.252  25.812  -2.482  1.00 9.85  ? 508  TYR B CZ    1 
ATOM   7938  O OH    . TYR B  1  508 ? 53.141  24.470  -2.197  1.00 11.30 ? 508  TYR B OH    1 
ATOM   7939  N N     . VAL B  1  509 ? 55.918  29.900  -5.435  1.00 8.92  ? 509  VAL B N     1 
ATOM   7940  C CA    . VAL B  1  509 ? 56.729  29.183  -6.414  1.00 8.96  ? 509  VAL B CA    1 
ATOM   7941  C C     . VAL B  1  509 ? 58.201  29.552  -6.269  1.00 10.40 ? 509  VAL B C     1 
ATOM   7942  O O     . VAL B  1  509 ? 59.083  28.718  -6.477  1.00 10.89 ? 509  VAL B O     1 
ATOM   7943  C CB    . VAL B  1  509 ? 56.246  29.470  -7.853  1.00 9.89  ? 509  VAL B CB    1 
ATOM   7944  C CG1   . VAL B  1  509 ? 57.087  28.692  -8.856  1.00 10.55 ? 509  VAL B CG1   1 
ATOM   7945  C CG2   . VAL B  1  509 ? 54.779  29.075  -7.985  1.00 11.50 ? 509  VAL B CG2   1 
ATOM   7946  N N     . GLY B  1  510 ? 58.470  30.799  -5.906  1.00 9.18  ? 510  GLY B N     1 
ATOM   7947  C CA    . GLY B  1  510 ? 59.847  31.216  -5.721  1.00 9.45  ? 510  GLY B CA    1 
ATOM   7948  C C     . GLY B  1  510 ? 60.519  30.389  -4.639  1.00 10.07 ? 510  GLY B C     1 
ATOM   7949  O O     . GLY B  1  510 ? 61.671  29.982  -4.789  1.00 12.59 ? 510  GLY B O     1 
ATOM   7950  N N     . ILE B  1  511 ? 59.802  30.144  -3.544  1.00 10.75 ? 511  ILE B N     1 
ATOM   7951  C CA    . ILE B  1  511 ? 60.336  29.354  -2.437  1.00 10.14 ? 511  ILE B CA    1 
ATOM   7952  C C     . ILE B  1  511 ? 60.511  27.898  -2.862  1.00 11.95 ? 511  ILE B C     1 
ATOM   7953  O O     . ILE B  1  511 ? 61.487  27.254  -2.489  1.00 12.56 ? 511  ILE B O     1 
ATOM   7954  C CB    . ILE B  1  511 ? 59.406  29.430  -1.195  1.00 10.81 ? 511  ILE B CB    1 
ATOM   7955  C CG1   . ILE B  1  511 ? 59.444  30.843  -0.605  1.00 10.93 ? 511  ILE B CG1   1 
ATOM   7956  C CG2   . ILE B  1  511 ? 59.831  28.405  -0.150  1.00 11.91 ? 511  ILE B CG2   1 
ATOM   7957  C CD1   . ILE B  1  511 ? 60.820  31.280  -0.099  1.00 12.79 ? 511  ILE B CD1   1 
ATOM   7958  N N     . LYS B  1  512 ? 59.573  27.380  -3.646  1.00 12.38 ? 512  LYS B N     1 
ATOM   7959  C CA    . LYS B  1  512 ? 59.676  26.000  -4.116  1.00 13.86 ? 512  LYS B CA    1 
ATOM   7960  C C     . LYS B  1  512 ? 60.919  25.833  -4.985  1.00 13.47 ? 512  LYS B C     1 
ATOM   7961  O O     . LYS B  1  512 ? 61.573  24.796  -4.951  1.00 15.46 ? 512  LYS B O     1 
ATOM   7962  C CB    . LYS B  1  512 ? 58.430  25.603  -4.914  1.00 14.29 ? 512  LYS B CB    1 
ATOM   7963  C CG    . LYS B  1  512 ? 57.132  25.675  -4.119  1.00 17.16 ? 512  LYS B CG    1 
ATOM   7964  C CD    . LYS B  1  512 ? 57.069  24.640  -2.998  1.00 20.71 ? 512  LYS B CD    1 
ATOM   7965  C CE    . LYS B  1  512 ? 56.825  23.240  -3.544  1.00 22.79 ? 512  LYS B CE    1 
ATOM   7966  N NZ    . LYS B  1  512 ? 56.562  22.258  -2.454  1.00 24.85 ? 512  LYS B NZ    1 
ATOM   7967  N N     . ILE B  1  513 ? 61.241  26.861  -5.762  1.00 13.08 ? 513  ILE B N     1 
ATOM   7968  C CA    . ILE B  1  513 ? 62.417  26.824  -6.627  1.00 13.13 ? 513  ILE B CA    1 
ATOM   7969  C C     . ILE B  1  513 ? 63.681  26.886  -5.770  1.00 13.91 ? 513  ILE B C     1 
ATOM   7970  O O     . ILE B  1  513 ? 64.664  26.195  -6.045  1.00 14.82 ? 513  ILE B O     1 
ATOM   7971  C CB    . ILE B  1  513 ? 62.417  28.006  -7.643  1.00 11.91 ? 513  ILE B CB    1 
ATOM   7972  C CG1   . ILE B  1  513 ? 61.316  27.791  -8.685  1.00 13.06 ? 513  ILE B CG1   1 
ATOM   7973  C CG2   . ILE B  1  513 ? 63.789  28.130  -8.310  1.00 11.99 ? 513  ILE B CG2   1 
ATOM   7974  C CD1   . ILE B  1  513 ? 61.116  28.972  -9.609  1.00 12.75 ? 513  ILE B CD1   1 
ATOM   7975  N N     . LEU B  1  514 ? 63.653  27.709  -4.727  1.00 14.01 ? 514  LEU B N     1 
ATOM   7976  C CA    . LEU B  1  514 ? 64.806  27.832  -3.837  1.00 15.18 ? 514  LEU B CA    1 
ATOM   7977  C C     . LEU B  1  514 ? 65.046  26.533  -3.081  1.00 16.87 ? 514  LEU B C     1 
ATOM   7978  O O     . LEU B  1  514 ? 66.191  26.135  -2.865  1.00 17.74 ? 514  LEU B O     1 
ATOM   7979  C CB    . LEU B  1  514 ? 64.609  28.981  -2.842  1.00 14.12 ? 514  LEU B CB    1 
ATOM   7980  C CG    . LEU B  1  514 ? 64.668  30.398  -3.422  1.00 13.86 ? 514  LEU B CG    1 
ATOM   7981  C CD1   . LEU B  1  514 ? 64.547  31.407  -2.297  1.00 14.90 ? 514  LEU B CD1   1 
ATOM   7982  C CD2   . LEU B  1  514 ? 65.980  30.599  -4.179  1.00 12.59 ? 514  LEU B CD2   1 
ATOM   7983  N N     . GLN B  1  515 ? 63.966  25.871  -2.679  1.00 16.33 ? 515  GLN B N     1 
ATOM   7984  C CA    . GLN B  1  515 ? 64.093  24.609  -1.961  1.00 18.12 ? 515  GLN B CA    1 
ATOM   7985  C C     . GLN B  1  515 ? 64.642  23.556  -2.914  1.00 18.72 ? 515  GLN B C     1 
ATOM   7986  O O     . GLN B  1  515 ? 65.396  22.669  -2.519  1.00 20.05 ? 515  GLN B O     1 
ATOM   7987  C CB    . GLN B  1  515 ? 62.738  24.162  -1.410  1.00 17.45 ? 515  GLN B CB    1 
ATOM   7988  C CG    . GLN B  1  515 ? 62.088  25.176  -0.481  1.00 17.71 ? 515  GLN B CG    1 
ATOM   7989  C CD    . GLN B  1  515 ? 60.829  24.649  0.183   1.00 19.63 ? 515  GLN B CD    1 
ATOM   7990  O OE1   . GLN B  1  515 ? 60.049  23.918  -0.427  1.00 20.42 ? 515  GLN B OE1   1 
ATOM   7991  N NE2   . GLN B  1  515 ? 60.617  25.035  1.434   1.00 21.31 ? 515  GLN B NE2   1 
ATOM   7992  N N     . GLU B  1  516 ? 64.259  23.669  -4.179  1.00 18.65 ? 516  GLU B N     1 
ATOM   7993  C CA    . GLU B  1  516 ? 64.723  22.735  -5.194  1.00 20.30 ? 516  GLU B CA    1 
ATOM   7994  C C     . GLU B  1  516 ? 66.221  22.939  -5.414  1.00 20.16 ? 516  GLU B C     1 
ATOM   7995  O O     . GLU B  1  516 ? 66.976  21.974  -5.510  1.00 21.03 ? 516  GLU B O     1 
ATOM   7996  C CB    . GLU B  1  516 ? 63.948  22.956  -6.497  1.00 21.32 ? 516  GLU B CB    1 
ATOM   7997  C CG    . GLU B  1  516 ? 64.130  21.857  -7.526  1.00 25.42 ? 516  GLU B CG    1 
ATOM   7998  C CD    . GLU B  1  516 ? 63.172  21.988  -8.688  1.00 27.73 ? 516  GLU B CD    1 
ATOM   7999  O OE1   . GLU B  1  516 ? 63.288  22.968  -9.451  1.00 29.71 ? 516  GLU B OE1   1 
ATOM   8000  O OE2   . GLU B  1  516 ? 62.299  21.107  -8.834  1.00 29.55 ? 516  GLU B OE2   1 
ATOM   8001  N N     . ARG B  1  517 ? 66.651  24.196  -5.483  1.00 19.28 ? 517  ARG B N     1 
ATOM   8002  C CA    . ARG B  1  517 ? 68.068  24.501  -5.675  1.00 19.72 ? 517  ARG B CA    1 
ATOM   8003  C C     . ARG B  1  517 ? 68.877  24.043  -4.463  1.00 20.89 ? 517  ARG B C     1 
ATOM   8004  O O     . ARG B  1  517 ? 69.999  23.557  -4.596  1.00 20.90 ? 517  ARG B O     1 
ATOM   8005  C CB    . ARG B  1  517 ? 68.279  26.011  -5.900  1.00 18.44 ? 517  ARG B CB    1 
ATOM   8006  C CG    . ARG B  1  517 ? 67.852  26.527  -7.268  1.00 17.56 ? 517  ARG B CG    1 
ATOM   8007  C CD    . ARG B  1  517 ? 68.630  25.861  -8.405  1.00 19.90 ? 517  ARG B CD    1 
ATOM   8008  N NE    . ARG B  1  517 ? 70.058  26.197  -8.447  1.00 17.64 ? 517  ARG B NE    1 
ATOM   8009  C CZ    . ARG B  1  517 ? 70.582  27.251  -9.070  1.00 17.93 ? 517  ARG B CZ    1 
ATOM   8010  N NH1   . ARG B  1  517 ? 69.801  28.101  -9.719  1.00 17.96 ? 517  ARG B NH1   1 
ATOM   8011  N NH2   . ARG B  1  517 ? 71.897  27.443  -9.065  1.00 18.33 ? 517  ARG B NH2   1 
ATOM   8012  N N     . SER B  1  518 ? 68.301  24.195  -3.278  1.00 21.16 ? 518  SER B N     1 
ATOM   8013  C CA    . SER B  1  518 ? 68.985  23.783  -2.061  1.00 23.70 ? 518  SER B CA    1 
ATOM   8014  C C     . SER B  1  518 ? 69.263  22.286  -2.083  1.00 24.59 ? 518  SER B C     1 
ATOM   8015  O O     . SER B  1  518 ? 70.362  21.840  -1.742  1.00 25.39 ? 518  SER B O     1 
ATOM   8016  C CB    . SER B  1  518 ? 68.139  24.115  -0.828  1.00 24.29 ? 518  SER B CB    1 
ATOM   8017  O OG    . SER B  1  518 ? 68.029  25.513  -0.654  1.00 28.33 ? 518  SER B OG    1 
ATOM   8018  N N     . ALA B  1  519 ? 68.260  21.517  -2.487  1.00 24.98 ? 519  ALA B N     1 
ATOM   8019  C CA    . ALA B  1  519 ? 68.381  20.069  -2.552  1.00 26.11 ? 519  ALA B CA    1 
ATOM   8020  C C     . ALA B  1  519 ? 69.388  19.617  -3.603  1.00 27.56 ? 519  ALA B C     1 
ATOM   8021  O O     . ALA B  1  519 ? 70.037  18.588  -3.437  1.00 28.41 ? 519  ALA B O     1 
ATOM   8022  C CB    . ALA B  1  519 ? 67.022  19.455  -2.836  1.00 25.33 ? 519  ALA B CB    1 
ATOM   8023  N N     . SER B  1  520 ? 69.526  20.386  -4.679  1.00 28.87 ? 520  SER B N     1 
ATOM   8024  C CA    . SER B  1  520 ? 70.454  20.016  -5.745  1.00 29.87 ? 520  SER B CA    1 
ATOM   8025  C C     . SER B  1  520 ? 71.877  20.523  -5.524  1.00 30.51 ? 520  SER B C     1 
ATOM   8026  O O     . SER B  1  520 ? 72.776  20.199  -6.297  1.00 30.66 ? 520  SER B O     1 
ATOM   8027  C CB    . SER B  1  520 ? 69.938  20.511  -7.103  1.00 30.03 ? 520  SER B CB    1 
ATOM   8028  O OG    . SER B  1  520 ? 70.152  21.898  -7.258  1.00 29.72 ? 520  SER B OG    1 
ATOM   8029  N N     . ASP B  1  521 ? 72.087  21.324  -4.482  1.00 31.75 ? 521  ASP B N     1 
ATOM   8030  C CA    . ASP B  1  521 ? 73.426  21.837  -4.205  1.00 33.20 ? 521  ASP B CA    1 
ATOM   8031  C C     . ASP B  1  521 ? 74.346  20.716  -3.743  1.00 33.71 ? 521  ASP B C     1 
ATOM   8032  O O     . ASP B  1  521 ? 75.555  20.983  -3.579  1.00 34.92 ? 521  ASP B O     1 
ATOM   8033  C CB    . ASP B  1  521 ? 73.402  22.934  -3.130  1.00 33.74 ? 521  ASP B CB    1 
ATOM   8034  C CG    . ASP B  1  521 ? 72.840  24.241  -3.639  1.00 34.87 ? 521  ASP B CG    1 
ATOM   8035  O OD1   . ASP B  1  521 ? 73.105  24.587  -4.811  1.00 35.21 ? 521  ASP B OD1   1 
ATOM   8036  O OD2   . ASP B  1  521 ? 72.146  24.928  -2.860  1.00 36.28 ? 521  ASP B OD2   1 
ATOM   8037  O OXT   . ASP B  1  521 ? 73.848  19.587  -3.548  1.00 33.47 ? 521  ASP B OXT   1 
HETATM 8038  C C1    . IPA C  2  .   ? 67.571  -18.031 -27.379 1.00 20.25 ? 522  IPA A C1    1 
HETATM 8039  C C2    . IPA C  2  .   ? 67.265  -19.130 -26.402 1.00 20.81 ? 522  IPA A C2    1 
HETATM 8040  C C3    . IPA C  2  .   ? 68.508  -19.994 -26.421 1.00 19.68 ? 522  IPA A C3    1 
HETATM 8041  O O2    . IPA C  2  .   ? 66.180  -20.010 -26.847 1.00 21.01 ? 522  IPA A O2    1 
HETATM 8042  P PA    . FAD D  3  .   ? 74.194  -5.601  -33.116 1.00 6.03  ? 523  FAD A PA    1 
HETATM 8043  O O1A   . FAD D  3  .   ? 74.306  -4.953  -31.779 1.00 9.18  ? 523  FAD A O1A   1 
HETATM 8044  O O2A   . FAD D  3  .   ? 73.529  -4.915  -34.099 1.00 7.06  ? 523  FAD A O2A   1 
HETATM 8045  O O5B   . FAD D  3  .   ? 75.654  -5.602  -33.512 1.00 7.80  ? 523  FAD A O5B   1 
HETATM 8046  C C5B   . FAD D  3  .   ? 76.210  -5.941  -34.827 1.00 7.14  ? 523  FAD A C5B   1 
HETATM 8047  C C4B   . FAD D  3  .   ? 77.280  -4.905  -35.120 1.00 6.27  ? 523  FAD A C4B   1 
HETATM 8048  O O4B   . FAD D  3  .   ? 77.982  -5.316  -36.376 1.00 6.79  ? 523  FAD A O4B   1 
HETATM 8049  C C3B   . FAD D  3  .   ? 76.778  -3.439  -35.400 1.00 7.82  ? 523  FAD A C3B   1 
HETATM 8050  O O3B   . FAD D  3  .   ? 77.429  -2.501  -34.594 1.00 7.02  ? 523  FAD A O3B   1 
HETATM 8051  C C2B   . FAD D  3  .   ? 77.009  -3.275  -36.939 1.00 6.41  ? 523  FAD A C2B   1 
HETATM 8052  O O2B   . FAD D  3  .   ? 77.207  -1.929  -37.313 1.00 7.42  ? 523  FAD A O2B   1 
HETATM 8053  C C1B   . FAD D  3  .   ? 78.231  -4.106  -37.165 1.00 6.44  ? 523  FAD A C1B   1 
HETATM 8054  N N9A   . FAD D  3  .   ? 78.440  -4.655  -38.509 1.00 6.27  ? 523  FAD A N9A   1 
HETATM 8055  C C8A   . FAD D  3  .   ? 77.511  -5.284  -39.323 1.00 5.18  ? 523  FAD A C8A   1 
HETATM 8056  N N7A   . FAD D  3  .   ? 78.027  -5.684  -40.487 1.00 7.66  ? 523  FAD A N7A   1 
HETATM 8057  C C5A   . FAD D  3  .   ? 79.346  -5.309  -40.424 1.00 5.05  ? 523  FAD A C5A   1 
HETATM 8058  C C6A   . FAD D  3  .   ? 80.457  -5.450  -41.386 1.00 6.21  ? 523  FAD A C6A   1 
HETATM 8059  N N6A   . FAD D  3  .   ? 80.332  -6.039  -42.544 1.00 9.13  ? 523  FAD A N6A   1 
HETATM 8060  N N1A   . FAD D  3  .   ? 81.675  -4.928  -40.966 1.00 6.08  ? 523  FAD A N1A   1 
HETATM 8061  C C2A   . FAD D  3  .   ? 81.836  -4.303  -39.747 1.00 6.76  ? 523  FAD A C2A   1 
HETATM 8062  N N3A   . FAD D  3  .   ? 80.870  -4.128  -38.805 1.00 5.73  ? 523  FAD A N3A   1 
HETATM 8063  C C4A   . FAD D  3  .   ? 79.642  -4.641  -39.195 1.00 6.15  ? 523  FAD A C4A   1 
HETATM 8064  N N1    . FAD D  3  .   ? 66.407  -5.179  -26.918 1.00 5.63  ? 523  FAD A N1    1 
HETATM 8065  C C2    . FAD D  3  .   ? 66.239  -5.087  -25.600 1.00 6.18  ? 523  FAD A C2    1 
HETATM 8066  O O2    . FAD D  3  .   ? 66.516  -5.988  -24.851 1.00 5.83  ? 523  FAD A O2    1 
HETATM 8067  N N3    . FAD D  3  .   ? 65.709  -3.901  -25.002 1.00 4.68  ? 523  FAD A N3    1 
HETATM 8068  C C4    . FAD D  3  .   ? 65.150  -2.876  -25.769 1.00 6.81  ? 523  FAD A C4    1 
HETATM 8069  O O4    . FAD D  3  .   ? 64.619  -1.941  -25.218 1.00 9.00  ? 523  FAD A O4    1 
HETATM 8070  C C4X   . FAD D  3  .   ? 65.252  -3.003  -27.221 1.00 6.14  ? 523  FAD A C4X   1 
HETATM 8071  N N5    . FAD D  3  .   ? 64.704  -2.051  -28.049 1.00 7.26  ? 523  FAD A N5    1 
HETATM 8072  C C5X   . FAD D  3  .   ? 65.097  -2.060  -29.379 1.00 6.33  ? 523  FAD A C5X   1 
HETATM 8073  C C6    . FAD D  3  .   ? 64.762  -0.918  -30.185 1.00 5.86  ? 523  FAD A C6    1 
HETATM 8074  C C7    . FAD D  3  .   ? 65.217  -0.807  -31.505 1.00 7.35  ? 523  FAD A C7    1 
HETATM 8075  C C7M   . FAD D  3  .   ? 64.878  0.429   -32.316 1.00 9.30  ? 523  FAD A C7M   1 
HETATM 8076  C C8    . FAD D  3  .   ? 66.015  -1.898  -32.101 1.00 7.04  ? 523  FAD A C8    1 
HETATM 8077  C C8M   . FAD D  3  .   ? 66.551  -1.844  -33.510 1.00 5.79  ? 523  FAD A C8M   1 
HETATM 8078  C C9    . FAD D  3  .   ? 66.298  -3.056  -31.330 1.00 6.08  ? 523  FAD A C9    1 
HETATM 8079  C C9A   . FAD D  3  .   ? 65.879  -3.134  -29.973 1.00 5.51  ? 523  FAD A C9A   1 
HETATM 8080  N N10   . FAD D  3  .   ? 66.217  -4.248  -29.085 1.00 5.59  ? 523  FAD A N10   1 
HETATM 8081  C C10   . FAD D  3  .   ? 65.974  -4.179  -27.750 1.00 4.59  ? 523  FAD A C10   1 
HETATM 8082  C "C1'" . FAD D  3  .   ? 66.862  -5.460  -29.664 1.00 6.26  ? 523  FAD A "C1'" 1 
HETATM 8083  C "C2'" . FAD D  3  .   ? 68.372  -5.545  -29.286 1.00 6.35  ? 523  FAD A "C2'" 1 
HETATM 8084  O "O2'" . FAD D  3  .   ? 68.890  -4.206  -29.185 1.00 7.98  ? 523  FAD A "O2'" 1 
HETATM 8085  C "C3'" . FAD D  3  .   ? 69.085  -6.330  -30.385 1.00 6.58  ? 523  FAD A "C3'" 1 
HETATM 8086  O "O3'" . FAD D  3  .   ? 68.452  -7.611  -30.480 1.00 6.57  ? 523  FAD A "O3'" 1 
HETATM 8087  C "C4'" . FAD D  3  .   ? 70.570  -6.531  -30.030 1.00 6.94  ? 523  FAD A "C4'" 1 
HETATM 8088  O "O4'" . FAD D  3  .   ? 71.219  -5.275  -29.788 1.00 7.21  ? 523  FAD A "O4'" 1 
HETATM 8089  C "C5'" . FAD D  3  .   ? 71.218  -7.280  -31.175 1.00 6.59  ? 523  FAD A "C5'" 1 
HETATM 8090  O "O5'" . FAD D  3  .   ? 72.696  -7.614  -30.811 1.00 6.92  ? 523  FAD A "O5'" 1 
HETATM 8091  P P     . FAD D  3  .   ? 73.669  -8.140  -31.865 1.00 6.67  ? 523  FAD A P     1 
HETATM 8092  O O1P   . FAD D  3  .   ? 75.028  -8.188  -31.193 1.00 7.66  ? 523  FAD A O1P   1 
HETATM 8093  O O2P   . FAD D  3  .   ? 73.218  -9.317  -32.477 1.00 7.99  ? 523  FAD A O2P   1 
HETATM 8094  O O3P   . FAD D  3  .   ? 73.718  -7.167  -32.977 1.00 5.20  ? 523  FAD A O3P   1 
HETATM 8095  C C1    . NAG E  4  .   ? 59.783  -19.856 -20.507 1.00 16.33 ? 524  NAG A C1    1 
HETATM 8096  C C2    . NAG E  4  .   ? 58.330  -19.535 -20.881 1.00 17.67 ? 524  NAG A C2    1 
HETATM 8097  C C3    . NAG E  4  .   ? 57.482  -20.816 -20.857 1.00 20.00 ? 524  NAG A C3    1 
HETATM 8098  C C4    . NAG E  4  .   ? 58.144  -21.940 -21.668 1.00 20.59 ? 524  NAG A C4    1 
HETATM 8099  C C5    . NAG E  4  .   ? 59.602  -22.121 -21.237 1.00 19.73 ? 524  NAG A C5    1 
HETATM 8100  C C6    . NAG E  4  .   ? 60.343  -23.149 -22.073 1.00 19.20 ? 524  NAG A C6    1 
HETATM 8101  C C7    . NAG E  4  .   ? 57.508  -17.333 -20.302 1.00 16.99 ? 524  NAG A C7    1 
HETATM 8102  C C8    . NAG E  4  .   ? 56.767  -16.472 -19.292 1.00 17.20 ? 524  NAG A C8    1 
HETATM 8103  N N2    . NAG E  4  .   ? 57.792  -18.580 -19.931 1.00 17.74 ? 524  NAG A N2    1 
HETATM 8104  O O3    . NAG E  4  .   ? 56.197  -20.540 -21.394 1.00 21.89 ? 524  NAG A O3    1 
HETATM 8105  O O4    . NAG E  4  .   ? 57.435  -23.158 -21.468 1.00 22.62 ? 524  NAG A O4    1 
HETATM 8106  O O5    . NAG E  4  .   ? 60.311  -20.873 -21.368 1.00 17.45 ? 524  NAG A O5    1 
HETATM 8107  O O6    . NAG E  4  .   ? 60.507  -22.703 -23.411 1.00 21.04 ? 524  NAG A O6    1 
HETATM 8108  O O7    . NAG E  4  .   ? 57.810  -16.868 -21.400 1.00 15.19 ? 524  NAG A O7    1 
HETATM 8109  C C1    . NAG F  4  .   ? 70.825  -18.068 -11.894 1.00 16.58 ? 525  NAG A C1    1 
HETATM 8110  C C2    . NAG F  4  .   ? 70.572  -19.094 -10.778 1.00 20.09 ? 525  NAG A C2    1 
HETATM 8111  C C3    . NAG F  4  .   ? 69.074  -19.322 -10.524 1.00 23.90 ? 525  NAG A C3    1 
HETATM 8112  C C4    . NAG F  4  .   ? 68.336  -17.987 -10.376 1.00 22.22 ? 525  NAG A C4    1 
HETATM 8113  C C5    . NAG F  4  .   ? 68.633  -17.141 -11.610 1.00 19.34 ? 525  NAG A C5    1 
HETATM 8114  C C6    . NAG F  4  .   ? 67.931  -15.799 -11.618 1.00 16.36 ? 525  NAG A C6    1 
HETATM 8115  C C7    . NAG F  4  .   ? 72.389  -20.680 -10.645 1.00 21.41 ? 525  NAG A C7    1 
HETATM 8116  C C8    . NAG F  4  .   ? 73.015  -21.975 -11.140 1.00 20.80 ? 525  NAG A C8    1 
HETATM 8117  N N2    . NAG F  4  .   ? 71.196  -20.355 -11.137 1.00 21.09 ? 525  NAG A N2    1 
HETATM 8118  O O3    . NAG F  4  .   ? 68.913  -20.097 -9.320  1.00 29.56 ? 525  NAG A O3    1 
HETATM 8119  O O4    . NAG F  4  .   ? 66.914  -18.215 -10.254 1.00 25.61 ? 525  NAG A O4    1 
HETATM 8120  O O5    . NAG F  4  .   ? 70.049  -16.880 -11.682 1.00 16.77 ? 525  NAG A O5    1 
HETATM 8121  O O6    . NAG F  4  .   ? 68.219  -15.088 -12.813 1.00 14.20 ? 525  NAG A O6    1 
HETATM 8122  O O7    . NAG F  4  .   ? 72.987  -19.985 -9.823  1.00 23.23 ? 525  NAG A O7    1 
HETATM 8123  C C1    . NAG G  4  .   ? 66.270  -17.656 -9.152  1.00 31.10 ? 526  NAG A C1    1 
HETATM 8124  C C2    . NAG G  4  .   ? 64.758  -17.953 -9.240  1.00 32.68 ? 526  NAG A C2    1 
HETATM 8125  C C3    . NAG G  4  .   ? 64.033  -17.559 -7.935  1.00 35.84 ? 526  NAG A C3    1 
HETATM 8126  C C4    . NAG G  4  .   ? 64.738  -18.227 -6.743  1.00 38.47 ? 526  NAG A C4    1 
HETATM 8127  C C5    . NAG G  4  .   ? 66.201  -17.793 -6.742  1.00 37.18 ? 526  NAG A C5    1 
HETATM 8128  C C6    . NAG G  4  .   ? 66.973  -18.387 -5.577  1.00 38.03 ? 526  NAG A C6    1 
HETATM 8129  C C7    . NAG G  4  .   ? 64.187  -17.780 -11.584 1.00 30.27 ? 526  NAG A C7    1 
HETATM 8130  C C8    . NAG G  4  .   ? 64.085  -16.824 -12.762 1.00 30.14 ? 526  NAG A C8    1 
HETATM 8131  N N2    . NAG G  4  .   ? 64.172  -17.245 -10.365 1.00 30.67 ? 526  NAG A N2    1 
HETATM 8132  O O3    . NAG G  4  .   ? 62.679  -17.981 -7.999  1.00 36.39 ? 526  NAG A O3    1 
HETATM 8133  O O4    . NAG G  4  .   ? 64.112  -17.930 -5.464  1.00 43.25 ? 526  NAG A O4    1 
HETATM 8134  O O5    . NAG G  4  .   ? 66.838  -18.243 -7.962  1.00 33.90 ? 526  NAG A O5    1 
HETATM 8135  O O6    . NAG G  4  .   ? 68.294  -17.871 -5.517  1.00 39.95 ? 526  NAG A O6    1 
HETATM 8136  O O7    . NAG G  4  .   ? 64.282  -18.990 -11.787 1.00 30.28 ? 526  NAG A O7    1 
HETATM 8137  C C1    . FUL H  5  .   ? 67.934  -21.096 -9.357  1.00 35.50 ? 527  FUL A C1    1 
HETATM 8138  C C2    . FUL H  5  .   ? 67.786  -21.713 -7.962  1.00 38.35 ? 527  FUL A C2    1 
HETATM 8139  O O2    . FUL H  5  .   ? 67.422  -20.710 -7.027  1.00 39.07 ? 527  FUL A O2    1 
HETATM 8140  C C3    . FUL H  5  .   ? 66.720  -22.807 -7.983  1.00 39.74 ? 527  FUL A C3    1 
HETATM 8141  O O3    . FUL H  5  .   ? 66.650  -23.427 -6.708  1.00 41.43 ? 527  FUL A O3    1 
HETATM 8142  C C4    . FUL H  5  .   ? 67.065  -23.848 -9.049  1.00 40.34 ? 527  FUL A C4    1 
HETATM 8143  O O4    . FUL H  5  .   ? 68.271  -24.510 -8.694  1.00 41.43 ? 527  FUL A O4    1 
HETATM 8144  C C5    . FUL H  5  .   ? 67.237  -23.158 -10.408 1.00 40.25 ? 527  FUL A C5    1 
HETATM 8145  C C6    . FUL H  5  .   ? 67.694  -24.115 -11.493 1.00 40.46 ? 527  FUL A C6    1 
HETATM 8146  O O5    . FUL H  5  .   ? 68.233  -22.114 -10.311 1.00 37.79 ? 527  FUL A O5    1 
HETATM 8147  C C1    . MAN I  6  .   ? 63.688  -16.637 -5.178  1.00 46.60 ? 528  MAN A C1    1 
HETATM 8148  C C2    . MAN I  6  .   ? 63.899  -16.306 -3.686  1.00 47.90 ? 528  MAN A C2    1 
HETATM 8149  C C3    . MAN I  6  .   ? 62.934  -17.069 -2.758  1.00 48.90 ? 528  MAN A C3    1 
HETATM 8150  C C4    . MAN I  6  .   ? 61.494  -17.023 -3.278  1.00 49.69 ? 528  MAN A C4    1 
HETATM 8151  C C5    . MAN I  6  .   ? 61.472  -17.439 -4.748  1.00 49.76 ? 528  MAN A C5    1 
HETATM 8152  C C6    . MAN I  6  .   ? 60.093  -17.412 -5.376  1.00 50.90 ? 528  MAN A C6    1 
HETATM 8153  O O2    . MAN I  6  .   ? 63.737  -14.913 -3.479  1.00 48.23 ? 528  MAN A O2    1 
HETATM 8154  O O3    . MAN I  6  .   ? 62.978  -16.491 -1.461  1.00 49.84 ? 528  MAN A O3    1 
HETATM 8155  O O4    . MAN I  6  .   ? 60.680  -17.900 -2.514  1.00 49.85 ? 528  MAN A O4    1 
HETATM 8156  O O5    . MAN I  6  .   ? 62.304  -16.539 -5.517  1.00 48.47 ? 528  MAN A O5    1 
HETATM 8157  O O6    . MAN I  6  .   ? 60.121  -16.499 -6.490  1.00 52.26 ? 528  MAN A O6    1 
HETATM 8158  C C1    . MAN J  6  .   ? 58.919  -16.363 -7.186  1.00 52.66 ? 529  MAN A C1    1 
HETATM 8159  C C2    . MAN J  6  .   ? 59.010  -15.104 -8.053  1.00 52.63 ? 529  MAN A C2    1 
HETATM 8160  C C3    . MAN J  6  .   ? 59.008  -13.846 -7.168  1.00 53.02 ? 529  MAN A C3    1 
HETATM 8161  C C4    . MAN J  6  .   ? 57.808  -13.854 -6.213  1.00 53.23 ? 529  MAN A C4    1 
HETATM 8162  C C5    . MAN J  6  .   ? 57.786  -15.164 -5.419  1.00 53.27 ? 529  MAN A C5    1 
HETATM 8163  C C6    . MAN J  6  .   ? 56.567  -15.298 -4.527  1.00 53.26 ? 529  MAN A C6    1 
HETATM 8164  O O2    . MAN J  6  .   ? 57.923  -15.065 -8.960  1.00 52.72 ? 529  MAN A O2    1 
HETATM 8165  O O3    . MAN J  6  .   ? 58.968  -12.682 -7.980  1.00 52.82 ? 529  MAN A O3    1 
HETATM 8166  O O4    . MAN J  6  .   ? 57.901  -12.756 -5.318  1.00 53.42 ? 529  MAN A O4    1 
HETATM 8167  O O5    . MAN J  6  .   ? 57.782  -16.289 -6.325  1.00 52.77 ? 529  MAN A O5    1 
HETATM 8168  O O6    . MAN J  6  .   ? 55.908  -16.538 -4.736  1.00 53.29 ? 529  MAN A O6    1 
HETATM 8169  C C1    . NAG K  4  .   ? 53.854  -23.792 -36.823 1.00 24.46 ? 530  NAG A C1    1 
HETATM 8170  C C2    . NAG K  4  .   ? 53.993  -24.831 -37.940 1.00 27.79 ? 530  NAG A C2    1 
HETATM 8171  C C3    . NAG K  4  .   ? 53.713  -26.229 -37.384 1.00 31.60 ? 530  NAG A C3    1 
HETATM 8172  C C4    . NAG K  4  .   ? 54.638  -26.515 -36.199 1.00 32.14 ? 530  NAG A C4    1 
HETATM 8173  C C5    . NAG K  4  .   ? 54.483  -25.401 -35.153 1.00 29.75 ? 530  NAG A C5    1 
HETATM 8174  C C6    . NAG K  4  .   ? 55.433  -25.556 -33.979 1.00 30.04 ? 530  NAG A C6    1 
HETATM 8175  C C7    . NAG K  4  .   ? 53.543  -24.060 -40.175 1.00 29.15 ? 530  NAG A C7    1 
HETATM 8176  C C8    . NAG K  4  .   ? 52.574  -23.285 -41.052 1.00 29.06 ? 530  NAG A C8    1 
HETATM 8177  N N2    . NAG K  4  .   ? 53.077  -24.538 -39.026 1.00 28.69 ? 530  NAG A N2    1 
HETATM 8178  O O3    . NAG K  4  .   ? 53.918  -27.213 -38.415 1.00 35.24 ? 530  NAG A O3    1 
HETATM 8179  O O4    . NAG K  4  .   ? 54.298  -27.791 -35.616 1.00 36.37 ? 530  NAG A O4    1 
HETATM 8180  O O5    . NAG K  4  .   ? 54.754  -24.109 -35.750 1.00 25.61 ? 530  NAG A O5    1 
HETATM 8181  O O6    . NAG K  4  .   ? 56.787  -25.450 -34.395 1.00 30.59 ? 530  NAG A O6    1 
HETATM 8182  O O7    . NAG K  4  .   ? 54.709  -24.217 -40.539 1.00 30.92 ? 530  NAG A O7    1 
HETATM 8183  C C1    . NAG L  4  .   ? 55.353  -28.588 -35.186 1.00 40.36 ? 531  NAG A C1    1 
HETATM 8184  C C2    . NAG L  4  .   ? 54.820  -29.691 -34.262 1.00 41.29 ? 531  NAG A C2    1 
HETATM 8185  C C3    . NAG L  4  .   ? 55.949  -30.650 -33.875 1.00 42.67 ? 531  NAG A C3    1 
HETATM 8186  C C4    . NAG L  4  .   ? 56.647  -31.181 -35.128 1.00 42.85 ? 531  NAG A C4    1 
HETATM 8187  C C5    . NAG L  4  .   ? 57.110  -30.009 -35.997 1.00 43.01 ? 531  NAG A C5    1 
HETATM 8188  C C6    . NAG L  4  .   ? 57.753  -30.471 -37.293 1.00 43.17 ? 531  NAG A C6    1 
HETATM 8189  C C7    . NAG L  4  .   ? 52.927  -29.029 -32.929 1.00 42.23 ? 531  NAG A C7    1 
HETATM 8190  C C8    . NAG L  4  .   ? 52.396  -28.099 -31.851 1.00 42.86 ? 531  NAG A C8    1 
HETATM 8191  N N2    . NAG L  4  .   ? 54.246  -29.108 -33.065 1.00 41.66 ? 531  NAG A N2    1 
HETATM 8192  O O3    . NAG L  4  .   ? 55.418  -31.735 -33.127 1.00 43.55 ? 531  NAG A O3    1 
HETATM 8193  O O4    . NAG L  4  .   ? 57.765  -31.974 -34.754 1.00 43.75 ? 531  NAG A O4    1 
HETATM 8194  O O5    . NAG L  4  .   ? 55.980  -29.171 -36.342 1.00 41.81 ? 531  NAG A O5    1 
HETATM 8195  O O6    . NAG L  4  .   ? 57.150  -29.856 -38.422 1.00 44.37 ? 531  NAG A O6    1 
HETATM 8196  O O7    . NAG L  4  .   ? 52.141  -29.667 -33.632 1.00 42.80 ? 531  NAG A O7    1 
HETATM 8197  C C1    . FUC M  7  .   ? 52.755  -27.673 -39.050 1.00 39.07 ? 532  FUC A C1    1 
HETATM 8198  C C2    . FUC M  7  .   ? 53.131  -28.574 -40.232 1.00 40.64 ? 532  FUC A C2    1 
HETATM 8199  C C3    . FUC M  7  .   ? 53.748  -29.882 -39.724 1.00 41.79 ? 532  FUC A C3    1 
HETATM 8200  C C4    . FUC M  7  .   ? 52.800  -30.561 -38.732 1.00 41.98 ? 532  FUC A C4    1 
HETATM 8201  C C5    . FUC M  7  .   ? 52.440  -29.587 -37.605 1.00 41.57 ? 532  FUC A C5    1 
HETATM 8202  C C6    . FUC M  7  .   ? 51.411  -30.156 -36.648 1.00 41.50 ? 532  FUC A C6    1 
HETATM 8203  O O2    . FUC M  7  .   ? 54.056  -27.900 -41.073 1.00 41.49 ? 532  FUC A O2    1 
HETATM 8204  O O3    . FUC M  7  .   ? 53.999  -30.751 -40.818 1.00 43.35 ? 532  FUC A O3    1 
HETATM 8205  O O4    . FUC M  7  .   ? 51.617  -30.970 -39.404 1.00 42.12 ? 532  FUC A O4    1 
HETATM 8206  O O5    . FUC M  7  .   ? 51.885  -28.372 -38.158 1.00 40.42 ? 532  FUC A O5    1 
HETATM 8207  C C1    . NAG N  4  .   ? 45.657  16.487  -34.275 1.00 37.88 ? 533  NAG A C1    1 
HETATM 8208  C C2    . NAG N  4  .   ? 45.204  16.362  -35.743 1.00 40.12 ? 533  NAG A C2    1 
HETATM 8209  C C3    . NAG N  4  .   ? 43.685  16.167  -35.843 1.00 41.37 ? 533  NAG A C3    1 
HETATM 8210  C C4    . NAG N  4  .   ? 43.246  15.006  -34.956 1.00 41.31 ? 533  NAG A C4    1 
HETATM 8211  C C5    . NAG N  4  .   ? 43.733  15.256  -33.529 1.00 40.60 ? 533  NAG A C5    1 
HETATM 8212  C C6    . NAG N  4  .   ? 43.363  14.131  -32.584 1.00 39.44 ? 533  NAG A C6    1 
HETATM 8213  C C7    . NAG N  4  .   ? 46.183  17.424  -37.669 1.00 42.73 ? 533  NAG A C7    1 
HETATM 8214  C C8    . NAG N  4  .   ? 46.194  18.650  -38.567 1.00 42.63 ? 533  NAG A C8    1 
HETATM 8215  N N2    . NAG N  4  .   ? 45.595  17.546  -36.483 1.00 41.68 ? 533  NAG A N2    1 
HETATM 8216  O O3    . NAG N  4  .   ? 43.320  15.899  -37.191 1.00 42.73 ? 533  NAG A O3    1 
HETATM 8217  O O4    . NAG N  4  .   ? 41.829  14.894  -34.976 1.00 42.81 ? 533  NAG A O4    1 
HETATM 8218  O O5    . NAG N  4  .   ? 45.174  15.371  -33.510 1.00 38.90 ? 533  NAG A O5    1 
HETATM 8219  O O6    . NAG N  4  .   ? 43.641  14.486  -31.238 1.00 39.01 ? 533  NAG A O6    1 
HETATM 8220  O O7    . NAG N  4  .   ? 46.702  16.374  -38.054 1.00 43.02 ? 533  NAG A O7    1 
HETATM 8221  C C1    . IPA O  2  .   ? 42.679  28.925  -8.384  1.00 19.61 ? 522  IPA B C1    1 
HETATM 8222  C C2    . IPA O  2  .   ? 42.284  27.797  -7.475  1.00 21.76 ? 522  IPA B C2    1 
HETATM 8223  C C3    . IPA O  2  .   ? 43.470  26.858  -7.522  1.00 21.00 ? 522  IPA B C3    1 
HETATM 8224  O O2    . IPA O  2  .   ? 41.158  27.013  -7.990  1.00 20.21 ? 522  IPA B O2    1 
HETATM 8225  P PA    . FAD P  3  .   ? 49.458  41.161  -14.251 1.00 7.10  ? 523  FAD B PA    1 
HETATM 8226  O O1A   . FAD P  3  .   ? 49.594  41.839  -12.932 1.00 7.73  ? 523  FAD B O1A   1 
HETATM 8227  O O2A   . FAD P  3  .   ? 48.783  41.826  -15.238 1.00 7.35  ? 523  FAD B O2A   1 
HETATM 8228  O O5B   . FAD P  3  .   ? 50.910  41.142  -14.663 1.00 6.62  ? 523  FAD B O5B   1 
HETATM 8229  C C5B   . FAD P  3  .   ? 51.441  40.784  -15.986 1.00 7.84  ? 523  FAD B C5B   1 
HETATM 8230  C C4B   . FAD P  3  .   ? 52.527  41.792  -16.274 1.00 7.85  ? 523  FAD B C4B   1 
HETATM 8231  O O4B   . FAD P  3  .   ? 53.214  41.365  -17.533 1.00 8.29  ? 523  FAD B O4B   1 
HETATM 8232  C C3B   . FAD P  3  .   ? 52.051  43.266  -16.555 1.00 7.77  ? 523  FAD B C3B   1 
HETATM 8233  O O3B   . FAD P  3  .   ? 52.690  44.203  -15.738 1.00 7.90  ? 523  FAD B O3B   1 
HETATM 8234  C C2B   . FAD P  3  .   ? 52.309  43.432  -18.088 1.00 7.24  ? 523  FAD B C2B   1 
HETATM 8235  O O2B   . FAD P  3  .   ? 52.547  44.777  -18.443 1.00 8.16  ? 523  FAD B O2B   1 
HETATM 8236  C C1B   . FAD P  3  .   ? 53.514  42.571  -18.302 1.00 8.23  ? 523  FAD B C1B   1 
HETATM 8237  N N9A   . FAD P  3  .   ? 53.727  42.025  -19.643 1.00 7.16  ? 523  FAD B N9A   1 
HETATM 8238  C C8A   . FAD P  3  .   ? 52.789  41.426  -20.471 1.00 7.08  ? 523  FAD B C8A   1 
HETATM 8239  N N7A   . FAD P  3  .   ? 53.301  41.020  -21.628 1.00 7.22  ? 523  FAD B N7A   1 
HETATM 8240  C C5A   . FAD P  3  .   ? 54.633  41.366  -21.553 1.00 8.68  ? 523  FAD B C5A   1 
HETATM 8241  C C6A   . FAD P  3  .   ? 55.751  41.195  -22.503 1.00 9.00  ? 523  FAD B C6A   1 
HETATM 8242  N N6A   . FAD P  3  .   ? 55.621  40.623  -23.673 1.00 9.71  ? 523  FAD B N6A   1 
HETATM 8243  N N1A   . FAD P  3  .   ? 56.976  41.685  -22.066 1.00 8.83  ? 523  FAD B N1A   1 
HETATM 8244  C C2A   . FAD P  3  .   ? 57.146  42.290  -20.842 1.00 8.79  ? 523  FAD B C2A   1 
HETATM 8245  N N3A   . FAD P  3  .   ? 56.175  42.486  -19.907 1.00 9.41  ? 523  FAD B N3A   1 
HETATM 8246  C C4A   . FAD P  3  .   ? 54.938  42.008  -20.313 1.00 7.76  ? 523  FAD B C4A   1 
HETATM 8247  N N1    . FAD P  3  .   ? 41.634  41.627  -8.067  1.00 5.64  ? 523  FAD B N1    1 
HETATM 8248  C C2    . FAD P  3  .   ? 41.524  41.747  -6.738  1.00 6.92  ? 523  FAD B C2    1 
HETATM 8249  O O2    . FAD P  3  .   ? 41.872  40.879  -5.978  1.00 7.40  ? 523  FAD B O2    1 
HETATM 8250  N N3    . FAD P  3  .   ? 40.973  42.927  -6.139  1.00 5.84  ? 523  FAD B N3    1 
HETATM 8251  C C4    . FAD P  3  .   ? 40.441  43.968  -6.908  1.00 8.29  ? 523  FAD B C4    1 
HETATM 8252  O O4    . FAD P  3  .   ? 39.944  44.922  -6.349  1.00 7.65  ? 523  FAD B O4    1 
HETATM 8253  C C4X   . FAD P  3  .   ? 40.527  43.835  -8.365  1.00 6.01  ? 523  FAD B C4X   1 
HETATM 8254  N N5    . FAD P  3  .   ? 39.982  44.790  -9.195  1.00 6.69  ? 523  FAD B N5    1 
HETATM 8255  C C5X   . FAD P  3  .   ? 40.407  44.804  -10.517 1.00 6.98  ? 523  FAD B C5X   1 
HETATM 8256  C C6    . FAD P  3  .   ? 40.096  45.958  -11.319 1.00 6.92  ? 523  FAD B C6    1 
HETATM 8257  C C7    . FAD P  3  .   ? 40.540  46.064  -12.643 1.00 7.90  ? 523  FAD B C7    1 
HETATM 8258  C C7M   . FAD P  3  .   ? 40.178  47.289  -13.463 1.00 7.25  ? 523  FAD B C7M   1 
HETATM 8259  C C8    . FAD P  3  .   ? 41.342  44.979  -13.238 1.00 7.34  ? 523  FAD B C8    1 
HETATM 8260  C C8M   . FAD P  3  .   ? 41.868  45.035  -14.652 1.00 6.30  ? 523  FAD B C8M   1 
HETATM 8261  C C9    . FAD P  3  .   ? 41.628  43.822  -12.465 1.00 7.96  ? 523  FAD B C9    1 
HETATM 8262  C C9A   . FAD P  3  .   ? 41.191  43.730  -11.115 1.00 6.39  ? 523  FAD B C9A   1 
HETATM 8263  N N10   . FAD P  3  .   ? 41.505  42.600  -10.233 1.00 6.25  ? 523  FAD B N10   1 
HETATM 8264  C C10   . FAD P  3  .   ? 41.235  42.650  -8.899  1.00 5.68  ? 523  FAD B C10   1 
HETATM 8265  C "C1'" . FAD P  3  .   ? 42.150  41.396  -10.823 1.00 6.03  ? 523  FAD B "C1'" 1 
HETATM 8266  C "C2'" . FAD P  3  .   ? 43.662  41.309  -10.454 1.00 7.27  ? 523  FAD B "C2'" 1 
HETATM 8267  O "O2'" . FAD P  3  .   ? 44.191  42.647  -10.379 1.00 7.18  ? 523  FAD B "O2'" 1 
HETATM 8268  C "C3'" . FAD P  3  .   ? 44.361  40.506  -11.546 1.00 6.08  ? 523  FAD B "C3'" 1 
HETATM 8269  O "O3'" . FAD P  3  .   ? 43.696  39.239  -11.659 1.00 6.85  ? 523  FAD B "O3'" 1 
HETATM 8270  C "C4'" . FAD P  3  .   ? 45.837  40.272  -11.176 1.00 7.25  ? 523  FAD B "C4'" 1 
HETATM 8271  O "O4'" . FAD P  3  .   ? 46.521  41.514  -10.968 1.00 6.24  ? 523  FAD B "O4'" 1 
HETATM 8272  C "C5'" . FAD P  3  .   ? 46.466  39.479  -12.291 1.00 5.87  ? 523  FAD B "C5'" 1 
HETATM 8273  O "O5'" . FAD P  3  .   ? 47.950  39.189  -11.932 1.00 7.59  ? 523  FAD B "O5'" 1 
HETATM 8274  P P     . FAD P  3  .   ? 48.912  38.643  -12.975 1.00 6.55  ? 523  FAD B P     1 
HETATM 8275  O O1P   . FAD P  3  .   ? 50.270  38.577  -12.301 1.00 7.09  ? 523  FAD B O1P   1 
HETATM 8276  O O2P   . FAD P  3  .   ? 48.443  37.467  -13.562 1.00 7.16  ? 523  FAD B O2P   1 
HETATM 8277  O O3P   . FAD P  3  .   ? 48.977  39.601  -14.089 1.00 6.72  ? 523  FAD B O3P   1 
HETATM 8278  C C1    . NAG Q  4  .   ? 29.673  18.348  -16.105 1.00 28.67 ? 524  NAG B C1    1 
HETATM 8279  C C2    . NAG Q  4  .   ? 29.034  17.327  -15.158 1.00 29.19 ? 524  NAG B C2    1 
HETATM 8280  C C3    . NAG Q  4  .   ? 30.034  16.224  -14.798 1.00 30.56 ? 524  NAG B C3    1 
HETATM 8281  C C4    . NAG Q  4  .   ? 30.691  15.638  -16.051 1.00 32.43 ? 524  NAG B C4    1 
HETATM 8282  C C5    . NAG Q  4  .   ? 31.263  16.763  -16.917 1.00 32.29 ? 524  NAG B C5    1 
HETATM 8283  C C6    . NAG Q  4  .   ? 31.874  16.264  -18.215 1.00 33.22 ? 524  NAG B C6    1 
HETATM 8284  C C7    . NAG Q  4  .   ? 27.316  18.083  -13.641 1.00 29.58 ? 524  NAG B C7    1 
HETATM 8285  C C8    . NAG Q  4  .   ? 26.970  18.458  -12.210 1.00 30.18 ? 524  NAG B C8    1 
HETATM 8286  N N2    . NAG Q  4  .   ? 28.607  18.000  -13.946 1.00 28.29 ? 524  NAG B N2    1 
HETATM 8287  O O3    . NAG Q  4  .   ? 29.362  15.194  -14.090 1.00 29.55 ? 524  NAG B O3    1 
HETATM 8288  O O4    . NAG Q  4  .   ? 31.753  14.750  -15.659 1.00 35.09 ? 524  NAG B O4    1 
HETATM 8289  O O5    . NAG Q  4  .   ? 30.218  17.694  -17.261 1.00 29.81 ? 524  NAG B O5    1 
HETATM 8290  O O6    . NAG Q  4  .   ? 31.017  16.507  -19.319 1.00 36.44 ? 524  NAG B O6    1 
HETATM 8291  O O7    . NAG Q  4  .   ? 26.418  17.871  -14.457 1.00 30.09 ? 524  NAG B O7    1 
HETATM 8292  C C1    . NAG R  4  .   ? 28.697  23.227  -17.796 1.00 18.92 ? 525  NAG B C1    1 
HETATM 8293  C C2    . NAG R  4  .   ? 28.784  22.183  -18.915 1.00 21.91 ? 525  NAG B C2    1 
HETATM 8294  C C3    . NAG R  4  .   ? 28.405  20.799  -18.376 1.00 24.27 ? 525  NAG B C3    1 
HETATM 8295  C C4    . NAG R  4  .   ? 29.203  20.469  -17.110 1.00 23.91 ? 525  NAG B C4    1 
HETATM 8296  C C5    . NAG R  4  .   ? 29.069  21.603  -16.091 1.00 22.16 ? 525  NAG B C5    1 
HETATM 8297  C C6    . NAG R  4  .   ? 29.899  21.383  -14.839 1.00 22.97 ? 525  NAG B C6    1 
HETATM 8298  C C7    . NAG R  4  .   ? 28.356  22.784  -21.215 1.00 22.89 ? 525  NAG B C7    1 
HETATM 8299  C C8    . NAG R  4  .   ? 27.337  23.098  -22.302 1.00 23.91 ? 525  NAG B C8    1 
HETATM 8300  N N2    . NAG R  4  .   ? 27.884  22.548  -19.995 1.00 22.79 ? 525  NAG B N2    1 
HETATM 8301  O O3    . NAG R  4  .   ? 28.669  19.803  -19.383 1.00 27.97 ? 525  NAG B O3    1 
HETATM 8302  O O4    . NAG R  4  .   ? 28.711  19.245  -16.534 1.00 25.76 ? 525  NAG B O4    1 
HETATM 8303  O O5    . NAG R  4  .   ? 29.508  22.839  -16.682 1.00 20.23 ? 525  NAG B O5    1 
HETATM 8304  O O6    . NAG R  4  .   ? 31.248  21.071  -15.160 1.00 25.94 ? 525  NAG B O6    1 
HETATM 8305  O O7    . NAG R  4  .   ? 29.557  22.755  -21.489 1.00 24.92 ? 525  NAG B O7    1 
HETATM 8306  C C1    . FUC S  7  .   ? 27.553  19.366  -20.108 1.00 31.66 ? 526  FUC B C1    1 
HETATM 8307  C C2    . FUC S  7  .   ? 28.004  18.487  -21.280 1.00 33.29 ? 526  FUC B C2    1 
HETATM 8308  C C3    . FUC S  7  .   ? 28.552  17.151  -20.767 1.00 34.48 ? 526  FUC B C3    1 
HETATM 8309  C C4    . FUC S  7  .   ? 27.526  16.471  -19.856 1.00 34.94 ? 526  FUC B C4    1 
HETATM 8310  C C5    . FUC S  7  .   ? 27.108  17.426  -18.734 1.00 34.44 ? 526  FUC B C5    1 
HETATM 8311  C C6    . FUC S  7  .   ? 26.004  16.855  -17.866 1.00 35.14 ? 526  FUC B C6    1 
HETATM 8312  O O2    . FUC S  7  .   ? 29.008  19.160  -22.025 1.00 33.35 ? 526  FUC B O2    1 
HETATM 8313  O O3    . FUC S  7  .   ? 28.850  16.302  -21.865 1.00 35.50 ? 526  FUC B O3    1 
HETATM 8314  O O4    . FUC S  7  .   ? 26.386  16.099  -20.617 1.00 36.11 ? 526  FUC B O4    1 
HETATM 8315  O O5    . FUC S  7  .   ? 26.613  18.663  -19.295 1.00 32.99 ? 526  FUC B O5    1 
HETATM 8316  C C1    . BMA T  8  .   ? 31.566  13.402  -15.915 1.00 38.16 ? 527  BMA B C1    1 
HETATM 8317  C C2    . BMA T  8  .   ? 32.900  12.672  -15.741 1.00 39.34 ? 527  BMA B C2    1 
HETATM 8318  C C3    . BMA T  8  .   ? 32.705  11.163  -15.883 1.00 40.82 ? 527  BMA B C3    1 
HETATM 8319  C C4    . BMA T  8  .   ? 31.605  10.676  -14.940 1.00 40.34 ? 527  BMA B C4    1 
HETATM 8320  C C5    . BMA T  8  .   ? 30.328  11.492  -15.158 1.00 39.97 ? 527  BMA B C5    1 
HETATM 8321  C C6    . BMA T  8  .   ? 29.229  11.119  -14.181 1.00 41.03 ? 527  BMA B C6    1 
HETATM 8322  O O2    . BMA T  8  .   ? 33.440  12.966  -14.461 1.00 40.33 ? 527  BMA B O2    1 
HETATM 8323  O O3    . BMA T  8  .   ? 33.938  10.495  -15.565 1.00 42.65 ? 527  BMA B O3    1 
HETATM 8324  O O4    . BMA T  8  .   ? 31.344  9.302   -15.182 1.00 41.10 ? 527  BMA B O4    1 
HETATM 8325  O O5    . BMA T  8  .   ? 30.600  12.900  -14.977 1.00 39.02 ? 527  BMA B O5    1 
HETATM 8326  O O6    . BMA T  8  .   ? 29.596  11.441  -12.847 1.00 40.90 ? 527  BMA B O6    1 
HETATM 8327  C C1    . MAN U  6  .   ? 34.414  9.609   -16.538 1.00 44.62 ? 528  MAN B C1    1 
HETATM 8328  C C2    . MAN U  6  .   ? 35.602  8.816   -15.974 1.00 44.81 ? 528  MAN B C2    1 
HETATM 8329  C C3    . MAN U  6  .   ? 36.826  9.725   -15.818 1.00 45.30 ? 528  MAN B C3    1 
HETATM 8330  C C4    . MAN U  6  .   ? 37.140  10.420  -17.144 1.00 45.47 ? 528  MAN B C4    1 
HETATM 8331  C C5    . MAN U  6  .   ? 35.902  11.178  -17.632 1.00 45.91 ? 528  MAN B C5    1 
HETATM 8332  C C6    . MAN U  6  .   ? 36.106  11.823  -18.989 1.00 46.46 ? 528  MAN B C6    1 
HETATM 8333  O O2    . MAN U  6  .   ? 35.913  7.736   -16.840 1.00 45.91 ? 528  MAN B O2    1 
HETATM 8334  O O3    . MAN U  6  .   ? 37.946  8.959   -15.402 1.00 43.64 ? 528  MAN B O3    1 
HETATM 8335  O O4    . MAN U  6  .   ? 38.221  11.324  -16.966 1.00 46.23 ? 528  MAN B O4    1 
HETATM 8336  O O5    . MAN U  6  .   ? 34.782  10.271  -17.752 1.00 45.20 ? 528  MAN B O5    1 
HETATM 8337  O O6    . MAN U  6  .   ? 36.597  10.885  -19.936 1.00 46.55 ? 528  MAN B O6    1 
HETATM 8338  C C1    . NAG V  4  .   ? 46.092  28.811  7.006   1.00 15.51 ? 529  NAG B C1    1 
HETATM 8339  C C2    . NAG V  4  .   ? 45.854  27.760  8.102   1.00 18.96 ? 529  NAG B C2    1 
HETATM 8340  C C3    . NAG V  4  .   ? 44.362  27.467  8.264   1.00 20.16 ? 529  NAG B C3    1 
HETATM 8341  C C4    . NAG V  4  .   ? 43.659  28.787  8.563   1.00 19.84 ? 529  NAG B C4    1 
HETATM 8342  C C5    . NAG V  4  .   ? 43.890  29.705  7.360   1.00 18.36 ? 529  NAG B C5    1 
HETATM 8343  C C6    . NAG V  4  .   ? 43.170  31.039  7.407   1.00 17.02 ? 529  NAG B C6    1 
HETATM 8344  C C7    . NAG V  4  .   ? 47.654  26.212  8.486   1.00 22.01 ? 529  NAG B C7    1 
HETATM 8345  C C8    . NAG V  4  .   ? 48.336  24.899  8.131   1.00 22.24 ? 529  NAG B C8    1 
HETATM 8346  N N2    . NAG V  4  .   ? 46.573  26.542  7.785   1.00 20.62 ? 529  NAG B N2    1 
HETATM 8347  O O3    . NAG V  4  .   ? 44.161  26.532  9.342   1.00 22.68 ? 529  NAG B O3    1 
HETATM 8348  O O4    . NAG V  4  .   ? 42.253  28.581  8.801   1.00 22.94 ? 529  NAG B O4    1 
HETATM 8349  O O5    . NAG V  4  .   ? 45.299  29.989  7.245   1.00 14.22 ? 529  NAG B O5    1 
HETATM 8350  O O6    . NAG V  4  .   ? 43.399  31.770  6.209   1.00 16.98 ? 529  NAG B O6    1 
HETATM 8351  O O7    . NAG V  4  .   ? 48.109  26.918  9.391   1.00 23.85 ? 529  NAG B O7    1 
HETATM 8352  C C1    . NAG W  4  .   ? 41.719  29.349  9.828   1.00 28.28 ? 530  NAG B C1    1 
HETATM 8353  C C2    . NAG W  4  .   ? 40.191  29.318  9.775   1.00 29.06 ? 530  NAG B C2    1 
HETATM 8354  C C3    . NAG W  4  .   ? 39.596  30.076  10.975  1.00 32.38 ? 530  NAG B C3    1 
HETATM 8355  C C4    . NAG W  4  .   ? 40.237  29.647  12.309  1.00 34.37 ? 530  NAG B C4    1 
HETATM 8356  C C5    . NAG W  4  .   ? 41.767  29.647  12.193  1.00 33.57 ? 530  NAG B C5    1 
HETATM 8357  C C6    . NAG W  4  .   ? 42.471  29.122  13.435  1.00 33.79 ? 530  NAG B C6    1 
HETATM 8358  C C7    . NAG W  4  .   ? 39.262  29.204  7.551   1.00 27.77 ? 530  NAG B C7    1 
HETATM 8359  C C8    . NAG W  4  .   ? 38.240  29.865  6.641   1.00 27.55 ? 530  NAG B C8    1 
HETATM 8360  N N2    . NAG W  4  .   ? 39.749  29.942  8.542   1.00 27.56 ? 530  NAG B N2    1 
HETATM 8361  O O3    . NAG W  4  .   ? 38.196  29.841  11.031  1.00 31.69 ? 530  NAG B O3    1 
HETATM 8362  O O4    . NAG W  4  .   ? 39.836  30.564  13.352  1.00 38.73 ? 530  NAG B O4    1 
HETATM 8363  O O5    . NAG W  4  .   ? 42.181  28.825  11.080  1.00 30.21 ? 530  NAG B O5    1 
HETATM 8364  O O6    . NAG W  4  .   ? 42.366  27.708  13.533  1.00 35.91 ? 530  NAG B O6    1 
HETATM 8365  O O7    . NAG W  4  .   ? 39.600  28.037  7.351   1.00 28.57 ? 530  NAG B O7    1 
HETATM 8366  C C1    . BMA X  8  .   ? 38.980  30.073  14.330  1.00 42.61 ? 531  BMA B C1    1 
HETATM 8367  C C2    . BMA X  8  .   ? 38.881  31.078  15.482  1.00 43.76 ? 531  BMA B C2    1 
HETATM 8368  C C3    . BMA X  8  .   ? 37.899  30.557  16.529  1.00 44.98 ? 531  BMA B C3    1 
HETATM 8369  C C4    . BMA X  8  .   ? 36.547  30.259  15.877  1.00 45.70 ? 531  BMA B C4    1 
HETATM 8370  C C5    . BMA X  8  .   ? 36.709  29.346  14.651  1.00 45.97 ? 531  BMA B C5    1 
HETATM 8371  C C6    . BMA X  8  .   ? 35.411  29.247  13.875  1.00 47.50 ? 531  BMA B C6    1 
HETATM 8372  O O2    . BMA X  8  .   ? 38.425  32.329  14.987  1.00 44.79 ? 531  BMA B O2    1 
HETATM 8373  O O3    . BMA X  8  .   ? 37.731  31.531  17.548  1.00 44.82 ? 531  BMA B O3    1 
HETATM 8374  O O4    . BMA X  8  .   ? 35.689  29.636  16.821  1.00 46.54 ? 531  BMA B O4    1 
HETATM 8375  O O5    . BMA X  8  .   ? 37.690  29.889  13.735  1.00 43.98 ? 531  BMA B O5    1 
HETATM 8376  O O6    . BMA X  8  .   ? 35.162  30.504  13.213  1.00 49.52 ? 531  BMA B O6    1 
HETATM 8377  C C1    . MAN Y  6  .   ? 34.226  30.396  12.181  1.00 50.44 ? 532  MAN B C1    1 
HETATM 8378  C C2    . MAN Y  6  .   ? 34.352  31.610  11.249  1.00 50.76 ? 532  MAN B C2    1 
HETATM 8379  C C3    . MAN Y  6  .   ? 33.862  32.884  11.951  1.00 51.18 ? 532  MAN B C3    1 
HETATM 8380  C C4    . MAN Y  6  .   ? 32.454  32.680  12.518  1.00 51.29 ? 532  MAN B C4    1 
HETATM 8381  C C5    . MAN Y  6  .   ? 32.424  31.435  13.411  1.00 51.55 ? 532  MAN B C5    1 
HETATM 8382  C C6    . MAN Y  6  .   ? 31.036  31.107  13.923  1.00 52.18 ? 532  MAN B C6    1 
HETATM 8383  O O2    . MAN Y  6  .   ? 33.596  31.391  10.067  1.00 50.12 ? 532  MAN B O2    1 
HETATM 8384  O O3    . MAN Y  6  .   ? 33.855  33.968  11.033  1.00 50.81 ? 532  MAN B O3    1 
HETATM 8385  O O4    . MAN Y  6  .   ? 32.080  33.820  13.277  1.00 50.79 ? 532  MAN B O4    1 
HETATM 8386  O O5    . MAN Y  6  .   ? 32.890  30.284  12.671  1.00 51.21 ? 532  MAN B O5    1 
HETATM 8387  O O6    . MAN Y  6  .   ? 31.008  29.829  14.542  1.00 52.62 ? 532  MAN B O6    1 
HETATM 8388  C C1    . NDG Z  9  .   ? 22.093  63.318  -16.048 1.00 40.31 ? 533  NDG B C1    1 
HETATM 8389  C C2    . NDG Z  9  .   ? 21.408  64.256  -17.055 1.00 42.38 ? 533  NDG B C2    1 
HETATM 8390  C C3    . NDG Z  9  .   ? 19.893  64.371  -16.833 1.00 43.59 ? 533  NDG B C3    1 
HETATM 8391  C C4    . NDG Z  9  .   ? 19.258  62.998  -16.648 1.00 43.53 ? 533  NDG B C4    1 
HETATM 8392  C C5    . NDG Z  9  .   ? 19.984  62.275  -15.517 1.00 43.24 ? 533  NDG B C5    1 
HETATM 8393  C C6    . NDG Z  9  .   ? 19.373  60.907  -15.224 1.00 43.66 ? 533  NDG B C6    1 
HETATM 8394  C C7    . NDG Z  9  .   ? 22.981  65.962  -17.727 1.00 45.02 ? 533  NDG B C7    1 
HETATM 8395  C C8    . NDG Z  9  .   ? 23.368  67.427  -17.697 1.00 44.73 ? 533  NDG B C8    1 
HETATM 8396  O O     . NDG Z  9  .   ? 21.371  62.081  -15.881 1.00 42.30 ? 533  NDG B O     1 
HETATM 8397  O O3    . NDG Z  9  .   ? 19.284  65.020  -17.941 1.00 44.04 ? 533  NDG B O3    1 
HETATM 8398  O O4    . NDG Z  9  .   ? 17.871  63.116  -16.355 1.00 44.90 ? 533  NDG B O4    1 
HETATM 8399  O O6    . NDG Z  9  .   ? 19.113  60.738  -13.834 1.00 43.56 ? 533  NDG B O6    1 
HETATM 8400  O O7    . NDG Z  9  .   ? 23.581  65.180  -18.456 1.00 45.93 ? 533  NDG B O7    1 
HETATM 8401  N N2    . NDG Z  9  .   ? 21.979  65.588  -16.939 1.00 43.89 ? 533  NDG B N2    1 
HETATM 8402  C C1    . NAG AA 4  .   ? 34.945  27.074  -1.673  1.00 17.90 ? 534  NAG B C1    1 
HETATM 8403  C C2    . NAG AA 4  .   ? 33.493  27.416  -2.026  1.00 19.41 ? 534  NAG B C2    1 
HETATM 8404  C C3    . NAG AA 4  .   ? 32.625  26.151  -1.979  1.00 22.77 ? 534  NAG B C3    1 
HETATM 8405  C C4    . NAG AA 4  .   ? 33.256  24.993  -2.771  1.00 23.89 ? 534  NAG B C4    1 
HETATM 8406  C C5    . NAG AA 4  .   ? 34.734  24.813  -2.391  1.00 23.08 ? 534  NAG B C5    1 
HETATM 8407  C C6    . NAG AA 4  .   ? 35.451  23.778  -3.239  1.00 23.16 ? 534  NAG B C6    1 
HETATM 8408  C C7    . NAG AA 4  .   ? 32.654  29.613  -1.467  1.00 16.96 ? 534  NAG B C7    1 
HETATM 8409  C C8    . NAG AA 4  .   ? 31.789  30.426  -0.520  1.00 17.10 ? 534  NAG B C8    1 
HETATM 8410  N N2    . NAG AA 4  .   ? 32.986  28.386  -1.074  1.00 18.02 ? 534  NAG B N2    1 
HETATM 8411  O O3    . NAG AA 4  .   ? 31.344  26.443  -2.517  1.00 24.84 ? 534  NAG B O3    1 
HETATM 8412  O O4    . NAG AA 4  .   ? 32.536  23.773  -2.493  1.00 26.24 ? 534  NAG B O4    1 
HETATM 8413  O O5    . NAG AA 4  .   ? 35.442  26.061  -2.552  1.00 21.62 ? 534  NAG B O5    1 
HETATM 8414  O O6    . NAG AA 4  .   ? 35.694  24.262  -4.552  1.00 24.48 ? 534  NAG B O6    1 
HETATM 8415  O O7    . NAG AA 4  .   ? 33.011  30.096  -2.539  1.00 15.15 ? 534  NAG B O7    1 
HETATM 8416  O O     . HOH BA 10 .   ? 97.535  -1.081  -20.383 1.00 32.41 ? 534  HOH A O     1 
HETATM 8417  O O     . HOH BA 10 .   ? 59.332  12.894  -18.437 1.00 32.94 ? 535  HOH A O     1 
HETATM 8418  O O     . HOH BA 10 .   ? 62.473  3.290   -46.814 1.00 32.16 ? 536  HOH A O     1 
HETATM 8419  O O     . HOH BA 10 .   ? 58.447  7.260   -5.882  1.00 43.89 ? 537  HOH A O     1 
HETATM 8420  O O     . HOH BA 10 .   ? 60.715  -17.456 -9.533  1.00 38.41 ? 538  HOH A O     1 
HETATM 8421  O O     . HOH BA 10 .   ? 76.510  -30.483 -39.467 1.00 39.50 ? 539  HOH A O     1 
HETATM 8422  O O     . HOH BA 10 .   ? 57.013  8.941   -9.871  1.00 33.48 ? 540  HOH A O     1 
HETATM 8423  O O     . HOH BA 10 .   ? 95.235  -22.395 -35.439 1.00 33.05 ? 541  HOH A O     1 
HETATM 8424  O O     . HOH BA 10 .   ? 90.070  -23.106 -32.186 1.00 43.66 ? 542  HOH A O     1 
HETATM 8425  O O     . HOH BA 10 .   ? 51.012  11.954  -12.354 1.00 39.47 ? 543  HOH A O     1 
HETATM 8426  O O     . HOH BA 10 .   ? 83.217  -27.826 -31.499 1.00 28.69 ? 544  HOH A O     1 
HETATM 8427  O O     . HOH BA 10 .   ? 51.744  1.316   -9.884  1.00 19.19 ? 545  HOH A O     1 
HETATM 8428  O O     . HOH BA 10 .   ? 64.903  1.873   -46.180 1.00 25.73 ? 546  HOH A O     1 
HETATM 8429  O O     . HOH BA 10 .   ? 68.793  -3.687  -50.228 1.00 31.39 ? 547  HOH A O     1 
HETATM 8430  O O     . HOH BA 10 .   ? 61.191  12.915  -24.344 1.00 26.74 ? 548  HOH A O     1 
HETATM 8431  O O     . HOH BA 10 .   ? 46.569  7.517   -10.063 1.00 27.80 ? 549  HOH A O     1 
HETATM 8432  O O     . HOH BA 10 .   ? 62.336  11.128  -22.277 1.00 40.07 ? 550  HOH A O     1 
HETATM 8433  O O     . HOH BA 10 .   ? 77.741  7.295   -46.796 1.00 31.07 ? 551  HOH A O     1 
HETATM 8434  O O     . HOH BA 10 .   ? 82.553  -18.744 -59.429 1.00 44.00 ? 552  HOH A O     1 
HETATM 8435  O O     . HOH BA 10 .   ? 79.744  -20.072 -61.038 1.00 34.43 ? 553  HOH A O     1 
HETATM 8436  O O     . HOH BA 10 .   ? 64.109  -12.990 -4.858  1.00 41.16 ? 554  HOH A O     1 
HETATM 8437  O O     . HOH BA 10 .   ? 61.461  12.102  -42.412 1.00 34.35 ? 555  HOH A O     1 
HETATM 8438  O O     . HOH BA 10 .   ? 97.162  3.307   -41.518 1.00 35.17 ? 556  HOH A O     1 
HETATM 8439  O O     . HOH BA 10 .   ? 67.982  3.402   -8.041  1.00 36.22 ? 557  HOH A O     1 
HETATM 8440  O O     . HOH BA 10 .   ? 47.203  4.985   -9.818  1.00 33.25 ? 558  HOH A O     1 
HETATM 8441  O O     . HOH BA 10 .   ? 55.111  -8.854  -5.194  1.00 31.72 ? 559  HOH A O     1 
HETATM 8442  O O     . HOH BA 10 .   ? 48.709  13.123  -39.868 1.00 29.94 ? 560  HOH A O     1 
HETATM 8443  O O     . HOH BA 10 .   ? 67.354  -6.667  -6.922  1.00 29.76 ? 561  HOH A O     1 
HETATM 8444  O O     . HOH BA 10 .   ? 91.722  -26.818 -27.815 1.00 38.78 ? 562  HOH A O     1 
HETATM 8445  O O     . HOH BA 10 .   ? 60.516  17.235  -29.095 1.00 33.17 ? 563  HOH A O     1 
HETATM 8446  O O     . HOH BA 10 .   ? 61.709  9.797   -40.824 1.00 28.56 ? 564  HOH A O     1 
HETATM 8447  O O     . HOH BA 10 .   ? 84.345  -8.018  -12.815 1.00 42.05 ? 565  HOH A O     1 
HETATM 8448  O O     . HOH BA 10 .   ? 83.077  10.353  -36.666 1.00 34.52 ? 566  HOH A O     1 
HETATM 8449  O O     . HOH BA 10 .   ? 87.060  -8.204  -19.509 1.00 39.86 ? 567  HOH A O     1 
HETATM 8450  O O     . HOH BA 10 .   ? 70.832  -21.595 -8.144  1.00 40.86 ? 568  HOH A O     1 
HETATM 8451  O O     . HOH BA 10 .   ? 43.877  -14.024 -19.628 1.00 40.45 ? 569  HOH A O     1 
HETATM 8452  O O     . HOH BA 10 .   ? 40.043  13.099  -34.946 1.00 40.52 ? 570  HOH A O     1 
HETATM 8453  O O     . HOH BA 10 .   ? 88.269  -19.803 -13.994 1.00 36.91 ? 571  HOH A O     1 
HETATM 8454  O O     . HOH BA 10 .   ? 95.872  -20.710 -39.881 1.00 37.20 ? 572  HOH A O     1 
HETATM 8455  O O     . HOH BA 10 .   ? 40.094  -18.537 -32.108 1.00 37.37 ? 573  HOH A O     1 
HETATM 8456  O O     . HOH BA 10 .   ? 47.354  -2.210  -43.448 1.00 39.43 ? 574  HOH A O     1 
HETATM 8457  O O     . HOH BA 10 .   ? 76.560  -5.443  -7.587  1.00 47.25 ? 575  HOH A O     1 
HETATM 8458  O O     . HOH BA 10 .   ? 91.282  -6.436  -18.289 1.00 41.10 ? 576  HOH A O     1 
HETATM 8459  O O     . HOH BA 10 .   ? 68.853  1.654   -6.141  1.00 38.94 ? 577  HOH A O     1 
HETATM 8460  O O     . HOH BA 10 .   ? 61.527  -1.335  -5.402  1.00 36.40 ? 578  HOH A O     1 
HETATM 8461  O O     . HOH BA 10 .   ? 57.736  -24.022 -42.680 1.00 42.67 ? 579  HOH A O     1 
HETATM 8462  O O     . HOH BA 10 .   ? 39.061  -13.400 -17.347 1.00 33.48 ? 580  HOH A O     1 
HETATM 8463  O O     . HOH BA 10 .   ? 66.068  11.139  -15.712 1.00 36.42 ? 581  HOH A O     1 
HETATM 8464  O O     . HOH BA 10 .   ? 36.046  -3.802  -14.170 1.00 41.07 ? 582  HOH A O     1 
HETATM 8465  O O     . HOH BA 10 .   ? 75.721  -29.070 -27.302 1.00 39.09 ? 583  HOH A O     1 
HETATM 8466  O O     . HOH BA 10 .   ? 75.936  -13.932 -6.537  1.00 44.63 ? 584  HOH A O     1 
HETATM 8467  O O     . HOH BA 10 .   ? 34.656  -19.343 -31.620 1.00 36.42 ? 585  HOH A O     1 
HETATM 8468  O O     . HOH BA 10 .   ? 90.501  -1.083  -20.196 1.00 27.67 ? 586  HOH A O     1 
HETATM 8469  O O     . HOH BA 10 .   ? 58.165  -24.867 -36.402 1.00 29.36 ? 587  HOH A O     1 
HETATM 8470  O O     . HOH BA 10 .   ? 55.779  -17.183 -8.990  1.00 34.45 ? 588  HOH A O     1 
HETATM 8471  O O     . HOH BA 10 .   ? 70.540  -22.824 -52.819 1.00 42.37 ? 589  HOH A O     1 
HETATM 8472  O O     . HOH BA 10 .   ? 71.321  1.099   -24.084 1.00 8.71  ? 590  HOH A O     1 
HETATM 8473  O O     . HOH BA 10 .   ? 82.004  -27.246 -52.850 1.00 38.48 ? 591  HOH A O     1 
HETATM 8474  O O     . HOH BA 10 .   ? 62.781  -24.937 -34.192 1.00 34.46 ? 592  HOH A O     1 
HETATM 8475  O O     . HOH BA 10 .   ? 71.176  -6.396  -35.053 1.00 7.98  ? 593  HOH A O     1 
HETATM 8476  O O     . HOH BA 10 .   ? 71.121  -28.352 -31.934 1.00 35.45 ? 594  HOH A O     1 
HETATM 8477  O O     . HOH BA 10 .   ? 68.602  -5.309  -44.233 1.00 22.56 ? 595  HOH A O     1 
HETATM 8478  O O     . HOH BA 10 .   ? 62.766  13.544  -31.173 1.00 25.80 ? 596  HOH A O     1 
HETATM 8479  O O     . HOH BA 10 .   ? 75.042  13.551  -23.209 1.00 31.28 ? 597  HOH A O     1 
HETATM 8480  O O     . HOH BA 10 .   ? 39.852  7.708   -32.337 1.00 30.90 ? 598  HOH A O     1 
HETATM 8481  O O     . HOH BA 10 .   ? 89.074  -26.113 -48.627 1.00 28.74 ? 599  HOH A O     1 
HETATM 8482  O O     . HOH BA 10 .   ? 53.382  -2.610  -45.570 1.00 31.03 ? 600  HOH A O     1 
HETATM 8483  O O     . HOH BA 10 .   ? 88.579  9.398   -45.252 1.00 28.83 ? 601  HOH A O     1 
HETATM 8484  O O     . HOH BA 10 .   ? 64.363  -25.585 -22.753 1.00 24.76 ? 602  HOH A O     1 
HETATM 8485  O O     . HOH BA 10 .   ? 69.206  2.246   -45.372 1.00 32.26 ? 603  HOH A O     1 
HETATM 8486  O O     . HOH BA 10 .   ? 68.380  -1.577  -57.678 1.00 35.70 ? 604  HOH A O     1 
HETATM 8487  O O     . HOH BA 10 .   ? 102.605 -2.479  -38.264 1.00 29.60 ? 605  HOH A O     1 
HETATM 8488  O O     . HOH BA 10 .   ? 57.587  -24.402 -39.047 1.00 29.89 ? 606  HOH A O     1 
HETATM 8489  O O     . HOH BA 10 .   ? 39.171  11.875  -19.433 1.00 31.03 ? 607  HOH A O     1 
HETATM 8490  O O     . HOH BA 10 .   ? 68.901  -26.141 -35.192 1.00 29.43 ? 608  HOH A O     1 
HETATM 8491  O O     . HOH BA 10 .   ? 53.496  8.978   -37.320 1.00 26.15 ? 609  HOH A O     1 
HETATM 8492  O O     . HOH BA 10 .   ? 60.533  9.961   -13.065 1.00 31.38 ? 610  HOH A O     1 
HETATM 8493  O O     . HOH BA 10 .   ? 64.362  -27.435 -28.485 1.00 45.75 ? 611  HOH A O     1 
HETATM 8494  O O     . HOH BA 10 .   ? 87.569  -26.296 -21.955 1.00 33.72 ? 612  HOH A O     1 
HETATM 8495  O O     . HOH BA 10 .   ? 55.443  -0.003  -25.907 1.00 27.97 ? 613  HOH A O     1 
HETATM 8496  O O     . HOH BA 10 .   ? 61.782  -23.894 -44.529 1.00 25.98 ? 614  HOH A O     1 
HETATM 8497  O O     . HOH BA 10 .   ? 81.020  -13.794 -8.384  1.00 27.47 ? 615  HOH A O     1 
HETATM 8498  O O     . HOH BA 10 .   ? 43.681  18.221  -16.224 1.00 39.67 ? 616  HOH A O     1 
HETATM 8499  O O     . HOH BA 10 .   ? 102.011 -3.414  -45.249 1.00 30.69 ? 617  HOH A O     1 
HETATM 8500  O O     . HOH BA 10 .   ? 97.451  -20.671 -41.982 1.00 28.59 ? 618  HOH A O     1 
HETATM 8501  O O     . HOH BA 10 .   ? 81.501  -21.816 -26.649 1.00 25.49 ? 619  HOH A O     1 
HETATM 8502  O O     . HOH BA 10 .   ? 98.554  -3.964  -35.045 1.00 27.23 ? 620  HOH A O     1 
HETATM 8503  O O     . HOH BA 10 .   ? 42.854  -13.018 -17.054 1.00 34.42 ? 621  HOH A O     1 
HETATM 8504  O O     . HOH BA 10 .   ? 42.157  -0.398  -40.740 1.00 31.62 ? 622  HOH A O     1 
HETATM 8505  O O     . HOH BA 10 .   ? 80.549  -7.948  -59.241 1.00 30.76 ? 623  HOH A O     1 
HETATM 8506  O O     . HOH BA 10 .   ? 36.873  -17.623 -35.243 1.00 29.14 ? 624  HOH A O     1 
HETATM 8507  O O     . HOH BA 10 .   ? 59.430  -14.403 -38.588 1.00 7.37  ? 625  HOH A O     1 
HETATM 8508  O O     . HOH BA 10 .   ? 56.588  19.954  -35.729 1.00 28.28 ? 626  HOH A O     1 
HETATM 8509  O O     . HOH BA 10 .   ? 77.100  -24.400 -13.563 1.00 41.38 ? 627  HOH A O     1 
HETATM 8510  O O     . HOH BA 10 .   ? 95.951  -14.230 -47.424 1.00 30.58 ? 628  HOH A O     1 
HETATM 8511  O O     . HOH BA 10 .   ? 58.509  -20.148 -43.814 1.00 29.32 ? 629  HOH A O     1 
HETATM 8512  O O     . HOH BA 10 .   ? 94.413  -12.341 -48.641 1.00 38.03 ? 630  HOH A O     1 
HETATM 8513  O O     . HOH BA 10 .   ? 77.008  10.910  -11.755 1.00 41.66 ? 631  HOH A O     1 
HETATM 8514  O O     . HOH BA 10 .   ? 58.296  -26.005 -21.055 1.00 35.30 ? 632  HOH A O     1 
HETATM 8515  O O     . HOH BA 10 .   ? 63.086  -22.889 -26.774 1.00 31.43 ? 633  HOH A O     1 
HETATM 8516  O O     . HOH BA 10 .   ? 57.390  -2.939  -49.670 1.00 37.92 ? 634  HOH A O     1 
HETATM 8517  O O     . HOH BA 10 .   ? 80.995  -29.788 -48.751 1.00 34.13 ? 635  HOH A O     1 
HETATM 8518  O O     . HOH BA 10 .   ? 59.859  -16.092 -50.206 1.00 36.79 ? 636  HOH A O     1 
HETATM 8519  O O     . HOH BA 10 .   ? 40.005  -7.105  -17.182 1.00 35.33 ? 637  HOH A O     1 
HETATM 8520  O O     . HOH BA 10 .   ? 47.178  -15.676 -14.589 1.00 31.79 ? 638  HOH A O     1 
HETATM 8521  O O     . HOH BA 10 .   ? 87.758  9.813   -30.705 1.00 36.57 ? 639  HOH A O     1 
HETATM 8522  O O     . HOH BA 10 .   ? 63.406  14.179  -42.111 1.00 33.37 ? 640  HOH A O     1 
HETATM 8523  O O     . HOH BA 10 .   ? 52.045  -15.812 -45.304 1.00 29.20 ? 641  HOH A O     1 
HETATM 8524  O O     . HOH BA 10 .   ? 70.723  -0.561  -7.413  1.00 28.31 ? 642  HOH A O     1 
HETATM 8525  O O     . HOH BA 10 .   ? 90.885  -10.611 -15.924 1.00 42.41 ? 643  HOH A O     1 
HETATM 8526  O O     . HOH BA 10 .   ? 68.205  -7.340  -9.260  1.00 30.48 ? 644  HOH A O     1 
HETATM 8527  O O     . HOH BA 10 .   ? 59.485  1.289   -48.883 1.00 27.26 ? 645  HOH A O     1 
HETATM 8528  O O     . HOH BA 10 .   ? 44.996  14.834  -28.080 1.00 32.11 ? 646  HOH A O     1 
HETATM 8529  O O     . HOH BA 10 .   ? 54.495  -0.886  -44.175 1.00 37.69 ? 647  HOH A O     1 
HETATM 8530  O O     . HOH BA 10 .   ? 31.649  -1.288  -20.276 1.00 28.73 ? 648  HOH A O     1 
HETATM 8531  O O     . HOH BA 10 .   ? 53.760  -10.179 -47.557 1.00 34.80 ? 649  HOH A O     1 
HETATM 8532  O O     . HOH BA 10 .   ? 47.472  13.347  -33.101 1.00 35.27 ? 650  HOH A O     1 
HETATM 8533  O O     . HOH BA 10 .   ? 97.448  -17.159 -20.503 1.00 33.02 ? 651  HOH A O     1 
HETATM 8534  O O     . HOH BA 10 .   ? 81.284  -5.587  -13.724 1.00 31.41 ? 652  HOH A O     1 
HETATM 8535  O O     . HOH BA 10 .   ? 76.196  -29.115 -48.130 1.00 38.08 ? 653  HOH A O     1 
HETATM 8536  O O     . HOH BA 10 .   ? 80.013  -12.254 -10.189 1.00 38.37 ? 654  HOH A O     1 
HETATM 8537  O O     . HOH BA 10 .   ? 78.882  -17.982 -8.784  1.00 31.73 ? 655  HOH A O     1 
HETATM 8538  O O     . HOH BA 10 .   ? 97.416  -3.403  -19.083 1.00 35.45 ? 656  HOH A O     1 
HETATM 8539  O O     . HOH BA 10 .   ? 59.334  9.010   -24.630 1.00 40.73 ? 657  HOH A O     1 
HETATM 8540  O O     . HOH BA 10 .   ? 61.432  3.806   -6.956  1.00 29.64 ? 658  HOH A O     1 
HETATM 8541  O O     . HOH BA 10 .   ? 96.134  2.778   -26.515 1.00 37.77 ? 659  HOH A O     1 
HETATM 8542  O O     . HOH BA 10 .   ? 84.741  -26.905 -49.227 1.00 27.61 ? 660  HOH A O     1 
HETATM 8543  O O     . HOH BA 10 .   ? 82.303  -29.963 -53.504 1.00 38.16 ? 661  HOH A O     1 
HETATM 8544  O O     . HOH BA 10 .   ? 102.816 -7.187  -41.669 1.00 36.15 ? 662  HOH A O     1 
HETATM 8545  O O     . HOH BA 10 .   ? 89.243  -28.011 -23.586 1.00 37.71 ? 663  HOH A O     1 
HETATM 8546  O O     . HOH BA 10 .   ? 65.612  11.322  -19.158 1.00 36.04 ? 664  HOH A O     1 
HETATM 8547  O O     . HOH BA 10 .   ? 47.744  -16.931 -25.455 1.00 35.16 ? 665  HOH A O     1 
HETATM 8548  O O     . HOH BA 10 .   ? 82.599  -16.540 -63.605 1.00 37.39 ? 666  HOH A O     1 
HETATM 8549  O O     . HOH BA 10 .   ? 100.477 -10.868 -40.836 1.00 42.62 ? 667  HOH A O     1 
HETATM 8550  O O     . HOH BA 10 .   ? 69.982  -18.732 -50.223 1.00 29.17 ? 668  HOH A O     1 
HETATM 8551  O O     . HOH BA 10 .   ? 98.130  1.509   -36.738 1.00 35.02 ? 669  HOH A O     1 
HETATM 8552  O O     . HOH BA 10 .   ? 62.190  10.107  -44.045 1.00 33.86 ? 670  HOH A O     1 
HETATM 8553  O O     . HOH BA 10 .   ? 98.775  -15.143 -39.144 1.00 44.85 ? 671  HOH A O     1 
HETATM 8554  O O     . HOH BA 10 .   ? 97.264  -17.829 -44.340 1.00 42.81 ? 672  HOH A O     1 
HETATM 8555  O O     . HOH BA 10 .   ? 74.987  8.424   -8.664  1.00 38.30 ? 673  HOH A O     1 
HETATM 8556  O O     . HOH BA 10 .   ? 61.171  -10.214 -7.385  1.00 44.11 ? 674  HOH A O     1 
HETATM 8557  O O     . HOH BA 10 .   ? 89.606  7.394   -30.240 1.00 42.22 ? 675  HOH A O     1 
HETATM 8558  O O     . HOH BA 10 .   ? 61.149  -18.997 -14.919 1.00 32.90 ? 676  HOH A O     1 
HETATM 8559  O O     . HOH BA 10 .   ? 78.463  -1.845  -9.736  1.00 31.14 ? 677  HOH A O     1 
HETATM 8560  O O     . HOH BA 10 .   ? 55.663  -5.208  -49.860 1.00 37.36 ? 678  HOH A O     1 
HETATM 8561  O O     . HOH BA 10 .   ? 58.472  -7.616  -25.387 1.00 36.45 ? 679  HOH A O     1 
HETATM 8562  O O     . HOH BA 10 .   ? 44.216  6.948   -39.076 1.00 34.56 ? 680  HOH A O     1 
HETATM 8563  O O     . HOH BA 10 .   ? 85.103  12.347  -26.815 1.00 40.17 ? 681  HOH A O     1 
HETATM 8564  O O     . HOH BA 10 .   ? 62.548  -14.364 -9.401  1.00 37.52 ? 682  HOH A O     1 
HETATM 8565  O O     . HOH BA 10 .   ? 56.430  -26.971 -39.773 1.00 36.70 ? 683  HOH A O     1 
HETATM 8566  O O     . HOH BA 10 .   ? 93.624  2.795   -19.875 1.00 44.70 ? 684  HOH A O     1 
HETATM 8567  O O     . HOH BA 10 .   ? 90.601  -20.217 -18.089 1.00 38.19 ? 685  HOH A O     1 
HETATM 8568  O O     . HOH BA 10 .   ? 60.231  -33.321 -35.857 1.00 47.89 ? 686  HOH A O     1 
HETATM 8569  O O     . HOH BA 10 .   ? 63.588  15.378  -37.804 1.00 37.97 ? 687  HOH A O     1 
HETATM 8570  O O     . HOH BA 10 .   ? 79.670  3.962   -10.860 1.00 34.62 ? 688  HOH A O     1 
HETATM 8571  O O     . HOH BA 10 .   ? 43.853  -17.115 -24.710 1.00 35.06 ? 689  HOH A O     1 
HETATM 8572  O O     . HOH BA 10 .   ? 54.546  11.788  -22.994 1.00 30.43 ? 690  HOH A O     1 
HETATM 8573  O O     . HOH BA 10 .   ? 52.484  -6.757  -44.246 1.00 36.06 ? 691  HOH A O     1 
HETATM 8574  O O     . HOH BA 10 .   ? 53.240  -17.579 -12.145 1.00 30.06 ? 692  HOH A O     1 
HETATM 8575  O O     . HOH BA 10 .   ? 83.487  -20.362 -11.158 1.00 36.53 ? 693  HOH A O     1 
HETATM 8576  O O     . HOH BA 10 .   ? 67.097  -7.295  -22.385 1.00 6.89  ? 694  HOH A O     1 
HETATM 8577  O O     . HOH BA 10 .   ? 38.105  -6.203  -19.738 1.00 32.98 ? 695  HOH A O     1 
HETATM 8578  O O     . HOH BA 10 .   ? 86.732  -0.697  -16.239 1.00 33.90 ? 696  HOH A O     1 
HETATM 8579  O O     . HOH BA 10 .   ? 58.048  10.041  -43.722 1.00 29.63 ? 697  HOH A O     1 
HETATM 8580  O O     . HOH BA 10 .   ? 70.693  -24.659 -13.089 1.00 38.82 ? 698  HOH A O     1 
HETATM 8581  O O     . HOH BA 10 .   ? 54.513  -14.130 -36.908 1.00 7.97  ? 699  HOH A O     1 
HETATM 8582  O O     . HOH BA 10 .   ? 62.627  -3.675  -49.694 1.00 39.17 ? 700  HOH A O     1 
HETATM 8583  O O     . HOH BA 10 .   ? 86.386  -28.807 -46.795 1.00 36.64 ? 701  HOH A O     1 
HETATM 8584  O O     . HOH BA 10 .   ? 61.355  -20.673 -26.712 1.00 43.10 ? 702  HOH A O     1 
HETATM 8585  O O     . HOH BA 10 .   ? 69.334  -24.428 -17.176 1.00 36.09 ? 703  HOH A O     1 
HETATM 8586  O O     . HOH BA 10 .   ? 103.909 -11.022 -43.012 1.00 39.55 ? 704  HOH A O     1 
HETATM 8587  O O     . HOH BA 10 .   ? 57.025  -13.234 -37.556 1.00 7.80  ? 705  HOH A O     1 
HETATM 8588  O O     . HOH BA 10 .   ? 93.879  5.840   -20.279 1.00 44.17 ? 706  HOH A O     1 
HETATM 8589  O O     . HOH BA 10 .   ? 60.804  -10.073 -19.561 1.00 9.33  ? 707  HOH A O     1 
HETATM 8590  O O     . HOH BA 10 .   ? 70.885  3.262   -5.380  1.00 33.72 ? 708  HOH A O     1 
HETATM 8591  O O     . HOH BA 10 .   ? 47.579  -13.525 -20.401 1.00 19.85 ? 709  HOH A O     1 
HETATM 8592  O O     . HOH BA 10 .   ? 95.839  -29.473 -46.447 1.00 33.24 ? 710  HOH A O     1 
HETATM 8593  O O     . HOH BA 10 .   ? 63.053  9.519   -14.445 1.00 30.77 ? 711  HOH A O     1 
HETATM 8594  O O     . HOH BA 10 .   ? 58.201  -20.187 -28.904 1.00 35.17 ? 712  HOH A O     1 
HETATM 8595  O O     . HOH BA 10 .   ? 97.834  -18.019 -41.640 1.00 34.64 ? 713  HOH A O     1 
HETATM 8596  O O     . HOH BA 10 .   ? 49.876  -12.861 -17.954 1.00 32.08 ? 714  HOH A O     1 
HETATM 8597  O O     . HOH BA 10 .   ? 100.590 1.202   -37.513 1.00 41.61 ? 715  HOH A O     1 
HETATM 8598  O O     . HOH BA 10 .   ? 58.483  14.107  -16.199 1.00 36.92 ? 716  HOH A O     1 
HETATM 8599  O O     . HOH BA 10 .   ? 81.031  -9.723  -11.158 1.00 41.78 ? 717  HOH A O     1 
HETATM 8600  O O     . HOH BA 10 .   ? 38.476  14.401  -19.901 1.00 35.66 ? 718  HOH A O     1 
HETATM 8601  O O     . HOH BA 10 .   ? 81.057  -2.655  -9.263  1.00 38.60 ? 719  HOH A O     1 
HETATM 8602  O O     . HOH BA 10 .   ? 85.542  10.807  -38.379 1.00 37.54 ? 720  HOH A O     1 
HETATM 8603  O O     . HOH BA 10 .   ? 68.893  14.298  -16.144 1.00 32.42 ? 721  HOH A O     1 
HETATM 8604  O O     . HOH BA 10 .   ? 38.433  -11.373 -15.693 1.00 45.14 ? 722  HOH A O     1 
HETATM 8605  O O     . HOH BA 10 .   ? 70.109  -28.576 -25.655 1.00 43.25 ? 723  HOH A O     1 
HETATM 8606  O O     . HOH BA 10 .   ? 68.702  -23.622 -58.211 1.00 41.27 ? 724  HOH A O     1 
HETATM 8607  O O     . HOH BA 10 .   ? 89.202  7.807   -32.747 1.00 46.24 ? 725  HOH A O     1 
HETATM 8608  O O     . HOH BA 10 .   ? 74.978  13.748  -14.413 1.00 41.86 ? 726  HOH A O     1 
HETATM 8609  O O     . HOH BA 10 .   ? 86.504  10.772  -33.457 1.00 36.00 ? 727  HOH A O     1 
HETATM 8610  O O     . HOH BA 10 .   ? 76.349  12.318  -18.348 1.00 41.26 ? 728  HOH A O     1 
HETATM 8611  O O     . HOH BA 10 .   ? 66.328  6.391   -46.657 1.00 36.41 ? 729  HOH A O     1 
HETATM 8612  O O     . HOH BA 10 .   ? 72.060  16.922  -28.332 1.00 36.72 ? 730  HOH A O     1 
HETATM 8613  O O     . HOH BA 10 .   ? 70.454  -25.438 -50.562 1.00 40.41 ? 731  HOH A O     1 
HETATM 8614  O O     . HOH BA 10 .   ? 61.908  9.503   -16.928 1.00 35.00 ? 732  HOH A O     1 
HETATM 8615  O O     . HOH BA 10 .   ? 74.468  9.777   -48.315 1.00 31.12 ? 733  HOH A O     1 
HETATM 8616  O O     . HOH BA 10 .   ? 83.498  -25.494 -54.075 1.00 35.26 ? 734  HOH A O     1 
HETATM 8617  O O     . HOH BA 10 .   ? 82.752  -27.081 -22.086 1.00 41.10 ? 735  HOH A O     1 
HETATM 8618  O O     . HOH BA 10 .   ? 103.692 -9.396  -47.508 1.00 34.96 ? 736  HOH A O     1 
HETATM 8619  O O     . HOH BA 10 .   ? 41.620  8.234   -35.436 1.00 32.47 ? 737  HOH A O     1 
HETATM 8620  O O     . HOH BA 10 .   ? 67.006  -9.964  -55.595 1.00 37.01 ? 738  HOH A O     1 
HETATM 8621  O O     . HOH BA 10 .   ? 45.526  4.711   -39.812 1.00 43.95 ? 739  HOH A O     1 
HETATM 8622  O O     . HOH BA 10 .   ? 66.672  -4.999  -46.372 1.00 34.46 ? 740  HOH A O     1 
HETATM 8623  O O     . HOH BA 10 .   ? 63.064  -22.481 -15.037 1.00 39.00 ? 741  HOH A O     1 
HETATM 8624  O O     . HOH BA 10 .   ? 64.876  10.744  -45.166 1.00 39.04 ? 742  HOH A O     1 
HETATM 8625  O O     . HOH BA 10 .   ? 66.740  -12.582 -53.286 1.00 33.91 ? 743  HOH A O     1 
HETATM 8626  O O     . HOH BA 10 .   ? 77.770  16.130  -33.201 1.00 39.19 ? 744  HOH A O     1 
HETATM 8627  O O     . HOH BA 10 .   ? 61.279  -24.064 -37.265 1.00 33.61 ? 745  HOH A O     1 
HETATM 8628  O O     . HOH BA 10 .   ? 55.989  -24.739 -30.024 1.00 38.47 ? 746  HOH A O     1 
HETATM 8629  O O     . HOH BA 10 .   ? 79.639  1.488   -51.488 1.00 41.85 ? 747  HOH A O     1 
HETATM 8630  O O     . HOH BA 10 .   ? 73.468  -25.265 -59.285 1.00 42.46 ? 748  HOH A O     1 
HETATM 8631  O O     . HOH BA 10 .   ? 69.648  -12.601 -9.151  1.00 40.12 ? 749  HOH A O     1 
HETATM 8632  O O     . HOH BA 10 .   ? 79.431  -28.899 -46.696 1.00 37.40 ? 750  HOH A O     1 
HETATM 8633  O O     . HOH BA 10 .   ? 96.169  -23.366 -39.032 1.00 41.49 ? 751  HOH A O     1 
HETATM 8634  O O     . HOH BA 10 .   ? 74.123  14.132  -36.739 1.00 31.37 ? 752  HOH A O     1 
HETATM 8635  O O     . HOH BA 10 .   ? 84.085  -13.312 -54.360 1.00 41.04 ? 753  HOH A O     1 
HETATM 8636  O O     . HOH BA 10 .   ? 60.344  6.955   -45.293 1.00 31.22 ? 754  HOH A O     1 
HETATM 8637  O O     . HOH BA 10 .   ? 85.510  -5.337  -52.632 1.00 39.25 ? 755  HOH A O     1 
HETATM 8638  O O     . HOH BA 10 .   ? 83.627  -7.094  -53.541 1.00 37.84 ? 756  HOH A O     1 
HETATM 8639  O O     . HOH BA 10 .   ? 80.686  -26.992 -24.547 1.00 41.86 ? 757  HOH A O     1 
HETATM 8640  O O     . HOH BA 10 .   ? 46.172  -16.700 -23.269 1.00 34.57 ? 758  HOH A O     1 
HETATM 8641  O O     . HOH BA 10 .   ? 61.388  9.009   -9.177  1.00 41.11 ? 759  HOH A O     1 
HETATM 8642  O O     . HOH BA 10 .   ? 68.688  -28.750 -34.450 1.00 38.11 ? 760  HOH A O     1 
HETATM 8643  O O     . HOH BA 10 .   ? 92.376  -23.270 -30.923 1.00 48.49 ? 761  HOH A O     1 
HETATM 8644  O O     . HOH BA 10 .   ? 38.315  11.213  -34.477 1.00 38.98 ? 762  HOH A O     1 
HETATM 8645  O O     . HOH BA 10 .   ? 63.559  -28.256 -22.098 1.00 40.86 ? 763  HOH A O     1 
HETATM 8646  O O     . HOH BA 10 .   ? 29.730  2.863   -27.496 1.00 31.95 ? 764  HOH A O     1 
HETATM 8647  O O     . HOH BA 10 .   ? 54.827  14.470  -42.075 1.00 43.68 ? 765  HOH A O     1 
HETATM 8648  O O     . HOH BA 10 .   ? 81.594  14.473  -34.158 1.00 38.47 ? 766  HOH A O     1 
HETATM 8649  O O     . HOH BA 10 .   ? 46.564  12.873  -36.058 1.00 32.45 ? 767  HOH A O     1 
HETATM 8650  O O     . HOH BA 10 .   ? 96.182  0.650   -28.396 1.00 38.30 ? 768  HOH A O     1 
HETATM 8651  O O     . HOH BA 10 .   ? 53.563  -16.804 -7.379  1.00 44.33 ? 769  HOH A O     1 
HETATM 8652  O O     . HOH BA 10 .   ? 83.291  -31.004 -39.827 1.00 38.08 ? 770  HOH A O     1 
HETATM 8653  O O     . HOH BA 10 .   ? 34.113  -0.291  -15.334 1.00 37.45 ? 771  HOH A O     1 
HETATM 8654  O O     . HOH BA 10 .   ? 88.345  -18.354 -18.574 1.00 33.70 ? 772  HOH A O     1 
HETATM 8655  O O     . HOH BA 10 .   ? 92.221  -8.426  -16.946 1.00 45.63 ? 773  HOH A O     1 
HETATM 8656  O O     . HOH BA 10 .   ? 92.503  -20.444 -49.765 1.00 39.19 ? 774  HOH A O     1 
HETATM 8657  O O     . HOH BA 10 .   ? 91.329  -5.654  -51.667 1.00 35.71 ? 775  HOH A O     1 
HETATM 8658  O O     . HOH BA 10 .   ? 69.180  -1.024  -49.867 1.00 39.76 ? 776  HOH A O     1 
HETATM 8659  O O     . HOH BA 10 .   ? 73.435  -3.962  -36.726 1.00 7.22  ? 777  HOH A O     1 
HETATM 8660  O O     . HOH BA 10 .   ? 94.839  -17.701 -47.803 1.00 39.03 ? 778  HOH A O     1 
HETATM 8661  O O     . HOH BA 10 .   ? 71.528  0.291   -52.836 1.00 43.15 ? 779  HOH A O     1 
HETATM 8662  O O     . HOH BA 10 .   ? 34.486  4.037   -19.386 1.00 35.10 ? 780  HOH A O     1 
HETATM 8663  O O     . HOH BA 10 .   ? 84.938  -22.050 -58.007 1.00 43.33 ? 781  HOH A O     1 
HETATM 8664  O O     . HOH BA 10 .   ? 52.249  7.410   -9.410  1.00 35.56 ? 782  HOH A O     1 
HETATM 8665  O O     . HOH BA 10 .   ? 100.245 -13.502 -40.632 1.00 45.61 ? 783  HOH A O     1 
HETATM 8666  O O     . HOH BA 10 .   ? 58.973  -25.089 -32.232 1.00 38.32 ? 784  HOH A O     1 
HETATM 8667  O O     . HOH BA 10 .   ? 80.237  -16.970 -65.166 1.00 31.65 ? 785  HOH A O     1 
HETATM 8668  O O     . HOH BA 10 .   ? 100.832 -3.862  -19.814 1.00 40.75 ? 786  HOH A O     1 
HETATM 8669  O O     . HOH BA 10 .   ? 80.664  6.421   -45.340 1.00 38.98 ? 787  HOH A O     1 
HETATM 8670  O O     . HOH BA 10 .   ? 73.380  14.805  -34.060 1.00 47.03 ? 788  HOH A O     1 
HETATM 8671  O O     . HOH BA 10 .   ? 39.344  15.076  -29.099 1.00 37.51 ? 789  HOH A O     1 
HETATM 8672  O O     . HOH BA 10 .   ? 35.047  -2.464  -18.295 1.00 46.02 ? 790  HOH A O     1 
HETATM 8673  O O     . HOH BA 10 .   ? 101.637 0.372   -39.879 1.00 38.25 ? 791  HOH A O     1 
HETATM 8674  O O     . HOH BA 10 .   ? 86.239  -26.215 -18.515 1.00 47.38 ? 792  HOH A O     1 
HETATM 8675  O O     . HOH BA 10 .   ? 70.747  15.077  -38.419 1.00 38.19 ? 793  HOH A O     1 
HETATM 8676  O O     . HOH BA 10 .   ? 78.698  16.783  -28.124 1.00 43.42 ? 794  HOH A O     1 
HETATM 8677  O O     . HOH BA 10 .   ? 36.640  8.978   -34.366 1.00 38.70 ? 795  HOH A O     1 
HETATM 8678  O O     . HOH BA 10 .   ? 89.671  -16.189 -17.252 1.00 39.39 ? 796  HOH A O     1 
HETATM 8679  O O     . HOH BA 10 .   ? 86.733  -3.652  -54.676 1.00 45.29 ? 797  HOH A O     1 
HETATM 8680  O O     . HOH BA 10 .   ? 51.329  -8.085  -46.278 1.00 44.51 ? 798  HOH A O     1 
HETATM 8681  O O     . HOH BA 10 .   ? 77.440  11.816  -43.933 1.00 39.34 ? 799  HOH A O     1 
HETATM 8682  O O     . HOH BA 10 .   ? 95.400  -6.986  -51.509 1.00 40.81 ? 800  HOH A O     1 
HETATM 8683  O O     . HOH BA 10 .   ? 62.082  -14.253 -50.032 1.00 45.15 ? 801  HOH A O     1 
HETATM 8684  O O     . HOH BA 10 .   ? 48.369  8.775   -11.826 1.00 47.00 ? 802  HOH A O     1 
HETATM 8685  O O     . HOH BA 10 .   ? 75.241  -31.980 -42.145 1.00 45.56 ? 803  HOH A O     1 
HETATM 8686  O O     . HOH BA 10 .   ? 84.171  -30.367 -31.467 1.00 46.58 ? 804  HOH A O     1 
HETATM 8687  O O     . HOH BA 10 .   ? 59.303  9.806   -17.138 1.00 44.28 ? 805  HOH A O     1 
HETATM 8688  O O     . HOH BA 10 .   ? 74.498  13.677  -39.313 1.00 47.56 ? 806  HOH A O     1 
HETATM 8689  O O     . HOH BA 10 .   ? 95.938  2.622   -21.208 1.00 38.19 ? 807  HOH A O     1 
HETATM 8690  O O     . HOH BA 10 .   ? 51.045  10.353  -43.186 1.00 41.34 ? 808  HOH A O     1 
HETATM 8691  O O     . HOH BA 10 .   ? 72.936  -26.761 -18.430 1.00 42.04 ? 809  HOH A O     1 
HETATM 8692  O O     . HOH BA 10 .   ? 56.470  -6.574  -4.815  1.00 40.98 ? 810  HOH A O     1 
HETATM 8693  O O     . HOH BA 10 .   ? 52.491  15.859  -17.425 1.00 39.08 ? 811  HOH A O     1 
HETATM 8694  O O     . HOH BA 10 .   ? 72.506  -10.725 -8.524  1.00 32.91 ? 812  HOH A O     1 
HETATM 8695  O O     . HOH BA 10 .   ? 78.313  14.282  -38.496 1.00 47.62 ? 813  HOH A O     1 
HETATM 8696  O O     . HOH BA 10 .   ? 59.705  -18.022 -17.088 1.00 36.25 ? 814  HOH A O     1 
HETATM 8697  O O     . HOH BA 10 .   ? 97.772  4.625   -29.250 1.00 35.82 ? 815  HOH A O     1 
HETATM 8698  O O     . HOH BA 10 .   ? 32.460  1.988   -18.643 1.00 44.19 ? 816  HOH A O     1 
HETATM 8699  O O     . HOH BA 10 .   ? 86.385  -16.642 -50.809 1.00 39.83 ? 817  HOH A O     1 
HETATM 8700  O O     . HOH BA 10 .   ? 61.356  8.598   -23.152 1.00 40.35 ? 818  HOH A O     1 
HETATM 8701  O O     . HOH BA 10 .   ? 68.508  15.809  -22.584 1.00 40.59 ? 819  HOH A O     1 
HETATM 8702  O O     . HOH BA 10 .   ? 61.496  -18.664 -47.336 1.00 38.44 ? 820  HOH A O     1 
HETATM 8703  O O     . HOH BA 10 .   ? 56.361  -19.276 -45.110 1.00 39.21 ? 821  HOH A O     1 
HETATM 8704  O O     . HOH BA 10 .   ? 88.279  -19.026 -56.556 1.00 33.18 ? 822  HOH A O     1 
HETATM 8705  O O     . HOH BA 10 .   ? 73.039  -3.777  -55.493 1.00 33.48 ? 823  HOH A O     1 
HETATM 8706  O O     . HOH BA 10 .   ? 46.247  15.236  -30.691 1.00 38.73 ? 824  HOH A O     1 
HETATM 8707  O O     . HOH BA 10 .   ? 96.448  -17.398 -17.484 1.00 37.54 ? 825  HOH A O     1 
HETATM 8708  O O     . HOH BA 10 .   ? 60.682  -5.828  -40.988 1.00 5.89  ? 826  HOH A O     1 
HETATM 8709  O O     . HOH BA 10 .   ? 54.984  -23.540 -21.679 1.00 43.28 ? 827  HOH A O     1 
HETATM 8710  O O     . HOH BA 10 .   ? 71.026  13.366  -44.301 1.00 33.13 ? 828  HOH A O     1 
HETATM 8711  O O     . HOH BA 10 .   ? 67.504  5.551   -30.813 1.00 9.92  ? 829  HOH A O     1 
HETATM 8712  O O     . HOH BA 10 .   ? 57.859  -1.752  -37.922 1.00 8.23  ? 830  HOH A O     1 
HETATM 8713  O O     . HOH BA 10 .   ? 77.777  -7.699  -31.856 1.00 7.75  ? 831  HOH A O     1 
HETATM 8714  O O     . HOH BA 10 .   ? 51.281  -10.859 -6.780  1.00 10.07 ? 832  HOH A O     1 
HETATM 8715  O O     . HOH BA 10 .   ? 69.285  7.568   -27.449 1.00 9.94  ? 833  HOH A O     1 
HETATM 8716  O O     . HOH BA 10 .   ? 85.538  -22.939 -36.088 1.00 10.53 ? 834  HOH A O     1 
HETATM 8717  O O     . HOH BA 10 .   ? 71.138  -9.073  -34.312 1.00 7.31  ? 835  HOH A O     1 
HETATM 8718  O O     . HOH BA 10 .   ? 69.572  -15.732 -31.438 1.00 10.89 ? 836  HOH A O     1 
HETATM 8719  O O     . HOH BA 10 .   ? 57.217  -10.041 -15.440 1.00 9.27  ? 837  HOH A O     1 
HETATM 8720  O O     . HOH BA 10 .   ? 81.446  -13.900 -16.390 1.00 11.69 ? 838  HOH A O     1 
HETATM 8721  O O     . HOH BA 10 .   ? 64.285  1.136   -20.608 1.00 10.04 ? 839  HOH A O     1 
HETATM 8722  O O     . HOH BA 10 .   ? 68.839  -5.506  -33.906 1.00 10.74 ? 840  HOH A O     1 
HETATM 8723  O O     . HOH BA 10 .   ? 67.418  -10.975 -22.577 1.00 8.48  ? 841  HOH A O     1 
HETATM 8724  O O     . HOH BA 10 .   ? 55.356  -0.326  -19.677 1.00 9.75  ? 842  HOH A O     1 
HETATM 8725  O O     . HOH BA 10 .   ? 60.814  -11.663 -12.376 1.00 11.51 ? 843  HOH A O     1 
HETATM 8726  O O     . HOH BA 10 .   ? 90.886  -20.109 -29.687 1.00 11.59 ? 844  HOH A O     1 
HETATM 8727  O O     . HOH BA 10 .   ? 78.217  -7.990  -43.258 1.00 7.52  ? 845  HOH A O     1 
HETATM 8728  O O     . HOH BA 10 .   ? 56.196  -4.413  -10.157 1.00 9.19  ? 846  HOH A O     1 
HETATM 8729  O O     . HOH BA 10 .   ? 70.320  -20.655 -39.918 1.00 9.18  ? 847  HOH A O     1 
HETATM 8730  O O     . HOH BA 10 .   ? 73.165  -7.204  -50.006 1.00 12.50 ? 848  HOH A O     1 
HETATM 8731  O O     . HOH BA 10 .   ? 77.685  5.631   -36.825 1.00 10.66 ? 849  HOH A O     1 
HETATM 8732  O O     . HOH BA 10 .   ? 47.881  1.290   -36.302 1.00 10.26 ? 850  HOH A O     1 
HETATM 8733  O O     . HOH BA 10 .   ? 75.813  -7.494  -50.197 1.00 8.37  ? 851  HOH A O     1 
HETATM 8734  O O     . HOH BA 10 .   ? 54.194  -17.772 -31.026 1.00 13.95 ? 852  HOH A O     1 
HETATM 8735  O O     . HOH BA 10 .   ? 76.271  -5.464  -42.715 1.00 9.52  ? 853  HOH A O     1 
HETATM 8736  O O     . HOH BA 10 .   ? 48.849  -17.385 -42.586 1.00 13.79 ? 854  HOH A O     1 
HETATM 8737  O O     . HOH BA 10 .   ? 42.158  9.185   -25.367 1.00 13.03 ? 855  HOH A O     1 
HETATM 8738  O O     . HOH BA 10 .   ? 49.545  -9.433  -29.538 1.00 11.30 ? 856  HOH A O     1 
HETATM 8739  O O     . HOH BA 10 .   ? 38.890  2.175   -19.225 1.00 11.71 ? 857  HOH A O     1 
HETATM 8740  O O     . HOH BA 10 .   ? 74.064  -5.763  -38.563 1.00 8.02  ? 858  HOH A O     1 
HETATM 8741  O O     . HOH BA 10 .   ? 60.195  -17.072 -27.551 1.00 14.32 ? 859  HOH A O     1 
HETATM 8742  O O     . HOH BA 10 .   ? 96.048  -17.108 -30.787 1.00 13.42 ? 860  HOH A O     1 
HETATM 8743  O O     . HOH BA 10 .   ? 49.125  -3.010  -34.390 1.00 12.80 ? 861  HOH A O     1 
HETATM 8744  O O     . HOH BA 10 .   ? 51.432  -8.902  -31.465 1.00 12.30 ? 862  HOH A O     1 
HETATM 8745  O O     . HOH BA 10 .   ? 60.844  -8.395  -33.318 1.00 9.16  ? 863  HOH A O     1 
HETATM 8746  O O     . HOH BA 10 .   ? 50.484  -9.559  -41.577 1.00 14.37 ? 864  HOH A O     1 
HETATM 8747  O O     . HOH BA 10 .   ? 51.285  -3.411  -41.264 1.00 13.11 ? 865  HOH A O     1 
HETATM 8748  O O     . HOH BA 10 .   ? 65.797  -20.539 -29.619 1.00 14.45 ? 866  HOH A O     1 
HETATM 8749  O O     . HOH BA 10 .   ? 67.463  -15.235 -29.920 1.00 12.26 ? 867  HOH A O     1 
HETATM 8750  O O     . HOH BA 10 .   ? 49.611  -0.291  -38.011 1.00 13.31 ? 868  HOH A O     1 
HETATM 8751  O O     . HOH BA 10 .   ? 58.313  3.615   -40.560 1.00 9.81  ? 869  HOH A O     1 
HETATM 8752  O O     . HOH BA 10 .   ? 43.261  -14.372 -40.565 1.00 10.22 ? 870  HOH A O     1 
HETATM 8753  O O     . HOH BA 10 .   ? 99.336  -12.937 -27.477 1.00 10.84 ? 871  HOH A O     1 
HETATM 8754  O O     . HOH BA 10 .   ? 57.025  -19.687 -41.379 1.00 14.54 ? 872  HOH A O     1 
HETATM 8755  O O     . HOH BA 10 .   ? 57.145  3.578   -12.006 1.00 12.87 ? 873  HOH A O     1 
HETATM 8756  O O     . HOH BA 10 .   ? 43.558  -16.668 -29.554 1.00 13.63 ? 874  HOH A O     1 
HETATM 8757  O O     . HOH BA 10 .   ? 39.287  -12.537 -40.380 1.00 13.24 ? 875  HOH A O     1 
HETATM 8758  O O     . HOH BA 10 .   ? 48.958  -11.276 -43.108 1.00 12.77 ? 876  HOH A O     1 
HETATM 8759  O O     . HOH BA 10 .   ? 69.543  -16.467 -14.923 1.00 11.91 ? 877  HOH A O     1 
HETATM 8760  O O     . HOH BA 10 .   ? 81.059  -11.886 -12.661 1.00 16.07 ? 878  HOH A O     1 
HETATM 8761  O O     . HOH BA 10 .   ? 67.172  -7.490  -33.022 1.00 12.36 ? 879  HOH A O     1 
HETATM 8762  O O     . HOH BA 10 .   ? 74.691  -4.040  -45.373 1.00 13.66 ? 880  HOH A O     1 
HETATM 8763  O O     . HOH BA 10 .   ? 38.665  -3.694  -12.572 1.00 13.14 ? 881  HOH A O     1 
HETATM 8764  O O     . HOH BA 10 .   ? 39.562  -7.619  -24.338 1.00 13.00 ? 882  HOH A O     1 
HETATM 8765  O O     . HOH BA 10 .   ? 103.281 -4.579  -24.503 1.00 10.51 ? 883  HOH A O     1 
HETATM 8766  O O     . HOH BA 10 .   ? 65.271  -11.704 -30.001 1.00 11.62 ? 884  HOH A O     1 
HETATM 8767  O O     . HOH BA 10 .   ? 82.964  -15.617 -14.702 1.00 16.52 ? 885  HOH A O     1 
HETATM 8768  O O     . HOH BA 10 .   ? 43.161  -0.741  -10.337 1.00 15.42 ? 886  HOH A O     1 
HETATM 8769  O O     . HOH BA 10 .   ? 64.629  -20.238 -44.106 1.00 12.75 ? 887  HOH A O     1 
HETATM 8770  O O     . HOH BA 10 .   ? 70.920  0.539   -9.981  1.00 16.53 ? 888  HOH A O     1 
HETATM 8771  O O     . HOH BA 10 .   ? 63.542  -22.007 -37.124 1.00 16.35 ? 889  HOH A O     1 
HETATM 8772  O O     . HOH BA 10 .   ? 50.586  -9.368  -20.816 1.00 13.03 ? 890  HOH A O     1 
HETATM 8773  O O     . HOH BA 10 .   ? 95.485  -1.538  -27.025 1.00 13.34 ? 891  HOH A O     1 
HETATM 8774  O O     . HOH BA 10 .   ? 87.878  4.462   -42.087 1.00 13.79 ? 892  HOH A O     1 
HETATM 8775  O O     . HOH BA 10 .   ? 77.555  -3.293  -43.881 1.00 11.51 ? 893  HOH A O     1 
HETATM 8776  O O     . HOH BA 10 .   ? 74.161  10.008  -15.707 1.00 13.19 ? 894  HOH A O     1 
HETATM 8777  O O     . HOH BA 10 .   ? 59.610  3.362   -13.790 1.00 11.42 ? 895  HOH A O     1 
HETATM 8778  O O     . HOH BA 10 .   ? 64.929  -14.843 -16.163 1.00 12.69 ? 896  HOH A O     1 
HETATM 8779  O O     . HOH BA 10 .   ? 74.475  -1.334  -45.230 1.00 13.73 ? 897  HOH A O     1 
HETATM 8780  O O     . HOH BA 10 .   ? 82.061  -5.330  -49.969 1.00 14.57 ? 898  HOH A O     1 
HETATM 8781  O O     . HOH BA 10 .   ? 66.257  6.639   -39.261 1.00 12.64 ? 899  HOH A O     1 
HETATM 8782  O O     . HOH BA 10 .   ? 71.564  -7.144  -37.705 1.00 9.77  ? 900  HOH A O     1 
HETATM 8783  O O     . HOH BA 10 .   ? 70.193  7.963   -36.929 1.00 12.38 ? 901  HOH A O     1 
HETATM 8784  O O     . HOH BA 10 .   ? 84.384  -26.284 -36.867 1.00 14.60 ? 902  HOH A O     1 
HETATM 8785  O O     . HOH BA 10 .   ? 34.384  -2.561  -26.401 1.00 13.43 ? 903  HOH A O     1 
HETATM 8786  O O     . HOH BA 10 .   ? 68.590  -16.466 -17.465 1.00 15.04 ? 904  HOH A O     1 
HETATM 8787  O O     . HOH BA 10 .   ? 79.931  -1.886  -43.735 1.00 14.45 ? 905  HOH A O     1 
HETATM 8788  O O     . HOH BA 10 .   ? 73.725  -9.404  -19.697 1.00 14.31 ? 906  HOH A O     1 
HETATM 8789  O O     . HOH BA 10 .   ? 56.942  5.586   -37.768 1.00 16.72 ? 907  HOH A O     1 
HETATM 8790  O O     . HOH BA 10 .   ? 95.317  -5.614  -30.114 1.00 14.37 ? 908  HOH A O     1 
HETATM 8791  O O     . HOH BA 10 .   ? 102.397 -6.913  -25.770 1.00 11.46 ? 909  HOH A O     1 
HETATM 8792  O O     . HOH BA 10 .   ? 65.120  -12.965 -48.618 1.00 22.35 ? 910  HOH A O     1 
HETATM 8793  O O     . HOH BA 10 .   ? 46.436  2.538   -32.496 1.00 12.65 ? 911  HOH A O     1 
HETATM 8794  O O     . HOH BA 10 .   ? 51.260  9.675   -16.046 1.00 15.28 ? 912  HOH A O     1 
HETATM 8795  O O     . HOH BA 10 .   ? 55.657  6.467   -40.039 1.00 16.69 ? 913  HOH A O     1 
HETATM 8796  O O     . HOH BA 10 .   ? 79.442  -28.628 -42.307 1.00 21.10 ? 914  HOH A O     1 
HETATM 8797  O O     . HOH BA 10 .   ? 79.133  -12.381 -62.219 1.00 16.14 ? 915  HOH A O     1 
HETATM 8798  O O     . HOH BA 10 .   ? 73.131  12.633  -32.502 1.00 14.61 ? 916  HOH A O     1 
HETATM 8799  O O     . HOH BA 10 .   ? 71.550  -0.456  -48.536 1.00 15.86 ? 917  HOH A O     1 
HETATM 8800  O O     . HOH BA 10 .   ? 43.784  -12.780 -23.898 1.00 13.67 ? 918  HOH A O     1 
HETATM 8801  O O     . HOH BA 10 .   ? 78.629  -23.972 -23.232 1.00 14.91 ? 919  HOH A O     1 
HETATM 8802  O O     . HOH BA 10 .   ? 61.929  -2.956  -27.869 1.00 17.62 ? 920  HOH A O     1 
HETATM 8803  O O     . HOH BA 10 .   ? 82.986  -1.690  -47.893 1.00 15.98 ? 921  HOH A O     1 
HETATM 8804  O O     . HOH BA 10 .   ? 79.211  -23.146 -25.677 1.00 14.44 ? 922  HOH A O     1 
HETATM 8805  O O     . HOH BA 10 .   ? 75.950  0.845   -44.190 1.00 11.35 ? 923  HOH A O     1 
HETATM 8806  O O     . HOH BA 10 .   ? 74.359  -25.033 -43.014 1.00 14.98 ? 924  HOH A O     1 
HETATM 8807  O O     . HOH BA 10 .   ? 57.346  -17.278 -24.062 1.00 17.00 ? 925  HOH A O     1 
HETATM 8808  O O     . HOH BA 10 .   ? 77.580  10.745  -20.222 1.00 18.29 ? 926  HOH A O     1 
HETATM 8809  O O     . HOH BA 10 .   ? 64.323  -6.590  -47.607 1.00 13.74 ? 927  HOH A O     1 
HETATM 8810  O O     . HOH BA 10 .   ? 86.911  -26.354 -35.786 1.00 18.31 ? 928  HOH A O     1 
HETATM 8811  O O     . HOH BA 10 .   ? 44.598  5.870   -13.373 1.00 15.39 ? 929  HOH A O     1 
HETATM 8812  O O     . HOH BA 10 .   ? 49.146  16.288  -24.781 1.00 21.13 ? 930  HOH A O     1 
HETATM 8813  O O     . HOH BA 10 .   ? 46.900  13.407  -26.460 1.00 16.18 ? 931  HOH A O     1 
HETATM 8814  O O     . HOH BA 10 .   ? 41.440  -9.166  -14.195 1.00 13.21 ? 932  HOH A O     1 
HETATM 8815  O O     . HOH BA 10 .   ? 41.535  -10.741 -16.562 1.00 19.21 ? 933  HOH A O     1 
HETATM 8816  O O     . HOH BA 10 .   ? 82.216  1.626   -42.773 1.00 16.75 ? 934  HOH A O     1 
HETATM 8817  O O     . HOH BA 10 .   ? 34.358  -15.287 -32.425 1.00 16.48 ? 935  HOH A O     1 
HETATM 8818  O O     . HOH BA 10 .   ? 99.798  -5.019  -28.610 1.00 16.86 ? 936  HOH A O     1 
HETATM 8819  O O     . HOH BA 10 .   ? 98.646  -7.738  -32.363 1.00 20.01 ? 937  HOH A O     1 
HETATM 8820  O O     . HOH BA 10 .   ? 36.142  -4.749  -22.578 1.00 14.65 ? 938  HOH A O     1 
HETATM 8821  O O     . HOH BA 10 .   ? 102.395 -12.435 -37.084 1.00 17.98 ? 939  HOH A O     1 
HETATM 8822  O O     . HOH BA 10 .   ? 67.391  4.101   -14.522 1.00 21.28 ? 940  HOH A O     1 
HETATM 8823  O O     . HOH BA 10 .   ? 70.131  -16.212 -57.378 1.00 20.43 ? 941  HOH A O     1 
HETATM 8824  O O     . HOH BA 10 .   ? 54.739  -11.805 -45.696 1.00 16.75 ? 942  HOH A O     1 
HETATM 8825  O O     . HOH BA 10 .   ? 76.213  11.402  -14.682 1.00 22.13 ? 943  HOH A O     1 
HETATM 8826  O O     . HOH BA 10 .   ? 45.700  -1.966  -10.156 1.00 14.53 ? 944  HOH A O     1 
HETATM 8827  O O     . HOH BA 10 .   ? 54.913  6.835   -10.022 1.00 24.13 ? 945  HOH A O     1 
HETATM 8828  O O     . HOH BA 10 .   ? 77.586  -26.832 -25.918 1.00 17.02 ? 946  HOH A O     1 
HETATM 8829  O O     . HOH BA 10 .   ? 39.392  1.771   -9.235  1.00 16.22 ? 947  HOH A O     1 
HETATM 8830  O O     . HOH BA 10 .   ? 54.388  -14.576 -45.961 1.00 18.82 ? 948  HOH A O     1 
HETATM 8831  O O     . HOH BA 10 .   ? 33.903  -8.812  -37.920 1.00 22.98 ? 949  HOH A O     1 
HETATM 8832  O O     . HOH BA 10 .   ? 72.087  -15.720 -30.040 1.00 14.56 ? 950  HOH A O     1 
HETATM 8833  O O     . HOH BA 10 .   ? 68.234  -0.511  -46.587 1.00 22.51 ? 951  HOH A O     1 
HETATM 8834  O O     . HOH BA 10 .   ? 56.654  -21.906 -38.984 1.00 16.28 ? 952  HOH A O     1 
HETATM 8835  O O     . HOH BA 10 .   ? 44.719  -13.743 -15.080 1.00 21.91 ? 953  HOH A O     1 
HETATM 8836  O O     . HOH BA 10 .   ? 41.756  -15.543 -27.922 1.00 15.91 ? 954  HOH A O     1 
HETATM 8837  O O     . HOH BA 10 .   ? 69.665  7.278   -39.804 1.00 13.03 ? 955  HOH A O     1 
HETATM 8838  O O     . HOH BA 10 .   ? 39.299  -5.834  -37.833 1.00 14.13 ? 956  HOH A O     1 
HETATM 8839  O O     . HOH BA 10 .   ? 54.344  -19.240 -26.840 1.00 22.98 ? 957  HOH A O     1 
HETATM 8840  O O     . HOH BA 10 .   ? 62.791  9.737   -27.172 1.00 17.52 ? 958  HOH A O     1 
HETATM 8841  O O     . HOH BA 10 .   ? 96.728  -3.912  -28.228 1.00 17.27 ? 959  HOH A O     1 
HETATM 8842  O O     . HOH BA 10 .   ? 61.048  -15.322 -24.576 1.00 14.67 ? 960  HOH A O     1 
HETATM 8843  O O     . HOH BA 10 .   ? 45.084  -14.077 -10.987 1.00 17.40 ? 961  HOH A O     1 
HETATM 8844  O O     . HOH BA 10 .   ? 71.970  10.450  -33.908 1.00 14.63 ? 962  HOH A O     1 
HETATM 8845  O O     . HOH BA 10 .   ? 41.416  0.713   -29.760 1.00 14.77 ? 963  HOH A O     1 
HETATM 8846  O O     . HOH BA 10 .   ? 62.997  -16.766 -15.996 1.00 15.25 ? 964  HOH A O     1 
HETATM 8847  O O     . HOH BA 10 .   ? 98.520  -16.880 -28.673 1.00 19.13 ? 965  HOH A O     1 
HETATM 8848  O O     . HOH BA 10 .   ? 46.959  0.101   -34.065 1.00 16.27 ? 966  HOH A O     1 
HETATM 8849  O O     . HOH BA 10 .   ? 36.349  2.451   -9.666  1.00 20.99 ? 967  HOH A O     1 
HETATM 8850  O O     . HOH BA 10 .   ? 59.013  16.597  -35.265 1.00 23.86 ? 968  HOH A O     1 
HETATM 8851  O O     . HOH BA 10 .   ? 88.075  -27.521 -41.410 1.00 15.18 ? 969  HOH A O     1 
HETATM 8852  O O     . HOH BA 10 .   ? 46.559  -17.830 -27.862 1.00 21.64 ? 970  HOH A O     1 
HETATM 8853  O O     . HOH BA 10 .   ? 86.213  -15.908 -48.566 1.00 21.28 ? 971  HOH A O     1 
HETATM 8854  O O     . HOH BA 10 .   ? 100.378 -14.897 -30.425 1.00 19.45 ? 972  HOH A O     1 
HETATM 8855  O O     . HOH BA 10 .   ? 77.475  3.394   -14.087 1.00 17.21 ? 973  HOH A O     1 
HETATM 8856  O O     . HOH BA 10 .   ? 64.780  13.974  -39.902 1.00 20.69 ? 974  HOH A O     1 
HETATM 8857  O O     . HOH BA 10 .   ? 76.676  3.084   -45.845 1.00 18.44 ? 975  HOH A O     1 
HETATM 8858  O O     . HOH BA 10 .   ? 45.245  -18.941 -35.570 1.00 17.50 ? 976  HOH A O     1 
HETATM 8859  O O     . HOH BA 10 .   ? 65.555  -2.336  -47.445 1.00 18.49 ? 977  HOH A O     1 
HETATM 8860  O O     . HOH BA 10 .   ? 49.673  -23.802 -36.218 1.00 24.17 ? 978  HOH A O     1 
HETATM 8861  O O     . HOH BA 10 .   ? 82.718  -22.528 -56.614 1.00 20.69 ? 979  HOH A O     1 
HETATM 8862  O O     . HOH BA 10 .   ? 96.446  -22.304 -25.702 1.00 19.57 ? 980  HOH A O     1 
HETATM 8863  O O     . HOH BA 10 .   ? 37.576  0.267   -30.551 1.00 16.30 ? 981  HOH A O     1 
HETATM 8864  O O     . HOH BA 10 .   ? 55.526  -16.112 -12.229 1.00 23.11 ? 982  HOH A O     1 
HETATM 8865  O O     . HOH BA 10 .   ? 82.452  -8.449  -50.094 1.00 19.91 ? 983  HOH A O     1 
HETATM 8866  O O     . HOH BA 10 .   ? 80.629  4.351   -41.210 1.00 16.36 ? 984  HOH A O     1 
HETATM 8867  O O     . HOH BA 10 .   ? 41.739  -11.317 -22.649 1.00 18.29 ? 985  HOH A O     1 
HETATM 8868  O O     . HOH BA 10 .   ? 78.099  -6.932  -57.987 1.00 19.98 ? 986  HOH A O     1 
HETATM 8869  O O     . HOH BA 10 .   ? 44.296  8.019   -36.459 1.00 21.89 ? 987  HOH A O     1 
HETATM 8870  O O     . HOH BA 10 .   ? 73.192  -22.340 -59.461 1.00 16.57 ? 988  HOH A O     1 
HETATM 8871  O O     . HOH BA 10 .   ? 96.140  -1.452  -48.873 1.00 22.08 ? 989  HOH A O     1 
HETATM 8872  O O     . HOH BA 10 .   ? 50.250  -22.748 -39.011 1.00 25.74 ? 990  HOH A O     1 
HETATM 8873  O O     . HOH BA 10 .   ? 34.688  -2.446  -34.270 1.00 20.04 ? 991  HOH A O     1 
HETATM 8874  O O     . HOH BA 10 .   ? 48.838  10.886  -15.670 1.00 22.45 ? 992  HOH A O     1 
HETATM 8875  O O     . HOH BA 10 .   ? 84.342  -17.063 -52.148 1.00 17.53 ? 993  HOH A O     1 
HETATM 8876  O O     . HOH BA 10 .   ? 50.711  -14.642 -43.193 1.00 18.09 ? 994  HOH A O     1 
HETATM 8877  O O     . HOH BA 10 .   ? 91.496  2.649   -21.504 1.00 16.48 ? 995  HOH A O     1 
HETATM 8878  O O     . HOH BA 10 .   ? 63.921  11.983  -29.254 1.00 20.88 ? 996  HOH A O     1 
HETATM 8879  O O     . HOH BA 10 .   ? 68.037  -11.630 -11.255 1.00 22.48 ? 997  HOH A O     1 
HETATM 8880  O O     . HOH BA 10 .   ? 99.606  -18.264 -30.905 1.00 18.29 ? 998  HOH A O     1 
HETATM 8881  O O     . HOH BA 10 .   ? 83.796  -15.610 -59.437 1.00 21.32 ? 999  HOH A O     1 
HETATM 8882  O O     . HOH BA 10 .   ? 59.960  15.279  -32.953 1.00 21.61 ? 1000 HOH A O     1 
HETATM 8883  O O     . HOH BA 10 .   ? 36.704  -0.982  -15.373 1.00 20.43 ? 1001 HOH A O     1 
HETATM 8884  O O     . HOH BA 10 .   ? 89.066  1.474   -20.890 1.00 16.21 ? 1002 HOH A O     1 
HETATM 8885  O O     . HOH BA 10 .   ? 82.518  1.175   -17.856 1.00 22.86 ? 1003 HOH A O     1 
HETATM 8886  O O     . HOH BA 10 .   ? 45.767  8.258   -13.289 1.00 19.88 ? 1004 HOH A O     1 
HETATM 8887  O O     . HOH BA 10 .   ? 53.985  8.621   -40.351 1.00 21.05 ? 1005 HOH A O     1 
HETATM 8888  O O     . HOH BA 10 .   ? 89.005  -24.534 -34.936 1.00 21.88 ? 1006 HOH A O     1 
HETATM 8889  O O     . HOH BA 10 .   ? 87.192  -22.652 -33.847 1.00 18.62 ? 1007 HOH A O     1 
HETATM 8890  O O     . HOH BA 10 .   ? 94.503  -4.756  -39.608 1.00 17.73 ? 1008 HOH A O     1 
HETATM 8891  O O     . HOH BA 10 .   ? 66.472  -9.500  -10.270 1.00 15.34 ? 1009 HOH A O     1 
HETATM 8892  O O     . HOH BA 10 .   ? 62.297  0.688   -9.448  1.00 21.54 ? 1010 HOH A O     1 
HETATM 8893  O O     . HOH BA 10 .   ? 83.643  8.215   -35.104 1.00 18.17 ? 1011 HOH A O     1 
HETATM 8894  O O     . HOH BA 10 .   ? 57.124  -16.059 -48.562 1.00 25.54 ? 1012 HOH A O     1 
HETATM 8895  O O     . HOH BA 10 .   ? 95.040  1.982   -24.226 1.00 27.84 ? 1013 HOH A O     1 
HETATM 8896  O O     . HOH BA 10 .   ? 72.129  4.781   -9.512  1.00 22.98 ? 1014 HOH A O     1 
HETATM 8897  O O     . HOH BA 10 .   ? 56.815  -0.005  -45.669 1.00 14.60 ? 1015 HOH A O     1 
HETATM 8898  O O     . HOH BA 10 .   ? 42.848  13.460  -27.255 1.00 22.07 ? 1016 HOH A O     1 
HETATM 8899  O O     . HOH BA 10 .   ? 49.331  -14.167 -15.600 1.00 19.52 ? 1017 HOH A O     1 
HETATM 8900  O O     . HOH BA 10 .   ? 60.608  -17.642 -23.163 1.00 16.58 ? 1018 HOH A O     1 
HETATM 8901  O O     . HOH BA 10 .   ? 76.501  -3.886  -56.120 1.00 20.78 ? 1019 HOH A O     1 
HETATM 8902  O O     . HOH BA 10 .   ? 67.434  11.799  -21.195 1.00 21.27 ? 1020 HOH A O     1 
HETATM 8903  O O     . HOH BA 10 .   ? 79.452  6.039   -39.432 1.00 18.42 ? 1021 HOH A O     1 
HETATM 8904  O O     . HOH BA 10 .   ? 98.811  -6.623  -19.444 1.00 32.91 ? 1022 HOH A O     1 
HETATM 8905  O O     . HOH BA 10 .   ? 37.532  -11.538 -25.206 1.00 22.72 ? 1023 HOH A O     1 
HETATM 8906  O O     . HOH BA 10 .   ? 76.100  -27.750 -39.760 1.00 25.57 ? 1024 HOH A O     1 
HETATM 8907  O O     . HOH BA 10 .   ? 76.169  14.275  -34.943 1.00 21.17 ? 1025 HOH A O     1 
HETATM 8908  O O     . HOH BA 10 .   ? 39.036  1.890   -29.016 1.00 21.58 ? 1026 HOH A O     1 
HETATM 8909  O O     . HOH BA 10 .   ? 71.926  2.867   -45.221 1.00 21.94 ? 1027 HOH A O     1 
HETATM 8910  O O     . HOH BA 10 .   ? 66.536  8.368   -44.905 1.00 22.00 ? 1028 HOH A O     1 
HETATM 8911  O O     . HOH BA 10 .   ? 66.541  -24.371 -18.964 1.00 22.31 ? 1029 HOH A O     1 
HETATM 8912  O O     . HOH BA 10 .   ? 87.061  -7.299  -50.269 1.00 23.54 ? 1030 HOH A O     1 
HETATM 8913  O O     . HOH BA 10 .   ? 92.959  -24.251 -27.981 1.00 26.16 ? 1031 HOH A O     1 
HETATM 8914  O O     . HOH BA 10 .   ? 32.095  -7.531  -34.306 1.00 21.02 ? 1032 HOH A O     1 
HETATM 8915  O O     . HOH BA 10 .   ? 76.752  -17.874 -10.631 1.00 20.87 ? 1033 HOH A O     1 
HETATM 8916  O O     . HOH BA 10 .   ? 99.437  -6.878  -22.099 1.00 21.01 ? 1034 HOH A O     1 
HETATM 8917  O O     . HOH BA 10 .   ? 84.553  2.084   -44.222 1.00 21.21 ? 1035 HOH A O     1 
HETATM 8918  O O     . HOH BA 10 .   ? 98.588  -11.515 -25.125 1.00 18.92 ? 1036 HOH A O     1 
HETATM 8919  O O     . HOH BA 10 .   ? 81.661  -11.120 -54.206 1.00 25.22 ? 1037 HOH A O     1 
HETATM 8920  O O     . HOH BA 10 .   ? 79.989  2.109   -17.358 1.00 16.50 ? 1038 HOH A O     1 
HETATM 8921  O O     . HOH BA 10 .   ? 40.032  -1.793  -36.521 1.00 16.85 ? 1039 HOH A O     1 
HETATM 8922  O O     . HOH BA 10 .   ? 70.011  3.113   -9.829  1.00 22.95 ? 1040 HOH A O     1 
HETATM 8923  O O     . HOH BA 10 .   ? 85.355  11.031  -29.316 1.00 25.47 ? 1041 HOH A O     1 
HETATM 8924  O O     . HOH BA 10 .   ? 52.827  -11.658 -43.820 1.00 17.60 ? 1042 HOH A O     1 
HETATM 8925  O O     . HOH BA 10 .   ? 35.496  -15.295 -28.597 1.00 24.91 ? 1043 HOH A O     1 
HETATM 8926  O O     . HOH BA 10 .   ? 75.950  11.812  -40.563 1.00 19.59 ? 1044 HOH A O     1 
HETATM 8927  O O     . HOH BA 10 .   ? 49.129  -20.029 -42.829 1.00 18.22 ? 1045 HOH A O     1 
HETATM 8928  O O     . HOH BA 10 .   ? 57.298  -6.853  -22.388 1.00 18.13 ? 1046 HOH A O     1 
HETATM 8929  O O     . HOH BA 10 .   ? 36.324  1.972   -18.847 1.00 24.38 ? 1047 HOH A O     1 
HETATM 8930  O O     . HOH BA 10 .   ? 99.708  -2.697  -27.095 1.00 21.98 ? 1048 HOH A O     1 
HETATM 8931  O O     . HOH BA 10 .   ? 93.952  -24.873 -38.785 1.00 32.78 ? 1049 HOH A O     1 
HETATM 8932  O O     . HOH BA 10 .   ? 43.716  -16.893 -34.354 1.00 20.76 ? 1050 HOH A O     1 
HETATM 8933  O O     . HOH BA 10 .   ? 98.207  -9.870  -21.578 1.00 27.31 ? 1051 HOH A O     1 
HETATM 8934  O O     . HOH BA 10 .   ? 94.489  -8.680  -18.331 1.00 20.50 ? 1052 HOH A O     1 
HETATM 8935  O O     . HOH BA 10 .   ? 76.900  -12.516 -60.688 1.00 29.26 ? 1053 HOH A O     1 
HETATM 8936  O O     . HOH BA 10 .   ? 45.795  3.964   -11.811 1.00 25.58 ? 1054 HOH A O     1 
HETATM 8937  O O     . HOH BA 10 .   ? 101.115 -3.060  -42.455 1.00 25.75 ? 1055 HOH A O     1 
HETATM 8938  O O     . HOH BA 10 .   ? 72.819  -7.466  -10.963 1.00 18.16 ? 1056 HOH A O     1 
HETATM 8939  O O     . HOH BA 10 .   ? 35.484  5.229   -29.381 1.00 20.51 ? 1057 HOH A O     1 
HETATM 8940  O O     . HOH BA 10 .   ? 65.329  5.747   -14.559 1.00 19.61 ? 1058 HOH A O     1 
HETATM 8941  O O     . HOH BA 10 .   ? 95.522  -16.284 -45.396 1.00 26.26 ? 1059 HOH A O     1 
HETATM 8942  O O     . HOH BA 10 .   ? 82.560  -27.779 -35.503 1.00 20.03 ? 1060 HOH A O     1 
HETATM 8943  O O     . HOH BA 10 .   ? 83.523  10.821  -32.994 1.00 32.52 ? 1061 HOH A O     1 
HETATM 8944  O O     . HOH BA 10 .   ? 42.930  -7.779  -45.208 1.00 23.00 ? 1062 HOH A O     1 
HETATM 8945  O O     . HOH BA 10 .   ? 60.805  -5.394  -5.377  1.00 21.52 ? 1063 HOH A O     1 
HETATM 8946  O O     . HOH BA 10 .   ? 86.574  2.349   -16.892 1.00 24.01 ? 1064 HOH A O     1 
HETATM 8947  O O     . HOH BA 10 .   ? 69.543  -23.687 -48.627 1.00 21.91 ? 1065 HOH A O     1 
HETATM 8948  O O     . HOH BA 10 .   ? 37.005  -0.722  -34.315 1.00 19.37 ? 1066 HOH A O     1 
HETATM 8949  O O     . HOH BA 10 .   ? 95.662  -19.333 -21.962 1.00 25.58 ? 1067 HOH A O     1 
HETATM 8950  O O     . HOH BA 10 .   ? 70.481  -12.734 -54.043 1.00 22.34 ? 1068 HOH A O     1 
HETATM 8951  O O     . HOH BA 10 .   ? 57.320  -17.615 -15.607 1.00 19.76 ? 1069 HOH A O     1 
HETATM 8952  O O     . HOH BA 10 .   ? 43.159  -13.404 -12.855 1.00 16.75 ? 1070 HOH A O     1 
HETATM 8953  O O     . HOH BA 10 .   ? 28.997  -5.626  -30.858 1.00 16.22 ? 1071 HOH A O     1 
HETATM 8954  O O     . HOH BA 10 .   ? 37.900  -6.818  -22.425 1.00 17.45 ? 1072 HOH A O     1 
HETATM 8955  O O     . HOH BA 10 .   ? 58.273  6.188   -40.948 1.00 14.06 ? 1073 HOH A O     1 
HETATM 8956  O O     . HOH BA 10 .   ? 78.618  0.522   -43.368 1.00 14.34 ? 1074 HOH A O     1 
HETATM 8957  O O     . HOH BA 10 .   ? 52.800  -9.045  -42.859 1.00 16.72 ? 1075 HOH A O     1 
HETATM 8958  O O     . HOH BA 10 .   ? 49.532  -15.424 -10.067 1.00 17.11 ? 1076 HOH A O     1 
HETATM 8959  O O     . HOH BA 10 .   ? 48.097  20.356  -31.403 1.00 18.64 ? 1077 HOH A O     1 
HETATM 8960  O O     . HOH BA 10 .   ? 50.572  -12.200 -45.008 1.00 17.52 ? 1078 HOH A O     1 
HETATM 8961  O O     . HOH BA 10 .   ? 39.190  -10.228 -23.536 1.00 17.40 ? 1079 HOH A O     1 
HETATM 8962  O O     . HOH BA 10 .   ? 102.539 -9.007  -24.008 1.00 16.88 ? 1080 HOH A O     1 
HETATM 8963  O O     . HOH BA 10 .   ? 41.290  -4.003  -37.981 1.00 19.85 ? 1081 HOH A O     1 
HETATM 8964  O O     . HOH BA 10 .   ? 87.697  -28.900 -39.266 1.00 18.11 ? 1082 HOH A O     1 
HETATM 8965  O O     . HOH BA 10 .   ? 54.932  15.991  -21.681 1.00 17.79 ? 1083 HOH A O     1 
HETATM 8966  O O     . HOH BA 10 .   ? 63.315  5.806   -45.625 1.00 21.51 ? 1084 HOH A O     1 
HETATM 8967  O O     . HOH BA 10 .   ? 42.496  -14.960 -25.097 1.00 19.06 ? 1085 HOH A O     1 
HETATM 8968  O O     . HOH BA 10 .   ? 100.087 -6.135  -36.206 1.00 19.68 ? 1086 HOH A O     1 
HETATM 8969  O O     . HOH BA 10 .   ? 45.322  -14.018 -21.979 1.00 20.39 ? 1087 HOH A O     1 
HETATM 8970  O O     . HOH BA 10 .   ? 70.259  -21.941 -13.173 1.00 31.04 ? 1088 HOH A O     1 
HETATM 8971  O O     . HOH BA 10 .   ? 35.225  -15.075 -34.941 1.00 22.53 ? 1089 HOH A O     1 
HETATM 8972  O O     . HOH BA 10 .   ? 37.846  -14.388 -25.789 1.00 19.65 ? 1090 HOH A O     1 
HETATM 8973  O O     . HOH BA 10 .   ? 37.774  -4.031  -36.553 1.00 20.56 ? 1091 HOH A O     1 
HETATM 8974  O O     . HOH BA 10 .   ? 80.589  -20.524 -57.345 1.00 23.02 ? 1092 HOH A O     1 
HETATM 8975  O O     . HOH BA 10 .   ? 71.172  0.650   -46.162 1.00 22.16 ? 1093 HOH A O     1 
HETATM 8976  O O     . HOH BA 10 .   ? 70.531  -22.156 -59.823 1.00 21.80 ? 1094 HOH A O     1 
HETATM 8977  O O     . HOH BA 10 .   ? 83.843  -14.429 -51.949 1.00 20.89 ? 1095 HOH A O     1 
HETATM 8978  O O     . HOH BA 10 .   ? 65.922  -23.217 -29.495 1.00 25.19 ? 1096 HOH A O     1 
HETATM 8979  O O     . HOH BA 10 .   ? 80.065  9.807   -38.573 1.00 23.54 ? 1097 HOH A O     1 
HETATM 8980  O O     . HOH BA 10 .   ? 33.379  -5.301  -33.346 1.00 21.25 ? 1098 HOH A O     1 
HETATM 8981  O O     . HOH BA 10 .   ? 60.063  1.857   -8.446  1.00 23.53 ? 1099 HOH A O     1 
HETATM 8982  O O     . HOH BA 10 .   ? 35.452  -4.672  -35.752 1.00 20.42 ? 1100 HOH A O     1 
HETATM 8983  O O     . HOH BA 10 .   ? 87.316  -24.421 -49.778 1.00 20.60 ? 1101 HOH A O     1 
HETATM 8984  O O     . HOH BA 10 .   ? 89.025  1.822   -18.251 1.00 27.63 ? 1102 HOH A O     1 
HETATM 8985  O O     . HOH BA 10 .   ? 62.420  -19.497 -45.370 1.00 21.67 ? 1103 HOH A O     1 
HETATM 8986  O O     . HOH BA 10 .   ? 85.500  -16.743 -15.224 1.00 21.84 ? 1104 HOH A O     1 
HETATM 8987  O O     . HOH BA 10 .   ? 64.319  14.971  -35.294 1.00 22.57 ? 1105 HOH A O     1 
HETATM 8988  O O     . HOH BA 10 .   ? 93.678  -2.378  -18.878 1.00 23.10 ? 1106 HOH A O     1 
HETATM 8989  O O     . HOH BA 10 .   ? 72.674  1.164   -50.610 1.00 26.63 ? 1107 HOH A O     1 
HETATM 8990  O O     . HOH BA 10 .   ? 100.735 -0.197  -42.221 1.00 19.95 ? 1108 HOH A O     1 
HETATM 8991  O O     . HOH BA 10 .   ? 37.375  -6.413  -39.512 1.00 23.44 ? 1109 HOH A O     1 
HETATM 8992  O O     . HOH BA 10 .   ? 59.672  -2.481  -25.917 1.00 21.97 ? 1110 HOH A O     1 
HETATM 8993  O O     . HOH BA 10 .   ? 94.174  -19.733 -36.141 1.00 17.43 ? 1111 HOH A O     1 
HETATM 8994  O O     . HOH BA 10 .   ? 69.848  12.453  -19.848 1.00 23.58 ? 1112 HOH A O     1 
HETATM 8995  O O     . HOH BA 10 .   ? 51.012  -16.658 -13.372 1.00 25.23 ? 1113 HOH A O     1 
HETATM 8996  O O     . HOH BA 10 .   ? 87.156  -18.292 -52.411 1.00 25.20 ? 1114 HOH A O     1 
HETATM 8997  O O     . HOH BA 10 .   ? 87.549  -12.686 -16.130 1.00 19.81 ? 1115 HOH A O     1 
HETATM 8998  O O     . HOH BA 10 .   ? 51.797  -24.847 -33.112 1.00 27.90 ? 1116 HOH A O     1 
HETATM 8999  O O     . HOH BA 10 .   ? 74.559  11.284  -21.865 1.00 20.08 ? 1117 HOH A O     1 
HETATM 9000  O O     . HOH BA 10 .   ? 39.544  5.454   -12.584 1.00 24.83 ? 1118 HOH A O     1 
HETATM 9001  O O     . HOH BA 10 .   ? 39.503  -4.585  -17.830 1.00 25.82 ? 1119 HOH A O     1 
HETATM 9002  O O     . HOH BA 10 .   ? 84.703  9.032   -20.084 1.00 22.12 ? 1120 HOH A O     1 
HETATM 9003  O O     . HOH BA 10 .   ? 81.553  -27.578 -50.098 1.00 21.05 ? 1121 HOH A O     1 
HETATM 9004  O O     . HOH BA 10 .   ? 90.722  -22.399 -28.322 1.00 25.49 ? 1122 HOH A O     1 
HETATM 9005  O O     . HOH BA 10 .   ? 42.512  -3.377  -40.232 1.00 23.66 ? 1123 HOH A O     1 
HETATM 9006  O O     . HOH BA 10 .   ? 90.400  -29.511 -39.964 1.00 28.32 ? 1124 HOH A O     1 
HETATM 9007  O O     . HOH BA 10 .   ? 49.625  -16.428 -22.953 1.00 21.59 ? 1125 HOH A O     1 
HETATM 9008  O O     . HOH BA 10 .   ? 67.638  14.049  -40.216 1.00 23.92 ? 1126 HOH A O     1 
HETATM 9009  O O     . HOH BA 10 .   ? 43.969  12.185  -19.808 1.00 24.02 ? 1127 HOH A O     1 
HETATM 9010  O O     . HOH BA 10 .   ? 45.328  20.650  -30.897 1.00 26.76 ? 1128 HOH A O     1 
HETATM 9011  O O     . HOH BA 10 .   ? 86.811  8.069   -41.472 1.00 24.51 ? 1129 HOH A O     1 
HETATM 9012  O O     . HOH BA 10 .   ? 52.220  -1.852  -43.296 1.00 24.43 ? 1130 HOH A O     1 
HETATM 9013  O O     . HOH BA 10 .   ? 93.610  5.019   -46.159 1.00 27.85 ? 1131 HOH A O     1 
HETATM 9014  O O     . HOH BA 10 .   ? 55.067  -8.399  -49.496 1.00 21.18 ? 1132 HOH A O     1 
HETATM 9015  O O     . HOH BA 10 .   ? 93.859  -19.343 -38.832 1.00 20.97 ? 1133 HOH A O     1 
HETATM 9016  O O     . HOH BA 10 .   ? 85.185  -28.506 -38.418 1.00 36.10 ? 1134 HOH A O     1 
HETATM 9017  O O     . HOH BA 10 .   ? 76.296  -10.286 -59.577 1.00 24.36 ? 1135 HOH A O     1 
HETATM 9018  O O     . HOH BA 10 .   ? 54.519  -12.331 -6.143  1.00 35.17 ? 1136 HOH A O     1 
HETATM 9019  O O     . HOH BA 10 .   ? 91.501  -27.154 -25.011 1.00 30.40 ? 1137 HOH A O     1 
HETATM 9020  O O     . HOH BA 10 .   ? 59.653  -22.228 -35.993 1.00 21.11 ? 1138 HOH A O     1 
HETATM 9021  O O     . HOH BA 10 .   ? 103.289 -5.214  -20.687 1.00 23.00 ? 1139 HOH A O     1 
HETATM 9022  O O     . HOH BA 10 .   ? 54.924  -20.029 -29.494 1.00 22.92 ? 1140 HOH A O     1 
HETATM 9023  O O     . HOH BA 10 .   ? 85.220  -28.886 -44.150 1.00 25.30 ? 1141 HOH A O     1 
HETATM 9024  O O     . HOH BA 10 .   ? 75.518  -21.988 -61.259 1.00 28.00 ? 1142 HOH A O     1 
HETATM 9025  O O     . HOH BA 10 .   ? 37.608  -8.902  -40.771 1.00 20.45 ? 1143 HOH A O     1 
HETATM 9026  O O     . HOH BA 10 .   ? 72.186  -26.490 -21.052 1.00 26.95 ? 1144 HOH A O     1 
HETATM 9027  O O     . HOH BA 10 .   ? 83.139  -19.584 -13.972 1.00 27.48 ? 1145 HOH A O     1 
HETATM 9028  O O     . HOH BA 10 .   ? 83.364  -12.829 -14.036 1.00 24.01 ? 1146 HOH A O     1 
HETATM 9029  O O     . HOH BA 10 .   ? 38.355  4.426   -28.972 1.00 26.02 ? 1147 HOH A O     1 
HETATM 9030  O O     . HOH BA 10 .   ? 79.833  13.580  -36.088 1.00 24.86 ? 1148 HOH A O     1 
HETATM 9031  O O     . HOH BA 10 .   ? 68.251  -23.922 -30.621 1.00 24.40 ? 1149 HOH A O     1 
HETATM 9032  O O     . HOH BA 10 .   ? 59.861  2.374   -46.359 1.00 23.46 ? 1150 HOH A O     1 
HETATM 9033  O O     . HOH BA 10 .   ? 70.200  -17.724 -47.582 1.00 19.75 ? 1151 HOH A O     1 
HETATM 9034  O O     . HOH BA 10 .   ? 90.215  -16.760 -49.025 1.00 22.25 ? 1152 HOH A O     1 
HETATM 9035  O O     . HOH BA 10 .   ? 46.484  16.196  -24.628 1.00 20.23 ? 1153 HOH A O     1 
HETATM 9036  O O     . HOH BA 10 .   ? 57.587  10.336  -15.254 1.00 27.23 ? 1154 HOH A O     1 
HETATM 9037  O O     . HOH BA 10 .   ? 70.869  12.590  -41.416 1.00 27.54 ? 1155 HOH A O     1 
HETATM 9038  O O     . HOH BA 10 .   ? 63.504  -18.731 -26.400 1.00 21.87 ? 1156 HOH A O     1 
HETATM 9039  O O     . HOH BA 10 .   ? 81.708  -0.963  -50.024 1.00 26.62 ? 1157 HOH A O     1 
HETATM 9040  O O     . HOH BA 10 .   ? 32.919  -16.249 -28.683 1.00 22.51 ? 1158 HOH A O     1 
HETATM 9041  O O     . HOH BA 10 .   ? 42.154  5.606   -11.522 1.00 25.93 ? 1159 HOH A O     1 
HETATM 9042  O O     . HOH BA 10 .   ? 102.010 -7.695  -21.670 1.00 26.93 ? 1160 HOH A O     1 
HETATM 9043  O O     . HOH BA 10 .   ? 56.983  10.559  -12.543 1.00 29.28 ? 1161 HOH A O     1 
HETATM 9044  O O     . HOH BA 10 .   ? 78.426  1.435   -11.165 1.00 20.27 ? 1162 HOH A O     1 
HETATM 9045  O O     . HOH BA 10 .   ? 101.753 -17.511 -32.483 1.00 32.03 ? 1163 HOH A O     1 
HETATM 9046  O O     . HOH BA 10 .   ? 56.640  -5.904  -24.792 1.00 23.89 ? 1164 HOH A O     1 
HETATM 9047  O O     . HOH BA 10 .   ? 49.131  -14.023 -46.457 1.00 29.83 ? 1165 HOH A O     1 
HETATM 9048  O O     . HOH BA 10 .   ? 72.564  12.292  -19.715 1.00 30.74 ? 1166 HOH A O     1 
HETATM 9049  O O     . HOH BA 10 .   ? 50.218  -5.513  -42.574 1.00 26.27 ? 1167 HOH A O     1 
HETATM 9050  O O     . HOH BA 10 .   ? 86.704  8.183   -34.703 1.00 24.21 ? 1168 HOH A O     1 
HETATM 9051  O O     . HOH BA 10 .   ? 74.108  -9.439  -58.815 1.00 33.02 ? 1169 HOH A O     1 
HETATM 9052  O O     . HOH BA 10 .   ? 68.774  -23.575 -33.175 1.00 24.63 ? 1170 HOH A O     1 
HETATM 9053  O O     . HOH BA 10 .   ? 93.151  -18.727 -21.124 1.00 21.44 ? 1171 HOH A O     1 
HETATM 9054  O O     . HOH BA 10 .   ? 79.201  1.409   -14.302 1.00 23.66 ? 1172 HOH A O     1 
HETATM 9055  O O     . HOH BA 10 .   ? 92.220  7.224   -35.387 1.00 19.81 ? 1173 HOH A O     1 
HETATM 9056  O O     . HOH BA 10 .   ? 66.267  -18.018 -49.381 1.00 23.31 ? 1174 HOH A O     1 
HETATM 9057  O O     . HOH BA 10 .   ? 78.699  3.440   -43.147 1.00 23.98 ? 1175 HOH A O     1 
HETATM 9058  O O     . HOH BA 10 .   ? 65.865  -22.753 -26.266 1.00 22.54 ? 1176 HOH A O     1 
HETATM 9059  O O     . HOH BA 10 .   ? 79.817  -5.655  -8.091  1.00 26.67 ? 1177 HOH A O     1 
HETATM 9060  O O     . HOH BA 10 .   ? 93.695  -27.533 -40.039 1.00 34.28 ? 1178 HOH A O     1 
HETATM 9061  O O     . HOH BA 10 .   ? 100.237 -10.299 -23.560 1.00 26.84 ? 1179 HOH A O     1 
HETATM 9062  O O     . HOH BA 10 .   ? 102.473 -15.426 -36.846 1.00 23.76 ? 1180 HOH A O     1 
HETATM 9063  O O     . HOH BA 10 .   ? 82.688  -10.956 -51.804 1.00 24.68 ? 1181 HOH A O     1 
HETATM 9064  O O     . HOH BA 10 .   ? 98.517  -19.104 -24.468 1.00 26.49 ? 1182 HOH A O     1 
HETATM 9065  O O     . HOH BA 10 .   ? 48.166  16.431  -17.461 1.00 29.97 ? 1183 HOH A O     1 
HETATM 9066  O O     . HOH BA 10 .   ? 101.214 -18.013 -35.053 1.00 23.24 ? 1184 HOH A O     1 
HETATM 9067  O O     . HOH BA 10 .   ? 56.552  4.378   -7.467  1.00 27.53 ? 1185 HOH A O     1 
HETATM 9068  O O     . HOH BA 10 .   ? 71.637  -9.701  -58.023 1.00 24.74 ? 1186 HOH A O     1 
HETATM 9069  O O     . HOH BA 10 .   ? 43.026  10.541  -33.808 1.00 33.72 ? 1187 HOH A O     1 
HETATM 9070  O O     . HOH BA 10 .   ? 73.915  13.896  -25.637 1.00 26.37 ? 1188 HOH A O     1 
HETATM 9071  O O     . HOH BA 10 .   ? 42.752  -17.629 -39.867 1.00 26.46 ? 1189 HOH A O     1 
HETATM 9072  O O     . HOH BA 10 .   ? 32.409  -0.961  -26.612 1.00 22.58 ? 1190 HOH A O     1 
HETATM 9073  O O     . HOH BA 10 .   ? 100.074 -15.400 -26.754 1.00 24.14 ? 1191 HOH A O     1 
HETATM 9074  O O     . HOH BA 10 .   ? 73.591  -28.389 -31.004 1.00 27.77 ? 1192 HOH A O     1 
HETATM 9075  O O     . HOH BA 10 .   ? 91.934  -21.987 -34.111 1.00 29.57 ? 1193 HOH A O     1 
HETATM 9076  O O     . HOH BA 10 .   ? 41.619  5.691   -35.534 1.00 22.37 ? 1194 HOH A O     1 
HETATM 9077  O O     . HOH BA 10 .   ? 35.882  -10.390 -39.348 1.00 24.77 ? 1195 HOH A O     1 
HETATM 9078  O O     . HOH BA 10 .   ? 75.012  1.408   -49.505 1.00 23.45 ? 1196 HOH A O     1 
HETATM 9079  O O     . HOH BA 10 .   ? 82.610  5.508   -42.706 1.00 25.06 ? 1197 HOH A O     1 
HETATM 9080  O O     . HOH BA 10 .   ? 49.425  -0.860  -40.724 1.00 23.65 ? 1198 HOH A O     1 
HETATM 9081  O O     . HOH BA 10 .   ? 47.220  12.894  -17.778 1.00 31.64 ? 1199 HOH A O     1 
HETATM 9082  O O     . HOH BA 10 .   ? 88.832  -29.293 -44.313 1.00 29.71 ? 1200 HOH A O     1 
HETATM 9083  O O     . HOH BA 10 .   ? 54.762  18.739  -33.721 1.00 22.86 ? 1201 HOH A O     1 
HETATM 9084  O O     . HOH BA 10 .   ? 60.297  -20.134 -24.374 1.00 25.90 ? 1202 HOH A O     1 
HETATM 9085  O O     . HOH BA 10 .   ? 96.995  -5.596  -46.533 1.00 27.66 ? 1203 HOH A O     1 
HETATM 9086  O O     . HOH BA 10 .   ? 33.634  1.727   -10.617 1.00 25.08 ? 1204 HOH A O     1 
HETATM 9087  O O     . HOH BA 10 .   ? 72.749  -25.795 -52.932 1.00 24.19 ? 1205 HOH A O     1 
HETATM 9088  O O     . HOH BA 10 .   ? 79.874  14.993  -31.930 1.00 20.72 ? 1206 HOH A O     1 
HETATM 9089  O O     . HOH BA 10 .   ? 79.982  13.773  -28.304 1.00 24.55 ? 1207 HOH A O     1 
HETATM 9090  O O     . HOH BA 10 .   ? 71.100  -14.894 -9.824  1.00 29.50 ? 1208 HOH A O     1 
HETATM 9091  O O     . HOH BA 10 .   ? 88.158  8.920   -22.989 1.00 27.06 ? 1209 HOH A O     1 
HETATM 9092  O O     . HOH BA 10 .   ? 59.901  -4.426  -49.361 1.00 32.86 ? 1210 HOH A O     1 
HETATM 9093  O O     . HOH BA 10 .   ? 56.876  -0.716  -48.250 1.00 28.53 ? 1211 HOH A O     1 
HETATM 9094  O O     . HOH BA 10 .   ? 36.418  1.978   -32.457 1.00 26.33 ? 1212 HOH A O     1 
HETATM 9095  O O     . HOH BA 10 .   ? 75.722  -20.086 -9.541  1.00 28.30 ? 1213 HOH A O     1 
HETATM 9096  O O     . HOH BA 10 .   ? 75.080  -25.755 -15.318 1.00 21.43 ? 1214 HOH A O     1 
HETATM 9097  O O     . HOH BA 10 .   ? 43.780  -19.485 -37.645 1.00 26.59 ? 1215 HOH A O     1 
HETATM 9098  O O     . HOH BA 10 .   ? 68.299  -22.401 -15.828 1.00 26.50 ? 1216 HOH A O     1 
HETATM 9099  O O     . HOH BA 10 .   ? 37.563  -17.284 -28.721 1.00 24.56 ? 1217 HOH A O     1 
HETATM 9100  O O     . HOH BA 10 .   ? 91.307  6.581   -21.519 1.00 26.29 ? 1218 HOH A O     1 
HETATM 9101  O O     . HOH BA 10 .   ? 54.675  -17.545 -45.883 1.00 34.75 ? 1219 HOH A O     1 
HETATM 9102  O O     . HOH BA 10 .   ? 62.198  6.646   -7.938  1.00 29.85 ? 1220 HOH A O     1 
HETATM 9103  O O     . HOH BA 10 .   ? 42.661  -17.518 -31.990 1.00 32.65 ? 1221 HOH A O     1 
HETATM 9104  O O     . HOH BA 10 .   ? 82.440  -23.636 -18.628 1.00 22.95 ? 1222 HOH A O     1 
HETATM 9105  O O     . HOH BA 10 .   ? 77.377  -19.279 -62.264 1.00 31.06 ? 1223 HOH A O     1 
HETATM 9106  O O     . HOH BA 10 .   ? 69.457  16.042  -24.884 1.00 40.92 ? 1224 HOH A O     1 
HETATM 9107  O O     . HOH BA 10 .   ? 58.101  11.319  -29.769 1.00 34.76 ? 1225 HOH A O     1 
HETATM 9108  O O     . HOH BA 10 .   ? 84.883  -8.810  -51.797 1.00 31.05 ? 1226 HOH A O     1 
HETATM 9109  O O     . HOH BA 10 .   ? 35.486  -10.824 -23.466 1.00 30.65 ? 1227 HOH A O     1 
HETATM 9110  O O     . HOH BA 10 .   ? 82.026  7.324   -16.369 1.00 28.25 ? 1228 HOH A O     1 
HETATM 9111  O O     . HOH BA 10 .   ? 102.646 -12.687 -39.743 1.00 26.95 ? 1229 HOH A O     1 
HETATM 9112  O O     . HOH BA 10 .   ? 80.052  10.197  -13.505 1.00 27.32 ? 1230 HOH A O     1 
HETATM 9113  O O     . HOH BA 10 .   ? 85.051  -23.534 -26.960 1.00 34.65 ? 1231 HOH A O     1 
HETATM 9114  O O     . HOH BA 10 .   ? 84.935  3.182   -48.160 1.00 40.60 ? 1232 HOH A O     1 
HETATM 9115  O O     . HOH BA 10 .   ? 83.104  -21.819 -15.560 1.00 26.83 ? 1233 HOH A O     1 
HETATM 9116  O O     . HOH BA 10 .   ? 98.969  -20.535 -26.946 1.00 39.93 ? 1234 HOH A O     1 
HETATM 9117  O O     . HOH BA 10 .   ? 90.867  -13.909 -17.917 1.00 26.55 ? 1235 HOH A O     1 
HETATM 9118  O O     . HOH BA 10 .   ? 70.722  14.087  -26.210 1.00 22.16 ? 1236 HOH A O     1 
HETATM 9119  O O     . HOH BA 10 .   ? 72.401  4.335   -47.336 1.00 27.12 ? 1237 HOH A O     1 
HETATM 9120  O O     . HOH BA 10 .   ? 85.712  -24.427 -23.190 1.00 26.03 ? 1238 HOH A O     1 
HETATM 9121  O O     . HOH BA 10 .   ? 75.176  -27.546 -36.851 1.00 29.01 ? 1239 HOH A O     1 
HETATM 9122  O O     . HOH BA 10 .   ? 89.903  1.178   -53.381 1.00 25.46 ? 1240 HOH A O     1 
HETATM 9123  O O     . HOH BA 10 .   ? 72.900  -13.111 -9.763  1.00 27.25 ? 1241 HOH A O     1 
HETATM 9124  O O     . HOH BA 10 .   ? 46.209  -13.165 -17.896 1.00 30.16 ? 1242 HOH A O     1 
HETATM 9125  O O     . HOH BA 10 .   ? 81.152  10.805  -20.822 1.00 27.10 ? 1243 HOH A O     1 
HETATM 9126  O O     . HOH BA 10 .   ? 79.203  -10.067 -8.924  1.00 31.90 ? 1244 HOH A O     1 
HETATM 9127  O O     . HOH BA 10 .   ? 81.471  -12.370 -60.864 1.00 27.38 ? 1245 HOH A O     1 
HETATM 9128  O O     . HOH BA 10 .   ? 83.176  -14.501 -61.882 1.00 30.24 ? 1246 HOH A O     1 
HETATM 9129  O O     . HOH BA 10 .   ? 35.396  -15.446 -25.799 1.00 29.22 ? 1247 HOH A O     1 
HETATM 9130  O O     . HOH BA 10 .   ? 73.865  -26.049 -49.978 1.00 30.90 ? 1248 HOH A O     1 
HETATM 9131  O O     . HOH BA 10 .   ? 34.639  -6.308  -38.183 1.00 30.13 ? 1249 HOH A O     1 
HETATM 9132  O O     . HOH BA 10 .   ? 73.648  -17.109 -9.296  1.00 23.01 ? 1250 HOH A O     1 
HETATM 9133  O O     . HOH BA 10 .   ? 35.175  -0.276  -19.840 1.00 24.52 ? 1251 HOH A O     1 
HETATM 9134  O O     . HOH BA 10 .   ? 60.263  -16.584 -47.356 1.00 35.39 ? 1252 HOH A O     1 
HETATM 9135  O O     . HOH BA 10 .   ? 73.747  -4.722  -7.429  1.00 28.44 ? 1253 HOH A O     1 
HETATM 9136  O O     . HOH BA 10 .   ? 77.642  -29.440 -30.957 1.00 36.49 ? 1254 HOH A O     1 
HETATM 9137  O O     . HOH BA 10 .   ? 70.846  -7.862  -8.948  1.00 29.37 ? 1255 HOH A O     1 
HETATM 9138  O O     . HOH BA 10 .   ? 75.233  -27.798 -42.777 1.00 24.15 ? 1256 HOH A O     1 
HETATM 9139  O O     . HOH BA 10 .   ? 62.593  -15.491 -47.647 1.00 27.12 ? 1257 HOH A O     1 
HETATM 9140  O O     . HOH BA 10 .   ? 63.086  4.972   -24.785 1.00 27.67 ? 1258 HOH A O     1 
HETATM 9141  O O     . HOH BA 10 .   ? 43.999  10.282  -12.828 1.00 44.81 ? 1259 HOH A O     1 
HETATM 9142  O O     . HOH BA 10 .   ? 94.950  -5.101  -48.297 1.00 30.34 ? 1260 HOH A O     1 
HETATM 9143  O O     . HOH BA 10 .   ? 83.779  -0.649  -16.403 1.00 24.92 ? 1261 HOH A O     1 
HETATM 9144  O O     . HOH BA 10 .   ? 62.116  2.969   -23.369 1.00 13.17 ? 1262 HOH A O     1 
HETATM 9145  O O     . HOH BA 10 .   ? 69.900  -3.081  -43.380 1.00 15.05 ? 1263 HOH A O     1 
HETATM 9146  O O     . HOH BA 10 .   ? 49.651  4.951   -10.954 1.00 22.57 ? 1264 HOH A O     1 
HETATM 9147  O O     . HOH BA 10 .   ? 52.928  -14.531 -5.865  1.00 24.12 ? 1265 HOH A O     1 
HETATM 9148  O O     . HOH BA 10 .   ? 87.694  -15.241 -15.574 1.00 24.34 ? 1266 HOH A O     1 
HETATM 9149  O O     . HOH BA 10 .   ? 90.308  -24.762 -18.770 1.00 30.46 ? 1267 HOH A O     1 
HETATM 9150  O O     . HOH BA 10 .   ? 87.061  -18.990 -16.334 1.00 28.05 ? 1268 HOH A O     1 
HETATM 9151  O O     . HOH BA 10 .   ? 52.684  17.175  -34.356 1.00 24.56 ? 1269 HOH A O     1 
HETATM 9152  O O     . HOH BA 10 .   ? 66.347  -24.043 -45.244 1.00 29.78 ? 1270 HOH A O     1 
HETATM 9153  O O     . HOH BA 10 .   ? 59.093  15.488  -30.448 1.00 22.72 ? 1271 HOH A O     1 
HETATM 9154  O O     . HOH BA 10 .   ? 52.557  16.386  -20.338 1.00 25.33 ? 1272 HOH A O     1 
HETATM 9155  O O     . HOH BA 10 .   ? 89.599  -19.416 -50.118 1.00 31.75 ? 1273 HOH A O     1 
HETATM 9156  O O     . HOH BA 10 .   ? 62.462  13.728  -26.484 1.00 28.86 ? 1274 HOH A O     1 
HETATM 9157  O O     . HOH BA 10 .   ? 75.038  -8.750  -9.756  1.00 24.68 ? 1275 HOH A O     1 
HETATM 9158  O O     . HOH BA 10 .   ? 86.675  -8.814  -16.470 1.00 28.27 ? 1276 HOH A O     1 
HETATM 9159  O O     . HOH BA 10 .   ? 30.033  2.258   -31.112 1.00 24.22 ? 1277 HOH A O     1 
HETATM 9160  O O     . HOH BA 10 .   ? 30.837  -3.979  -32.697 1.00 34.40 ? 1278 HOH A O     1 
HETATM 9161  O O     . HOH BA 10 .   ? 66.632  -25.052 -34.652 1.00 30.85 ? 1279 HOH A O     1 
HETATM 9162  O O     . HOH BA 10 .   ? 78.399  6.201   -10.107 1.00 30.12 ? 1280 HOH A O     1 
HETATM 9163  O O     . HOH BA 10 .   ? 83.622  8.021   -42.160 1.00 27.03 ? 1281 HOH A O     1 
HETATM 9164  O O     . HOH BA 10 .   ? 80.408  -12.639 -57.973 1.00 29.89 ? 1282 HOH A O     1 
HETATM 9165  O O     . HOH BA 10 .   ? 80.710  -7.232  -11.596 1.00 28.38 ? 1283 HOH A O     1 
HETATM 9166  O O     . HOH BA 10 .   ? 77.982  -27.716 -44.365 1.00 25.80 ? 1284 HOH A O     1 
HETATM 9167  O O     . HOH BA 10 .   ? 58.574  -18.869 -25.964 1.00 32.20 ? 1285 HOH A O     1 
HETATM 9168  O O     . HOH BA 10 .   ? 72.486  -10.507 -55.801 1.00 28.12 ? 1286 HOH A O     1 
HETATM 9169  O O     . HOH BA 10 .   ? 56.682  3.284   -45.972 1.00 31.79 ? 1287 HOH A O     1 
HETATM 9170  O O     . HOH BA 10 .   ? 101.711 -12.624 -22.609 1.00 30.81 ? 1288 HOH A O     1 
HETATM 9171  O O     . HOH BA 10 .   ? 38.147  4.305   -32.336 1.00 31.42 ? 1289 HOH A O     1 
HETATM 9172  O O     . HOH BA 10 .   ? 67.736  -10.083 -52.976 1.00 29.95 ? 1290 HOH A O     1 
HETATM 9173  O O     . HOH BA 10 .   ? 58.163  -2.314  -7.440  1.00 33.07 ? 1291 HOH A O     1 
HETATM 9174  O O     . HOH BA 10 .   ? 74.980  3.634   -47.829 1.00 30.37 ? 1292 HOH A O     1 
HETATM 9175  O O     . HOH BA 10 .   ? 80.789  -3.721  -55.614 1.00 35.30 ? 1293 HOH A O     1 
HETATM 9176  O O     . HOH BA 10 .   ? 60.146  13.175  -29.739 1.00 27.42 ? 1294 HOH A O     1 
HETATM 9177  O O     . HOH BA 10 .   ? 93.044  -6.508  -49.647 1.00 30.96 ? 1295 HOH A O     1 
HETATM 9178  O O     . HOH BA 10 .   ? 101.374 -4.910  -38.572 1.00 29.84 ? 1296 HOH A O     1 
HETATM 9179  O O     . HOH BA 10 .   ? 67.659  3.944   -46.335 1.00 32.58 ? 1297 HOH A O     1 
HETATM 9180  O O     . HOH BA 10 .   ? 40.916  15.271  -26.955 1.00 26.23 ? 1298 HOH A O     1 
HETATM 9181  O O     . HOH BA 10 .   ? 62.404  -24.435 -24.632 1.00 27.28 ? 1299 HOH A O     1 
HETATM 9182  O O     . HOH BA 10 .   ? 101.176 -8.521  -39.794 1.00 30.33 ? 1300 HOH A O     1 
HETATM 9183  O O     . HOH BA 10 .   ? 48.605  15.348  -36.365 1.00 26.95 ? 1301 HOH A O     1 
HETATM 9184  O O     . HOH BA 10 .   ? 96.090  6.019   -26.713 1.00 29.95 ? 1302 HOH A O     1 
HETATM 9185  O O     . HOH BA 10 .   ? 37.656  14.653  -22.652 1.00 30.86 ? 1303 HOH A O     1 
HETATM 9186  O O     . HOH BA 10 .   ? 49.905  -16.296 -19.452 1.00 25.63 ? 1304 HOH A O     1 
HETATM 9187  O O     . HOH BA 10 .   ? 39.882  -15.032 -24.015 1.00 29.15 ? 1305 HOH A O     1 
HETATM 9188  O O     . HOH BA 10 .   ? 92.968  -16.632 -49.840 1.00 33.30 ? 1306 HOH A O     1 
HETATM 9189  O O     . HOH BA 10 .   ? 77.399  -1.354  -55.268 1.00 31.75 ? 1307 HOH A O     1 
HETATM 9190  O O     . HOH BA 10 .   ? 44.790  10.644  -35.794 1.00 31.93 ? 1308 HOH A O     1 
HETATM 9191  O O     . HOH BA 10 .   ? 65.398  5.935   -8.152  1.00 38.93 ? 1309 HOH A O     1 
HETATM 9192  O O     . HOH BA 10 .   ? 48.388  -24.217 -40.235 1.00 29.21 ? 1310 HOH A O     1 
HETATM 9193  O O     . HOH BA 10 .   ? 69.182  -21.886 -50.614 1.00 31.71 ? 1311 HOH A O     1 
HETATM 9194  O O     . HOH BA 10 .   ? 50.470  17.493  -16.615 1.00 28.61 ? 1312 HOH A O     1 
HETATM 9195  O O     . HOH BA 10 .   ? 83.365  5.181   -47.191 1.00 31.30 ? 1313 HOH A O     1 
HETATM 9196  O O     . HOH BA 10 .   ? 50.794  7.350   -11.588 1.00 27.12 ? 1314 HOH A O     1 
HETATM 9197  O O     . HOH BA 10 .   ? 53.262  -24.642 -30.958 1.00 29.10 ? 1315 HOH A O     1 
HETATM 9198  O O     . HOH BA 10 .   ? 77.012  1.694   -51.310 1.00 34.01 ? 1316 HOH A O     1 
HETATM 9199  O O     . HOH BA 10 .   ? 47.812  -23.135 -32.299 1.00 39.44 ? 1317 HOH A O     1 
HETATM 9200  O O     . HOH BA 10 .   ? 51.377  -17.277 -9.307  1.00 28.24 ? 1318 HOH A O     1 
HETATM 9201  O O     . HOH BA 10 .   ? 82.437  -29.324 -37.669 1.00 26.37 ? 1319 HOH A O     1 
HETATM 9202  O O     . HOH BA 10 .   ? 57.841  -17.611 -12.941 1.00 36.73 ? 1320 HOH A O     1 
HETATM 9203  O O     . HOH BA 10 .   ? 46.945  -15.822 -11.870 1.00 30.88 ? 1321 HOH A O     1 
HETATM 9204  O O     . HOH BA 10 .   ? 59.310  11.899  -26.055 1.00 30.53 ? 1322 HOH A O     1 
HETATM 9205  O O     . HOH BA 10 .   ? 41.173  -19.031 -36.916 1.00 39.78 ? 1323 HOH A O     1 
HETATM 9206  O O     . HOH BA 10 .   ? 82.620  -24.096 -25.638 1.00 34.59 ? 1324 HOH A O     1 
HETATM 9207  O O     . HOH BA 10 .   ? 64.483  -24.113 -35.977 1.00 40.42 ? 1325 HOH A O     1 
HETATM 9208  O O     . HOH BA 10 .   ? 58.584  0.130   -26.853 1.00 43.02 ? 1326 HOH A O     1 
HETATM 9209  O O     . HOH BA 10 .   ? 79.373  -25.874 -20.326 1.00 25.47 ? 1327 HOH A O     1 
HETATM 9210  O O     . HOH BA 10 .   ? 75.304  -28.961 -33.152 1.00 40.52 ? 1328 HOH A O     1 
HETATM 9211  O O     . HOH BA 10 .   ? 84.654  -24.918 -20.726 1.00 38.62 ? 1329 HOH A O     1 
HETATM 9212  O O     . HOH BA 10 .   ? 39.819  -0.226  -38.725 1.00 26.76 ? 1330 HOH A O     1 
HETATM 9213  O O     . HOH BA 10 .   ? 34.822  -0.137  -12.141 1.00 42.39 ? 1331 HOH A O     1 
HETATM 9214  O O     . HOH BA 10 .   ? 77.312  -8.324  -8.450  1.00 35.97 ? 1332 HOH A O     1 
HETATM 9215  O O     . HOH BA 10 .   ? 89.934  -3.210  -17.281 1.00 27.67 ? 1333 HOH A O     1 
HETATM 9216  O O     . HOH BA 10 .   ? 82.631  11.819  -17.675 1.00 37.48 ? 1334 HOH A O     1 
HETATM 9217  O O     . HOH BA 10 .   ? 80.681  4.526   -15.541 1.00 32.57 ? 1335 HOH A O     1 
HETATM 9218  O O     . HOH BA 10 .   ? 53.979  -22.417 -29.396 1.00 30.66 ? 1336 HOH A O     1 
HETATM 9219  O O     . HOH BA 10 .   ? 59.649  8.084   -42.472 1.00 27.74 ? 1337 HOH A O     1 
HETATM 9220  O O     . HOH BA 10 .   ? 96.339  -16.309 -40.369 1.00 28.14 ? 1338 HOH A O     1 
HETATM 9221  O O     . HOH BA 10 .   ? 74.953  13.617  -44.230 1.00 36.66 ? 1339 HOH A O     1 
HETATM 9222  O O     . HOH BA 10 .   ? 62.351  17.090  -33.004 1.00 40.97 ? 1340 HOH A O     1 
HETATM 9223  O O     . HOH BA 10 .   ? 57.603  -6.332  -51.414 1.00 33.52 ? 1341 HOH A O     1 
HETATM 9224  O O     . HOH BA 10 .   ? 40.010  -4.490  -43.039 1.00 31.68 ? 1342 HOH A O     1 
HETATM 9225  O O     . HOH BA 10 .   ? 97.361  3.654   -47.619 1.00 30.17 ? 1343 HOH A O     1 
HETATM 9226  O O     . HOH BA 10 .   ? 80.412  -10.157 -57.524 1.00 31.73 ? 1344 HOH A O     1 
HETATM 9227  O O     . HOH BA 10 .   ? 100.877 -22.617 -31.421 1.00 30.04 ? 1345 HOH A O     1 
HETATM 9228  O O     . HOH BA 10 .   ? 34.302  4.014   -31.439 1.00 38.54 ? 1346 HOH A O     1 
HETATM 9229  O O     . HOH BA 10 .   ? 82.712  -1.984  -14.283 1.00 33.32 ? 1347 HOH A O     1 
HETATM 9230  O O     . HOH BA 10 .   ? 67.319  -25.208 -47.492 1.00 34.23 ? 1348 HOH A O     1 
HETATM 9231  O O     . HOH BA 10 .   ? 56.585  -25.440 -23.030 1.00 44.25 ? 1349 HOH A O     1 
HETATM 9232  O O     . HOH BA 10 .   ? 76.088  15.812  -43.427 1.00 33.39 ? 1350 HOH A O     1 
HETATM 9233  O O     . HOH BA 10 .   ? 100.435 -20.503 -29.614 1.00 38.40 ? 1351 HOH A O     1 
HETATM 9234  O O     . HOH BA 10 .   ? 63.589  -24.904 -29.282 1.00 37.29 ? 1352 HOH A O     1 
HETATM 9235  O O     . HOH BA 10 .   ? 48.880  -18.997 -16.481 1.00 37.66 ? 1353 HOH A O     1 
HETATM 9236  O O     . HOH BA 10 .   ? 50.653  17.927  -14.031 1.00 31.85 ? 1366 HOH A O     1 
HETATM 9237  O O     . HOH BA 10 .   ? 62.969  16.068  -30.704 1.00 34.90 ? 1504 HOH A O     1 
HETATM 9238  O O     . HOH BA 10 .   ? 59.492  16.640  -16.121 1.00 44.31 ? 1584 HOH A O     1 
HETATM 9239  O O     . HOH CA 10 .   ? 37.964  7.523   -13.327 1.00 23.59 ? 535  HOH B O     1 
HETATM 9240  O O     . HOH CA 10 .   ? 39.316  11.590  -14.579 1.00 34.29 ? 590  HOH B O     1 
HETATM 9241  O O     . HOH CA 10 .   ? 36.172  7.272   -19.220 1.00 30.71 ? 625  HOH B O     1 
HETATM 9242  O O     . HOH CA 10 .   ? 36.551  14.083  -16.180 1.00 37.31 ? 826  HOH B O     1 
HETATM 9243  O O     . HOH CA 10 .   ? 36.076  36.883  -0.726  1.00 7.57  ? 829  HOH B O     1 
HETATM 9244  O O     . HOH CA 10 .   ? 45.471  26.078  -20.975 1.00 7.65  ? 830  HOH B O     1 
HETATM 9245  O O     . HOH CA 10 .   ? 53.344  38.712  -24.360 1.00 10.83 ? 831  HOH B O     1 
HETATM 9246  O O     . HOH CA 10 .   ? 36.011  35.276  6.519   1.00 11.48 ? 832  HOH B O     1 
HETATM 9247  O O     . HOH CA 10 .   ? 35.827  41.109  -22.020 1.00 8.53  ? 833  HOH B O     1 
HETATM 9248  O O     . HOH CA 10 .   ? 44.637  54.350  -8.646  1.00 11.29 ? 834  HOH B O     1 
HETATM 9249  O O     . HOH CA 10 .   ? 34.537  32.520  -19.667 1.00 8.04  ? 835  HOH B O     1 
HETATM 9250  O O     . HOH CA 10 .   ? 30.723  46.549  -0.831  1.00 9.28  ? 836  HOH B O     1 
HETATM 9251  O O     . HOH CA 10 .   ? 56.619  32.811  2.568   1.00 13.23 ? 837  HOH B O     1 
HETATM 9252  O O     . HOH CA 10 .   ? 48.428  39.353  -31.073 1.00 12.46 ? 838  HOH B O     1 
HETATM 9253  O O     . HOH CA 10 .   ? 29.655  32.781  -18.027 1.00 7.97  ? 839  HOH B O     1 
HETATM 9254  O O     . HOH CA 10 .   ? 39.684  48.087  -1.790  1.00 10.81 ? 840  HOH B O     1 
HETATM 9255  O O     . HOH CA 10 .   ? 48.733  42.725  -17.874 1.00 7.56  ? 841  HOH B O     1 
HETATM 9256  O O     . HOH CA 10 .   ? 29.320  29.109  -12.133 1.00 11.56 ? 842  HOH B O     1 
HETATM 9257  O O     . HOH CA 10 .   ? 44.774  31.084  -12.541 1.00 11.60 ? 843  HOH B O     1 
HETATM 9258  O O     . HOH CA 10 .   ? 32.575  36.935  3.407   1.00 10.76 ? 844  HOH B O     1 
HETATM 9259  O O     . HOH CA 10 .   ? 49.264  40.856  -19.717 1.00 8.61  ? 845  HOH B O     1 
HETATM 9260  O O     . HOH CA 10 .   ? 46.841  39.575  -18.790 1.00 8.77  ? 846  HOH B O     1 
HETATM 9261  O O     . HOH CA 10 .   ? 46.388  37.761  -15.421 1.00 8.24  ? 847  HOH B O     1 
HETATM 9262  O O     . HOH CA 10 .   ? 52.970  38.929  -13.015 1.00 8.63  ? 848  HOH B O     1 
HETATM 9263  O O     . HOH CA 10 .   ? 33.225  45.173  -18.992 1.00 10.17 ? 849  HOH B O     1 
HETATM 9264  O O     . HOH CA 10 .   ? 40.828  26.334  -10.654 1.00 11.61 ? 850  HOH B O     1 
HETATM 9265  O O     . HOH CA 10 .   ? 42.352  39.522  -3.471  1.00 7.65  ? 851  HOH B O     1 
HETATM 9266  O O     . HOH CA 10 .   ? 42.657  35.879  -3.759  1.00 9.14  ? 852  HOH B O     1 
HETATM 9267  O O     . HOH CA 10 .   ? 26.585  36.033  12.143  1.00 9.24  ? 853  HOH B O     1 
HETATM 9268  O O     . HOH CA 10 .   ? 23.025  48.234  -17.371 1.00 11.80 ? 854  HOH B O     1 
HETATM 9269  O O     . HOH CA 10 .   ? 31.468  42.385  8.761   1.00 10.71 ? 855  HOH B O     1 
HETATM 9270  O O     . HOH CA 10 .   ? 51.129  39.156  -31.337 1.00 8.52  ? 856  HOH B O     1 
HETATM 9271  O O     . HOH CA 10 .   ? 32.191  33.698  -18.668 1.00 7.80  ? 857  HOH B O     1 
HETATM 9272  O O     . HOH CA 10 .   ? 46.662  47.962  -5.294  1.00 10.63 ? 858  HOH B O     1 
HETATM 9273  O O     . HOH CA 10 .   ? 33.768  50.503  -21.748 1.00 10.44 ? 859  HOH B O     1 
HETATM 9274  O O     . HOH CA 10 .   ? 25.600  37.494  -22.628 1.00 15.30 ? 860  HOH B O     1 
HETATM 9275  O O     . HOH CA 10 .   ? 51.580  41.218  -23.802 1.00 10.41 ? 861  HOH B O     1 
HETATM 9276  O O     . HOH CA 10 .   ? 35.484  29.941  -8.601  1.00 15.12 ? 862  HOH B O     1 
HETATM 9277  O O     . HOH CA 10 .   ? 44.131  41.305  -15.026 1.00 12.71 ? 863  HOH B O     1 
HETATM 9278  O O     . HOH CA 10 .   ? 36.077  38.450  -14.426 1.00 10.71 ? 864  HOH B O     1 
HETATM 9279  O O     . HOH CA 10 .   ? 24.911  37.467  -10.620 1.00 14.76 ? 865  HOH B O     1 
HETATM 9280  O O     . HOH CA 10 .   ? 46.382  32.097  9.047   1.00 31.36 ? 866  HOH B O     1 
HETATM 9281  O O     . HOH CA 10 .   ? 42.681  31.599  -10.970 1.00 12.07 ? 867  HOH B O     1 
HETATM 9282  O O     . HOH CA 10 .   ? 42.856  52.391  -12.077 1.00 9.98  ? 868  HOH B O     1 
HETATM 9283  O O     . HOH CA 10 .   ? 24.393  44.012  -15.478 1.00 13.27 ? 869  HOH B O     1 
HETATM 9284  O O     . HOH CA 10 .   ? 49.884  42.642  -26.584 1.00 12.60 ? 870  HOH B O     1 
HETATM 9285  O O     . HOH CA 10 .   ? 32.129  27.130  -22.411 1.00 13.36 ? 871  HOH B O     1 
HETATM 9286  O O     . HOH CA 10 .   ? 40.540  35.200  -11.125 1.00 11.33 ? 872  HOH B O     1 
HETATM 9287  O O     . HOH CA 10 .   ? 32.630  50.425  6.936   1.00 11.99 ? 873  HOH B O     1 
HETATM 9288  O O     . HOH CA 10 .   ? 52.875  43.338  -25.026 1.00 9.38  ? 874  HOH B O     1 
HETATM 9289  O O     . HOH CA 10 .   ? 49.298  21.559  -24.082 1.00 11.98 ? 875  HOH B O     1 
HETATM 9290  O O     . HOH CA 10 .   ? 24.821  46.685  -18.958 1.00 12.51 ? 876  HOH B O     1 
HETATM 9291  O O     . HOH CA 10 .   ? 39.560  40.226  -28.700 1.00 13.44 ? 877  HOH B O     1 
HETATM 9292  O O     . HOH CA 10 .   ? 26.530  43.745  -22.271 1.00 12.80 ? 878  HOH B O     1 
HETATM 9293  O O     . HOH CA 10 .   ? 14.808  39.425  -5.442  1.00 12.62 ? 879  HOH B O     1 
HETATM 9294  O O     . HOH CA 10 .   ? 44.671  30.399  4.001   1.00 10.98 ? 880  HOH B O     1 
HETATM 9295  O O     . HOH CA 10 .   ? 39.625  26.611  -25.087 1.00 11.84 ? 881  HOH B O     1 
HETATM 9296  O O     . HOH CA 10 .   ? 52.919  57.502  -1.599  1.00 18.16 ? 882  HOH B O     1 
HETATM 9297  O O     . HOH CA 10 .   ? 25.930  37.416  -1.940  1.00 13.11 ? 883  HOH B O     1 
HETATM 9298  O O     . HOH CA 10 .   ? 38.669  24.802  -18.048 1.00 15.21 ? 884  HOH B O     1 
HETATM 9299  O O     . HOH CA 10 .   ? 42.332  39.336  -14.189 1.00 11.29 ? 885  HOH B O     1 
HETATM 9300  O O     . HOH CA 10 .   ? 37.420  49.868  -4.511  1.00 15.19 ? 886  HOH B O     1 
HETATM 9301  O O     . HOH CA 10 .   ? 66.021  26.535  -10.784 1.00 15.83 ? 887  HOH B O     1 
HETATM 9302  O O     . HOH CA 10 .   ? 60.560  23.533  -17.217 1.00 12.50 ? 888  HOH B O     1 
HETATM 9303  O O     . HOH CA 10 .   ? 32.317  52.637  -18.876 1.00 13.51 ? 889  HOH B O     1 
HETATM 9304  O O     . HOH CA 10 .   ? 52.945  52.355  -18.054 1.00 12.20 ? 890  HOH B O     1 
HETATM 9305  O O     . HOH CA 10 .   ? 14.238  49.212  -0.129  1.00 14.68 ? 891  HOH B O     1 
HETATM 9306  O O     . HOH CA 10 .   ? 46.287  47.409  8.775   1.00 13.14 ? 892  HOH B O     1 
HETATM 9307  O O     . HOH CA 10 .   ? 43.770  30.540  1.462   1.00 18.24 ? 893  HOH B O     1 
HETATM 9308  O O     . HOH CA 10 .   ? 19.007  34.265  -4.906  1.00 13.20 ? 894  HOH B O     1 
HETATM 9309  O O     . HOH CA 10 .   ? 34.926  50.175  5.186   1.00 12.46 ? 895  HOH B O     1 
HETATM 9310  O O     . HOH CA 10 .   ? 21.062  44.919  8.769   1.00 12.65 ? 896  HOH B O     1 
HETATM 9311  O O     . HOH CA 10 .   ? 49.589  56.838  2.992   1.00 14.39 ? 897  HOH B O     1 
HETATM 9312  O O     . HOH CA 10 .   ? 17.653  56.258  -6.263  1.00 15.38 ? 898  HOH B O     1 
HETATM 9313  O O     . HOH CA 10 .   ? 18.633  30.422  -10.680 1.00 15.15 ? 899  HOH B O     1 
HETATM 9314  O O     . HOH CA 10 .   ? 42.826  51.031  4.318   1.00 14.59 ? 900  HOH B O     1 
HETATM 9315  O O     . HOH CA 10 .   ? 74.555  33.744  -8.619  1.00 14.65 ? 901  HOH B O     1 
HETATM 9316  O O     . HOH CA 10 .   ? 45.029  54.004  -21.089 1.00 13.78 ? 902  HOH B O     1 
HETATM 9317  O O     . HOH CA 10 .   ? 41.688  37.446  8.588   1.00 12.31 ? 903  HOH B O     1 
HETATM 9318  O O     . HOH CA 10 .   ? 18.416  32.732  -21.598 1.00 13.24 ? 904  HOH B O     1 
HETATM 9319  O O     . HOH CA 10 .   ? 57.321  41.201  -31.141 1.00 16.40 ? 905  HOH B O     1 
HETATM 9320  O O     . HOH CA 10 .   ? 41.796  53.464  -20.466 1.00 12.76 ? 906  HOH B O     1 
HETATM 9321  O O     . HOH CA 10 .   ? 46.846  46.202  -29.831 1.00 17.00 ? 907  HOH B O     1 
HETATM 9322  O O     . HOH CA 10 .   ? 18.582  60.658  -8.116  1.00 15.33 ? 908  HOH B O     1 
HETATM 9323  O O     . HOH CA 10 .   ? 20.334  32.743  7.872   1.00 16.23 ? 909  HOH B O     1 
HETATM 9324  O O     . HOH CA 10 .   ? 26.564  38.048  -12.546 1.00 13.10 ? 910  HOH B O     1 
HETATM 9325  O O     . HOH CA 10 .   ? 32.482  29.669  -5.079  1.00 14.88 ? 911  HOH B O     1 
HETATM 9326  O O     . HOH CA 10 .   ? 21.627  49.551  -13.474 1.00 14.56 ? 912  HOH B O     1 
HETATM 9327  O O     . HOH CA 10 .   ? 13.930  43.241  6.308   1.00 15.04 ? 913  HOH B O     1 
HETATM 9328  O O     . HOH CA 10 .   ? 40.162  32.138  2.743   1.00 13.60 ? 914  HOH B O     1 
HETATM 9329  O O     . HOH CA 10 .   ? 24.097  29.584  -23.622 1.00 14.87 ? 915  HOH B O     1 
HETATM 9330  O O     . HOH CA 10 .   ? 19.963  52.708  5.698   1.00 15.43 ? 916  HOH B O     1 
HETATM 9331  O O     . HOH CA 10 .   ? 56.259  34.993  6.271   1.00 15.68 ? 917  HOH B O     1 
HETATM 9332  O O     . HOH CA 10 .   ? 54.620  18.287  -23.477 1.00 16.15 ? 918  HOH B O     1 
HETATM 9333  O O     . HOH CA 10 .   ? 58.243  31.140  4.181   1.00 16.33 ? 919  HOH B O     1 
HETATM 9334  O O     . HOH CA 10 .   ? 16.676  37.803  4.692   1.00 14.03 ? 920  HOH B O     1 
HETATM 9335  O O     . HOH CA 10 .   ? 35.560  26.791  -5.648  1.00 28.25 ? 921  HOH B O     1 
HETATM 9336  O O     . HOH CA 10 .   ? 19.511  54.923  -17.710 1.00 22.34 ? 922  HOH B O     1 
HETATM 9337  O O     . HOH CA 10 .   ? 51.283  47.530  -25.370 1.00 13.68 ? 923  HOH B O     1 
HETATM 9338  O O     . HOH CA 10 .   ? 51.583  58.170  4.133   1.00 21.40 ? 924  HOH B O     1 
HETATM 9339  O O     . HOH CA 10 .   ? 54.259  23.546  -6.772  1.00 15.25 ? 925  HOH B O     1 
HETATM 9340  O O     . HOH CA 10 .   ? 71.453  24.277  -6.835  1.00 19.34 ? 926  HOH B O     1 
HETATM 9341  O O     . HOH CA 10 .   ? 63.251  50.959  -23.211 1.00 19.05 ? 927  HOH B O     1 
HETATM 9342  O O     . HOH CA 10 .   ? 30.840  30.722  6.718   1.00 20.31 ? 928  HOH B O     1 
HETATM 9343  O O     . HOH CA 10 .   ? 59.208  20.144  -18.059 1.00 16.48 ? 929  HOH B O     1 
HETATM 9344  O O     . HOH CA 10 .   ? 47.875  20.670  -34.163 1.00 16.05 ? 930  HOH B O     1 
HETATM 9345  O O     . HOH CA 10 .   ? 48.963  37.552  -0.873  1.00 13.02 ? 931  HOH B O     1 
HETATM 9346  O O     . HOH CA 10 .   ? 55.965  50.992  -22.443 1.00 16.46 ? 932  HOH B O     1 
HETATM 9347  O O     . HOH CA 10 .   ? 52.553  19.889  -6.837  1.00 17.35 ? 933  HOH B O     1 
HETATM 9348  O O     . HOH CA 10 .   ? 40.787  44.298  -28.449 1.00 19.84 ? 934  HOH B O     1 
HETATM 9349  O O     . HOH CA 10 .   ? 48.388  59.456  -13.885 1.00 16.22 ? 935  HOH B O     1 
HETATM 9350  O O     . HOH CA 10 .   ? 22.134  46.923  -15.256 1.00 17.27 ? 936  HOH B O     1 
HETATM 9351  O O     . HOH CA 10 .   ? 29.508  27.591  -7.878  1.00 20.84 ? 937  HOH B O     1 
HETATM 9352  O O     . HOH CA 10 .   ? 40.376  33.763  -29.822 1.00 22.05 ? 938  HOH B O     1 
HETATM 9353  O O     . HOH CA 10 .   ? 26.567  56.528  2.863   1.00 18.76 ? 939  HOH B O     1 
HETATM 9354  O O     . HOH CA 10 .   ? 71.208  29.389  -11.956 1.00 13.93 ? 940  HOH B O     1 
HETATM 9355  O O     . HOH CA 10 .   ? 70.492  40.886  -11.198 1.00 15.93 ? 941  HOH B O     1 
HETATM 9356  O O     . HOH CA 10 .   ? 32.098  46.873  -26.753 1.00 18.85 ? 942  HOH B O     1 
HETATM 9357  O O     . HOH CA 10 .   ? 45.573  54.651  -18.176 1.00 14.48 ? 943  HOH B O     1 
HETATM 9358  O O     . HOH CA 10 .   ? 36.198  31.553  -5.723  1.00 14.34 ? 944  HOH B O     1 
HETATM 9359  O O     . HOH CA 10 .   ? 11.810  49.337  9.387   1.00 16.78 ? 945  HOH B O     1 
HETATM 9360  O O     . HOH CA 10 .   ? 8.549   34.300  -18.035 1.00 25.28 ? 946  HOH B O     1 
HETATM 9361  O O     . HOH CA 10 .   ? 49.773  45.432  -26.465 1.00 17.94 ? 947  HOH B O     1 
HETATM 9362  O O     . HOH CA 10 .   ? 31.736  24.901  -19.895 1.00 20.70 ? 948  HOH B O     1 
HETATM 9363  O O     . HOH CA 10 .   ? 25.366  30.626  -0.588  1.00 21.95 ? 949  HOH B O     1 
HETATM 9364  O O     . HOH CA 10 .   ? 53.747  22.707  -4.202  1.00 16.77 ? 950  HOH B O     1 
HETATM 9365  O O     . HOH CA 10 .   ? 51.960  28.959  8.335   1.00 16.77 ? 951  HOH B O     1 
HETATM 9366  O O     . HOH CA 10 .   ? 14.557  41.089  -18.864 1.00 16.87 ? 952  HOH B O     1 
HETATM 9367  O O     . HOH CA 10 .   ? 31.044  53.346  -21.273 1.00 19.09 ? 953  HOH B O     1 
HETATM 9368  O O     . HOH CA 10 .   ? 29.921  34.996  -26.840 1.00 17.57 ? 954  HOH B O     1 
HETATM 9369  O O     . HOH CA 10 .   ? 62.068  39.045  -31.518 1.00 25.01 ? 955  HOH B O     1 
HETATM 9370  O O     . HOH CA 10 .   ? 27.094  48.156  8.972   1.00 19.32 ? 956  HOH B O     1 
HETATM 9371  O O     . HOH CA 10 .   ? 55.222  44.717  -24.979 1.00 15.42 ? 957  HOH B O     1 
HETATM 9372  O O     . HOH CA 10 .   ? 11.542  49.227  0.108   1.00 24.88 ? 958  HOH B O     1 
HETATM 9373  O O     . HOH CA 10 .   ? 58.253  44.752  -29.015 1.00 17.18 ? 959  HOH B O     1 
HETATM 9374  O O     . HOH CA 10 .   ? 20.121  33.164  3.809   1.00 20.66 ? 960  HOH B O     1 
HETATM 9375  O O     . HOH CA 10 .   ? 52.745  50.300  4.620   1.00 20.70 ? 961  HOH B O     1 
HETATM 9376  O O     . HOH CA 10 .   ? 18.692  30.018  -15.379 1.00 18.28 ? 962  HOH B O     1 
HETATM 9377  O O     . HOH CA 10 .   ? 77.549  40.152  -6.907  1.00 15.07 ? 963  HOH B O     1 
HETATM 9378  O O     . HOH CA 10 .   ? 48.266  39.377  7.996   1.00 16.72 ? 964  HOH B O     1 
HETATM 9379  O O     . HOH CA 10 .   ? 15.227  45.092  -17.630 1.00 17.35 ? 965  HOH B O     1 
HETATM 9380  O O     . HOH CA 10 .   ? 38.823  52.611  -26.922 1.00 20.77 ? 966  HOH B O     1 
HETATM 9381  O O     . HOH CA 10 .   ? 24.145  35.737  -24.167 1.00 13.19 ? 967  HOH B O     1 
HETATM 9382  O O     . HOH CA 10 .   ? 25.837  32.233  -24.199 1.00 16.16 ? 968  HOH B O     1 
HETATM 9383  O O     . HOH CA 10 .   ? 20.363  28.185  -16.796 1.00 19.30 ? 969  HOH B O     1 
HETATM 9384  O O     . HOH CA 10 .   ? 40.730  52.694  4.269   1.00 17.15 ? 970  HOH B O     1 
HETATM 9385  O O     . HOH CA 10 .   ? 41.879  55.010  -26.093 1.00 20.80 ? 971  HOH B O     1 
HETATM 9386  O O     . HOH CA 10 .   ? 32.407  29.245  3.326   1.00 18.29 ? 972  HOH B O     1 
HETATM 9387  O O     . HOH CA 10 .   ? 16.919  35.846  -3.867  1.00 16.11 ? 973  HOH B O     1 
HETATM 9388  O O     . HOH CA 10 .   ? 47.228  31.044  -11.167 1.00 16.36 ? 974  HOH B O     1 
HETATM 9389  O O     . HOH CA 10 .   ? 12.138  46.003  3.619   1.00 22.69 ? 975  HOH B O     1 
HETATM 9390  O O     . HOH CA 10 .   ? 37.197  43.844  -9.017  1.00 22.35 ? 976  HOH B O     1 
HETATM 9391  O O     . HOH CA 10 .   ? 34.782  58.566  -6.877  1.00 23.18 ? 977  HOH B O     1 
HETATM 9392  O O     . HOH CA 10 .   ? 43.161  35.219  7.554   1.00 19.33 ? 978  HOH B O     1 
HETATM 9393  O O     . HOH CA 10 .   ? 43.324  46.028  -27.905 1.00 20.44 ? 979  HOH B O     1 
HETATM 9394  O O     . HOH CA 10 .   ? 9.595   31.748  -13.450 1.00 16.30 ? 980  HOH B O     1 
HETATM 9395  O O     . HOH CA 10 .   ? 9.788   44.514  -7.359  1.00 24.04 ? 981  HOH B O     1 
HETATM 9396  O O     . HOH CA 10 .   ? 60.641  57.730  -10.790 1.00 26.36 ? 982  HOH B O     1 
HETATM 9397  O O     . HOH CA 10 .   ? 41.797  22.477  -0.117  1.00 21.06 ? 983  HOH B O     1 
HETATM 9398  O O     . HOH CA 10 .   ? 57.741  38.017  -31.353 1.00 21.84 ? 984  HOH B O     1 
HETATM 9399  O O     . HOH CA 10 .   ? 9.198   37.813  -18.943 1.00 25.01 ? 985  HOH B O     1 
HETATM 9400  O O     . HOH CA 10 .   ? 73.669  29.643  -9.758  1.00 17.69 ? 986  HOH B O     1 
HETATM 9401  O O     . HOH CA 10 .   ? 55.715  26.045  -38.374 1.00 20.34 ? 987  HOH B O     1 
HETATM 9402  O O     . HOH CA 10 .   ? 64.410  48.254  -2.182  1.00 16.35 ? 988  HOH B O     1 
HETATM 9403  O O     . HOH CA 10 .   ? 30.366  53.496  9.023   1.00 25.21 ? 989  HOH B O     1 
HETATM 9404  O O     . HOH CA 10 .   ? 21.731  29.193  -8.851  1.00 25.11 ? 990  HOH B O     1 
HETATM 9405  O O     . HOH CA 10 .   ? 38.161  30.046  3.011   1.00 18.64 ? 991  HOH B O     1 
HETATM 9406  O O     . HOH CA 10 .   ? 69.646  37.879  0.610   1.00 18.48 ? 992  HOH B O     1 
HETATM 9407  O O     . HOH CA 10 .   ? 70.826  45.009  -8.229  1.00 20.41 ? 993  HOH B O     1 
HETATM 9408  O O     . HOH CA 10 .   ? 47.222  57.298  -15.170 1.00 15.76 ? 994  HOH B O     1 
HETATM 9409  O O     . HOH CA 10 .   ? 47.213  49.587  -26.379 1.00 21.01 ? 995  HOH B O     1 
HETATM 9410  O O     . HOH CA 10 .   ? 32.278  30.961  -29.643 1.00 28.35 ? 996  HOH B O     1 
HETATM 9411  O O     . HOH CA 10 .   ? 16.588  47.646  -10.811 1.00 17.84 ? 997  HOH B O     1 
HETATM 9412  O O     . HOH CA 10 .   ? 69.340  26.621  -17.201 1.00 17.08 ? 998  HOH B O     1 
HETATM 9413  O O     . HOH CA 10 .   ? 74.785  41.585  -9.687  1.00 20.04 ? 999  HOH B O     1 
HETATM 9414  O O     . HOH CA 10 .   ? 56.209  18.791  -31.327 1.00 16.25 ? 1000 HOH B O     1 
HETATM 9415  O O     . HOH CA 10 .   ? 16.914  31.459  -8.940  1.00 17.08 ? 1001 HOH B O     1 
HETATM 9416  O O     . HOH CA 10 .   ? 40.882  24.149  -7.490  1.00 18.08 ? 1002 HOH B O     1 
HETATM 9417  O O     . HOH CA 10 .   ? 62.100  23.893  -14.942 1.00 20.13 ? 1003 HOH B O     1 
HETATM 9418  O O     . HOH CA 10 .   ? 45.422  30.500  -38.489 1.00 17.88 ? 1004 HOH B O     1 
HETATM 9419  O O     . HOH CA 10 .   ? 50.303  19.464  -18.472 1.00 18.36 ? 1005 HOH B O     1 
HETATM 9420  O O     . HOH CA 10 .   ? 57.838  47.948  0.869   1.00 18.63 ? 1006 HOH B O     1 
HETATM 9421  O O     . HOH CA 10 .   ? 25.295  24.005  -19.864 1.00 18.73 ? 1007 HOH B O     1 
HETATM 9422  O O     . HOH CA 10 .   ? 21.608  55.108  5.802   1.00 20.93 ? 1008 HOH B O     1 
HETATM 9423  O O     . HOH CA 10 .   ? 59.067  54.854  -16.268 1.00 21.64 ? 1009 HOH B O     1 
HETATM 9424  O O     . HOH CA 10 .   ? 56.112  39.704  7.472   1.00 23.11 ? 1010 HOH B O     1 
HETATM 9425  O O     . HOH CA 10 .   ? 18.291  39.251  -26.210 1.00 18.51 ? 1011 HOH B O     1 
HETATM 9426  O O     . HOH CA 10 .   ? 52.678  18.627  -25.580 1.00 16.73 ? 1012 HOH B O     1 
HETATM 9427  O O     . HOH CA 10 .   ? 63.684  55.558  -4.314  1.00 20.91 ? 1013 HOH B O     1 
HETATM 9428  O O     . HOH CA 10 .   ? 29.367  32.278  -27.056 1.00 17.08 ? 1014 HOH B O     1 
HETATM 9429  O O     . HOH CA 10 .   ? 58.834  33.971  4.863   1.00 17.96 ? 1015 HOH B O     1 
HETATM 9430  O O     . HOH CA 10 .   ? 32.515  40.121  -3.653  1.00 19.24 ? 1016 HOH B O     1 
HETATM 9431  O O     . HOH CA 10 .   ? 25.253  41.671  -23.593 1.00 18.25 ? 1017 HOH B O     1 
HETATM 9432  O O     . HOH CA 10 .   ? 36.113  41.381  13.472  1.00 22.14 ? 1018 HOH B O     1 
HETATM 9433  O O     . HOH CA 10 .   ? 12.775  47.160  -11.588 1.00 17.44 ? 1019 HOH B O     1 
HETATM 9434  O O     . HOH CA 10 .   ? 52.187  34.172  -41.594 1.00 21.94 ? 1020 HOH B O     1 
HETATM 9435  O O     . HOH CA 10 .   ? 24.595  32.657  3.233   1.00 21.18 ? 1021 HOH B O     1 
HETATM 9436  O O     . HOH CA 10 .   ? 57.363  18.872  -16.689 1.00 21.07 ? 1022 HOH B O     1 
HETATM 9437  O O     . HOH CA 10 .   ? 45.598  33.870  -35.112 1.00 23.71 ? 1023 HOH B O     1 
HETATM 9438  O O     . HOH CA 10 .   ? 60.061  55.709  -1.343  1.00 21.63 ? 1024 HOH B O     1 
HETATM 9439  O O     . HOH CA 10 .   ? 66.867  49.315  -2.760  1.00 18.43 ? 1025 HOH B O     1 
HETATM 9440  O O     . HOH CA 10 .   ? 53.615  39.644  -39.119 1.00 19.79 ? 1026 HOH B O     1 
HETATM 9441  O O     . HOH CA 10 .   ? 74.661  39.913  -3.202  1.00 21.91 ? 1027 HOH B O     1 
HETATM 9442  O O     . HOH CA 10 .   ? 58.822  57.400  -14.434 1.00 33.19 ? 1028 HOH B O     1 
HETATM 9443  O O     . HOH CA 10 .   ? 57.786  24.117  -37.620 1.00 29.73 ? 1029 HOH B O     1 
HETATM 9444  O O     . HOH CA 10 .   ? 11.482  42.405  -3.630  1.00 19.33 ? 1030 HOH B O     1 
HETATM 9445  O O     . HOH CA 10 .   ? 74.064  38.999  -13.724 1.00 21.48 ? 1031 HOH B O     1 
HETATM 9446  O O     . HOH CA 10 .   ? 37.984  56.687  -8.593  1.00 20.16 ? 1032 HOH B O     1 
HETATM 9447  O O     . HOH CA 10 .   ? 67.854  22.192  -9.092  1.00 22.05 ? 1033 HOH B O     1 
HETATM 9448  O O     . HOH CA 10 .   ? 12.713  35.257  -6.158  1.00 22.14 ? 1034 HOH B O     1 
HETATM 9449  O O     . HOH CA 10 .   ? 61.463  30.398  -29.864 1.00 21.29 ? 1035 HOH B O     1 
HETATM 9450  O O     . HOH CA 10 .   ? 46.442  47.322  -27.285 1.00 18.74 ? 1036 HOH B O     1 
HETATM 9451  O O     . HOH CA 10 .   ? 10.582  31.735  -9.706  1.00 22.76 ? 1037 HOH B O     1 
HETATM 9452  O O     . HOH CA 10 .   ? 50.222  21.172  3.933   1.00 22.35 ? 1038 HOH B O     1 
HETATM 9453  O O     . HOH CA 10 .   ? 44.365  22.993  -29.562 1.00 17.02 ? 1039 HOH B O     1 
HETATM 9454  O O     . HOH CA 10 .   ? 71.335  45.145  -30.018 1.00 26.05 ? 1040 HOH B O     1 
HETATM 9455  O O     . HOH CA 10 .   ? 47.442  51.679  9.220   1.00 23.40 ? 1041 HOH B O     1 
HETATM 9456  O O     . HOH CA 10 .   ? 75.359  31.856  -11.342 1.00 23.34 ? 1042 HOH B O     1 
HETATM 9457  O O     . HOH CA 10 .   ? 16.980  52.948  -16.157 1.00 30.00 ? 1043 HOH B O     1 
HETATM 9458  O O     . HOH CA 10 .   ? 48.871  42.018  11.471  1.00 27.14 ? 1044 HOH B O     1 
HETATM 9459  O O     . HOH CA 10 .   ? 24.639  63.084  -5.800  1.00 21.03 ? 1045 HOH B O     1 
HETATM 9460  O O     . HOH CA 10 .   ? 22.687  60.714  -7.119  1.00 20.68 ? 1046 HOH B O     1 
HETATM 9461  O O     . HOH CA 10 .   ? 68.834  26.949  -19.825 1.00 25.19 ? 1047 HOH B O     1 
HETATM 9462  O O     . HOH CA 10 .   ? 73.758  35.046  -6.195  1.00 18.68 ? 1048 HOH B O     1 
HETATM 9463  O O     . HOH CA 10 .   ? 28.080  35.117  -24.897 1.00 17.84 ? 1049 HOH B O     1 
HETATM 9464  O O     . HOH CA 10 .   ? 55.354  48.942  1.386   1.00 17.82 ? 1050 HOH B O     1 
HETATM 9465  O O     . HOH CA 10 .   ? 70.856  27.358  -3.124  1.00 24.06 ? 1051 HOH B O     1 
HETATM 9466  O O     . HOH CA 10 .   ? 43.302  22.908  -11.854 1.00 23.26 ? 1052 HOH B O     1 
HETATM 9467  O O     . HOH CA 10 .   ? 59.015  31.364  -40.251 1.00 26.90 ? 1053 HOH B O     1 
HETATM 9468  O O     . HOH CA 10 .   ? 24.404  26.938  -24.071 1.00 21.93 ? 1054 HOH B O     1 
HETATM 9469  O O     . HOH CA 10 .   ? 51.848  42.711  -37.222 1.00 20.39 ? 1055 HOH B O     1 
HETATM 9470  O O     . HOH CA 10 .   ? 31.811  41.045  -5.991  1.00 20.89 ? 1056 HOH B O     1 
HETATM 9471  O O     . HOH CA 10 .   ? 45.197  59.291  -1.207  1.00 20.33 ? 1057 HOH B O     1 
HETATM 9472  O O     . HOH CA 10 .   ? 46.499  40.342  -16.175 1.00 8.90  ? 1058 HOH B O     1 
HETATM 9473  O O     . HOH CA 10 .   ? 18.497  33.470  5.954   1.00 16.98 ? 1059 HOH B O     1 
HETATM 9474  O O     . HOH CA 10 .   ? 4.140   40.937  -11.859 1.00 17.41 ? 1060 HOH B O     1 
HETATM 9475  O O     . HOH CA 10 .   ? 24.701  31.331  8.792   1.00 16.81 ? 1061 HOH B O     1 
HETATM 9476  O O     . HOH CA 10 .   ? 33.806  53.038  -22.133 1.00 16.09 ? 1062 HOH B O     1 
HETATM 9477  O O     . HOH CA 10 .   ? 14.370  36.764  -4.593  1.00 21.83 ? 1063 HOH B O     1 
HETATM 9478  O O     . HOH CA 10 .   ? 28.044  37.934  -23.948 1.00 15.03 ? 1064 HOH B O     1 
HETATM 9479  O O     . HOH CA 10 .   ? 53.821  47.119  -24.659 1.00 17.99 ? 1065 HOH B O     1 
HETATM 9480  O O     . HOH CA 10 .   ? 20.484  33.025  -3.079  1.00 21.42 ? 1066 HOH B O     1 
HETATM 9481  O O     . HOH CA 10 .   ? 25.767  34.843  -26.088 1.00 19.32 ? 1067 HOH B O     1 
HETATM 9482  O O     . HOH CA 10 .   ? 16.573  43.021  -19.033 1.00 17.62 ? 1068 HOH B O     1 
HETATM 9483  O O     . HOH CA 10 .   ? 46.787  36.806  -39.033 1.00 19.01 ? 1069 HOH B O     1 
HETATM 9484  O O     . HOH CA 10 .   ? 18.801  50.482  8.578   1.00 20.90 ? 1070 HOH B O     1 
HETATM 9485  O O     . HOH CA 10 .   ? 12.996  43.030  -17.577 1.00 23.08 ? 1071 HOH B O     1 
HETATM 9486  O O     . HOH CA 10 .   ? 40.798  23.526  -10.616 1.00 19.64 ? 1072 HOH B O     1 
HETATM 9487  O O     . HOH CA 10 .   ? 30.359  26.963  -10.610 1.00 24.58 ? 1073 HOH B O     1 
HETATM 9488  O O     . HOH CA 10 .   ? 13.102  40.117  -3.445  1.00 21.70 ? 1074 HOH B O     1 
HETATM 9489  O O     . HOH CA 10 .   ? 17.632  32.088  -6.171  1.00 16.21 ? 1075 HOH B O     1 
HETATM 9490  O O     . HOH CA 10 .   ? 12.626  40.457  -20.631 1.00 24.62 ? 1076 HOH B O     1 
HETATM 9491  O O     . HOH CA 10 .   ? 42.713  58.760  -2.609  1.00 19.80 ? 1077 HOH B O     1 
HETATM 9492  O O     . HOH CA 10 .   ? 50.470  18.855  -24.004 1.00 21.92 ? 1078 HOH B O     1 
HETATM 9493  O O     . HOH CA 10 .   ? 54.730  52.587  -20.717 1.00 23.78 ? 1079 HOH B O     1 
HETATM 9494  O O     . HOH CA 10 .   ? 13.056  32.621  -6.801  1.00 21.27 ? 1080 HOH B O     1 
HETATM 9495  O O     . HOH CA 10 .   ? 25.758  50.390  10.391  1.00 21.22 ? 1081 HOH B O     1 
HETATM 9496  O O     . HOH CA 10 .   ? 16.920  36.204  2.344   1.00 24.75 ? 1082 HOH B O     1 
HETATM 9497  O O     . HOH CA 10 .   ? 45.351  49.930  8.946   1.00 24.49 ? 1083 HOH B O     1 
HETATM 9498  O O     . HOH CA 10 .   ? 37.149  27.475  -26.971 1.00 29.00 ? 1084 HOH B O     1 
HETATM 9499  O O     . HOH CA 10 .   ? 53.792  48.280  7.458   1.00 17.30 ? 1085 HOH B O     1 
HETATM 9500  O O     . HOH CA 10 .   ? 59.223  31.997  -33.069 1.00 22.31 ? 1086 HOH B O     1 
HETATM 9501  O O     . HOH CA 10 .   ? 17.927  43.857  -21.401 1.00 22.79 ? 1087 HOH B O     1 
HETATM 9502  O O     . HOH CA 10 .   ? 21.283  33.756  0.701   1.00 34.13 ? 1088 HOH B O     1 
HETATM 9503  O O     . HOH CA 10 .   ? 54.741  60.155  -17.799 1.00 27.51 ? 1089 HOH B O     1 
HETATM 9504  O O     . HOH CA 10 .   ? 62.724  33.928  2.700   1.00 24.34 ? 1090 HOH B O     1 
HETATM 9505  O O     . HOH CA 10 .   ? 17.495  29.722  -12.995 1.00 26.31 ? 1091 HOH B O     1 
HETATM 9506  O O     . HOH CA 10 .   ? 24.849  46.050  -21.671 1.00 23.99 ? 1092 HOH B O     1 
HETATM 9507  O O     . HOH CA 10 .   ? 43.597  39.438  9.397   1.00 23.59 ? 1093 HOH B O     1 
HETATM 9508  O O     . HOH CA 10 .   ? 45.909  46.621  11.309  1.00 22.96 ? 1094 HOH B O     1 
HETATM 9509  O O     . HOH CA 10 .   ? 61.895  38.057  2.183   1.00 26.70 ? 1095 HOH B O     1 
HETATM 9510  O O     . HOH CA 10 .   ? 65.167  47.870  -34.563 1.00 23.30 ? 1096 HOH B O     1 
HETATM 9511  O O     . HOH CA 10 .   ? 29.765  34.589  12.944  1.00 25.26 ? 1097 HOH B O     1 
HETATM 9512  O O     . HOH CA 10 .   ? 48.218  24.259  -40.478 1.00 20.11 ? 1098 HOH B O     1 
HETATM 9513  O O     . HOH CA 10 .   ? 58.068  27.063  5.169   1.00 25.33 ? 1099 HOH B O     1 
HETATM 9514  O O     . HOH CA 10 .   ? 24.425  57.935  3.212   1.00 23.60 ? 1100 HOH B O     1 
HETATM 9515  O O     . HOH CA 10 .   ? 58.425  32.338  -42.824 1.00 18.54 ? 1101 HOH B O     1 
HETATM 9516  O O     . HOH CA 10 .   ? 68.610  44.386  -0.194  1.00 26.14 ? 1102 HOH B O     1 
HETATM 9517  O O     . HOH CA 10 .   ? 60.501  29.698  3.772   1.00 26.51 ? 1103 HOH B O     1 
HETATM 9518  O O     . HOH CA 10 .   ? 30.327  38.129  -30.533 1.00 28.57 ? 1104 HOH B O     1 
HETATM 9519  O O     . HOH CA 10 .   ? 45.467  24.259  -41.134 1.00 28.06 ? 1105 HOH B O     1 
HETATM 9520  O O     . HOH CA 10 .   ? 34.725  24.613  -17.064 1.00 21.33 ? 1106 HOH B O     1 
HETATM 9521  O O     . HOH CA 10 .   ? 26.233  54.259  7.347   1.00 23.70 ? 1107 HOH B O     1 
HETATM 9522  O O     . HOH CA 10 .   ? 46.429  59.259  -22.970 1.00 23.99 ? 1108 HOH B O     1 
HETATM 9523  O O     . HOH CA 10 .   ? 47.225  20.301  -1.629  1.00 28.11 ? 1109 HOH B O     1 
HETATM 9524  O O     . HOH CA 10 .   ? 50.159  58.147  -3.258  1.00 28.12 ? 1110 HOH B O     1 
HETATM 9525  O O     . HOH CA 10 .   ? 40.606  39.880  -35.166 1.00 24.99 ? 1111 HOH B O     1 
HETATM 9526  O O     . HOH CA 10 .   ? 51.675  61.035  -16.395 1.00 26.66 ? 1112 HOH B O     1 
HETATM 9527  O O     . HOH CA 10 .   ? 61.903  20.023  -16.902 1.00 27.44 ? 1113 HOH B O     1 
HETATM 9528  O O     . HOH CA 10 .   ? 23.222  60.061  1.673   1.00 24.32 ? 1114 HOH B O     1 
HETATM 9529  O O     . HOH CA 10 .   ? 36.745  56.416  1.859   1.00 28.90 ? 1115 HOH B O     1 
HETATM 9530  O O     . HOH CA 10 .   ? 55.564  57.137  5.188   1.00 28.86 ? 1116 HOH B O     1 
HETATM 9531  O O     . HOH CA 10 .   ? 57.126  45.270  -31.310 1.00 26.13 ? 1117 HOH B O     1 
HETATM 9532  O O     . HOH CA 10 .   ? 64.360  29.480  -30.053 1.00 26.63 ? 1118 HOH B O     1 
HETATM 9533  O O     . HOH CA 10 .   ? 12.788  38.064  -21.884 1.00 22.15 ? 1119 HOH B O     1 
HETATM 9534  O O     . HOH CA 10 .   ? 51.573  58.477  -21.841 1.00 20.37 ? 1120 HOH B O     1 
HETATM 9535  O O     . HOH CA 10 .   ? 8.726   41.647  -14.435 1.00 28.07 ? 1121 HOH B O     1 
HETATM 9536  O O     . HOH CA 10 .   ? 54.471  48.237  4.528   1.00 24.18 ? 1122 HOH B O     1 
HETATM 9537  O O     . HOH CA 10 .   ? 35.567  29.743  -28.306 1.00 31.08 ? 1123 HOH B O     1 
HETATM 9538  O O     . HOH CA 10 .   ? 29.711  55.518  -21.914 1.00 19.34 ? 1124 HOH B O     1 
HETATM 9539  O O     . HOH CA 10 .   ? 14.783  42.282  1.231   1.00 24.31 ? 1125 HOH B O     1 
HETATM 9540  O O     . HOH CA 10 .   ? 15.085  52.361  6.528   1.00 25.51 ? 1126 HOH B O     1 
HETATM 9541  O O     . HOH CA 10 .   ? 56.596  34.360  -41.843 1.00 19.15 ? 1127 HOH B O     1 
HETATM 9542  O O     . HOH CA 10 .   ? 24.833  30.477  -3.889  1.00 19.68 ? 1128 HOH B O     1 
HETATM 9543  O O     . HOH CA 10 .   ? 48.534  19.710  0.826   1.00 23.39 ? 1129 HOH B O     1 
HETATM 9544  O O     . HOH CA 10 .   ? 60.088  23.324  -7.888  1.00 31.96 ? 1130 HOH B O     1 
HETATM 9545  O O     . HOH CA 10 .   ? 54.031  20.503  -1.514  1.00 28.14 ? 1131 HOH B O     1 
HETATM 9546  O O     . HOH CA 10 .   ? 59.657  29.442  -33.045 1.00 21.43 ? 1132 HOH B O     1 
HETATM 9547  O O     . HOH CA 10 .   ? 72.029  42.769  -9.261  1.00 22.23 ? 1133 HOH B O     1 
HETATM 9548  O O     . HOH CA 10 .   ? 11.494  43.451  4.976   1.00 28.97 ? 1134 HOH B O     1 
HETATM 9549  O O     . HOH CA 10 .   ? 21.573  50.931  7.233   1.00 22.12 ? 1135 HOH B O     1 
HETATM 9550  O O     . HOH CA 10 .   ? 28.253  40.117  -29.585 1.00 31.28 ? 1136 HOH B O     1 
HETATM 9551  O O     . HOH CA 10 .   ? 55.295  56.463  -20.001 1.00 32.85 ? 1137 HOH B O     1 
HETATM 9552  O O     . HOH CA 10 .   ? 70.617  30.190  -26.610 1.00 33.08 ? 1138 HOH B O     1 
HETATM 9553  O O     . HOH CA 10 .   ? 76.485  28.615  -16.190 1.00 28.25 ? 1139 HOH B O     1 
HETATM 9554  O O     . HOH CA 10 .   ? 50.320  48.109  -30.771 1.00 28.19 ? 1140 HOH B O     1 
HETATM 9555  O O     . HOH CA 10 .   ? 75.485  36.239  -4.567  1.00 24.61 ? 1141 HOH B O     1 
HETATM 9556  O O     . HOH CA 10 .   ? 22.133  63.229  -4.892  1.00 27.92 ? 1142 HOH B O     1 
HETATM 9557  O O     . HOH CA 10 .   ? 77.355  38.107  -5.145  1.00 26.01 ? 1143 HOH B O     1 
HETATM 9558  O O     . HOH CA 10 .   ? 66.186  32.738  1.112   1.00 25.15 ? 1144 HOH B O     1 
HETATM 9559  O O     . HOH CA 10 .   ? 73.636  27.371  -5.759  1.00 27.32 ? 1145 HOH B O     1 
HETATM 9560  O O     . HOH CA 10 .   ? 18.012  29.413  -20.921 1.00 25.37 ? 1146 HOH B O     1 
HETATM 9561  O O     . HOH CA 10 .   ? 23.706  22.805  -21.681 1.00 28.79 ? 1147 HOH B O     1 
HETATM 9562  O O     . HOH CA 10 .   ? 37.611  56.878  -25.114 1.00 39.93 ? 1148 HOH B O     1 
HETATM 9563  O O     . HOH CA 10 .   ? 78.443  42.276  -5.552  1.00 17.32 ? 1149 HOH B O     1 
HETATM 9564  O O     . HOH CA 10 .   ? 47.815  47.815  -31.798 1.00 28.69 ? 1150 HOH B O     1 
HETATM 9565  O O     . HOH CA 10 .   ? 10.134  44.698  -15.533 1.00 26.17 ? 1151 HOH B O     1 
HETATM 9566  O O     . HOH CA 10 .   ? 31.737  51.153  11.341  1.00 25.54 ? 1152 HOH B O     1 
HETATM 9567  O O     . HOH CA 10 .   ? 48.171  59.133  -0.965  1.00 23.76 ? 1153 HOH B O     1 
HETATM 9568  O O     . HOH CA 10 .   ? 45.267  29.001  -28.497 1.00 19.62 ? 1154 HOH B O     1 
HETATM 9569  O O     . HOH CA 10 .   ? 60.690  22.176  -4.338  1.00 23.51 ? 1155 HOH B O     1 
HETATM 9570  O O     . HOH CA 10 .   ? 51.931  49.580  -27.024 1.00 23.59 ? 1156 HOH B O     1 
HETATM 9571  O O     . HOH CA 10 .   ? 73.574  39.505  -31.749 1.00 25.68 ? 1157 HOH B O     1 
HETATM 9572  O O     . HOH CA 10 .   ? 57.328  54.113  2.454   1.00 26.09 ? 1158 HOH B O     1 
HETATM 9573  O O     . HOH CA 10 .   ? 34.902  61.709  -13.825 1.00 26.81 ? 1159 HOH B O     1 
HETATM 9574  O O     . HOH CA 10 .   ? 57.645  48.173  -24.000 1.00 25.21 ? 1160 HOH B O     1 
HETATM 9575  O O     . HOH CA 10 .   ? 38.535  51.589  -6.187  1.00 19.94 ? 1161 HOH B O     1 
HETATM 9576  O O     . HOH CA 10 .   ? 49.445  60.781  -6.853  1.00 29.91 ? 1162 HOH B O     1 
HETATM 9577  O O     . HOH CA 10 .   ? 25.511  34.086  1.125   1.00 28.08 ? 1163 HOH B O     1 
HETATM 9578  O O     . HOH CA 10 .   ? 63.680  55.881  -26.740 1.00 30.44 ? 1164 HOH B O     1 
HETATM 9579  O O     . HOH CA 10 .   ? 34.812  49.301  -27.449 1.00 21.89 ? 1165 HOH B O     1 
HETATM 9580  O O     . HOH CA 10 .   ? 62.250  54.693  -22.680 1.00 31.39 ? 1166 HOH B O     1 
HETATM 9581  O O     . HOH CA 10 .   ? 41.503  54.761  2.412   1.00 33.08 ? 1167 HOH B O     1 
HETATM 9582  O O     . HOH CA 10 .   ? 54.789  26.315  -42.131 1.00 32.42 ? 1168 HOH B O     1 
HETATM 9583  O O     . HOH CA 10 .   ? 35.791  29.223  -4.259  1.00 21.54 ? 1169 HOH B O     1 
HETATM 9584  O O     . HOH CA 10 .   ? 34.903  44.380  -6.897  1.00 30.06 ? 1170 HOH B O     1 
HETATM 9585  O O     . HOH CA 10 .   ? 62.075  49.245  1.862   1.00 30.68 ? 1171 HOH B O     1 
HETATM 9586  O O     . HOH CA 10 .   ? 29.873  45.963  -25.418 1.00 22.89 ? 1172 HOH B O     1 
HETATM 9587  O O     . HOH CA 10 .   ? 51.395  19.038  -20.923 1.00 25.70 ? 1173 HOH B O     1 
HETATM 9588  O O     . HOH CA 10 .   ? 74.597  28.188  -11.969 1.00 25.91 ? 1174 HOH B O     1 
HETATM 9589  O O     . HOH CA 10 .   ? 57.416  23.030  0.225   1.00 25.44 ? 1175 HOH B O     1 
HETATM 9590  O O     . HOH CA 10 .   ? 60.102  48.811  -25.309 1.00 26.30 ? 1176 HOH B O     1 
HETATM 9591  O O     . HOH CA 10 .   ? 64.240  48.247  0.877   1.00 32.58 ? 1177 HOH B O     1 
HETATM 9592  O O     . HOH CA 10 .   ? 64.115  21.942  -16.086 1.00 34.50 ? 1178 HOH B O     1 
HETATM 9593  O O     . HOH CA 10 .   ? 30.176  29.396  -27.363 1.00 33.19 ? 1179 HOH B O     1 
HETATM 9594  O O     . HOH CA 10 .   ? 39.292  21.236  -3.829  1.00 27.97 ? 1180 HOH B O     1 
HETATM 9595  O O     . HOH CA 10 .   ? 61.836  54.921  -16.289 1.00 27.06 ? 1181 HOH B O     1 
HETATM 9596  O O     . HOH CA 10 .   ? 37.513  31.401  -28.724 1.00 29.67 ? 1182 HOH B O     1 
HETATM 9597  O O     . HOH CA 10 .   ? 77.190  39.457  -2.541  1.00 34.07 ? 1183 HOH B O     1 
HETATM 9598  O O     . HOH CA 10 .   ? 10.561  31.500  -6.970  1.00 30.59 ? 1184 HOH B O     1 
HETATM 9599  O O     . HOH CA 10 .   ? 43.424  50.456  10.882  1.00 33.04 ? 1185 HOH B O     1 
HETATM 9600  O O     . HOH CA 10 .   ? 23.910  33.185  -27.169 1.00 23.79 ? 1186 HOH B O     1 
HETATM 9601  O O     . HOH CA 10 .   ? 71.496  30.213  -21.445 1.00 30.48 ? 1187 HOH B O     1 
HETATM 9602  O O     . HOH CA 10 .   ? 54.199  50.049  -24.347 1.00 29.19 ? 1188 HOH B O     1 
HETATM 9603  O O     . HOH CA 10 .   ? 74.108  25.795  -8.224  1.00 32.64 ? 1189 HOH B O     1 
HETATM 9604  O O     . HOH CA 10 .   ? 11.929  55.375  0.416   1.00 28.76 ? 1190 HOH B O     1 
HETATM 9605  O O     . HOH CA 10 .   ? 56.701  57.462  -1.808  1.00 29.60 ? 1191 HOH B O     1 
HETATM 9606  O O     . HOH CA 10 .   ? 26.431  30.298  5.451   1.00 27.97 ? 1192 HOH B O     1 
HETATM 9607  O O     . HOH CA 10 .   ? 74.075  40.272  -0.576  1.00 32.52 ? 1193 HOH B O     1 
HETATM 9608  O O     . HOH CA 10 .   ? 17.597  52.542  7.416   1.00 33.59 ? 1194 HOH B O     1 
HETATM 9609  O O     . HOH CA 10 .   ? 39.786  62.143  -16.516 1.00 34.04 ? 1195 HOH B O     1 
HETATM 9610  O O     . HOH CA 10 .   ? 46.161  39.123  9.858   1.00 35.66 ? 1196 HOH B O     1 
HETATM 9611  O O     . HOH CA 10 .   ? 56.011  23.400  5.426   1.00 29.23 ? 1197 HOH B O     1 
HETATM 9612  O O     . HOH CA 10 .   ? 65.863  24.218  -9.236  1.00 32.16 ? 1198 HOH B O     1 
HETATM 9613  O O     . HOH CA 10 .   ? 66.617  53.294  -2.847  1.00 26.01 ? 1199 HOH B O     1 
HETATM 9614  O O     . HOH CA 10 .   ? 10.192  46.998  6.893   1.00 27.77 ? 1200 HOH B O     1 
HETATM 9615  O O     . HOH CA 10 .   ? 60.457  49.485  -29.515 1.00 34.04 ? 1201 HOH B O     1 
HETATM 9616  O O     . HOH CA 10 .   ? 51.585  36.611  -40.728 1.00 32.61 ? 1202 HOH B O     1 
HETATM 9617  O O     . HOH CA 10 .   ? 39.577  58.937  -10.533 1.00 28.30 ? 1203 HOH B O     1 
HETATM 9618  O O     . HOH CA 10 .   ? 74.884  44.051  -8.452  1.00 35.60 ? 1204 HOH B O     1 
HETATM 9619  O O     . HOH CA 10 .   ? 49.267  37.399  -39.861 1.00 31.34 ? 1205 HOH B O     1 
HETATM 9620  O O     . HOH CA 10 .   ? 54.162  53.009  8.460   1.00 31.76 ? 1206 HOH B O     1 
HETATM 9621  O O     . HOH CA 10 .   ? 45.082  17.268  -27.076 1.00 32.35 ? 1207 HOH B O     1 
HETATM 9622  O O     . HOH CA 10 .   ? 34.867  42.289  -30.490 1.00 32.62 ? 1208 HOH B O     1 
HETATM 9623  O O     . HOH CA 10 .   ? 36.687  59.937  -5.247  1.00 29.81 ? 1209 HOH B O     1 
HETATM 9624  O O     . HOH CA 10 .   ? 66.435  19.359  -6.395  1.00 33.36 ? 1210 HOH B O     1 
HETATM 9625  O O     . HOH CA 10 .   ? 64.174  24.561  -30.545 1.00 25.72 ? 1211 HOH B O     1 
HETATM 9626  O O     . HOH CA 10 .   ? 12.230  46.192  -15.389 1.00 24.03 ? 1212 HOH B O     1 
HETATM 9627  O O     . HOH CA 10 .   ? 44.353  49.221  -26.704 1.00 29.09 ? 1213 HOH B O     1 
HETATM 9628  O O     . HOH CA 10 .   ? 69.926  41.857  -20.781 1.00 25.02 ? 1214 HOH B O     1 
HETATM 9629  O O     . HOH CA 10 .   ? 48.504  18.577  -12.219 1.00 30.86 ? 1215 HOH B O     1 
HETATM 9630  O O     . HOH CA 10 .   ? 47.637  50.932  -28.725 1.00 31.08 ? 1216 HOH B O     1 
HETATM 9631  O O     . HOH CA 10 .   ? 52.636  45.129  -36.491 1.00 29.52 ? 1217 HOH B O     1 
HETATM 9632  O O     . HOH CA 10 .   ? 19.276  59.433  -0.546  1.00 33.77 ? 1218 HOH B O     1 
HETATM 9633  O O     . HOH CA 10 .   ? 56.900  35.471  -35.591 1.00 29.22 ? 1219 HOH B O     1 
HETATM 9634  O O     . HOH CA 10 .   ? 14.753  54.588  -12.649 1.00 23.53 ? 1220 HOH B O     1 
HETATM 9635  O O     . HOH CA 10 .   ? 28.218  60.264  3.670   1.00 33.72 ? 1221 HOH B O     1 
HETATM 9636  O O     . HOH CA 10 .   ? 42.053  21.831  -28.500 1.00 24.01 ? 1222 HOH B O     1 
HETATM 9637  O O     . HOH CA 10 .   ? 38.673  54.203  -5.649  1.00 27.84 ? 1223 HOH B O     1 
HETATM 9638  O O     . HOH CA 10 .   ? 65.081  43.548  1.489   1.00 30.57 ? 1224 HOH B O     1 
HETATM 9639  O O     . HOH CA 10 .   ? 44.066  25.254  -31.523 1.00 31.59 ? 1225 HOH B O     1 
HETATM 9640  O O     . HOH CA 10 .   ? 66.637  19.685  -9.058  1.00 36.03 ? 1226 HOH B O     1 
HETATM 9641  O O     . HOH CA 10 .   ? 18.086  57.371  -14.742 1.00 35.08 ? 1227 HOH B O     1 
HETATM 9642  O O     . HOH CA 10 .   ? 10.833  52.450  -10.030 1.00 26.79 ? 1228 HOH B O     1 
HETATM 9643  O O     . HOH CA 10 .   ? 43.711  20.911  -16.133 1.00 29.22 ? 1229 HOH B O     1 
HETATM 9644  O O     . HOH CA 10 .   ? 28.563  29.317  6.706   1.00 27.71 ? 1230 HOH B O     1 
HETATM 9645  O O     . HOH CA 10 .   ? 33.817  26.903  -24.897 1.00 27.18 ? 1231 HOH B O     1 
HETATM 9646  O O     . HOH CA 10 .   ? 23.102  60.234  -14.272 1.00 38.32 ? 1232 HOH B O     1 
HETATM 9647  O O     . HOH CA 10 .   ? 59.341  46.062  2.299   1.00 34.15 ? 1233 HOH B O     1 
HETATM 9648  O O     . HOH CA 10 .   ? 67.828  53.784  -16.628 1.00 23.65 ? 1234 HOH B O     1 
HETATM 9649  O O     . HOH CA 10 .   ? 71.269  23.979  -28.843 1.00 29.65 ? 1235 HOH B O     1 
HETATM 9650  O O     . HOH CA 10 .   ? 10.184  32.441  -16.141 1.00 31.80 ? 1236 HOH B O     1 
HETATM 9651  O O     . HOH CA 10 .   ? 52.566  27.257  -43.284 1.00 27.19 ? 1237 HOH B O     1 
HETATM 9652  O O     . HOH CA 10 .   ? 11.004  36.506  -20.674 1.00 41.27 ? 1238 HOH B O     1 
HETATM 9653  O O     . HOH CA 10 .   ? 10.619  36.094  -4.446  1.00 27.90 ? 1239 HOH B O     1 
HETATM 9654  O O     . HOH CA 10 .   ? 77.787  31.396  -18.067 1.00 36.20 ? 1240 HOH B O     1 
HETATM 9655  O O     . HOH CA 10 .   ? 73.296  24.791  -34.172 1.00 30.36 ? 1241 HOH B O     1 
HETATM 9656  O O     . HOH CA 10 .   ? 45.213  43.746  -24.531 1.00 15.37 ? 1242 HOH B O     1 
HETATM 9657  O O     . HOH CA 10 .   ? 64.322  27.245  -31.527 1.00 20.46 ? 1243 HOH B O     1 
HETATM 9658  O O     . HOH CA 10 .   ? 62.340  27.949  -33.366 1.00 21.70 ? 1244 HOH B O     1 
HETATM 9659  O O     . HOH CA 10 .   ? 32.875  22.184  -17.254 1.00 27.76 ? 1245 HOH B O     1 
HETATM 9660  O O     . HOH CA 10 .   ? 25.112  51.936  8.053   1.00 24.24 ? 1246 HOH B O     1 
HETATM 9661  O O     . HOH CA 10 .   ? 10.329  42.260  -16.818 1.00 25.40 ? 1247 HOH B O     1 
HETATM 9662  O O     . HOH CA 10 .   ? 28.253  32.287  12.879  1.00 26.45 ? 1248 HOH B O     1 
HETATM 9663  O O     . HOH CA 10 .   ? 32.488  22.318  -19.881 1.00 25.67 ? 1249 HOH B O     1 
HETATM 9664  O O     . HOH CA 10 .   ? 7.378   39.490  -15.524 1.00 25.24 ? 1250 HOH B O     1 
HETATM 9665  O O     . HOH CA 10 .   ? 50.308  24.500  -42.323 1.00 33.79 ? 1251 HOH B O     1 
HETATM 9666  O O     . HOH CA 10 .   ? 12.725  29.682  -9.902  1.00 30.78 ? 1252 HOH B O     1 
HETATM 9667  O O     . HOH CA 10 .   ? 36.243  44.402  -31.418 1.00 25.68 ? 1253 HOH B O     1 
HETATM 9668  O O     . HOH CA 10 .   ? 50.351  50.345  -29.070 1.00 28.18 ? 1254 HOH B O     1 
HETATM 9669  O O     . HOH CA 10 .   ? 63.335  19.048  -22.445 1.00 27.40 ? 1255 HOH B O     1 
HETATM 9670  O O     . HOH CA 10 .   ? 33.403  28.999  5.946   1.00 30.31 ? 1256 HOH B O     1 
HETATM 9671  O O     . HOH CA 10 .   ? 70.260  48.717  -5.511  1.00 25.37 ? 1257 HOH B O     1 
HETATM 9672  O O     . HOH CA 10 .   ? 72.320  43.528  -0.256  1.00 32.16 ? 1258 HOH B O     1 
HETATM 9673  O O     . HOH CA 10 .   ? 41.301  22.952  -26.153 1.00 31.56 ? 1259 HOH B O     1 
HETATM 9674  O O     . HOH CA 10 .   ? 36.888  26.189  -7.740  1.00 27.75 ? 1260 HOH B O     1 
HETATM 9675  O O     . HOH CA 10 .   ? 62.895  31.404  3.295   1.00 22.97 ? 1261 HOH B O     1 
HETATM 9676  O O     . HOH CA 10 .   ? 31.580  49.805  -27.343 1.00 27.45 ? 1262 HOH B O     1 
HETATM 9677  O O     . HOH CA 10 .   ? 27.542  54.105  9.533   1.00 27.09 ? 1263 HOH B O     1 
HETATM 9678  O O     . HOH CA 10 .   ? 37.603  47.590  9.337   1.00 26.27 ? 1264 HOH B O     1 
HETATM 9679  O O     . HOH CA 10 .   ? 70.875  23.907  -16.451 1.00 27.83 ? 1265 HOH B O     1 
HETATM 9680  O O     . HOH CA 10 .   ? 33.153  44.420  11.716  1.00 35.02 ? 1266 HOH B O     1 
HETATM 9681  O O     . HOH CA 10 .   ? 26.381  65.578  -5.224  1.00 31.00 ? 1267 HOH B O     1 
HETATM 9682  O O     . HOH CA 10 .   ? 29.783  62.835  -2.286  1.00 29.15 ? 1268 HOH B O     1 
HETATM 9683  O O     . HOH CA 10 .   ? 38.305  56.327  4.201   1.00 27.98 ? 1269 HOH B O     1 
HETATM 9684  O O     . HOH CA 10 .   ? 14.828  46.703  -19.736 1.00 25.93 ? 1270 HOH B O     1 
HETATM 9685  O O     . HOH CA 10 .   ? 71.104  32.310  -28.413 1.00 31.09 ? 1271 HOH B O     1 
HETATM 9686  O O     . HOH CA 10 .   ? 33.120  26.015  -10.425 1.00 32.27 ? 1272 HOH B O     1 
HETATM 9687  O O     . HOH CA 10 .   ? 62.047  27.437  2.544   1.00 34.95 ? 1273 HOH B O     1 
HETATM 9688  O O     . HOH CA 10 .   ? 56.184  16.337  -17.373 1.00 30.97 ? 1274 HOH B O     1 
HETATM 9689  O O     . HOH CA 10 .   ? 34.454  48.110  -29.817 1.00 29.39 ? 1275 HOH B O     1 
HETATM 9690  O O     . HOH CA 10 .   ? 45.463  25.006  5.877   1.00 28.04 ? 1276 HOH B O     1 
HETATM 9691  O O     . HOH CA 10 .   ? 31.616  19.628  -20.463 1.00 30.72 ? 1277 HOH B O     1 
HETATM 9692  O O     . HOH CA 10 .   ? 27.473  45.362  -24.069 1.00 33.05 ? 1278 HOH B O     1 
HETATM 9693  O O     . HOH CA 10 .   ? 43.456  29.226  -37.025 1.00 38.41 ? 1279 HOH B O     1 
HETATM 9694  O O     . HOH CA 10 .   ? 47.029  20.695  3.470   1.00 32.77 ? 1280 HOH B O     1 
HETATM 9695  O O     . HOH CA 10 .   ? 61.664  17.359  -24.187 1.00 33.50 ? 1281 HOH B O     1 
HETATM 9696  O O     . HOH CA 10 .   ? 64.372  42.982  -35.515 1.00 31.54 ? 1282 HOH B O     1 
HETATM 9697  O O     . HOH CA 10 .   ? 50.944  26.936  9.418   1.00 29.46 ? 1283 HOH B O     1 
HETATM 9698  O O     . HOH CA 10 .   ? 75.197  31.346  -7.839  1.00 27.88 ? 1284 HOH B O     1 
HETATM 9699  O O     . HOH CA 10 .   ? 13.556  54.663  5.975   1.00 28.46 ? 1285 HOH B O     1 
HETATM 9700  O O     . HOH CA 10 .   ? 15.168  59.384  1.080   1.00 30.90 ? 1286 HOH B O     1 
HETATM 9701  O O     . HOH CA 10 .   ? 76.934  29.245  -13.515 1.00 44.91 ? 1287 HOH B O     1 
HETATM 9702  O O     . HOH CA 10 .   ? 24.683  23.125  -17.304 1.00 24.84 ? 1288 HOH B O     1 
HETATM 9703  O O     . HOH CA 10 .   ? 54.778  60.730  -9.757  1.00 33.44 ? 1289 HOH B O     1 
HETATM 9704  O O     . HOH CA 10 .   ? 43.628  23.044  -14.459 1.00 27.00 ? 1290 HOH B O     1 
HETATM 9705  O O     . HOH CA 10 .   ? 40.063  33.814  13.786  1.00 47.47 ? 1291 HOH B O     1 
HETATM 9706  O O     . HOH CA 10 .   ? 30.608  37.779  13.720  1.00 39.43 ? 1292 HOH B O     1 
HETATM 9707  O O     . HOH CA 10 .   ? 75.629  26.029  -10.542 1.00 33.59 ? 1293 HOH B O     1 
HETATM 9708  O O     . HOH CA 10 .   ? 35.812  54.789  -22.510 1.00 26.18 ? 1294 HOH B O     1 
HETATM 9709  O O     . HOH CA 10 .   ? 9.951   40.495  -19.103 1.00 30.34 ? 1295 HOH B O     1 
HETATM 9710  O O     . HOH CA 10 .   ? 36.348  27.273  3.224   1.00 38.59 ? 1296 HOH B O     1 
HETATM 9711  O O     . HOH CA 10 .   ? 16.746  65.637  -0.455  1.00 36.11 ? 1297 HOH B O     1 
HETATM 9712  O O     . HOH CA 10 .   ? 62.656  20.288  -3.587  1.00 32.10 ? 1298 HOH B O     1 
HETATM 9713  O O     . HOH CA 10 .   ? 41.935  41.955  -29.152 1.00 29.72 ? 1299 HOH B O     1 
HETATM 9714  O O     . HOH CA 10 .   ? 35.115  30.785  -31.299 1.00 45.64 ? 1300 HOH B O     1 
HETATM 9715  O O     . HOH CA 10 .   ? 55.586  41.110  10.531  1.00 30.93 ? 1301 HOH B O     1 
HETATM 9716  O O     . HOH CA 10 .   ? 22.246  31.052  6.806   1.00 27.19 ? 1302 HOH B O     1 
HETATM 9717  O O     . HOH CA 10 .   ? 38.134  23.899  -7.760  1.00 32.09 ? 1303 HOH B O     1 
HETATM 9718  O O     . HOH CA 10 .   ? 44.719  61.327  2.399   1.00 37.47 ? 1304 HOH B O     1 
HETATM 9719  O O     . HOH CA 10 .   ? 51.512  33.025  12.244  1.00 37.24 ? 1305 HOH B O     1 
HETATM 9720  O O     . HOH CA 10 .   ? 34.978  28.880  1.576   1.00 34.14 ? 1306 HOH B O     1 
HETATM 9721  O O     . HOH CA 10 .   ? 37.401  32.650  -31.036 1.00 33.04 ? 1307 HOH B O     1 
HETATM 9722  O O     . HOH CA 10 .   ? 15.279  42.476  -24.275 1.00 36.41 ? 1308 HOH B O     1 
HETATM 9723  O O     . HOH CA 10 .   ? 37.104  33.082  9.734   1.00 39.13 ? 1309 HOH B O     1 
HETATM 9724  O O     . HOH CA 10 .   ? 38.244  60.713  -7.561  1.00 38.17 ? 1310 HOH B O     1 
HETATM 9725  O O     . HOH CA 10 .   ? 32.105  46.177  -29.418 1.00 28.74 ? 1311 HOH B O     1 
HETATM 9726  O O     . HOH CA 10 .   ? 26.680  29.727  9.490   1.00 26.12 ? 1313 HOH B O     1 
HETATM 9727  O O     . HOH CA 10 .   ? 18.752  27.846  -18.892 1.00 31.50 ? 1314 HOH B O     1 
HETATM 9728  O O     . HOH CA 10 .   ? 32.252  55.686  9.121   1.00 38.03 ? 1315 HOH B O     1 
HETATM 9729  O O     . HOH CA 10 .   ? 47.894  21.529  -40.211 1.00 34.42 ? 1316 HOH B O     1 
HETATM 9730  O O     . HOH CA 10 .   ? 56.416  51.434  3.482   1.00 43.13 ? 1317 HOH B O     1 
HETATM 9731  O O     . HOH CA 10 .   ? 7.482   45.740  -7.329  1.00 35.22 ? 1318 HOH B O     1 
HETATM 9732  O O     . HOH CA 10 .   ? 53.216  63.208  -14.238 1.00 35.78 ? 1319 HOH B O     1 
HETATM 9733  O O     . HOH CA 10 .   ? 8.084   30.547  -9.810  1.00 31.28 ? 1320 HOH B O     1 
HETATM 9734  O O     . HOH CA 10 .   ? 65.687  26.504  0.541   1.00 34.27 ? 1321 HOH B O     1 
HETATM 9735  O O     . HOH CA 10 .   ? 28.234  62.878  -16.291 1.00 38.60 ? 1322 HOH B O     1 
HETATM 9736  O O     . HOH CA 10 .   ? 48.533  29.933  9.497   1.00 32.28 ? 1323 HOH B O     1 
HETATM 9737  O O     . HOH CA 10 .   ? 46.455  49.986  -31.163 1.00 34.84 ? 1324 HOH B O     1 
HETATM 9738  O O     . HOH CA 10 .   ? 71.442  52.885  -8.080  1.00 46.40 ? 1325 HOH B O     1 
HETATM 9739  O O     . HOH CA 10 .   ? 40.311  52.902  10.505  1.00 45.83 ? 1326 HOH B O     1 
HETATM 9740  O O     . HOH CA 10 .   ? 27.086  57.934  -23.162 1.00 31.27 ? 1327 HOH B O     1 
HETATM 9741  O O     . HOH CA 10 .   ? 72.830  45.805  -1.663  1.00 37.73 ? 1328 HOH B O     1 
HETATM 9742  O O     . HOH CA 10 .   ? 44.216  48.658  12.731  1.00 36.15 ? 1329 HOH B O     1 
HETATM 9743  O O     . HOH CA 10 .   ? 64.956  30.423  1.649   1.00 38.25 ? 1330 HOH B O     1 
HETATM 9744  O O     . HOH CA 10 .   ? 71.529  28.958  1.393   1.00 36.78 ? 1331 HOH B O     1 
HETATM 9745  O O     . HOH CA 10 .   ? 76.331  38.181  -20.912 1.00 34.62 ? 1332 HOH B O     1 
HETATM 9746  O O     . HOH CA 10 .   ? 52.552  48.319  -32.717 1.00 40.46 ? 1333 HOH B O     1 
HETATM 9747  O O     . HOH CA 10 .   ? 13.106  36.084  -1.711  1.00 39.51 ? 1334 HOH B O     1 
HETATM 9748  O O     . HOH CA 10 .   ? 14.313  48.855  -9.998  1.00 31.49 ? 1335 HOH B O     1 
HETATM 9749  O O     . HOH CA 10 .   ? 65.963  21.593  -32.943 1.00 39.52 ? 1336 HOH B O     1 
HETATM 9750  O O     . HOH CA 10 .   ? 55.102  34.694  8.722   1.00 38.41 ? 1337 HOH B O     1 
HETATM 9751  O O     . HOH CA 10 .   ? 5.487   49.110  -11.939 1.00 38.67 ? 1338 HOH B O     1 
HETATM 9752  O O     . HOH CA 10 .   ? 60.380  39.283  5.766   1.00 32.38 ? 1339 HOH B O     1 
HETATM 9753  O O     . HOH CA 10 .   ? 10.959  55.740  2.929   1.00 39.89 ? 1340 HOH B O     1 
HETATM 9754  O O     . HOH CA 10 .   ? 36.206  29.338  9.361   1.00 31.71 ? 1341 HOH B O     1 
HETATM 9755  O O     . HOH CA 10 .   ? 68.528  56.376  -25.691 1.00 34.23 ? 1342 HOH B O     1 
HETATM 9756  O O     . HOH CA 10 .   ? 18.473  46.120  8.658   1.00 19.43 ? 1343 HOH B O     1 
HETATM 9757  O O     . HOH CA 10 .   ? 14.811  48.582  9.769   1.00 19.80 ? 1344 HOH B O     1 
HETATM 9758  O O     . HOH CA 10 .   ? 65.744  45.679  -1.553  1.00 29.18 ? 1345 HOH B O     1 
HETATM 9759  O O     . HOH CA 10 .   ? 13.365  56.359  3.704   1.00 25.18 ? 1346 HOH B O     1 
HETATM 9760  O O     . HOH CA 10 .   ? 43.866  42.980  -31.225 1.00 30.87 ? 1347 HOH B O     1 
HETATM 9761  O O     . HOH CA 10 .   ? 76.345  43.529  -23.783 1.00 30.30 ? 1348 HOH B O     1 
HETATM 9762  O O     . HOH CA 10 .   ? 43.265  36.254  -33.868 1.00 38.36 ? 1349 HOH B O     1 
HETATM 9763  O O     . HOH CA 10 .   ? 75.338  40.528  -17.621 1.00 32.28 ? 1350 HOH B O     1 
HETATM 9764  O O     . HOH CA 10 .   ? 26.491  68.939  -8.978  1.00 41.36 ? 1351 HOH B O     1 
HETATM 9765  O O     . HOH CA 10 .   ? 77.994  39.191  -22.735 1.00 35.49 ? 1352 HOH B O     1 
HETATM 9766  O O     . HOH CA 10 .   ? 67.688  20.708  0.672   1.00 32.89 ? 1353 HOH B O     1 
HETATM 9767  O O     . HOH CA 10 .   ? 10.487  46.471  -0.378  1.00 33.25 ? 1354 HOH B O     1 
HETATM 9768  O O     . HOH CA 10 .   ? 67.602  26.449  -31.253 1.00 34.00 ? 1355 HOH B O     1 
HETATM 9769  O O     . HOH CA 10 .   ? 42.423  29.848  -34.673 1.00 37.26 ? 1356 HOH B O     1 
HETATM 9770  O O     . HOH CA 10 .   ? 55.425  36.392  -38.590 1.00 29.20 ? 1357 HOH B O     1 
HETATM 9771  O O     . HOH CA 10 .   ? 55.432  29.879  -46.258 1.00 44.88 ? 1358 HOH B O     1 
HETATM 9772  O O     . HOH CA 10 .   ? 72.483  24.460  -0.058  1.00 38.11 ? 1359 HOH B O     1 
HETATM 9773  O O     . HOH CA 10 .   ? 19.464  57.170  6.132   1.00 33.34 ? 1360 HOH B O     1 
HETATM 9774  O O     . HOH CA 10 .   ? 78.361  41.766  -1.928  1.00 32.59 ? 1361 HOH B O     1 
HETATM 9775  O O     . HOH CA 10 .   ? 72.537  20.429  -31.023 1.00 40.71 ? 1362 HOH B O     1 
HETATM 9776  O O     . HOH CA 10 .   ? 77.007  47.228  -21.093 1.00 43.11 ? 1363 HOH B O     1 
HETATM 9777  O O     . HOH CA 10 .   ? 28.879  30.002  11.627  1.00 36.33 ? 1364 HOH B O     1 
HETATM 9778  O O     . HOH CA 10 .   ? 67.124  24.574  -15.115 1.00 35.11 ? 1365 HOH B O     1 
HETATM 9779  O O     . HOH CA 10 .   ? 38.022  21.886  -9.777  1.00 34.71 ? 1367 HOH B O     1 
HETATM 9780  O O     . HOH CA 10 .   ? 21.270  62.045  -11.587 1.00 27.48 ? 1368 HOH B O     1 
HETATM 9781  O O     . HOH CA 10 .   ? 33.342  47.243  -7.776  1.00 35.00 ? 1369 HOH B O     1 
HETATM 9782  O O     . HOH CA 10 .   ? 30.964  29.809  9.981   1.00 40.07 ? 1370 HOH B O     1 
HETATM 9783  O O     . HOH CA 10 .   ? 59.089  54.554  -23.256 1.00 32.53 ? 1371 HOH B O     1 
HETATM 9784  O O     . HOH CA 10 .   ? 28.157  22.449  -11.659 1.00 28.91 ? 1372 HOH B O     1 
HETATM 9785  O O     . HOH CA 10 .   ? 39.689  32.869  9.370   1.00 40.25 ? 1373 HOH B O     1 
HETATM 9786  O O     . HOH CA 10 .   ? 45.184  42.668  -38.868 1.00 46.98 ? 1374 HOH B O     1 
HETATM 9787  O O     . HOH CA 10 .   ? 60.405  18.217  -19.617 1.00 42.78 ? 1375 HOH B O     1 
HETATM 9788  O O     . HOH CA 10 .   ? 53.794  17.623  -11.129 1.00 44.18 ? 1376 HOH B O     1 
HETATM 9789  O O     . HOH CA 10 .   ? 67.784  42.372  1.359   1.00 40.33 ? 1377 HOH B O     1 
HETATM 9790  O O     . HOH CA 10 .   ? 50.870  22.977  10.951  1.00 42.61 ? 1378 HOH B O     1 
HETATM 9791  O O     . HOH CA 10 .   ? 46.425  64.449  -12.663 1.00 40.35 ? 1379 HOH B O     1 
HETATM 9792  O O     . HOH CA 10 .   ? 37.886  33.374  12.311  1.00 39.97 ? 1380 HOH B O     1 
HETATM 9793  O O     . HOH CA 10 .   ? 38.616  28.064  -7.387  1.00 22.17 ? 1381 HOH B O     1 
HETATM 9794  O O     . HOH CA 10 .   ? 29.583  34.677  -30.835 1.00 43.96 ? 1382 HOH B O     1 
HETATM 9795  O O     . HOH CA 10 .   ? 43.627  41.405  -25.316 1.00 25.67 ? 1383 HOH B O     1 
HETATM 9796  O O     . HOH CA 10 .   ? 55.904  38.627  -40.372 1.00 29.52 ? 1384 HOH B O     1 
HETATM 9797  O O     . HOH CA 10 .   ? 70.291  17.626  -31.272 1.00 34.04 ? 1385 HOH B O     1 
HETATM 9798  O O     . HOH CA 10 .   ? 57.077  16.681  -19.731 1.00 32.23 ? 1386 HOH B O     1 
HETATM 9799  O O     . HOH CA 10 .   ? 50.699  17.117  -36.846 1.00 27.74 ? 1387 HOH B O     1 
HETATM 9800  O O     . HOH CA 10 .   ? 27.090  40.278  -25.192 1.00 36.49 ? 1388 HOH B O     1 
HETATM 9801  O O     . HOH CA 10 .   ? 56.628  41.020  5.053   1.00 28.29 ? 1389 HOH B O     1 
HETATM 9802  O O     . HOH CA 10 .   ? 33.147  56.987  3.704   1.00 25.02 ? 1390 HOH B O     1 
HETATM 9803  O O     . HOH CA 10 .   ? 55.473  33.830  -39.113 1.00 27.60 ? 1391 HOH B O     1 
HETATM 9804  O O     . HOH CA 10 .   ? 65.330  21.590  -0.023  1.00 29.11 ? 1392 HOH B O     1 
HETATM 9805  O O     . HOH CA 10 .   ? 58.203  25.042  3.184   1.00 22.69 ? 1393 HOH B O     1 
HETATM 9806  O O     . HOH CA 10 .   ? 41.232  28.580  -30.414 1.00 26.84 ? 1394 HOH B O     1 
HETATM 9807  O O     . HOH CA 10 .   ? 39.199  22.806  -16.502 1.00 35.31 ? 1395 HOH B O     1 
HETATM 9808  O O     . HOH CA 10 .   ? 27.149  30.893  -26.199 1.00 24.89 ? 1396 HOH B O     1 
HETATM 9809  O O     . HOH CA 10 .   ? 56.602  24.587  -7.823  1.00 25.81 ? 1397 HOH B O     1 
HETATM 9810  O O     . HOH CA 10 .   ? 34.969  55.959  -5.796  1.00 31.36 ? 1398 HOH B O     1 
HETATM 9811  O O     . HOH CA 10 .   ? 33.497  28.112  -6.975  1.00 25.95 ? 1399 HOH B O     1 
HETATM 9812  O O     . HOH CA 10 .   ? 38.049  54.461  10.657  1.00 30.81 ? 1400 HOH B O     1 
HETATM 9813  O O     . HOH CA 10 .   ? 43.067  60.848  -21.717 1.00 24.43 ? 1401 HOH B O     1 
HETATM 9814  O O     . HOH CA 10 .   ? 32.875  44.046  -30.918 1.00 37.16 ? 1402 HOH B O     1 
HETATM 9815  O O     . HOH CA 10 .   ? 52.683  38.577  10.321  1.00 33.56 ? 1403 HOH B O     1 
HETATM 9816  O O     . HOH CA 10 .   ? 23.413  55.244  7.678   1.00 34.32 ? 1404 HOH B O     1 
HETATM 9817  O O     . HOH CA 10 .   ? 76.001  46.298  -23.685 1.00 29.05 ? 1405 HOH B O     1 
HETATM 9818  O O     . HOH CA 10 .   ? 42.524  40.250  11.825  1.00 33.77 ? 1406 HOH B O     1 
HETATM 9819  O O     . HOH CA 10 .   ? 67.487  17.614  0.370   1.00 42.57 ? 1407 HOH B O     1 
HETATM 9820  O O     . HOH CA 10 .   ? 15.241  39.745  1.605   1.00 38.14 ? 1408 HOH B O     1 
HETATM 9821  O O     . HOH CA 10 .   ? 68.240  27.845  -2.519  1.00 29.35 ? 1409 HOH B O     1 
HETATM 9822  O O     . HOH CA 10 .   ? 48.892  19.018  -36.379 1.00 32.95 ? 1410 HOH B O     1 
HETATM 9823  O O     . HOH CA 10 .   ? 55.704  21.840  -37.735 1.00 28.10 ? 1411 HOH B O     1 
HETATM 9824  O O     . HOH CA 10 .   ? 63.767  18.514  -5.408  1.00 36.70 ? 1412 HOH B O     1 
HETATM 9825  O O     . HOH CA 10 .   ? 28.683  42.143  -26.334 1.00 30.03 ? 1413 HOH B O     1 
HETATM 9826  O O     . HOH CA 10 .   ? 58.990  21.563  -6.205  1.00 35.75 ? 1414 HOH B O     1 
HETATM 9827  O O     . HOH CA 10 .   ? 52.628  22.369  5.367   1.00 35.90 ? 1415 HOH B O     1 
HETATM 9828  O O     . HOH CA 10 .   ? 63.489  19.740  -0.613  1.00 37.05 ? 1416 HOH B O     1 
HETATM 9829  O O     . HOH CA 10 .   ? 66.336  35.699  2.891   1.00 39.22 ? 1417 HOH B O     1 
HETATM 9830  O O     . HOH CA 10 .   ? 72.218  21.646  -28.100 1.00 41.80 ? 1418 HOH B O     1 
HETATM 9831  O O     . HOH CA 10 .   ? 20.765  62.071  -8.710  1.00 31.71 ? 1419 HOH B O     1 
HETATM 9832  O O     . HOH CA 10 .   ? 68.588  18.846  -21.751 1.00 41.53 ? 1420 HOH B O     1 
HETATM 9833  O O     . HOH CA 10 .   ? 57.757  35.613  -33.047 1.00 30.54 ? 1421 HOH B O     1 
HETATM 9834  O O     . HOH CA 10 .   ? 25.506  47.234  -23.998 1.00 33.77 ? 1422 HOH B O     1 
HETATM 9835  O O     . HOH CA 10 .   ? 67.523  23.933  -34.271 1.00 32.59 ? 1423 HOH B O     1 
HETATM 9836  O O     . HOH CA 10 .   ? 38.868  40.887  13.429  1.00 33.87 ? 1424 HOH B O     1 
HETATM 9837  O O     . HOH CA 10 .   ? 16.705  62.514  -7.242  1.00 31.73 ? 1425 HOH B O     1 
HETATM 9838  O O     . HOH CA 10 .   ? 56.257  42.687  -36.712 1.00 31.30 ? 1426 HOH B O     1 
HETATM 9839  O O     . HOH CA 10 .   ? 32.276  57.541  6.410   1.00 30.63 ? 1427 HOH B O     1 
HETATM 9840  O O     . HOH CA 10 .   ? 45.839  19.168  -5.749  1.00 42.78 ? 1428 HOH B O     1 
HETATM 9841  O O     . HOH CA 10 .   ? 29.134  36.366  -28.876 1.00 30.08 ? 1429 HOH B O     1 
HETATM 9842  O O     . HOH CA 10 .   ? 58.046  52.191  -23.912 1.00 32.84 ? 1430 HOH B O     1 
HETATM 9843  O O     . HOH CA 10 .   ? 59.568  15.692  -20.264 1.00 33.76 ? 1431 HOH B O     1 
HETATM 9844  O O     . HOH CA 10 .   ? 30.858  18.604  -12.154 1.00 33.18 ? 1432 HOH B O     1 
HETATM 9845  O O     . HOH CA 10 .   ? 61.965  46.129  2.715   1.00 30.97 ? 1433 HOH B O     1 
HETATM 9846  O O     . HOH CA 10 .   ? 63.679  28.309  0.436   1.00 28.70 ? 1434 HOH B O     1 
HETATM 9847  O O     . HOH CA 10 .   ? 61.836  21.592  -31.762 1.00 33.96 ? 1435 HOH B O     1 
HETATM 9848  O O     . HOH CA 10 .   ? 77.885  34.140  -20.679 1.00 36.53 ? 1436 HOH B O     1 
HETATM 9849  O O     . HOH CA 10 .   ? 79.450  37.472  -27.958 1.00 37.09 ? 1437 HOH B O     1 
HETATM 9850  O O     . HOH CA 10 .   ? 62.183  16.862  -26.880 1.00 32.67 ? 1438 HOH B O     1 
HETATM 9851  O O     . HOH CA 10 .   ? 49.805  56.570  -29.661 1.00 42.07 ? 1439 HOH B O     1 
HETATM 9852  O O     . HOH CA 10 .   ? 51.932  58.138  6.710   1.00 34.10 ? 1440 HOH B O     1 
HETATM 9853  O O     . HOH CA 10 .   ? 50.252  38.140  9.201   1.00 34.38 ? 1441 HOH B O     1 
HETATM 9854  O O     . HOH CA 10 .   ? 13.319  40.244  -0.668  1.00 36.84 ? 1442 HOH B O     1 
HETATM 9855  O O     . HOH CA 10 .   ? 51.276  59.129  0.194   1.00 38.00 ? 1443 HOH B O     1 
HETATM 9856  O O     . HOH CA 10 .   ? 42.544  50.781  -27.883 1.00 47.57 ? 1444 HOH B O     1 
HETATM 9857  O O     . HOH CA 10 .   ? 48.661  61.537  -15.713 1.00 43.53 ? 1445 HOH B O     1 
HETATM 9858  O O     . HOH CA 10 .   ? 59.788  33.528  -35.131 1.00 45.24 ? 1446 HOH B O     1 
HETATM 9859  O O     . HOH CA 10 .   ? 50.891  55.115  9.805   1.00 32.97 ? 1447 HOH B O     1 
HETATM 9860  O O     . HOH CA 10 .   ? 37.793  22.759  -25.390 1.00 45.84 ? 1448 HOH B O     1 
HETATM 9861  O O     . HOH CA 10 .   ? 54.514  36.901  9.809   1.00 34.41 ? 1449 HOH B O     1 
HETATM 9862  O O     . HOH CA 10 .   ? 22.376  24.644  -13.383 1.00 37.22 ? 1450 HOH B O     1 
HETATM 9863  O O     . HOH CA 10 .   ? 75.967  24.107  -12.457 1.00 30.00 ? 1451 HOH B O     1 
HETATM 9864  O O     . HOH CA 10 .   ? 73.636  36.956  -2.763  1.00 31.30 ? 1452 HOH B O     1 
HETATM 9865  O O     . HOH CA 10 .   ? 36.245  56.754  5.977   1.00 35.96 ? 1453 HOH B O     1 
HETATM 9866  O O     . HOH CA 10 .   ? 31.521  27.548  -26.070 1.00 49.95 ? 1454 HOH B O     1 
HETATM 9867  O O     . HOH CA 10 .   ? 47.677  53.589  -29.154 1.00 40.53 ? 1455 HOH B O     1 
HETATM 9868  O O     . HOH CA 10 .   ? 39.339  22.004  -12.323 1.00 32.94 ? 1456 HOH B O     1 
HETATM 9869  O O     . HOH CA 10 .   ? 26.739  49.041  -22.767 1.00 33.99 ? 1457 HOH B O     1 
HETATM 9870  O O     . HOH CA 10 .   ? 30.617  46.838  -6.846  1.00 31.57 ? 1458 HOH B O     1 
HETATM 9871  O O     . HOH CA 10 .   ? 76.592  41.780  -19.723 1.00 31.63 ? 1459 HOH B O     1 
HETATM 9872  O O     . HOH CA 10 .   ? 28.472  46.560  -27.862 1.00 42.73 ? 1460 HOH B O     1 
HETATM 9873  O O     . HOH CA 10 .   ? 45.683  20.983  0.408   1.00 33.98 ? 1461 HOH B O     1 
HETATM 9874  O O     . HOH CA 10 .   ? 36.400  47.087  -31.422 1.00 39.42 ? 1462 HOH B O     1 
HETATM 9875  O O     . HOH CA 10 .   ? 58.343  56.988  -18.090 1.00 32.76 ? 1464 HOH B O     1 
HETATM 9876  O O     . HOH CA 10 .   ? 19.046  59.331  1.894   1.00 31.32 ? 1465 HOH B O     1 
HETATM 9877  O O     . HOH CA 10 .   ? 36.181  36.307  11.858  1.00 44.74 ? 1466 HOH B O     1 
HETATM 9878  O O     . HOH CA 10 .   ? 43.776  33.594  10.064  1.00 41.37 ? 1467 HOH B O     1 
HETATM 9879  O O     . HOH CA 10 .   ? 66.334  40.115  0.615   1.00 36.26 ? 1468 HOH B O     1 
HETATM 9880  O O     . HOH CA 10 .   ? 26.217  21.992  -13.685 1.00 28.47 ? 1469 HOH B O     1 
HETATM 9881  O O     . HOH CA 10 .   ? 57.653  33.370  -37.432 1.00 34.97 ? 1470 HOH B O     1 
HETATM 9882  O O     . HOH CA 10 .   ? 36.711  50.547  11.952  1.00 35.24 ? 1471 HOH B O     1 
HETATM 9883  O O     . HOH CA 10 .   ? 46.837  46.689  -34.397 1.00 37.54 ? 1472 HOH B O     1 
HETATM 9884  O O     . HOH CA 10 .   ? 68.907  51.695  -27.210 1.00 31.60 ? 1473 HOH B O     1 
HETATM 9885  O O     . HOH CA 10 .   ? 63.282  56.466  -11.140 1.00 42.64 ? 1474 HOH B O     1 
HETATM 9886  O O     . HOH CA 10 .   ? 52.771  54.127  -28.212 1.00 35.87 ? 1475 HOH B O     1 
HETATM 9887  O O     . HOH CA 10 .   ? 42.893  19.710  -11.667 1.00 47.52 ? 1476 HOH B O     1 
HETATM 9888  O O     . HOH CA 10 .   ? 45.598  60.962  -7.569  1.00 46.84 ? 1477 HOH B O     1 
HETATM 9889  O O     . HOH CA 10 .   ? 18.096  33.826  2.255   1.00 37.31 ? 1478 HOH B O     1 
HETATM 9890  O O     . HOH CA 10 .   ? 38.824  43.331  -30.652 1.00 33.18 ? 1479 HOH B O     1 
HETATM 9891  O O     . HOH CA 10 .   ? 22.585  31.199  4.183   1.00 37.02 ? 1480 HOH B O     1 
HETATM 9892  O O     . HOH CA 10 .   ? 43.694  44.964  -38.353 1.00 45.36 ? 1481 HOH B O     1 
HETATM 9893  O O     . HOH CA 10 .   ? 36.904  55.453  -3.913  1.00 37.45 ? 1482 HOH B O     1 
HETATM 9894  O O     . HOH CA 10 .   ? 62.105  47.427  -33.997 1.00 32.61 ? 1483 HOH B O     1 
HETATM 9895  O O     . HOH CA 10 .   ? 41.445  34.416  -34.268 1.00 32.60 ? 1484 HOH B O     1 
HETATM 9896  O O     . HOH CA 10 .   ? 22.728  33.532  -1.498  1.00 29.15 ? 1485 HOH B O     1 
HETATM 9897  O O     . HOH CA 10 .   ? 50.242  60.614  4.454   1.00 33.15 ? 1486 HOH B O     1 
HETATM 9898  O O     . HOH CA 10 .   ? 69.904  18.233  -26.946 1.00 31.92 ? 1487 HOH B O     1 
HETATM 9899  O O     . HOH CA 10 .   ? 49.129  13.005  -4.216  1.00 40.84 ? 1488 HOH B O     1 
HETATM 9900  O O     . HOH CA 10 .   ? 59.830  23.352  4.608   1.00 34.45 ? 1489 HOH B O     1 
HETATM 9901  O O     . HOH CA 10 .   ? 56.491  16.711  -13.571 1.00 32.50 ? 1490 HOH B O     1 
HETATM 9902  O O     . HOH CA 10 .   ? 45.283  21.415  -33.718 1.00 36.83 ? 1491 HOH B O     1 
HETATM 9903  O O     . HOH CA 10 .   ? 13.391  51.749  -13.693 1.00 39.10 ? 1492 HOH B O     1 
HETATM 9904  O O     . HOH CA 10 .   ? 27.318  64.820  -7.636  1.00 38.10 ? 1493 HOH B O     1 
HETATM 9905  O O     . HOH CA 10 .   ? 16.023  28.386  -18.833 1.00 38.12 ? 1494 HOH B O     1 
HETATM 9906  O O     . HOH CA 10 .   ? 51.090  17.832  -8.749  1.00 29.55 ? 1495 HOH B O     1 
HETATM 9907  O O     . HOH CA 10 .   ? 44.255  63.099  -6.581  1.00 39.48 ? 1496 HOH B O     1 
HETATM 9908  O O     . HOH CA 10 .   ? 15.164  31.638  -4.909  1.00 33.26 ? 1497 HOH B O     1 
HETATM 9909  O O     . HOH CA 10 .   ? 77.568  25.991  -16.589 1.00 39.49 ? 1498 HOH B O     1 
HETATM 9910  O O     . HOH CA 10 .   ? 66.410  30.529  -31.712 1.00 40.43 ? 1499 HOH B O     1 
HETATM 9911  O O     . HOH CA 10 .   ? 56.929  27.439  -40.643 1.00 36.28 ? 1500 HOH B O     1 
HETATM 9912  O O     . HOH CA 10 .   ? 38.067  49.746  -28.128 1.00 36.49 ? 1501 HOH B O     1 
HETATM 9913  O O     . HOH CA 10 .   ? 17.353  65.990  -16.352 1.00 39.09 ? 1502 HOH B O     1 
HETATM 9914  O O     . HOH CA 10 .   ? 58.098  45.507  4.545   1.00 38.19 ? 1503 HOH B O     1 
HETATM 9915  O O     . HOH CA 10 .   ? 39.948  16.799  -0.370  1.00 41.88 ? 1505 HOH B O     1 
HETATM 9916  O O     . HOH CA 10 .   ? 48.524  44.567  12.286  1.00 36.53 ? 1506 HOH B O     1 
HETATM 9917  O O     . HOH CA 10 .   ? 58.050  30.386  -44.572 1.00 38.02 ? 1507 HOH B O     1 
HETATM 9918  O O     . HOH CA 10 .   ? 43.349  24.755  3.187   1.00 31.69 ? 1508 HOH B O     1 
HETATM 9919  O O     . HOH CA 10 .   ? 46.054  59.821  -25.997 1.00 37.67 ? 1509 HOH B O     1 
HETATM 9920  O O     . HOH CA 10 .   ? 13.664  51.536  -9.812  1.00 40.67 ? 1510 HOH B O     1 
HETATM 9921  O O     . HOH CA 10 .   ? 49.769  21.631  6.665   1.00 39.84 ? 1511 HOH B O     1 
HETATM 9922  O O     . HOH CA 10 .   ? 45.492  24.209  -33.836 1.00 32.32 ? 1512 HOH B O     1 
HETATM 9923  O O     . HOH CA 10 .   ? 58.765  41.745  -37.915 1.00 44.21 ? 1513 HOH B O     1 
HETATM 9924  O O     . HOH CA 10 .   ? 51.521  17.420  -39.451 1.00 39.84 ? 1514 HOH B O     1 
HETATM 9925  O O     . HOH CA 10 .   ? 18.492  32.946  -1.070  1.00 46.16 ? 1515 HOH B O     1 
HETATM 9926  O O     . HOH CA 10 .   ? 45.035  38.900  -37.892 1.00 43.13 ? 1516 HOH B O     1 
HETATM 9927  O O     . HOH CA 10 .   ? 44.977  28.078  -31.453 1.00 33.01 ? 1517 HOH B O     1 
HETATM 9928  O O     . HOH CA 10 .   ? 30.255  41.941  -30.783 1.00 41.38 ? 1518 HOH B O     1 
HETATM 9929  O O     . HOH CA 10 .   ? 23.676  43.253  -25.381 1.00 40.63 ? 1519 HOH B O     1 
HETATM 9930  O O     . HOH CA 10 .   ? 38.825  25.017  -28.758 1.00 43.67 ? 1520 HOH B O     1 
HETATM 9931  O O     . HOH CA 10 .   ? 65.830  41.744  -33.394 1.00 44.12 ? 1521 HOH B O     1 
HETATM 9932  O O     . HOH CA 10 .   ? 67.434  18.961  -33.905 1.00 42.37 ? 1522 HOH B O     1 
HETATM 9933  O O     . HOH CA 10 .   ? 60.139  21.646  -1.811  1.00 41.47 ? 1523 HOH B O     1 
HETATM 9934  O O     . HOH CA 10 .   ? 47.235  14.662  -3.451  1.00 34.94 ? 1524 HOH B O     1 
HETATM 9935  O O     . HOH CA 10 .   ? 30.724  27.493  1.825   1.00 40.18 ? 1525 HOH B O     1 
HETATM 9936  O O     . HOH CA 10 .   ? 32.164  63.652  -1.227  1.00 41.02 ? 1526 HOH B O     1 
HETATM 9937  O O     . HOH CA 10 .   ? 61.584  31.679  -39.415 1.00 44.54 ? 1527 HOH B O     1 
HETATM 9938  O O     . HOH CA 10 .   ? 55.161  50.720  7.516   1.00 38.47 ? 1528 HOH B O     1 
HETATM 9939  O O     . HOH CA 10 .   ? 58.714  20.924  -34.292 1.00 32.22 ? 1529 HOH B O     1 
HETATM 9940  O O     . HOH CA 10 .   ? 40.389  22.670  -18.755 1.00 38.29 ? 1530 HOH B O     1 
HETATM 9941  O O     . HOH CA 10 .   ? 11.347  48.544  -15.947 1.00 35.91 ? 1531 HOH B O     1 
HETATM 9942  O O     . HOH CA 10 .   ? 33.666  39.318  -6.420  1.00 38.54 ? 1532 HOH B O     1 
HETATM 9943  O O     . HOH CA 10 .   ? 19.527  53.849  -20.263 1.00 37.75 ? 1533 HOH B O     1 
HETATM 9944  O O     . HOH CA 10 .   ? 39.962  16.705  -20.063 1.00 39.91 ? 1534 HOH B O     1 
HETATM 9945  O O     . HOH CA 10 .   ? 57.014  43.809  -34.241 1.00 37.32 ? 1536 HOH B O     1 
HETATM 9946  O O     . HOH CA 10 .   ? 70.861  27.871  -31.432 1.00 46.01 ? 1537 HOH B O     1 
HETATM 9947  O O     . HOH CA 10 .   ? 46.416  62.104  -19.146 1.00 32.14 ? 1538 HOH B O     1 
HETATM 9948  O O     . HOH CA 10 .   ? 21.549  65.700  -5.493  1.00 46.28 ? 1539 HOH B O     1 
HETATM 9949  O O     . HOH CA 10 .   ? 14.381  63.141  -6.050  1.00 37.85 ? 1540 HOH B O     1 
HETATM 9950  O O     . HOH CA 10 .   ? 59.537  55.294  1.381   1.00 43.20 ? 1541 HOH B O     1 
HETATM 9951  O O     . HOH CA 10 .   ? 63.197  28.615  -38.021 1.00 41.29 ? 1542 HOH B O     1 
HETATM 9952  O O     . HOH CA 10 .   ? 40.217  48.442  -27.485 1.00 29.34 ? 1543 HOH B O     1 
HETATM 9953  O O     . HOH CA 10 .   ? 62.899  17.487  -20.249 1.00 48.01 ? 1544 HOH B O     1 
HETATM 9954  O O     . HOH CA 10 .   ? 63.974  34.131  -36.441 1.00 39.05 ? 1545 HOH B O     1 
HETATM 9955  O O     . HOH CA 10 .   ? 41.009  45.446  -32.622 1.00 36.98 ? 1546 HOH B O     1 
HETATM 9956  O O     . HOH CA 10 .   ? 56.355  37.173  7.929   1.00 47.73 ? 1547 HOH B O     1 
HETATM 9957  O O     . HOH CA 10 .   ? 34.870  27.402  -9.040  1.00 47.91 ? 1548 HOH B O     1 
HETATM 9958  O O     . HOH CA 10 .   ? 12.187  57.755  -1.047  1.00 38.71 ? 1549 HOH B O     1 
HETATM 9959  O O     . HOH CA 10 .   ? 32.833  21.364  -5.979  1.00 42.39 ? 1550 HOH B O     1 
HETATM 9960  O O     . HOH CA 10 .   ? 50.487  60.394  -4.501  1.00 47.35 ? 1551 HOH B O     1 
HETATM 9961  O O     . HOH CA 10 .   ? 43.403  43.007  12.592  1.00 39.35 ? 1552 HOH B O     1 
HETATM 9962  O O     . HOH CA 10 .   ? 17.947  50.911  -19.779 1.00 43.05 ? 1553 HOH B O     1 
HETATM 9963  O O     . HOH CA 10 .   ? 25.390  51.478  -24.125 1.00 47.79 ? 1554 HOH B O     1 
HETATM 9964  O O     . HOH CA 10 .   ? 37.896  57.997  -3.758  1.00 39.07 ? 1555 HOH B O     1 
HETATM 9965  O O     . HOH CA 10 .   ? 28.256  24.693  -10.199 1.00 34.77 ? 1556 HOH B O     1 
HETATM 9966  O O     . HOH CA 10 .   ? 47.149  36.522  10.456  1.00 41.23 ? 1557 HOH B O     1 
HETATM 9967  O O     . HOH CA 10 .   ? 27.026  24.959  -7.021  1.00 41.97 ? 1558 HOH B O     1 
HETATM 9968  O O     . HOH CA 10 .   ? 69.757  20.920  -26.921 1.00 41.47 ? 1559 HOH B O     1 
HETATM 9969  O O     . HOH CA 10 .   ? 69.710  28.484  -29.018 1.00 42.45 ? 1560 HOH B O     1 
HETATM 9970  O O     . HOH CA 10 .   ? 40.995  58.036  -0.185  1.00 43.64 ? 1561 HOH B O     1 
HETATM 9971  O O     . HOH CA 10 .   ? 50.399  57.607  9.057   1.00 42.83 ? 1562 HOH B O     1 
HETATM 9972  O O     . HOH CA 10 .   ? 13.530  62.095  -3.592  1.00 36.05 ? 1563 HOH B O     1 
HETATM 9973  O O     . HOH CA 10 .   ? 18.136  64.747  -6.022  1.00 46.69 ? 1564 HOH B O     1 
HETATM 9974  O O     . HOH CA 10 .   ? 33.451  63.621  -11.165 1.00 40.89 ? 1565 HOH B O     1 
HETATM 9975  O O     . HOH CA 10 .   ? 33.692  53.481  13.448  1.00 49.28 ? 1566 HOH B O     1 
HETATM 9976  O O     . HOH CA 10 .   ? 58.454  26.422  8.076   1.00 44.13 ? 1567 HOH B O     1 
HETATM 9977  O O     . HOH CA 10 .   ? 60.162  37.886  -33.086 1.00 37.68 ? 1569 HOH B O     1 
HETATM 9978  O O     . HOH CA 10 .   ? 14.400  29.431  -7.805  1.00 44.72 ? 1570 HOH B O     1 
HETATM 9979  O O     . HOH CA 10 .   ? 38.682  62.098  -19.396 1.00 42.31 ? 1571 HOH B O     1 
HETATM 9980  O O     . HOH CA 10 .   ? 46.721  17.952  -2.774  1.00 36.25 ? 1573 HOH B O     1 
HETATM 9981  O O     . HOH CA 10 .   ? 63.367  42.984  3.648   1.00 44.87 ? 1574 HOH B O     1 
HETATM 9982  O O     . HOH CA 10 .   ? 44.366  22.800  1.738   1.00 45.75 ? 1575 HOH B O     1 
HETATM 9983  O O     . HOH CA 10 .   ? 45.559  28.199  11.795  1.00 40.79 ? 1576 HOH B O     1 
HETATM 9984  O O     . HOH CA 10 .   ? 67.923  30.075  3.439   1.00 45.41 ? 1577 HOH B O     1 
HETATM 9985  O O     . HOH CA 10 .   ? 54.450  45.233  8.733   1.00 39.38 ? 1578 HOH B O     1 
HETATM 9986  O O     . HOH CA 10 .   ? 39.920  20.755  1.003   1.00 38.75 ? 1579 HOH B O     1 
HETATM 9987  O O     . HOH CA 10 .   ? 73.142  31.579  -3.624  1.00 44.59 ? 1580 HOH B O     1 
HETATM 9988  O O     . HOH CA 10 .   ? 61.837  43.683  -35.448 1.00 43.38 ? 1581 HOH B O     1 
HETATM 9989  O O     . HOH CA 10 .   ? 62.147  31.945  -36.346 1.00 49.65 ? 1582 HOH B O     1 
HETATM 9990  O O     . HOH CA 10 .   ? 64.442  39.390  -33.219 1.00 33.66 ? 1583 HOH B O     1 
HETATM 9991  O O     . HOH CA 10 .   ? 24.294  63.598  1.531   1.00 43.85 ? 1585 HOH B O     1 
HETATM 9992  O O     . HOH CA 10 .   ? 71.585  50.871  -26.098 1.00 33.71 ? 1586 HOH B O     1 
HETATM 9993  O O     . HOH CA 10 .   ? 71.460  47.196  -9.640  1.00 38.62 ? 1587 HOH B O     1 
HETATM 9994  O O     . HOH CA 10 .   ? 56.063  23.634  8.012   1.00 45.74 ? 1588 HOH B O     1 
HETATM 9995  O O     . HOH CA 10 .   ? 66.506  20.702  -16.038 1.00 47.79 ? 1589 HOH B O     1 
HETATM 9996  O O     . HOH CA 10 .   ? 75.438  34.344  -21.770 1.00 40.94 ? 1590 HOH B O     1 
HETATM 9997  O O     . HOH CA 10 .   ? 11.409  28.770  -14.056 1.00 44.49 ? 1591 HOH B O     1 
HETATM 9998  O O     . HOH CA 10 .   ? 46.086  18.162  -12.989 1.00 33.63 ? 1592 HOH B O     1 
HETATM 9999  O O     . HOH CA 10 .   ? 43.544  29.562  -30.071 1.00 34.06 ? 1593 HOH B O     1 
HETATM 10000 O O     . HOH CA 10 .   ? 21.179  30.055  -4.342  1.00 30.65 ? 1594 HOH B O     1 
HETATM 10001 O O     . HOH CA 10 .   ? 21.713  59.369  -0.140  1.00 38.30 ? 1595 HOH B O     1 
HETATM 10002 O O     . HOH CA 10 .   ? 48.139  33.842  8.957   1.00 27.37 ? 1596 HOH B O     1 
HETATM 10003 O O     . HOH CA 10 .   ? 15.680  62.228  -15.495 1.00 47.23 ? 1597 HOH B O     1 
HETATM 10004 O O     . HOH CA 10 .   ? 28.154  44.498  -26.401 1.00 40.42 ? 1598 HOH B O     1 
# 
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   LEU 1   1   1   LEU LEU A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   THR 4   4   4   THR THR A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   HIS 7   7   7   HIS HIS A . n 
A 1 8   ASP 8   8   8   ASP ASP A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  TYR 11  11  11  TYR TYR A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  PHE 14  14  14  PHE PHE A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  TYR 16  16  16  TYR TYR A . n 
A 1 17  ASP 17  17  17  ASP ASP A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  GLY 35  35  35  GLY GLY A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  CYS 39  39  39  CYS CYS A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  ASP 70  70  70  ASP ASP A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  GLN 77  77  77  GLN GLN A . n 
A 1 78  GLN 78  78  78  GLN GLN A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  ASP 93  93  93  ASP ASP A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  ASN 97  97  97  ASN ASN A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 ARG 101 101 101 ARG ARG A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 THR 119 119 119 THR THR A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 TYR 122 122 122 TYR TYR A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 TRP 129 129 129 TRP TRP A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 ASN 135 135 135 ASN ASN A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 TYR 138 138 138 TYR TYR A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 TRP 140 140 140 TRP TRP A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 GLU 142 142 142 GLU GLU A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 TYR 147 147 147 TYR TYR A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 GLN 152 152 152 GLN GLN A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 HIS 168 168 168 HIS HIS A . n 
A 1 169 PRO 169 169 169 PRO PRO A . n 
A 1 170 ASN 170 170 170 ASN ASN A . n 
A 1 171 HIS 171 171 171 HIS HIS A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 SER 174 174 174 SER SER A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 HIS 177 177 177 HIS HIS A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 THR 181 181 181 THR THR A . n 
A 1 182 ARG 182 182 182 ARG ARG A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 PHE 188 188 188 PHE PHE A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 ASN 190 190 190 ASN ASN A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 HIS 195 195 195 HIS HIS A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 ARG 210 210 210 ARG ARG A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 HIS 214 214 214 HIS HIS A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 GLU 218 218 218 GLU GLU A . n 
A 1 219 LYS 219 219 219 LYS LYS A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 ASN 224 224 224 ASN ASN A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 PRO 226 226 226 PRO PRO A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 TYR 235 235 235 TYR TYR A . n 
A 1 236 ARG 236 236 236 ARG ARG A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 SER 238 238 238 SER SER 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 THR 241 241 241 THR THR A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 HIS 243 243 243 HIS HIS A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ARG 248 248 248 ARG ARG A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 LYS 250 250 250 LYS LYS A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 GLU 252 252 252 GLU GLU A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 ILE 254 254 254 ILE ILE A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 GLY 261 261 261 GLY GLY A . n 
A 1 262 THR 262 262 262 THR THR A . n 
A 1 263 PRO 263 263 263 PRO PRO A . n 
A 1 264 GLN 264 264 264 GLN GLN A . n 
A 1 265 LEU 265 265 265 LEU LEU A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 SER 269 269 269 SER SER A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 VAL 271 271 271 VAL VAL A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 PRO 273 273 273 PRO PRO A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 TYR 276 276 276 TYR TYR A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ASN 281 281 281 ASN ASN A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 PRO 283 283 283 PRO PRO A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 HIS 288 288 288 HIS HIS A . n 
A 1 289 PRO 289 289 289 PRO PRO A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 VAL 291 291 291 VAL VAL A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 GLN 293 293 293 GLN GLN A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 LEU 295 295 295 LEU LEU A . n 
A 1 296 HIS 296 296 296 HIS HIS A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 ARG 300 300 300 ARG ARG A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 PHE 302 302 302 PHE PHE A . n 
A 1 303 ILE 303 303 303 ILE ILE A . n 
A 1 304 ASN 304 304 304 ASN ASN A . n 
A 1 305 ILE 305 305 305 ILE ILE A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 PRO 308 308 308 PRO PRO A . n 
A 1 309 ASN 309 309 309 ASN ASN A . n 
A 1 310 PRO 310 310 310 PRO PRO A . n 
A 1 311 ILE 311 311 311 ILE ILE A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 PRO 313 313 313 PRO PRO A . n 
A 1 314 THR 314 314 314 THR THR A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 THR 317 317 317 THR THR A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 GLY 320 320 320 GLY GLY A . n 
A 1 321 ILE 321 321 321 ILE ILE A . n 
A 1 322 SER 322 322 322 SER SER A . n 
A 1 323 ASN 323 323 323 ASN ASN A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 PHE 325 325 325 PHE PHE A . n 
A 1 326 TYR 326 326 326 TYR TYR A . n 
A 1 327 GLN 327 327 327 GLN GLN A . n 
A 1 328 CYS 328 328 328 CYS CYS A . n 
A 1 329 SER 329 329 329 SER SER A . n 
A 1 330 PHE 330 330 330 PHE PHE A . n 
A 1 331 SER 331 331 331 SER SER 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 PRO 334 334 334 PRO PRO A . n 
A 1 335 PHE 335 335 335 PHE PHE A . n 
A 1 336 THR 336 336 336 THR THR A . n 
A 1 337 THR 337 337 337 THR THR A . n 
A 1 338 PRO 338 338 338 PRO PRO A . n 
A 1 339 PRO 339 339 339 PRO PRO A . n 
A 1 340 PHE 340 340 340 PHE PHE A . n 
A 1 341 GLY 341 341 341 GLY GLY A . n 
A 1 342 PHE 342 342 342 PHE PHE A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 PRO 344 344 344 PRO PRO A . n 
A 1 345 SER 345 345 345 SER SER A . n 
A 1 346 SER 346 346 346 SER SER A . n 
A 1 347 SER 347 347 347 SER SER A . n 
A 1 348 TYR 348 348 348 TYR TYR A . n 
A 1 349 PRO 349 349 349 PRO PRO A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 PRO 351 351 351 PRO PRO A . n 
A 1 352 ASN 352 352 352 ASN ASN A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 THR 354 354 354 THR THR A . n 
A 1 355 PHE 355 355 355 PHE PHE A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 HIS 357 357 357 HIS HIS A . n 
A 1 358 PHE 358 358 358 PHE PHE A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 SER 360 360 360 SER SER A . n 
A 1 361 LYS 361 361 361 LYS LYS A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 ALA 363 363 363 ALA ALA A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 LEU 366 366 366 LEU LEU A . n 
A 1 367 SER 367 367 367 SER SER A . n 
A 1 368 TYR 368 368 368 TYR TYR A . n 
A 1 369 GLY 369 369 369 GLY GLY A . n 
A 1 370 SER 370 370 370 SER SER A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 THR 372 372 372 THR THR A . n 
A 1 373 LEU 373 373 373 LEU LEU A . n 
A 1 374 LYS 374 374 374 LYS LYS A . n 
A 1 375 SER 375 375 375 SER SER A . n 
A 1 376 SER 376 376 376 SER SER A . n 
A 1 377 SER 377 377 377 SER SER A . n 
A 1 378 ASN 378 378 378 ASN ASN A . n 
A 1 379 VAL 379 379 379 VAL VAL A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 SER 382 382 382 SER SER A . n 
A 1 383 PRO 383 383 383 PRO PRO A . n 
A 1 384 ASN 384 384 384 ASN ASN A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 LYS 386 386 386 LYS LYS A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 ASN 388 388 388 ASN ASN A . n 
A 1 389 TYR 389 389 389 TYR TYR A . n 
A 1 390 TYR 390 390 390 TYR TYR A . n 
A 1 391 SER 391 391 391 SER SER A . n 
A 1 392 ASN 392 392 392 ASN ASN A . n 
A 1 393 LEU 393 393 393 LEU LEU A . n 
A 1 394 THR 394 394 394 THR THR A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 LEU 396 396 396 LEU LEU A . n 
A 1 397 SER 397 397 397 SER SER A . n 
A 1 398 HIS 398 398 398 HIS HIS A . n 
A 1 399 CYS 399 399 399 CYS CYS A . n 
A 1 400 VAL 400 400 400 VAL VAL A . n 
A 1 401 SER 401 401 401 SER SER A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 MET 403 403 403 MET MET A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 LYS 405 405 405 LYS LYS A . n 
A 1 406 ILE 406 406 406 ILE ILE A . n 
A 1 407 GLY 407 407 407 GLY GLY A . n 
A 1 408 GLU 408 408 408 GLU GLU A . n 
A 1 409 LEU 409 409 409 LEU LEU A . n 
A 1 410 LEU 410 410 410 LEU LEU A . n 
A 1 411 SER 411 411 411 SER SER A . n 
A 1 412 THR 412 412 412 THR THR A . n 
A 1 413 ASP 413 413 413 ASP ASP A . n 
A 1 414 ALA 414 414 414 ALA ALA A . n 
A 1 415 LEU 415 415 415 LEU LEU A . n 
A 1 416 LYS 416 416 416 LYS LYS A . n 
A 1 417 PRO 417 417 417 PRO PRO A . n 
A 1 418 TYR 418 418 418 TYR TYR A . n 
A 1 419 LYS 419 419 419 LYS LYS A . n 
A 1 420 VAL 420 420 420 VAL VAL A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 ASP 422 422 422 ASP ASP A . n 
A 1 423 LEU 423 423 423 LEU LEU A . n 
A 1 424 PRO 424 424 424 PRO PRO A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 VAL 426 426 426 VAL VAL A . n 
A 1 427 GLU 427 427 427 GLU GLU A . n 
A 1 428 GLY 428 428 428 GLY GLY A . n 
A 1 429 PHE 429 429 429 PHE PHE A . n 
A 1 430 ASN 430 430 430 ASN ASN A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 LEU 432 432 432 LEU LEU A . n 
A 1 433 GLY 433 433 433 GLY GLY A . n 
A 1 434 ILE 434 434 434 ILE ILE A . n 
A 1 435 PRO 435 435 435 PRO PRO A . n 
A 1 436 LEU 436 436 436 LEU LEU A . n 
A 1 437 PRO 437 437 437 PRO PRO A . n 
A 1 438 LYS 438 438 438 LYS LYS A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 GLN 440 440 440 GLN GLN A . n 
A 1 441 THR 441 441 441 THR THR A . n 
A 1 442 ASP 442 442 442 ASP ASP A . n 
A 1 443 ASP 443 443 443 ASP ASP A . n 
A 1 444 ALA 444 444 444 ALA ALA A . n 
A 1 445 ALA 445 445 445 ALA ALA A . n 
A 1 446 PHE 446 446 446 PHE PHE A . n 
A 1 447 GLU 447 447 447 GLU GLU A . n 
A 1 448 THR 448 448 448 THR THR A . n 
A 1 449 PHE 449 449 449 PHE PHE A . n 
A 1 450 CYS 450 450 450 CYS CYS A . n 
A 1 451 ARG 451 451 451 ARG ARG A . n 
A 1 452 GLU 452 452 452 GLU GLU A . n 
A 1 453 SER 453 453 453 SER SER A . n 
A 1 454 VAL 454 454 454 VAL VAL A . n 
A 1 455 ALA 455 455 455 ALA ALA A . n 
A 1 456 SER 456 456 456 SER SER A . n 
A 1 457 TYR 457 457 457 TYR TYR A . n 
A 1 458 TRP 458 458 458 TRP TRP A . n 
A 1 459 HIS 459 459 459 HIS HIS A . n 
A 1 460 TYR 460 460 460 TYR TYR A . n 
A 1 461 HIS 461 461 461 HIS HIS A . n 
A 1 462 GLY 462 462 462 GLY GLY A . n 
A 1 463 GLY 463 463 463 GLY GLY A . n 
A 1 464 CYS 464 464 464 CYS CYS A . n 
A 1 465 LEU 465 465 465 LEU LEU A . n 
A 1 466 VAL 466 466 466 VAL VAL A . n 
A 1 467 GLY 467 467 467 GLY GLY A . n 
A 1 468 LYS 468 468 468 LYS LYS A . n 
A 1 469 VAL 469 469 469 VAL VAL A . n 
A 1 470 LEU 470 470 470 LEU LEU A . n 
A 1 471 ASP 471 471 471 ASP ASP A . n 
A 1 472 GLY 472 472 472 GLY GLY A . n 
A 1 473 ASP 473 473 473 ASP ASP A . n 
A 1 474 PHE 474 474 474 PHE PHE A . n 
A 1 475 ARG 475 475 475 ARG ARG A . n 
A 1 476 VAL 476 476 476 VAL VAL A . n 
A 1 477 THR 477 477 477 THR THR A . n 
A 1 478 GLY 478 478 478 GLY GLY A . n 
A 1 479 ILE 479 479 479 ILE ILE A . n 
A 1 480 ASN 480 480 480 ASN ASN A . n 
A 1 481 ALA 481 481 481 ALA ALA A . n 
A 1 482 LEU 482 482 482 LEU LEU A . n 
A 1 483 ARG 483 483 483 ARG ARG A . n 
A 1 484 VAL 484 484 484 VAL VAL A . n 
A 1 485 VAL 485 485 485 VAL VAL A . n 
A 1 486 ASP 486 486 486 ASP ASP A . n 
A 1 487 GLY 487 487 487 GLY GLY A . n 
A 1 488 SER 488 488 488 SER SER A . n 
A 1 489 THR 489 489 489 THR THR A . n 
A 1 490 PHE 490 490 490 PHE PHE A . n 
A 1 491 PRO 491 491 491 PRO PRO A . n 
A 1 492 TYR 492 492 492 TYR TYR A . n 
A 1 493 THR 493 493 493 THR THR A . n 
A 1 494 PRO 494 494 494 PRO PRO A . n 
A 1 495 ALA 495 495 495 ALA ALA A . n 
A 1 496 SER 496 496 496 SER SER A . n 
A 1 497 HIS 497 497 497 HIS HIS A . n 
A 1 498 PRO 498 498 498 PRO PRO A . n 
A 1 499 GLN 499 499 499 GLN GLN A . n 
A 1 500 GLY 500 500 500 GLY GLY A . n 
A 1 501 PHE 501 501 501 PHE PHE A . n 
A 1 502 TYR 502 502 502 TYR TYR A . n 
A 1 503 LEU 503 503 503 LEU LEU A . n 
A 1 504 MET 504 504 504 MET MET A . n 
A 1 505 LEU 505 505 505 LEU LEU A . n 
A 1 506 GLY 506 506 506 GLY GLY A . n 
A 1 507 ARG 507 507 507 ARG ARG A . n 
A 1 508 TYR 508 508 508 TYR TYR A . n 
A 1 509 VAL 509 509 509 VAL VAL A . n 
A 1 510 GLY 510 510 510 GLY GLY A . n 
A 1 511 ILE 511 511 511 ILE ILE A . n 
A 1 512 LYS 512 512 512 LYS LYS A . n 
A 1 513 ILE 513 513 513 ILE ILE A . n 
A 1 514 LEU 514 514 514 LEU LEU A . n 
A 1 515 GLN 515 515 515 GLN GLN A . n 
A 1 516 GLU 516 516 516 GLU GLU A . n 
A 1 517 ARG 517 517 517 ARG ARG A . n 
A 1 518 SER 518 518 518 SER SER A . n 
A 1 519 ALA 519 519 519 ALA ALA A . n 
A 1 520 SER 520 520 520 SER SER A . n 
A 1 521 ASP 521 521 521 ASP ASP A . n 
B 1 1   LEU 1   1   1   LEU LEU B . n 
B 1 2   ALA 2   2   2   ALA ALA B . n 
B 1 3   THR 3   3   3   THR THR B . n 
B 1 4   THR 4   4   4   THR THR B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   ASP 6   6   6   ASP ASP B . n 
B 1 7   HIS 7   7   7   HIS HIS B . n 
B 1 8   ASP 8   8   8   ASP ASP B . n 
B 1 9   PHE 9   9   9   PHE PHE B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  TYR 11  11  11  TYR TYR B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  SER 13  13  13  SER SER B . n 
B 1 14  PHE 14  14  14  PHE PHE B . n 
B 1 15  ALA 15  15  15  ALA ALA B . n 
B 1 16  TYR 16  16  16  TYR TYR B . n 
B 1 17  ASP 17  17  17  ASP ASP B . n 
B 1 18  ALA 18  18  18  ALA ALA B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  ASP 20  20  20  ASP ASP B . n 
B 1 21  LEU 21  21  21  LEU LEU B . n 
B 1 22  GLU 22  22  22  GLU GLU B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  GLY 25  25  25  GLY GLY B . n 
B 1 26  SER 26  26  26  SER SER B . n 
B 1 27  TYR 27  27  27  TYR TYR B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  TYR 29  29  29  TYR TYR B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  ILE 31  31  31  ILE ILE B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  GLY 34  34  34  GLY GLY B . n 
B 1 35  GLY 35  35  35  GLY GLY B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  SER 37  37  37  SER SER B . n 
B 1 38  GLY 38  38  38  GLY GLY B . n 
B 1 39  CYS 39  39  39  CYS CYS B . n 
B 1 40  PRO 40  40  40  PRO PRO B . n 
B 1 41  LEU 41  41  41  LEU LEU B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  TYR 49  49  49  TYR TYR B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ARG 56  56  56  ARG ARG B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  THR 61  61  61  THR THR B . n 
B 1 62  ALA 62  62  62  ALA ALA B . n 
B 1 63  TYR 63  63  63  TYR TYR B . n 
B 1 64  PRO 64  64  64  PRO PRO B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  VAL 66  66  66  VAL VAL B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  THR 68  68  68  THR THR B . n 
B 1 69  ALA 69  69  69  ALA ALA B . n 
B 1 70  ASP 70  70  70  ASP ASP B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  PHE 72  72  72  PHE PHE B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  TYR 74  74  74  TYR TYR B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  GLN 77  77  77  GLN GLN B . n 
B 1 78  GLN 78  78  78  GLN GLN B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  LYS 83  83  83  LYS LYS B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  PRO 85  85  85  PRO PRO B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  GLU 87  87  87  GLU GLU B . n 
B 1 88  ARG 88  88  88  ARG ARG B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  VAL 90  90  90  VAL VAL B . n 
B 1 91  SER 91  91  91  SER SER B . n 
B 1 92  GLU 92  92  92  GLU GLU B . n 
B 1 93  ASP 93  93  93  ASP ASP B . n 
B 1 94  GLY 94  94  94  GLY GLY B . n 
B 1 95  ILE 95  95  95  ILE ILE B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  ASN 97  97  97  ASN ASN B . n 
B 1 98  VAL 98  98  98  VAL VAL B . n 
B 1 99  ARG 99  99  99  ARG ARG B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 ARG 101 101 101 ARG ARG B . n 
B 1 102 VAL 102 102 102 VAL VAL B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 GLY 105 105 105 GLY GLY B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 ILE 108 108 108 ILE ILE B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 VAL 113 113 113 VAL VAL B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ARG 116 116 116 ARG ARG B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 THR 119 119 119 THR THR B . n 
B 1 120 SER 120 120 120 SER SER B . n 
B 1 121 ILE 121 121 121 ILE ILE B . n 
B 1 122 TYR 122 122 122 TYR TYR B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 SER 125 125 125 SER SER B . n 
B 1 126 GLY 126 126 126 GLY GLY B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 TRP 129 129 129 TRP TRP B . n 
B 1 130 ASP 130 130 130 ASP ASP B . n 
B 1 131 MET 131 131 131 MET MET B . n 
B 1 132 ASP 132 132 132 ASP ASP B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 ASN 135 135 135 ASN ASN B . n 
B 1 136 GLN 136 136 136 GLN GLN B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 TYR 138 138 138 TYR TYR B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 TRP 140 140 140 TRP TRP B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 GLU 142 142 142 GLU GLU B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 THR 144 144 144 THR THR B . n 
B 1 145 ILE 145 145 145 ILE ILE B . n 
B 1 146 VAL 146 146 146 VAL VAL B . n 
B 1 147 TYR 147 147 147 TYR TYR B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 SER 151 151 151 SER SER B . n 
B 1 152 GLN 152 152 152 GLN GLN B . n 
B 1 153 SER 153 153 153 SER SER B . n 
B 1 154 TRP 154 154 154 TRP TRP B . n 
B 1 155 GLN 155 155 155 GLN GLN B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 LYS 159 159 159 LYS LYS B . n 
B 1 160 THR 160 160 160 THR THR B . n 
B 1 161 ALA 161 161 161 ALA ALA B . n 
B 1 162 PHE 162 162 162 PHE PHE B . n 
B 1 163 LEU 163 163 163 LEU LEU B . n 
B 1 164 GLU 164 164 164 GLU GLU B . n 
B 1 165 ALA 165 165 165 ALA ALA B . n 
B 1 166 GLY 166 166 166 GLY GLY B . n 
B 1 167 VAL 167 167 167 VAL VAL B . n 
B 1 168 HIS 168 168 168 HIS HIS B . n 
B 1 169 PRO 169 169 169 PRO PRO B . n 
B 1 170 ASN 170 170 170 ASN ASN B . n 
B 1 171 HIS 171 171 171 HIS HIS B . n 
B 1 172 GLY 172 172 172 GLY GLY B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 SER 174 174 174 SER SER B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 HIS 177 177 177 HIS HIS B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLU 179 179 179 GLU GLU B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 THR 181 181 181 THR THR B . n 
B 1 182 ARG 182 182 182 ARG ARG B . n 
B 1 183 ILE 183 183 183 ILE ILE B . n 
B 1 184 THR 184 184 184 THR THR B . n 
B 1 185 GLY 185 185 185 GLY GLY B . n 
B 1 186 SER 186 186 186 SER SER B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 PHE 188 188 188 PHE PHE B . n 
B 1 189 ASP 189 189 189 ASP ASP B . n 
B 1 190 ASN 190 190 190 ASN ASN B . n 
B 1 191 LYS 191 191 191 LYS LYS B . n 
B 1 192 GLY 192 192 192 GLY GLY B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 HIS 195 195 195 HIS HIS B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 ASP 198 198 198 ASP ASP B . n 
B 1 199 GLU 199 199 199 GLU GLU B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 ASN 202 202 202 ASN ASN B . n 
B 1 203 LYS 203 203 203 LYS LYS B . n 
B 1 204 GLY 204 204 204 GLY GLY B . n 
B 1 205 ASN 205 205 205 ASN ASN B . n 
B 1 206 SER 206 206 206 SER SER B . n 
B 1 207 ASN 207 207 207 ASN ASN B . n 
B 1 208 ASN 208 208 208 ASN ASN B . n 
B 1 209 LEU 209 209 209 LEU LEU B . n 
B 1 210 ARG 210 210 210 ARG ARG B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 GLY 212 212 212 GLY GLY B . n 
B 1 213 VAL 213 213 213 VAL VAL B . n 
B 1 214 HIS 214 214 214 HIS HIS B . n 
B 1 215 ALA 215 215 215 ALA ALA B . n 
B 1 216 SER 216 216 216 SER SER B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 GLU 218 218 218 GLU GLU B . n 
B 1 219 LYS 219 219 219 LYS LYS B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 ILE 221 221 221 ILE ILE B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 ASN 224 224 224 ASN ASN B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 PRO 226 226 226 PRO PRO B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 LEU 228 228 228 LEU LEU B . n 
B 1 229 THR 229 229 229 THR THR B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 THR 231 231 231 THR THR B . n 
B 1 232 GLY 232 232 232 GLY GLY B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ILE 234 234 234 ILE ILE B . n 
B 1 235 TYR 235 235 235 TYR TYR B . n 
B 1 236 ARG 236 236 236 ARG ARG B . n 
B 1 237 ASP 237 237 237 ASP ASP B . n 
B 1 238 SER 238 238 238 SER SER 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 THR 241 241 241 THR THR B . n 
B 1 242 PRO 242 242 242 PRO PRO B . n 
B 1 243 HIS 243 243 243 HIS HIS B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ALA 245 245 245 ALA ALA B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ARG 248 248 248 ARG ARG B . n 
B 1 249 SER 249 249 249 SER SER B . n 
B 1 250 LYS 250 250 250 LYS LYS B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 GLU 252 252 252 GLU GLU B . n 
B 1 253 VAL 253 253 253 VAL VAL B . n 
B 1 254 ILE 254 254 254 ILE ILE B . n 
B 1 255 VAL 255 255 255 VAL VAL B . n 
B 1 256 SER 256 256 256 SER SER B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 ILE 260 260 260 ILE ILE B . n 
B 1 261 GLY 261 261 261 GLY GLY B . n 
B 1 262 THR 262 262 262 THR THR B . n 
B 1 263 PRO 263 263 263 PRO PRO B . n 
B 1 264 GLN 264 264 264 GLN GLN B . n 
B 1 265 LEU 265 265 265 LEU LEU B . n 
B 1 266 LEU 266 266 266 LEU LEU B . n 
B 1 267 LEU 267 267 267 LEU LEU B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 SER 269 269 269 SER SER B . n 
B 1 270 GLY 270 270 270 GLY GLY B . n 
B 1 271 VAL 271 271 271 VAL VAL B . n 
B 1 272 GLY 272 272 272 GLY GLY B . n 
B 1 273 PRO 273 273 273 PRO PRO B . n 
B 1 274 GLU 274 274 274 GLU GLU B . n 
B 1 275 SER 275 275 275 SER SER B . n 
B 1 276 TYR 276 276 276 TYR TYR B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 SER 278 278 278 SER SER B . n 
B 1 279 SER 279 279 279 SER SER B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 ASN 281 281 281 ASN ASN B . n 
B 1 282 ILE 282 282 282 ILE ILE B . n 
B 1 283 PRO 283 283 283 PRO PRO B . n 
B 1 284 VAL 284 284 284 VAL VAL B . n 
B 1 285 VAL 285 285 285 VAL VAL B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 SER 287 287 287 SER SER B . n 
B 1 288 HIS 288 288 288 HIS HIS B . n 
B 1 289 PRO 289 289 289 PRO PRO B . n 
B 1 290 TYR 290 290 290 TYR TYR B . n 
B 1 291 VAL 291 291 291 VAL VAL B . n 
B 1 292 GLY 292 292 292 GLY GLY B . n 
B 1 293 GLN 293 293 293 GLN GLN B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 LEU 295 295 295 LEU LEU B . n 
B 1 296 HIS 296 296 296 HIS HIS B . n 
B 1 297 ASP 297 297 297 ASP ASP B . n 
B 1 298 ASN 298 298 298 ASN ASN B . n 
B 1 299 PRO 299 299 299 PRO PRO B . n 
B 1 300 ARG 300 300 300 ARG ARG B . n 
B 1 301 ASN 301 301 301 ASN ASN B . n 
B 1 302 PHE 302 302 302 PHE PHE B . n 
B 1 303 ILE 303 303 303 ILE ILE B . n 
B 1 304 ASN 304 304 304 ASN ASN B . n 
B 1 305 ILE 305 305 305 ILE ILE B . n 
B 1 306 LEU 306 306 306 LEU LEU B . n 
B 1 307 PRO 307 307 307 PRO PRO B . n 
B 1 308 PRO 308 308 308 PRO PRO B . n 
B 1 309 ASN 309 309 309 ASN ASN B . n 
B 1 310 PRO 310 310 310 PRO PRO B . n 
B 1 311 ILE 311 311 311 ILE ILE B . n 
B 1 312 GLU 312 312 312 GLU GLU B . n 
B 1 313 PRO 313 313 313 PRO PRO B . n 
B 1 314 THR 314 314 314 THR THR B . n 
B 1 315 ILE 315 315 315 ILE ILE B . n 
B 1 316 VAL 316 316 316 VAL VAL B . n 
B 1 317 THR 317 317 317 THR THR B . n 
B 1 318 VAL 318 318 318 VAL VAL B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 GLY 320 320 320 GLY GLY B . n 
B 1 321 ILE 321 321 321 ILE ILE B . n 
B 1 322 SER 322 322 322 SER SER B . n 
B 1 323 ASN 323 323 323 ASN ASN B . n 
B 1 324 ASP 324 324 324 ASP ASP B . n 
B 1 325 PHE 325 325 325 PHE PHE B . n 
B 1 326 TYR 326 326 326 TYR TYR B . n 
B 1 327 GLN 327 327 327 GLN GLN B . n 
B 1 328 CYS 328 328 328 CYS CYS B . n 
B 1 329 SER 329 329 329 SER SER B . n 
B 1 330 PHE 330 330 330 PHE PHE B . n 
B 1 331 SER 331 331 331 SER SER 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 PRO 334 334 334 PRO PRO B . n 
B 1 335 PHE 335 335 335 PHE PHE B . n 
B 1 336 THR 336 336 336 THR THR B . n 
B 1 337 THR 337 337 337 THR THR B . n 
B 1 338 PRO 338 338 338 PRO PRO B . n 
B 1 339 PRO 339 339 339 PRO PRO B . n 
B 1 340 PHE 340 340 340 PHE PHE B . n 
B 1 341 GLY 341 341 341 GLY GLY B . n 
B 1 342 PHE 342 342 342 PHE PHE B . n 
B 1 343 PHE 343 343 343 PHE PHE B . n 
B 1 344 PRO 344 344 344 PRO PRO B . n 
B 1 345 SER 345 345 345 SER SER B . n 
B 1 346 SER 346 346 346 SER SER B . n 
B 1 347 SER 347 347 347 SER SER B . n 
B 1 348 TYR 348 348 348 TYR TYR B . n 
B 1 349 PRO 349 349 349 PRO PRO B . n 
B 1 350 LEU 350 350 350 LEU LEU B . n 
B 1 351 PRO 351 351 351 PRO PRO B . n 
B 1 352 ASN 352 352 352 ASN ASN B . n 
B 1 353 SER 353 353 353 SER SER B . n 
B 1 354 THR 354 354 354 THR THR B . n 
B 1 355 PHE 355 355 355 PHE PHE B . n 
B 1 356 ALA 356 356 356 ALA ALA B . n 
B 1 357 HIS 357 357 357 HIS HIS B . n 
B 1 358 PHE 358 358 358 PHE PHE B . n 
B 1 359 ALA 359 359 359 ALA ALA B . n 
B 1 360 SER 360 360 360 SER SER B . n 
B 1 361 LYS 361 361 361 LYS LYS B . n 
B 1 362 VAL 362 362 362 VAL VAL B . n 
B 1 363 ALA 363 363 363 ALA ALA B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 PRO 365 365 365 PRO PRO B . n 
B 1 366 LEU 366 366 366 LEU LEU B . n 
B 1 367 SER 367 367 367 SER SER B . n 
B 1 368 TYR 368 368 368 TYR TYR B . n 
B 1 369 GLY 369 369 369 GLY GLY B . n 
B 1 370 SER 370 370 370 SER SER B . n 
B 1 371 LEU 371 371 371 LEU LEU B . n 
B 1 372 THR 372 372 372 THR THR B . n 
B 1 373 LEU 373 373 373 LEU LEU B . n 
B 1 374 LYS 374 374 374 LYS LYS B . n 
B 1 375 SER 375 375 375 SER SER B . n 
B 1 376 SER 376 376 376 SER SER B . n 
B 1 377 SER 377 377 377 SER SER B . n 
B 1 378 ASN 378 378 378 ASN ASN B . n 
B 1 379 VAL 379 379 379 VAL VAL B . n 
B 1 380 ARG 380 380 380 ARG ARG B . n 
B 1 381 VAL 381 381 381 VAL VAL B . n 
B 1 382 SER 382 382 382 SER SER B . n 
B 1 383 PRO 383 383 383 PRO PRO B . n 
B 1 384 ASN 384 384 384 ASN ASN B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 LYS 386 386 386 LYS LYS B . n 
B 1 387 PHE 387 387 387 PHE PHE B . n 
B 1 388 ASN 388 388 388 ASN ASN B . n 
B 1 389 TYR 389 389 389 TYR TYR B . n 
B 1 390 TYR 390 390 390 TYR TYR B . n 
B 1 391 SER 391 391 391 SER SER B . n 
B 1 392 ASN 392 392 392 ASN ASN B . n 
B 1 393 LEU 393 393 393 LEU LEU B . n 
B 1 394 THR 394 394 394 THR THR B . n 
B 1 395 ASP 395 395 395 ASP ASP B . n 
B 1 396 LEU 396 396 396 LEU LEU B . n 
B 1 397 SER 397 397 397 SER SER B . n 
B 1 398 HIS 398 398 398 HIS HIS B . n 
B 1 399 CYS 399 399 399 CYS CYS B . n 
B 1 400 VAL 400 400 400 VAL VAL B . n 
B 1 401 SER 401 401 401 SER SER B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 MET 403 403 403 MET MET B . n 
B 1 404 LYS 404 404 404 LYS LYS B . n 
B 1 405 LYS 405 405 405 LYS LYS B . n 
B 1 406 ILE 406 406 406 ILE ILE B . n 
B 1 407 GLY 407 407 407 GLY GLY B . n 
B 1 408 GLU 408 408 408 GLU GLU B . n 
B 1 409 LEU 409 409 409 LEU LEU B . n 
B 1 410 LEU 410 410 410 LEU LEU B . n 
B 1 411 SER 411 411 411 SER SER B . n 
B 1 412 THR 412 412 412 THR THR B . n 
B 1 413 ASP 413 413 413 ASP ASP B . n 
B 1 414 ALA 414 414 414 ALA ALA B . n 
B 1 415 LEU 415 415 415 LEU LEU B . n 
B 1 416 LYS 416 416 416 LYS LYS B . n 
B 1 417 PRO 417 417 417 PRO PRO B . n 
B 1 418 TYR 418 418 418 TYR TYR B . n 
B 1 419 LYS 419 419 419 LYS LYS B . n 
B 1 420 VAL 420 420 420 VAL VAL B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 ASP 422 422 422 ASP ASP B . n 
B 1 423 LEU 423 423 423 LEU LEU B . n 
B 1 424 PRO 424 424 424 PRO PRO B . n 
B 1 425 GLY 425 425 425 GLY GLY B . n 
B 1 426 VAL 426 426 426 VAL VAL B . n 
B 1 427 GLU 427 427 427 GLU GLU B . n 
B 1 428 GLY 428 428 428 GLY GLY B . n 
B 1 429 PHE 429 429 429 PHE PHE B . n 
B 1 430 ASN 430 430 430 ASN ASN B . n 
B 1 431 ILE 431 431 431 ILE ILE B . n 
B 1 432 LEU 432 432 432 LEU LEU B . n 
B 1 433 GLY 433 433 433 GLY GLY B . n 
B 1 434 ILE 434 434 434 ILE ILE B . n 
B 1 435 PRO 435 435 435 PRO PRO B . n 
B 1 436 LEU 436 436 436 LEU LEU B . n 
B 1 437 PRO 437 437 437 PRO PRO B . n 
B 1 438 LYS 438 438 438 LYS LYS B . n 
B 1 439 ASP 439 439 439 ASP ASP B . n 
B 1 440 GLN 440 440 440 GLN GLN B . n 
B 1 441 THR 441 441 441 THR THR B . n 
B 1 442 ASP 442 442 442 ASP ASP B . n 
B 1 443 ASP 443 443 443 ASP ASP B . n 
B 1 444 ALA 444 444 444 ALA ALA B . n 
B 1 445 ALA 445 445 445 ALA ALA B . n 
B 1 446 PHE 446 446 446 PHE PHE B . n 
B 1 447 GLU 447 447 447 GLU GLU B . n 
B 1 448 THR 448 448 448 THR THR B . n 
B 1 449 PHE 449 449 449 PHE PHE B . n 
B 1 450 CYS 450 450 450 CYS CYS B . n 
B 1 451 ARG 451 451 451 ARG ARG B . n 
B 1 452 GLU 452 452 452 GLU GLU B . n 
B 1 453 SER 453 453 453 SER SER B . n 
B 1 454 VAL 454 454 454 VAL VAL B . n 
B 1 455 ALA 455 455 455 ALA ALA B . n 
B 1 456 SER 456 456 456 SER SER B . n 
B 1 457 TYR 457 457 457 TYR TYR B . n 
B 1 458 TRP 458 458 458 TRP TRP B . n 
B 1 459 HIS 459 459 459 HIS HIS B . n 
B 1 460 TYR 460 460 460 TYR TYR B . n 
B 1 461 HIS 461 461 461 HIS HIS B . n 
B 1 462 GLY 462 462 462 GLY GLY B . n 
B 1 463 GLY 463 463 463 GLY GLY B . n 
B 1 464 CYS 464 464 464 CYS CYS B . n 
B 1 465 LEU 465 465 465 LEU LEU B . n 
B 1 466 VAL 466 466 466 VAL VAL B . n 
B 1 467 GLY 467 467 467 GLY GLY B . n 
B 1 468 LYS 468 468 468 LYS LYS B . n 
B 1 469 VAL 469 469 469 VAL VAL B . n 
B 1 470 LEU 470 470 470 LEU LEU B . n 
B 1 471 ASP 471 471 471 ASP ASP B . n 
B 1 472 GLY 472 472 472 GLY GLY B . n 
B 1 473 ASP 473 473 473 ASP ASP B . n 
B 1 474 PHE 474 474 474 PHE PHE B . n 
B 1 475 ARG 475 475 475 ARG ARG B . n 
B 1 476 VAL 476 476 476 VAL VAL B . n 
B 1 477 THR 477 477 477 THR THR B . n 
B 1 478 GLY 478 478 478 GLY GLY B . n 
B 1 479 ILE 479 479 479 ILE ILE B . n 
B 1 480 ASN 480 480 480 ASN ASN B . n 
B 1 481 ALA 481 481 481 ALA ALA B . n 
B 1 482 LEU 482 482 482 LEU LEU B . n 
B 1 483 ARG 483 483 483 ARG ARG B . n 
B 1 484 VAL 484 484 484 VAL VAL B . n 
B 1 485 VAL 485 485 485 VAL VAL B . n 
B 1 486 ASP 486 486 486 ASP ASP B . n 
B 1 487 GLY 487 487 487 GLY GLY B . n 
B 1 488 SER 488 488 488 SER SER B . n 
B 1 489 THR 489 489 489 THR THR B . n 
B 1 490 PHE 490 490 490 PHE PHE B . n 
B 1 491 PRO 491 491 491 PRO PRO B . n 
B 1 492 TYR 492 492 492 TYR TYR B . n 
B 1 493 THR 493 493 493 THR THR B . n 
B 1 494 PRO 494 494 494 PRO PRO B . n 
B 1 495 ALA 495 495 495 ALA ALA B . n 
B 1 496 SER 496 496 496 SER SER B . n 
B 1 497 HIS 497 497 497 HIS HIS B . n 
B 1 498 PRO 498 498 498 PRO PRO B . n 
B 1 499 GLN 499 499 499 GLN GLN B . n 
B 1 500 GLY 500 500 500 GLY GLY B . n 
B 1 501 PHE 501 501 501 PHE PHE B . n 
B 1 502 TYR 502 502 502 TYR TYR B . n 
B 1 503 LEU 503 503 503 LEU LEU B . n 
B 1 504 MET 504 504 504 MET MET B . n 
B 1 505 LEU 505 505 505 LEU LEU B . n 
B 1 506 GLY 506 506 506 GLY GLY B . n 
B 1 507 ARG 507 507 507 ARG ARG B . n 
B 1 508 TYR 508 508 508 TYR TYR B . n 
B 1 509 VAL 509 509 509 VAL VAL B . n 
B 1 510 GLY 510 510 510 GLY GLY B . n 
B 1 511 ILE 511 511 511 ILE ILE B . n 
B 1 512 LYS 512 512 512 LYS LYS B . n 
B 1 513 ILE 513 513 513 ILE ILE B . n 
B 1 514 LEU 514 514 514 LEU LEU B . n 
B 1 515 GLN 515 515 515 GLN GLN B . n 
B 1 516 GLU 516 516 516 GLU GLU B . n 
B 1 517 ARG 517 517 517 ARG ARG B . n 
B 1 518 SER 518 518 518 SER SER B . n 
B 1 519 ALA 519 519 519 ALA ALA B . n 
B 1 520 SER 520 520 520 SER SER B . n 
B 1 521 ASP 521 521 521 ASP ASP B . n 
# 
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  IPA 1   522  522  IPA IPA A . 
D  3  FAD 1   523  523  FAD FAD A . 
E  4  NAG 1   524  524  NAG NAG A . 
F  4  NAG 1   525  525  NAG NAG A . 
G  4  NAG 2   526  526  NAG NAG A . 
H  5  FUL 3   527  527  FUL FUL A . 
I  6  MAN 4   528  528  MAN MAN A . 
J  6  MAN 5   529  529  MAN MAN A . 
K  4  NAG 1   530  530  NAG NAG A . 
L  4  NAG 2   531  531  NAG NAG A . 
M  7  FUC 3   532  532  FUC FUC A . 
N  4  NAG 1   533  533  NAG NAG A . 
O  2  IPA 1   522  522  IPA IPA B . 
P  3  FAD 1   523  523  FAD FAD B . 
Q  4  NAG 1   524  524  NAG NAG B . 
R  4  NAG 2   525  525  NAG NAG B . 
S  7  FUC 3   526  526  FUC FUC B . 
T  8  BMA 4   527  527  BMA BMA B . 
U  6  MAN 5   528  528  MAN MAN B . 
V  4  NAG 1   529  529  NAG NAG B . 
W  4  NAG 2   530  530  NAG NAG B . 
X  8  BMA 3   531  531  BMA BMA B . 
Y  6  MAN 4   532  532  MAN MAN B . 
Z  9  NDG 1   533  533  NDG NDG B . 
AA 4  NAG 1   534  534  NAG NAG B . 
BA 10 HOH 1   534  534  HOH HOH A . 
BA 10 HOH 2   535  535  HOH HOH A . 
BA 10 HOH 3   536  536  HOH HOH A . 
BA 10 HOH 4   537  537  HOH HOH A . 
BA 10 HOH 5   538  538  HOH HOH A . 
BA 10 HOH 6   539  539  HOH HOH A . 
BA 10 HOH 7   540  540  HOH HOH A . 
BA 10 HOH 8   541  541  HOH HOH A . 
BA 10 HOH 9   542  542  HOH HOH A . 
BA 10 HOH 10  543  543  HOH HOH A . 
BA 10 HOH 11  544  544  HOH HOH A . 
BA 10 HOH 12  545  545  HOH HOH A . 
BA 10 HOH 13  546  546  HOH HOH A . 
BA 10 HOH 14  547  547  HOH HOH A . 
BA 10 HOH 15  548  548  HOH HOH A . 
BA 10 HOH 16  549  549  HOH HOH A . 
BA 10 HOH 17  550  550  HOH HOH A . 
BA 10 HOH 18  551  551  HOH HOH A . 
BA 10 HOH 19  552  552  HOH HOH A . 
BA 10 HOH 20  553  553  HOH HOH A . 
BA 10 HOH 21  554  554  HOH HOH A . 
BA 10 HOH 22  555  555  HOH HOH A . 
BA 10 HOH 23  556  556  HOH HOH A . 
BA 10 HOH 24  557  557  HOH HOH A . 
BA 10 HOH 25  558  558  HOH HOH A . 
BA 10 HOH 26  559  559  HOH HOH A . 
BA 10 HOH 27  560  560  HOH HOH A . 
BA 10 HOH 28  561  561  HOH HOH A . 
BA 10 HOH 29  562  562  HOH HOH A . 
BA 10 HOH 30  563  563  HOH HOH A . 
BA 10 HOH 31  564  564  HOH HOH A . 
BA 10 HOH 32  565  565  HOH HOH A . 
BA 10 HOH 33  566  566  HOH HOH A . 
BA 10 HOH 34  567  567  HOH HOH A . 
BA 10 HOH 35  568  568  HOH HOH A . 
BA 10 HOH 36  569  569  HOH HOH A . 
BA 10 HOH 37  570  570  HOH HOH A . 
BA 10 HOH 38  571  571  HOH HOH A . 
BA 10 HOH 39  572  572  HOH HOH A . 
BA 10 HOH 40  573  573  HOH HOH A . 
BA 10 HOH 41  574  574  HOH HOH A . 
BA 10 HOH 42  575  575  HOH HOH A . 
BA 10 HOH 43  576  576  HOH HOH A . 
BA 10 HOH 44  577  577  HOH HOH A . 
BA 10 HOH 45  578  578  HOH HOH A . 
BA 10 HOH 46  579  579  HOH HOH A . 
BA 10 HOH 47  580  580  HOH HOH A . 
BA 10 HOH 48  581  581  HOH HOH A . 
BA 10 HOH 49  582  582  HOH HOH A . 
BA 10 HOH 50  583  583  HOH HOH A . 
BA 10 HOH 51  584  584  HOH HOH A . 
BA 10 HOH 52  585  585  HOH HOH A . 
BA 10 HOH 53  586  586  HOH HOH A . 
BA 10 HOH 54  587  587  HOH HOH A . 
BA 10 HOH 55  588  588  HOH HOH A . 
BA 10 HOH 56  589  589  HOH HOH A . 
BA 10 HOH 57  590  590  HOH HOH A . 
BA 10 HOH 58  591  591  HOH HOH A . 
BA 10 HOH 59  592  592  HOH HOH A . 
BA 10 HOH 60  593  593  HOH HOH A . 
BA 10 HOH 61  594  594  HOH HOH A . 
BA 10 HOH 62  595  595  HOH HOH A . 
BA 10 HOH 63  596  596  HOH HOH A . 
BA 10 HOH 64  597  597  HOH HOH A . 
BA 10 HOH 65  598  598  HOH HOH A . 
BA 10 HOH 66  599  599  HOH HOH A . 
BA 10 HOH 67  600  600  HOH HOH A . 
BA 10 HOH 68  601  601  HOH HOH A . 
BA 10 HOH 69  602  602  HOH HOH A . 
BA 10 HOH 70  603  603  HOH HOH A . 
BA 10 HOH 71  604  604  HOH HOH A . 
BA 10 HOH 72  605  605  HOH HOH A . 
BA 10 HOH 73  606  606  HOH HOH A . 
BA 10 HOH 74  607  607  HOH HOH A . 
BA 10 HOH 75  608  608  HOH HOH A . 
BA 10 HOH 76  609  609  HOH HOH A . 
BA 10 HOH 77  610  610  HOH HOH A . 
BA 10 HOH 78  611  611  HOH HOH A . 
BA 10 HOH 79  612  612  HOH HOH A . 
BA 10 HOH 80  613  613  HOH HOH A . 
BA 10 HOH 81  614  614  HOH HOH A . 
BA 10 HOH 82  615  615  HOH HOH A . 
BA 10 HOH 83  616  616  HOH HOH A . 
BA 10 HOH 84  617  617  HOH HOH A . 
BA 10 HOH 85  618  618  HOH HOH A . 
BA 10 HOH 86  619  619  HOH HOH A . 
BA 10 HOH 87  620  620  HOH HOH A . 
BA 10 HOH 88  621  621  HOH HOH A . 
BA 10 HOH 89  622  622  HOH HOH A . 
BA 10 HOH 90  623  623  HOH HOH A . 
BA 10 HOH 91  624  624  HOH HOH A . 
BA 10 HOH 92  625  625  HOH HOH A . 
BA 10 HOH 93  626  626  HOH HOH A . 
BA 10 HOH 94  627  627  HOH HOH A . 
BA 10 HOH 95  628  628  HOH HOH A . 
BA 10 HOH 96  629  629  HOH HOH A . 
BA 10 HOH 97  630  630  HOH HOH A . 
BA 10 HOH 98  631  631  HOH HOH A . 
BA 10 HOH 99  632  632  HOH HOH A . 
BA 10 HOH 100 633  633  HOH HOH A . 
BA 10 HOH 101 634  634  HOH HOH A . 
BA 10 HOH 102 635  635  HOH HOH A . 
BA 10 HOH 103 636  636  HOH HOH A . 
BA 10 HOH 104 637  637  HOH HOH A . 
BA 10 HOH 105 638  638  HOH HOH A . 
BA 10 HOH 106 639  639  HOH HOH A . 
BA 10 HOH 107 640  640  HOH HOH A . 
BA 10 HOH 108 641  641  HOH HOH A . 
BA 10 HOH 109 642  642  HOH HOH A . 
BA 10 HOH 110 643  643  HOH HOH A . 
BA 10 HOH 111 644  644  HOH HOH A . 
BA 10 HOH 112 645  645  HOH HOH A . 
BA 10 HOH 113 646  646  HOH HOH A . 
BA 10 HOH 114 647  647  HOH HOH A . 
BA 10 HOH 115 648  648  HOH HOH A . 
BA 10 HOH 116 649  649  HOH HOH A . 
BA 10 HOH 117 650  650  HOH HOH A . 
BA 10 HOH 118 651  651  HOH HOH A . 
BA 10 HOH 119 652  652  HOH HOH A . 
BA 10 HOH 120 653  653  HOH HOH A . 
BA 10 HOH 121 654  654  HOH HOH A . 
BA 10 HOH 122 655  655  HOH HOH A . 
BA 10 HOH 123 656  656  HOH HOH A . 
BA 10 HOH 124 657  657  HOH HOH A . 
BA 10 HOH 125 658  658  HOH HOH A . 
BA 10 HOH 126 659  659  HOH HOH A . 
BA 10 HOH 127 660  660  HOH HOH A . 
BA 10 HOH 128 661  661  HOH HOH A . 
BA 10 HOH 129 662  662  HOH HOH A . 
BA 10 HOH 130 663  663  HOH HOH A . 
BA 10 HOH 131 664  664  HOH HOH A . 
BA 10 HOH 132 665  665  HOH HOH A . 
BA 10 HOH 133 666  666  HOH HOH A . 
BA 10 HOH 134 667  667  HOH HOH A . 
BA 10 HOH 135 668  668  HOH HOH A . 
BA 10 HOH 136 669  669  HOH HOH A . 
BA 10 HOH 137 670  670  HOH HOH A . 
BA 10 HOH 138 671  671  HOH HOH A . 
BA 10 HOH 139 672  672  HOH HOH A . 
BA 10 HOH 140 673  673  HOH HOH A . 
BA 10 HOH 141 674  674  HOH HOH A . 
BA 10 HOH 142 675  675  HOH HOH A . 
BA 10 HOH 143 676  676  HOH HOH A . 
BA 10 HOH 144 677  677  HOH HOH A . 
BA 10 HOH 145 678  678  HOH HOH A . 
BA 10 HOH 146 679  679  HOH HOH A . 
BA 10 HOH 147 680  680  HOH HOH A . 
BA 10 HOH 148 681  681  HOH HOH A . 
BA 10 HOH 149 682  682  HOH HOH A . 
BA 10 HOH 150 683  683  HOH HOH A . 
BA 10 HOH 151 684  684  HOH HOH A . 
BA 10 HOH 152 685  685  HOH HOH A . 
BA 10 HOH 153 686  686  HOH HOH A . 
BA 10 HOH 154 687  687  HOH HOH A . 
BA 10 HOH 155 688  688  HOH HOH A . 
BA 10 HOH 156 689  689  HOH HOH A . 
BA 10 HOH 157 690  690  HOH HOH A . 
BA 10 HOH 158 691  691  HOH HOH A . 
BA 10 HOH 159 692  692  HOH HOH A . 
BA 10 HOH 160 693  693  HOH HOH A . 
BA 10 HOH 161 694  694  HOH HOH A . 
BA 10 HOH 162 695  695  HOH HOH A . 
BA 10 HOH 163 696  696  HOH HOH A . 
BA 10 HOH 164 697  697  HOH HOH A . 
BA 10 HOH 165 698  698  HOH HOH A . 
BA 10 HOH 166 699  699  HOH HOH A . 
BA 10 HOH 167 700  700  HOH HOH A . 
BA 10 HOH 168 701  701  HOH HOH A . 
BA 10 HOH 169 702  702  HOH HOH A . 
BA 10 HOH 170 703  703  HOH HOH A . 
BA 10 HOH 171 704  704  HOH HOH A . 
BA 10 HOH 172 705  705  HOH HOH A . 
BA 10 HOH 173 706  706  HOH HOH A . 
BA 10 HOH 174 707  707  HOH HOH A . 
BA 10 HOH 175 708  708  HOH HOH A . 
BA 10 HOH 176 709  709  HOH HOH A . 
BA 10 HOH 177 710  710  HOH HOH A . 
BA 10 HOH 178 711  711  HOH HOH A . 
BA 10 HOH 179 712  712  HOH HOH A . 
BA 10 HOH 180 713  713  HOH HOH A . 
BA 10 HOH 181 714  714  HOH HOH A . 
BA 10 HOH 182 715  715  HOH HOH A . 
BA 10 HOH 183 716  716  HOH HOH A . 
BA 10 HOH 184 717  717  HOH HOH A . 
BA 10 HOH 185 718  718  HOH HOH A . 
BA 10 HOH 186 719  719  HOH HOH A . 
BA 10 HOH 187 720  720  HOH HOH A . 
BA 10 HOH 188 721  721  HOH HOH A . 
BA 10 HOH 189 722  722  HOH HOH A . 
BA 10 HOH 190 723  723  HOH HOH A . 
BA 10 HOH 191 724  724  HOH HOH A . 
BA 10 HOH 192 725  725  HOH HOH A . 
BA 10 HOH 193 726  726  HOH HOH A . 
BA 10 HOH 194 727  727  HOH HOH A . 
BA 10 HOH 195 728  728  HOH HOH A . 
BA 10 HOH 196 729  729  HOH HOH A . 
BA 10 HOH 197 730  730  HOH HOH A . 
BA 10 HOH 198 731  731  HOH HOH A . 
BA 10 HOH 199 732  732  HOH HOH A . 
BA 10 HOH 200 733  733  HOH HOH A . 
BA 10 HOH 201 734  734  HOH HOH A . 
BA 10 HOH 202 735  735  HOH HOH A . 
BA 10 HOH 203 736  736  HOH HOH A . 
BA 10 HOH 204 737  737  HOH HOH A . 
BA 10 HOH 205 738  738  HOH HOH A . 
BA 10 HOH 206 739  739  HOH HOH A . 
BA 10 HOH 207 740  740  HOH HOH A . 
BA 10 HOH 208 741  741  HOH HOH A . 
BA 10 HOH 209 742  742  HOH HOH A . 
BA 10 HOH 210 743  743  HOH HOH A . 
BA 10 HOH 211 744  744  HOH HOH A . 
BA 10 HOH 212 745  745  HOH HOH A . 
BA 10 HOH 213 746  746  HOH HOH A . 
BA 10 HOH 214 747  747  HOH HOH A . 
BA 10 HOH 215 748  748  HOH HOH A . 
BA 10 HOH 216 749  749  HOH HOH A . 
BA 10 HOH 217 750  750  HOH HOH A . 
BA 10 HOH 218 751  751  HOH HOH A . 
BA 10 HOH 219 752  752  HOH HOH A . 
BA 10 HOH 220 753  753  HOH HOH A . 
BA 10 HOH 221 754  754  HOH HOH A . 
BA 10 HOH 222 755  755  HOH HOH A . 
BA 10 HOH 223 756  756  HOH HOH A . 
BA 10 HOH 224 757  757  HOH HOH A . 
BA 10 HOH 225 758  758  HOH HOH A . 
BA 10 HOH 226 759  759  HOH HOH A . 
BA 10 HOH 227 760  760  HOH HOH A . 
BA 10 HOH 228 761  761  HOH HOH A . 
BA 10 HOH 229 762  762  HOH HOH A . 
BA 10 HOH 230 763  763  HOH HOH A . 
BA 10 HOH 231 764  764  HOH HOH A . 
BA 10 HOH 232 765  765  HOH HOH A . 
BA 10 HOH 233 766  766  HOH HOH A . 
BA 10 HOH 234 767  767  HOH HOH A . 
BA 10 HOH 235 768  768  HOH HOH A . 
BA 10 HOH 236 769  769  HOH HOH A . 
BA 10 HOH 237 770  770  HOH HOH A . 
BA 10 HOH 238 771  771  HOH HOH A . 
BA 10 HOH 239 772  772  HOH HOH A . 
BA 10 HOH 240 773  773  HOH HOH A . 
BA 10 HOH 241 774  774  HOH HOH A . 
BA 10 HOH 242 775  775  HOH HOH A . 
BA 10 HOH 243 776  776  HOH HOH A . 
BA 10 HOH 244 777  777  HOH HOH A . 
BA 10 HOH 245 778  778  HOH HOH A . 
BA 10 HOH 246 779  779  HOH HOH A . 
BA 10 HOH 247 780  780  HOH HOH A . 
BA 10 HOH 248 781  781  HOH HOH A . 
BA 10 HOH 249 782  782  HOH HOH A . 
BA 10 HOH 250 783  783  HOH HOH A . 
BA 10 HOH 251 784  784  HOH HOH A . 
BA 10 HOH 252 785  785  HOH HOH A . 
BA 10 HOH 253 786  786  HOH HOH A . 
BA 10 HOH 254 787  787  HOH HOH A . 
BA 10 HOH 255 788  788  HOH HOH A . 
BA 10 HOH 256 789  789  HOH HOH A . 
BA 10 HOH 257 790  790  HOH HOH A . 
BA 10 HOH 258 791  791  HOH HOH A . 
BA 10 HOH 259 792  792  HOH HOH A . 
BA 10 HOH 260 793  793  HOH HOH A . 
BA 10 HOH 261 794  794  HOH HOH A . 
BA 10 HOH 262 795  795  HOH HOH A . 
BA 10 HOH 263 796  796  HOH HOH A . 
BA 10 HOH 264 797  797  HOH HOH A . 
BA 10 HOH 265 798  798  HOH HOH A . 
BA 10 HOH 266 799  799  HOH HOH A . 
BA 10 HOH 267 800  800  HOH HOH A . 
BA 10 HOH 268 801  801  HOH HOH A . 
BA 10 HOH 269 802  802  HOH HOH A . 
BA 10 HOH 270 803  803  HOH HOH A . 
BA 10 HOH 271 804  804  HOH HOH A . 
BA 10 HOH 272 805  805  HOH HOH A . 
BA 10 HOH 273 806  806  HOH HOH A . 
BA 10 HOH 274 807  807  HOH HOH A . 
BA 10 HOH 275 808  808  HOH HOH A . 
BA 10 HOH 276 809  809  HOH HOH A . 
BA 10 HOH 277 810  810  HOH HOH A . 
BA 10 HOH 278 811  811  HOH HOH A . 
BA 10 HOH 279 812  812  HOH HOH A . 
BA 10 HOH 280 813  813  HOH HOH A . 
BA 10 HOH 281 814  814  HOH HOH A . 
BA 10 HOH 282 815  815  HOH HOH A . 
BA 10 HOH 283 816  816  HOH HOH A . 
BA 10 HOH 284 817  817  HOH HOH A . 
BA 10 HOH 285 818  818  HOH HOH A . 
BA 10 HOH 286 819  819  HOH HOH A . 
BA 10 HOH 287 820  820  HOH HOH A . 
BA 10 HOH 288 821  821  HOH HOH A . 
BA 10 HOH 289 822  822  HOH HOH A . 
BA 10 HOH 290 823  823  HOH HOH A . 
BA 10 HOH 291 824  824  HOH HOH A . 
BA 10 HOH 292 825  825  HOH HOH A . 
BA 10 HOH 293 826  826  HOH HOH A . 
BA 10 HOH 294 827  827  HOH HOH A . 
BA 10 HOH 295 828  828  HOH HOH A . 
BA 10 HOH 296 829  829  HOH HOH A . 
BA 10 HOH 297 830  830  HOH HOH A . 
BA 10 HOH 298 831  831  HOH HOH A . 
BA 10 HOH 299 832  832  HOH HOH A . 
BA 10 HOH 300 833  833  HOH HOH A . 
BA 10 HOH 301 834  834  HOH HOH A . 
BA 10 HOH 302 835  835  HOH HOH A . 
BA 10 HOH 303 836  836  HOH HOH A . 
BA 10 HOH 304 837  837  HOH HOH A . 
BA 10 HOH 305 838  838  HOH HOH A . 
BA 10 HOH 306 839  839  HOH HOH A . 
BA 10 HOH 307 840  840  HOH HOH A . 
BA 10 HOH 308 841  841  HOH HOH A . 
BA 10 HOH 309 842  842  HOH HOH A . 
BA 10 HOH 310 843  843  HOH HOH A . 
BA 10 HOH 311 844  844  HOH HOH A . 
BA 10 HOH 312 845  845  HOH HOH A . 
BA 10 HOH 313 846  846  HOH HOH A . 
BA 10 HOH 314 847  847  HOH HOH A . 
BA 10 HOH 315 848  848  HOH HOH A . 
BA 10 HOH 316 849  849  HOH HOH A . 
BA 10 HOH 317 850  850  HOH HOH A . 
BA 10 HOH 318 851  851  HOH HOH A . 
BA 10 HOH 319 852  852  HOH HOH A . 
BA 10 HOH 320 853  853  HOH HOH A . 
BA 10 HOH 321 854  854  HOH HOH A . 
BA 10 HOH 322 855  855  HOH HOH A . 
BA 10 HOH 323 856  856  HOH HOH A . 
BA 10 HOH 324 857  857  HOH HOH A . 
BA 10 HOH 325 858  858  HOH HOH A . 
BA 10 HOH 326 859  859  HOH HOH A . 
BA 10 HOH 327 860  860  HOH HOH A . 
BA 10 HOH 328 861  861  HOH HOH A . 
BA 10 HOH 329 862  862  HOH HOH A . 
BA 10 HOH 330 863  863  HOH HOH A . 
BA 10 HOH 331 864  864  HOH HOH A . 
BA 10 HOH 332 865  865  HOH HOH A . 
BA 10 HOH 333 866  866  HOH HOH A . 
BA 10 HOH 334 867  867  HOH HOH A . 
BA 10 HOH 335 868  868  HOH HOH A . 
BA 10 HOH 336 869  869  HOH HOH A . 
BA 10 HOH 337 870  870  HOH HOH A . 
BA 10 HOH 338 871  871  HOH HOH A . 
BA 10 HOH 339 872  872  HOH HOH A . 
BA 10 HOH 340 873  873  HOH HOH A . 
BA 10 HOH 341 874  874  HOH HOH A . 
BA 10 HOH 342 875  875  HOH HOH A . 
BA 10 HOH 343 876  876  HOH HOH A . 
BA 10 HOH 344 877  877  HOH HOH A . 
BA 10 HOH 345 878  878  HOH HOH A . 
BA 10 HOH 346 879  879  HOH HOH A . 
BA 10 HOH 347 880  880  HOH HOH A . 
BA 10 HOH 348 881  881  HOH HOH A . 
BA 10 HOH 349 882  882  HOH HOH A . 
BA 10 HOH 350 883  883  HOH HOH A . 
BA 10 HOH 351 884  884  HOH HOH A . 
BA 10 HOH 352 885  885  HOH HOH A . 
BA 10 HOH 353 886  886  HOH HOH A . 
BA 10 HOH 354 887  887  HOH HOH A . 
BA 10 HOH 355 888  888  HOH HOH A . 
BA 10 HOH 356 889  889  HOH HOH A . 
BA 10 HOH 357 890  890  HOH HOH A . 
BA 10 HOH 358 891  891  HOH HOH A . 
BA 10 HOH 359 892  892  HOH HOH A . 
BA 10 HOH 360 893  893  HOH HOH A . 
BA 10 HOH 361 894  894  HOH HOH A . 
BA 10 HOH 362 895  895  HOH HOH A . 
BA 10 HOH 363 896  896  HOH HOH A . 
BA 10 HOH 364 897  897  HOH HOH A . 
BA 10 HOH 365 898  898  HOH HOH A . 
BA 10 HOH 366 899  899  HOH HOH A . 
BA 10 HOH 367 900  900  HOH HOH A . 
BA 10 HOH 368 901  901  HOH HOH A . 
BA 10 HOH 369 902  902  HOH HOH A . 
BA 10 HOH 370 903  903  HOH HOH A . 
BA 10 HOH 371 904  904  HOH HOH A . 
BA 10 HOH 372 905  905  HOH HOH A . 
BA 10 HOH 373 906  906  HOH HOH A . 
BA 10 HOH 374 907  907  HOH HOH A . 
BA 10 HOH 375 908  908  HOH HOH A . 
BA 10 HOH 376 909  909  HOH HOH A . 
BA 10 HOH 377 910  910  HOH HOH A . 
BA 10 HOH 378 911  911  HOH HOH A . 
BA 10 HOH 379 912  912  HOH HOH A . 
BA 10 HOH 380 913  913  HOH HOH A . 
BA 10 HOH 381 914  914  HOH HOH A . 
BA 10 HOH 382 915  915  HOH HOH A . 
BA 10 HOH 383 916  916  HOH HOH A . 
BA 10 HOH 384 917  917  HOH HOH A . 
BA 10 HOH 385 918  918  HOH HOH A . 
BA 10 HOH 386 919  919  HOH HOH A . 
BA 10 HOH 387 920  920  HOH HOH A . 
BA 10 HOH 388 921  921  HOH HOH A . 
BA 10 HOH 389 922  922  HOH HOH A . 
BA 10 HOH 390 923  923  HOH HOH A . 
BA 10 HOH 391 924  924  HOH HOH A . 
BA 10 HOH 392 925  925  HOH HOH A . 
BA 10 HOH 393 926  926  HOH HOH A . 
BA 10 HOH 394 927  927  HOH HOH A . 
BA 10 HOH 395 928  928  HOH HOH A . 
BA 10 HOH 396 929  929  HOH HOH A . 
BA 10 HOH 397 930  930  HOH HOH A . 
BA 10 HOH 398 931  931  HOH HOH A . 
BA 10 HOH 399 932  932  HOH HOH A . 
BA 10 HOH 400 933  933  HOH HOH A . 
BA 10 HOH 401 934  934  HOH HOH A . 
BA 10 HOH 402 935  935  HOH HOH A . 
BA 10 HOH 403 936  936  HOH HOH A . 
BA 10 HOH 404 937  937  HOH HOH A . 
BA 10 HOH 405 938  938  HOH HOH A . 
BA 10 HOH 406 939  939  HOH HOH A . 
BA 10 HOH 407 940  940  HOH HOH A . 
BA 10 HOH 408 941  941  HOH HOH A . 
BA 10 HOH 409 942  942  HOH HOH A . 
BA 10 HOH 410 943  943  HOH HOH A . 
BA 10 HOH 411 944  944  HOH HOH A . 
BA 10 HOH 412 945  945  HOH HOH A . 
BA 10 HOH 413 946  946  HOH HOH A . 
BA 10 HOH 414 947  947  HOH HOH A . 
BA 10 HOH 415 948  948  HOH HOH A . 
BA 10 HOH 416 949  949  HOH HOH A . 
BA 10 HOH 417 950  950  HOH HOH A . 
BA 10 HOH 418 951  951  HOH HOH A . 
BA 10 HOH 419 952  952  HOH HOH A . 
BA 10 HOH 420 953  953  HOH HOH A . 
BA 10 HOH 421 954  954  HOH HOH A . 
BA 10 HOH 422 955  955  HOH HOH A . 
BA 10 HOH 423 956  956  HOH HOH A . 
BA 10 HOH 424 957  957  HOH HOH A . 
BA 10 HOH 425 958  958  HOH HOH A . 
BA 10 HOH 426 959  959  HOH HOH A . 
BA 10 HOH 427 960  960  HOH HOH A . 
BA 10 HOH 428 961  961  HOH HOH A . 
BA 10 HOH 429 962  962  HOH HOH A . 
BA 10 HOH 430 963  963  HOH HOH A . 
BA 10 HOH 431 964  964  HOH HOH A . 
BA 10 HOH 432 965  965  HOH HOH A . 
BA 10 HOH 433 966  966  HOH HOH A . 
BA 10 HOH 434 967  967  HOH HOH A . 
BA 10 HOH 435 968  968  HOH HOH A . 
BA 10 HOH 436 969  969  HOH HOH A . 
BA 10 HOH 437 970  970  HOH HOH A . 
BA 10 HOH 438 971  971  HOH HOH A . 
BA 10 HOH 439 972  972  HOH HOH A . 
BA 10 HOH 440 973  973  HOH HOH A . 
BA 10 HOH 441 974  974  HOH HOH A . 
BA 10 HOH 442 975  975  HOH HOH A . 
BA 10 HOH 443 976  976  HOH HOH A . 
BA 10 HOH 444 977  977  HOH HOH A . 
BA 10 HOH 445 978  978  HOH HOH A . 
BA 10 HOH 446 979  979  HOH HOH A . 
BA 10 HOH 447 980  980  HOH HOH A . 
BA 10 HOH 448 981  981  HOH HOH A . 
BA 10 HOH 449 982  982  HOH HOH A . 
BA 10 HOH 450 983  983  HOH HOH A . 
BA 10 HOH 451 984  984  HOH HOH A . 
BA 10 HOH 452 985  985  HOH HOH A . 
BA 10 HOH 453 986  986  HOH HOH A . 
BA 10 HOH 454 987  987  HOH HOH A . 
BA 10 HOH 455 988  988  HOH HOH A . 
BA 10 HOH 456 989  989  HOH HOH A . 
BA 10 HOH 457 990  990  HOH HOH A . 
BA 10 HOH 458 991  991  HOH HOH A . 
BA 10 HOH 459 992  992  HOH HOH A . 
BA 10 HOH 460 993  993  HOH HOH A . 
BA 10 HOH 461 994  994  HOH HOH A . 
BA 10 HOH 462 995  995  HOH HOH A . 
BA 10 HOH 463 996  996  HOH HOH A . 
BA 10 HOH 464 997  997  HOH HOH A . 
BA 10 HOH 465 998  998  HOH HOH A . 
BA 10 HOH 466 999  999  HOH HOH A . 
BA 10 HOH 467 1000 1000 HOH HOH A . 
BA 10 HOH 468 1001 1001 HOH HOH A . 
BA 10 HOH 469 1002 1002 HOH HOH A . 
BA 10 HOH 470 1003 1003 HOH HOH A . 
BA 10 HOH 471 1004 1004 HOH HOH A . 
BA 10 HOH 472 1005 1005 HOH HOH A . 
BA 10 HOH 473 1006 1006 HOH HOH A . 
BA 10 HOH 474 1007 1007 HOH HOH A . 
BA 10 HOH 475 1008 1008 HOH HOH A . 
BA 10 HOH 476 1009 1009 HOH HOH A . 
BA 10 HOH 477 1010 1010 HOH HOH A . 
BA 10 HOH 478 1011 1011 HOH HOH A . 
BA 10 HOH 479 1012 1012 HOH HOH A . 
BA 10 HOH 480 1013 1013 HOH HOH A . 
BA 10 HOH 481 1014 1014 HOH HOH A . 
BA 10 HOH 482 1015 1015 HOH HOH A . 
BA 10 HOH 483 1016 1016 HOH HOH A . 
BA 10 HOH 484 1017 1017 HOH HOH A . 
BA 10 HOH 485 1018 1018 HOH HOH A . 
BA 10 HOH 486 1019 1019 HOH HOH A . 
BA 10 HOH 487 1020 1020 HOH HOH A . 
BA 10 HOH 488 1021 1021 HOH HOH A . 
BA 10 HOH 489 1022 1022 HOH HOH A . 
BA 10 HOH 490 1023 1023 HOH HOH A . 
BA 10 HOH 491 1024 1024 HOH HOH A . 
BA 10 HOH 492 1025 1025 HOH HOH A . 
BA 10 HOH 493 1026 1026 HOH HOH A . 
BA 10 HOH 494 1027 1027 HOH HOH A . 
BA 10 HOH 495 1028 1028 HOH HOH A . 
BA 10 HOH 496 1029 1029 HOH HOH A . 
BA 10 HOH 497 1030 1030 HOH HOH A . 
BA 10 HOH 498 1031 1031 HOH HOH A . 
BA 10 HOH 499 1032 1032 HOH HOH A . 
BA 10 HOH 500 1033 1033 HOH HOH A . 
BA 10 HOH 501 1034 1034 HOH HOH A . 
BA 10 HOH 502 1035 1035 HOH HOH A . 
BA 10 HOH 503 1036 1036 HOH HOH A . 
BA 10 HOH 504 1037 1037 HOH HOH A . 
BA 10 HOH 505 1038 1038 HOH HOH A . 
BA 10 HOH 506 1039 1039 HOH HOH A . 
BA 10 HOH 507 1040 1040 HOH HOH A . 
BA 10 HOH 508 1041 1041 HOH HOH A . 
BA 10 HOH 509 1042 1042 HOH HOH A . 
BA 10 HOH 510 1043 1043 HOH HOH A . 
BA 10 HOH 511 1044 1044 HOH HOH A . 
BA 10 HOH 512 1045 1045 HOH HOH A . 
BA 10 HOH 513 1046 1046 HOH HOH A . 
BA 10 HOH 514 1047 1047 HOH HOH A . 
BA 10 HOH 515 1048 1048 HOH HOH A . 
BA 10 HOH 516 1049 1049 HOH HOH A . 
BA 10 HOH 517 1050 1050 HOH HOH A . 
BA 10 HOH 518 1051 1051 HOH HOH A . 
BA 10 HOH 519 1052 1052 HOH HOH A . 
BA 10 HOH 520 1053 1053 HOH HOH A . 
BA 10 HOH 521 1054 1054 HOH HOH A . 
BA 10 HOH 522 1055 1055 HOH HOH A . 
BA 10 HOH 523 1056 1056 HOH HOH A . 
BA 10 HOH 524 1057 1057 HOH HOH A . 
BA 10 HOH 525 1058 1058 HOH HOH A . 
BA 10 HOH 526 1059 1059 HOH HOH A . 
BA 10 HOH 527 1060 1060 HOH HOH A . 
BA 10 HOH 528 1061 1061 HOH HOH A . 
BA 10 HOH 529 1062 1062 HOH HOH A . 
BA 10 HOH 530 1063 1063 HOH HOH A . 
BA 10 HOH 531 1064 1064 HOH HOH A . 
BA 10 HOH 532 1065 1065 HOH HOH A . 
BA 10 HOH 533 1066 1066 HOH HOH A . 
BA 10 HOH 534 1067 1067 HOH HOH A . 
BA 10 HOH 535 1068 1068 HOH HOH A . 
BA 10 HOH 536 1069 1069 HOH HOH A . 
BA 10 HOH 537 1070 1070 HOH HOH A . 
BA 10 HOH 538 1071 1071 HOH HOH A . 
BA 10 HOH 539 1072 1072 HOH HOH A . 
BA 10 HOH 540 1073 1073 HOH HOH A . 
BA 10 HOH 541 1074 1074 HOH HOH A . 
BA 10 HOH 542 1075 1075 HOH HOH A . 
BA 10 HOH 543 1076 1076 HOH HOH A . 
BA 10 HOH 544 1077 1077 HOH HOH A . 
BA 10 HOH 545 1078 1078 HOH HOH A . 
BA 10 HOH 546 1079 1079 HOH HOH A . 
BA 10 HOH 547 1080 1080 HOH HOH A . 
BA 10 HOH 548 1081 1081 HOH HOH A . 
BA 10 HOH 549 1082 1082 HOH HOH A . 
BA 10 HOH 550 1083 1083 HOH HOH A . 
BA 10 HOH 551 1084 1084 HOH HOH A . 
BA 10 HOH 552 1085 1085 HOH HOH A . 
BA 10 HOH 553 1086 1086 HOH HOH A . 
BA 10 HOH 554 1087 1087 HOH HOH A . 
BA 10 HOH 555 1088 1088 HOH HOH A . 
BA 10 HOH 556 1089 1089 HOH HOH A . 
BA 10 HOH 557 1090 1090 HOH HOH A . 
BA 10 HOH 558 1091 1091 HOH HOH A . 
BA 10 HOH 559 1092 1092 HOH HOH A . 
BA 10 HOH 560 1093 1093 HOH HOH A . 
BA 10 HOH 561 1094 1094 HOH HOH A . 
BA 10 HOH 562 1095 1095 HOH HOH A . 
BA 10 HOH 563 1096 1096 HOH HOH A . 
BA 10 HOH 564 1097 1097 HOH HOH A . 
BA 10 HOH 565 1098 1098 HOH HOH A . 
BA 10 HOH 566 1099 1099 HOH HOH A . 
BA 10 HOH 567 1100 1100 HOH HOH A . 
BA 10 HOH 568 1101 1101 HOH HOH A . 
BA 10 HOH 569 1102 1102 HOH HOH A . 
BA 10 HOH 570 1103 1103 HOH HOH A . 
BA 10 HOH 571 1104 1104 HOH HOH A . 
BA 10 HOH 572 1105 1105 HOH HOH A . 
BA 10 HOH 573 1106 1106 HOH HOH A . 
BA 10 HOH 574 1107 1107 HOH HOH A . 
BA 10 HOH 575 1108 1108 HOH HOH A . 
BA 10 HOH 576 1109 1109 HOH HOH A . 
BA 10 HOH 577 1110 1110 HOH HOH A . 
BA 10 HOH 578 1111 1111 HOH HOH A . 
BA 10 HOH 579 1112 1112 HOH HOH A . 
BA 10 HOH 580 1113 1113 HOH HOH A . 
BA 10 HOH 581 1114 1114 HOH HOH A . 
BA 10 HOH 582 1115 1115 HOH HOH A . 
BA 10 HOH 583 1116 1116 HOH HOH A . 
BA 10 HOH 584 1117 1117 HOH HOH A . 
BA 10 HOH 585 1118 1118 HOH HOH A . 
BA 10 HOH 586 1119 1119 HOH HOH A . 
BA 10 HOH 587 1120 1120 HOH HOH A . 
BA 10 HOH 588 1121 1121 HOH HOH A . 
BA 10 HOH 589 1122 1122 HOH HOH A . 
BA 10 HOH 590 1123 1123 HOH HOH A . 
BA 10 HOH 591 1124 1124 HOH HOH A . 
BA 10 HOH 592 1125 1125 HOH HOH A . 
BA 10 HOH 593 1126 1126 HOH HOH A . 
BA 10 HOH 594 1127 1127 HOH HOH A . 
BA 10 HOH 595 1128 1128 HOH HOH A . 
BA 10 HOH 596 1129 1129 HOH HOH A . 
BA 10 HOH 597 1130 1130 HOH HOH A . 
BA 10 HOH 598 1131 1131 HOH HOH A . 
BA 10 HOH 599 1132 1132 HOH HOH A . 
BA 10 HOH 600 1133 1133 HOH HOH A . 
BA 10 HOH 601 1134 1134 HOH HOH A . 
BA 10 HOH 602 1135 1135 HOH HOH A . 
BA 10 HOH 603 1136 1136 HOH HOH A . 
BA 10 HOH 604 1137 1137 HOH HOH A . 
BA 10 HOH 605 1138 1138 HOH HOH A . 
BA 10 HOH 606 1139 1139 HOH HOH A . 
BA 10 HOH 607 1140 1140 HOH HOH A . 
BA 10 HOH 608 1141 1141 HOH HOH A . 
BA 10 HOH 609 1142 1142 HOH HOH A . 
BA 10 HOH 610 1143 1143 HOH HOH A . 
BA 10 HOH 611 1144 1144 HOH HOH A . 
BA 10 HOH 612 1145 1145 HOH HOH A . 
BA 10 HOH 613 1146 1146 HOH HOH A . 
BA 10 HOH 614 1147 1147 HOH HOH A . 
BA 10 HOH 615 1148 1148 HOH HOH A . 
BA 10 HOH 616 1149 1149 HOH HOH A . 
BA 10 HOH 617 1150 1150 HOH HOH A . 
BA 10 HOH 618 1151 1151 HOH HOH A . 
BA 10 HOH 619 1152 1152 HOH HOH A . 
BA 10 HOH 620 1153 1153 HOH HOH A . 
BA 10 HOH 621 1154 1154 HOH HOH A . 
BA 10 HOH 622 1155 1155 HOH HOH A . 
BA 10 HOH 623 1156 1156 HOH HOH A . 
BA 10 HOH 624 1157 1157 HOH HOH A . 
BA 10 HOH 625 1158 1158 HOH HOH A . 
BA 10 HOH 626 1159 1159 HOH HOH A . 
BA 10 HOH 627 1160 1160 HOH HOH A . 
BA 10 HOH 628 1161 1161 HOH HOH A . 
BA 10 HOH 629 1162 1162 HOH HOH A . 
BA 10 HOH 630 1163 1163 HOH HOH A . 
BA 10 HOH 631 1164 1164 HOH HOH A . 
BA 10 HOH 632 1165 1165 HOH HOH A . 
BA 10 HOH 633 1166 1166 HOH HOH A . 
BA 10 HOH 634 1167 1167 HOH HOH A . 
BA 10 HOH 635 1168 1168 HOH HOH A . 
BA 10 HOH 636 1169 1169 HOH HOH A . 
BA 10 HOH 637 1170 1170 HOH HOH A . 
BA 10 HOH 638 1171 1171 HOH HOH A . 
BA 10 HOH 639 1172 1172 HOH HOH A . 
BA 10 HOH 640 1173 1173 HOH HOH A . 
BA 10 HOH 641 1174 1174 HOH HOH A . 
BA 10 HOH 642 1175 1175 HOH HOH A . 
BA 10 HOH 643 1176 1176 HOH HOH A . 
BA 10 HOH 644 1177 1177 HOH HOH A . 
BA 10 HOH 645 1178 1178 HOH HOH A . 
BA 10 HOH 646 1179 1179 HOH HOH A . 
BA 10 HOH 647 1180 1180 HOH HOH A . 
BA 10 HOH 648 1181 1181 HOH HOH A . 
BA 10 HOH 649 1182 1182 HOH HOH A . 
BA 10 HOH 650 1183 1183 HOH HOH A . 
BA 10 HOH 651 1184 1184 HOH HOH A . 
BA 10 HOH 652 1185 1185 HOH HOH A . 
BA 10 HOH 653 1186 1186 HOH HOH A . 
BA 10 HOH 654 1187 1187 HOH HOH A . 
BA 10 HOH 655 1188 1188 HOH HOH A . 
BA 10 HOH 656 1189 1189 HOH HOH A . 
BA 10 HOH 657 1190 1190 HOH HOH A . 
BA 10 HOH 658 1191 1191 HOH HOH A . 
BA 10 HOH 659 1192 1192 HOH HOH A . 
BA 10 HOH 660 1193 1193 HOH HOH A . 
BA 10 HOH 661 1194 1194 HOH HOH A . 
BA 10 HOH 662 1195 1195 HOH HOH A . 
BA 10 HOH 663 1196 1196 HOH HOH A . 
BA 10 HOH 664 1197 1197 HOH HOH A . 
BA 10 HOH 665 1198 1198 HOH HOH A . 
BA 10 HOH 666 1199 1199 HOH HOH A . 
BA 10 HOH 667 1200 1200 HOH HOH A . 
BA 10 HOH 668 1201 1201 HOH HOH A . 
BA 10 HOH 669 1202 1202 HOH HOH A . 
BA 10 HOH 670 1203 1203 HOH HOH A . 
BA 10 HOH 671 1204 1204 HOH HOH A . 
BA 10 HOH 672 1205 1205 HOH HOH A . 
BA 10 HOH 673 1206 1206 HOH HOH A . 
BA 10 HOH 674 1207 1207 HOH HOH A . 
BA 10 HOH 675 1208 1208 HOH HOH A . 
BA 10 HOH 676 1209 1209 HOH HOH A . 
BA 10 HOH 677 1210 1210 HOH HOH A . 
BA 10 HOH 678 1211 1211 HOH HOH A . 
BA 10 HOH 679 1212 1212 HOH HOH A . 
BA 10 HOH 680 1213 1213 HOH HOH A . 
BA 10 HOH 681 1214 1214 HOH HOH A . 
BA 10 HOH 682 1215 1215 HOH HOH A . 
BA 10 HOH 683 1216 1216 HOH HOH A . 
BA 10 HOH 684 1217 1217 HOH HOH A . 
BA 10 HOH 685 1218 1218 HOH HOH A . 
BA 10 HOH 686 1219 1219 HOH HOH A . 
BA 10 HOH 687 1220 1220 HOH HOH A . 
BA 10 HOH 688 1221 1221 HOH HOH A . 
BA 10 HOH 689 1222 1222 HOH HOH A . 
BA 10 HOH 690 1223 1223 HOH HOH A . 
BA 10 HOH 691 1224 1224 HOH HOH A . 
BA 10 HOH 692 1225 1225 HOH HOH A . 
BA 10 HOH 693 1226 1226 HOH HOH A . 
BA 10 HOH 694 1227 1227 HOH HOH A . 
BA 10 HOH 695 1228 1228 HOH HOH A . 
BA 10 HOH 696 1229 1229 HOH HOH A . 
BA 10 HOH 697 1230 1230 HOH HOH A . 
BA 10 HOH 698 1231 1231 HOH HOH A . 
BA 10 HOH 699 1232 1232 HOH HOH A . 
BA 10 HOH 700 1233 1233 HOH HOH A . 
BA 10 HOH 701 1234 1234 HOH HOH A . 
BA 10 HOH 702 1235 1235 HOH HOH A . 
BA 10 HOH 703 1236 1236 HOH HOH A . 
BA 10 HOH 704 1237 1237 HOH HOH A . 
BA 10 HOH 705 1238 1238 HOH HOH A . 
BA 10 HOH 706 1239 1239 HOH HOH A . 
BA 10 HOH 707 1240 1240 HOH HOH A . 
BA 10 HOH 708 1241 1241 HOH HOH A . 
BA 10 HOH 709 1242 1242 HOH HOH A . 
BA 10 HOH 710 1243 1243 HOH HOH A . 
BA 10 HOH 711 1244 1244 HOH HOH A . 
BA 10 HOH 712 1245 1245 HOH HOH A . 
BA 10 HOH 713 1246 1246 HOH HOH A . 
BA 10 HOH 714 1247 1247 HOH HOH A . 
BA 10 HOH 715 1248 1248 HOH HOH A . 
BA 10 HOH 716 1249 1249 HOH HOH A . 
BA 10 HOH 717 1250 1250 HOH HOH A . 
BA 10 HOH 718 1251 1251 HOH HOH A . 
BA 10 HOH 719 1252 1252 HOH HOH A . 
BA 10 HOH 720 1253 1253 HOH HOH A . 
BA 10 HOH 721 1254 1254 HOH HOH A . 
BA 10 HOH 722 1255 1255 HOH HOH A . 
BA 10 HOH 723 1256 1256 HOH HOH A . 
BA 10 HOH 724 1257 1257 HOH HOH A . 
BA 10 HOH 725 1258 1258 HOH HOH A . 
BA 10 HOH 726 1259 1259 HOH HOH A . 
BA 10 HOH 727 1260 1260 HOH HOH A . 
BA 10 HOH 728 1261 1261 HOH HOH A . 
BA 10 HOH 729 1262 1262 HOH HOH A . 
BA 10 HOH 730 1263 1263 HOH HOH A . 
BA 10 HOH 731 1264 1264 HOH HOH A . 
BA 10 HOH 732 1265 1265 HOH HOH A . 
BA 10 HOH 733 1266 1266 HOH HOH A . 
BA 10 HOH 734 1267 1267 HOH HOH A . 
BA 10 HOH 735 1268 1268 HOH HOH A . 
BA 10 HOH 736 1269 1269 HOH HOH A . 
BA 10 HOH 737 1270 1270 HOH HOH A . 
BA 10 HOH 738 1271 1271 HOH HOH A . 
BA 10 HOH 739 1272 1272 HOH HOH A . 
BA 10 HOH 740 1273 1273 HOH HOH A . 
BA 10 HOH 741 1274 1274 HOH HOH A . 
BA 10 HOH 742 1275 1275 HOH HOH A . 
BA 10 HOH 743 1276 1276 HOH HOH A . 
BA 10 HOH 744 1277 1277 HOH HOH A . 
BA 10 HOH 745 1278 1278 HOH HOH A . 
BA 10 HOH 746 1279 1279 HOH HOH A . 
BA 10 HOH 747 1280 1280 HOH HOH A . 
BA 10 HOH 748 1281 1281 HOH HOH A . 
BA 10 HOH 749 1282 1282 HOH HOH A . 
BA 10 HOH 750 1283 1283 HOH HOH A . 
BA 10 HOH 751 1284 1284 HOH HOH A . 
BA 10 HOH 752 1285 1285 HOH HOH A . 
BA 10 HOH 753 1286 1286 HOH HOH A . 
BA 10 HOH 754 1287 1287 HOH HOH A . 
BA 10 HOH 755 1288 1288 HOH HOH A . 
BA 10 HOH 756 1289 1289 HOH HOH A . 
BA 10 HOH 757 1290 1290 HOH HOH A . 
BA 10 HOH 758 1291 1291 HOH HOH A . 
BA 10 HOH 759 1292 1292 HOH HOH A . 
BA 10 HOH 760 1293 1293 HOH HOH A . 
BA 10 HOH 761 1294 1294 HOH HOH A . 
BA 10 HOH 762 1295 1295 HOH HOH A . 
BA 10 HOH 763 1296 1296 HOH HOH A . 
BA 10 HOH 764 1297 1297 HOH HOH A . 
BA 10 HOH 765 1298 1298 HOH HOH A . 
BA 10 HOH 766 1299 1299 HOH HOH A . 
BA 10 HOH 767 1300 1300 HOH HOH A . 
BA 10 HOH 768 1301 1301 HOH HOH A . 
BA 10 HOH 769 1302 1302 HOH HOH A . 
BA 10 HOH 770 1303 1303 HOH HOH A . 
BA 10 HOH 771 1304 1304 HOH HOH A . 
BA 10 HOH 772 1305 1305 HOH HOH A . 
BA 10 HOH 773 1306 1306 HOH HOH A . 
BA 10 HOH 774 1307 1307 HOH HOH A . 
BA 10 HOH 775 1308 1308 HOH HOH A . 
BA 10 HOH 776 1309 1309 HOH HOH A . 
BA 10 HOH 777 1310 1310 HOH HOH A . 
BA 10 HOH 778 1311 1311 HOH HOH A . 
BA 10 HOH 779 1312 1312 HOH HOH A . 
BA 10 HOH 780 1313 1313 HOH HOH A . 
BA 10 HOH 781 1314 1314 HOH HOH A . 
BA 10 HOH 782 1315 1315 HOH HOH A . 
BA 10 HOH 783 1316 1316 HOH HOH A . 
BA 10 HOH 784 1317 1317 HOH HOH A . 
BA 10 HOH 785 1318 1318 HOH HOH A . 
BA 10 HOH 786 1319 1319 HOH HOH A . 
BA 10 HOH 787 1320 1320 HOH HOH A . 
BA 10 HOH 788 1321 1321 HOH HOH A . 
BA 10 HOH 789 1322 1322 HOH HOH A . 
BA 10 HOH 790 1323 1323 HOH HOH A . 
BA 10 HOH 791 1324 1324 HOH HOH A . 
BA 10 HOH 792 1325 1325 HOH HOH A . 
BA 10 HOH 793 1326 1326 HOH HOH A . 
BA 10 HOH 794 1327 1327 HOH HOH A . 
BA 10 HOH 795 1328 1328 HOH HOH A . 
BA 10 HOH 796 1329 1329 HOH HOH A . 
BA 10 HOH 797 1330 1330 HOH HOH A . 
BA 10 HOH 798 1331 1331 HOH HOH A . 
BA 10 HOH 799 1332 1332 HOH HOH A . 
BA 10 HOH 800 1333 1333 HOH HOH A . 
BA 10 HOH 801 1334 1334 HOH HOH A . 
BA 10 HOH 802 1335 1335 HOH HOH A . 
BA 10 HOH 803 1336 1336 HOH HOH A . 
BA 10 HOH 804 1337 1337 HOH HOH A . 
BA 10 HOH 805 1338 1338 HOH HOH A . 
BA 10 HOH 806 1339 1339 HOH HOH A . 
BA 10 HOH 807 1340 1340 HOH HOH A . 
BA 10 HOH 808 1341 1341 HOH HOH A . 
BA 10 HOH 809 1342 1342 HOH HOH A . 
BA 10 HOH 810 1343 1343 HOH HOH A . 
BA 10 HOH 811 1344 1344 HOH HOH A . 
BA 10 HOH 812 1345 1345 HOH HOH A . 
BA 10 HOH 813 1346 1346 HOH HOH A . 
BA 10 HOH 814 1347 1347 HOH HOH A . 
BA 10 HOH 815 1348 1348 HOH HOH A . 
BA 10 HOH 816 1349 1349 HOH HOH A . 
BA 10 HOH 817 1350 1350 HOH HOH A . 
BA 10 HOH 818 1351 1351 HOH HOH A . 
BA 10 HOH 819 1352 1352 HOH HOH A . 
BA 10 HOH 820 1353 1353 HOH HOH A . 
BA 10 HOH 821 1366 1366 HOH HOH A . 
BA 10 HOH 822 1504 1504 HOH HOH A . 
BA 10 HOH 823 1584 1584 HOH HOH A . 
CA 10 HOH 1   535  535  HOH HOH B . 
CA 10 HOH 2   590  590  HOH HOH B . 
CA 10 HOH 3   625  625  HOH HOH B . 
CA 10 HOH 4   826  826  HOH HOH B . 
CA 10 HOH 5   829  829  HOH HOH B . 
CA 10 HOH 6   830  830  HOH HOH B . 
CA 10 HOH 7   831  831  HOH HOH B . 
CA 10 HOH 8   832  832  HOH HOH B . 
CA 10 HOH 9   833  833  HOH HOH B . 
CA 10 HOH 10  834  834  HOH HOH B . 
CA 10 HOH 11  835  835  HOH HOH B . 
CA 10 HOH 12  836  836  HOH HOH B . 
CA 10 HOH 13  837  837  HOH HOH B . 
CA 10 HOH 14  838  838  HOH HOH B . 
CA 10 HOH 15  839  839  HOH HOH B . 
CA 10 HOH 16  840  840  HOH HOH B . 
CA 10 HOH 17  841  841  HOH HOH B . 
CA 10 HOH 18  842  842  HOH HOH B . 
CA 10 HOH 19  843  843  HOH HOH B . 
CA 10 HOH 20  844  844  HOH HOH B . 
CA 10 HOH 21  845  845  HOH HOH B . 
CA 10 HOH 22  846  846  HOH HOH B . 
CA 10 HOH 23  847  847  HOH HOH B . 
CA 10 HOH 24  848  848  HOH HOH B . 
CA 10 HOH 25  849  849  HOH HOH B . 
CA 10 HOH 26  850  850  HOH HOH B . 
CA 10 HOH 27  851  851  HOH HOH B . 
CA 10 HOH 28  852  852  HOH HOH B . 
CA 10 HOH 29  853  853  HOH HOH B . 
CA 10 HOH 30  854  854  HOH HOH B . 
CA 10 HOH 31  855  855  HOH HOH B . 
CA 10 HOH 32  856  856  HOH HOH B . 
CA 10 HOH 33  857  857  HOH HOH B . 
CA 10 HOH 34  858  858  HOH HOH B . 
CA 10 HOH 35  859  859  HOH HOH B . 
CA 10 HOH 36  860  860  HOH HOH B . 
CA 10 HOH 37  861  861  HOH HOH B . 
CA 10 HOH 38  862  862  HOH HOH B . 
CA 10 HOH 39  863  863  HOH HOH B . 
CA 10 HOH 40  864  864  HOH HOH B . 
CA 10 HOH 41  865  865  HOH HOH B . 
CA 10 HOH 42  866  866  HOH HOH B . 
CA 10 HOH 43  867  867  HOH HOH B . 
CA 10 HOH 44  868  868  HOH HOH B . 
CA 10 HOH 45  869  869  HOH HOH B . 
CA 10 HOH 46  870  870  HOH HOH B . 
CA 10 HOH 47  871  871  HOH HOH B . 
CA 10 HOH 48  872  872  HOH HOH B . 
CA 10 HOH 49  873  873  HOH HOH B . 
CA 10 HOH 50  874  874  HOH HOH B . 
CA 10 HOH 51  875  875  HOH HOH B . 
CA 10 HOH 52  876  876  HOH HOH B . 
CA 10 HOH 53  877  877  HOH HOH B . 
CA 10 HOH 54  878  878  HOH HOH B . 
CA 10 HOH 55  879  879  HOH HOH B . 
CA 10 HOH 56  880  880  HOH HOH B . 
CA 10 HOH 57  881  881  HOH HOH B . 
CA 10 HOH 58  882  882  HOH HOH B . 
CA 10 HOH 59  883  883  HOH HOH B . 
CA 10 HOH 60  884  884  HOH HOH B . 
CA 10 HOH 61  885  885  HOH HOH B . 
CA 10 HOH 62  886  886  HOH HOH B . 
CA 10 HOH 63  887  887  HOH HOH B . 
CA 10 HOH 64  888  888  HOH HOH B . 
CA 10 HOH 65  889  889  HOH HOH B . 
CA 10 HOH 66  890  890  HOH HOH B . 
CA 10 HOH 67  891  891  HOH HOH B . 
CA 10 HOH 68  892  892  HOH HOH B . 
CA 10 HOH 69  893  893  HOH HOH B . 
CA 10 HOH 70  894  894  HOH HOH B . 
CA 10 HOH 71  895  895  HOH HOH B . 
CA 10 HOH 72  896  896  HOH HOH B . 
CA 10 HOH 73  897  897  HOH HOH B . 
CA 10 HOH 74  898  898  HOH HOH B . 
CA 10 HOH 75  899  899  HOH HOH B . 
CA 10 HOH 76  900  900  HOH HOH B . 
CA 10 HOH 77  901  901  HOH HOH B . 
CA 10 HOH 78  902  902  HOH HOH B . 
CA 10 HOH 79  903  903  HOH HOH B . 
CA 10 HOH 80  904  904  HOH HOH B . 
CA 10 HOH 81  905  905  HOH HOH B . 
CA 10 HOH 82  906  906  HOH HOH B . 
CA 10 HOH 83  907  907  HOH HOH B . 
CA 10 HOH 84  908  908  HOH HOH B . 
CA 10 HOH 85  909  909  HOH HOH B . 
CA 10 HOH 86  910  910  HOH HOH B . 
CA 10 HOH 87  911  911  HOH HOH B . 
CA 10 HOH 88  912  912  HOH HOH B . 
CA 10 HOH 89  913  913  HOH HOH B . 
CA 10 HOH 90  914  914  HOH HOH B . 
CA 10 HOH 91  915  915  HOH HOH B . 
CA 10 HOH 92  916  916  HOH HOH B . 
CA 10 HOH 93  917  917  HOH HOH B . 
CA 10 HOH 94  918  918  HOH HOH B . 
CA 10 HOH 95  919  919  HOH HOH B . 
CA 10 HOH 96  920  920  HOH HOH B . 
CA 10 HOH 97  921  921  HOH HOH B . 
CA 10 HOH 98  922  922  HOH HOH B . 
CA 10 HOH 99  923  923  HOH HOH B . 
CA 10 HOH 100 924  924  HOH HOH B . 
CA 10 HOH 101 925  925  HOH HOH B . 
CA 10 HOH 102 926  926  HOH HOH B . 
CA 10 HOH 103 927  927  HOH HOH B . 
CA 10 HOH 104 928  928  HOH HOH B . 
CA 10 HOH 105 929  929  HOH HOH B . 
CA 10 HOH 106 930  930  HOH HOH B . 
CA 10 HOH 107 931  931  HOH HOH B . 
CA 10 HOH 108 932  932  HOH HOH B . 
CA 10 HOH 109 933  933  HOH HOH B . 
CA 10 HOH 110 934  934  HOH HOH B . 
CA 10 HOH 111 935  935  HOH HOH B . 
CA 10 HOH 112 936  936  HOH HOH B . 
CA 10 HOH 113 937  937  HOH HOH B . 
CA 10 HOH 114 938  938  HOH HOH B . 
CA 10 HOH 115 939  939  HOH HOH B . 
CA 10 HOH 116 940  940  HOH HOH B . 
CA 10 HOH 117 941  941  HOH HOH B . 
CA 10 HOH 118 942  942  HOH HOH B . 
CA 10 HOH 119 943  943  HOH HOH B . 
CA 10 HOH 120 944  944  HOH HOH B . 
CA 10 HOH 121 945  945  HOH HOH B . 
CA 10 HOH 122 946  946  HOH HOH B . 
CA 10 HOH 123 947  947  HOH HOH B . 
CA 10 HOH 124 948  948  HOH HOH B . 
CA 10 HOH 125 949  949  HOH HOH B . 
CA 10 HOH 126 950  950  HOH HOH B . 
CA 10 HOH 127 951  951  HOH HOH B . 
CA 10 HOH 128 952  952  HOH HOH B . 
CA 10 HOH 129 953  953  HOH HOH B . 
CA 10 HOH 130 954  954  HOH HOH B . 
CA 10 HOH 131 955  955  HOH HOH B . 
CA 10 HOH 132 956  956  HOH HOH B . 
CA 10 HOH 133 957  957  HOH HOH B . 
CA 10 HOH 134 958  958  HOH HOH B . 
CA 10 HOH 135 959  959  HOH HOH B . 
CA 10 HOH 136 960  960  HOH HOH B . 
CA 10 HOH 137 961  961  HOH HOH B . 
CA 10 HOH 138 962  962  HOH HOH B . 
CA 10 HOH 139 963  963  HOH HOH B . 
CA 10 HOH 140 964  964  HOH HOH B . 
CA 10 HOH 141 965  965  HOH HOH B . 
CA 10 HOH 142 966  966  HOH HOH B . 
CA 10 HOH 143 967  967  HOH HOH B . 
CA 10 HOH 144 968  968  HOH HOH B . 
CA 10 HOH 145 969  969  HOH HOH B . 
CA 10 HOH 146 970  970  HOH HOH B . 
CA 10 HOH 147 971  971  HOH HOH B . 
CA 10 HOH 148 972  972  HOH HOH B . 
CA 10 HOH 149 973  973  HOH HOH B . 
CA 10 HOH 150 974  974  HOH HOH B . 
CA 10 HOH 151 975  975  HOH HOH B . 
CA 10 HOH 152 976  976  HOH HOH B . 
CA 10 HOH 153 977  977  HOH HOH B . 
CA 10 HOH 154 978  978  HOH HOH B . 
CA 10 HOH 155 979  979  HOH HOH B . 
CA 10 HOH 156 980  980  HOH HOH B . 
CA 10 HOH 157 981  981  HOH HOH B . 
CA 10 HOH 158 982  982  HOH HOH B . 
CA 10 HOH 159 983  983  HOH HOH B . 
CA 10 HOH 160 984  984  HOH HOH B . 
CA 10 HOH 161 985  985  HOH HOH B . 
CA 10 HOH 162 986  986  HOH HOH B . 
CA 10 HOH 163 987  987  HOH HOH B . 
CA 10 HOH 164 988  988  HOH HOH B . 
CA 10 HOH 165 989  989  HOH HOH B . 
CA 10 HOH 166 990  990  HOH HOH B . 
CA 10 HOH 167 991  991  HOH HOH B . 
CA 10 HOH 168 992  992  HOH HOH B . 
CA 10 HOH 169 993  993  HOH HOH B . 
CA 10 HOH 170 994  994  HOH HOH B . 
CA 10 HOH 171 995  995  HOH HOH B . 
CA 10 HOH 172 996  996  HOH HOH B . 
CA 10 HOH 173 997  997  HOH HOH B . 
CA 10 HOH 174 998  998  HOH HOH B . 
CA 10 HOH 175 999  999  HOH HOH B . 
CA 10 HOH 176 1000 1000 HOH HOH B . 
CA 10 HOH 177 1001 1001 HOH HOH B . 
CA 10 HOH 178 1002 1002 HOH HOH B . 
CA 10 HOH 179 1003 1003 HOH HOH B . 
CA 10 HOH 180 1004 1004 HOH HOH B . 
CA 10 HOH 181 1005 1005 HOH HOH B . 
CA 10 HOH 182 1006 1006 HOH HOH B . 
CA 10 HOH 183 1007 1007 HOH HOH B . 
CA 10 HOH 184 1008 1008 HOH HOH B . 
CA 10 HOH 185 1009 1009 HOH HOH B . 
CA 10 HOH 186 1010 1010 HOH HOH B . 
CA 10 HOH 187 1011 1011 HOH HOH B . 
CA 10 HOH 188 1012 1012 HOH HOH B . 
CA 10 HOH 189 1013 1013 HOH HOH B . 
CA 10 HOH 190 1014 1014 HOH HOH B . 
CA 10 HOH 191 1015 1015 HOH HOH B . 
CA 10 HOH 192 1016 1016 HOH HOH B . 
CA 10 HOH 193 1017 1017 HOH HOH B . 
CA 10 HOH 194 1018 1018 HOH HOH B . 
CA 10 HOH 195 1019 1019 HOH HOH B . 
CA 10 HOH 196 1020 1020 HOH HOH B . 
CA 10 HOH 197 1021 1021 HOH HOH B . 
CA 10 HOH 198 1022 1022 HOH HOH B . 
CA 10 HOH 199 1023 1023 HOH HOH B . 
CA 10 HOH 200 1024 1024 HOH HOH B . 
CA 10 HOH 201 1025 1025 HOH HOH B . 
CA 10 HOH 202 1026 1026 HOH HOH B . 
CA 10 HOH 203 1027 1027 HOH HOH B . 
CA 10 HOH 204 1028 1028 HOH HOH B . 
CA 10 HOH 205 1029 1029 HOH HOH B . 
CA 10 HOH 206 1030 1030 HOH HOH B . 
CA 10 HOH 207 1031 1031 HOH HOH B . 
CA 10 HOH 208 1032 1032 HOH HOH B . 
CA 10 HOH 209 1033 1033 HOH HOH B . 
CA 10 HOH 210 1034 1034 HOH HOH B . 
CA 10 HOH 211 1035 1035 HOH HOH B . 
CA 10 HOH 212 1036 1036 HOH HOH B . 
CA 10 HOH 213 1037 1037 HOH HOH B . 
CA 10 HOH 214 1038 1038 HOH HOH B . 
CA 10 HOH 215 1039 1039 HOH HOH B . 
CA 10 HOH 216 1040 1040 HOH HOH B . 
CA 10 HOH 217 1041 1041 HOH HOH B . 
CA 10 HOH 218 1042 1042 HOH HOH B . 
CA 10 HOH 219 1043 1043 HOH HOH B . 
CA 10 HOH 220 1044 1044 HOH HOH B . 
CA 10 HOH 221 1045 1045 HOH HOH B . 
CA 10 HOH 222 1046 1046 HOH HOH B . 
CA 10 HOH 223 1047 1047 HOH HOH B . 
CA 10 HOH 224 1048 1048 HOH HOH B . 
CA 10 HOH 225 1049 1049 HOH HOH B . 
CA 10 HOH 226 1050 1050 HOH HOH B . 
CA 10 HOH 227 1051 1051 HOH HOH B . 
CA 10 HOH 228 1052 1052 HOH HOH B . 
CA 10 HOH 229 1053 1053 HOH HOH B . 
CA 10 HOH 230 1054 1054 HOH HOH B . 
CA 10 HOH 231 1055 1055 HOH HOH B . 
CA 10 HOH 232 1056 1056 HOH HOH B . 
CA 10 HOH 233 1057 1057 HOH HOH B . 
CA 10 HOH 234 1058 1058 HOH HOH B . 
CA 10 HOH 235 1059 1059 HOH HOH B . 
CA 10 HOH 236 1060 1060 HOH HOH B . 
CA 10 HOH 237 1061 1061 HOH HOH B . 
CA 10 HOH 238 1062 1062 HOH HOH B . 
CA 10 HOH 239 1063 1063 HOH HOH B . 
CA 10 HOH 240 1064 1064 HOH HOH B . 
CA 10 HOH 241 1065 1065 HOH HOH B . 
CA 10 HOH 242 1066 1066 HOH HOH B . 
CA 10 HOH 243 1067 1067 HOH HOH B . 
CA 10 HOH 244 1068 1068 HOH HOH B . 
CA 10 HOH 245 1069 1069 HOH HOH B . 
CA 10 HOH 246 1070 1070 HOH HOH B . 
CA 10 HOH 247 1071 1071 HOH HOH B . 
CA 10 HOH 248 1072 1072 HOH HOH B . 
CA 10 HOH 249 1073 1073 HOH HOH B . 
CA 10 HOH 250 1074 1074 HOH HOH B . 
CA 10 HOH 251 1075 1075 HOH HOH B . 
CA 10 HOH 252 1076 1076 HOH HOH B . 
CA 10 HOH 253 1077 1077 HOH HOH B . 
CA 10 HOH 254 1078 1078 HOH HOH B . 
CA 10 HOH 255 1079 1079 HOH HOH B . 
CA 10 HOH 256 1080 1080 HOH HOH B . 
CA 10 HOH 257 1081 1081 HOH HOH B . 
CA 10 HOH 258 1082 1082 HOH HOH B . 
CA 10 HOH 259 1083 1083 HOH HOH B . 
CA 10 HOH 260 1084 1084 HOH HOH B . 
CA 10 HOH 261 1085 1085 HOH HOH B . 
CA 10 HOH 262 1086 1086 HOH HOH B . 
CA 10 HOH 263 1087 1087 HOH HOH B . 
CA 10 HOH 264 1088 1088 HOH HOH B . 
CA 10 HOH 265 1089 1089 HOH HOH B . 
CA 10 HOH 266 1090 1090 HOH HOH B . 
CA 10 HOH 267 1091 1091 HOH HOH B . 
CA 10 HOH 268 1092 1092 HOH HOH B . 
CA 10 HOH 269 1093 1093 HOH HOH B . 
CA 10 HOH 270 1094 1094 HOH HOH B . 
CA 10 HOH 271 1095 1095 HOH HOH B . 
CA 10 HOH 272 1096 1096 HOH HOH B . 
CA 10 HOH 273 1097 1097 HOH HOH B . 
CA 10 HOH 274 1098 1098 HOH HOH B . 
CA 10 HOH 275 1099 1099 HOH HOH B . 
CA 10 HOH 276 1100 1100 HOH HOH B . 
CA 10 HOH 277 1101 1101 HOH HOH B . 
CA 10 HOH 278 1102 1102 HOH HOH B . 
CA 10 HOH 279 1103 1103 HOH HOH B . 
CA 10 HOH 280 1104 1104 HOH HOH B . 
CA 10 HOH 281 1105 1105 HOH HOH B . 
CA 10 HOH 282 1106 1106 HOH HOH B . 
CA 10 HOH 283 1107 1107 HOH HOH B . 
CA 10 HOH 284 1108 1108 HOH HOH B . 
CA 10 HOH 285 1109 1109 HOH HOH B . 
CA 10 HOH 286 1110 1110 HOH HOH B . 
CA 10 HOH 287 1111 1111 HOH HOH B . 
CA 10 HOH 288 1112 1112 HOH HOH B . 
CA 10 HOH 289 1113 1113 HOH HOH B . 
CA 10 HOH 290 1114 1114 HOH HOH B . 
CA 10 HOH 291 1115 1115 HOH HOH B . 
CA 10 HOH 292 1116 1116 HOH HOH B . 
CA 10 HOH 293 1117 1117 HOH HOH B . 
CA 10 HOH 294 1118 1118 HOH HOH B . 
CA 10 HOH 295 1119 1119 HOH HOH B . 
CA 10 HOH 296 1120 1120 HOH HOH B . 
CA 10 HOH 297 1121 1121 HOH HOH B . 
CA 10 HOH 298 1122 1122 HOH HOH B . 
CA 10 HOH 299 1123 1123 HOH HOH B . 
CA 10 HOH 300 1124 1124 HOH HOH B . 
CA 10 HOH 301 1125 1125 HOH HOH B . 
CA 10 HOH 302 1126 1126 HOH HOH B . 
CA 10 HOH 303 1127 1127 HOH HOH B . 
CA 10 HOH 304 1128 1128 HOH HOH B . 
CA 10 HOH 305 1129 1129 HOH HOH B . 
CA 10 HOH 306 1130 1130 HOH HOH B . 
CA 10 HOH 307 1131 1131 HOH HOH B . 
CA 10 HOH 308 1132 1132 HOH HOH B . 
CA 10 HOH 309 1133 1133 HOH HOH B . 
CA 10 HOH 310 1134 1134 HOH HOH B . 
CA 10 HOH 311 1135 1135 HOH HOH B . 
CA 10 HOH 312 1136 1136 HOH HOH B . 
CA 10 HOH 313 1137 1137 HOH HOH B . 
CA 10 HOH 314 1138 1138 HOH HOH B . 
CA 10 HOH 315 1139 1139 HOH HOH B . 
CA 10 HOH 316 1140 1140 HOH HOH B . 
CA 10 HOH 317 1141 1141 HOH HOH B . 
CA 10 HOH 318 1142 1142 HOH HOH B . 
CA 10 HOH 319 1143 1143 HOH HOH B . 
CA 10 HOH 320 1144 1144 HOH HOH B . 
CA 10 HOH 321 1145 1145 HOH HOH B . 
CA 10 HOH 322 1146 1146 HOH HOH B . 
CA 10 HOH 323 1147 1147 HOH HOH B . 
CA 10 HOH 324 1148 1148 HOH HOH B . 
CA 10 HOH 325 1149 1149 HOH HOH B . 
CA 10 HOH 326 1150 1150 HOH HOH B . 
CA 10 HOH 327 1151 1151 HOH HOH B . 
CA 10 HOH 328 1152 1152 HOH HOH B . 
CA 10 HOH 329 1153 1153 HOH HOH B . 
CA 10 HOH 330 1154 1154 HOH HOH B . 
CA 10 HOH 331 1155 1155 HOH HOH B . 
CA 10 HOH 332 1156 1156 HOH HOH B . 
CA 10 HOH 333 1157 1157 HOH HOH B . 
CA 10 HOH 334 1158 1158 HOH HOH B . 
CA 10 HOH 335 1159 1159 HOH HOH B . 
CA 10 HOH 336 1160 1160 HOH HOH B . 
CA 10 HOH 337 1161 1161 HOH HOH B . 
CA 10 HOH 338 1162 1162 HOH HOH B . 
CA 10 HOH 339 1163 1163 HOH HOH B . 
CA 10 HOH 340 1164 1164 HOH HOH B . 
CA 10 HOH 341 1165 1165 HOH HOH B . 
CA 10 HOH 342 1166 1166 HOH HOH B . 
CA 10 HOH 343 1167 1167 HOH HOH B . 
CA 10 HOH 344 1168 1168 HOH HOH B . 
CA 10 HOH 345 1169 1169 HOH HOH B . 
CA 10 HOH 346 1170 1170 HOH HOH B . 
CA 10 HOH 347 1171 1171 HOH HOH B . 
CA 10 HOH 348 1172 1172 HOH HOH B . 
CA 10 HOH 349 1173 1173 HOH HOH B . 
CA 10 HOH 350 1174 1174 HOH HOH B . 
CA 10 HOH 351 1175 1175 HOH HOH B . 
CA 10 HOH 352 1176 1176 HOH HOH B . 
CA 10 HOH 353 1177 1177 HOH HOH B . 
CA 10 HOH 354 1178 1178 HOH HOH B . 
CA 10 HOH 355 1179 1179 HOH HOH B . 
CA 10 HOH 356 1180 1180 HOH HOH B . 
CA 10 HOH 357 1181 1181 HOH HOH B . 
CA 10 HOH 358 1182 1182 HOH HOH B . 
CA 10 HOH 359 1183 1183 HOH HOH B . 
CA 10 HOH 360 1184 1184 HOH HOH B . 
CA 10 HOH 361 1185 1185 HOH HOH B . 
CA 10 HOH 362 1186 1186 HOH HOH B . 
CA 10 HOH 363 1187 1187 HOH HOH B . 
CA 10 HOH 364 1188 1188 HOH HOH B . 
CA 10 HOH 365 1189 1189 HOH HOH B . 
CA 10 HOH 366 1190 1190 HOH HOH B . 
CA 10 HOH 367 1191 1191 HOH HOH B . 
CA 10 HOH 368 1192 1192 HOH HOH B . 
CA 10 HOH 369 1193 1193 HOH HOH B . 
CA 10 HOH 370 1194 1194 HOH HOH B . 
CA 10 HOH 371 1195 1195 HOH HOH B . 
CA 10 HOH 372 1196 1196 HOH HOH B . 
CA 10 HOH 373 1197 1197 HOH HOH B . 
CA 10 HOH 374 1198 1198 HOH HOH B . 
CA 10 HOH 375 1199 1199 HOH HOH B . 
CA 10 HOH 376 1200 1200 HOH HOH B . 
CA 10 HOH 377 1201 1201 HOH HOH B . 
CA 10 HOH 378 1202 1202 HOH HOH B . 
CA 10 HOH 379 1203 1203 HOH HOH B . 
CA 10 HOH 380 1204 1204 HOH HOH B . 
CA 10 HOH 381 1205 1205 HOH HOH B . 
CA 10 HOH 382 1206 1206 HOH HOH B . 
CA 10 HOH 383 1207 1207 HOH HOH B . 
CA 10 HOH 384 1208 1208 HOH HOH B . 
CA 10 HOH 385 1209 1209 HOH HOH B . 
CA 10 HOH 386 1210 1210 HOH HOH B . 
CA 10 HOH 387 1211 1211 HOH HOH B . 
CA 10 HOH 388 1212 1212 HOH HOH B . 
CA 10 HOH 389 1213 1213 HOH HOH B . 
CA 10 HOH 390 1214 1214 HOH HOH B . 
CA 10 HOH 391 1215 1215 HOH HOH B . 
CA 10 HOH 392 1216 1216 HOH HOH B . 
CA 10 HOH 393 1217 1217 HOH HOH B . 
CA 10 HOH 394 1218 1218 HOH HOH B . 
CA 10 HOH 395 1219 1219 HOH HOH B . 
CA 10 HOH 396 1220 1220 HOH HOH B . 
CA 10 HOH 397 1221 1221 HOH HOH B . 
CA 10 HOH 398 1222 1222 HOH HOH B . 
CA 10 HOH 399 1223 1223 HOH HOH B . 
CA 10 HOH 400 1224 1224 HOH HOH B . 
CA 10 HOH 401 1225 1225 HOH HOH B . 
CA 10 HOH 402 1226 1226 HOH HOH B . 
CA 10 HOH 403 1227 1227 HOH HOH B . 
CA 10 HOH 404 1228 1228 HOH HOH B . 
CA 10 HOH 405 1229 1229 HOH HOH B . 
CA 10 HOH 406 1230 1230 HOH HOH B . 
CA 10 HOH 407 1231 1231 HOH HOH B . 
CA 10 HOH 408 1232 1232 HOH HOH B . 
CA 10 HOH 409 1233 1233 HOH HOH B . 
CA 10 HOH 410 1234 1234 HOH HOH B . 
CA 10 HOH 411 1235 1235 HOH HOH B . 
CA 10 HOH 412 1236 1236 HOH HOH B . 
CA 10 HOH 413 1237 1237 HOH HOH B . 
CA 10 HOH 414 1238 1238 HOH HOH B . 
CA 10 HOH 415 1239 1239 HOH HOH B . 
CA 10 HOH 416 1240 1240 HOH HOH B . 
CA 10 HOH 417 1241 1241 HOH HOH B . 
CA 10 HOH 418 1242 1242 HOH HOH B . 
CA 10 HOH 419 1243 1243 HOH HOH B . 
CA 10 HOH 420 1244 1244 HOH HOH B . 
CA 10 HOH 421 1245 1245 HOH HOH B . 
CA 10 HOH 422 1246 1246 HOH HOH B . 
CA 10 HOH 423 1247 1247 HOH HOH B . 
CA 10 HOH 424 1248 1248 HOH HOH B . 
CA 10 HOH 425 1249 1249 HOH HOH B . 
CA 10 HOH 426 1250 1250 HOH HOH B . 
CA 10 HOH 427 1251 1251 HOH HOH B . 
CA 10 HOH 428 1252 1252 HOH HOH B . 
CA 10 HOH 429 1253 1253 HOH HOH B . 
CA 10 HOH 430 1254 1254 HOH HOH B . 
CA 10 HOH 431 1255 1255 HOH HOH B . 
CA 10 HOH 432 1256 1256 HOH HOH B . 
CA 10 HOH 433 1257 1257 HOH HOH B . 
CA 10 HOH 434 1258 1258 HOH HOH B . 
CA 10 HOH 435 1259 1259 HOH HOH B . 
CA 10 HOH 436 1260 1260 HOH HOH B . 
CA 10 HOH 437 1261 1261 HOH HOH B . 
CA 10 HOH 438 1262 1262 HOH HOH B . 
CA 10 HOH 439 1263 1263 HOH HOH B . 
CA 10 HOH 440 1264 1264 HOH HOH B . 
CA 10 HOH 441 1265 1265 HOH HOH B . 
CA 10 HOH 442 1266 1266 HOH HOH B . 
CA 10 HOH 443 1267 1267 HOH HOH B . 
CA 10 HOH 444 1268 1268 HOH HOH B . 
CA 10 HOH 445 1269 1269 HOH HOH B . 
CA 10 HOH 446 1270 1270 HOH HOH B . 
CA 10 HOH 447 1271 1271 HOH HOH B . 
CA 10 HOH 448 1272 1272 HOH HOH B . 
CA 10 HOH 449 1273 1273 HOH HOH B . 
CA 10 HOH 450 1274 1274 HOH HOH B . 
CA 10 HOH 451 1275 1275 HOH HOH B . 
CA 10 HOH 452 1276 1276 HOH HOH B . 
CA 10 HOH 453 1277 1277 HOH HOH B . 
CA 10 HOH 454 1278 1278 HOH HOH B . 
CA 10 HOH 455 1279 1279 HOH HOH B . 
CA 10 HOH 456 1280 1280 HOH HOH B . 
CA 10 HOH 457 1281 1281 HOH HOH B . 
CA 10 HOH 458 1282 1282 HOH HOH B . 
CA 10 HOH 459 1283 1283 HOH HOH B . 
CA 10 HOH 460 1284 1284 HOH HOH B . 
CA 10 HOH 461 1285 1285 HOH HOH B . 
CA 10 HOH 462 1286 1286 HOH HOH B . 
CA 10 HOH 463 1287 1287 HOH HOH B . 
CA 10 HOH 464 1288 1288 HOH HOH B . 
CA 10 HOH 465 1289 1289 HOH HOH B . 
CA 10 HOH 466 1290 1290 HOH HOH B . 
CA 10 HOH 467 1291 1291 HOH HOH B . 
CA 10 HOH 468 1292 1292 HOH HOH B . 
CA 10 HOH 469 1293 1293 HOH HOH B . 
CA 10 HOH 470 1294 1294 HOH HOH B . 
CA 10 HOH 471 1295 1295 HOH HOH B . 
CA 10 HOH 472 1296 1296 HOH HOH B . 
CA 10 HOH 473 1297 1297 HOH HOH B . 
CA 10 HOH 474 1298 1298 HOH HOH B . 
CA 10 HOH 475 1299 1299 HOH HOH B . 
CA 10 HOH 476 1300 1300 HOH HOH B . 
CA 10 HOH 477 1301 1301 HOH HOH B . 
CA 10 HOH 478 1302 1302 HOH HOH B . 
CA 10 HOH 479 1303 1303 HOH HOH B . 
CA 10 HOH 480 1304 1304 HOH HOH B . 
CA 10 HOH 481 1305 1305 HOH HOH B . 
CA 10 HOH 482 1306 1306 HOH HOH B . 
CA 10 HOH 483 1307 1307 HOH HOH B . 
CA 10 HOH 484 1308 1308 HOH HOH B . 
CA 10 HOH 485 1309 1309 HOH HOH B . 
CA 10 HOH 486 1310 1310 HOH HOH B . 
CA 10 HOH 487 1311 1311 HOH HOH B . 
CA 10 HOH 488 1313 1313 HOH HOH B . 
CA 10 HOH 489 1314 1314 HOH HOH B . 
CA 10 HOH 490 1315 1315 HOH HOH B . 
CA 10 HOH 491 1316 1316 HOH HOH B . 
CA 10 HOH 492 1317 1317 HOH HOH B . 
CA 10 HOH 493 1318 1318 HOH HOH B . 
CA 10 HOH 494 1319 1319 HOH HOH B . 
CA 10 HOH 495 1320 1320 HOH HOH B . 
CA 10 HOH 496 1321 1321 HOH HOH B . 
CA 10 HOH 497 1322 1322 HOH HOH B . 
CA 10 HOH 498 1323 1323 HOH HOH B . 
CA 10 HOH 499 1324 1324 HOH HOH B . 
CA 10 HOH 500 1325 1325 HOH HOH B . 
CA 10 HOH 501 1326 1326 HOH HOH B . 
CA 10 HOH 502 1327 1327 HOH HOH B . 
CA 10 HOH 503 1328 1328 HOH HOH B . 
CA 10 HOH 504 1329 1329 HOH HOH B . 
CA 10 HOH 505 1330 1330 HOH HOH B . 
CA 10 HOH 506 1331 1331 HOH HOH B . 
CA 10 HOH 507 1332 1332 HOH HOH B . 
CA 10 HOH 508 1333 1333 HOH HOH B . 
CA 10 HOH 509 1334 1334 HOH HOH B . 
CA 10 HOH 510 1335 1335 HOH HOH B . 
CA 10 HOH 511 1336 1336 HOH HOH B . 
CA 10 HOH 512 1337 1337 HOH HOH B . 
CA 10 HOH 513 1338 1338 HOH HOH B . 
CA 10 HOH 514 1339 1339 HOH HOH B . 
CA 10 HOH 515 1340 1340 HOH HOH B . 
CA 10 HOH 516 1341 1341 HOH HOH B . 
CA 10 HOH 517 1342 1342 HOH HOH B . 
CA 10 HOH 518 1343 1343 HOH HOH B . 
CA 10 HOH 519 1344 1344 HOH HOH B . 
CA 10 HOH 520 1345 1345 HOH HOH B . 
CA 10 HOH 521 1346 1346 HOH HOH B . 
CA 10 HOH 522 1347 1347 HOH HOH B . 
CA 10 HOH 523 1348 1348 HOH HOH B . 
CA 10 HOH 524 1349 1349 HOH HOH B . 
CA 10 HOH 525 1350 1350 HOH HOH B . 
CA 10 HOH 526 1351 1351 HOH HOH B . 
CA 10 HOH 527 1352 1352 HOH HOH B . 
CA 10 HOH 528 1353 1353 HOH HOH B . 
CA 10 HOH 529 1354 1354 HOH HOH B . 
CA 10 HOH 530 1355 1355 HOH HOH B . 
CA 10 HOH 531 1356 1356 HOH HOH B . 
CA 10 HOH 532 1357 1357 HOH HOH B . 
CA 10 HOH 533 1358 1358 HOH HOH B . 
CA 10 HOH 534 1359 1359 HOH HOH B . 
CA 10 HOH 535 1360 1360 HOH HOH B . 
CA 10 HOH 536 1361 1361 HOH HOH B . 
CA 10 HOH 537 1362 1362 HOH HOH B . 
CA 10 HOH 538 1363 1363 HOH HOH B . 
CA 10 HOH 539 1364 1364 HOH HOH B . 
CA 10 HOH 540 1365 1365 HOH HOH B . 
CA 10 HOH 541 1367 1367 HOH HOH B . 
CA 10 HOH 542 1368 1368 HOH HOH B . 
CA 10 HOH 543 1369 1369 HOH HOH B . 
CA 10 HOH 544 1370 1370 HOH HOH B . 
CA 10 HOH 545 1371 1371 HOH HOH B . 
CA 10 HOH 546 1372 1372 HOH HOH B . 
CA 10 HOH 547 1373 1373 HOH HOH B . 
CA 10 HOH 548 1374 1374 HOH HOH B . 
CA 10 HOH 549 1375 1375 HOH HOH B . 
CA 10 HOH 550 1376 1376 HOH HOH B . 
CA 10 HOH 551 1377 1377 HOH HOH B . 
CA 10 HOH 552 1378 1378 HOH HOH B . 
CA 10 HOH 553 1379 1379 HOH HOH B . 
CA 10 HOH 554 1380 1380 HOH HOH B . 
CA 10 HOH 555 1381 1381 HOH HOH B . 
CA 10 HOH 556 1382 1382 HOH HOH B . 
CA 10 HOH 557 1383 1383 HOH HOH B . 
CA 10 HOH 558 1384 1384 HOH HOH B . 
CA 10 HOH 559 1385 1385 HOH HOH B . 
CA 10 HOH 560 1386 1386 HOH HOH B . 
CA 10 HOH 561 1387 1387 HOH HOH B . 
CA 10 HOH 562 1388 1388 HOH HOH B . 
CA 10 HOH 563 1389 1389 HOH HOH B . 
CA 10 HOH 564 1390 1390 HOH HOH B . 
CA 10 HOH 565 1391 1391 HOH HOH B . 
CA 10 HOH 566 1392 1392 HOH HOH B . 
CA 10 HOH 567 1393 1393 HOH HOH B . 
CA 10 HOH 568 1394 1394 HOH HOH B . 
CA 10 HOH 569 1395 1395 HOH HOH B . 
CA 10 HOH 570 1396 1396 HOH HOH B . 
CA 10 HOH 571 1397 1397 HOH HOH B . 
CA 10 HOH 572 1398 1398 HOH HOH B . 
CA 10 HOH 573 1399 1399 HOH HOH B . 
CA 10 HOH 574 1400 1400 HOH HOH B . 
CA 10 HOH 575 1401 1401 HOH HOH B . 
CA 10 HOH 576 1402 1402 HOH HOH B . 
CA 10 HOH 577 1403 1403 HOH HOH B . 
CA 10 HOH 578 1404 1404 HOH HOH B . 
CA 10 HOH 579 1405 1405 HOH HOH B . 
CA 10 HOH 580 1406 1406 HOH HOH B . 
CA 10 HOH 581 1407 1407 HOH HOH B . 
CA 10 HOH 582 1408 1408 HOH HOH B . 
CA 10 HOH 583 1409 1409 HOH HOH B . 
CA 10 HOH 584 1410 1410 HOH HOH B . 
CA 10 HOH 585 1411 1411 HOH HOH B . 
CA 10 HOH 586 1412 1412 HOH HOH B . 
CA 10 HOH 587 1413 1413 HOH HOH B . 
CA 10 HOH 588 1414 1414 HOH HOH B . 
CA 10 HOH 589 1415 1415 HOH HOH B . 
CA 10 HOH 590 1416 1416 HOH HOH B . 
CA 10 HOH 591 1417 1417 HOH HOH B . 
CA 10 HOH 592 1418 1418 HOH HOH B . 
CA 10 HOH 593 1419 1419 HOH HOH B . 
CA 10 HOH 594 1420 1420 HOH HOH B . 
CA 10 HOH 595 1421 1421 HOH HOH B . 
CA 10 HOH 596 1422 1422 HOH HOH B . 
CA 10 HOH 597 1423 1423 HOH HOH B . 
CA 10 HOH 598 1424 1424 HOH HOH B . 
CA 10 HOH 599 1425 1425 HOH HOH B . 
CA 10 HOH 600 1426 1426 HOH HOH B . 
CA 10 HOH 601 1427 1427 HOH HOH B . 
CA 10 HOH 602 1428 1428 HOH HOH B . 
CA 10 HOH 603 1429 1429 HOH HOH B . 
CA 10 HOH 604 1430 1430 HOH HOH B . 
CA 10 HOH 605 1431 1431 HOH HOH B . 
CA 10 HOH 606 1432 1432 HOH HOH B . 
CA 10 HOH 607 1433 1433 HOH HOH B . 
CA 10 HOH 608 1434 1434 HOH HOH B . 
CA 10 HOH 609 1435 1435 HOH HOH B . 
CA 10 HOH 610 1436 1436 HOH HOH B . 
CA 10 HOH 611 1437 1437 HOH HOH B . 
CA 10 HOH 612 1438 1438 HOH HOH B . 
CA 10 HOH 613 1439 1439 HOH HOH B . 
CA 10 HOH 614 1440 1440 HOH HOH B . 
CA 10 HOH 615 1441 1441 HOH HOH B . 
CA 10 HOH 616 1442 1442 HOH HOH B . 
CA 10 HOH 617 1443 1443 HOH HOH B . 
CA 10 HOH 618 1444 1444 HOH HOH B . 
CA 10 HOH 619 1445 1445 HOH HOH B . 
CA 10 HOH 620 1446 1446 HOH HOH B . 
CA 10 HOH 621 1447 1447 HOH HOH B . 
CA 10 HOH 622 1448 1448 HOH HOH B . 
CA 10 HOH 623 1449 1449 HOH HOH B . 
CA 10 HOH 624 1450 1450 HOH HOH B . 
CA 10 HOH 625 1451 1451 HOH HOH B . 
CA 10 HOH 626 1452 1452 HOH HOH B . 
CA 10 HOH 627 1453 1453 HOH HOH B . 
CA 10 HOH 628 1454 1454 HOH HOH B . 
CA 10 HOH 629 1455 1455 HOH HOH B . 
CA 10 HOH 630 1456 1456 HOH HOH B . 
CA 10 HOH 631 1457 1457 HOH HOH B . 
CA 10 HOH 632 1458 1458 HOH HOH B . 
CA 10 HOH 633 1459 1459 HOH HOH B . 
CA 10 HOH 634 1460 1460 HOH HOH B . 
CA 10 HOH 635 1461 1461 HOH HOH B . 
CA 10 HOH 636 1462 1462 HOH HOH B . 
CA 10 HOH 637 1464 1464 HOH HOH B . 
CA 10 HOH 638 1465 1465 HOH HOH B . 
CA 10 HOH 639 1466 1466 HOH HOH B . 
CA 10 HOH 640 1467 1467 HOH HOH B . 
CA 10 HOH 641 1468 1468 HOH HOH B . 
CA 10 HOH 642 1469 1469 HOH HOH B . 
CA 10 HOH 643 1470 1470 HOH HOH B . 
CA 10 HOH 644 1471 1471 HOH HOH B . 
CA 10 HOH 645 1472 1472 HOH HOH B . 
CA 10 HOH 646 1473 1473 HOH HOH B . 
CA 10 HOH 647 1474 1474 HOH HOH B . 
CA 10 HOH 648 1475 1475 HOH HOH B . 
CA 10 HOH 649 1476 1476 HOH HOH B . 
CA 10 HOH 650 1477 1477 HOH HOH B . 
CA 10 HOH 651 1478 1478 HOH HOH B . 
CA 10 HOH 652 1479 1479 HOH HOH B . 
CA 10 HOH 653 1480 1480 HOH HOH B . 
CA 10 HOH 654 1481 1481 HOH HOH B . 
CA 10 HOH 655 1482 1482 HOH HOH B . 
CA 10 HOH 656 1483 1483 HOH HOH B . 
CA 10 HOH 657 1484 1484 HOH HOH B . 
CA 10 HOH 658 1485 1485 HOH HOH B . 
CA 10 HOH 659 1486 1486 HOH HOH B . 
CA 10 HOH 660 1487 1487 HOH HOH B . 
CA 10 HOH 661 1488 1488 HOH HOH B . 
CA 10 HOH 662 1489 1489 HOH HOH B . 
CA 10 HOH 663 1490 1490 HOH HOH B . 
CA 10 HOH 664 1491 1491 HOH HOH B . 
CA 10 HOH 665 1492 1492 HOH HOH B . 
CA 10 HOH 666 1493 1493 HOH HOH B . 
CA 10 HOH 667 1494 1494 HOH HOH B . 
CA 10 HOH 668 1495 1495 HOH HOH B . 
CA 10 HOH 669 1496 1496 HOH HOH B . 
CA 10 HOH 670 1497 1497 HOH HOH B . 
CA 10 HOH 671 1498 1498 HOH HOH B . 
CA 10 HOH 672 1499 1499 HOH HOH B . 
CA 10 HOH 673 1500 1500 HOH HOH B . 
CA 10 HOH 674 1501 1501 HOH HOH B . 
CA 10 HOH 675 1502 1502 HOH HOH B . 
CA 10 HOH 676 1503 1503 HOH HOH B . 
CA 10 HOH 677 1505 1505 HOH HOH B . 
CA 10 HOH 678 1506 1506 HOH HOH B . 
CA 10 HOH 679 1507 1507 HOH HOH B . 
CA 10 HOH 680 1508 1508 HOH HOH B . 
CA 10 HOH 681 1509 1509 HOH HOH B . 
CA 10 HOH 682 1510 1510 HOH HOH B . 
CA 10 HOH 683 1511 1511 HOH HOH B . 
CA 10 HOH 684 1512 1512 HOH HOH B . 
CA 10 HOH 685 1513 1513 HOH HOH B . 
CA 10 HOH 686 1514 1514 HOH HOH B . 
CA 10 HOH 687 1515 1515 HOH HOH B . 
CA 10 HOH 688 1516 1516 HOH HOH B . 
CA 10 HOH 689 1517 1517 HOH HOH B . 
CA 10 HOH 690 1518 1518 HOH HOH B . 
CA 10 HOH 691 1519 1519 HOH HOH B . 
CA 10 HOH 692 1520 1520 HOH HOH B . 
CA 10 HOH 693 1521 1521 HOH HOH B . 
CA 10 HOH 694 1522 1522 HOH HOH B . 
CA 10 HOH 695 1523 1523 HOH HOH B . 
CA 10 HOH 696 1524 1524 HOH HOH B . 
CA 10 HOH 697 1525 1525 HOH HOH B . 
CA 10 HOH 698 1526 1526 HOH HOH B . 
CA 10 HOH 699 1527 1527 HOH HOH B . 
CA 10 HOH 700 1528 1528 HOH HOH B . 
CA 10 HOH 701 1529 1529 HOH HOH B . 
CA 10 HOH 702 1530 1530 HOH HOH B . 
CA 10 HOH 703 1531 1531 HOH HOH B . 
CA 10 HOH 704 1532 1532 HOH HOH B . 
CA 10 HOH 705 1533 1533 HOH HOH B . 
CA 10 HOH 706 1534 1534 HOH HOH B . 
CA 10 HOH 707 1536 1536 HOH HOH B . 
CA 10 HOH 708 1537 1537 HOH HOH B . 
CA 10 HOH 709 1538 1538 HOH HOH B . 
CA 10 HOH 710 1539 1539 HOH HOH B . 
CA 10 HOH 711 1540 1540 HOH HOH B . 
CA 10 HOH 712 1541 1541 HOH HOH B . 
CA 10 HOH 713 1542 1542 HOH HOH B . 
CA 10 HOH 714 1543 1543 HOH HOH B . 
CA 10 HOH 715 1544 1544 HOH HOH B . 
CA 10 HOH 716 1545 1545 HOH HOH B . 
CA 10 HOH 717 1546 1546 HOH HOH B . 
CA 10 HOH 718 1547 1547 HOH HOH B . 
CA 10 HOH 719 1548 1548 HOH HOH B . 
CA 10 HOH 720 1549 1549 HOH HOH B . 
CA 10 HOH 721 1550 1550 HOH HOH B . 
CA 10 HOH 722 1551 1551 HOH HOH B . 
CA 10 HOH 723 1552 1552 HOH HOH B . 
CA 10 HOH 724 1553 1553 HOH HOH B . 
CA 10 HOH 725 1554 1554 HOH HOH B . 
CA 10 HOH 726 1555 1555 HOH HOH B . 
CA 10 HOH 727 1556 1556 HOH HOH B . 
CA 10 HOH 728 1557 1557 HOH HOH B . 
CA 10 HOH 729 1558 1558 HOH HOH B . 
CA 10 HOH 730 1559 1559 HOH HOH B . 
CA 10 HOH 731 1560 1560 HOH HOH B . 
CA 10 HOH 732 1561 1561 HOH HOH B . 
CA 10 HOH 733 1562 1562 HOH HOH B . 
CA 10 HOH 734 1563 1563 HOH HOH B . 
CA 10 HOH 735 1564 1564 HOH HOH B . 
CA 10 HOH 736 1565 1565 HOH HOH B . 
CA 10 HOH 737 1566 1566 HOH HOH B . 
CA 10 HOH 738 1567 1567 HOH HOH B . 
CA 10 HOH 739 1569 1569 HOH HOH B . 
CA 10 HOH 740 1570 1570 HOH HOH B . 
CA 10 HOH 741 1571 1571 HOH HOH B . 
CA 10 HOH 742 1573 1573 HOH HOH B . 
CA 10 HOH 743 1574 1574 HOH HOH B . 
CA 10 HOH 744 1575 1575 HOH HOH B . 
CA 10 HOH 745 1576 1576 HOH HOH B . 
CA 10 HOH 746 1577 1577 HOH HOH B . 
CA 10 HOH 747 1578 1578 HOH HOH B . 
CA 10 HOH 748 1579 1579 HOH HOH B . 
CA 10 HOH 749 1580 1580 HOH HOH B . 
CA 10 HOH 750 1581 1581 HOH HOH B . 
CA 10 HOH 751 1582 1582 HOH HOH B . 
CA 10 HOH 752 1583 1583 HOH HOH B . 
CA 10 HOH 753 1585 1585 HOH HOH B . 
CA 10 HOH 754 1586 1586 HOH HOH B . 
CA 10 HOH 755 1587 1587 HOH HOH B . 
CA 10 HOH 756 1588 1588 HOH HOH B . 
CA 10 HOH 757 1589 1589 HOH HOH B . 
CA 10 HOH 758 1590 1590 HOH HOH B . 
CA 10 HOH 759 1591 1591 HOH HOH B . 
CA 10 HOH 760 1592 1592 HOH HOH B . 
CA 10 HOH 761 1593 1593 HOH HOH B . 
CA 10 HOH 762 1594 1594 HOH HOH B . 
CA 10 HOH 763 1595 1595 HOH HOH B . 
CA 10 HOH 764 1596 1596 HOH HOH B . 
CA 10 HOH 765 1597 1597 HOH HOH B . 
CA 10 HOH 766 1598 1598 HOH HOH B . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 118 A ASN 118 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 135 A ASN 135 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 352 A ASN 352 ? ASN 'GLYCOSYLATION SITE' 
4 A ASN 392 A ASN 392 ? ASN 'GLYCOSYLATION SITE' 
5 B ASN 118 B ASN 118 ? ASN 'GLYCOSYLATION SITE' 
6 B ASN 135 B ASN 135 ? ASN 'GLYCOSYLATION SITE' 
7 B ASN 392 B ASN 392 ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_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,J,K,L,M,N,BA    
2 1 B,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,CA 
# 
_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_
_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 
1 'Structure model' 1 0 2009-03-24 
2 'Structure model' 1 1 2011-07-13 
# 
_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         ? 
# 
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' 'Non-polymer description'   
2 2 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
CNS         1.2   ?               package 'Axel T. Brunger' axel.brunger@yale.edu refinement        http://cns-online.org/ 
Fortran_77 ? 1 
PDB_EXTRACT 3.006 'June 11, 2008' package PDB               help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++        ? 2 
MAR345dtb   .     ?               ?       ?                 ?                     'data collection' ? ?          ? 3 
DENZO       .     ?               ?       ?                 ?                     'data reduction'  ? ?          ? 4 
SCALEPACK   .     ?               ?       ?                 ?                     'data scaling'    ? ?          ? 5 
AMoRE       .     ?               ?       ?                 ?                     phasing           ? ?          ? 6 
# 
_pdbx_entry_details.sequence_details     
;AUTHORS STATE THAT SINCE THE PROTEIN WAS PURIFIED FROM A NATURAL SOURCE, THIS DIFFERENCE BETWEEN THE DEPOSITED SEQUENCE AND UNIPROT DATABASE COULD INDICATE NATURAL VARIATION.
;
_pdbx_entry_details.entry_id             3GDP 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
# 
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 ND2 B ASN 352 ? ? C1 B NDG 533  ? ? 1.46 
2 1 NH1 A ARG 475 ? B O  A HOH 1007 ? ? 1.60 
3 1 OD1 B ASP 70  ? B O  B HOH 1555 ? ? 2.02 
4 1 NH1 A ARG 210 ? B O  A HOH 959  ? ? 2.10 
# 
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 ARG A 101 ? ? -150.68 74.61   
2  1 LYS A 250 ? ? 72.62   -7.11   
3  1 TYR A 390 ? ? 59.27   18.93   
4  1 CYS A 464 ? ? -154.85 60.14   
5  1 LYS A 468 ? ? -122.28 -51.16  
6  1 ASP A 486 ? ? 179.67  -163.86 
7  1 ARG B 101 ? ? -150.73 73.06   
8  1 LYS B 250 ? ? 69.57   -5.59   
9  1 CYS B 464 ? ? -156.70 61.73   
10 1 ASP B 486 ? ? -177.67 -164.69 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     N 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     NDG 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      533 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     O1L 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    M 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    NDG 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     1 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    O1L 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2  'ISOPROPYL ALCOHOL'                         IPA 
3  'FLAVIN-ADENINE DINUCLEOTIDE'               FAD 
4  N-ACETYL-D-GLUCOSAMINE                      NAG 
5  BETA-L-FUCOSE                               FUL 
6  ALPHA-D-MANNOSE                             MAN 
7  ALPHA-L-FUCOSE                              FUC 
8  BETA-D-MANNOSE                              BMA 
9  '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 
10 water                                       HOH 
# 
